data_5DLT # _entry.id 5DLT # _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 5DLT WWPDB D_1000213407 # _pdbx_database_status.status_code REL _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.entry_id 5DLT _pdbx_database_status.recvd_initial_deposition_date 2015-09-07 _pdbx_database_status.SG_entry N _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site PDBE _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? _pdbx_database_status.pdb_format_compatible Y # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Hausmann, J.' 1 'Joosten, R.P.' 2 'Perrakis, A.' 3 # _citation.abstract ? _citation.abstract_id_CAS ? _citation.book_id_ISBN ? _citation.book_publisher ? _citation.book_publisher_city ? _citation.book_title ? _citation.coordinate_linkage ? _citation.country UK _citation.database_id_Medline ? _citation.details ? _citation.id primary _citation.journal_abbrev 'Nat Commun' _citation.journal_id_ASTM ? _citation.journal_id_CSD ? _citation.journal_id_ISSN 2041-1723 _citation.journal_full ? _citation.journal_issue ? _citation.journal_volume 7 _citation.language ? _citation.page_first 11248 _citation.page_last 11248 _citation.title 'Steroid binding to Autotaxin links bile salts and lysophosphatidic acid signalling.' _citation.year 2016 _citation.database_id_CSD ? _citation.pdbx_database_id_DOI 10.1038/ncomms11248 _citation.pdbx_database_id_PubMed 27075612 _citation.unpublished_flag ? # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Keune, W.J.' 1 primary 'Hausmann, J.' 2 primary 'Bolier, R.' 3 primary 'Tolenaars, D.' 4 primary 'Kremer, A.' 5 primary 'Heidebrecht, T.' 6 primary 'Joosten, R.P.' 7 primary 'Sunkara, M.' 8 primary 'Morris, A.J.' 9 primary 'Matas-Rico, E.' 10 primary 'Moolenaar, W.H.' 11 primary 'Oude Elferink, R.P.' 12 primary 'Perrakis, A.' 13 # _cell.angle_alpha 98.720 _cell.angle_alpha_esd ? _cell.angle_beta 105.800 _cell.angle_beta_esd ? _cell.angle_gamma 99.970 _cell.angle_gamma_esd ? _cell.entry_id 5DLT _cell.details ? _cell.formula_units_Z ? _cell.length_a 53.671 _cell.length_a_esd ? _cell.length_b 63.482 _cell.length_b_esd ? _cell.length_c 70.715 _cell.length_c_esd ? _cell.volume ? _cell.volume_esd ? _cell.Z_PDB 1 _cell.reciprocal_angle_alpha ? _cell.reciprocal_angle_beta ? _cell.reciprocal_angle_gamma ? _cell.reciprocal_angle_alpha_esd ? _cell.reciprocal_angle_beta_esd ? _cell.reciprocal_angle_gamma_esd ? _cell.reciprocal_length_a ? _cell.reciprocal_length_b ? _cell.reciprocal_length_c ? _cell.reciprocal_length_a_esd ? _cell.reciprocal_length_b_esd ? _cell.reciprocal_length_c_esd ? _cell.pdbx_unique_axis ? # _symmetry.entry_id 5DLT _symmetry.cell_setting ? _symmetry.Int_Tables_number 1 _symmetry.space_group_name_Hall ? _symmetry.space_group_name_H-M 'P 1' _symmetry.pdbx_full_space_group_name_H-M ? # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer man 'Ectonucleotide pyrophosphatase/phosphodiesterase family member 2' 95117.641 1 3.1.4.39 N410A ? ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 2 ? ? ? ? 3 non-polymer man BETA-D-MANNOSE 180.156 1 ? ? ? ? 4 non-polymer syn 'ZINC ION' 65.409 2 ? ? ? ? 5 non-polymer syn 7alpha-hydroxycholesterol 402.653 1 ? ? ? ? 6 non-polymer syn 'CALCIUM ION' 40.078 1 ? ? ? ? 7 non-polymer syn 'IODIDE ION' 126.904 10 ? ? ? ? 8 non-polymer syn 'THIOCYANATE ION' 58.082 11 ? ? ? ? 9 non-polymer syn 'SODIUM ION' 22.990 2 ? ? ? ? 10 non-polymer syn GLYCEROL 92.094 7 ? ? ? ? 11 water nat water 18.015 526 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'E-NPP 2,Autotaxin,Extracellular lysophospholipase D,LysoPLD' # _entity_poly.entity_id 1 _entity_poly.type 'polypeptide(L)' _entity_poly.nstd_linkage no _entity_poly.nstd_monomer yes _entity_poly.pdbx_seq_one_letter_code ;AEWDEGPPTVLSDSPWTNTSGSCKGRCFELQEVGPPDCRCDNLCKSYSSCCHDFDELCLKTARGWECTKDRCGEVRNEEN ACHCSEDCLSRGDCCTNYQVVCKGESHWVDDDCEEIKVPECPAGFVRPPLIIFSVDGFRASYMKKGSKVMPNIEKLRSCG THAPYMRPVYPTK(TPO)FPNLYTLATGLYPESHGIVGNSMYDPVFDASFHLRGREKFNHRWWGGQPLWITATKQGVRAG TFFWSVSIPHERRILTILQWLSLPDNERPSVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKTVGQLMDGLKQLRLHRCV NVIFVGDHGMEDVTCDRTEFLSNYLTNVDDITLVPGTLGRIRAKSINNSKYDPKTIIAALTCKKPDQHFKPYMKQHLPKR LHYANNRRIEDIHLLVDRRWHVARKPLDVYKKPSGKCFFQGDHGFDNKVNSMQTVFVGYGPTFKYRTKVPPFENIELYNV MCDLLGLKPAPNNGTHGSLNHLLRTNTFRPTMPDEVSRPNYPGIMYLQSEFDLGCTCDDKVEPKNKLEEFNKRLHTKGST KERHLLYGRPAVLYRTSYDILYHTDFESGYSEIFLMPLWTSYTISKQAEVSSIPEHLTNCVRPDVRVSPGFSQNCLAYKN DKQMSYGFLFPPYLSSSPEAKYDAFLVTNMVPMYPAFKRVWAYFQRVLVKKYASERNGVNVISGPIFDYNYDGLRDTEDE IKQYVEGSSIPVPTHYYSIITSCLDFTQPADKCDGPLSVSSFILPHRPDNDESCASSEDESKWVEELMKMHTARVRDIEH LTGLDFYRKTSRSYSEILTLKTYLHTYESEI ; _entity_poly.pdbx_seq_one_letter_code_can ;AEWDEGPPTVLSDSPWTNTSGSCKGRCFELQEVGPPDCRCDNLCKSYSSCCHDFDELCLKTARGWECTKDRCGEVRNEEN ACHCSEDCLSRGDCCTNYQVVCKGESHWVDDDCEEIKVPECPAGFVRPPLIIFSVDGFRASYMKKGSKVMPNIEKLRSCG THAPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDASFHLRGREKFNHRWWGGQPLWITATKQGVRAGTFFW SVSIPHERRILTILQWLSLPDNERPSVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKTVGQLMDGLKQLRLHRCVNVIF VGDHGMEDVTCDRTEFLSNYLTNVDDITLVPGTLGRIRAKSINNSKYDPKTIIAALTCKKPDQHFKPYMKQHLPKRLHYA NNRRIEDIHLLVDRRWHVARKPLDVYKKPSGKCFFQGDHGFDNKVNSMQTVFVGYGPTFKYRTKVPPFENIELYNVMCDL LGLKPAPNNGTHGSLNHLLRTNTFRPTMPDEVSRPNYPGIMYLQSEFDLGCTCDDKVEPKNKLEEFNKRLHTKGSTKERH LLYGRPAVLYRTSYDILYHTDFESGYSEIFLMPLWTSYTISKQAEVSSIPEHLTNCVRPDVRVSPGFSQNCLAYKNDKQM SYGFLFPPYLSSSPEAKYDAFLVTNMVPMYPAFKRVWAYFQRVLVKKYASERNGVNVISGPIFDYNYDGLRDTEDEIKQY VEGSSIPVPTHYYSIITSCLDFTQPADKCDGPLSVSSFILPHRPDNDESCASSEDESKWVEELMKMHTARVRDIEHLTGL DFYRKTSRSYSEILTLKTYLHTYESEI ; _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 ALA n 1 2 GLU n 1 3 TRP n 1 4 ASP n 1 5 GLU n 1 6 GLY n 1 7 PRO n 1 8 PRO n 1 9 THR n 1 10 VAL n 1 11 LEU n 1 12 SER n 1 13 ASP n 1 14 SER n 1 15 PRO n 1 16 TRP n 1 17 THR n 1 18 ASN n 1 19 THR n 1 20 SER n 1 21 GLY n 1 22 SER n 1 23 CYS n 1 24 LYS n 1 25 GLY n 1 26 ARG n 1 27 CYS n 1 28 PHE n 1 29 GLU n 1 30 LEU n 1 31 GLN n 1 32 GLU n 1 33 VAL n 1 34 GLY n 1 35 PRO n 1 36 PRO n 1 37 ASP n 1 38 CYS n 1 39 ARG n 1 40 CYS n 1 41 ASP n 1 42 ASN n 1 43 LEU n 1 44 CYS n 1 45 LYS n 1 46 SER n 1 47 TYR n 1 48 SER n 1 49 SER n 1 50 CYS n 1 51 CYS n 1 52 HIS n 1 53 ASP n 1 54 PHE n 1 55 ASP n 1 56 GLU n 1 57 LEU n 1 58 CYS n 1 59 LEU n 1 60 LYS n 1 61 THR n 1 62 ALA n 1 63 ARG n 1 64 GLY n 1 65 TRP n 1 66 GLU n 1 67 CYS n 1 68 THR n 1 69 LYS n 1 70 ASP n 1 71 ARG n 1 72 CYS n 1 73 GLY n 1 74 GLU n 1 75 VAL n 1 76 ARG n 1 77 ASN n 1 78 GLU n 1 79 GLU n 1 80 ASN n 1 81 ALA n 1 82 CYS n 1 83 HIS n 1 84 CYS n 1 85 SER n 1 86 GLU n 1 87 ASP n 1 88 CYS n 1 89 LEU n 1 90 SER n 1 91 ARG n 1 92 GLY n 1 93 ASP n 1 94 CYS n 1 95 CYS n 1 96 THR n 1 97 ASN n 1 98 TYR n 1 99 GLN n 1 100 VAL n 1 101 VAL n 1 102 CYS n 1 103 LYS n 1 104 GLY n 1 105 GLU n 1 106 SER n 1 107 HIS n 1 108 TRP n 1 109 VAL n 1 110 ASP n 1 111 ASP n 1 112 ASP n 1 113 CYS n 1 114 GLU n 1 115 GLU n 1 116 ILE n 1 117 LYS n 1 118 VAL n 1 119 PRO n 1 120 GLU n 1 121 CYS n 1 122 PRO n 1 123 ALA n 1 124 GLY n 1 125 PHE n 1 126 VAL n 1 127 ARG n 1 128 PRO n 1 129 PRO n 1 130 LEU n 1 131 ILE n 1 132 ILE n 1 133 PHE n 1 134 SER n 1 135 VAL n 1 136 ASP n 1 137 GLY n 1 138 PHE n 1 139 ARG n 1 140 ALA n 1 141 SER n 1 142 TYR n 1 143 MET n 1 144 LYS n 1 145 LYS n 1 146 GLY n 1 147 SER n 1 148 LYS n 1 149 VAL n 1 150 MET n 1 151 PRO n 1 152 ASN n 1 153 ILE n 1 154 GLU n 1 155 LYS n 1 156 LEU n 1 157 ARG n 1 158 SER n 1 159 CYS n 1 160 GLY n 1 161 THR n 1 162 HIS n 1 163 ALA n 1 164 PRO n 1 165 TYR n 1 166 MET n 1 167 ARG n 1 168 PRO n 1 169 VAL n 1 170 TYR n 1 171 PRO n 1 172 THR n 1 173 LYS n 1 174 TPO n 1 175 PHE n 1 176 PRO n 1 177 ASN n 1 178 LEU n 1 179 TYR n 1 180 THR n 1 181 LEU n 1 182 ALA n 1 183 THR n 1 184 GLY n 1 185 LEU n 1 186 TYR n 1 187 PRO n 1 188 GLU n 1 189 SER n 1 190 HIS n 1 191 GLY n 1 192 ILE n 1 193 VAL n 1 194 GLY n 1 195 ASN n 1 196 SER n 1 197 MET n 1 198 TYR n 1 199 ASP n 1 200 PRO n 1 201 VAL n 1 202 PHE n 1 203 ASP n 1 204 ALA n 1 205 SER n 1 206 PHE n 1 207 HIS n 1 208 LEU n 1 209 ARG n 1 210 GLY n 1 211 ARG n 1 212 GLU n 1 213 LYS n 1 214 PHE n 1 215 ASN n 1 216 HIS n 1 217 ARG n 1 218 TRP n 1 219 TRP n 1 220 GLY n 1 221 GLY n 1 222 GLN n 1 223 PRO n 1 224 LEU n 1 225 TRP n 1 226 ILE n 1 227 THR n 1 228 ALA n 1 229 THR n 1 230 LYS n 1 231 GLN n 1 232 GLY n 1 233 VAL n 1 234 ARG n 1 235 ALA n 1 236 GLY n 1 237 THR n 1 238 PHE n 1 239 PHE n 1 240 TRP n 1 241 SER n 1 242 VAL n 1 243 SER n 1 244 ILE n 1 245 PRO n 1 246 HIS n 1 247 GLU n 1 248 ARG n 1 249 ARG n 1 250 ILE n 1 251 LEU n 1 252 THR n 1 253 ILE n 1 254 LEU n 1 255 GLN n 1 256 TRP n 1 257 LEU n 1 258 SER n 1 259 LEU n 1 260 PRO n 1 261 ASP n 1 262 ASN n 1 263 GLU n 1 264 ARG n 1 265 PRO n 1 266 SER n 1 267 VAL n 1 268 TYR n 1 269 ALA n 1 270 PHE n 1 271 TYR n 1 272 SER n 1 273 GLU n 1 274 GLN n 1 275 PRO n 1 276 ASP n 1 277 PHE n 1 278 SER n 1 279 GLY n 1 280 HIS n 1 281 LYS n 1 282 TYR n 1 283 GLY n 1 284 PRO n 1 285 PHE n 1 286 GLY n 1 287 PRO n 1 288 GLU n 1 289 MET n 1 290 THR n 1 291 ASN n 1 292 PRO n 1 293 LEU n 1 294 ARG n 1 295 GLU n 1 296 ILE n 1 297 ASP n 1 298 LYS n 1 299 THR n 1 300 VAL n 1 301 GLY n 1 302 GLN n 1 303 LEU n 1 304 MET n 1 305 ASP n 1 306 GLY n 1 307 LEU n 1 308 LYS n 1 309 GLN n 1 310 LEU n 1 311 ARG n 1 312 LEU n 1 313 HIS n 1 314 ARG n 1 315 CYS n 1 316 VAL n 1 317 ASN n 1 318 VAL n 1 319 ILE n 1 320 PHE n 1 321 VAL n 1 322 GLY n 1 323 ASP n 1 324 HIS n 1 325 GLY n 1 326 MET n 1 327 GLU n 1 328 ASP n 1 329 VAL n 1 330 THR n 1 331 CYS n 1 332 ASP n 1 333 ARG n 1 334 THR n 1 335 GLU n 1 336 PHE n 1 337 LEU n 1 338 SER n 1 339 ASN n 1 340 TYR n 1 341 LEU n 1 342 THR n 1 343 ASN n 1 344 VAL n 1 345 ASP n 1 346 ASP n 1 347 ILE n 1 348 THR n 1 349 LEU n 1 350 VAL n 1 351 PRO n 1 352 GLY n 1 353 THR n 1 354 LEU n 1 355 GLY n 1 356 ARG n 1 357 ILE n 1 358 ARG n 1 359 ALA n 1 360 LYS n 1 361 SER n 1 362 ILE n 1 363 ASN n 1 364 ASN n 1 365 SER n 1 366 LYS n 1 367 TYR n 1 368 ASP n 1 369 PRO n 1 370 LYS n 1 371 THR n 1 372 ILE n 1 373 ILE n 1 374 ALA n 1 375 ALA n 1 376 LEU n 1 377 THR n 1 378 CYS n 1 379 LYS n 1 380 LYS n 1 381 PRO n 1 382 ASP n 1 383 GLN n 1 384 HIS n 1 385 PHE n 1 386 LYS n 1 387 PRO n 1 388 TYR n 1 389 MET n 1 390 LYS n 1 391 GLN n 1 392 HIS n 1 393 LEU n 1 394 PRO n 1 395 LYS n 1 396 ARG n 1 397 LEU n 1 398 HIS n 1 399 TYR n 1 400 ALA n 1 401 ASN n 1 402 ASN n 1 403 ARG n 1 404 ARG n 1 405 ILE n 1 406 GLU n 1 407 ASP n 1 408 ILE n 1 409 HIS n 1 410 LEU n 1 411 LEU n 1 412 VAL n 1 413 ASP n 1 414 ARG n 1 415 ARG n 1 416 TRP n 1 417 HIS n 1 418 VAL n 1 419 ALA n 1 420 ARG n 1 421 LYS n 1 422 PRO n 1 423 LEU n 1 424 ASP n 1 425 VAL n 1 426 TYR n 1 427 LYS n 1 428 LYS n 1 429 PRO n 1 430 SER n 1 431 GLY n 1 432 LYS n 1 433 CYS n 1 434 PHE n 1 435 PHE n 1 436 GLN n 1 437 GLY n 1 438 ASP n 1 439 HIS n 1 440 GLY n 1 441 PHE n 1 442 ASP n 1 443 ASN n 1 444 LYS n 1 445 VAL n 1 446 ASN n 1 447 SER n 1 448 MET n 1 449 GLN n 1 450 THR n 1 451 VAL n 1 452 PHE n 1 453 VAL n 1 454 GLY n 1 455 TYR n 1 456 GLY n 1 457 PRO n 1 458 THR n 1 459 PHE n 1 460 LYS n 1 461 TYR n 1 462 ARG n 1 463 THR n 1 464 LYS n 1 465 VAL n 1 466 PRO n 1 467 PRO n 1 468 PHE n 1 469 GLU n 1 470 ASN n 1 471 ILE n 1 472 GLU n 1 473 LEU n 1 474 TYR n 1 475 ASN n 1 476 VAL n 1 477 MET n 1 478 CYS n 1 479 ASP n 1 480 LEU n 1 481 LEU n 1 482 GLY n 1 483 LEU n 1 484 LYS n 1 485 PRO n 1 486 ALA n 1 487 PRO n 1 488 ASN n 1 489 ASN n 1 490 GLY n 1 491 THR n 1 492 HIS n 1 493 GLY n 1 494 SER n 1 495 LEU n 1 496 ASN n 1 497 HIS n 1 498 LEU n 1 499 LEU n 1 500 ARG n 1 501 THR n 1 502 ASN n 1 503 THR n 1 504 PHE n 1 505 ARG n 1 506 PRO n 1 507 THR n 1 508 MET n 1 509 PRO n 1 510 ASP n 1 511 GLU n 1 512 VAL n 1 513 SER n 1 514 ARG n 1 515 PRO n 1 516 ASN n 1 517 TYR n 1 518 PRO n 1 519 GLY n 1 520 ILE n 1 521 MET n 1 522 TYR n 1 523 LEU n 1 524 GLN n 1 525 SER n 1 526 GLU n 1 527 PHE n 1 528 ASP n 1 529 LEU n 1 530 GLY n 1 531 CYS n 1 532 THR n 1 533 CYS n 1 534 ASP n 1 535 ASP n 1 536 LYS n 1 537 VAL n 1 538 GLU n 1 539 PRO n 1 540 LYS n 1 541 ASN n 1 542 LYS n 1 543 LEU n 1 544 GLU n 1 545 GLU n 1 546 PHE n 1 547 ASN n 1 548 LYS n 1 549 ARG n 1 550 LEU n 1 551 HIS n 1 552 THR n 1 553 LYS n 1 554 GLY n 1 555 SER n 1 556 THR n 1 557 LYS n 1 558 GLU n 1 559 ARG n 1 560 HIS n 1 561 LEU n 1 562 LEU n 1 563 TYR n 1 564 GLY n 1 565 ARG n 1 566 PRO n 1 567 ALA n 1 568 VAL n 1 569 LEU n 1 570 TYR n 1 571 ARG n 1 572 THR n 1 573 SER n 1 574 TYR n 1 575 ASP n 1 576 ILE n 1 577 LEU n 1 578 TYR n 1 579 HIS n 1 580 THR n 1 581 ASP n 1 582 PHE n 1 583 GLU n 1 584 SER n 1 585 GLY n 1 586 TYR n 1 587 SER n 1 588 GLU n 1 589 ILE n 1 590 PHE n 1 591 LEU n 1 592 MET n 1 593 PRO n 1 594 LEU n 1 595 TRP n 1 596 THR n 1 597 SER n 1 598 TYR n 1 599 THR n 1 600 ILE n 1 601 SER n 1 602 LYS n 1 603 GLN n 1 604 ALA n 1 605 GLU n 1 606 VAL n 1 607 SER n 1 608 SER n 1 609 ILE n 1 610 PRO n 1 611 GLU n 1 612 HIS n 1 613 LEU n 1 614 THR n 1 615 ASN n 1 616 CYS n 1 617 VAL n 1 618 ARG n 1 619 PRO n 1 620 ASP n 1 621 VAL n 1 622 ARG n 1 623 VAL n 1 624 SER n 1 625 PRO n 1 626 GLY n 1 627 PHE n 1 628 SER n 1 629 GLN n 1 630 ASN n 1 631 CYS n 1 632 LEU n 1 633 ALA n 1 634 TYR n 1 635 LYS n 1 636 ASN n 1 637 ASP n 1 638 LYS n 1 639 GLN n 1 640 MET n 1 641 SER n 1 642 TYR n 1 643 GLY n 1 644 PHE n 1 645 LEU n 1 646 PHE n 1 647 PRO n 1 648 PRO n 1 649 TYR n 1 650 LEU n 1 651 SER n 1 652 SER n 1 653 SER n 1 654 PRO n 1 655 GLU n 1 656 ALA n 1 657 LYS n 1 658 TYR n 1 659 ASP n 1 660 ALA n 1 661 PHE n 1 662 LEU n 1 663 VAL n 1 664 THR n 1 665 ASN n 1 666 MET n 1 667 VAL n 1 668 PRO n 1 669 MET n 1 670 TYR n 1 671 PRO n 1 672 ALA n 1 673 PHE n 1 674 LYS n 1 675 ARG n 1 676 VAL n 1 677 TRP n 1 678 ALA n 1 679 TYR n 1 680 PHE n 1 681 GLN n 1 682 ARG n 1 683 VAL n 1 684 LEU n 1 685 VAL n 1 686 LYS n 1 687 LYS n 1 688 TYR n 1 689 ALA n 1 690 SER n 1 691 GLU n 1 692 ARG n 1 693 ASN n 1 694 GLY n 1 695 VAL n 1 696 ASN n 1 697 VAL n 1 698 ILE n 1 699 SER n 1 700 GLY n 1 701 PRO n 1 702 ILE n 1 703 PHE n 1 704 ASP n 1 705 TYR n 1 706 ASN n 1 707 TYR n 1 708 ASP n 1 709 GLY n 1 710 LEU n 1 711 ARG n 1 712 ASP n 1 713 THR n 1 714 GLU n 1 715 ASP n 1 716 GLU n 1 717 ILE n 1 718 LYS n 1 719 GLN n 1 720 TYR n 1 721 VAL n 1 722 GLU n 1 723 GLY n 1 724 SER n 1 725 SER n 1 726 ILE n 1 727 PRO n 1 728 VAL n 1 729 PRO n 1 730 THR n 1 731 HIS n 1 732 TYR n 1 733 TYR n 1 734 SER n 1 735 ILE n 1 736 ILE n 1 737 THR n 1 738 SER n 1 739 CYS n 1 740 LEU n 1 741 ASP n 1 742 PHE n 1 743 THR n 1 744 GLN n 1 745 PRO n 1 746 ALA n 1 747 ASP n 1 748 LYS n 1 749 CYS n 1 750 ASP n 1 751 GLY n 1 752 PRO n 1 753 LEU n 1 754 SER n 1 755 VAL n 1 756 SER n 1 757 SER n 1 758 PHE n 1 759 ILE n 1 760 LEU n 1 761 PRO n 1 762 HIS n 1 763 ARG n 1 764 PRO n 1 765 ASP n 1 766 ASN n 1 767 ASP n 1 768 GLU n 1 769 SER n 1 770 CYS n 1 771 ALA n 1 772 SER n 1 773 SER n 1 774 GLU n 1 775 ASP n 1 776 GLU n 1 777 SER n 1 778 LYS n 1 779 TRP n 1 780 VAL n 1 781 GLU n 1 782 GLU n 1 783 LEU n 1 784 MET n 1 785 LYS n 1 786 MET n 1 787 HIS n 1 788 THR n 1 789 ALA n 1 790 ARG n 1 791 VAL n 1 792 ARG n 1 793 ASP n 1 794 ILE n 1 795 GLU n 1 796 HIS n 1 797 LEU n 1 798 THR n 1 799 GLY n 1 800 LEU n 1 801 ASP n 1 802 PHE n 1 803 TYR n 1 804 ARG n 1 805 LYS n 1 806 THR n 1 807 SER n 1 808 ARG n 1 809 SER n 1 810 TYR n 1 811 SER n 1 812 GLU n 1 813 ILE n 1 814 LEU n 1 815 THR n 1 816 LEU n 1 817 LYS n 1 818 THR n 1 819 TYR n 1 820 LEU n 1 821 HIS n 1 822 THR n 1 823 TYR n 1 824 GLU n 1 825 SER n 1 826 GLU n 1 827 ILE n # _entity_src_gen.entity_id 1 _entity_src_gen.pdbx_src_id 1 _entity_src_gen.pdbx_alt_source_flag sample _entity_src_gen.pdbx_seq_type 'Biological sequence' _entity_src_gen.pdbx_beg_seq_num 1 _entity_src_gen.pdbx_end_seq_num 827 _entity_src_gen.gene_src_common_name 'norway Rat' _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene 'Enpp2, Atx, Npps2' _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 'Rattus norvegicus' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 10116 _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 human _entity_src_gen.pdbx_host_org_scientific_name 'Homo sapiens' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 9606 _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 HEK293 _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 ENPP2_RAT _struct_ref.pdbx_db_accession Q64610 _struct_ref.pdbx_db_isoform Q64610-2 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;AEWDEGPPTVLSDSPWTNTSGSCKGRCFELQEVGPPDCRCDNLCKSYSSCCHDFDELCLKTARGWECTKDRCGEVRNEEN ACHCSEDCLSRGDCCTNYQVVCKGESHWVDDDCEEIKVPECPAGFVRPPLIIFSVDGFRASYMKKGSKVMPNIEKLRSCG THAPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDASFHLRGREKFNHRWWGGQPLWITATKQGVRAGTFFW SVSIPHERRILTILQWLSLPDNERPSVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKTVGQLMDGLKQLRLHRCVNVIF VGDHGMEDVTCDRTEFLSNYLTNVDDITLVPGTLGRIRAKSINNSKYDPKTIIANLTCKKPDQHFKPYMKQHLPKRLHYA NNRRIEDIHLLVDRRWHVARKPLDVYKKPSGKCFFQGDHGFDNKVNSMQTVFVGYGPTFKYRTKVPPFENIELYNVMCDL LGLKPAPNNGTHGSLNHLLRTNTFRPTMPDEVSRPNYPGIMYLQSEFDLGCTCDDKVEPKNKLEELNKRLHTKGSRKERH LLYGRPAVLYRTSYDILYHTDFESGYSEIFLMPLWTSYTISKQAEVSSIPEHLTNCVRPDVRVSPGFSQNCLAYKNDKQM SYGFLFPPYLSSSPEAKYDAFLVTNMVPMYPAFKRVWAYFQRVLVKKYASERNGVNVISGPIFDYNYDGLRDTEDEIKQY VEGSSIPVPTHYYSIITSCLDFTQPADKCDGPLSVSSFILPHRPDNDESCNSSEDESKWVEELMKMHTARVRDIEHLTGL DFYRKTSRSYSEILTLKTYLHTYESEI ; _struct_ref.pdbx_align_begin 36 # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 5DLT _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 1 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 827 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession Q64610 _struct_ref_seq.db_align_beg 36 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 862 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 36 _struct_ref_seq.pdbx_auth_seq_align_end 862 # 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 5DLT ALA A 375 ? UNP Q64610 ASN 410 'engineered mutation' 410 1 1 5DLT PHE A 546 ? UNP Q64610 LEU 581 'cloning artifact' 581 2 1 5DLT THR A 556 ? UNP Q64610 ARG 591 'cloning artifact' 591 3 1 5DLT ALA A 771 ? UNP Q64610 ASN 806 'engineered mutation' 806 4 # 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 5JK non-polymer . 7alpha-hydroxycholesterol '(3beta,7alpha,9beta,14beta)-cholest-5-ene-3,7-diol' 'C27 H46 O2' 402.653 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 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 GOL non-polymer . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3' 92.094 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 IOD non-polymer . 'IODIDE ION' ? 'I -1' 126.904 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 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NA non-polymer . 'SODIUM ION' ? 'Na 1' 22.990 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 SCN non-polymer . 'THIOCYANATE ION' ? 'C N S -1' 58.082 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TPO 'L-peptide linking' n PHOSPHOTHREONINE PHOSPHONOTHREONINE 'C4 H10 N O6 P' 199.099 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 ZN non-polymer . 'ZINC ION' ? 'Zn 2' 65.409 # _exptl.absorpt_coefficient_mu ? _exptl.absorpt_correction_T_max ? _exptl.absorpt_correction_T_min ? _exptl.absorpt_correction_type ? _exptl.absorpt_process_details ? _exptl.entry_id 5DLT _exptl.crystals_number 1 _exptl.details ? _exptl.method 'X-RAY DIFFRACTION' _exptl.method_details ? # _exptl_crystal.colour ? _exptl_crystal.density_diffrn ? _exptl_crystal.density_Matthews 2.35 _exptl_crystal.density_method ? _exptl_crystal.density_percent_sol 47.60 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.id 1 _exptl_crystal.preparation ? _exptl_crystal.size_max ? _exptl_crystal.size_mid ? _exptl_crystal.size_min ? _exptl_crystal.size_rad ? _exptl_crystal.colour_lustre ? _exptl_crystal.colour_modifier ? _exptl_crystal.colour_primary ? _exptl_crystal.density_meas ? _exptl_crystal.density_meas_esd ? _exptl_crystal.density_meas_gt ? _exptl_crystal.density_meas_lt ? _exptl_crystal.density_meas_temp ? _exptl_crystal.density_meas_temp_esd ? _exptl_crystal.density_meas_temp_gt ? _exptl_crystal.density_meas_temp_lt ? _exptl_crystal.pdbx_crystal_image_url ? _exptl_crystal.pdbx_crystal_image_format ? _exptl_crystal.pdbx_mosaicity ? _exptl_crystal.pdbx_mosaicity_esd ? # _exptl_crystal_grow.apparatus ? _exptl_crystal_grow.atmosphere ? _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.details ? _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.method_ref ? _exptl_crystal_grow.pH 6.0 _exptl_crystal_grow.pressure ? _exptl_crystal_grow.pressure_esd ? _exptl_crystal_grow.seeding ? _exptl_crystal_grow.seeding_ref ? _exptl_crystal_grow.temp 293 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.temp_esd ? _exptl_crystal_grow.time ? _exptl_crystal_grow.pdbx_details 'PEG 3350, 0.1M ammonium iodide 0.3M sodium thiocyanate, 23.5mg/ml heparin sulfate' _exptl_crystal_grow.pdbx_pH_range ? # _diffrn.ambient_environment ? _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.ambient_temp_esd ? _diffrn.crystal_id 1 _diffrn.crystal_support ? _diffrn.crystal_treatment ? _diffrn.details ? _diffrn.id 1 _diffrn.ambient_pressure ? _diffrn.ambient_pressure_esd ? _diffrn.ambient_pressure_gt ? _diffrn.ambient_pressure_lt ? _diffrn.ambient_temp_gt ? _diffrn.ambient_temp_lt ? # _diffrn_detector.details ? _diffrn_detector.detector PIXEL _diffrn_detector.diffrn_id 1 _diffrn_detector.type 'DECTRIS PILATUS 6M-F' _diffrn_detector.area_resol_mean ? _diffrn_detector.dtime ? _diffrn_detector.pdbx_frames_total ? _diffrn_detector.pdbx_collection_time_total ? _diffrn_detector.pdbx_collection_date 2011-08-30 # _diffrn_radiation.collimation ? _diffrn_radiation.diffrn_id 1 _diffrn_radiation.filter_edge ? _diffrn_radiation.inhomogeneity ? _diffrn_radiation.monochromator ? _diffrn_radiation.polarisn_norm ? _diffrn_radiation.polarisn_ratio ? _diffrn_radiation.probe ? _diffrn_radiation.type ? _diffrn_radiation.xray_symbol ? _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.pdbx_wavelength_list ? _diffrn_radiation.pdbx_wavelength ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_analyzer ? _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.97935 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.current ? _diffrn_source.details ? _diffrn_source.diffrn_id 1 _diffrn_source.power ? _diffrn_source.size ? _diffrn_source.source SYNCHROTRON _diffrn_source.target ? _diffrn_source.type 'ESRF BEAMLINE ID29' _diffrn_source.voltage ? _diffrn_source.take-off_angle ? _diffrn_source.pdbx_wavelength_list 0.97935 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_synchrotron_beamline ID29 _diffrn_source.pdbx_synchrotron_site ESRF # _reflns.B_iso_Wilson_estimate 29.61 _reflns.entry_id 5DLT _reflns.data_reduction_details ? _reflns.data_reduction_method ? _reflns.d_resolution_high 1.600 _reflns.d_resolution_low 44.020 _reflns.details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.number_all ? _reflns.number_obs 105202 _reflns.observed_criterion ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.observed_criterion_I_max ? _reflns.observed_criterion_I_min ? _reflns.observed_criterion_sigma_F ? _reflns.observed_criterion_sigma_I ? _reflns.percent_possible_obs 92.100 _reflns.R_free_details ? _reflns.Rmerge_F_all ? _reflns.Rmerge_F_obs ? _reflns.Friedel_coverage ? _reflns.number_gt ? _reflns.threshold_expression ? _reflns.pdbx_redundancy 2.000 _reflns.pdbx_Rmerge_I_obs 0.065 _reflns.pdbx_Rmerge_I_all ? _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_av_sigmaI ? _reflns.pdbx_netI_over_sigmaI 6.700 _reflns.pdbx_res_netI_over_av_sigmaI_2 ? _reflns.pdbx_res_netI_over_sigmaI_2 ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_d_res_high_opt ? _reflns.pdbx_d_res_low_opt ? _reflns.pdbx_d_res_opt_method ? _reflns.phase_calculation_details ? _reflns.pdbx_Rrim_I_all ? _reflns.pdbx_Rpim_I_all 0.061 _reflns.pdbx_d_opt ? _reflns.pdbx_number_measured_all 205646 _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.pdbx_CC_half 0.997 _reflns.pdbx_R_split ? # loop_ _reflns_shell.d_res_high _reflns_shell.d_res_low _reflns_shell.meanI_over_sigI_all _reflns_shell.meanI_over_sigI_obs _reflns_shell.number_measured_all _reflns_shell.number_measured_obs _reflns_shell.number_possible _reflns_shell.number_unique_all _reflns_shell.number_unique_obs _reflns_shell.percent_possible_all _reflns_shell.percent_possible_obs _reflns_shell.Rmerge_F_all _reflns_shell.Rmerge_F_obs _reflns_shell.Rmerge_I_all _reflns_shell.Rmerge_I_obs _reflns_shell.meanI_over_sigI_gt _reflns_shell.meanI_over_uI_all _reflns_shell.meanI_over_uI_gt _reflns_shell.number_measured_gt _reflns_shell.number_unique_gt _reflns_shell.percent_possible_gt _reflns_shell.Rmerge_F_gt _reflns_shell.Rmerge_I_gt _reflns_shell.pdbx_redundancy _reflns_shell.pdbx_Rsym_value _reflns_shell.pdbx_chi_squared _reflns_shell.pdbx_netI_over_sigmaI_all _reflns_shell.pdbx_netI_over_sigmaI_obs _reflns_shell.pdbx_Rrim_I_all _reflns_shell.pdbx_Rpim_I_all _reflns_shell.pdbx_rejects _reflns_shell.pdbx_ordinal _reflns_shell.pdbx_diffrn_id _reflns_shell.pdbx_CC_half _reflns_shell.pdbx_R_split 1.600 1.630 ? 0.800 9720 ? ? 5091 ? 88.900 ? ? ? ? 0.868 ? ? ? ? ? ? ? ? 1.900 ? ? ? ? ? 0.815 0 1 1 0.437 ? 8.760 44.020 ? 23.900 1345 ? ? 643 ? 92.000 ? ? ? ? 0.029 ? ? ? ? ? ? ? ? 2.100 ? ? ? ? ? 0.027 0 2 1 0.996 ? # _refine.aniso_B[1][1] 0.2200 _refine.aniso_B[1][2] -0.0200 _refine.aniso_B[1][3] 0.3300 _refine.aniso_B[2][2] 0.2100 _refine.aniso_B[2][3] 0.1000 _refine.aniso_B[3][3] -0.5600 _refine.B_iso_max 103.320 _refine.B_iso_mean 28.7890 _refine.B_iso_min 11.550 _refine.correlation_coeff_Fo_to_Fc 0.9700 _refine.correlation_coeff_Fo_to_Fc_free 0.9620 _refine.details 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : WITH TLS ADDED' _refine.diff_density_max ? _refine.diff_density_max_esd ? _refine.diff_density_min ? _refine.diff_density_min_esd ? _refine.diff_density_rms ? _refine.diff_density_rms_esd ? _refine.entry_id 5DLT _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.ls_abs_structure_details ? _refine.ls_abs_structure_Flack ? _refine.ls_abs_structure_Flack_esd ? _refine.ls_abs_structure_Rogers ? _refine.ls_abs_structure_Rogers_esd ? _refine.ls_d_res_high 1.6000 _refine.ls_d_res_low 44.020 _refine.ls_extinction_coef ? _refine.ls_extinction_coef_esd ? _refine.ls_extinction_expression ? _refine.ls_extinction_method ? _refine.ls_goodness_of_fit_all ? _refine.ls_goodness_of_fit_all_esd ? _refine.ls_goodness_of_fit_obs ? _refine.ls_goodness_of_fit_obs_esd ? _refine.ls_hydrogen_treatment ? _refine.ls_matrix_type sparse _refine.ls_number_constraints ? _refine.ls_number_parameters ? _refine.ls_number_reflns_all ? _refine.ls_number_reflns_obs 99938 _refine.ls_number_reflns_R_free 5262 _refine.ls_number_reflns_R_work 99938 _refine.ls_number_restraints ? _refine.ls_percent_reflns_obs 92.1100 _refine.ls_percent_reflns_R_free 5.0000 _refine.ls_R_factor_all ? _refine.ls_R_factor_obs 0.1725 _refine.ls_R_factor_R_free 0.1964 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_R_factor_R_work 0.1713 _refine.ls_R_Fsqd_factor_obs ? _refine.ls_R_I_factor_obs ? _refine.ls_redundancy_reflns_all ? _refine.ls_redundancy_reflns_obs ? _refine.ls_restrained_S_all ? _refine.ls_restrained_S_obs ? _refine.ls_shift_over_esd_max ? _refine.ls_shift_over_esd_mean ? _refine.ls_structure_factor_coef ? _refine.ls_weighting_details ? _refine.ls_weighting_scheme ? _refine.ls_wR_factor_all ? _refine.ls_wR_factor_obs ? _refine.ls_wR_factor_R_free 0.1920 _refine.ls_wR_factor_R_work 0.1660 _refine.occupancy_max ? _refine.occupancy_min ? _refine.solvent_model_details MASK _refine.solvent_model_param_bsol ? _refine.solvent_model_param_ksol ? _refine.ls_R_factor_gt ? _refine.ls_goodness_of_fit_gt ? _refine.ls_goodness_of_fit_ref ? _refine.ls_shift_over_su_max ? _refine.ls_shift_over_su_max_lt ? _refine.ls_shift_over_su_mean ? _refine.ls_shift_over_su_mean_lt ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 0.000 _refine.pdbx_ls_sigma_Fsqd ? _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_starting_model 2xr9 _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_overall_ESU_R 0.0910 _refine.pdbx_overall_ESU_R_Free 0.0880 _refine.pdbx_solvent_vdw_probe_radii 1.0000 _refine.pdbx_solvent_ion_probe_radii 0.7000 _refine.pdbx_solvent_shrinkage_radii 0.7000 _refine.pdbx_real_space_R ? _refine.pdbx_density_correlation ? _refine.pdbx_pd_number_of_powder_patterns ? _refine.pdbx_pd_number_of_points ? _refine.pdbx_pd_meas_number_of_points ? _refine.pdbx_pd_proc_ls_prof_R_factor ? _refine.pdbx_pd_proc_ls_prof_wR_factor ? _refine.pdbx_pd_Marquardt_correlation_coeff ? _refine.pdbx_pd_Fsqrd_R_factor ? _refine.pdbx_pd_ls_matrix_band_width ? _refine.pdbx_overall_phase_error ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_diffrn_id 1 _refine.overall_SU_B 4.7220 _refine.overall_SU_ML 0.0760 _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_average_fsc_overall ? _refine.pdbx_average_fsc_work ? _refine.pdbx_average_fsc_free ? # _refine_hist.cycle_id final _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.d_res_high 1.6000 _refine_hist.d_res_low 44.020 _refine_hist.pdbx_number_atoms_ligand 158 _refine_hist.number_atoms_solvent 528 _refine_hist.number_atoms_total 7117 _refine_hist.pdbx_number_residues_total 796 _refine_hist.pdbx_B_iso_mean_ligand 38.66 _refine_hist.pdbx_B_iso_mean_solvent 32.56 _refine_hist.pdbx_number_atoms_protein 6431 _refine_hist.pdbx_number_atoms_nucleic_acid 0 # loop_ _refine_ls_restr.pdbx_refine_id _refine_ls_restr.criterion _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.number _refine_ls_restr.rejects _refine_ls_restr.type _refine_ls_restr.weight _refine_ls_restr.pdbx_restraint_function 'X-RAY DIFFRACTION' ? 0.012 0.022 6849 ? r_bond_refined_d ? ? 'X-RAY DIFFRACTION' ? 0.002 0.020 6289 ? r_bond_other_d ? ? 'X-RAY DIFFRACTION' ? 1.450 1.972 9284 ? r_angle_refined_deg ? ? 'X-RAY DIFFRACTION' ? 0.955 3.000 14557 ? r_angle_other_deg ? ? 'X-RAY DIFFRACTION' ? 6.214 5.000 814 ? r_dihedral_angle_1_deg ? ? 'X-RAY DIFFRACTION' ? 33.694 23.169 325 ? r_dihedral_angle_2_deg ? ? 'X-RAY DIFFRACTION' ? 12.180 15.000 1131 ? r_dihedral_angle_3_deg ? ? 'X-RAY DIFFRACTION' ? 16.806 15.000 51 ? r_dihedral_angle_4_deg ? ? 'X-RAY DIFFRACTION' ? 0.085 0.200 984 ? r_chiral_restr ? ? 'X-RAY DIFFRACTION' ? 0.006 0.021 7571 ? r_gen_planes_refined ? ? 'X-RAY DIFFRACTION' ? 0.002 0.020 1608 ? r_gen_planes_other ? ? 'X-RAY DIFFRACTION' ? 1.491 1.852 3217 ? r_mcbond_it ? ? 'X-RAY DIFFRACTION' ? 1.467 1.845 3207 ? r_mcbond_other ? ? 'X-RAY DIFFRACTION' ? 2.295 2.755 4011 ? r_mcangle_it ? ? 'X-RAY DIFFRACTION' ? 11.517 5.000 13 ? r_sphericity_bonded ? ? # loop_ _refine_ls_shell.pdbx_refine_id _refine_ls_shell.d_res_high _refine_ls_shell.d_res_low _refine_ls_shell.number_reflns_all _refine_ls_shell.number_reflns_obs _refine_ls_shell.number_reflns_R_free _refine_ls_shell.number_reflns_R_work _refine_ls_shell.percent_reflns_obs _refine_ls_shell.percent_reflns_R_free _refine_ls_shell.R_factor_all _refine_ls_shell.R_factor_obs _refine_ls_shell.R_factor_R_free _refine_ls_shell.R_factor_R_free_error _refine_ls_shell.R_factor_R_work _refine_ls_shell.redundancy_reflns_all _refine_ls_shell.redundancy_reflns_obs _refine_ls_shell.wR_factor_all _refine_ls_shell.wR_factor_obs _refine_ls_shell.wR_factor_R_free _refine_ls_shell.wR_factor_R_work _refine_ls_shell.pdbx_total_number_of_bins_used _refine_ls_shell.pdbx_phase_error _refine_ls_shell.pdbx_fsc_work _refine_ls_shell.pdbx_fsc_free 'X-RAY DIFFRACTION' 1.600 1.642 . . 361 7049 87.434 . . . 0.353 . 0.331 . . . . . . . . . . 'X-RAY DIFFRACTION' 1.642 1.687 . . 383 7194 91.731 . . . 0.299 . 0.311 . . . . . . . . . . 'X-RAY DIFFRACTION' 1.687 1.735 . . 370 6971 91.637 . . . 0.301 . 0.286 . . . . . . . . . . 'X-RAY DIFFRACTION' 1.735 1.789 . . 364 6713 91.105 . . . 0.262 . 0.260 . . . . . . . . . . 'X-RAY DIFFRACTION' 1.789 1.847 . . 321 6479 90.102 . . . 0.242 . 0.235 . . . . . . . . . . 'X-RAY DIFFRACTION' 1.847 1.912 . . 353 6218 89.768 . . . 0.253 . 0.214 . . . . . . . . . . 'X-RAY DIFFRACTION' 1.912 1.984 . . 325 5926 89.020 . . . 0.227 . 0.193 . . . . . . . . . . 'X-RAY DIFFRACTION' 1.984 2.065 . . 293 5957 93.089 . . . 0.204 . 0.169 . . . . . . . . . . 'X-RAY DIFFRACTION' 2.065 2.157 . . 295 5754 93.551 . . . 0.201 . 0.164 . . . . . . . . . . 'X-RAY DIFFRACTION' 2.157 2.262 . . 309 5558 93.902 . . . 0.197 . 0.160 . . . . . . . . . . 'X-RAY DIFFRACTION' 2.262 2.384 . . 281 5201 93.629 . . . 0.184 . 0.153 . . . . . . . . . . 'X-RAY DIFFRACTION' 2.384 2.529 . . 279 4944 92.787 . . . 0.193 . 0.151 . . . . . . . . . . 'X-RAY DIFFRACTION' 2.529 2.703 . . 252 4718 95.011 . . . 0.176 . 0.142 . . . . . . . . . . 'X-RAY DIFFRACTION' 2.703 2.919 . . 251 4408 95.354 . . . 0.178 . 0.153 . . . . . . . . . . 'X-RAY DIFFRACTION' 2.919 3.197 . . 184 4039 94.559 . . . 0.198 . 0.153 . . . . . . . . . . 'X-RAY DIFFRACTION' 3.197 3.574 . . 181 3650 93.828 . . . 0.166 . 0.148 . . . . . . . . . . 'X-RAY DIFFRACTION' 3.574 4.124 . . 152 3237 94.983 . . . 0.157 . 0.134 . . . . . . . . . . 'X-RAY DIFFRACTION' 4.124 5.047 . . 150 2713 94.582 . . . 0.129 . 0.128 . . . . . . . . . . 'X-RAY DIFFRACTION' 5.047 7.116 . . 101 2081 93.248 . . . 0.244 . 0.188 . . . . . . . . . . 'X-RAY DIFFRACTION' 7.116 44 . . 57 1128 91.577 . . . 0.164 . 0.203 . . . . . . . . . . # _struct.entry_id 5DLT _struct.title 'Crystal structure of Autotaxin (ENPP2) with 7-alpha-hydroxycholesterol' _struct.pdbx_descriptor 'Ectonucleotide pyrophosphatase/phosphodiesterase family member 2 (E.C.3.1.4.39)' _struct.pdbx_model_details ? _struct.pdbx_formula_weight ? _struct.pdbx_formula_weight_method ? _struct.pdbx_model_type_details ? _struct.pdbx_CASP_flag ? # _struct_keywords.entry_id 5DLT _struct_keywords.text 'Autotaxin, ENPP2, LPA, steroids, bile salts, hydrolase' _struct_keywords.pdbx_keywords HYDROLASE # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 2 ? D N N 3 ? E N N 4 ? F N N 4 ? G N N 5 ? H N N 6 ? I N N 7 ? J N N 7 ? K N N 7 ? L N N 7 ? M N N 7 ? N N N 7 ? O N N 7 ? P N N 7 ? Q N N 7 ? R N N 7 ? S N N 8 ? T N N 8 ? U N N 8 ? V N N 8 ? W N N 8 ? X N N 8 ? Y N N 8 ? Z N N 8 ? AA N N 8 ? BA N N 8 ? CA N N 9 ? DA N N 9 ? EA N N 10 ? FA N N 10 ? GA N N 10 ? HA N N 10 ? IA N N 10 ? JA N N 10 ? KA N N 10 ? LA N N 8 ? MA N N 11 ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 AA1 ASP A 53 ? CYS A 58 ? ASP A 88 CYS A 93 1 ? 6 HELX_P HELX_P2 AA2 THR A 68 ? CYS A 72 ? THR A 103 CYS A 107 5 ? 5 HELX_P HELX_P3 AA3 ASP A 87 ? GLY A 92 ? ASP A 122 GLY A 127 1 ? 6 HELX_P HELX_P4 AA4 ASN A 97 ? LYS A 103 ? ASN A 132 LYS A 138 1 ? 7 HELX_P HELX_P5 AA5 HIS A 107 ? ASP A 111 ? HIS A 142 ASP A 146 5 ? 5 HELX_P HELX_P6 AA6 ARG A 139 ? GLY A 146 ? ARG A 174 GLY A 181 5 ? 8 HELX_P HELX_P7 AA7 MET A 150 ? GLY A 160 ? MET A 185 GLY A 195 1 ? 11 HELX_P HELX_P8 AA8 LYS A 173 ? GLY A 184 ? LYS A 208 GLY A 219 1 ? 12 HELX_P HELX_P9 AA9 TYR A 186 ? GLY A 191 ? TYR A 221 GLY A 226 1 ? 6 HELX_P HELX_P10 AB1 ARG A 211 ? TRP A 219 ? ARG A 246 TRP A 254 5 ? 9 HELX_P HELX_P11 AB2 PRO A 223 ? GLN A 231 ? PRO A 258 GLN A 266 1 ? 9 HELX_P HELX_P12 AB3 PRO A 245 ? SER A 258 ? PRO A 280 SER A 293 1 ? 14 HELX_P HELX_P13 AB4 ASP A 276 ? GLY A 283 ? ASP A 311 GLY A 318 1 ? 8 HELX_P HELX_P14 AB5 GLY A 286 ? GLU A 288 ? GLY A 321 GLU A 323 5 ? 3 HELX_P HELX_P15 AB6 MET A 289 ? LEU A 310 ? MET A 324 LEU A 345 1 ? 22 HELX_P HELX_P16 AB7 SER A 338 ? TYR A 340 ? SER A 373 TYR A 375 5 ? 3 HELX_P HELX_P17 AB8 ASN A 343 ? ASP A 345 ? ASN A 378 ASP A 380 5 ? 3 HELX_P HELX_P18 AB9 ASP A 368 ? LEU A 376 ? ASP A 403 LEU A 411 1 ? 9 HELX_P HELX_P19 AC1 GLN A 391 ? LEU A 393 ? GLN A 426 LEU A 428 5 ? 3 HELX_P HELX_P20 AC2 PRO A 394 ? HIS A 398 ? PRO A 429 HIS A 433 5 ? 5 HELX_P HELX_P21 AC3 VAL A 445 ? GLN A 449 ? VAL A 480 GLN A 484 5 ? 5 HELX_P HELX_P22 AC4 GLU A 472 ? LEU A 481 ? GLU A 507 LEU A 516 1 ? 10 HELX_P HELX_P23 AC5 LEU A 495 ? LEU A 499 ? LEU A 530 LEU A 534 5 ? 5 HELX_P HELX_P24 AC6 LEU A 523 ? PHE A 527 ? LEU A 558 PHE A 562 5 ? 5 HELX_P HELX_P25 AC7 ASN A 541 ? ASN A 547 ? ASN A 576 ASN A 582 5 ? 7 HELX_P HELX_P26 AC8 SER A 555 ? LEU A 561 ? SER A 590 LEU A 596 1 ? 7 HELX_P HELX_P27 AC9 PRO A 610 ? THR A 614 ? PRO A 645 THR A 649 5 ? 5 HELX_P HELX_P28 AD1 SER A 624 ? SER A 628 ? SER A 659 SER A 663 5 ? 5 HELX_P HELX_P29 AD2 ASN A 630 ? ASP A 637 ? ASN A 665 ASP A 672 1 ? 8 HELX_P HELX_P30 AD3 PRO A 647 ? SER A 651 ? PRO A 682 SER A 686 5 ? 5 HELX_P HELX_P31 AD4 SER A 653 ? TYR A 658 ? SER A 688 TYR A 693 1 ? 6 HELX_P HELX_P32 AD5 ASP A 659 ? THR A 664 ? ASP A 694 THR A 699 5 ? 6 HELX_P HELX_P33 AD6 TYR A 670 ? VAL A 683 ? TYR A 705 VAL A 718 1 ? 14 HELX_P HELX_P34 AD7 VAL A 683 ? ASN A 693 ? VAL A 718 ASN A 728 1 ? 11 HELX_P HELX_P35 AD8 THR A 713 ? ILE A 717 ? THR A 748 ILE A 752 5 ? 5 HELX_P HELX_P36 AD9 PRO A 745 ? CYS A 749 ? PRO A 780 CYS A 784 5 ? 5 HELX_P HELX_P37 AE1 ASP A 775 ? LYS A 778 ? ASP A 810 LYS A 813 5 ? 4 HELX_P HELX_P38 AE2 TRP A 779 ? HIS A 787 ? TRP A 814 HIS A 822 1 ? 9 HELX_P HELX_P39 AE3 ARG A 790 ? GLY A 799 ? ARG A 825 GLY A 834 1 ? 10 HELX_P HELX_P40 AE4 SER A 809 ? TYR A 819 ? SER A 844 TYR A 854 1 ? 11 # _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 disulf1 disulf ? ? A CYS 23 SG ? ? ? 1_555 A CYS 40 SG ? ? A CYS 58 A CYS 75 1_555 ? ? ? ? ? ? ? 2.024 ? disulf2 disulf ? ? A CYS 27 SG ? ? ? 1_555 A CYS 58 SG ? ? A CYS 62 A CYS 93 1_555 ? ? ? ? ? ? ? 2.014 ? disulf3 disulf ? ? A CYS 38 SG ? ? ? 1_555 A CYS 51 SG ? ? A CYS 73 A CYS 86 1_555 ? ? ? ? ? ? ? 2.057 ? disulf4 disulf ? ? A CYS 44 SG ? ? ? 1_555 A CYS 50 SG ? ? A CYS 79 A CYS 85 1_555 ? ? ? ? ? ? ? 2.076 ? disulf5 disulf ? ? A CYS 67 SG ? ? ? 1_555 A CYS 84 SG ? ? A CYS 102 A CYS 119 1_555 ? ? ? ? ? ? ? 2.032 ? disulf6 disulf ? ? A CYS 72 SG ? ? ? 1_555 A CYS 102 SG ? ? A CYS 107 A CYS 137 1_555 ? ? ? ? ? ? ? 2.051 ? disulf7 disulf ? ? A CYS 82 SG ? ? ? 1_555 A CYS 95 SG ? ? A CYS 117 A CYS 130 1_555 ? ? ? ? ? ? ? 2.038 ? disulf8 disulf ? ? A CYS 88 SG ? ? ? 1_555 A CYS 94 SG ? ? A CYS 123 A CYS 129 1_555 ? ? ? ? ? ? ? 2.032 ? disulf9 disulf ? ? A CYS 113 SG ? ? ? 1_555 A CYS 159 SG ? ? A CYS 148 A CYS 194 1_555 ? ? ? ? ? ? ? 2.056 ? disulf10 disulf ? ? A CYS 121 SG ? ? ? 1_555 A CYS 315 SG ? ? A CYS 156 A CYS 350 1_555 ? ? ? ? ? ? ? 2.012 ? disulf11 disulf ? ? A CYS 331 SG ? ? ? 1_555 A CYS 433 SG ? ? A CYS 366 A CYS 468 1_555 ? ? ? ? ? ? ? 2.055 ? disulf12 disulf ? ? A CYS 378 SG ? ? ? 1_555 A CYS 770 SG ? ? A CYS 413 A CYS 805 1_555 ? ? ? ? ? ? ? 2.045 ? disulf13 disulf ? ? A CYS 531 SG ? ? ? 1_555 A CYS 631 SG ? ? A CYS 566 A CYS 666 1_555 ? ? ? ? ? ? ? 2.053 ? disulf14 disulf ? ? A CYS 533 SG ? ? ? 1_555 A CYS 616 SG ? ? A CYS 568 A CYS 651 1_555 ? ? ? ? ? ? ? 2.042 ? disulf15 disulf ? ? A CYS 739 SG ? ? ? 1_555 A CYS 749 SG ? ? A CYS 774 A CYS 784 1_555 ? ? ? ? ? ? ? 2.073 ? metalc1 metalc ? ? A ASP 136 OD1 ? ? ? 1_555 F ZN . ZN ? ? A ASP 171 A ZN 905 1_555 ? ? ? ? ? ? ? 1.934 ? covale1 covale both ? A LYS 173 C ? ? ? 1_555 A TPO 174 N ? ? A LYS 208 A TPO 209 1_555 ? ? ? ? ? ? ? 1.326 ? metalc2 metalc ? ? A TPO 174 OG1 ? ? ? 1_555 F ZN . ZN ? ? A TPO 209 A ZN 905 1_555 ? ? ? ? ? ? ? 1.961 ? metalc3 metalc ? ? A TPO 174 O1P ? ? ? 1_555 F ZN . ZN ? ? A TPO 209 A ZN 905 1_555 ? ? ? ? ? ? ? 2.511 ? metalc4 metalc ? ? A TPO 174 O1P ? ? ? 1_555 E ZN . ZN ? ? A TPO 209 A ZN 904 1_555 ? ? ? ? ? ? ? 2.481 ? covale2 covale both ? A TPO 174 C ? ? ? 1_555 A PHE 175 N ? ? A TPO 209 A PHE 210 1_555 ? ? ? ? ? ? ? 1.328 ? metalc5 metalc ? ? A ASP 276 OD1 ? ? ? 1_555 E ZN . ZN ? ? A ASP 311 A ZN 904 1_555 ? ? ? ? ? ? ? 2.660 ? metalc6 metalc ? ? A ASP 276 OD2 ? ? ? 1_555 E ZN . ZN ? ? A ASP 311 A ZN 904 1_555 ? ? ? ? ? ? ? 2.050 ? metalc7 metalc ? ? A HIS 280 NE2 ? ? ? 1_555 E ZN . ZN ? ? A HIS 315 A ZN 904 1_555 ? ? ? ? ? ? ? 2.055 ? metalc8 metalc ? ? A ASP 323 OD2 ? ? ? 1_555 F ZN . ZN ? ? A ASP 358 A ZN 905 1_555 ? ? ? ? ? ? ? 2.159 ? metalc9 metalc ? ? A HIS 324 NE2 ? ? ? 1_555 F ZN . ZN ? ? A HIS 359 A ZN 905 1_555 ? ? ? ? ? ? ? 2.008 ? metalc10 metalc ? ? A HIS 439 NE2 ? ? ? 1_555 E ZN . ZN ? ? A HIS 474 A ZN 904 1_555 ? ? ? ? ? ? ? 2.043 ? covale3 covale one ? A ASN 489 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 524 A NAG 901 1_555 ? ? ? ? ? ? ? 1.422 ? metalc11 metalc ? ? A TYR 634 O ? ? ? 1_555 CA NA . NA ? ? A TYR 669 A NA 928 1_555 ? ? ? ? ? ? ? 2.376 ? metalc12 metalc ? ? A ASP 637 O ? ? ? 1_555 CA NA . NA ? ? A ASP 672 A NA 928 1_555 ? ? ? ? ? ? ? 2.310 ? metalc13 metalc ? ? A MET 640 O ? ? ? 1_555 CA NA . NA ? ? A MET 675 A NA 928 1_555 ? ? ? ? ? ? ? 2.218 ? metalc14 metalc ? ? A ASP 704 OD1 ? ? ? 1_555 H CA . CA ? ? A ASP 739 A CA 907 1_555 ? ? ? ? ? ? ? 2.315 ? metalc15 metalc ? ? A ASN 706 OD1 ? ? ? 1_555 H CA . CA ? ? A ASN 741 A CA 907 1_555 ? ? ? ? ? ? ? 2.317 ? metalc16 metalc ? ? A ASP 708 OD1 ? ? ? 1_555 H CA . CA ? ? A ASP 743 A CA 907 1_555 ? ? ? ? ? ? ? 2.404 ? metalc17 metalc ? ? A LEU 710 O ? ? ? 1_555 H CA . CA ? ? A LEU 745 A CA 907 1_555 ? ? ? ? ? ? ? 2.356 ? metalc18 metalc ? ? A ASP 712 OD1 ? ? ? 1_555 H CA . CA ? ? A ASP 747 A CA 907 1_555 ? ? ? ? ? ? ? 2.296 ? metalc19 metalc ? ? A ASN 766 O ? ? ? 1_555 DA NA . NA ? ? A ASN 801 A NA 929 1_555 ? ? ? ? ? ? ? 2.441 ? metalc20 metalc ? ? A SER 769 O ? ? ? 1_555 DA NA . NA ? ? A SER 804 A NA 929 1_555 ? ? ? ? ? ? ? 2.383 ? metalc21 metalc ? ? A SER 772 OG ? ? ? 1_555 DA NA . NA ? ? A SER 807 A NA 929 1_555 ? ? ? ? ? ? ? 2.417 ? covale4 covale both ? B NAG . O4 ? ? ? 1_555 C NAG . C1 ? ? A NAG 901 A NAG 902 1_555 ? ? ? ? ? ? ? 1.418 ? covale5 covale both ? C NAG . O4 ? ? ? 1_555 D BMA . C1 ? ? A NAG 902 A BMA 903 1_555 ? ? ? ? ? ? ? 1.450 ? metalc22 metalc ? ? E ZN . ZN ? ? ? 1_555 MA HOH . O ? ? A ZN 904 A HOH 1236 1_555 ? ? ? ? ? ? ? 2.100 ? metalc23 metalc ? ? H CA . CA ? ? ? 1_555 MA HOH . O ? ? A CA 907 A HOH 1318 1_555 ? ? ? ? ? ? ? 2.324 ? metalc24 metalc ? ? CA NA . NA ? ? ? 1_555 FA GOL . O2 ? ? A NA 928 A GOL 931 1_555 ? ? ? ? ? ? ? 2.363 ? metalc25 metalc ? ? CA NA . NA ? ? ? 1_555 MA HOH . O ? ? A NA 928 A HOH 1357 1_555 ? ? ? ? ? ? ? 2.423 ? metalc26 metalc ? ? CA NA . NA ? ? ? 1_555 MA HOH . O ? ? A NA 928 A HOH 1414 1_555 ? ? ? ? ? ? ? 2.822 ? metalc27 metalc ? ? DA NA . NA ? ? ? 1_555 MA HOH . O ? ? A NA 929 A HOH 1361 1_555 ? ? ? ? ? ? ? 2.291 ? metalc28 metalc ? ? DA NA . NA ? ? ? 1_555 MA HOH . O ? ? A NA 929 A HOH 1400 1_555 ? ? ? ? ? ? ? 2.350 ? metalc29 metalc ? ? DA NA . NA ? ? ? 1_555 MA HOH . O ? ? A NA 929 A HOH 1438 1_555 ? ? ? ? ? ? ? 2.407 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? metalc ? ? covale ? ? # 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 PRO 35 A . ? PRO 70 A PRO 36 A ? PRO 71 A 1 6.44 2 TYR 170 A . ? TYR 205 A PRO 171 A ? PRO 206 A 1 -10.79 3 GLN 274 A . ? GLN 309 A PRO 275 A ? PRO 310 A 1 9.62 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA1 ? 6 ? AA2 ? 2 ? AA3 ? 2 ? AA4 ? 2 ? AA5 ? 2 ? AA6 ? 4 ? AA7 ? 2 ? AA8 ? 7 ? AA9 ? 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 AA1 1 2 ? parallel AA1 2 3 ? parallel AA1 3 4 ? anti-parallel AA1 4 5 ? anti-parallel AA1 5 6 ? parallel AA2 1 2 ? parallel AA3 1 2 ? anti-parallel AA4 1 2 ? anti-parallel AA5 1 2 ? parallel AA6 1 2 ? anti-parallel AA6 2 3 ? anti-parallel AA6 3 4 ? anti-parallel AA7 1 2 ? anti-parallel AA8 1 2 ? anti-parallel AA8 2 3 ? anti-parallel AA8 3 4 ? anti-parallel AA8 4 5 ? anti-parallel AA8 5 6 ? anti-parallel AA8 6 7 ? anti-parallel AA9 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 AA1 1 VAL A 267 ? PRO A 275 ? VAL A 302 PRO A 310 AA1 2 LEU A 130 ? ASP A 136 ? LEU A 165 ASP A 171 AA1 3 ASN A 317 ? GLY A 322 ? ASN A 352 GLY A 357 AA1 4 PHE A 452 ? TYR A 455 ? PHE A 487 TYR A 490 AA1 5 THR A 161 ? HIS A 162 ? THR A 196 HIS A 197 AA1 6 THR A 463 ? LYS A 464 ? THR A 498 LYS A 499 AA2 1 MET A 166 ? ARG A 167 ? MET A 201 ARG A 202 AA2 2 PHE A 468 ? GLU A 469 ? PHE A 503 GLU A 504 AA3 1 MET A 197 ? ASP A 199 ? MET A 232 ASP A 234 AA3 2 ALA A 204 ? PHE A 206 ? ALA A 239 PHE A 241 AA4 1 GLU A 327 ? ASP A 328 ? GLU A 362 ASP A 363 AA4 2 GLY A 437 ? ASP A 438 ? GLY A 472 ASP A 473 AA5 1 THR A 334 ? PHE A 336 ? THR A 369 PHE A 371 AA5 2 HIS A 417 ? ALA A 419 ? HIS A 452 ALA A 454 AA6 1 ILE A 347 ? VAL A 350 ? ILE A 382 VAL A 385 AA6 2 LEU A 354 ? ALA A 359 ? LEU A 389 ALA A 394 AA6 3 ILE A 408 ? VAL A 412 ? ILE A 443 VAL A 447 AA6 4 PHE A 385 ? MET A 389 ? PHE A 420 MET A 424 AA7 1 ALA A 567 ? VAL A 568 ? ALA A 602 VAL A 603 AA7 2 LEU A 800 ? ASP A 801 ? LEU A 835 ASP A 836 AA8 1 TYR A 574 ? TYR A 578 ? TYR A 609 TYR A 613 AA8 2 GLU A 583 ? SER A 587 ? GLU A 618 SER A 622 AA8 3 PRO A 593 ? ILE A 600 ? PRO A 628 ILE A 635 AA8 4 VAL A 695 ? ILE A 702 ? VAL A 730 ILE A 737 AA8 5 HIS A 731 ? CYS A 739 ? HIS A 766 CYS A 774 AA8 6 LEU A 753 ? PRO A 761 ? LEU A 788 PRO A 796 AA8 7 THR A 788 ? ALA A 789 ? THR A 823 ALA A 824 AA9 1 SER A 641 ? PHE A 644 ? SER A 676 PHE A 679 AA9 2 MET A 666 ? MET A 669 ? MET A 701 MET 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 AA1 1 2 O PHE A 270 ? O PHE A 305 N SER A 134 ? N SER A 169 AA1 2 3 N PHE A 133 ? N PHE A 168 O ILE A 319 ? O ILE A 354 AA1 3 4 N VAL A 318 ? N VAL A 353 O TYR A 455 ? O TYR A 490 AA1 4 5 O GLY A 454 ? O GLY A 489 N THR A 161 ? N THR A 196 AA1 5 6 N HIS A 162 ? N HIS A 197 O THR A 463 ? O THR A 498 AA2 1 2 N ARG A 167 ? N ARG A 202 O PHE A 468 ? O PHE A 503 AA3 1 2 N MET A 197 ? N MET A 232 O PHE A 206 ? O PHE A 241 AA4 1 2 N GLU A 327 ? N GLU A 362 O ASP A 438 ? O ASP A 473 AA5 1 2 N GLU A 335 ? N GLU A 370 O ALA A 419 ? O ALA A 454 AA6 1 2 N THR A 348 ? N THR A 383 O ARG A 358 ? O ARG A 393 AA6 2 3 N GLY A 355 ? N GLY A 390 O LEU A 410 ? O LEU A 445 AA6 3 4 O HIS A 409 ? O HIS A 444 N TYR A 388 ? N TYR A 423 AA7 1 2 N ALA A 567 ? N ALA A 602 O ASP A 801 ? O ASP A 836 AA8 1 2 N ASP A 575 ? N ASP A 610 O TYR A 586 ? O TYR A 621 AA8 2 3 N GLU A 583 ? N GLU A 618 O SER A 597 ? O SER A 632 AA8 3 4 N TYR A 598 ? N TYR A 633 O VAL A 697 ? O VAL A 732 AA8 4 5 N ASN A 696 ? N ASN A 731 O THR A 737 ? O THR A 772 AA8 5 6 N ILE A 736 ? N ILE A 771 O SER A 756 ? O SER A 791 AA8 6 7 N SER A 757 ? N SER A 792 O ALA A 789 ? O ALA A 824 AA9 1 2 N GLY A 643 ? N GLY A 678 O VAL A 667 ? O VAL A 702 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software A ZN 904 ? 5 'binding site for residue ZN A 904' AC2 Software A ZN 905 ? 4 'binding site for residue ZN A 905' AC3 Software A 5JK 906 ? 12 'binding site for residue 5JK A 906' AC4 Software A CA 907 ? 6 'binding site for residue CA A 907' AC5 Software A IOD 908 ? 2 'binding site for residue IOD A 908' AC6 Software A IOD 909 ? 2 'binding site for residue IOD A 909' AC7 Software A IOD 910 ? 1 'binding site for residue IOD A 910' AC8 Software A IOD 911 ? 1 'binding site for residue IOD A 911' AC9 Software A IOD 912 ? 2 'binding site for residue IOD A 912' AD1 Software A IOD 913 ? 2 'binding site for residue IOD A 913' AD2 Software A IOD 914 ? 2 'binding site for residue IOD A 914' AD3 Software A IOD 915 ? 1 'binding site for residue IOD A 915' AD4 Software A IOD 916 ? 1 'binding site for residue IOD A 916' AD5 Software A IOD 917 ? 2 'binding site for residue IOD A 917' AD6 Software A SCN 918 ? 2 'binding site for residue SCN A 918' AD7 Software A SCN 919 ? 5 'binding site for residue SCN A 919' AD8 Software A SCN 920 ? 3 'binding site for residue SCN A 920' AD9 Software A SCN 921 ? 5 'binding site for residue SCN A 921' AE1 Software A SCN 922 ? 2 'binding site for residue SCN A 922' AE2 Software A SCN 923 ? 8 'binding site for residue SCN A 923' AE3 Software A SCN 924 ? 4 'binding site for residue SCN A 924' AE4 Software A SCN 926 ? 5 'binding site for residue SCN A 926' AE5 Software A SCN 927 ? 2 'binding site for residue SCN A 927' AE6 Software A NA 928 ? 6 'binding site for residue NA A 928' AE7 Software A NA 929 ? 6 'binding site for residue NA A 929' AE8 Software A GOL 930 ? 3 'binding site for residue GOL A 930' AE9 Software A GOL 931 ? 6 'binding site for residue GOL A 931' AF1 Software A GOL 932 ? 4 'binding site for residue GOL A 932' AF2 Software A GOL 933 ? 9 'binding site for residue GOL A 933' AF3 Software A GOL 934 ? 3 'binding site for residue GOL A 934' AF4 Software A GOL 935 ? 10 'binding site for residue GOL A 935' AF5 Software A GOL 936 ? 9 'binding site for residue GOL A 936' AF6 Software A SCN 937 ? 6 'binding site for residue SCN A 937' AF7 Software A ASN 524 ? 13 'binding site for Poly-Saccharide residues NAG A 901 through BMA A 903 bound to ASN A 524' # 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 TPO A 174 ? TPO A 209 . ? 1_555 ? 2 AC1 5 ASP A 276 ? ASP A 311 . ? 1_555 ? 3 AC1 5 HIS A 280 ? HIS A 315 . ? 1_555 ? 4 AC1 5 HIS A 439 ? HIS A 474 . ? 1_555 ? 5 AC1 5 HOH MA . ? HOH A 1236 . ? 1_555 ? 6 AC2 4 ASP A 136 ? ASP A 171 . ? 1_555 ? 7 AC2 4 TPO A 174 ? TPO A 209 . ? 1_555 ? 8 AC2 4 ASP A 323 ? ASP A 358 . ? 1_555 ? 9 AC2 4 HIS A 324 ? HIS A 359 . ? 1_555 ? 10 AC3 12 LEU A 43 ? LEU A 78 . ? 1_555 ? 11 AC3 12 TYR A 179 ? TYR A 214 . ? 1_555 ? 12 AC3 12 LYS A 213 ? LYS A 248 . ? 1_555 ? 13 AC3 12 TRP A 219 ? TRP A 254 . ? 1_555 ? 14 AC3 12 TRP A 225 ? TRP A 260 . ? 1_555 ? 15 AC3 12 ILE A 226 ? ILE A 261 . ? 1_555 ? 16 AC3 12 TRP A 240 ? TRP A 275 . ? 1_555 ? 17 AC3 12 PHE A 742 ? PHE A 777 . ? 1_655 ? 18 AC3 12 THR A 743 ? THR A 778 . ? 1_655 ? 19 AC3 12 SCN T . ? SCN A 919 . ? 1_555 ? 20 AC3 12 HOH MA . ? HOH A 1002 . ? 1_555 ? 21 AC3 12 HOH MA . ? HOH A 1114 . ? 1_555 ? 22 AC4 6 ASP A 704 ? ASP A 739 . ? 1_555 ? 23 AC4 6 ASN A 706 ? ASN A 741 . ? 1_555 ? 24 AC4 6 ASP A 708 ? ASP A 743 . ? 1_555 ? 25 AC4 6 LEU A 710 ? LEU A 745 . ? 1_555 ? 26 AC4 6 ASP A 712 ? ASP A 747 . ? 1_555 ? 27 AC4 6 HOH MA . ? HOH A 1318 . ? 1_555 ? 28 AC5 2 ASN A 195 ? ASN A 230 . ? 1_555 ? 29 AC5 2 ARG A 356 ? ARG A 391 . ? 1_555 ? 30 AC6 2 MET A 197 ? MET A 232 . ? 1_555 ? 31 AC6 2 ARG A 358 ? ARG A 393 . ? 1_555 ? 32 AC7 1 ARG A 127 ? ARG A 162 . ? 1_555 ? 33 AC8 1 ARG A 217 ? ARG A 252 . ? 1_555 ? 34 AC9 2 GLN A 99 ? GLN A 134 . ? 1_556 ? 35 AC9 2 HOH MA . ? HOH A 1287 . ? 1_556 ? 36 AD1 2 LEU A 529 ? LEU A 564 . ? 1_555 ? 37 AD1 2 PRO A 619 ? PRO A 654 . ? 1_555 ? 38 AD2 2 ASN A 541 ? ASN A 576 . ? 1_555 ? 39 AD2 2 ASN A 547 ? ASN A 582 . ? 1_555 ? 40 AD3 1 LEU A 753 ? LEU A 788 . ? 1_555 ? 41 AD4 1 ASP A 747 ? ASP A 782 . ? 1_555 ? 42 AD5 2 ARG A 505 ? ARG A 540 . ? 1_555 ? 43 AD5 2 SER A 811 ? SER A 846 . ? 1_555 ? 44 AD6 2 TYR A 642 ? TYR A 677 . ? 1_555 ? 45 AD6 2 LYS A 674 ? LYS A 709 . ? 1_555 ? 46 AD7 5 TRP A 225 ? TRP A 260 . ? 1_555 ? 47 AD7 5 PHE A 238 ? PHE A 273 . ? 1_555 ? 48 AD7 5 PHE A 239 ? PHE A 274 . ? 1_555 ? 49 AD7 5 5JK G . ? 5JK A 906 . ? 1_555 ? 50 AD7 5 HOH MA . ? HOH A 1307 . ? 1_555 ? 51 AD8 3 LYS A 45 ? LYS A 80 . ? 1_555 ? 52 AD8 3 VAL A 242 ? VAL A 277 . ? 1_555 ? 53 AD8 3 SER A 243 ? SER A 278 . ? 1_555 ? 54 AD9 5 HIS A 246 ? HIS A 281 . ? 1_555 ? 55 AD9 5 SER A 272 ? SER A 307 . ? 1_555 ? 56 AD9 5 ILE A 296 ? ILE A 331 . ? 1_555 ? 57 AD9 5 THR A 299 ? THR A 334 . ? 1_555 ? 58 AD9 5 HOH MA . ? HOH A 1126 . ? 1_555 ? 59 AE1 2 TYR A 461 ? TYR A 496 . ? 1_555 ? 60 AE1 2 ARG A 500 ? ARG A 535 . ? 1_555 ? 61 AE2 8 HIS A 190 ? HIS A 225 . ? 1_555 ? 62 AE2 8 ARG A 217 ? ARG A 252 . ? 1_555 ? 63 AE2 8 TRP A 218 ? TRP A 253 . ? 1_555 ? 64 AE2 8 GLY A 220 ? GLY A 255 . ? 1_555 ? 65 AE2 8 ARG A 404 ? ARG A 439 . ? 1_555 ? 66 AE2 8 LYS A 602 ? LYS A 637 . ? 1_655 ? 67 AE2 8 GOL JA . ? GOL A 935 . ? 1_655 ? 68 AE2 8 HOH MA . ? HOH A 1018 . ? 1_555 ? 69 AE3 4 PRO A 287 ? PRO A 322 . ? 1_545 ? 70 AE3 4 THR A 572 ? THR A 607 . ? 1_555 ? 71 AE3 4 SER A 573 ? SER A 608 . ? 1_555 ? 72 AE3 4 ILE A 589 ? ILE A 624 . ? 1_555 ? 73 AE4 5 LYS A 45 ? LYS A 80 . ? 1_555 ? 74 AE4 5 SER A 48 ? SER A 83 . ? 1_555 ? 75 AE4 5 SER A 49 ? SER A 84 . ? 1_555 ? 76 AE4 5 CYS A 50 ? CYS A 85 . ? 1_555 ? 77 AE4 5 ASP A 55 ? ASP A 90 . ? 1_555 ? 78 AE5 2 THR A 713 ? THR A 748 . ? 1_555 ? 79 AE5 2 GLU A 714 ? GLU A 749 . ? 1_555 ? 80 AE6 6 TYR A 634 ? TYR A 669 . ? 1_555 ? 81 AE6 6 ASP A 637 ? ASP A 672 . ? 1_555 ? 82 AE6 6 MET A 640 ? MET A 675 . ? 1_555 ? 83 AE6 6 GOL FA . ? GOL A 931 . ? 1_555 ? 84 AE6 6 HOH MA . ? HOH A 1357 . ? 1_555 ? 85 AE6 6 HOH MA . ? HOH A 1414 . ? 1_555 ? 86 AE7 6 ASN A 766 ? ASN A 801 . ? 1_555 ? 87 AE7 6 SER A 769 ? SER A 804 . ? 1_555 ? 88 AE7 6 SER A 772 ? SER A 807 . ? 1_555 ? 89 AE7 6 HOH MA . ? HOH A 1361 . ? 1_555 ? 90 AE7 6 HOH MA . ? HOH A 1400 . ? 1_555 ? 91 AE7 6 HOH MA . ? HOH A 1438 . ? 1_555 ? 92 AE8 3 PRO A 506 ? PRO A 541 . ? 1_555 ? 93 AE8 3 THR A 507 ? THR A 542 . ? 1_555 ? 94 AE8 3 MET A 508 ? MET A 543 . ? 1_555 ? 95 AE9 6 TYR A 634 ? TYR A 669 . ? 1_555 ? 96 AE9 6 LYS A 635 ? LYS A 670 . ? 1_555 ? 97 AE9 6 MET A 640 ? MET A 675 . ? 1_555 ? 98 AE9 6 SER A 641 ? SER A 676 . ? 1_555 ? 99 AE9 6 TYR A 642 ? TYR A 677 . ? 1_555 ? 100 AE9 6 NA CA . ? NA A 928 . ? 1_555 ? 101 AF1 4 PRO A 487 ? PRO A 522 . ? 1_555 ? 102 AF1 4 NAG B . ? NAG A 901 . ? 1_555 ? 103 AF1 4 NAG C . ? NAG A 902 . ? 1_555 ? 104 AF1 4 HOH MA . ? HOH A 1105 . ? 1_555 ? 105 AF2 9 CYS A 88 ? CYS A 123 . ? 1_555 ? 106 AF2 9 GLY A 92 ? GLY A 127 . ? 1_555 ? 107 AF2 9 ASP A 93 ? ASP A 128 . ? 1_555 ? 108 AF2 9 CYS A 94 ? CYS A 129 . ? 1_555 ? 109 AF2 9 LEU A 251 ? LEU A 286 . ? 1_555 ? 110 AF2 9 LEU A 254 ? LEU A 289 . ? 1_555 ? 111 AF2 9 GLY A 306 ? GLY A 341 . ? 1_555 ? 112 AF2 9 GLN A 309 ? GLN A 344 . ? 1_555 ? 113 AF2 9 LEU A 310 ? LEU A 345 . ? 1_555 ? 114 AF3 3 PRO A 36 ? PRO A 71 . ? 1_455 ? 115 AF3 3 PRO A 164 ? PRO A 199 . ? 1_555 ? 116 AF3 3 TYR A 165 ? TYR A 200 . ? 1_555 ? 117 AF4 10 HIS A 216 ? HIS A 251 . ? 1_455 ? 118 AF4 10 ARG A 217 ? ARG A 252 . ? 1_455 ? 119 AF4 10 TRP A 219 ? TRP A 254 . ? 1_455 ? 120 AF4 10 LYS A 602 ? LYS A 637 . ? 1_555 ? 121 AF4 10 SER A 690 ? SER A 725 . ? 1_555 ? 122 AF4 10 GLU A 691 ? GLU A 726 . ? 1_555 ? 123 AF4 10 ASN A 693 ? ASN A 728 . ? 1_555 ? 124 AF4 10 PHE A 742 ? PHE A 777 . ? 1_555 ? 125 AF4 10 SCN X . ? SCN A 923 . ? 1_455 ? 126 AF4 10 HOH MA . ? HOH A 1101 . ? 1_455 ? 127 AF5 9 PRO A 351 ? PRO A 386 . ? 1_555 ? 128 AF5 9 GLY A 352 ? GLY A 387 . ? 1_555 ? 129 AF5 9 HIS A 417 ? HIS A 452 . ? 1_555 ? 130 AF5 9 VAL A 418 ? VAL A 453 . ? 1_555 ? 131 AF5 9 ALA A 419 ? ALA A 454 . ? 1_555 ? 132 AF5 9 LYS A 542 ? LYS A 577 . ? 1_665 ? 133 AF5 9 HOH MA . ? HOH A 1007 . ? 1_555 ? 134 AF5 9 HOH MA . ? HOH A 1298 . ? 1_555 ? 135 AF5 9 HOH MA . ? HOH A 1403 . ? 1_555 ? 136 AF6 6 VAL A 412 ? VAL A 447 . ? 1_555 ? 137 AF6 6 ARG A 414 ? ARG A 449 . ? 1_555 ? 138 AF6 6 ASP A 442 ? ASP A 477 . ? 1_555 ? 139 AF6 6 VAL A 445 ? VAL A 480 . ? 1_555 ? 140 AF6 6 HOH MA . ? HOH A 1276 . ? 1_555 ? 141 AF6 6 HOH MA . ? HOH A 1284 . ? 1_555 ? 142 AF7 13 LEU A 185 ? LEU A 220 . ? 1_555 ? 143 AF7 13 PRO A 487 ? PRO A 522 . ? 1_555 ? 144 AF7 13 ASN A 489 ? ASN A 524 . ? 1_555 ? 145 AF7 13 LEU A 710 ? LEU A 745 . ? 1_555 ? 146 AF7 13 HIS A 796 ? HIS A 831 . ? 1_555 ? 147 AF7 13 GOL GA . ? GOL A 932 . ? 1_555 ? 148 AF7 13 HOH MA . ? HOH A 1001 . ? 1_555 ? 149 AF7 13 HOH MA . ? HOH A 1049 . ? 1_555 ? 150 AF7 13 HOH MA . ? HOH A 1054 . ? 1_555 ? 151 AF7 13 HOH MA . ? HOH A 1083 . ? 1_555 ? 152 AF7 13 HOH MA . ? HOH A 1120 . ? 1_555 ? 153 AF7 13 HOH MA . ? HOH A 1204 . ? 1_555 ? 154 AF7 13 HOH MA . ? HOH A 1211 . ? 1_555 ? # _atom_sites.entry_id 5DLT _atom_sites.fract_transf_matrix[1][1] 0.018632 _atom_sites.fract_transf_matrix[1][2] 0.003275 _atom_sites.fract_transf_matrix[1][3] 0.006095 _atom_sites.fract_transf_matrix[2][1] -0.000000 _atom_sites.fract_transf_matrix[2][2] 0.015994 _atom_sites.fract_transf_matrix[2][3] 0.003431 _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] 0.015031 _atom_sites.fract_transf_vector[1] 0.000000 _atom_sites.fract_transf_vector[2] 0.000000 _atom_sites.fract_transf_vector[3] 0.000000 # loop_ _atom_type.symbol _atom_type.scat_Cromer_Mann_a1 _atom_type.scat_Cromer_Mann_b1 _atom_type.scat_Cromer_Mann_a2 _atom_type.scat_Cromer_Mann_b2 _atom_type.scat_Cromer_Mann_a3 _atom_type.scat_Cromer_Mann_b3 _atom_type.scat_Cromer_Mann_a4 _atom_type.scat_Cromer_Mann_b4 _atom_type.scat_Cromer_Mann_c C 2.310 20.844 1.020 10.208 1.589 0.569 0.865 51.651 0.216 CA 8.627 10.442 7.387 0.660 1.590 85.748 1.021 178.437 1.669 H 0.493 10.511 0.323 26.126 0.140 3.142 0.041 57.800 0.003 I 20.147 4.347 18.995 0.381 7.514 27.766 2.273 66.878 3.748 N 12.213 0.006 3.132 9.893 2.013 28.997 1.166 0.583 -11.529 NA 4.763 3.285 3.174 8.842 1.267 0.314 1.113 129.424 0.733 O 3.049 13.277 2.287 5.701 1.546 0.324 0.867 32.909 0.251 P 6.435 1.907 4.179 27.157 1.780 0.526 1.491 68.164 1.268 S 6.905 1.468 5.203 22.215 1.438 0.254 1.586 56.172 1.050 ZN 14.074 3.266 7.032 0.233 5.162 10.316 2.410 58.710 0.992 # 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 . GLY A 1 21 ? 47.048 8.718 19.717 1.00 48.89 ? 56 GLY A N 1 ATOM 2 C CA . GLY A 1 21 ? 46.828 9.783 20.750 1.00 48.74 ? 56 GLY A CA 1 ATOM 3 C C . GLY A 1 21 ? 45.696 10.789 20.555 1.00 48.57 ? 56 GLY A C 1 ATOM 4 O O . GLY A 1 21 ? 45.484 11.639 21.428 1.00 50.20 ? 56 GLY A O 1 ATOM 5 N N . SER A 1 22 ? 44.948 10.676 19.451 1.00 46.71 ? 57 SER A N 1 ATOM 6 C CA . SER A 1 22 ? 43.962 11.678 19.032 1.00 44.69 ? 57 SER A CA 1 ATOM 7 C C . SER A 1 22 ? 42.712 11.001 18.471 1.00 41.80 ? 57 SER A C 1 ATOM 8 O O . SER A 1 22 ? 42.793 9.911 17.895 1.00 40.89 ? 57 SER A O 1 ATOM 9 C CB . SER A 1 22 ? 44.569 12.567 17.946 1.00 45.64 ? 57 SER A CB 1 ATOM 10 O OG . SER A 1 22 ? 43.664 13.580 17.524 1.00 45.38 ? 57 SER A OG 1 ATOM 11 N N . CYS A 1 23 ? 41.566 11.656 18.618 1.00 39.31 ? 58 CYS A N 1 ATOM 12 C CA . CYS A 1 23 ? 40.302 11.116 18.091 1.00 40.34 ? 58 CYS A CA 1 ATOM 13 C C . CYS A 1 23 ? 39.956 11.604 16.674 1.00 42.19 ? 58 CYS A C 1 ATOM 14 O O . CYS A 1 23 ? 38.908 11.238 16.148 1.00 40.51 ? 58 CYS A O 1 ATOM 15 C CB . CYS A 1 23 ? 39.148 11.366 19.084 1.00 37.62 ? 58 CYS A CB 1 ATOM 16 S SG . CYS A 1 23 ? 39.243 10.371 20.604 1.00 35.84 ? 58 CYS A SG 1 ATOM 17 N N . LYS A 1 24 ? 40.840 12.375 16.031 1.00 46.53 ? 59 LYS A N 1 ATOM 18 C CA . LYS A 1 24 ? 40.584 12.846 14.663 1.00 48.20 ? 59 LYS A CA 1 ATOM 19 C C . LYS A 1 24 ? 40.305 11.653 13.757 1.00 46.15 ? 59 LYS A C 1 ATOM 20 O O . LYS A 1 24 ? 41.114 10.731 13.678 1.00 44.28 ? 59 LYS A O 1 ATOM 21 C CB . LYS A 1 24 ? 41.767 13.661 14.123 1.00 56.00 ? 59 LYS A CB 1 ATOM 22 C CG . LYS A 1 24 ? 41.430 14.512 12.900 1.00 60.59 ? 59 LYS A CG 1 ATOM 23 C CD . LYS A 1 24 ? 42.670 15.090 12.221 1.00 65.89 ? 59 LYS A CD 1 ATOM 24 C CE . LYS A 1 24 ? 43.445 16.063 13.107 1.00 69.58 ? 59 LYS A CE 1 ATOM 25 N NZ . LYS A 1 24 ? 42.623 17.218 13.569 1.00 70.63 ? 59 LYS A NZ 1 ATOM 26 N N . GLY A 1 25 ? 39.131 11.652 13.122 1.00 45.64 ? 60 GLY A N 1 ATOM 27 C CA . GLY A 1 25 ? 38.705 10.546 12.257 1.00 43.81 ? 60 GLY A CA 1 ATOM 28 C C . GLY A 1 25 ? 38.303 9.269 12.981 1.00 43.41 ? 60 GLY A C 1 ATOM 29 O O . GLY A 1 25 ? 38.151 8.226 12.339 1.00 46.73 ? 60 GLY A O 1 ATOM 30 N N . ARG A 1 26 ? 38.121 9.340 14.303 1.00 41.55 ? 61 ARG A N 1 ATOM 31 C CA . ARG A 1 26 ? 37.838 8.165 15.129 1.00 38.47 ? 61 ARG A CA 1 ATOM 32 C C . ARG A 1 26 ? 36.624 8.302 16.055 1.00 35.29 ? 61 ARG A C 1 ATOM 33 O O . ARG A 1 26 ? 36.332 7.384 16.808 1.00 32.05 ? 61 ARG A O 1 ATOM 34 C CB . ARG A 1 26 ? 39.065 7.842 15.988 1.00 40.26 ? 61 ARG A CB 1 ATOM 35 C CG . ARG A 1 26 ? 40.299 7.414 15.213 1.00 40.31 ? 61 ARG A CG 1 ATOM 36 C CD . ARG A 1 26 ? 41.479 7.236 16.148 1.00 39.89 ? 61 ARG A CD 1 ATOM 37 N NE . ARG A 1 26 ? 41.193 6.282 17.223 1.00 38.01 ? 61 ARG A NE 1 ATOM 38 C CZ . ARG A 1 26 ? 41.774 6.271 18.424 1.00 37.10 ? 61 ARG A CZ 1 ATOM 39 N NH1 . ARG A 1 26 ? 42.718 7.158 18.758 1.00 37.71 ? 61 ARG A NH1 1 ATOM 40 N NH2 . ARG A 1 26 ? 41.403 5.361 19.310 1.00 33.86 ? 61 ARG A NH2 1 ATOM 41 N N . CYS A 1 27 ? 35.899 9.416 16.005 1.00 36.60 ? 62 CYS A N 1 ATOM 42 C CA . CYS A 1 27 ? 34.824 9.642 16.961 1.00 35.39 ? 62 CYS A CA 1 ATOM 43 C C . CYS A 1 27 ? 33.741 8.586 16.867 1.00 32.60 ? 62 CYS A C 1 ATOM 44 O O . CYS A 1 27 ? 33.251 8.292 15.791 1.00 31.67 ? 62 CYS A O 1 ATOM 45 C CB . CYS A 1 27 ? 34.210 11.017 16.773 1.00 38.65 ? 62 CYS A CB 1 ATOM 46 S SG . CYS A 1 27 ? 35.346 12.317 17.270 1.00 45.71 ? 62 CYS A SG 1 ATOM 47 N N . PHE A 1 28 ? 33.420 7.990 18.012 1.00 30.72 ? 63 PHE A N 1 ATOM 48 C CA . PHE A 1 28 ? 32.464 6.901 18.106 1.00 31.60 ? 63 PHE A CA 1 ATOM 49 C C . PHE A 1 28 ? 32.748 5.733 17.178 1.00 32.34 ? 63 PHE A C 1 ATOM 50 O O . PHE A 1 28 ? 31.824 5.019 16.779 1.00 30.50 ? 63 PHE A O 1 ATOM 51 C CB . PHE A 1 28 ? 31.043 7.437 17.933 1.00 31.78 ? 63 PHE A CB 1 ATOM 52 C CG . PHE A 1 28 ? 30.738 8.551 18.874 1.00 31.25 ? 63 PHE A CG 1 ATOM 53 C CD1 . PHE A 1 28 ? 30.453 8.286 20.205 1.00 32.96 ? 63 PHE A CD1 1 ATOM 54 C CD2 . PHE A 1 28 ? 30.825 9.872 18.458 1.00 34.10 ? 63 PHE A CD2 1 ATOM 55 C CE1 . PHE A 1 28 ? 30.212 9.321 21.091 1.00 32.73 ? 63 PHE A CE1 1 ATOM 56 C CE2 . PHE A 1 28 ? 30.591 10.909 19.339 1.00 32.94 ? 63 PHE A CE2 1 ATOM 57 C CZ . PHE A 1 28 ? 30.283 10.636 20.655 1.00 34.31 ? 63 PHE A CZ 1 ATOM 58 N N . GLU A 1 29 ? 34.034 5.509 16.889 1.00 32.88 ? 64 GLU A N 1 ATOM 59 C CA . GLU A 1 29 ? 34.459 4.377 16.066 1.00 33.19 ? 64 GLU A CA 1 ATOM 60 C C . GLU A 1 29 ? 34.007 3.076 16.724 1.00 31.86 ? 64 GLU A C 1 ATOM 61 O O . GLU A 1 29 ? 33.956 2.986 17.946 1.00 30.53 ? 64 GLU A O 1 ATOM 62 C CB . GLU A 1 29 ? 35.990 4.354 15.878 1.00 35.19 ? 64 GLU A CB 1 ATOM 63 C CG . GLU A 1 29 ? 36.752 3.940 17.135 1.00 38.25 ? 64 GLU A CG 1 ATOM 64 C CD . GLU A 1 29 ? 38.252 4.223 17.102 1.00 42.98 ? 64 GLU A CD 1 ATOM 65 O OE1 . GLU A 1 29 ? 38.808 4.601 16.045 1.00 43.16 ? 64 GLU A OE1 1 ATOM 66 O OE2 . GLU A 1 29 ? 38.873 4.061 18.174 1.00 42.96 ? 64 GLU A OE2 1 ATOM 67 N N . LEU A 1 30 ? 33.675 2.088 15.895 1.00 34.37 ? 65 LEU A N 1 ATOM 68 C CA . LEU A 1 30 ? 33.280 0.750 16.358 1.00 38.04 ? 65 LEU A CA 1 ATOM 69 C C . LEU A 1 30 ? 34.485 -0.162 16.649 1.00 43.45 ? 65 LEU A C 1 ATOM 70 O O . LEU A 1 30 ? 34.349 -1.146 17.371 1.00 46.74 ? 65 LEU A O 1 ATOM 71 C CB . LEU A 1 30 ? 32.348 0.095 15.329 1.00 35.74 ? 65 LEU A CB 1 ATOM 72 C CG . LEU A 1 30 ? 30.988 0.789 15.199 1.00 34.67 ? 65 LEU A CG 1 ATOM 73 C CD1 . LEU A 1 30 ? 30.361 0.468 13.850 1.00 36.13 ? 65 LEU A CD1 1 ATOM 74 C CD2 . LEU A 1 30 ? 30.061 0.389 16.341 1.00 33.87 ? 65 LEU A CD2 1 ATOM 75 N N . GLN A 1 31 ? 35.648 0.185 16.099 1.00 50.01 ? 66 GLN A N 1 ATOM 76 C CA . GLN A 1 31 ? 36.911 -0.506 16.370 1.00 58.09 ? 66 GLN A CA 1 ATOM 77 C C . GLN A 1 31 ? 37.162 -0.684 17.872 1.00 59.07 ? 66 GLN A C 1 ATOM 78 O O . GLN A 1 31 ? 36.937 0.229 18.663 1.00 54.42 ? 66 GLN A O 1 ATOM 79 C CB . GLN A 1 31 ? 38.079 0.275 15.740 1.00 65.03 ? 66 GLN A CB 1 ATOM 80 C CG . GLN A 1 31 ? 39.422 -0.444 15.738 1.00 72.87 ? 66 GLN A CG 1 ATOM 81 C CD . GLN A 1 31 ? 39.451 -1.611 14.766 1.00 79.73 ? 66 GLN A CD 1 ATOM 82 O OE1 . GLN A 1 31 ? 39.385 -1.419 13.548 1.00 83.17 ? 66 GLN A OE1 1 ATOM 83 N NE2 . GLN A 1 31 ? 39.546 -2.830 15.297 1.00 82.64 ? 66 GLN A NE2 1 ATOM 84 N N . GLU A 1 32 ? 37.655 -1.862 18.238 1.00 64.98 ? 67 GLU A N 1 ATOM 85 C CA . GLU A 1 32 ? 37.880 -2.230 19.644 1.00 69.55 ? 67 GLU A CA 1 ATOM 86 C C . GLU A 1 32 ? 39.319 -1.872 20.042 1.00 64.79 ? 67 GLU A C 1 ATOM 87 O O . GLU A 1 32 ? 40.261 -2.569 19.658 1.00 65.18 ? 67 GLU A O 1 ATOM 88 C CB . GLU A 1 32 ? 37.571 -3.724 19.907 1.00 72.70 ? 67 GLU A CB 1 ATOM 89 C CG . GLU A 1 32 ? 38.140 -4.751 18.920 1.00 78.55 ? 67 GLU A CG 1 ATOM 90 C CD . GLU A 1 32 ? 37.219 -5.038 17.739 1.00 81.83 ? 67 GLU A CD 1 ATOM 91 O OE1 . GLU A 1 32 ? 37.091 -4.159 16.858 1.00 80.63 ? 67 GLU A OE1 1 ATOM 92 O OE2 . GLU A 1 32 ? 36.635 -6.142 17.681 1.00 84.85 ? 67 GLU A OE2 1 ATOM 93 N N . VAL A 1 33 ? 39.485 -0.772 20.780 1.00 57.88 ? 68 VAL A N 1 ATOM 94 C CA . VAL A 1 33 ? 40.814 -0.300 21.191 1.00 53.80 ? 68 VAL A CA 1 ATOM 95 C C . VAL A 1 33 ? 41.067 -0.726 22.636 1.00 54.90 ? 68 VAL A C 1 ATOM 96 O O . VAL A 1 33 ? 40.319 -0.352 23.544 1.00 51.51 ? 68 VAL A O 1 ATOM 97 C CB . VAL A 1 33 ? 40.958 1.229 21.029 1.00 53.34 ? 68 VAL A CB 1 ATOM 98 C CG1 . VAL A 1 33 ? 42.344 1.698 21.461 1.00 54.08 ? 68 VAL A CG1 1 ATOM 99 C CG2 . VAL A 1 33 ? 40.693 1.632 19.584 1.00 54.17 ? 68 VAL A CG2 1 ATOM 100 N N . GLY A 1 34 ? 42.114 -1.528 22.835 1.00 53.85 ? 69 GLY A N 1 ATOM 101 C CA . GLY A 1 34 ? 42.465 -2.052 24.156 1.00 53.17 ? 69 GLY A CA 1 ATOM 102 C C . GLY A 1 34 ? 43.423 -1.132 24.901 1.00 52.21 ? 69 GLY A C 1 ATOM 103 O O . GLY A 1 34 ? 44.024 -0.242 24.294 1.00 48.60 ? 69 GLY A O 1 ATOM 104 N N . PRO A 1 35 ? 43.584 -1.351 26.224 1.00 54.90 ? 70 PRO A N 1 ATOM 105 C CA . PRO A 1 35 ? 44.502 -0.534 27.023 1.00 57.53 ? 70 PRO A CA 1 ATOM 106 C C . PRO A 1 35 ? 45.973 -0.809 26.684 1.00 59.10 ? 70 PRO A C 1 ATOM 107 O O . PRO A 1 35 ? 46.283 -1.917 26.231 1.00 55.72 ? 70 PRO A O 1 ATOM 108 C CB . PRO A 1 35 ? 44.196 -0.968 28.462 1.00 58.98 ? 70 PRO A CB 1 ATOM 109 C CG . PRO A 1 35 ? 43.690 -2.360 28.336 1.00 56.83 ? 70 PRO A CG 1 ATOM 110 C CD . PRO A 1 35 ? 42.933 -2.397 27.038 1.00 55.12 ? 70 PRO A CD 1 ATOM 111 N N . PRO A 1 36 ? 46.874 0.158 26.902 1.00 59.26 ? 71 PRO A N 1 ATOM 112 C CA . PRO A 1 36 ? 46.589 1.423 27.567 1.00 59.31 ? 71 PRO A CA 1 ATOM 113 C C . PRO A 1 36 ? 46.097 2.538 26.629 1.00 58.55 ? 71 PRO A C 1 ATOM 114 O O . PRO A 1 36 ? 46.017 3.692 27.057 1.00 65.07 ? 71 PRO A O 1 ATOM 115 C CB . PRO A 1 36 ? 47.972 1.807 28.103 1.00 59.05 ? 71 PRO A CB 1 ATOM 116 C CG . PRO A 1 36 ? 48.921 1.273 27.069 1.00 59.59 ? 71 PRO A CG 1 ATOM 117 C CD . PRO A 1 36 ? 48.198 0.218 26.263 1.00 57.39 ? 71 PRO A CD 1 ATOM 118 N N . ASP A 1 37 ? 45.761 2.210 25.379 1.00 54.33 ? 72 ASP A N 1 ATOM 119 C CA . ASP A 1 37 ? 45.586 3.233 24.345 1.00 50.45 ? 72 ASP A CA 1 ATOM 120 C C . ASP A 1 37 ? 44.312 4.022 24.579 1.00 45.24 ? 72 ASP A C 1 ATOM 121 O O . ASP A 1 37 ? 43.311 3.456 25.046 1.00 44.62 ? 72 ASP A O 1 ATOM 122 C CB . ASP A 1 37 ? 45.565 2.599 22.962 1.00 53.10 ? 72 ASP A CB 1 ATOM 123 C CG . ASP A 1 37 ? 46.867 1.909 22.632 1.00 56.08 ? 72 ASP A CG 1 ATOM 124 O OD1 . ASP A 1 37 ? 47.828 2.603 22.242 1.00 61.26 ? 72 ASP A OD1 1 ATOM 125 O OD2 . ASP A 1 37 ? 46.927 0.672 22.783 1.00 55.56 ? 72 ASP A OD2 1 ATOM 126 N N . CYS A 1 38 ? 44.360 5.319 24.276 1.00 41.58 ? 73 CYS A N 1 ATOM 127 C CA . CYS A 1 38 ? 43.221 6.202 24.526 1.00 38.02 ? 73 CYS A CA 1 ATOM 128 C C . CYS A 1 38 ? 42.125 5.944 23.495 1.00 36.34 ? 73 CYS A C 1 ATOM 129 O O . CYS A 1 38 ? 42.393 5.703 22.317 1.00 33.03 ? 73 CYS A O 1 ATOM 130 C CB . CYS A 1 38 ? 43.625 7.681 24.538 1.00 39.77 ? 73 CYS A CB 1 ATOM 131 S SG . CYS A 1 38 ? 44.145 8.416 22.965 1.00 44.68 ? 73 CYS A SG 1 ATOM 132 N N . ARG A 1 39 ? 40.887 6.012 23.972 1.00 34.98 ? 74 ARG A N 1 ATOM 133 C CA . ARG A 1 39 ? 39.733 5.581 23.221 1.00 34.18 ? 74 ARG A CA 1 ATOM 134 C C . ARG A 1 39 ? 38.903 6.750 22.718 1.00 32.34 ? 74 ARG A C 1 ATOM 135 O O . ARG A 1 39 ? 39.033 7.892 23.190 1.00 30.36 ? 74 ARG A O 1 ATOM 136 C CB . ARG A 1 39 ? 38.905 4.655 24.090 1.00 35.57 ? 74 ARG A CB 1 ATOM 137 C CG . ARG A 1 39 ? 39.577 3.301 24.312 1.00 37.18 ? 74 ARG A CG 1 ATOM 138 C CD . ARG A 1 39 ? 39.002 2.552 25.493 1.00 37.51 ? 74 ARG A CD 1 ATOM 139 N NE . ARG A 1 39 ? 37.545 2.442 25.416 1.00 37.06 ? 74 ARG A NE 1 ATOM 140 C CZ . ARG A 1 39 ? 36.782 1.786 26.286 1.00 39.49 ? 74 ARG A CZ 1 ATOM 141 N NH1 . ARG A 1 39 ? 37.320 1.139 27.321 1.00 41.93 ? 74 ARG A NH1 1 ATOM 142 N NH2 . ARG A 1 39 ? 35.460 1.762 26.113 1.00 38.40 ? 74 ARG A NH2 1 ATOM 143 N N . CYS A 1 40 ? 38.079 6.454 21.720 1.00 30.74 ? 75 CYS A N 1 ATOM 144 C CA . CYS A 1 40 ? 37.207 7.441 21.093 1.00 30.75 ? 75 CYS A CA 1 ATOM 145 C C . CYS A 1 40 ? 35.785 6.909 20.917 1.00 29.67 ? 75 CYS A C 1 ATOM 146 O O . CYS A 1 40 ? 34.979 7.504 20.199 1.00 29.19 ? 75 CYS A O 1 ATOM 147 C CB . CYS A 1 40 ? 37.797 7.861 19.740 1.00 31.97 ? 75 CYS A CB 1 ATOM 148 S SG . CYS A 1 40 ? 39.493 8.507 19.857 1.00 34.24 ? 75 CYS A SG 1 ATOM 149 N N . ASP A 1 41 ? 35.468 5.825 21.615 1.00 27.87 ? 76 ASP A N 1 ATOM 150 C CA . ASP A 1 41 ? 34.200 5.122 21.420 1.00 28.72 ? 76 ASP A CA 1 ATOM 151 C C . ASP A 1 41 ? 33.150 5.610 22.414 1.00 26.86 ? 76 ASP A C 1 ATOM 152 O O . ASP A 1 41 ? 33.442 6.405 23.309 1.00 24.99 ? 76 ASP A O 1 ATOM 153 C CB . ASP A 1 41 ? 34.405 3.601 21.582 1.00 29.87 ? 76 ASP A CB 1 ATOM 154 C CG . ASP A 1 41 ? 34.882 3.228 22.970 1.00 31.38 ? 76 ASP A CG 1 ATOM 155 O OD1 . ASP A 1 41 ? 36.088 3.359 23.232 1.00 33.05 ? 76 ASP A OD1 1 ATOM 156 O OD2 . ASP A 1 41 ? 34.051 2.841 23.815 1.00 34.42 ? 76 ASP A OD2 1 ATOM 157 N N . ASN A 1 42 ? 31.928 5.119 22.216 1.00 25.30 ? 77 ASN A N 1 ATOM 158 C CA . ASN A 1 42 ? 30.767 5.332 23.089 1.00 26.68 ? 77 ASN A CA 1 ATOM 159 C C . ASN A 1 42 ? 30.982 5.326 24.585 1.00 26.43 ? 77 ASN A C 1 ATOM 160 O O . ASN A 1 42 ? 30.304 6.058 25.306 1.00 28.20 ? 77 ASN A O 1 ATOM 161 C CB . ASN A 1 42 ? 29.762 4.200 22.869 1.00 28.26 ? 77 ASN A CB 1 ATOM 162 C CG . ASN A 1 42 ? 28.934 4.384 21.636 1.00 28.31 ? 77 ASN A CG 1 ATOM 163 O OD1 . ASN A 1 42 ? 29.368 5.024 20.667 1.00 33.39 ? 77 ASN A OD1 1 ATOM 164 N ND2 . ASN A 1 42 ? 27.734 3.820 21.652 1.00 25.49 ? 77 ASN A ND2 1 ATOM 165 N N . LEU A 1 43 ? 31.827 4.426 25.059 1.00 27.01 ? 78 LEU A N 1 ATOM 166 C CA . LEU A 1 43 ? 32.008 4.247 26.488 1.00 28.22 ? 78 LEU A CA 1 ATOM 167 C C . LEU A 1 43 ? 33.326 4.768 27.018 1.00 28.46 ? 78 LEU A C 1 ATOM 168 O O . LEU A 1 43 ? 33.616 4.557 28.179 1.00 27.97 ? 78 LEU A O 1 ATOM 169 C CB . LEU A 1 43 ? 31.835 2.769 26.849 1.00 30.89 ? 78 LEU A CB 1 ATOM 170 C CG . LEU A 1 43 ? 30.397 2.258 26.737 1.00 32.00 ? 78 LEU A CG 1 ATOM 171 C CD1 . LEU A 1 43 ? 30.384 0.766 27.031 1.00 34.61 ? 78 LEU A CD1 1 ATOM 172 C CD2 . LEU A 1 43 ? 29.446 2.996 27.663 1.00 30.96 ? 78 LEU A CD2 1 ATOM 173 N N . CYS A 1 44 ? 34.122 5.476 26.213 1.00 27.50 ? 79 CYS A N 1 ATOM 174 C CA . CYS A 1 44 ? 35.451 5.883 26.693 1.00 27.43 ? 79 CYS A CA 1 ATOM 175 C C . CYS A 1 44 ? 35.408 6.738 27.983 1.00 28.13 ? 79 CYS A C 1 ATOM 176 O O . CYS A 1 44 ? 36.277 6.598 28.845 1.00 29.36 ? 79 CYS A O 1 ATOM 177 C CB . CYS A 1 44 ? 36.265 6.549 25.569 1.00 28.40 ? 79 CYS A CB 1 ATOM 178 S SG . CYS A 1 44 ? 35.782 8.214 25.069 1.00 26.92 ? 79 CYS A SG 1 ATOM 179 N N . LYS A 1 45 ? 34.388 7.592 28.103 1.00 27.45 ? 80 LYS A N 1 ATOM 180 C CA . LYS A 1 45 ? 34.184 8.449 29.287 1.00 30.69 ? 80 LYS A CA 1 ATOM 181 C C . LYS A 1 45 ? 33.875 7.622 30.544 1.00 30.50 ? 80 LYS A C 1 ATOM 182 O O . LYS A 1 45 ? 34.326 7.969 31.633 1.00 34.04 ? 80 LYS A O 1 ATOM 183 C CB . LYS A 1 45 ? 33.033 9.438 29.077 1.00 30.99 ? 80 LYS A CB 1 ATOM 184 C CG . LYS A 1 45 ? 33.198 10.451 27.953 1.00 35.15 ? 80 LYS A CG 1 ATOM 185 C CD . LYS A 1 45 ? 34.125 11.585 28.331 1.00 39.81 ? 80 LYS A CD 1 ATOM 186 C CE . LYS A 1 45 ? 33.396 12.677 29.085 1.00 43.19 ? 80 LYS A CE 1 ATOM 187 N NZ . LYS A 1 45 ? 34.361 13.550 29.791 1.00 46.58 ? 80 LYS A NZ 1 ATOM 188 N N . SER A 1 46 ? 33.128 6.537 30.374 1.00 29.91 ? 81 SER A N 1 ATOM 189 C CA . SER A 1 46 ? 32.742 5.655 31.478 1.00 31.46 ? 81 SER A CA 1 ATOM 190 C C . SER A 1 46 ? 33.927 4.896 32.086 1.00 34.67 ? 81 SER A C 1 ATOM 191 O O . SER A 1 46 ? 33.909 4.592 33.281 1.00 35.78 ? 81 SER A O 1 ATOM 192 C CB . SER A 1 46 ? 31.673 4.659 30.993 1.00 29.03 ? 81 SER A CB 1 ATOM 193 O OG . SER A 1 46 ? 30.513 5.345 30.555 1.00 29.44 ? 81 SER A OG 1 ATOM 194 N N . TYR A 1 47 ? 34.927 4.578 31.261 1.00 36.69 ? 82 TYR A N 1 ATOM 195 C CA . TYR A 1 47 ? 36.197 3.985 31.713 1.00 38.81 ? 82 TYR A CA 1 ATOM 196 C C . TYR A 1 47 ? 37.307 5.028 31.933 1.00 40.66 ? 82 TYR A C 1 ATOM 197 O O . TYR A 1 47 ? 38.468 4.646 32.099 1.00 46.13 ? 82 TYR A O 1 ATOM 198 C CB . TYR A 1 47 ? 36.709 2.954 30.699 1.00 37.19 ? 82 TYR A CB 1 ATOM 199 C CG . TYR A 1 47 ? 35.833 1.730 30.470 1.00 38.53 ? 82 TYR A CG 1 ATOM 200 C CD1 . TYR A 1 47 ? 34.812 1.748 29.520 1.00 38.54 ? 82 TYR A CD1 1 ATOM 201 C CD2 . TYR A 1 47 ? 36.061 0.538 31.159 1.00 39.18 ? 82 TYR A CD2 1 ATOM 202 C CE1 . TYR A 1 47 ? 34.018 0.637 29.283 1.00 38.99 ? 82 TYR A CE1 1 ATOM 203 C CE2 . TYR A 1 47 ? 35.272 -0.588 30.928 1.00 36.92 ? 82 TYR A CE2 1 ATOM 204 C CZ . TYR A 1 47 ? 34.255 -0.535 29.984 1.00 37.56 ? 82 TYR A CZ 1 ATOM 205 O OH . TYR A 1 47 ? 33.459 -1.637 29.737 1.00 38.90 ? 82 TYR A OH 1 ATOM 206 N N . SER A 1 48 ? 36.969 6.326 31.935 1.00 39.00 ? 83 SER A N 1 ATOM 207 C CA . SER A 1 48 ? 37.948 7.415 32.067 1.00 39.20 ? 83 SER A CA 1 ATOM 208 C C . SER A 1 48 ? 39.167 7.227 31.157 1.00 38.68 ? 83 SER A C 1 ATOM 209 O O . SER A 1 48 ? 40.313 7.389 31.586 1.00 39.07 ? 83 SER A O 1 ATOM 210 C CB . SER A 1 48 ? 38.395 7.575 33.537 1.00 41.03 ? 83 SER A CB 1 ATOM 211 O OG . SER A 1 48 ? 37.337 8.051 34.355 1.00 44.79 ? 83 SER A OG 1 ATOM 212 N N . SER A 1 49 ? 38.902 6.900 29.897 1.00 37.72 ? 84 SER A N 1 ATOM 213 C CA . SER A 1 49 ? 39.936 6.458 28.966 1.00 36.93 ? 84 SER A CA 1 ATOM 214 C C . SER A 1 49 ? 39.935 7.191 27.623 1.00 33.79 ? 84 SER A C 1 ATOM 215 O O . SER A 1 49 ? 40.585 6.734 26.691 1.00 30.50 ? 84 SER A O 1 ATOM 216 C CB . SER A 1 49 ? 39.739 4.970 28.705 1.00 37.64 ? 84 SER A CB 1 ATOM 217 O OG . SER A 1 49 ? 38.448 4.737 28.144 1.00 41.01 ? 84 SER A OG 1 ATOM 218 N N . CYS A 1 50 ? 39.223 8.312 27.500 1.00 32.83 ? 85 CYS A N 1 ATOM 219 C CA . CYS A 1 50 ? 39.149 8.995 26.201 1.00 32.01 ? 85 CYS A CA 1 ATOM 220 C C . CYS A 1 50 ? 40.447 9.701 25.886 1.00 33.33 ? 85 CYS A C 1 ATOM 221 O O . CYS A 1 50 ? 41.153 10.113 26.800 1.00 32.69 ? 85 CYS A O 1 ATOM 222 C CB . CYS A 1 50 ? 38.028 10.015 26.149 1.00 32.45 ? 85 CYS A CB 1 ATOM 223 S SG . CYS A 1 50 ? 36.413 9.401 26.651 1.00 31.22 ? 85 CYS A SG 1 ATOM 224 N N . CYS A 1 51 ? 40.752 9.859 24.594 1.00 35.36 ? 86 CYS A N 1 ATOM 225 C CA . CYS A 1 51 ? 41.868 10.711 24.189 1.00 37.83 ? 86 CYS A CA 1 ATOM 226 C C . CYS A 1 51 ? 41.595 12.136 24.607 1.00 41.11 ? 86 CYS A C 1 ATOM 227 O O . CYS A 1 51 ? 40.436 12.520 24.825 1.00 36.97 ? 86 CYS A O 1 ATOM 228 C CB . CYS A 1 51 ? 42.109 10.682 22.680 1.00 38.62 ? 86 CYS A CB 1 ATOM 229 S SG . CYS A 1 51 ? 42.434 9.037 22.007 1.00 40.19 ? 86 CYS A SG 1 ATOM 230 N N . HIS A 1 52 ? 42.688 12.900 24.696 1.00 44.50 ? 87 HIS A N 1 ATOM 231 C CA . HIS A 1 52 ? 42.701 14.287 25.167 1.00 46.57 ? 87 HIS A CA 1 ATOM 232 C C . HIS A 1 52 ? 41.750 15.200 24.408 1.00 44.41 ? 87 HIS A C 1 ATOM 233 O O . HIS A 1 52 ? 41.196 16.120 24.989 1.00 47.01 ? 87 HIS A O 1 ATOM 234 C CB . HIS A 1 52 ? 44.129 14.869 25.074 1.00 51.99 ? 87 HIS A CB 1 ATOM 235 C CG . HIS A 1 52 ? 44.591 15.152 23.671 1.00 54.41 ? 87 HIS A CG 1 ATOM 236 N ND1 . HIS A 1 52 ? 45.110 14.179 22.842 1.00 57.16 ? 87 HIS A ND1 1 ATOM 237 C CD2 . HIS A 1 52 ? 44.608 16.302 22.956 1.00 57.30 ? 87 HIS A CD2 1 ATOM 238 C CE1 . HIS A 1 52 ? 45.428 14.719 21.678 1.00 58.83 ? 87 HIS A CE1 1 ATOM 239 N NE2 . HIS A 1 52 ? 45.132 16.005 21.721 1.00 59.79 ? 87 HIS A NE2 1 ATOM 240 N N . ASP A 1 53 ? 41.577 14.942 23.115 1.00 43.50 ? 88 ASP A N 1 ATOM 241 C CA . ASP A 1 53 ? 40.726 15.763 22.255 1.00 42.79 ? 88 ASP A CA 1 ATOM 242 C C . ASP A 1 53 ? 39.353 15.135 21.979 1.00 43.11 ? 88 ASP A C 1 ATOM 243 O O . ASP A 1 53 ? 38.679 15.523 21.020 1.00 41.25 ? 88 ASP A O 1 ATOM 244 C CB . ASP A 1 53 ? 41.470 16.090 20.952 1.00 42.54 ? 88 ASP A CB 1 ATOM 245 C CG . ASP A 1 53 ? 41.873 14.852 20.160 1.00 44.51 ? 88 ASP A CG 1 ATOM 246 O OD1 . ASP A 1 53 ? 41.577 13.700 20.581 1.00 42.72 ? 88 ASP A OD1 1 ATOM 247 O OD2 . ASP A 1 53 ? 42.493 15.029 19.089 1.00 46.16 ? 88 ASP A OD2 1 ATOM 248 N N . PHE A 1 54 ? 38.935 14.180 22.816 1.00 41.25 ? 89 PHE A N 1 ATOM 249 C CA . PHE A 1 54 ? 37.659 13.496 22.605 1.00 40.68 ? 89 PHE A CA 1 ATOM 250 C C . PHE A 1 54 ? 36.526 14.494 22.762 1.00 43.76 ? 89 PHE A C 1 ATOM 251 O O . PHE A 1 54 ? 35.705 14.684 21.851 1.00 42.15 ? 89 PHE A O 1 ATOM 252 C CB . PHE A 1 54 ? 37.464 12.347 23.598 1.00 37.42 ? 89 PHE A CB 1 ATOM 253 C CG . PHE A 1 54 ? 36.100 11.712 23.517 1.00 35.23 ? 89 PHE A CG 1 ATOM 254 C CD1 . PHE A 1 54 ? 35.809 10.799 22.511 1.00 35.06 ? 89 PHE A CD1 1 ATOM 255 C CD2 . PHE A 1 54 ? 35.108 12.050 24.416 1.00 35.03 ? 89 PHE A CD2 1 ATOM 256 C CE1 . PHE A 1 54 ? 34.552 10.226 22.412 1.00 32.97 ? 89 PHE A CE1 1 ATOM 257 C CE2 . PHE A 1 54 ? 33.847 11.480 24.326 1.00 34.51 ? 89 PHE A CE2 1 ATOM 258 C CZ . PHE A 1 54 ? 33.571 10.571 23.317 1.00 33.72 ? 89 PHE A CZ 1 ATOM 259 N N . ASP A 1 55 ? 36.531 15.147 23.919 1.00 46.81 ? 90 ASP A N 1 ATOM 260 C CA . ASP A 1 55 ? 35.450 16.031 24.324 1.00 53.41 ? 90 ASP A CA 1 ATOM 261 C C . ASP A 1 55 ? 35.290 17.234 23.387 1.00 54.69 ? 90 ASP A C 1 ATOM 262 O O . ASP A 1 55 ? 34.190 17.758 23.293 1.00 59.00 ? 90 ASP A O 1 ATOM 263 C CB . ASP A 1 55 ? 35.606 16.477 25.792 1.00 52.04 ? 90 ASP A CB 1 ATOM 264 C CG . ASP A 1 55 ? 35.893 15.298 26.751 1.00 54.44 ? 90 ASP A CG 1 ATOM 265 O OD1 . ASP A 1 55 ? 37.019 14.745 26.693 1.00 57.75 ? 90 ASP A OD1 1 ATOM 266 O OD2 . ASP A 1 55 ? 35.009 14.932 27.560 1.00 51.49 ? 90 ASP A OD2 1 ATOM 267 N N . GLU A 1 56 ? 36.353 17.646 22.684 1.00 58.95 ? 91 GLU A N 1 ATOM 268 C CA . GLU A 1 56 ? 36.255 18.732 21.691 1.00 60.09 ? 91 GLU A CA 1 ATOM 269 C C . GLU A 1 56 ? 35.925 18.264 20.276 1.00 61.50 ? 91 GLU A C 1 ATOM 270 O O . GLU A 1 56 ? 35.087 18.873 19.616 1.00 67.55 ? 91 GLU A O 1 ATOM 271 C CB . GLU A 1 56 ? 37.516 19.613 21.683 1.00 65.80 ? 91 GLU A CB 1 ATOM 272 C CG . GLU A 1 56 ? 38.781 19.015 21.074 1.00 68.03 ? 91 GLU A CG 1 ATOM 273 C CD . GLU A 1 56 ? 39.882 20.044 20.877 1.00 74.91 ? 91 GLU A CD 1 ATOM 274 O OE1 . GLU A 1 56 ? 39.883 21.080 21.586 1.00 76.95 ? 91 GLU A OE1 1 ATOM 275 O OE2 . GLU A 1 56 ? 40.756 19.809 20.007 1.00 75.23 ? 91 GLU A OE2 1 ATOM 276 N N . LEU A 1 57 ? 36.587 17.206 19.802 1.00 57.98 ? 92 LEU A N 1 ATOM 277 C CA . LEU A 1 57 ? 36.368 16.701 18.444 1.00 54.69 ? 92 LEU A CA 1 ATOM 278 C C . LEU A 1 57 ? 35.060 15.920 18.297 1.00 53.67 ? 92 LEU A C 1 ATOM 279 O O . LEU A 1 57 ? 34.378 16.060 17.283 1.00 52.45 ? 92 LEU A O 1 ATOM 280 C CB . LEU A 1 57 ? 37.533 15.817 17.976 1.00 55.94 ? 92 LEU A CB 1 ATOM 281 C CG . LEU A 1 57 ? 38.902 16.467 17.742 1.00 56.71 ? 92 LEU A CG 1 ATOM 282 C CD1 . LEU A 1 57 ? 39.875 15.415 17.228 1.00 56.21 ? 92 LEU A CD1 1 ATOM 283 C CD2 . LEU A 1 57 ? 38.821 17.635 16.765 1.00 58.90 ? 92 LEU A CD2 1 ATOM 284 N N . CYS A 1 58 ? 34.735 15.098 19.298 1.00 52.61 ? 93 CYS A N 1 ATOM 285 C CA . CYS A 1 58 ? 33.605 14.155 19.228 1.00 51.67 ? 93 CYS A CA 1 ATOM 286 C C . CYS A 1 58 ? 32.312 14.685 19.820 1.00 51.12 ? 93 CYS A C 1 ATOM 287 O O . CYS A 1 58 ? 31.235 14.336 19.339 1.00 53.78 ? 93 CYS A O 1 ATOM 288 C CB . CYS A 1 58 ? 33.978 12.828 19.907 1.00 47.49 ? 93 CYS A CB 1 ATOM 289 S SG . CYS A 1 58 ? 35.516 12.122 19.267 1.00 43.06 ? 93 CYS A SG 1 ATOM 290 N N . LEU A 1 59 ? 32.407 15.509 20.858 1.00 51.60 ? 94 LEU A N 1 ATOM 291 C CA . LEU A 1 59 ? 31.224 16.112 21.466 1.00 50.22 ? 94 LEU A CA 1 ATOM 292 C C . LEU A 1 59 ? 31.041 17.560 20.987 1.00 49.82 ? 94 LEU A C 1 ATOM 293 O O . LEU A 1 59 ? 30.890 18.467 21.790 1.00 54.53 ? 94 LEU A O 1 ATOM 294 C CB . LEU A 1 59 ? 31.317 16.029 22.990 1.00 47.98 ? 94 LEU A CB 1 ATOM 295 C CG . LEU A 1 59 ? 31.581 14.643 23.586 1.00 48.16 ? 94 LEU A CG 1 ATOM 296 C CD1 . LEU A 1 59 ? 31.695 14.713 25.099 1.00 44.74 ? 94 LEU A CD1 1 ATOM 297 C CD2 . LEU A 1 59 ? 30.490 13.661 23.182 1.00 48.10 ? 94 LEU A CD2 1 ATOM 298 N N . LYS A 1 60 ? 31.020 17.758 19.669 1.00 51.79 ? 95 LYS A N 1 ATOM 299 C CA . LYS A 1 60 ? 30.800 19.088 19.096 1.00 49.85 ? 95 LYS A CA 1 ATOM 300 C C . LYS A 1 60 ? 29.353 19.510 19.353 1.00 51.39 ? 95 LYS A C 1 ATOM 301 O O . LYS A 1 60 ? 28.430 18.726 19.100 1.00 46.49 ? 95 LYS A O 1 ATOM 302 C CB . LYS A 1 60 ? 31.053 19.083 17.595 1.00 50.48 ? 95 LYS A CB 1 ATOM 303 C CG . LYS A 1 60 ? 32.456 18.687 17.192 1.00 49.78 ? 95 LYS A CG 1 ATOM 304 C CD . LYS A 1 60 ? 32.636 18.744 15.693 1.00 52.09 ? 95 LYS A CD 1 ATOM 305 C CE . LYS A 1 60 ? 31.924 17.623 14.942 1.00 53.46 ? 95 LYS A CE 1 ATOM 306 N NZ . LYS A 1 60 ? 32.049 17.787 13.459 1.00 56.28 ? 95 LYS A NZ 1 ATOM 307 N N . THR A 1 61 ? 29.161 20.724 19.882 1.00 46.18 ? 96 THR A N 1 ATOM 308 C CA . THR A 1 61 ? 27.815 21.278 20.112 1.00 43.57 ? 96 THR A CA 1 ATOM 309 C C . THR A 1 61 ? 27.495 22.551 19.309 1.00 40.35 ? 96 THR A C 1 ATOM 310 O O . THR A 1 61 ? 26.356 23.019 19.343 1.00 37.92 ? 96 THR A O 1 ATOM 311 C CB . THR A 1 61 ? 27.565 21.560 21.604 1.00 45.63 ? 96 THR A CB 1 ATOM 312 O OG1 . THR A 1 61 ? 28.498 22.535 22.074 1.00 49.31 ? 96 THR A OG1 1 ATOM 313 C CG2 . THR A 1 61 ? 27.699 20.288 22.431 1.00 47.34 ? 96 THR A CG2 1 ATOM 314 N N . ALA A 1 62 ? 28.463 23.069 18.555 1.00 38.49 ? 97 ALA A N 1 ATOM 315 C CA . ALA A 1 62 ? 28.337 24.389 17.918 1.00 39.80 ? 97 ALA A CA 1 ATOM 316 C C . ALA A 1 62 ? 27.211 24.459 16.884 1.00 40.25 ? 97 ALA A C 1 ATOM 317 O O . ALA A 1 62 ? 27.104 23.588 16.008 1.00 36.16 ? 97 ALA A O 1 ATOM 318 C CB . ALA A 1 62 ? 29.647 24.808 17.284 1.00 41.32 ? 97 ALA A CB 1 ATOM 319 N N . ARG A 1 63 ? 26.387 25.506 17.024 1.00 38.67 ? 98 ARG A N 1 ATOM 320 C CA . ARG A 1 63 ? 25.206 25.790 16.195 1.00 38.21 ? 98 ARG A CA 1 ATOM 321 C C . ARG A 1 63 ? 24.037 24.817 16.404 1.00 36.84 ? 98 ARG A C 1 ATOM 322 O O . ARG A 1 63 ? 23.061 24.846 15.654 1.00 37.14 ? 98 ARG A O 1 ATOM 323 C CB . ARG A 1 63 ? 25.580 25.954 14.714 1.00 40.52 ? 98 ARG A CB 1 ATOM 324 C CG . ARG A 1 63 ? 26.715 26.944 14.497 1.00 41.54 ? 98 ARG A CG 1 ATOM 325 C CD . ARG A 1 63 ? 26.891 27.351 13.041 1.00 44.09 ? 98 ARG A CD 1 ATOM 326 N NE . ARG A 1 63 ? 25.841 28.264 12.587 1.00 46.72 ? 98 ARG A NE 1 ATOM 327 C CZ . ARG A 1 63 ? 25.679 28.701 11.335 1.00 49.48 ? 98 ARG A CZ 1 ATOM 328 N NH1 . ARG A 1 63 ? 26.500 28.321 10.353 1.00 50.31 ? 98 ARG A NH1 1 ATOM 329 N NH2 . ARG A 1 63 ? 24.671 29.528 11.057 1.00 51.23 ? 98 ARG A NH2 1 ATOM 330 N N . GLY A 1 64 ? 24.104 24.000 17.456 1.00 35.16 ? 99 GLY A N 1 ATOM 331 C CA . GLY A 1 64 ? 23.013 23.130 17.820 1.00 34.71 ? 99 GLY A CA 1 ATOM 332 C C . GLY A 1 64 ? 22.785 22.001 16.840 1.00 33.60 ? 99 GLY A C 1 ATOM 333 O O . GLY A 1 64 ? 23.670 21.658 16.067 1.00 33.68 ? 99 GLY A O 1 ATOM 334 N N . TRP A 1 65 ? 21.577 21.451 16.859 1.00 31.32 ? 100 TRP A N 1 ATOM 335 C CA . TRP A 1 65 ? 21.293 20.190 16.183 1.00 30.17 ? 100 TRP A CA 1 ATOM 336 C C . TRP A 1 65 ? 20.327 20.316 15.011 1.00 30.44 ? 100 TRP A C 1 ATOM 337 O O . TRP A 1 65 ? 19.878 19.290 14.496 1.00 29.81 ? 100 TRP A O 1 ATOM 338 C CB . TRP A 1 65 ? 20.754 19.176 17.189 1.00 30.41 ? 100 TRP A CB 1 ATOM 339 C CG . TRP A 1 65 ? 21.543 19.151 18.433 1.00 31.70 ? 100 TRP A CG 1 ATOM 340 C CD1 . TRP A 1 65 ? 21.236 19.780 19.588 1.00 32.36 ? 100 TRP A CD1 1 ATOM 341 C CD2 . TRP A 1 65 ? 22.784 18.473 18.657 1.00 32.30 ? 100 TRP A CD2 1 ATOM 342 N NE1 . TRP A 1 65 ? 22.196 19.538 20.529 1.00 33.85 ? 100 TRP A NE1 1 ATOM 343 C CE2 . TRP A 1 65 ? 23.168 18.745 19.984 1.00 32.90 ? 100 TRP A CE2 1 ATOM 344 C CE3 . TRP A 1 65 ? 23.605 17.660 17.870 1.00 33.24 ? 100 TRP A CE3 1 ATOM 345 C CZ2 . TRP A 1 65 ? 24.339 18.237 20.547 1.00 34.02 ? 100 TRP A CZ2 1 ATOM 346 C CZ3 . TRP A 1 65 ? 24.779 17.154 18.429 1.00 33.45 ? 100 TRP A CZ3 1 ATOM 347 C CH2 . TRP A 1 65 ? 25.131 17.445 19.756 1.00 34.51 ? 100 TRP A CH2 1 ATOM 348 N N . GLU A 1 66 ? 20.019 21.547 14.587 1.00 30.87 ? 101 GLU A N 1 ATOM 349 C CA . GLU A 1 66 ? 19.062 21.788 13.512 1.00 31.97 ? 101 GLU A CA 1 ATOM 350 C C . GLU A 1 66 ? 19.626 22.686 12.428 1.00 33.65 ? 101 GLU A C 1 ATOM 351 O O . GLU A 1 66 ? 20.115 23.781 12.714 1.00 34.08 ? 101 GLU A O 1 ATOM 352 C CB . GLU A 1 66 ? 17.808 22.427 14.085 1.00 34.62 ? 101 GLU A CB 1 ATOM 353 C CG . GLU A 1 66 ? 16.985 21.460 14.914 1.00 35.80 ? 101 GLU A CG 1 ATOM 354 C CD . GLU A 1 66 ? 15.850 22.117 15.664 1.00 37.96 ? 101 GLU A CD 1 ATOM 355 O OE1 . GLU A 1 66 ? 15.671 23.350 15.576 1.00 42.41 ? 101 GLU A OE1 1 ATOM 356 O OE2 . GLU A 1 66 ? 15.136 21.379 16.360 1.00 41.66 ? 101 GLU A OE2 1 ATOM 357 N N . CYS A 1 67 ? 19.541 22.234 11.178 1.00 33.39 ? 102 CYS A N 1 ATOM 358 C CA . CYS A 1 67 ? 19.812 23.096 10.047 1.00 36.14 ? 102 CYS A CA 1 ATOM 359 C C . CYS A 1 67 ? 18.816 24.267 10.047 1.00 36.34 ? 102 CYS A C 1 ATOM 360 O O . CYS A 1 67 ? 17.654 24.137 10.446 1.00 34.80 ? 102 CYS A O 1 ATOM 361 C CB . CYS A 1 67 ? 19.766 22.324 8.702 1.00 37.34 ? 102 CYS A CB 1 ATOM 362 S SG . CYS A 1 67 ? 21.163 21.189 8.423 1.00 38.68 ? 102 CYS A SG 1 ATOM 363 N N . THR A 1 68 ? 19.311 25.428 9.659 1.00 37.72 ? 103 THR A N 1 ATOM 364 C CA . THR A 1 68 ? 18.469 26.579 9.394 1.00 39.38 ? 103 THR A CA 1 ATOM 365 C C . THR A 1 68 ? 18.716 26.928 7.947 1.00 40.47 ? 103 THR A C 1 ATOM 366 O O . THR A 1 68 ? 19.739 26.527 7.386 1.00 40.43 ? 103 THR A O 1 ATOM 367 C CB . THR A 1 68 ? 18.830 27.739 10.328 1.00 39.87 ? 103 THR A CB 1 ATOM 368 O OG1 . THR A 1 68 ? 20.224 28.042 10.197 1.00 40.51 ? 103 THR A OG1 1 ATOM 369 C CG2 . THR A 1 68 ? 18.545 27.342 11.775 1.00 40.88 ? 103 THR A CG2 1 ATOM 370 N N . LYS A 1 69 ? 17.794 27.682 7.353 1.00 42.78 ? 104 LYS A N 1 ATOM 371 C CA . LYS A 1 69 ? 17.821 27.969 5.918 1.00 45.01 ? 104 LYS A CA 1 ATOM 372 C C . LYS A 1 69 ? 19.136 28.601 5.462 1.00 43.76 ? 104 LYS A C 1 ATOM 373 O O . LYS A 1 69 ? 19.650 28.260 4.393 1.00 42.05 ? 104 LYS A O 1 ATOM 374 C CB . LYS A 1 69 ? 16.617 28.844 5.523 1.00 48.31 ? 104 LYS A CB 1 ATOM 375 C CG . LYS A 1 69 ? 16.406 29.033 4.027 1.00 54.26 ? 104 LYS A CG 1 ATOM 376 C CD . LYS A 1 69 ? 16.034 27.738 3.305 1.00 58.77 ? 104 LYS A CD 1 ATOM 377 C CE . LYS A 1 69 ? 16.228 27.855 1.794 1.00 62.05 ? 104 LYS A CE 1 ATOM 378 N NZ . LYS A 1 69 ? 16.336 26.510 1.154 1.00 62.04 ? 104 LYS A NZ 1 ATOM 379 N N . ASP A 1 70 ? 19.679 29.502 6.280 1.00 43.42 ? 105 ASP A N 1 ATOM 380 C CA . ASP A 1 70 ? 20.956 30.170 5.975 1.00 44.36 ? 105 ASP A CA 1 ATOM 381 C C . ASP A 1 70 ? 22.172 29.238 5.872 1.00 42.46 ? 105 ASP A C 1 ATOM 382 O O . ASP A 1 70 ? 23.161 29.601 5.242 1.00 41.73 ? 105 ASP A O 1 ATOM 383 C CB . ASP A 1 70 ? 21.253 31.273 7.003 1.00 46.28 ? 105 ASP A CB 1 ATOM 384 C CG . ASP A 1 70 ? 21.444 30.731 8.397 1.00 47.75 ? 105 ASP A CG 1 ATOM 385 O OD1 . ASP A 1 70 ? 20.437 30.295 8.992 1.00 48.15 ? 105 ASP A OD1 1 ATOM 386 O OD2 . ASP A 1 70 ? 22.594 30.725 8.885 1.00 50.64 ? 105 ASP A OD2 1 ATOM 387 N N . ARG A 1 71 ? 22.102 28.065 6.507 1.00 40.56 ? 106 ARG A N 1 ATOM 388 C CA . ARG A 1 71 ? 23.179 27.057 6.440 1.00 39.36 ? 106 ARG A CA 1 ATOM 389 C C . ARG A 1 71 ? 23.154 26.139 5.205 1.00 38.78 ? 106 ARG A C 1 ATOM 390 O O . ARG A 1 71 ? 24.124 25.418 4.961 1.00 37.40 ? 106 ARG A O 1 ATOM 391 C CB . ARG A 1 71 ? 23.158 26.170 7.695 1.00 37.13 ? 106 ARG A CB 1 ATOM 392 C CG . ARG A 1 71 ? 23.535 26.897 8.970 1.00 38.32 ? 106 ARG A CG 1 ATOM 393 C CD . ARG A 1 71 ? 23.688 25.947 10.140 1.00 36.67 ? 106 ARG A CD 1 ATOM 394 N NE . ARG A 1 71 ? 24.744 24.956 9.913 1.00 34.82 ? 106 ARG A NE 1 ATOM 395 C CZ . ARG A 1 71 ? 25.082 23.993 10.777 1.00 34.22 ? 106 ARG A CZ 1 ATOM 396 N NH1 . ARG A 1 71 ? 24.471 23.889 11.950 1.00 33.54 ? 106 ARG A NH1 1 ATOM 397 N NH2 . ARG A 1 71 ? 26.053 23.135 10.473 1.00 33.16 ? 106 ARG A NH2 1 ATOM 398 N N . CYS A 1 72 ? 22.063 26.146 4.442 1.00 38.39 ? 107 CYS A N 1 ATOM 399 C CA . CYS A 1 72 ? 21.916 25.210 3.338 1.00 38.36 ? 107 CYS A CA 1 ATOM 400 C C . CYS A 1 72 ? 22.993 25.422 2.291 1.00 39.31 ? 107 CYS A C 1 ATOM 401 O O . CYS A 1 72 ? 23.244 26.544 1.868 1.00 39.97 ? 107 CYS A O 1 ATOM 402 C CB . CYS A 1 72 ? 20.526 25.302 2.721 1.00 39.31 ? 107 CYS A CB 1 ATOM 403 S SG . CYS A 1 72 ? 19.210 24.868 3.880 1.00 41.83 ? 107 CYS A SG 1 ATOM 404 N N . GLY A 1 73 ? 23.684 24.342 1.936 1.00 38.23 ? 108 GLY A N 1 ATOM 405 C CA . GLY A 1 73 ? 24.788 24.409 0.989 1.00 39.28 ? 108 GLY A CA 1 ATOM 406 C C . GLY A 1 73 ? 26.054 25.068 1.506 1.00 39.05 ? 108 GLY A C 1 ATOM 407 O O . GLY A 1 73 ? 26.945 25.368 0.716 1.00 40.38 ? 108 GLY A O 1 ATOM 408 N N . GLU A 1 74 ? 26.146 25.283 2.817 1.00 37.73 ? 109 GLU A N 1 ATOM 409 C CA . GLU A 1 74 ? 27.354 25.803 3.453 1.00 38.66 ? 109 GLU A CA 1 ATOM 410 C C . GLU A 1 74 ? 28.573 24.983 3.086 1.00 40.71 ? 109 GLU A C 1 ATOM 411 O O . GLU A 1 74 ? 28.475 23.785 2.773 1.00 38.37 ? 109 GLU A O 1 ATOM 412 C CB . GLU A 1 74 ? 27.220 25.786 4.991 1.00 39.32 ? 109 GLU A CB 1 ATOM 413 C CG . GLU A 1 74 ? 27.143 24.372 5.583 1.00 37.31 ? 109 GLU A CG 1 ATOM 414 C CD . GLU A 1 74 ? 26.890 24.320 7.076 1.00 36.29 ? 109 GLU A CD 1 ATOM 415 O OE1 . GLU A 1 74 ? 26.645 25.384 7.686 1.00 35.91 ? 109 GLU A OE1 1 ATOM 416 O OE2 . GLU A 1 74 ? 26.947 23.193 7.646 1.00 34.91 ? 109 GLU A OE2 1 ATOM 417 N N . VAL A 1 75 ? 29.725 25.632 3.143 1.00 43.87 ? 110 VAL A N 1 ATOM 418 C CA . VAL A 1 75 ? 30.987 24.920 3.158 1.00 45.93 ? 110 VAL A CA 1 ATOM 419 C C . VAL A 1 75 ? 31.061 24.304 4.548 1.00 45.36 ? 110 VAL A C 1 ATOM 420 O O . VAL A 1 75 ? 30.732 24.956 5.539 1.00 43.65 ? 110 VAL A O 1 ATOM 421 C CB . VAL A 1 75 ? 32.182 25.856 2.875 1.00 51.02 ? 110 VAL A CB 1 ATOM 422 C CG1 . VAL A 1 75 ? 33.516 25.128 3.057 1.00 52.30 ? 110 VAL A CG1 1 ATOM 423 C CG2 . VAL A 1 75 ? 32.072 26.412 1.463 1.00 52.14 ? 110 VAL A CG2 1 ATOM 424 N N . ARG A 1 76 ? 31.440 23.033 4.600 1.00 44.92 ? 111 ARG A N 1 ATOM 425 C CA . ARG A 1 76 ? 31.586 22.304 5.860 1.00 43.90 ? 111 ARG A CA 1 ATOM 426 C C . ARG A 1 76 ? 32.525 23.055 6.793 1.00 43.78 ? 111 ARG A C 1 ATOM 427 O O . ARG A 1 76 ? 33.631 23.415 6.394 1.00 44.71 ? 111 ARG A O 1 ATOM 428 C CB . ARG A 1 76 ? 32.134 20.900 5.586 1.00 41.33 ? 111 ARG A CB 1 ATOM 429 C CG . ARG A 1 76 ? 32.595 20.118 6.818 1.00 40.17 ? 111 ARG A CG 1 ATOM 430 C CD . ARG A 1 76 ? 33.028 18.721 6.423 1.00 39.25 ? 111 ARG A CD 1 ATOM 431 N NE . ARG A 1 76 ? 31.876 17.951 5.969 1.00 36.87 ? 111 ARG A NE 1 ATOM 432 C CZ . ARG A 1 76 ? 31.097 17.197 6.739 1.00 37.61 ? 111 ARG A CZ 1 ATOM 433 N NH1 . ARG A 1 76 ? 31.344 17.055 8.038 1.00 38.22 ? 111 ARG A NH1 1 ATOM 434 N NH2 . ARG A 1 76 ? 30.061 16.557 6.199 1.00 37.10 ? 111 ARG A NH2 1 ATOM 435 N N . ASN A 1 77 ? 32.053 23.317 8.009 1.00 42.02 ? 112 ASN A N 1 ATOM 436 C CA . ASN A 1 77 ? 32.897 23.754 9.110 1.00 43.33 ? 112 ASN A CA 1 ATOM 437 C C . ASN A 1 77 ? 32.945 22.620 10.123 1.00 44.36 ? 112 ASN A C 1 ATOM 438 O O . ASN A 1 77 ? 31.921 22.278 10.731 1.00 40.22 ? 112 ASN A O 1 ATOM 439 C CB . ASN A 1 77 ? 32.349 25.033 9.745 1.00 43.78 ? 112 ASN A CB 1 ATOM 440 C CG . ASN A 1 77 ? 33.301 25.638 10.767 1.00 46.47 ? 112 ASN A CG 1 ATOM 441 O OD1 . ASN A 1 77 ? 33.819 24.951 11.635 1.00 46.33 ? 112 ASN A OD1 1 ATOM 442 N ND2 . ASN A 1 77 ? 33.531 26.940 10.668 1.00 51.29 ? 112 ASN A ND2 1 ATOM 443 N N . GLU A 1 78 ? 34.139 22.068 10.329 1.00 43.60 ? 113 GLU A N 1 ATOM 444 C CA . GLU A 1 78 ? 34.297 20.884 11.173 1.00 45.43 ? 113 GLU A CA 1 ATOM 445 C C . GLU A 1 78 ? 33.933 21.086 12.646 1.00 42.85 ? 113 GLU A C 1 ATOM 446 O O . GLU A 1 78 ? 33.626 20.121 13.323 1.00 43.82 ? 113 GLU A O 1 ATOM 447 C CB . GLU A 1 78 ? 35.715 20.310 11.059 1.00 48.26 ? 113 GLU A CB 1 ATOM 448 C CG . GLU A 1 78 ? 36.101 19.826 9.663 1.00 50.52 ? 113 GLU A CG 1 ATOM 449 C CD . GLU A 1 78 ? 35.468 18.495 9.263 1.00 54.01 ? 113 GLU A CD 1 ATOM 450 O OE1 . GLU A 1 78 ? 34.473 18.030 9.884 1.00 54.20 ? 113 GLU A OE1 1 ATOM 451 O OE2 . GLU A 1 78 ? 35.981 17.895 8.296 1.00 55.69 ? 113 GLU A OE2 1 ATOM 452 N N . GLU A 1 79 ? 33.932 22.323 13.136 1.00 43.29 ? 114 GLU A N 1 ATOM 453 C CA . GLU A 1 79 ? 33.511 22.598 14.519 1.00 43.42 ? 114 GLU A CA 1 ATOM 454 C C . GLU A 1 79 ? 32.009 22.445 14.788 1.00 37.64 ? 114 GLU A C 1 ATOM 455 O O . GLU A 1 79 ? 31.609 22.405 15.949 1.00 37.45 ? 114 GLU A O 1 ATOM 456 C CB . GLU A 1 79 ? 33.937 24.005 14.939 1.00 48.29 ? 114 GLU A CB 1 ATOM 457 C CG . GLU A 1 79 ? 35.443 24.187 15.011 1.00 53.70 ? 114 GLU A CG 1 ATOM 458 C CD . GLU A 1 79 ? 35.846 25.629 15.224 1.00 58.28 ? 114 GLU A CD 1 ATOM 459 O OE1 . GLU A 1 79 ? 34.980 26.450 15.607 1.00 63.04 ? 114 GLU A OE1 1 ATOM 460 O OE2 . GLU A 1 79 ? 37.036 25.939 15.012 1.00 66.47 ? 114 GLU A OE2 1 ATOM 461 N N . ASN A 1 80 ? 31.190 22.381 13.735 1.00 33.76 ? 115 ASN A N 1 ATOM 462 C CA . ASN A 1 80 ? 29.744 22.300 13.888 1.00 33.17 ? 115 ASN A CA 1 ATOM 463 C C . ASN A 1 80 ? 29.306 20.913 14.360 1.00 31.27 ? 115 ASN A C 1 ATOM 464 O O . ASN A 1 80 ? 29.909 19.908 13.995 1.00 29.74 ? 115 ASN A O 1 ATOM 465 C CB . ASN A 1 80 ? 29.036 22.667 12.583 1.00 33.57 ? 115 ASN A CB 1 ATOM 466 C CG . ASN A 1 80 ? 29.109 24.155 12.277 1.00 35.40 ? 115 ASN A CG 1 ATOM 467 O OD1 . ASN A 1 80 ? 29.094 24.986 13.184 1.00 35.96 ? 115 ASN A OD1 1 ATOM 468 N ND2 . ASN A 1 80 ? 29.151 24.496 10.999 1.00 35.98 ? 115 ASN A ND2 1 ATOM 469 N N . ALA A 1 81 ? 28.261 20.891 15.170 1.00 30.93 ? 116 ALA A N 1 ATOM 470 C CA . ALA A 1 81 ? 27.734 19.659 15.764 1.00 30.99 ? 116 ALA A CA 1 ATOM 471 C C . ALA A 1 81 ? 27.192 18.712 14.710 1.00 30.22 ? 116 ALA A C 1 ATOM 472 O O . ALA A 1 81 ? 27.398 17.503 14.810 1.00 29.39 ? 116 ALA A O 1 ATOM 473 C CB . ALA A 1 81 ? 26.653 19.985 16.776 1.00 30.53 ? 116 ALA A CB 1 ATOM 474 N N . CYS A 1 82 ? 26.468 19.269 13.742 1.00 29.56 ? 117 CYS A N 1 ATOM 475 C CA . CYS A 1 82 ? 26.030 18.541 12.549 1.00 29.77 ? 117 CYS A CA 1 ATOM 476 C C . CYS A 1 82 ? 26.077 19.484 11.345 1.00 29.36 ? 117 CYS A C 1 ATOM 477 O O . CYS A 1 82 ? 26.357 20.681 11.499 1.00 29.01 ? 117 CYS A O 1 ATOM 478 C CB . CYS A 1 82 ? 24.635 17.919 12.748 1.00 30.58 ? 117 CYS A CB 1 ATOM 479 S SG . CYS A 1 82 ? 23.357 19.064 13.324 1.00 31.51 ? 117 CYS A SG 1 ATOM 480 N N . HIS A 1 83 ? 25.808 18.950 10.155 1.00 27.63 ? 118 HIS A N 1 ATOM 481 C CA . HIS A 1 83 ? 26.119 19.640 8.910 1.00 29.87 ? 118 HIS A CA 1 ATOM 482 C C . HIS A 1 83 ? 24.933 19.807 7.968 1.00 29.63 ? 118 HIS A C 1 ATOM 483 O O . HIS A 1 83 ? 23.986 19.016 7.978 1.00 29.16 ? 118 HIS A O 1 ATOM 484 C CB . HIS A 1 83 ? 27.291 18.934 8.237 1.00 29.19 ? 118 HIS A CB 1 ATOM 485 C CG . HIS A 1 83 ? 28.471 18.819 9.142 1.00 30.27 ? 118 HIS A CG 1 ATOM 486 N ND1 . HIS A 1 83 ? 29.342 19.865 9.357 1.00 31.32 ? 118 HIS A ND1 1 ATOM 487 C CD2 . HIS A 1 83 ? 28.847 17.837 9.991 1.00 31.56 ? 118 HIS A CD2 1 ATOM 488 C CE1 . HIS A 1 83 ? 30.243 19.503 10.254 1.00 32.02 ? 118 HIS A CE1 1 ATOM 489 N NE2 . HIS A 1 83 ? 29.966 18.277 10.652 1.00 32.03 ? 118 HIS A NE2 1 ATOM 490 N N . CYS A 1 84 ? 25.008 20.874 7.175 1.00 29.76 ? 119 CYS A N 1 ATOM 491 C CA . CYS A 1 84 ? 24.004 21.204 6.191 1.00 30.49 ? 119 CYS A CA 1 ATOM 492 C C . CYS A 1 84 ? 24.683 21.377 4.829 1.00 29.99 ? 119 CYS A C 1 ATOM 493 O O . CYS A 1 84 ? 24.149 22.027 3.940 1.00 29.79 ? 119 CYS A O 1 ATOM 494 C CB . CYS A 1 84 ? 23.267 22.474 6.630 1.00 33.36 ? 119 CYS A CB 1 ATOM 495 S SG . CYS A 1 84 ? 22.768 22.434 8.376 1.00 36.95 ? 119 CYS A SG 1 ATOM 496 N N . SER A 1 85 ? 25.842 20.738 4.682 1.00 29.69 ? 120 SER A N 1 ATOM 497 C CA . SER A 1 85 ? 26.681 20.844 3.483 1.00 31.13 ? 120 SER A CA 1 ATOM 498 C C . SER A 1 85 ? 26.326 19.742 2.483 1.00 31.60 ? 120 SER A C 1 ATOM 499 O O . SER A 1 85 ? 25.783 18.695 2.844 1.00 29.36 ? 120 SER A O 1 ATOM 500 C CB . SER A 1 85 ? 28.159 20.732 3.884 1.00 32.36 ? 120 SER A CB 1 ATOM 501 O OG . SER A 1 85 ? 28.368 19.630 4.767 1.00 33.08 ? 120 SER A OG 1 ATOM 502 N N . GLU A 1 86 ? 26.662 19.957 1.217 1.00 31.39 ? 121 GLU A N 1 ATOM 503 C CA . GLU A 1 86 ? 26.359 18.958 0.185 1.00 33.46 ? 121 GLU A CA 1 ATOM 504 C C . GLU A 1 86 ? 27.096 17.631 0.377 1.00 33.00 ? 121 GLU A C 1 ATOM 505 O O . GLU A 1 86 ? 26.712 16.644 -0.241 1.00 34.32 ? 121 GLU A O 1 ATOM 506 C CB . GLU A 1 86 ? 26.662 19.490 -1.222 1.00 37.42 ? 121 GLU A CB 1 ATOM 507 C CG . GLU A 1 86 ? 25.698 20.563 -1.714 1.00 41.16 ? 121 GLU A CG 1 ATOM 508 C CD . GLU A 1 86 ? 24.297 20.056 -2.009 1.00 42.31 ? 121 GLU A CD 1 ATOM 509 O OE1 . GLU A 1 86 ? 24.045 18.824 -2.040 1.00 43.72 ? 121 GLU A OE1 1 ATOM 510 O OE2 . GLU A 1 86 ? 23.428 20.921 -2.210 1.00 47.08 ? 121 GLU A OE2 1 ATOM 511 N N . ASP A 1 87 ? 28.143 17.599 1.208 1.00 31.61 ? 122 ASP A N 1 ATOM 512 C CA . ASP A 1 87 ? 28.850 16.354 1.494 1.00 30.81 ? 122 ASP A CA 1 ATOM 513 C C . ASP A 1 87 ? 28.346 15.582 2.718 1.00 31.06 ? 122 ASP A C 1 ATOM 514 O O . ASP A 1 87 ? 28.892 14.526 3.041 1.00 31.26 ? 122 ASP A O 1 ATOM 515 C CB . ASP A 1 87 ? 30.342 16.615 1.636 1.00 32.36 ? 122 ASP A CB 1 ATOM 516 C CG . ASP A 1 87 ? 30.699 17.477 2.838 1.00 33.71 ? 122 ASP A CG 1 ATOM 517 O OD1 . ASP A 1 87 ? 29.866 17.722 3.753 1.00 33.96 ? 122 ASP A OD1 1 ATOM 518 O OD2 . ASP A 1 87 ? 31.856 17.926 2.871 1.00 36.49 ? 122 ASP A OD2 1 ATOM 519 N N . CYS A 1 88 ? 27.309 16.084 3.384 1.00 31.10 ? 123 CYS A N 1 ATOM 520 C CA . CYS A 1 88 ? 26.997 15.589 4.719 1.00 30.26 ? 123 CYS A CA 1 ATOM 521 C C . CYS A 1 88 ? 26.440 14.162 4.706 1.00 32.10 ? 123 CYS A C 1 ATOM 522 O O . CYS A 1 88 ? 26.757 13.361 5.602 1.00 32.73 ? 123 CYS A O 1 ATOM 523 C CB . CYS A 1 88 ? 26.112 16.585 5.487 1.00 29.51 ? 123 CYS A CB 1 ATOM 524 S SG . CYS A 1 88 ? 24.406 16.781 4.942 1.00 28.75 ? 123 CYS A SG 1 ATOM 525 N N . LEU A 1 89 ? 25.643 13.813 3.698 1.00 34.54 ? 124 LEU A N 1 ATOM 526 C CA . LEU A 1 89 ? 25.217 12.402 3.561 1.00 37.09 ? 124 LEU A CA 1 ATOM 527 C C . LEU A 1 89 ? 26.439 11.468 3.380 1.00 37.73 ? 124 LEU A C 1 ATOM 528 O O . LEU A 1 89 ? 26.517 10.435 4.028 1.00 39.34 ? 124 LEU A O 1 ATOM 529 C CB . LEU A 1 89 ? 24.205 12.214 2.424 1.00 35.12 ? 124 LEU A CB 1 ATOM 530 C CG . LEU A 1 89 ? 22.862 12.925 2.610 1.00 34.99 ? 124 LEU A CG 1 ATOM 531 C CD1 . LEU A 1 89 ? 22.095 13.059 1.310 1.00 34.86 ? 124 LEU A CD1 1 ATOM 532 C CD2 . LEU A 1 89 ? 22.001 12.201 3.643 1.00 36.19 ? 124 LEU A CD2 1 ATOM 533 N N . SER A 1 90 ? 27.411 11.860 2.556 1.00 39.82 ? 125 SER A N 1 ATOM 534 C CA . SER A 1 90 ? 28.631 11.036 2.368 1.00 40.66 ? 125 SER A CA 1 ATOM 535 C C . SER A 1 90 ? 29.413 10.800 3.672 1.00 42.07 ? 125 SER A C 1 ATOM 536 O O . SER A 1 90 ? 29.896 9.700 3.919 1.00 42.21 ? 125 SER A O 1 ATOM 537 C CB . SER A 1 90 ? 29.572 11.662 1.351 1.00 40.68 ? 125 SER A CB 1 ATOM 538 O OG . SER A 1 90 ? 30.288 12.764 1.887 1.00 41.73 ? 125 SER A OG 1 ATOM 539 N N . ARG A 1 91 ? 29.538 11.855 4.478 1.00 43.35 ? 126 ARG A N 1 ATOM 540 C CA . ARG A 1 91 ? 30.268 11.813 5.747 1.00 41.80 ? 126 ARG A CA 1 ATOM 541 C C . ARG A 1 91 ? 29.431 11.221 6.884 1.00 39.06 ? 126 ARG A C 1 ATOM 542 O O . ARG A 1 91 ? 29.953 10.998 7.988 1.00 39.19 ? 126 ARG A O 1 ATOM 543 C CB . ARG A 1 91 ? 30.735 13.223 6.127 1.00 44.67 ? 126 ARG A CB 1 ATOM 544 C CG . ARG A 1 91 ? 31.767 13.839 5.179 1.00 47.12 ? 126 ARG A CG 1 ATOM 545 C CD . ARG A 1 91 ? 33.187 13.391 5.496 1.00 52.03 ? 126 ARG A CD 1 ATOM 546 N NE . ARG A 1 91 ? 33.565 13.627 6.900 1.00 56.29 ? 126 ARG A NE 1 ATOM 547 C CZ . ARG A 1 91 ? 34.147 14.728 7.392 1.00 58.86 ? 126 ARG A CZ 1 ATOM 548 N NH1 . ARG A 1 91 ? 34.455 15.769 6.619 1.00 59.42 ? 126 ARG A NH1 1 ATOM 549 N NH2 . ARG A 1 91 ? 34.428 14.789 8.695 1.00 58.16 ? 126 ARG A NH2 1 ATOM 550 N N . GLY A 1 92 ? 28.140 10.991 6.642 1.00 38.73 ? 127 GLY A N 1 ATOM 551 C CA . GLY A 1 92 ? 27.260 10.400 7.636 1.00 34.12 ? 127 GLY A CA 1 ATOM 552 C C . GLY A 1 92 ? 26.943 11.331 8.826 1.00 36.05 ? 127 GLY A C 1 ATOM 553 O O . GLY A 1 92 ? 26.784 10.856 9.960 1.00 34.50 ? 127 GLY A O 1 ATOM 554 N N . ASP A 1 93 ? 26.802 12.641 8.575 1.00 31.14 ? 128 ASP A N 1 ATOM 555 C CA . ASP A 1 93 ? 26.669 13.619 9.663 1.00 29.01 ? 128 ASP A CA 1 ATOM 556 C C . ASP A 1 93 ? 25.787 14.844 9.384 1.00 27.33 ? 128 ASP A C 1 ATOM 557 O O . ASP A 1 93 ? 25.985 15.896 9.990 1.00 26.29 ? 128 ASP A O 1 ATOM 558 C CB . ASP A 1 93 ? 28.056 14.053 10.122 1.00 30.80 ? 128 ASP A CB 1 ATOM 559 C CG . ASP A 1 93 ? 28.872 14.702 9.010 1.00 32.60 ? 128 ASP A CG 1 ATOM 560 O OD1 . ASP A 1 93 ? 28.325 15.005 7.925 1.00 34.14 ? 128 ASP A OD1 1 ATOM 561 O OD2 . ASP A 1 93 ? 30.072 14.947 9.241 1.00 34.58 ? 128 ASP A OD2 1 ATOM 562 N N . CYS A 1 94 ? 24.789 14.710 8.521 1.00 25.78 ? 129 CYS A N 1 ATOM 563 C CA . CYS A 1 94 ? 23.827 15.795 8.319 1.00 27.00 ? 129 CYS A CA 1 ATOM 564 C C . CYS A 1 94 ? 23.004 15.977 9.591 1.00 26.71 ? 129 CYS A C 1 ATOM 565 O O . CYS A 1 94 ? 22.740 15.001 10.283 1.00 25.34 ? 129 CYS A O 1 ATOM 566 C CB . CYS A 1 94 ? 22.825 15.496 7.204 1.00 27.27 ? 129 CYS A CB 1 ATOM 567 S SG . CYS A 1 94 ? 23.483 15.089 5.587 1.00 29.19 ? 129 CYS A SG 1 ATOM 568 N N . CYS A 1 95 ? 22.563 17.203 9.862 1.00 28.49 ? 130 CYS A N 1 ATOM 569 C CA . CYS A 1 95 ? 21.556 17.403 10.909 1.00 28.71 ? 130 CYS A CA 1 ATOM 570 C C . CYS A 1 95 ? 20.312 16.649 10.430 1.00 27.48 ? 130 CYS A C 1 ATOM 571 O O . CYS A 1 95 ? 20.057 16.546 9.224 1.00 27.15 ? 130 CYS A O 1 ATOM 572 C CB . CYS A 1 95 ? 21.242 18.889 11.144 1.00 29.52 ? 130 CYS A CB 1 ATOM 573 S SG . CYS A 1 95 ? 22.641 19.949 11.633 1.00 31.58 ? 130 CYS A SG 1 ATOM 574 N N . THR A 1 96 ? 19.539 16.112 11.361 1.00 26.02 ? 131 THR A N 1 ATOM 575 C CA . THR A 1 96 ? 18.433 15.231 10.967 1.00 25.39 ? 131 THR A CA 1 ATOM 576 C C . THR A 1 96 ? 17.334 15.931 10.177 1.00 25.55 ? 131 THR A C 1 ATOM 577 O O . THR A 1 96 ? 16.586 15.268 9.473 1.00 26.83 ? 131 THR A O 1 ATOM 578 C CB . THR A 1 96 ? 17.790 14.520 12.176 1.00 23.99 ? 131 THR A CB 1 ATOM 579 O OG1 . THR A 1 96 ? 17.264 15.495 13.082 1.00 26.34 ? 131 THR A OG1 1 ATOM 580 C CG2 . THR A 1 96 ? 18.810 13.647 12.884 1.00 24.29 ? 131 THR A CG2 1 ATOM 581 N N . ASN A 1 97 ? 17.228 17.253 10.289 1.00 26.83 ? 132 ASN A N 1 ATOM 582 C CA . ASN A 1 97 ? 16.251 18.025 9.511 1.00 28.11 ? 132 ASN A CA 1 ATOM 583 C C . ASN A 1 97 ? 16.820 18.613 8.221 1.00 29.41 ? 132 ASN A C 1 ATOM 584 O O . ASN A 1 97 ? 16.162 19.439 7.594 1.00 31.77 ? 132 ASN A O 1 ATOM 585 C CB . ASN A 1 97 ? 15.668 19.158 10.353 1.00 29.19 ? 132 ASN A CB 1 ATOM 586 C CG . ASN A 1 97 ? 16.693 20.247 10.672 1.00 29.82 ? 132 ASN A CG 1 ATOM 587 O OD1 . ASN A 1 97 ? 17.905 19.991 10.732 1.00 29.98 ? 132 ASN A OD1 1 ATOM 588 N ND2 . ASN A 1 97 ? 16.211 21.455 10.906 1.00 31.81 ? 132 ASN A ND2 1 ATOM 589 N N . TYR A 1 98 ? 18.033 18.210 7.845 1.00 29.75 ? 133 TYR A N 1 ATOM 590 C CA . TYR A 1 98 ? 18.722 18.757 6.656 1.00 30.33 ? 133 TYR A CA 1 ATOM 591 C C . TYR A 1 98 ? 17.844 18.790 5.393 1.00 32.72 ? 133 TYR A C 1 ATOM 592 O O . TYR A 1 98 ? 17.644 19.849 4.790 1.00 33.92 ? 133 TYR A O 1 ATOM 593 C CB . TYR A 1 98 ? 20.043 18.013 6.411 1.00 28.67 ? 133 TYR A CB 1 ATOM 594 C CG . TYR A 1 98 ? 20.677 18.268 5.054 1.00 29.12 ? 133 TYR A CG 1 ATOM 595 C CD1 . TYR A 1 98 ? 21.122 19.547 4.699 1.00 29.45 ? 133 TYR A CD1 1 ATOM 596 C CD2 . TYR A 1 98 ? 20.833 17.240 4.134 1.00 28.55 ? 133 TYR A CD2 1 ATOM 597 C CE1 . TYR A 1 98 ? 21.699 19.788 3.460 1.00 29.89 ? 133 TYR A CE1 1 ATOM 598 C CE2 . TYR A 1 98 ? 21.394 17.472 2.889 1.00 29.48 ? 133 TYR A CE2 1 ATOM 599 C CZ . TYR A 1 98 ? 21.832 18.746 2.565 1.00 30.45 ? 133 TYR A CZ 1 ATOM 600 O OH . TYR A 1 98 ? 22.397 18.965 1.334 1.00 31.26 ? 133 TYR A OH 1 ATOM 601 N N . GLN A 1 99 ? 17.300 17.643 5.004 1.00 33.69 ? 134 GLN A N 1 ATOM 602 C CA . GLN A 1 99 ? 16.470 17.586 3.789 1.00 34.65 ? 134 GLN A CA 1 ATOM 603 C C . GLN A 1 99 ? 15.162 18.354 3.927 1.00 34.23 ? 134 GLN A C 1 ATOM 604 O O . GLN A 1 99 ? 14.704 18.945 2.957 1.00 35.31 ? 134 GLN A O 1 ATOM 605 C CB . GLN A 1 99 ? 16.203 16.152 3.336 1.00 34.66 ? 134 GLN A CB 1 ATOM 606 C CG . GLN A 1 99 ? 17.368 15.533 2.592 1.00 35.02 ? 134 GLN A CG 1 ATOM 607 C CD . GLN A 1 99 ? 17.077 14.121 2.115 1.00 37.30 ? 134 GLN A CD 1 ATOM 608 O OE1 . GLN A 1 99 ? 16.071 13.506 2.495 1.00 36.72 ? 134 GLN A OE1 1 ATOM 609 N NE2 . GLN A 1 99 ? 17.956 13.602 1.276 1.00 37.43 ? 134 GLN A NE2 1 ATOM 610 N N . VAL A 1 100 ? 14.585 18.375 5.128 1.00 34.19 ? 135 VAL A N 1 ATOM 611 C CA . VAL A 1 100 ? 13.360 19.143 5.378 1.00 35.84 ? 135 VAL A CA 1 ATOM 612 C C . VAL A 1 100 ? 13.601 20.648 5.166 1.00 37.65 ? 135 VAL A C 1 ATOM 613 O O . VAL A 1 100 ? 12.826 21.338 4.492 1.00 41.33 ? 135 VAL A O 1 ATOM 614 C CB . VAL A 1 100 ? 12.805 18.883 6.812 1.00 36.60 ? 135 VAL A CB 1 ATOM 615 C CG1 . VAL A 1 100 ? 11.665 19.838 7.143 1.00 37.52 ? 135 VAL A CG1 1 ATOM 616 C CG2 . VAL A 1 100 ? 12.331 17.437 6.967 1.00 37.45 ? 135 VAL A CG2 1 ATOM 617 N N . VAL A 1 101 ? 14.683 21.157 5.742 1.00 35.74 ? 136 VAL A N 1 ATOM 618 C CA . VAL A 1 101 ? 14.986 22.582 5.668 1.00 35.63 ? 136 VAL A CA 1 ATOM 619 C C . VAL A 1 101 ? 15.580 22.953 4.306 1.00 35.88 ? 136 VAL A C 1 ATOM 620 O O . VAL A 1 101 ? 15.215 23.973 3.730 1.00 36.54 ? 136 VAL A O 1 ATOM 621 C CB . VAL A 1 101 ? 15.956 22.994 6.804 1.00 35.23 ? 136 VAL A CB 1 ATOM 622 C CG1 . VAL A 1 101 ? 16.390 24.450 6.664 1.00 35.20 ? 136 VAL A CG1 1 ATOM 623 C CG2 . VAL A 1 101 ? 15.298 22.761 8.163 1.00 34.97 ? 136 VAL A CG2 1 ATOM 624 N N . CYS A 1 102 ? 16.495 22.130 3.807 1.00 34.82 ? 137 CYS A N 1 ATOM 625 C CA . CYS A 1 102 ? 17.289 22.480 2.624 1.00 36.45 ? 137 CYS A CA 1 ATOM 626 C C . CYS A 1 102 ? 16.800 21.910 1.303 1.00 37.17 ? 137 CYS A C 1 ATOM 627 O O . CYS A 1 102 ? 17.191 22.419 0.251 1.00 36.74 ? 137 CYS A O 1 ATOM 628 C CB . CYS A 1 102 ? 18.755 22.087 2.845 1.00 37.08 ? 137 CYS A CB 1 ATOM 629 S SG . CYS A 1 102 ? 19.474 22.880 4.309 1.00 38.67 ? 137 CYS A SG 1 ATOM 630 N N . LYS A 1 103 ? 15.969 20.865 1.338 1.00 37.10 ? 138 LYS A N 1 ATOM 631 C CA . LYS A 1 103 ? 15.535 20.174 0.114 1.00 37.38 ? 138 LYS A CA 1 ATOM 632 C C . LYS A 1 103 ? 14.015 20.018 -0.026 1.00 37.57 ? 138 LYS A C 1 ATOM 633 O O . LYS A 1 103 ? 13.560 19.212 -0.824 1.00 40.07 ? 138 LYS A O 1 ATOM 634 C CB . LYS A 1 103 ? 16.218 18.802 0.000 1.00 36.18 ? 138 LYS A CB 1 ATOM 635 C CG . LYS A 1 103 ? 17.737 18.817 0.084 1.00 37.45 ? 138 LYS A CG 1 ATOM 636 C CD . LYS A 1 103 ? 18.382 19.543 -1.104 1.00 39.94 ? 138 LYS A CD 1 ATOM 637 C CE . LYS A 1 103 ? 19.893 19.547 -0.957 1.00 40.89 ? 138 LYS A CE 1 ATOM 638 N NZ . LYS A 1 103 ? 20.565 20.130 -2.147 1.00 44.16 ? 138 LYS A NZ 1 ATOM 639 N N . GLY A 1 104 ? 13.233 20.780 0.731 1.00 39.48 ? 139 GLY A N 1 ATOM 640 C CA . GLY A 1 104 ? 11.773 20.786 0.584 1.00 40.20 ? 139 GLY A CA 1 ATOM 641 C C . GLY A 1 104 ? 11.033 19.550 1.071 1.00 41.04 ? 139 GLY A C 1 ATOM 642 O O . GLY A 1 104 ? 9.826 19.427 0.853 1.00 41.00 ? 139 GLY A O 1 ATOM 643 N N . GLU A 1 105 ? 11.736 18.656 1.762 1.00 39.73 ? 140 GLU A N 1 ATOM 644 C CA . GLU A 1 105 ? 11.146 17.404 2.215 1.00 40.89 ? 140 GLU A CA 1 ATOM 645 C C . GLU A 1 105 ? 10.287 17.636 3.448 1.00 38.82 ? 140 GLU A C 1 ATOM 646 O O . GLU A 1 105 ? 10.421 18.643 4.143 1.00 38.33 ? 140 GLU A O 1 ATOM 647 C CB . GLU A 1 105 ? 12.230 16.356 2.504 1.00 43.79 ? 140 GLU A CB 1 ATOM 648 C CG . GLU A 1 105 ? 12.402 15.334 1.389 1.00 47.17 ? 140 GLU A CG 1 ATOM 649 C CD . GLU A 1 105 ? 11.439 14.167 1.544 1.00 51.48 ? 140 GLU A CD 1 ATOM 650 O OE1 . GLU A 1 105 ? 10.211 14.405 1.723 1.00 47.66 ? 140 GLU A OE1 1 ATOM 651 O OE2 . GLU A 1 105 ? 11.926 13.011 1.521 1.00 54.94 ? 140 GLU A OE2 1 ATOM 652 N N . SER A 1 106 ? 9.396 16.693 3.704 1.00 35.73 ? 141 SER A N 1 ATOM 653 C CA . SER A 1 106 ? 8.505 16.761 4.849 1.00 33.93 ? 141 SER A CA 1 ATOM 654 C C . SER A 1 106 ? 9.107 15.982 6.027 1.00 30.84 ? 141 SER A C 1 ATOM 655 O O . SER A 1 106 ? 9.874 15.029 5.821 1.00 29.94 ? 141 SER A O 1 ATOM 656 C CB . SER A 1 106 ? 7.148 16.177 4.461 1.00 33.93 ? 141 SER A CB 1 ATOM 657 O OG . SER A 1 106 ? 7.292 14.828 4.054 1.00 32.54 ? 141 SER A OG 1 ATOM 658 N N . HIS A 1 107 ? 8.774 16.404 7.249 1.00 29.63 ? 142 HIS A N 1 ATOM 659 C CA . HIS A 1 107 ? 9.071 15.618 8.456 1.00 27.80 ? 142 HIS A CA 1 ATOM 660 C C . HIS A 1 107 ? 8.330 14.297 8.366 1.00 25.96 ? 142 HIS A C 1 ATOM 661 O O . HIS A 1 107 ? 7.177 14.251 7.901 1.00 26.04 ? 142 HIS A O 1 ATOM 662 C CB . HIS A 1 107 ? 8.621 16.329 9.728 1.00 29.07 ? 142 HIS A CB 1 ATOM 663 C CG . HIS A 1 107 ? 9.460 17.505 10.104 1.00 30.58 ? 142 HIS A CG 1 ATOM 664 N ND1 . HIS A 1 107 ? 10.732 17.376 10.618 1.00 30.84 ? 142 HIS A ND1 1 ATOM 665 C CD2 . HIS A 1 107 ? 9.191 18.830 10.091 1.00 31.78 ? 142 HIS A CD2 1 ATOM 666 C CE1 . HIS A 1 107 ? 11.223 18.574 10.875 1.00 33.09 ? 142 HIS A CE1 1 ATOM 667 N NE2 . HIS A 1 107 ? 10.307 19.473 10.566 1.00 32.39 ? 142 HIS A NE2 1 ATOM 668 N N . TRP A 1 108 ? 8.975 13.237 8.848 1.00 26.17 ? 143 TRP A N 1 ATOM 669 C CA . TRP A 1 108 ? 8.378 11.913 8.896 1.00 24.69 ? 143 TRP A CA 1 ATOM 670 C C . TRP A 1 108 ? 6.994 11.921 9.575 1.00 24.64 ? 143 TRP A C 1 ATOM 671 O O . TRP A 1 108 ? 6.061 11.304 9.081 1.00 24.03 ? 143 TRP A O 1 ATOM 672 C CB . TRP A 1 108 ? 9.316 10.929 9.609 1.00 24.34 ? 143 TRP A CB 1 ATOM 673 C CG . TRP A 1 108 ? 8.729 9.559 9.775 1.00 22.78 ? 143 TRP A CG 1 ATOM 674 C CD1 . TRP A 1 108 ? 8.720 8.567 8.864 1.00 22.71 ? 143 TRP A CD1 1 ATOM 675 C CD2 . TRP A 1 108 ? 8.066 9.050 10.934 1.00 22.85 ? 143 TRP A CD2 1 ATOM 676 N NE1 . TRP A 1 108 ? 8.094 7.450 9.371 1.00 24.07 ? 143 TRP A NE1 1 ATOM 677 C CE2 . TRP A 1 108 ? 7.673 7.726 10.645 1.00 22.78 ? 143 TRP A CE2 1 ATOM 678 C CE3 . TRP A 1 108 ? 7.760 9.589 12.184 1.00 22.84 ? 143 TRP A CE3 1 ATOM 679 C CZ2 . TRP A 1 108 ? 7.009 6.928 11.569 1.00 22.87 ? 143 TRP A CZ2 1 ATOM 680 C CZ3 . TRP A 1 108 ? 7.090 8.804 13.097 1.00 22.71 ? 143 TRP A CZ3 1 ATOM 681 C CH2 . TRP A 1 108 ? 6.713 7.484 12.782 1.00 22.81 ? 143 TRP A CH2 1 ATOM 682 N N . VAL A 1 109 ? 6.865 12.637 10.684 1.00 24.87 ? 144 VAL A N 1 ATOM 683 C CA . VAL A 1 109 ? 5.604 12.664 11.439 1.00 26.31 ? 144 VAL A CA 1 ATOM 684 C C . VAL A 1 109 ? 4.431 13.268 10.647 1.00 28.59 ? 144 VAL A C 1 ATOM 685 O O . VAL A 1 109 ? 3.269 12.906 10.877 1.00 28.51 ? 144 VAL A O 1 ATOM 686 C CB . VAL A 1 109 ? 5.774 13.384 12.796 1.00 25.79 ? 144 VAL A CB 1 ATOM 687 C CG1 . VAL A 1 109 ? 5.887 14.900 12.609 1.00 27.16 ? 144 VAL A CG1 1 ATOM 688 C CG2 . VAL A 1 109 ? 4.651 13.010 13.757 1.00 26.42 ? 144 VAL A CG2 1 ATOM 689 N N . ASP A 1 110 ? 4.738 14.155 9.701 1.00 29.09 ? 145 ASP A N 1 ATOM 690 C CA . ASP A 1 110 ? 3.707 14.786 8.869 1.00 33.47 ? 145 ASP A CA 1 ATOM 691 C C . ASP A 1 110 ? 3.262 13.918 7.694 1.00 34.18 ? 145 ASP A C 1 ATOM 692 O O . ASP A 1 110 ? 2.295 14.248 7.045 1.00 37.72 ? 145 ASP A O 1 ATOM 693 C CB . ASP A 1 110 ? 4.177 16.159 8.393 1.00 34.88 ? 145 ASP A CB 1 ATOM 694 C CG . ASP A 1 110 ? 4.432 17.112 9.550 1.00 35.94 ? 145 ASP A CG 1 ATOM 695 O OD1 . ASP A 1 110 ? 3.625 17.142 10.489 1.00 38.29 ? 145 ASP A OD1 1 ATOM 696 O OD2 . ASP A 1 110 ? 5.443 17.830 9.537 1.00 38.07 ? 145 ASP A OD2 1 ATOM 697 N N . ASP A 1 111 ? 3.948 12.801 7.445 1.00 32.68 ? 146 ASP A N 1 ATOM 698 C CA . ASP A 1 111 ? 3.586 11.904 6.361 1.00 33.91 ? 146 ASP A CA 1 ATOM 699 C C . ASP A 1 111 ? 2.486 10.962 6.797 1.00 33.85 ? 146 ASP A C 1 ATOM 700 O O . ASP A 1 111 ? 2.446 10.549 7.958 1.00 30.95 ? 146 ASP A O 1 ATOM 701 C CB . ASP A 1 111 ? 4.805 11.096 5.908 1.00 33.85 ? 146 ASP A CB 1 ATOM 702 C CG . ASP A 1 111 ? 5.906 11.973 5.338 1.00 34.88 ? 146 ASP A CG 1 ATOM 703 O OD1 . ASP A 1 111 ? 5.599 13.105 4.916 1.00 34.28 ? 146 ASP A OD1 1 ATOM 704 O OD2 . ASP A 1 111 ? 7.078 11.529 5.310 1.00 33.71 ? 146 ASP A OD2 1 ATOM 705 N N . ASP A 1 112 ? 1.614 10.606 5.856 1.00 34.24 ? 147 ASP A N 1 ATOM 706 C CA . ASP A 1 112 ? 0.576 9.613 6.102 1.00 36.53 ? 147 ASP A CA 1 ATOM 707 C C . ASP A 1 112 ? 1.193 8.287 6.491 1.00 35.56 ? 147 ASP A C 1 ATOM 708 O O . ASP A 1 112 ? 2.254 7.902 6.005 1.00 35.41 ? 147 ASP A O 1 ATOM 709 C CB . ASP A 1 112 ? -0.290 9.354 4.858 1.00 39.61 ? 147 ASP A CB 1 ATOM 710 C CG . ASP A 1 112 ? -1.335 10.426 4.616 1.00 43.18 ? 147 ASP A CG 1 ATOM 711 O OD1 . ASP A 1 112 ? -1.620 11.236 5.524 1.00 46.94 ? 147 ASP A OD1 1 ATOM 712 O OD2 . ASP A 1 112 ? -1.895 10.429 3.506 1.00 45.23 ? 147 ASP A OD2 1 ATOM 713 N N . CYS A 1 113 ? 0.495 7.605 7.371 1.00 36.07 ? 148 CYS A N 1 ATOM 714 C CA . CYS A 1 113 ? 0.696 6.200 7.636 1.00 38.66 ? 148 CYS A CA 1 ATOM 715 C C . CYS A 1 113 ? 0.562 5.380 6.347 1.00 36.68 ? 148 CYS A C 1 ATOM 716 O O . CYS A 1 113 ? -0.482 5.424 5.699 1.00 36.62 ? 148 CYS A O 1 ATOM 717 C CB . CYS A 1 113 ? -0.395 5.780 8.610 1.00 46.44 ? 148 CYS A CB 1 ATOM 718 S SG . CYS A 1 113 ? -0.059 4.343 9.597 1.00 54.76 ? 148 CYS A SG 1 ATOM 719 N N . GLU A 1 114 ? 1.607 4.655 5.960 1.00 33.94 ? 149 GLU A N 1 ATOM 720 C CA . GLU A 1 114 ? 1.548 3.799 4.773 1.00 33.82 ? 149 GLU A CA 1 ATOM 721 C C . GLU A 1 114 ? 2.102 2.427 5.121 1.00 30.51 ? 149 GLU A C 1 ATOM 722 O O . GLU A 1 114 ? 3.238 2.308 5.569 1.00 28.67 ? 149 GLU A O 1 ATOM 723 C CB . GLU A 1 114 ? 2.352 4.419 3.613 1.00 36.57 ? 149 GLU A CB 1 ATOM 724 C CG . GLU A 1 114 ? 2.260 3.659 2.294 1.00 41.55 ? 149 GLU A CG 1 ATOM 725 C CD . GLU A 1 114 ? 3.207 4.179 1.202 1.00 47.27 ? 149 GLU A CD 1 ATOM 726 O OE1 . GLU A 1 114 ? 3.931 5.182 1.423 1.00 47.05 ? 149 GLU A OE1 1 ATOM 727 O OE2 . GLU A 1 114 ? 3.223 3.575 0.102 1.00 48.16 ? 149 GLU A OE2 1 ATOM 728 N N . GLU A 1 115 ? 1.316 1.393 4.854 1.00 28.37 ? 150 GLU A N 1 ATOM 729 C CA . GLU A 1 115 ? 1.715 0.024 5.150 1.00 29.59 ? 150 GLU A CA 1 ATOM 730 C C . GLU A 1 115 ? 3.070 -0.335 4.535 1.00 28.63 ? 150 GLU A C 1 ATOM 731 O O . GLU A 1 115 ? 3.362 0.065 3.399 1.00 27.26 ? 150 GLU A O 1 ATOM 732 C CB . GLU A 1 115 ? 0.631 -0.947 4.661 1.00 31.27 ? 150 GLU A CB 1 ATOM 733 C CG . GLU A 1 115 ? 0.903 -2.397 5.027 1.00 33.85 ? 150 GLU A CG 1 ATOM 734 C CD . GLU A 1 115 ? -0.314 -3.296 4.897 1.00 36.18 ? 150 GLU A CD 1 ATOM 735 O OE1 . GLU A 1 115 ? -1.368 -2.874 4.380 1.00 39.21 ? 150 GLU A OE1 1 ATOM 736 O OE2 . GLU A 1 115 ? -0.202 -4.447 5.335 1.00 37.13 ? 150 GLU A OE2 1 ATOM 737 N N . ILE A 1 116 ? 3.885 -1.076 5.288 1.00 26.37 ? 151 ILE A N 1 ATOM 738 C CA . ILE A 1 116 ? 5.198 -1.569 4.822 1.00 27.38 ? 151 ILE A CA 1 ATOM 739 C C . ILE A 1 116 ? 5.128 -3.083 4.671 1.00 28.70 ? 151 ILE A C 1 ATOM 740 O O . ILE A 1 116 ? 5.404 -3.826 5.622 1.00 29.25 ? 151 ILE A O 1 ATOM 741 C CB . ILE A 1 116 ? 6.364 -1.214 5.776 1.00 26.93 ? 151 ILE A CB 1 ATOM 742 C CG1 . ILE A 1 116 ? 6.377 0.276 6.134 1.00 28.64 ? 151 ILE A CG1 1 ATOM 743 C CG2 . ILE A 1 116 ? 7.702 -1.571 5.133 1.00 27.89 ? 151 ILE A CG2 1 ATOM 744 C CD1 . ILE A 1 116 ? 7.040 0.560 7.461 1.00 28.45 ? 151 ILE A CD1 1 ATOM 745 N N . LYS A 1 117 ? 4.784 -3.547 3.470 1.00 30.05 ? 152 LYS A N 1 ATOM 746 C CA . LYS A 1 117 ? 4.572 -4.982 3.242 1.00 33.03 ? 152 LYS A CA 1 ATOM 747 C C . LYS A 1 117 ? 5.863 -5.806 3.189 1.00 32.74 ? 152 LYS A C 1 ATOM 748 O O . LYS A 1 117 ? 5.862 -6.969 3.607 1.00 32.76 ? 152 LYS A O 1 ATOM 749 C CB . LYS A 1 117 ? 3.783 -5.213 1.967 1.00 36.27 ? 152 LYS A CB 1 ATOM 750 C CG . LYS A 1 117 ? 2.398 -4.602 1.967 1.00 40.46 ? 152 LYS A CG 1 ATOM 751 C CD . LYS A 1 117 ? 1.795 -4.668 0.575 1.00 44.87 ? 152 LYS A CD 1 ATOM 752 C CE . LYS A 1 117 ? 0.482 -3.908 0.498 1.00 51.40 ? 152 LYS A CE 1 ATOM 753 N NZ . LYS A 1 117 ? -0.587 -4.565 1.308 1.00 54.13 ? 152 LYS A NZ 1 ATOM 754 N N . VAL A 1 118 ? 6.939 -5.214 2.662 1.00 31.42 ? 153 VAL A N 1 ATOM 755 C CA . VAL A 1 118 ? 8.268 -5.849 2.595 1.00 30.95 ? 153 VAL A CA 1 ATOM 756 C C . VAL A 1 118 ? 9.325 -4.796 2.879 1.00 27.53 ? 153 VAL A C 1 ATOM 757 O O . VAL A 1 118 ? 9.065 -3.622 2.655 1.00 29.27 ? 153 VAL A O 1 ATOM 758 C CB . VAL A 1 118 ? 8.546 -6.485 1.209 1.00 34.19 ? 153 VAL A CB 1 ATOM 759 C CG1 . VAL A 1 118 ? 7.577 -7.622 0.940 1.00 36.28 ? 153 VAL A CG1 1 ATOM 760 C CG2 . VAL A 1 118 ? 8.468 -5.456 0.082 1.00 35.30 ? 153 VAL A CG2 1 ATOM 761 N N . PRO A 1 119 ? 10.513 -5.198 3.379 1.00 26.01 ? 154 PRO A N 1 ATOM 762 C CA . PRO A 1 119 ? 11.506 -4.177 3.636 1.00 24.26 ? 154 PRO A CA 1 ATOM 763 C C . PRO A 1 119 ? 11.855 -3.442 2.352 1.00 25.67 ? 154 PRO A C 1 ATOM 764 O O . PRO A 1 119 ? 11.949 -4.071 1.302 1.00 26.26 ? 154 PRO A O 1 ATOM 765 C CB . PRO A 1 119 ? 12.708 -4.967 4.146 1.00 25.84 ? 154 PRO A CB 1 ATOM 766 C CG . PRO A 1 119 ? 12.129 -6.245 4.672 1.00 26.72 ? 154 PRO A CG 1 ATOM 767 C CD . PRO A 1 119 ? 11.007 -6.537 3.739 1.00 26.13 ? 154 PRO A CD 1 ATOM 768 N N . GLU A 1 120 ? 11.966 -2.125 2.442 1.00 24.87 ? 155 GLU A N 1 ATOM 769 C CA . GLU A 1 120 ? 12.377 -1.287 1.306 1.00 26.14 ? 155 GLU A CA 1 ATOM 770 C C . GLU A 1 120 ? 13.725 -0.706 1.671 1.00 26.70 ? 155 GLU A C 1 ATOM 771 O O . GLU A 1 120 ? 13.821 0.407 2.160 1.00 29.10 ? 155 GLU A O 1 ATOM 772 C CB . GLU A 1 120 ? 11.334 -0.220 1.025 1.00 26.18 ? 155 GLU A CB 1 ATOM 773 C CG . GLU A 1 120 ? 10.013 -0.824 0.577 1.00 28.39 ? 155 GLU A CG 1 ATOM 774 C CD . GLU A 1 120 ? 8.911 0.200 0.347 1.00 29.26 ? 155 GLU A CD 1 ATOM 775 O OE1 . GLU A 1 120 ? 9.203 1.408 0.296 1.00 29.61 ? 155 GLU A OE1 1 ATOM 776 O OE2 . GLU A 1 120 ? 7.731 -0.201 0.239 1.00 32.16 ? 155 GLU A OE2 1 ATOM 777 N N . CYS A 1 121 ? 14.768 -1.504 1.460 1.00 27.86 ? 156 CYS A N 1 ATOM 778 C CA . CYS A 1 121 ? 16.101 -1.167 1.895 1.00 28.01 ? 156 CYS A CA 1 ATOM 779 C C . CYS A 1 121 ? 16.951 -0.784 0.700 1.00 28.41 ? 156 CYS A C 1 ATOM 780 O O . CYS A 1 121 ? 16.762 -1.330 -0.392 1.00 28.39 ? 156 CYS A O 1 ATOM 781 C CB . CYS A 1 121 ? 16.741 -2.337 2.644 1.00 30.00 ? 156 CYS A CB 1 ATOM 782 S SG . CYS A 1 121 ? 15.958 -2.680 4.251 1.00 32.45 ? 156 CYS A SG 1 ATOM 783 N N . PRO A 1 122 ? 17.901 0.150 0.896 1.00 27.79 ? 157 PRO A N 1 ATOM 784 C CA . PRO A 1 122 ? 18.762 0.531 -0.228 1.00 27.25 ? 157 PRO A CA 1 ATOM 785 C C . PRO A 1 122 ? 19.741 -0.557 -0.646 1.00 25.52 ? 157 PRO A C 1 ATOM 786 O O . PRO A 1 122 ? 19.867 -1.579 0.024 1.00 23.50 ? 157 PRO A O 1 ATOM 787 C CB . PRO A 1 122 ? 19.574 1.724 0.319 1.00 29.77 ? 157 PRO A CB 1 ATOM 788 C CG . PRO A 1 122 ? 18.971 2.114 1.605 1.00 29.20 ? 157 PRO A CG 1 ATOM 789 C CD . PRO A 1 122 ? 18.171 0.956 2.107 1.00 27.82 ? 157 PRO A CD 1 ATOM 790 N N . ALA A 1 123 ? 20.448 -0.318 -1.752 1.00 23.73 ? 158 ALA A N 1 ATOM 791 C CA . ALA A 1 123 ? 21.511 -1.209 -2.203 1.00 23.99 ? 158 ALA A CA 1 ATOM 792 C C . ALA A 1 123 ? 22.482 -1.593 -1.097 1.00 23.25 ? 158 ALA A C 1 ATOM 793 O O . ALA A 1 123 ? 22.831 -0.754 -0.283 1.00 23.49 ? 158 ALA A O 1 ATOM 794 C CB . ALA A 1 123 ? 22.292 -0.543 -3.314 1.00 24.64 ? 158 ALA A CB 1 ATOM 795 N N . GLY A 1 124 ? 22.880 -2.862 -1.047 1.00 24.11 ? 159 GLY A N 1 ATOM 796 C CA . GLY A 1 124 ? 23.913 -3.308 -0.103 1.00 24.39 ? 159 GLY A CA 1 ATOM 797 C C . GLY A 1 124 ? 23.407 -3.752 1.251 1.00 24.58 ? 159 GLY A C 1 ATOM 798 O O . GLY A 1 124 ? 24.152 -4.376 1.998 1.00 24.21 ? 159 GLY A O 1 ATOM 799 N N . PHE A 1 125 ? 22.150 -3.438 1.569 1.00 25.08 ? 160 PHE A N 1 ATOM 800 C CA . PHE A 1 125 ? 21.511 -3.922 2.792 1.00 25.27 ? 160 PHE A CA 1 ATOM 801 C C . PHE A 1 125 ? 21.070 -5.366 2.589 1.00 28.76 ? 160 PHE A C 1 ATOM 802 O O . PHE A 1 125 ? 20.360 -5.662 1.634 1.00 31.48 ? 160 PHE A O 1 ATOM 803 C CB . PHE A 1 125 ? 20.334 -3.021 3.178 1.00 24.37 ? 160 PHE A CB 1 ATOM 804 C CG . PHE A 1 125 ? 20.761 -1.761 3.859 1.00 23.45 ? 160 PHE A CG 1 ATOM 805 C CD1 . PHE A 1 125 ? 21.371 -0.741 3.135 1.00 24.12 ? 160 PHE A CD1 1 ATOM 806 C CD2 . PHE A 1 125 ? 20.618 -1.603 5.237 1.00 22.55 ? 160 PHE A CD2 1 ATOM 807 C CE1 . PHE A 1 125 ? 21.796 0.414 3.757 1.00 23.60 ? 160 PHE A CE1 1 ATOM 808 C CE2 . PHE A 1 125 ? 21.051 -0.455 5.857 1.00 22.55 ? 160 PHE A CE2 1 ATOM 809 C CZ . PHE A 1 125 ? 21.646 0.554 5.123 1.00 23.28 ? 160 PHE A CZ 1 ATOM 810 N N . VAL A 1 126 ? 21.509 -6.256 3.482 1.00 29.93 ? 161 VAL A N 1 ATOM 811 C CA . VAL A 1 126 ? 21.229 -7.707 3.390 1.00 29.51 ? 161 VAL A CA 1 ATOM 812 C C . VAL A 1 126 ? 20.104 -8.178 4.309 1.00 29.52 ? 161 VAL A C 1 ATOM 813 O O . VAL A 1 126 ? 19.615 -9.290 4.176 1.00 28.27 ? 161 VAL A O 1 ATOM 814 C CB . VAL A 1 126 ? 22.494 -8.559 3.665 1.00 33.06 ? 161 VAL A CB 1 ATOM 815 C CG1 . VAL A 1 126 ? 23.652 -8.094 2.784 1.00 35.80 ? 161 VAL A CG1 1 ATOM 816 C CG2 . VAL A 1 126 ? 22.888 -8.555 5.139 1.00 33.58 ? 161 VAL A CG2 1 ATOM 817 N N . ARG A 1 127 ? 19.700 -7.333 5.241 1.00 24.36 ? 162 ARG A N 1 ATOM 818 C CA . ARG A 1 127 ? 18.596 -7.638 6.141 1.00 23.24 ? 162 ARG A CA 1 ATOM 819 C C . ARG A 1 127 ? 18.087 -6.299 6.695 1.00 21.71 ? 162 ARG A C 1 ATOM 820 O O . ARG A 1 127 ? 18.861 -5.347 6.770 1.00 20.28 ? 162 ARG A O 1 ATOM 821 C CB . ARG A 1 127 ? 19.042 -8.582 7.270 1.00 24.90 ? 162 ARG A CB 1 ATOM 822 C CG . ARG A 1 127 ? 20.030 -7.986 8.274 1.00 24.95 ? 162 ARG A CG 1 ATOM 823 C CD . ARG A 1 127 ? 20.457 -9.015 9.330 1.00 25.91 ? 162 ARG A CD 1 ATOM 824 N NE . ARG A 1 127 ? 21.362 -10.035 8.789 1.00 26.35 ? 162 ARG A NE 1 ATOM 825 C CZ . ARG A 1 127 ? 22.670 -9.880 8.566 1.00 28.15 ? 162 ARG A CZ 1 ATOM 826 N NH1 . ARG A 1 127 ? 23.302 -8.730 8.822 1.00 26.65 ? 162 ARG A NH1 1 ATOM 827 N NH2 . ARG A 1 127 ? 23.361 -10.899 8.068 1.00 31.16 ? 162 ARG A NH2 1 ATOM 828 N N . PRO A 1 128 ? 16.814 -6.230 7.128 1.00 20.65 ? 163 PRO A N 1 ATOM 829 C CA . PRO A 1 128 ? 16.380 -4.976 7.764 1.00 20.39 ? 163 PRO A CA 1 ATOM 830 C C . PRO A 1 128 ? 17.099 -4.758 9.082 1.00 19.82 ? 163 PRO A C 1 ATOM 831 O O . PRO A 1 128 ? 17.102 -5.667 9.905 1.00 20.03 ? 163 PRO A O 1 ATOM 832 C CB . PRO A 1 128 ? 14.889 -5.187 8.019 1.00 20.96 ? 163 PRO A CB 1 ATOM 833 C CG . PRO A 1 128 ? 14.609 -6.616 7.736 1.00 22.78 ? 163 PRO A CG 1 ATOM 834 C CD . PRO A 1 128 ? 15.697 -7.149 6.869 1.00 21.61 ? 163 PRO A CD 1 ATOM 835 N N . PRO A 1 129 ? 17.732 -3.584 9.284 1.00 19.27 ? 164 PRO A N 1 ATOM 836 C CA . PRO A 1 129 ? 18.340 -3.369 10.588 1.00 17.34 ? 164 PRO A CA 1 ATOM 837 C C . PRO A 1 129 ? 17.276 -3.302 11.683 1.00 17.07 ? 164 PRO A C 1 ATOM 838 O O . PRO A 1 129 ? 16.088 -3.102 11.376 1.00 16.21 ? 164 PRO A O 1 ATOM 839 C CB . PRO A 1 129 ? 19.021 -2.003 10.450 1.00 17.53 ? 164 PRO A CB 1 ATOM 840 C CG . PRO A 1 129 ? 19.271 -1.864 8.965 1.00 18.10 ? 164 PRO A CG 1 ATOM 841 C CD . PRO A 1 129 ? 18.068 -2.504 8.338 1.00 18.88 ? 164 PRO A CD 1 ATOM 842 N N . LEU A 1 130 ? 17.716 -3.489 12.926 1.00 17.02 ? 165 LEU A N 1 ATOM 843 C CA . LEU A 1 130 ? 16.861 -3.313 14.104 1.00 16.12 ? 165 LEU A CA 1 ATOM 844 C C . LEU A 1 130 ? 17.469 -2.199 14.937 1.00 15.81 ? 165 LEU A C 1 ATOM 845 O O . LEU A 1 130 ? 18.691 -2.205 15.221 1.00 15.77 ? 165 LEU A O 1 ATOM 846 C CB . LEU A 1 130 ? 16.782 -4.600 14.921 1.00 16.50 ? 165 LEU A CB 1 ATOM 847 C CG . LEU A 1 130 ? 16.077 -4.529 16.280 1.00 16.45 ? 165 LEU A CG 1 ATOM 848 C CD1 . LEU A 1 130 ? 14.594 -4.215 16.092 1.00 17.69 ? 165 LEU A CD1 1 ATOM 849 C CD2 . LEU A 1 130 ? 16.282 -5.829 17.069 1.00 16.68 ? 165 LEU A CD2 1 ATOM 850 N N . ILE A 1 131 ? 16.617 -1.245 15.326 1.00 15.75 ? 166 ILE A N 1 ATOM 851 C CA . ILE A 1 131 ? 16.991 -0.228 16.296 1.00 16.08 ? 166 ILE A CA 1 ATOM 852 C C . ILE A 1 131 ? 16.085 -0.328 17.516 1.00 15.36 ? 166 ILE A C 1 ATOM 853 O O . ILE A 1 131 ? 14.853 -0.249 17.383 1.00 15.03 ? 166 ILE A O 1 ATOM 854 C CB . ILE A 1 131 ? 16.892 1.185 15.714 1.00 17.41 ? 166 ILE A CB 1 ATOM 855 C CG1 . ILE A 1 131 ? 17.761 1.306 14.453 1.00 19.50 ? 166 ILE A CG1 1 ATOM 856 C CG2 . ILE A 1 131 ? 17.353 2.195 16.751 1.00 17.96 ? 166 ILE A CG2 1 ATOM 857 C CD1 . ILE A 1 131 ? 17.521 2.582 13.686 1.00 21.69 ? 166 ILE A CD1 1 ATOM 858 N N . ILE A 1 132 ? 16.705 -0.518 18.677 1.00 14.83 ? 167 ILE A N 1 ATOM 859 C CA . ILE A 1 132 ? 16.000 -0.585 19.959 1.00 16.30 ? 167 ILE A CA 1 ATOM 860 C C . ILE A 1 132 ? 16.127 0.772 20.615 1.00 17.94 ? 167 ILE A C 1 ATOM 861 O O . ILE A 1 132 ? 17.230 1.211 20.876 1.00 19.72 ? 167 ILE A O 1 ATOM 862 C CB . ILE A 1 132 ? 16.605 -1.661 20.865 1.00 16.78 ? 167 ILE A CB 1 ATOM 863 C CG1 . ILE A 1 132 ? 16.484 -3.028 20.203 1.00 18.16 ? 167 ILE A CG1 1 ATOM 864 C CG2 . ILE A 1 132 ? 15.883 -1.686 22.218 1.00 16.89 ? 167 ILE A CG2 1 ATOM 865 C CD1 . ILE A 1 132 ? 17.697 -3.892 20.401 1.00 19.80 ? 167 ILE A CD1 1 ATOM 866 N N . PHE A 1 133 ? 14.993 1.433 20.843 1.00 17.71 ? 168 PHE A N 1 ATOM 867 C CA . PHE A 1 133 ? 14.955 2.779 21.397 1.00 16.24 ? 168 PHE A CA 1 ATOM 868 C C . PHE A 1 133 ? 14.394 2.594 22.805 1.00 16.44 ? 168 PHE A C 1 ATOM 869 O O . PHE A 1 133 ? 13.192 2.455 22.970 1.00 16.17 ? 168 PHE A O 1 ATOM 870 C CB . PHE A 1 133 ? 14.072 3.659 20.519 1.00 17.58 ? 168 PHE A CB 1 ATOM 871 C CG . PHE A 1 133 ? 14.143 5.116 20.844 1.00 17.61 ? 168 PHE A CG 1 ATOM 872 C CD1 . PHE A 1 133 ? 13.594 5.616 22.009 1.00 16.96 ? 168 PHE A CD1 1 ATOM 873 C CD2 . PHE A 1 133 ? 14.713 6.009 19.948 1.00 19.38 ? 168 PHE A CD2 1 ATOM 874 C CE1 . PHE A 1 133 ? 13.650 6.966 22.296 1.00 18.60 ? 168 PHE A CE1 1 ATOM 875 C CE2 . PHE A 1 133 ? 14.758 7.362 20.222 1.00 19.68 ? 168 PHE A CE2 1 ATOM 876 C CZ . PHE A 1 133 ? 14.237 7.849 21.397 1.00 19.64 ? 168 PHE A CZ 1 ATOM 877 N N . SER A 1 134 ? 15.287 2.571 23.795 1.00 17.81 ? 169 SER A N 1 ATOM 878 C CA . SER A 1 134 ? 14.945 2.294 25.196 1.00 19.16 ? 169 SER A CA 1 ATOM 879 C C . SER A 1 134 ? 14.774 3.594 25.990 1.00 17.98 ? 169 SER A C 1 ATOM 880 O O . SER A 1 134 ? 15.634 4.469 25.950 1.00 17.56 ? 169 SER A O 1 ATOM 881 C CB . SER A 1 134 ? 16.044 1.455 25.879 1.00 23.06 ? 169 SER A CB 1 ATOM 882 O OG . SER A 1 134 ? 15.864 0.094 25.576 1.00 30.79 ? 169 SER A OG 1 ATOM 883 N N . VAL A 1 135 ? 13.661 3.704 26.713 1.00 16.90 ? 170 VAL A N 1 ATOM 884 C CA . VAL A 1 135 ? 13.361 4.886 27.503 1.00 18.00 ? 170 VAL A CA 1 ATOM 885 C C . VAL A 1 135 ? 13.231 4.443 28.947 1.00 19.12 ? 170 VAL A C 1 ATOM 886 O O . VAL A 1 135 ? 12.565 3.506 29.231 1.00 22.64 ? 170 VAL A O 1 ATOM 887 C CB . VAL A 1 135 ? 12.106 5.640 27.003 1.00 18.21 ? 170 VAL A CB 1 ATOM 888 C CG1 . VAL A 1 135 ? 12.484 6.518 25.814 1.00 18.67 ? 170 VAL A CG1 1 ATOM 889 C CG2 . VAL A 1 135 ? 10.992 4.694 26.604 1.00 19.12 ? 170 VAL A CG2 1 ATOM 890 N N . ASP A 1 136 ? 13.969 5.075 29.826 1.00 18.59 ? 171 ASP A N 1 ATOM 891 C CA . ASP A 1 136 ? 14.006 4.665 31.224 1.00 17.20 ? 171 ASP A CA 1 ATOM 892 C C . ASP A 1 136 ? 12.783 5.227 31.956 1.00 18.76 ? 171 ASP A C 1 ATOM 893 O O . ASP A 1 136 ? 12.509 6.418 31.876 1.00 18.43 ? 171 ASP A O 1 ATOM 894 C CB . ASP A 1 136 ? 15.291 5.184 31.855 1.00 18.67 ? 171 ASP A CB 1 ATOM 895 C CG . ASP A 1 136 ? 15.655 4.453 33.115 1.00 20.43 ? 171 ASP A CG 1 ATOM 896 O OD1 . ASP A 1 136 ? 14.767 4.186 33.904 1.00 17.61 ? 171 ASP A OD1 1 ATOM 897 O OD2 . ASP A 1 136 ? 16.836 4.163 33.329 1.00 23.96 ? 171 ASP A OD2 1 ATOM 898 N N . GLY A 1 137 ? 12.097 4.382 32.717 1.00 16.11 ? 172 GLY A N 1 ATOM 899 C CA . GLY A 1 137 ? 10.978 4.822 33.534 1.00 16.54 ? 172 GLY A CA 1 ATOM 900 C C . GLY A 1 137 ? 9.751 5.353 32.813 1.00 17.60 ? 172 GLY A C 1 ATOM 901 O O . GLY A 1 137 ? 9.027 6.168 33.383 1.00 17.96 ? 172 GLY A O 1 ATOM 902 N N . PHE A 1 138 ? 9.530 4.924 31.561 1.00 18.22 ? 173 PHE A N 1 ATOM 903 C CA . PHE A 1 138 ? 8.386 5.348 30.771 1.00 18.58 ? 173 PHE A CA 1 ATOM 904 C C . PHE A 1 138 ? 7.195 4.478 31.146 1.00 19.12 ? 173 PHE A C 1 ATOM 905 O O . PHE A 1 138 ? 7.063 3.355 30.703 1.00 18.17 ? 173 PHE A O 1 ATOM 906 C CB . PHE A 1 138 ? 8.733 5.225 29.286 1.00 19.27 ? 173 PHE A CB 1 ATOM 907 C CG . PHE A 1 138 ? 7.823 6.014 28.352 1.00 19.05 ? 173 PHE A CG 1 ATOM 908 C CD1 . PHE A 1 138 ? 6.487 5.642 28.156 1.00 19.46 ? 173 PHE A CD1 1 ATOM 909 C CD2 . PHE A 1 138 ? 8.313 7.094 27.625 1.00 20.22 ? 173 PHE A CD2 1 ATOM 910 C CE1 . PHE A 1 138 ? 5.675 6.354 27.278 1.00 19.80 ? 173 PHE A CE1 1 ATOM 911 C CE2 . PHE A 1 138 ? 7.501 7.796 26.757 1.00 20.99 ? 173 PHE A CE2 1 ATOM 912 C CZ . PHE A 1 138 ? 6.184 7.436 26.578 1.00 20.08 ? 173 PHE A CZ 1 ATOM 913 N N . ARG A 1 139 ? 6.342 5.029 31.985 1.00 20.30 ? 174 ARG A N 1 ATOM 914 C CA . ARG A 1 139 ? 5.161 4.375 32.466 1.00 22.38 ? 174 ARG A CA 1 ATOM 915 C C . ARG A 1 139 ? 4.146 4.227 31.318 1.00 22.52 ? 174 ARG A C 1 ATOM 916 O O . ARG A 1 139 ? 4.001 5.143 30.496 1.00 22.46 ? 174 ARG A O 1 ATOM 917 C CB . ARG A 1 139 ? 4.595 5.245 33.581 1.00 25.57 ? 174 ARG A CB 1 ATOM 918 C CG . ARG A 1 139 ? 3.455 4.639 34.319 1.00 30.95 ? 174 ARG A CG 1 ATOM 919 C CD . ARG A 1 139 ? 3.022 5.575 35.425 1.00 30.35 ? 174 ARG A CD 1 ATOM 920 N NE . ARG A 1 139 ? 1.662 5.236 35.819 1.00 31.69 ? 174 ARG A NE 1 ATOM 921 C CZ . ARG A 1 139 ? 1.175 5.313 37.044 1.00 28.62 ? 174 ARG A CZ 1 ATOM 922 N NH1 . ARG A 1 139 ? 1.930 5.705 38.056 1.00 27.37 ? 174 ARG A NH1 1 ATOM 923 N NH2 . ARG A 1 139 ? -0.096 4.969 37.254 1.00 32.22 ? 174 ARG A NH2 1 ATOM 924 N N . ALA A 1 140 ? 3.459 3.080 31.278 1.00 20.61 ? 175 ALA A N 1 ATOM 925 C CA . ALA A 1 140 ? 2.501 2.782 30.227 1.00 22.39 ? 175 ALA A CA 1 ATOM 926 C C . ALA A 1 140 ? 1.476 3.877 30.045 1.00 22.20 ? 175 ALA A C 1 ATOM 927 O O . ALA A 1 140 ? 1.165 4.232 28.913 1.00 23.49 ? 175 ALA A O 1 ATOM 928 C CB . ALA A 1 140 ? 1.774 1.468 30.466 1.00 21.98 ? 175 ALA A CB 1 ATOM 929 N N . SER A 1 141 ? 0.941 4.403 31.143 1.00 21.20 ? 176 SER A N 1 ATOM 930 C CA . SER A 1 141 ? -0.101 5.413 31.037 1.00 23.27 ? 176 SER A CA 1 ATOM 931 C C . SER A 1 141 ? 0.374 6.738 30.432 1.00 24.10 ? 176 SER A C 1 ATOM 932 O O . SER A 1 141 ? -0.471 7.523 29.991 1.00 24.87 ? 176 SER A O 1 ATOM 933 C CB . SER A 1 141 ? -0.750 5.681 32.399 1.00 24.93 ? 176 SER A CB 1 ATOM 934 O OG . SER A 1 141 ? 0.220 6.130 33.321 1.00 27.15 ? 176 SER A OG 1 ATOM 935 N N . TYR A 1 142 ? 1.697 6.992 30.368 1.00 22.64 ? 177 TYR A N 1 ATOM 936 C CA . TYR A 1 142 ? 2.198 8.192 29.700 1.00 23.65 ? 177 TYR A CA 1 ATOM 937 C C . TYR A 1 142 ? 1.757 8.268 28.242 1.00 25.40 ? 177 TYR A C 1 ATOM 938 O O . TYR A 1 142 ? 1.638 9.365 27.696 1.00 27.04 ? 177 TYR A O 1 ATOM 939 C CB . TYR A 1 142 ? 3.730 8.326 29.757 1.00 22.15 ? 177 TYR A CB 1 ATOM 940 C CG . TYR A 1 142 ? 4.379 8.528 31.113 1.00 22.25 ? 177 TYR A CG 1 ATOM 941 C CD1 . TYR A 1 142 ? 3.659 8.988 32.224 1.00 23.88 ? 177 TYR A CD1 1 ATOM 942 C CD2 . TYR A 1 142 ? 5.735 8.308 31.273 1.00 21.28 ? 177 TYR A CD2 1 ATOM 943 C CE1 . TYR A 1 142 ? 4.279 9.169 33.451 1.00 24.65 ? 177 TYR A CE1 1 ATOM 944 C CE2 . TYR A 1 142 ? 6.374 8.513 32.497 1.00 21.42 ? 177 TYR A CE2 1 ATOM 945 C CZ . TYR A 1 142 ? 5.642 8.928 33.591 1.00 23.97 ? 177 TYR A CZ 1 ATOM 946 O OH . TYR A 1 142 ? 6.285 9.124 34.788 1.00 22.35 ? 177 TYR A OH 1 ATOM 947 N N . MET A 1 143 ? 1.508 7.118 27.614 1.00 25.11 ? 178 MET A N 1 ATOM 948 C CA . MET A 1 143 ? 0.952 7.090 26.253 1.00 27.86 ? 178 MET A CA 1 ATOM 949 C C . MET A 1 143 ? -0.423 7.768 26.117 1.00 30.46 ? 178 MET A C 1 ATOM 950 O O . MET A 1 143 ? -0.788 8.199 25.026 1.00 31.46 ? 178 MET A O 1 ATOM 951 C CB . MET A 1 143 ? 0.822 5.658 25.749 1.00 27.20 ? 178 MET A CB 1 ATOM 952 C CG . MET A 1 143 ? 2.129 4.947 25.457 1.00 27.89 ? 178 MET A CG 1 ATOM 953 S SD . MET A 1 143 ? 3.126 5.813 24.223 1.00 30.83 ? 178 MET A SD 1 ATOM 954 C CE . MET A 1 143 ? 4.250 4.497 23.782 1.00 33.56 ? 178 MET A CE 1 ATOM 955 N N . LYS A 1 144 ? -1.181 7.840 27.204 1.00 33.52 ? 179 LYS A N 1 ATOM 956 C CA . LYS A 1 144 ? -2.461 8.551 27.203 1.00 38.09 ? 179 LYS A CA 1 ATOM 957 C C . LYS A 1 144 ? -2.351 10.059 26.884 1.00 38.51 ? 179 LYS A C 1 ATOM 958 O O . LYS A 1 144 ? -3.328 10.652 26.449 1.00 40.41 ? 179 LYS A O 1 ATOM 959 C CB . LYS A 1 144 ? -3.189 8.360 28.539 1.00 40.46 ? 179 LYS A CB 1 ATOM 960 C CG . LYS A 1 144 ? -3.622 6.927 28.845 1.00 44.27 ? 179 LYS A CG 1 ATOM 961 C CD . LYS A 1 144 ? -4.737 6.413 27.938 1.00 49.18 ? 179 LYS A CD 1 ATOM 962 C CE . LYS A 1 144 ? -6.103 6.999 28.288 1.00 52.86 ? 179 LYS A CE 1 ATOM 963 N NZ . LYS A 1 144 ? -7.050 6.889 27.145 1.00 54.22 ? 179 LYS A NZ 1 ATOM 964 N N . LYS A 1 145 ? -1.182 10.661 27.106 1.00 38.15 ? 180 LYS A N 1 ATOM 965 C CA . LYS A 1 145 ? -0.960 12.086 26.837 1.00 40.16 ? 180 LYS A CA 1 ATOM 966 C C . LYS A 1 145 ? -1.080 12.416 25.349 1.00 42.27 ? 180 LYS A C 1 ATOM 967 O O . LYS A 1 145 ? -1.474 13.524 24.974 1.00 44.08 ? 180 LYS A O 1 ATOM 968 C CB . LYS A 1 145 ? 0.376 12.540 27.421 1.00 39.67 ? 180 LYS A CB 1 ATOM 969 C CG . LYS A 1 145 ? 0.288 12.640 28.939 1.00 41.75 ? 180 LYS A CG 1 ATOM 970 C CD . LYS A 1 145 ? 1.639 12.668 29.625 1.00 43.54 ? 180 LYS A CD 1 ATOM 971 C CE . LYS A 1 145 ? 1.530 12.405 31.128 1.00 44.92 ? 180 LYS A CE 1 ATOM 972 N NZ . LYS A 1 145 ? 0.814 13.480 31.870 1.00 46.82 ? 180 LYS A NZ 1 ATOM 973 N N . GLY A 1 146 ? -0.752 11.442 24.510 1.00 43.07 ? 181 GLY A N 1 ATOM 974 C CA . GLY A 1 146 ? -1.261 11.420 23.153 1.00 43.18 ? 181 GLY A CA 1 ATOM 975 C C . GLY A 1 146 ? -0.507 12.318 22.203 1.00 43.46 ? 181 GLY A C 1 ATOM 976 O O . GLY A 1 146 ? 0.567 12.834 22.524 1.00 38.98 ? 181 GLY A O 1 ATOM 977 N N . SER A 1 147 ? -1.124 12.515 21.041 1.00 43.01 ? 182 SER A N 1 ATOM 978 C CA . SER A 1 147 ? -0.503 13.160 19.885 1.00 45.54 ? 182 SER A CA 1 ATOM 979 C C . SER A 1 147 ? -0.067 14.609 20.107 1.00 46.41 ? 182 SER A C 1 ATOM 980 O O . SER A 1 147 ? 0.871 15.066 19.454 1.00 44.89 ? 182 SER A O 1 ATOM 981 C CB . SER A 1 147 ? -1.467 13.102 18.691 1.00 48.30 ? 182 SER A CB 1 ATOM 982 O OG . SER A 1 147 ? -0.797 13.428 17.492 1.00 56.69 ? 182 SER A OG 1 ATOM 983 N N . LYS A 1 148 ? -0.742 15.331 21.005 1.00 44.72 ? 183 LYS A N 1 ATOM 984 C CA . LYS A 1 148 ? -0.428 16.742 21.241 1.00 46.46 ? 183 LYS A CA 1 ATOM 985 C C . LYS A 1 148 ? 0.908 16.918 21.979 1.00 40.08 ? 183 LYS A C 1 ATOM 986 O O . LYS A 1 148 ? 1.570 17.929 21.807 1.00 40.01 ? 183 LYS A O 1 ATOM 987 C CB . LYS A 1 148 ? -1.580 17.438 22.001 1.00 53.31 ? 183 LYS A CB 1 ATOM 988 C CG . LYS A 1 148 ? -1.540 18.964 21.991 1.00 59.16 ? 183 LYS A CG 1 ATOM 989 C CD . LYS A 1 148 ? -1.874 19.562 20.621 1.00 63.58 ? 183 LYS A CD 1 ATOM 990 C CE . LYS A 1 148 ? -1.050 20.806 20.307 1.00 67.19 ? 183 LYS A CE 1 ATOM 991 N NZ . LYS A 1 148 ? 0.378 20.485 20.017 1.00 66.75 ? 183 LYS A NZ 1 ATOM 992 N N . VAL A 1 149 ? 1.305 15.923 22.770 1.00 35.59 ? 184 VAL A N 1 ATOM 993 C CA . VAL A 1 149 ? 2.588 15.940 23.499 1.00 32.51 ? 184 VAL A CA 1 ATOM 994 C C . VAL A 1 149 ? 3.689 15.131 22.771 1.00 28.79 ? 184 VAL A C 1 ATOM 995 O O . VAL A 1 149 ? 4.853 15.545 22.749 1.00 26.33 ? 184 VAL A O 1 ATOM 996 C CB . VAL A 1 149 ? 2.378 15.422 24.948 1.00 34.18 ? 184 VAL A CB 1 ATOM 997 C CG1 . VAL A 1 149 ? 3.678 15.392 25.747 1.00 33.17 ? 184 VAL A CG1 1 ATOM 998 C CG2 . VAL A 1 149 ? 1.347 16.297 25.658 1.00 35.66 ? 184 VAL A CG2 1 ATOM 999 N N . MET A 1 150 ? 3.305 13.988 22.198 1.00 25.87 ? 185 MET A N 1 ATOM 1000 C CA . MET A 1 150 ? 4.244 13.030 21.616 1.00 25.21 ? 185 MET A CA 1 ATOM 1001 C C . MET A 1 150 ? 3.776 12.584 20.210 1.00 24.13 ? 185 MET A C 1 ATOM 1002 O O . MET A 1 150 ? 3.429 11.426 20.015 1.00 21.26 ? 185 MET A O 1 ATOM 1003 C CB . MET A 1 150 ? 4.372 11.820 22.550 1.00 24.42 ? 185 MET A CB 1 ATOM 1004 C CG . MET A 1 150 ? 4.894 12.154 23.941 1.00 25.30 ? 185 MET A CG 1 ATOM 1005 S SD . MET A 1 150 ? 5.128 10.677 24.989 1.00 27.76 ? 185 MET A SD 1 ATOM 1006 C CE . MET A 1 150 ? 3.501 9.938 24.868 1.00 27.91 ? 185 MET A CE 1 ATOM 1007 N N . PRO A 1 151 ? 3.779 13.504 19.222 1.00 24.04 ? 186 PRO A N 1 ATOM 1008 C CA . PRO A 1 151 ? 3.239 13.120 17.903 1.00 24.38 ? 186 PRO A CA 1 ATOM 1009 C C . PRO A 1 151 ? 4.016 12.000 17.202 1.00 23.26 ? 186 PRO A C 1 ATOM 1010 O O . PRO A 1 151 ? 3.403 11.124 16.591 1.00 23.17 ? 186 PRO A O 1 ATOM 1011 C CB . PRO A 1 151 ? 3.307 14.425 17.098 1.00 25.40 ? 186 PRO A CB 1 ATOM 1012 C CG . PRO A 1 151 ? 4.298 15.299 17.812 1.00 24.81 ? 186 PRO A CG 1 ATOM 1013 C CD . PRO A 1 151 ? 4.141 14.935 19.261 1.00 25.34 ? 186 PRO A CD 1 ATOM 1014 N N . ASN A 1 152 ? 5.345 12.037 17.256 1.00 22.64 ? 187 ASN A N 1 ATOM 1015 C CA . ASN A 1 152 ? 6.157 10.982 16.634 1.00 21.66 ? 187 ASN A CA 1 ATOM 1016 C C . ASN A 1 152 ? 5.897 9.613 17.251 1.00 21.56 ? 187 ASN A C 1 ATOM 1017 O O . ASN A 1 152 ? 5.647 8.638 16.541 1.00 21.40 ? 187 ASN A O 1 ATOM 1018 C CB . ASN A 1 152 ? 7.656 11.306 16.702 1.00 21.75 ? 187 ASN A CB 1 ATOM 1019 C CG . ASN A 1 152 ? 8.056 12.431 15.776 1.00 22.80 ? 187 ASN A CG 1 ATOM 1020 O OD1 . ASN A 1 152 ? 8.273 12.215 14.587 1.00 23.68 ? 187 ASN A OD1 1 ATOM 1021 N ND2 . ASN A 1 152 ? 8.179 13.637 16.310 1.00 23.67 ? 187 ASN A ND2 1 ATOM 1022 N N . ILE A 1 153 ? 5.929 9.548 18.577 1.00 20.57 ? 188 ILE A N 1 ATOM 1023 C CA . ILE A 1 153 ? 5.696 8.284 19.275 1.00 21.49 ? 188 ILE A CA 1 ATOM 1024 C C . ILE A 1 153 ? 4.270 7.789 19.016 1.00 21.72 ? 188 ILE A C 1 ATOM 1025 O O . ILE A 1 153 ? 4.066 6.618 18.747 1.00 20.22 ? 188 ILE A O 1 ATOM 1026 C CB . ILE A 1 153 ? 5.975 8.429 20.787 1.00 21.13 ? 188 ILE A CB 1 ATOM 1027 C CG1 . ILE A 1 153 ? 7.480 8.638 21.010 1.00 21.33 ? 188 ILE A CG1 1 ATOM 1028 C CG2 . ILE A 1 153 ? 5.472 7.221 21.572 1.00 21.44 ? 188 ILE A CG2 1 ATOM 1029 C CD1 . ILE A 1 153 ? 7.832 9.166 22.388 1.00 21.47 ? 188 ILE A CD1 1 ATOM 1030 N N . GLU A 1 154 ? 3.288 8.688 19.053 1.00 24.20 ? 189 GLU A N 1 ATOM 1031 C CA . GLU A 1 154 ? 1.908 8.300 18.747 1.00 27.01 ? 189 GLU A CA 1 ATOM 1032 C C . GLU A 1 154 ? 1.761 7.741 17.328 1.00 24.66 ? 189 GLU A C 1 ATOM 1033 O O . GLU A 1 154 ? 0.978 6.813 17.124 1.00 22.44 ? 189 GLU A O 1 ATOM 1034 C CB . GLU A 1 154 ? 0.917 9.471 18.972 1.00 32.49 ? 189 GLU A CB 1 ATOM 1035 C CG . GLU A 1 154 ? -0.336 9.083 19.735 1.00 39.01 ? 189 GLU A CG 1 ATOM 1036 C CD . GLU A 1 154 ? -0.046 8.436 21.093 1.00 42.77 ? 189 GLU A CD 1 ATOM 1037 O OE1 . GLU A 1 154 ? -0.479 7.299 21.277 1.00 43.47 ? 189 GLU A OE1 1 ATOM 1038 O OE2 . GLU A 1 154 ? 0.631 9.020 21.975 1.00 55.10 ? 189 GLU A OE2 1 ATOM 1039 N N . LYS A 1 155 ? 2.505 8.296 16.363 1.00 23.64 ? 190 LYS A N 1 ATOM 1040 C CA . LYS A 1 155 ? 2.493 7.758 14.999 1.00 24.02 ? 190 LYS A CA 1 ATOM 1041 C C . LYS A 1 155 ? 3.091 6.360 14.965 1.00 22.25 ? 190 LYS A C 1 ATOM 1042 O O . LYS A 1 155 ? 2.502 5.453 14.378 1.00 21.67 ? 190 LYS A O 1 ATOM 1043 C CB . LYS A 1 155 ? 3.216 8.663 13.999 1.00 24.89 ? 190 LYS A CB 1 ATOM 1044 C CG . LYS A 1 155 ? 3.063 8.182 12.556 1.00 26.73 ? 190 LYS A CG 1 ATOM 1045 C CD . LYS A 1 155 ? 3.770 9.071 11.554 1.00 27.77 ? 190 LYS A CD 1 ATOM 1046 C CE . LYS A 1 155 ? 3.827 8.387 10.197 1.00 28.28 ? 190 LYS A CE 1 ATOM 1047 N NZ . LYS A 1 155 ? 4.610 9.161 9.215 1.00 29.96 ? 190 LYS A NZ 1 ATOM 1048 N N . LEU A 1 156 ? 4.251 6.175 15.583 1.00 20.65 ? 191 LEU A N 1 ATOM 1049 C CA . LEU A 1 156 ? 4.821 4.821 15.684 1.00 20.68 ? 191 LEU A CA 1 ATOM 1050 C C . LEU A 1 156 ? 3.816 3.835 16.289 1.00 21.32 ? 191 LEU A C 1 ATOM 1051 O O . LEU A 1 156 ? 3.600 2.744 15.768 1.00 20.95 ? 191 LEU A O 1 ATOM 1052 C CB . LEU A 1 156 ? 6.088 4.818 16.547 1.00 21.62 ? 191 LEU A CB 1 ATOM 1053 C CG . LEU A 1 156 ? 7.353 5.480 16.021 1.00 22.75 ? 191 LEU A CG 1 ATOM 1054 C CD1 . LEU A 1 156 ? 8.414 5.432 17.120 1.00 24.00 ? 191 LEU A CD1 1 ATOM 1055 C CD2 . LEU A 1 156 ? 7.856 4.775 14.770 1.00 22.48 ? 191 LEU A CD2 1 ATOM 1056 N N . ARG A 1 157 ? 3.214 4.248 17.394 1.00 22.08 ? 192 ARG A N 1 ATOM 1057 C CA . ARG A 1 157 ? 2.268 3.415 18.134 1.00 24.39 ? 192 ARG A CA 1 ATOM 1058 C C . ARG A 1 157 ? 1.037 3.080 17.286 1.00 24.53 ? 192 ARG A C 1 ATOM 1059 O O . ARG A 1 157 ? 0.666 1.911 17.189 1.00 23.20 ? 192 ARG A O 1 ATOM 1060 C CB . ARG A 1 157 ? 1.835 4.101 19.440 1.00 26.08 ? 192 ARG A CB 1 ATOM 1061 C CG . ARG A 1 157 ? 0.962 3.227 20.342 1.00 29.79 ? 192 ARG A CG 1 ATOM 1062 C CD . ARG A 1 157 ? 0.390 3.999 21.521 1.00 33.61 ? 192 ARG A CD 1 ATOM 1063 N NE . ARG A 1 157 ? -0.687 4.908 21.115 1.00 37.26 ? 192 ARG A NE 1 ATOM 1064 C CZ . ARG A 1 157 ? -1.951 4.562 20.831 1.00 42.97 ? 192 ARG A CZ 1 ATOM 1065 N NH1 . ARG A 1 157 ? -2.359 3.300 20.880 1.00 43.44 ? 192 ARG A NH1 1 ATOM 1066 N NH2 . ARG A 1 157 ? -2.822 5.503 20.476 1.00 46.71 ? 192 ARG A NH2 1 ATOM 1067 N N . SER A 1 158 ? 0.424 4.088 16.670 1.00 23.97 ? 193 SER A N 1 ATOM 1068 C CA . SER A 1 158 ? -0.817 3.855 15.913 1.00 26.89 ? 193 SER A CA 1 ATOM 1069 C C . SER A 1 158 ? -0.562 3.150 14.575 1.00 26.90 ? 193 SER A C 1 ATOM 1070 O O . SER A 1 158 ? -1.386 2.349 14.131 1.00 26.39 ? 193 SER A O 1 ATOM 1071 C CB . SER A 1 158 ? -1.620 5.157 15.729 1.00 28.85 ? 193 SER A CB 1 ATOM 1072 O OG . SER A 1 158 ? -0.861 6.133 15.036 1.00 33.48 ? 193 SER A OG 1 ATOM 1073 N N . CYS A 1 159 ? 0.577 3.428 13.944 1.00 26.97 ? 194 CYS A N 1 ATOM 1074 C CA . CYS A 1 159 ? 0.875 2.844 12.634 1.00 28.43 ? 194 CYS A CA 1 ATOM 1075 C C . CYS A 1 159 ? 1.476 1.467 12.727 1.00 24.08 ? 194 CYS A C 1 ATOM 1076 O O . CYS A 1 159 ? 1.257 0.649 11.838 1.00 23.76 ? 194 CYS A O 1 ATOM 1077 C CB . CYS A 1 159 ? 1.791 3.751 11.831 1.00 33.47 ? 194 CYS A CB 1 ATOM 1078 S SG . CYS A 1 159 ? 0.822 5.139 11.276 1.00 46.17 ? 194 CYS A SG 1 ATOM 1079 N N . GLY A 1 160 ? 2.220 1.204 13.792 1.00 19.77 ? 195 GLY A N 1 ATOM 1080 C CA . GLY A 1 160 ? 2.879 -0.080 13.947 1.00 19.51 ? 195 GLY A CA 1 ATOM 1081 C C . GLY A 1 160 ? 2.057 -1.053 14.770 1.00 19.28 ? 195 GLY A C 1 ATOM 1082 O O . GLY A 1 160 ? 0.812 -1.071 14.696 1.00 20.30 ? 195 GLY A O 1 ATOM 1083 N N . THR A 1 161 ? 2.783 -1.865 15.532 1.00 18.94 ? 196 THR A N 1 ATOM 1084 C CA . THR A 1 161 ? 2.235 -2.839 16.482 1.00 19.24 ? 196 THR A CA 1 ATOM 1085 C C . THR A 1 161 ? 2.481 -2.347 17.916 1.00 18.84 ? 196 THR A C 1 ATOM 1086 O O . THR A 1 161 ? 3.579 -1.876 18.231 1.00 20.23 ? 196 THR A O 1 ATOM 1087 C CB . THR A 1 161 ? 2.888 -4.213 16.244 1.00 19.69 ? 196 THR A CB 1 ATOM 1088 O OG1 . THR A 1 161 ? 2.544 -4.662 14.927 1.00 21.07 ? 196 THR A OG1 1 ATOM 1089 C CG2 . THR A 1 161 ? 2.425 -5.253 17.259 1.00 20.18 ? 196 THR A CG2 1 ATOM 1090 N N . HIS A 1 162 ? 1.477 -2.420 18.792 1.00 17.79 ? 197 HIS A N 1 ATOM 1091 C CA . HIS A 1 162 ? 1.688 -1.952 20.168 1.00 17.99 ? 197 HIS A CA 1 ATOM 1092 C C . HIS A 1 162 ? 0.859 -2.787 21.108 1.00 18.05 ? 197 HIS A C 1 ATOM 1093 O O . HIS A 1 162 ? -0.147 -3.371 20.700 1.00 17.28 ? 197 HIS A O 1 ATOM 1094 C CB . HIS A 1 162 ? 1.343 -0.459 20.316 1.00 18.96 ? 197 HIS A CB 1 ATOM 1095 C CG . HIS A 1 162 ? -0.122 -0.189 20.480 1.00 20.78 ? 197 HIS A CG 1 ATOM 1096 N ND1 . HIS A 1 162 ? -1.009 -0.237 19.428 1.00 21.68 ? 197 HIS A ND1 1 ATOM 1097 C CD2 . HIS A 1 162 ? -0.856 0.097 21.580 1.00 21.37 ? 197 HIS A CD2 1 ATOM 1098 C CE1 . HIS A 1 162 ? -2.230 0.025 19.870 1.00 23.47 ? 197 HIS A CE1 1 ATOM 1099 N NE2 . HIS A 1 162 ? -2.162 0.230 21.176 1.00 23.32 ? 197 HIS A NE2 1 ATOM 1100 N N . ALA A 1 163 ? 1.316 -2.840 22.353 1.00 17.70 ? 198 ALA A N 1 ATOM 1101 C CA . ALA A 1 163 ? 0.553 -3.411 23.450 1.00 19.74 ? 198 ALA A CA 1 ATOM 1102 C C . ALA A 1 163 ? 0.072 -2.266 24.345 1.00 19.54 ? 198 ALA A C 1 ATOM 1103 O O . ALA A 1 163 ? 0.701 -1.209 24.395 1.00 18.88 ? 198 ALA A O 1 ATOM 1104 C CB . ALA A 1 163 ? 1.411 -4.394 24.231 1.00 19.95 ? 198 ALA A CB 1 ATOM 1105 N N . PRO A 1 164 ? -1.050 -2.466 25.065 1.00 20.50 ? 199 PRO A N 1 ATOM 1106 C CA . PRO A 1 164 ? -1.470 -1.492 26.077 1.00 21.60 ? 199 PRO A CA 1 ATOM 1107 C C . PRO A 1 164 ? -0.387 -1.228 27.123 1.00 20.32 ? 199 PRO A C 1 ATOM 1108 O O . PRO A 1 164 ? -0.243 -0.099 27.611 1.00 20.07 ? 199 PRO A O 1 ATOM 1109 C CB . PRO A 1 164 ? -2.661 -2.173 26.736 1.00 22.30 ? 199 PRO A CB 1 ATOM 1110 C CG . PRO A 1 164 ? -3.207 -3.076 25.717 1.00 24.10 ? 199 PRO A CG 1 ATOM 1111 C CD . PRO A 1 164 ? -2.031 -3.550 24.922 1.00 21.76 ? 199 PRO A CD 1 ATOM 1112 N N . TYR A 1 165 ? 0.357 -2.275 27.460 1.00 18.72 ? 200 TYR A N 1 ATOM 1113 C CA . TYR A 1 165 ? 1.485 -2.153 28.352 1.00 17.66 ? 200 TYR A CA 1 ATOM 1114 C C . TYR A 1 165 ? 2.365 -3.394 28.220 1.00 16.58 ? 200 TYR A C 1 ATOM 1115 O O . TYR A 1 165 ? 1.934 -4.424 27.707 1.00 16.52 ? 200 TYR A O 1 ATOM 1116 C CB . TYR A 1 165 ? 1.037 -1.924 29.814 1.00 19.54 ? 200 TYR A CB 1 ATOM 1117 C CG . TYR A 1 165 ? 0.379 -3.102 30.511 1.00 23.20 ? 200 TYR A CG 1 ATOM 1118 C CD1 . TYR A 1 165 ? 1.163 -4.085 31.101 1.00 24.51 ? 200 TYR A CD1 1 ATOM 1119 C CD2 . TYR A 1 165 ? -1.009 -3.233 30.589 1.00 29.05 ? 200 TYR A CD2 1 ATOM 1120 C CE1 . TYR A 1 165 ? 0.610 -5.177 31.733 1.00 27.64 ? 200 TYR A CE1 1 ATOM 1121 C CE2 . TYR A 1 165 ? -1.582 -4.342 31.252 1.00 31.10 ? 200 TYR A CE2 1 ATOM 1122 C CZ . TYR A 1 165 ? -0.747 -5.304 31.825 1.00 31.52 ? 200 TYR A CZ 1 ATOM 1123 O OH . TYR A 1 165 ? -1.205 -6.446 32.491 1.00 38.68 ? 200 TYR A OH 1 ATOM 1124 N N . MET A 1 166 ? 3.590 -3.271 28.695 1.00 15.85 ? 201 MET A N 1 ATOM 1125 C CA . MET A 1 166 ? 4.518 -4.380 28.806 1.00 14.79 ? 201 MET A CA 1 ATOM 1126 C C . MET A 1 166 ? 4.895 -4.553 30.270 1.00 15.12 ? 201 MET A C 1 ATOM 1127 O O . MET A 1 166 ? 5.190 -3.575 30.950 1.00 14.80 ? 201 MET A O 1 ATOM 1128 C CB . MET A 1 166 ? 5.763 -4.116 27.957 1.00 15.14 ? 201 MET A CB 1 ATOM 1129 C CG . MET A 1 166 ? 6.722 -5.293 27.925 1.00 14.57 ? 201 MET A CG 1 ATOM 1130 S SD . MET A 1 166 ? 8.169 -5.119 26.884 1.00 16.11 ? 201 MET A SD 1 ATOM 1131 C CE . MET A 1 166 ? 9.049 -3.892 27.836 1.00 16.58 ? 201 MET A CE 1 ATOM 1132 N N . ARG A 1 167 ? 4.869 -5.793 30.750 1.00 14.19 ? 202 ARG A N 1 ATOM 1133 C CA . ARG A 1 167 ? 5.216 -6.092 32.129 1.00 13.79 ? 202 ARG A CA 1 ATOM 1134 C C . ARG A 1 167 ? 6.731 -6.252 32.279 1.00 13.11 ? 202 ARG A C 1 ATOM 1135 O O . ARG A 1 167 ? 7.330 -7.131 31.629 1.00 13.71 ? 202 ARG A O 1 ATOM 1136 C CB . ARG A 1 167 ? 4.525 -7.381 32.587 1.00 14.78 ? 202 ARG A CB 1 ATOM 1137 C CG . ARG A 1 167 ? 4.685 -7.681 34.079 1.00 15.55 ? 202 ARG A CG 1 ATOM 1138 C CD . ARG A 1 167 ? 3.918 -8.938 34.532 1.00 17.05 ? 202 ARG A CD 1 ATOM 1139 N NE . ARG A 1 167 ? 2.546 -8.807 34.105 1.00 17.73 ? 202 ARG A NE 1 ATOM 1140 C CZ . ARG A 1 167 ? 1.892 -9.570 33.232 1.00 16.99 ? 202 ARG A CZ 1 ATOM 1141 N NH1 . ARG A 1 167 ? 2.386 -10.717 32.775 1.00 18.73 ? 202 ARG A NH1 1 ATOM 1142 N NH2 . ARG A 1 167 ? 0.672 -9.209 32.880 1.00 16.40 ? 202 ARG A NH2 1 ATOM 1143 N N . PRO A 1 168 ? 7.354 -5.480 33.188 1.00 13.62 ? 203 PRO A N 1 ATOM 1144 C CA . PRO A 1 168 ? 8.774 -5.624 33.505 1.00 12.91 ? 203 PRO A CA 1 ATOM 1145 C C . PRO A 1 168 ? 9.033 -6.836 34.420 1.00 13.48 ? 203 PRO A C 1 ATOM 1146 O O . PRO A 1 168 ? 8.077 -7.526 34.825 1.00 13.72 ? 203 PRO A O 1 ATOM 1147 C CB . PRO A 1 168 ? 9.080 -4.308 34.206 1.00 14.37 ? 203 PRO A CB 1 ATOM 1148 C CG . PRO A 1 168 ? 7.801 -4.007 34.941 1.00 13.82 ? 203 PRO A CG 1 ATOM 1149 C CD . PRO A 1 168 ? 6.694 -4.509 34.079 1.00 13.17 ? 203 PRO A CD 1 ATOM 1150 N N . VAL A 1 169 ? 10.295 -7.122 34.720 1.00 13.31 ? 204 VAL A N 1 ATOM 1151 C CA . VAL A 1 169 ? 10.632 -8.175 35.682 1.00 13.60 ? 204 VAL A CA 1 ATOM 1152 C C . VAL A 1 169 ? 10.859 -7.512 37.017 1.00 14.49 ? 204 VAL A C 1 ATOM 1153 O O . VAL A 1 169 ? 11.134 -6.307 37.099 1.00 14.94 ? 204 VAL A O 1 ATOM 1154 C CB . VAL A 1 169 ? 11.913 -9.003 35.353 1.00 14.74 ? 204 VAL A CB 1 ATOM 1155 C CG1 . VAL A 1 169 ? 11.634 -9.993 34.257 1.00 15.54 ? 204 VAL A CG1 1 ATOM 1156 C CG2 . VAL A 1 169 ? 13.105 -8.110 35.079 1.00 13.91 ? 204 VAL A CG2 1 ATOM 1157 N N . TYR A 1 170 ? 10.726 -8.313 38.062 1.00 14.08 ? 205 TYR A N 1 ATOM 1158 C CA . TYR A 1 170 ? 11.039 -7.883 39.421 1.00 14.38 ? 205 TYR A CA 1 ATOM 1159 C C . TYR A 1 170 ? 12.521 -8.114 39.743 1.00 13.91 ? 205 TYR A C 1 ATOM 1160 O O . TYR A 1 170 ? 13.060 -9.128 39.328 1.00 14.41 ? 205 TYR A O 1 ATOM 1161 C CB . TYR A 1 170 ? 10.211 -8.713 40.403 1.00 13.44 ? 205 TYR A CB 1 ATOM 1162 C CG . TYR A 1 170 ? 10.351 -8.233 41.830 1.00 13.89 ? 205 TYR A CG 1 ATOM 1163 C CD1 . TYR A 1 170 ? 9.674 -7.078 42.263 1.00 14.57 ? 205 TYR A CD1 1 ATOM 1164 C CD2 . TYR A 1 170 ? 11.160 -8.912 42.739 1.00 14.53 ? 205 TYR A CD2 1 ATOM 1165 C CE1 . TYR A 1 170 ? 9.795 -6.634 43.569 1.00 14.48 ? 205 TYR A CE1 1 ATOM 1166 C CE2 . TYR A 1 170 ? 11.288 -8.478 44.034 1.00 14.98 ? 205 TYR A CE2 1 ATOM 1167 C CZ . TYR A 1 170 ? 10.614 -7.333 44.441 1.00 15.84 ? 205 TYR A CZ 1 ATOM 1168 O OH . TYR A 1 170 ? 10.750 -6.904 45.745 1.00 15.55 ? 205 TYR A OH 1 ATOM 1169 N N . PRO A 1 171 ? 13.179 -7.230 40.488 1.00 14.13 ? 206 PRO A N 1 ATOM 1170 C CA . PRO A 1 171 ? 12.657 -5.915 40.853 1.00 14.49 ? 206 PRO A CA 1 ATOM 1171 C C . PRO A 1 171 ? 12.578 -4.976 39.685 1.00 14.47 ? 206 PRO A C 1 ATOM 1172 O O . PRO A 1 171 ? 13.380 -5.067 38.746 1.00 14.41 ? 206 PRO A O 1 ATOM 1173 C CB . PRO A 1 171 ? 13.682 -5.393 41.828 1.00 15.38 ? 206 PRO A CB 1 ATOM 1174 C CG . PRO A 1 171 ? 14.951 -6.052 41.466 1.00 16.43 ? 206 PRO A CG 1 ATOM 1175 C CD . PRO A 1 171 ? 14.611 -7.376 40.855 1.00 15.13 ? 206 PRO A CD 1 ATOM 1176 N N . THR A 1 172 ? 11.626 -4.061 39.757 1.00 13.91 ? 207 THR A N 1 ATOM 1177 C CA . THR A 1 172 ? 11.324 -3.139 38.683 1.00 14.03 ? 207 THR A CA 1 ATOM 1178 C C . THR A 1 172 ? 12.293 -1.957 38.682 1.00 15.08 ? 207 THR A C 1 ATOM 1179 O O . THR A 1 172 ? 11.908 -0.768 38.812 1.00 15.66 ? 207 THR A O 1 ATOM 1180 C CB . THR A 1 172 ? 9.816 -2.740 38.653 1.00 14.11 ? 207 THR A CB 1 ATOM 1181 O OG1 . THR A 1 172 ? 9.393 -2.204 39.918 1.00 13.56 ? 207 THR A OG1 1 ATOM 1182 C CG2 . THR A 1 172 ? 8.970 -3.928 38.328 1.00 14.65 ? 207 THR A CG2 1 ATOM 1183 N N . LYS A 1 173 ? 13.555 -2.322 38.461 1.00 16.19 ? 208 LYS A N 1 ATOM 1184 C CA . LYS A 1 173 ? 14.692 -1.428 38.472 1.00 17.01 ? 208 LYS A CA 1 ATOM 1185 C C . LYS A 1 173 ? 15.368 -1.560 37.109 1.00 16.11 ? 208 LYS A C 1 ATOM 1186 O O . LYS A 1 173 ? 15.161 -2.547 36.383 1.00 14.38 ? 208 LYS A O 1 ATOM 1187 C CB . LYS A 1 173 ? 15.676 -1.855 39.551 1.00 18.14 ? 208 LYS A CB 1 ATOM 1188 C CG . LYS A 1 173 ? 15.089 -1.822 40.953 1.00 20.63 ? 208 LYS A CG 1 ATOM 1189 C CD . LYS A 1 173 ? 15.169 -0.426 41.513 1.00 22.58 ? 208 LYS A CD 1 ATOM 1190 C CE . LYS A 1 173 ? 14.973 -0.443 43.009 1.00 25.52 ? 208 LYS A CE 1 ATOM 1191 N NZ . LYS A 1 173 ? 15.376 0.848 43.585 1.00 30.40 ? 208 LYS A NZ 1 HETATM 1192 N N . TPO A 1 174 ? 16.204 -0.576 36.808 1.00 15.58 ? 209 TPO A N 1 HETATM 1193 C CA . TPO A 1 174 ? 16.848 -0.439 35.489 1.00 16.49 ? 209 TPO A CA 1 HETATM 1194 C CB . TPO A 1 174 ? 17.639 0.862 35.476 1.00 19.60 ? 209 TPO A CB 1 HETATM 1195 C CG2 . TPO A 1 174 ? 18.252 1.142 34.100 1.00 19.39 ? 209 TPO A CG2 1 HETATM 1196 O OG1 . TPO A 1 174 ? 16.732 1.914 35.710 1.00 21.82 ? 209 TPO A OG1 1 HETATM 1197 P P . TPO A 1 174 ? 16.988 2.812 37.027 1.00 42.96 ? 209 TPO A P 1 HETATM 1198 O O1P . TPO A 1 174 ? 15.922 3.858 36.832 1.00 27.22 ? 209 TPO A O1P 1 HETATM 1199 O O2P . TPO A 1 174 ? 16.772 1.886 38.234 1.00 21.28 ? 209 TPO A O2P 1 HETATM 1200 O O3P . TPO A 1 174 ? 18.390 3.428 36.960 1.00 29.64 ? 209 TPO A O3P 1 HETATM 1201 C C . TPO A 1 174 ? 17.734 -1.591 35.084 1.00 15.51 ? 209 TPO A C 1 HETATM 1202 O O . TPO A 1 174 ? 17.502 -2.208 34.036 1.00 14.38 ? 209 TPO A O 1 ATOM 1203 N N . PHE A 1 175 ? 18.776 -1.887 35.852 1.00 15.44 ? 210 PHE A N 1 ATOM 1204 C CA . PHE A 1 175 ? 19.755 -2.889 35.395 1.00 15.82 ? 210 PHE A CA 1 ATOM 1205 C C . PHE A 1 175 ? 19.148 -4.280 35.241 1.00 14.92 ? 210 PHE A C 1 ATOM 1206 O O . PHE A 1 175 ? 19.343 -4.933 34.227 1.00 14.66 ? 210 PHE A O 1 ATOM 1207 C CB . PHE A 1 175 ? 21.026 -2.911 36.239 1.00 19.48 ? 210 PHE A CB 1 ATOM 1208 C CG . PHE A 1 175 ? 22.094 -1.959 35.752 1.00 23.68 ? 210 PHE A CG 1 ATOM 1209 C CD1 . PHE A 1 175 ? 21.787 -0.659 35.386 1.00 27.46 ? 210 PHE A CD1 1 ATOM 1210 C CD2 . PHE A 1 175 ? 23.417 -2.367 35.696 1.00 29.27 ? 210 PHE A CD2 1 ATOM 1211 C CE1 . PHE A 1 175 ? 22.769 0.211 34.950 1.00 30.46 ? 210 PHE A CE1 1 ATOM 1212 C CE2 . PHE A 1 175 ? 24.410 -1.502 35.259 1.00 30.62 ? 210 PHE A CE2 1 ATOM 1213 C CZ . PHE A 1 175 ? 24.084 -0.212 34.876 1.00 29.60 ? 210 PHE A CZ 1 ATOM 1214 N N . PRO A 1 176 ? 18.328 -4.716 36.208 1.00 13.05 ? 211 PRO A N 1 ATOM 1215 C CA . PRO A 1 176 ? 17.723 -6.027 35.964 1.00 13.58 ? 211 PRO A CA 1 ATOM 1216 C C . PRO A 1 176 ? 16.848 -6.075 34.718 1.00 12.97 ? 211 PRO A C 1 ATOM 1217 O O . PRO A 1 176 ? 16.814 -7.086 34.019 1.00 13.19 ? 211 PRO A O 1 ATOM 1218 C CB . PRO A 1 176 ? 16.897 -6.269 37.232 1.00 12.43 ? 211 PRO A CB 1 ATOM 1219 C CG . PRO A 1 176 ? 17.611 -5.482 38.287 1.00 13.35 ? 211 PRO A CG 1 ATOM 1220 C CD . PRO A 1 176 ? 18.126 -4.247 37.604 1.00 13.92 ? 211 PRO A CD 1 ATOM 1221 N N . ASN A 1 177 ? 16.140 -4.993 34.437 1.00 14.02 ? 212 ASN A N 1 ATOM 1222 C CA . ASN A 1 177 ? 15.213 -4.982 33.305 1.00 13.34 ? 212 ASN A CA 1 ATOM 1223 C C . ASN A 1 177 ? 15.908 -4.793 31.963 1.00 14.05 ? 212 ASN A C 1 ATOM 1224 O O . ASN A 1 177 ? 15.552 -5.479 30.993 1.00 13.64 ? 212 ASN A O 1 ATOM 1225 C CB . ASN A 1 177 ? 14.094 -3.978 33.505 1.00 13.85 ? 212 ASN A CB 1 ATOM 1226 C CG . ASN A 1 177 ? 12.968 -4.570 34.292 1.00 12.83 ? 212 ASN A CG 1 ATOM 1227 O OD1 . ASN A 1 177 ? 12.094 -5.274 33.716 1.00 11.67 ? 212 ASN A OD1 1 ATOM 1228 N ND2 . ASN A 1 177 ? 12.990 -4.365 35.602 1.00 12.67 ? 212 ASN A ND2 1 ATOM 1229 N N . LEU A 1 178 ? 16.905 -3.924 31.925 1.00 15.20 ? 213 LEU A N 1 ATOM 1230 C CA . LEU A 1 178 ? 17.652 -3.745 30.683 1.00 17.06 ? 213 LEU A CA 1 ATOM 1231 C C . LEU A 1 178 ? 18.379 -5.052 30.320 1.00 14.94 ? 213 LEU A C 1 ATOM 1232 O O . LEU A 1 178 ? 18.345 -5.461 29.148 1.00 15.11 ? 213 LEU A O 1 ATOM 1233 C CB . LEU A 1 178 ? 18.596 -2.553 30.748 1.00 18.40 ? 213 LEU A CB 1 ATOM 1234 C CG . LEU A 1 178 ? 17.867 -1.188 30.669 1.00 22.68 ? 213 LEU A CG 1 ATOM 1235 C CD1 . LEU A 1 178 ? 18.937 -0.107 30.717 1.00 25.94 ? 213 LEU A CD1 1 ATOM 1236 C CD2 . LEU A 1 178 ? 16.979 -1.004 29.434 1.00 24.80 ? 213 LEU A CD2 1 ATOM 1237 N N . TYR A 1 179 ? 18.932 -5.755 31.317 1.00 13.93 ? 214 TYR A N 1 ATOM 1238 C CA . TYR A 1 179 ? 19.615 -7.023 31.026 1.00 13.21 ? 214 TYR A CA 1 ATOM 1239 C C . TYR A 1 179 ? 18.638 -8.149 30.705 1.00 13.26 ? 214 TYR A C 1 ATOM 1240 O O . TYR A 1 179 ? 18.935 -9.012 29.881 1.00 13.31 ? 214 TYR A O 1 ATOM 1241 C CB . TYR A 1 179 ? 20.643 -7.409 32.093 1.00 13.57 ? 214 TYR A CB 1 ATOM 1242 C CG . TYR A 1 179 ? 21.761 -8.272 31.530 1.00 13.13 ? 214 TYR A CG 1 ATOM 1243 C CD1 . TYR A 1 179 ? 22.475 -7.888 30.387 1.00 13.13 ? 214 TYR A CD1 1 ATOM 1244 C CD2 . TYR A 1 179 ? 22.107 -9.470 32.129 1.00 13.53 ? 214 TYR A CD2 1 ATOM 1245 C CE1 . TYR A 1 179 ? 23.510 -8.685 29.885 1.00 13.59 ? 214 TYR A CE1 1 ATOM 1246 C CE2 . TYR A 1 179 ? 23.108 -10.277 31.630 1.00 13.80 ? 214 TYR A CE2 1 ATOM 1247 C CZ . TYR A 1 179 ? 23.811 -9.880 30.489 1.00 13.68 ? 214 TYR A CZ 1 ATOM 1248 O OH . TYR A 1 179 ? 24.811 -10.692 30.019 1.00 14.96 ? 214 TYR A OH 1 ATOM 1249 N N . THR A 1 180 ? 17.458 -8.155 31.334 1.00 13.00 ? 215 THR A N 1 ATOM 1250 C CA . THR A 1 180 ? 16.402 -9.085 30.916 1.00 13.12 ? 215 THR A CA 1 ATOM 1251 C C . THR A 1 180 ? 15.968 -8.861 29.466 1.00 13.60 ? 215 THR A C 1 ATOM 1252 O O . THR A 1 180 ? 15.844 -9.829 28.730 1.00 13.84 ? 215 THR A O 1 ATOM 1253 C CB . THR A 1 180 ? 15.196 -9.020 31.847 1.00 13.30 ? 215 THR A CB 1 ATOM 1254 O OG1 . THR A 1 180 ? 15.534 -9.690 33.051 1.00 12.47 ? 215 THR A OG1 1 ATOM 1255 C CG2 . THR A 1 180 ? 13.947 -9.689 31.242 1.00 13.72 ? 215 THR A CG2 1 ATOM 1256 N N . LEU A 1 181 ? 15.769 -7.599 29.057 1.00 13.21 ? 216 LEU A N 1 ATOM 1257 C CA A LEU A 1 181 ? 15.411 -7.270 27.684 0.50 13.88 ? 216 LEU A CA 1 ATOM 1258 C CA B LEU A 1 181 ? 15.388 -7.299 27.688 0.50 13.82 ? 216 LEU A CA 1 ATOM 1259 C C . LEU A 1 181 ? 16.447 -7.880 26.753 1.00 13.93 ? 216 LEU A C 1 ATOM 1260 O O . LEU A 1 181 ? 16.117 -8.491 25.743 1.00 14.82 ? 216 LEU A O 1 ATOM 1261 C CB A LEU A 1 181 ? 15.367 -5.749 27.481 0.50 15.17 ? 216 LEU A CB 1 ATOM 1262 C CB B LEU A 1 181 ? 15.208 -5.788 27.467 0.50 15.01 ? 216 LEU A CB 1 ATOM 1263 C CG A LEU A 1 181 ? 15.062 -5.231 26.072 0.50 16.00 ? 216 LEU A CG 1 ATOM 1264 C CG B LEU A 1 181 ? 13.880 -5.218 27.989 0.50 15.25 ? 216 LEU A CG 1 ATOM 1265 C CD1 A LEU A 1 181 ? 13.719 -5.752 25.610 0.50 16.28 ? 216 LEU A CD1 1 ATOM 1266 C CD1 B LEU A 1 181 ? 14.002 -3.744 28.317 0.50 16.75 ? 216 LEU A CD1 1 ATOM 1267 C CD2 A LEU A 1 181 ? 15.112 -3.704 26.056 0.50 16.60 ? 216 LEU A CD2 1 ATOM 1268 C CD2 B LEU A 1 181 ? 12.768 -5.465 26.985 0.50 16.01 ? 216 LEU A CD2 1 ATOM 1269 N N . ALA A 1 182 ? 17.706 -7.726 27.120 1.00 12.87 ? 217 ALA A N 1 ATOM 1270 C CA . ALA A 1 182 ? 18.831 -8.168 26.291 1.00 13.68 ? 217 ALA A CA 1 ATOM 1271 C C . ALA A 1 182 ? 19.037 -9.678 26.195 1.00 13.92 ? 217 ALA A C 1 ATOM 1272 O O . ALA A 1 182 ? 19.649 -10.134 25.229 1.00 14.16 ? 217 ALA A O 1 ATOM 1273 C CB . ALA A 1 182 ? 20.110 -7.544 26.777 1.00 14.72 ? 217 ALA A CB 1 ATOM 1274 N N . THR A 1 183 ? 18.553 -10.434 27.178 1.00 12.40 ? 218 THR A N 1 ATOM 1275 C CA . THR A 1 183 ? 18.847 -11.875 27.311 1.00 12.62 ? 218 THR A CA 1 ATOM 1276 C C . THR A 1 183 ? 17.650 -12.816 27.287 1.00 12.63 ? 218 THR A C 1 ATOM 1277 O O . THR A 1 183 ? 17.833 -14.034 27.118 1.00 12.79 ? 218 THR A O 1 ATOM 1278 C CB . THR A 1 183 ? 19.570 -12.166 28.646 1.00 13.22 ? 218 THR A CB 1 ATOM 1279 O OG1 . THR A 1 183 ? 18.714 -11.764 29.743 1.00 13.20 ? 218 THR A OG1 1 ATOM 1280 C CG2 . THR A 1 183 ? 20.881 -11.481 28.720 1.00 12.88 ? 218 THR A CG2 1 ATOM 1281 N N . GLY A 1 184 ? 16.440 -12.304 27.538 1.00 12.13 ? 219 GLY A N 1 ATOM 1282 C CA . GLY A 1 184 ? 15.272 -13.176 27.643 1.00 12.33 ? 219 GLY A CA 1 ATOM 1283 C C . GLY A 1 184 ? 15.218 -13.959 28.952 1.00 12.94 ? 219 GLY A C 1 ATOM 1284 O O . GLY A 1 184 ? 14.395 -14.854 29.090 1.00 13.49 ? 219 GLY A O 1 ATOM 1285 N N . LEU A 1 185 ? 16.060 -13.596 29.918 1.00 12.18 ? 220 LEU A N 1 ATOM 1286 C CA . LEU A 1 185 ? 16.206 -14.346 31.162 1.00 13.30 ? 220 LEU A CA 1 ATOM 1287 C C . LEU A 1 185 ? 15.661 -13.565 32.341 1.00 12.46 ? 220 LEU A C 1 ATOM 1288 O O . LEU A 1 185 ? 15.731 -12.328 32.389 1.00 12.39 ? 220 LEU A O 1 ATOM 1289 C CB . LEU A 1 185 ? 17.679 -14.651 31.430 1.00 13.52 ? 220 LEU A CB 1 ATOM 1290 C CG . LEU A 1 185 ? 18.313 -15.651 30.490 1.00 13.87 ? 220 LEU A CG 1 ATOM 1291 C CD1 . LEU A 1 185 ? 19.808 -15.562 30.642 1.00 14.29 ? 220 LEU A CD1 1 ATOM 1292 C CD2 . LEU A 1 185 ? 17.851 -17.081 30.751 1.00 14.44 ? 220 LEU A CD2 1 ATOM 1293 N N . TYR A 1 186 ? 15.151 -14.312 33.319 1.00 12.37 ? 221 TYR A N 1 ATOM 1294 C CA . TYR A 1 186 ? 14.856 -13.765 34.626 1.00 11.65 ? 221 TYR A CA 1 ATOM 1295 C C . TYR A 1 186 ? 16.137 -13.305 35.268 1.00 12.17 ? 221 TYR A C 1 ATOM 1296 O O . TYR A 1 186 ? 17.166 -13.938 35.104 1.00 12.27 ? 221 TYR A O 1 ATOM 1297 C CB . TYR A 1 186 ? 14.234 -14.824 35.559 1.00 12.51 ? 221 TYR A CB 1 ATOM 1298 C CG . TYR A 1 186 ? 12.903 -15.344 35.091 1.00 11.55 ? 221 TYR A CG 1 ATOM 1299 C CD1 . TYR A 1 186 ? 11.833 -14.474 34.901 1.00 12.30 ? 221 TYR A CD1 1 ATOM 1300 C CD2 . TYR A 1 186 ? 12.727 -16.691 34.815 1.00 12.33 ? 221 TYR A CD2 1 ATOM 1301 C CE1 . TYR A 1 186 ? 10.595 -14.930 34.444 1.00 12.34 ? 221 TYR A CE1 1 ATOM 1302 C CE2 . TYR A 1 186 ? 11.518 -17.145 34.330 1.00 12.45 ? 221 TYR A CE2 1 ATOM 1303 C CZ . TYR A 1 186 ? 10.461 -16.271 34.158 1.00 12.37 ? 221 TYR A CZ 1 ATOM 1304 O OH . TYR A 1 186 ? 9.264 -16.762 33.720 1.00 13.28 ? 221 TYR A OH 1 ATOM 1305 N N . PRO A 1 187 ? 16.073 -12.221 36.055 1.00 12.50 ? 222 PRO A N 1 ATOM 1306 C CA . PRO A 1 187 ? 17.286 -11.820 36.822 1.00 12.86 ? 222 PRO A CA 1 ATOM 1307 C C . PRO A 1 187 ? 18.004 -12.918 37.613 1.00 14.15 ? 222 PRO A C 1 ATOM 1308 O O . PRO A 1 187 ? 19.253 -12.944 37.660 1.00 14.38 ? 222 PRO A O 1 ATOM 1309 C CB . PRO A 1 187 ? 16.758 -10.718 37.714 1.00 13.33 ? 222 PRO A CB 1 ATOM 1310 C CG . PRO A 1 187 ? 15.669 -10.088 36.894 1.00 12.83 ? 222 PRO A CG 1 ATOM 1311 C CD . PRO A 1 187 ? 15.010 -11.217 36.152 1.00 13.39 ? 222 PRO A CD 1 ATOM 1312 N N . GLU A 1 188 ? 17.251 -13.836 38.219 1.00 14.97 ? 223 GLU A N 1 ATOM 1313 C CA . GLU A 1 188 ? 17.880 -14.906 38.978 1.00 14.79 ? 223 GLU A CA 1 ATOM 1314 C C . GLU A 1 188 ? 18.802 -15.761 38.089 1.00 15.37 ? 223 GLU A C 1 ATOM 1315 O O . GLU A 1 188 ? 19.789 -16.299 38.581 1.00 15.88 ? 223 GLU A O 1 ATOM 1316 C CB . GLU A 1 188 ? 16.847 -15.784 39.698 1.00 15.36 ? 223 GLU A CB 1 ATOM 1317 C CG . GLU A 1 188 ? 15.961 -16.589 38.758 1.00 14.58 ? 223 GLU A CG 1 ATOM 1318 C CD . GLU A 1 188 ? 15.021 -17.521 39.457 1.00 15.28 ? 223 GLU A CD 1 ATOM 1319 O OE1 . GLU A 1 188 ? 14.948 -17.516 40.717 1.00 15.36 ? 223 GLU A OE1 1 ATOM 1320 O OE2 . GLU A 1 188 ? 14.314 -18.241 38.726 1.00 14.86 ? 223 GLU A OE2 1 ATOM 1321 N N . SER A 1 189 ? 18.486 -15.835 36.783 1.00 14.72 ? 224 SER A N 1 ATOM 1322 C CA . SER A 1 189 ? 19.279 -16.578 35.823 1.00 15.50 ? 224 SER A CA 1 ATOM 1323 C C . SER A 1 189 ? 20.367 -15.738 35.171 1.00 17.31 ? 224 SER A C 1 ATOM 1324 O O . SER A 1 189 ? 21.452 -16.257 34.956 1.00 19.10 ? 224 SER A O 1 ATOM 1325 C CB . SER A 1 189 ? 18.399 -17.228 34.750 1.00 15.03 ? 224 SER A CB 1 ATOM 1326 O OG . SER A 1 189 ? 17.628 -18.306 35.302 1.00 16.35 ? 224 SER A OG 1 ATOM 1327 N N . HIS A 1 190 ? 20.090 -14.484 34.807 1.00 15.52 ? 225 HIS A N 1 ATOM 1328 C CA . HIS A 1 190 ? 21.133 -13.663 34.173 1.00 14.73 ? 225 HIS A CA 1 ATOM 1329 C C . HIS A 1 190 ? 22.147 -13.072 35.179 1.00 15.62 ? 225 HIS A C 1 ATOM 1330 O O . HIS A 1 190 ? 23.254 -12.737 34.823 1.00 17.08 ? 225 HIS A O 1 ATOM 1331 C CB . HIS A 1 190 ? 20.570 -12.638 33.183 1.00 14.65 ? 225 HIS A CB 1 ATOM 1332 C CG . HIS A 1 190 ? 19.681 -11.561 33.737 1.00 13.01 ? 225 HIS A CG 1 ATOM 1333 N ND1 . HIS A 1 190 ? 20.084 -10.680 34.713 1.00 13.22 ? 225 HIS A ND1 1 ATOM 1334 C CD2 . HIS A 1 190 ? 18.501 -11.076 33.272 1.00 12.87 ? 225 HIS A CD2 1 ATOM 1335 C CE1 . HIS A 1 190 ? 19.159 -9.755 34.883 1.00 13.47 ? 225 HIS A CE1 1 ATOM 1336 N NE2 . HIS A 1 190 ? 18.183 -9.979 34.021 1.00 13.19 ? 225 HIS A NE2 1 ATOM 1337 N N . GLY A 1 191 ? 21.769 -13.019 36.452 1.00 13.99 ? 226 GLY A N 1 ATOM 1338 C CA . GLY A 1 191 ? 22.685 -12.632 37.512 1.00 15.63 ? 226 GLY A CA 1 ATOM 1339 C C . GLY A 1 191 ? 22.549 -11.199 37.993 1.00 14.62 ? 226 GLY A C 1 ATOM 1340 O O . GLY A 1 191 ? 23.022 -10.885 39.083 1.00 14.95 ? 226 GLY A O 1 ATOM 1341 N N . ILE A 1 192 ? 21.907 -10.324 37.216 1.00 14.34 ? 227 ILE A N 1 ATOM 1342 C CA . ILE A 1 192 ? 21.767 -8.916 37.600 1.00 14.41 ? 227 ILE A CA 1 ATOM 1343 C C . ILE A 1 192 ? 20.444 -8.804 38.350 1.00 14.22 ? 227 ILE A C 1 ATOM 1344 O O . ILE A 1 192 ? 19.407 -8.409 37.792 1.00 13.74 ? 227 ILE A O 1 ATOM 1345 C CB . ILE A 1 192 ? 21.849 -7.963 36.410 1.00 14.96 ? 227 ILE A CB 1 ATOM 1346 C CG1 . ILE A 1 192 ? 23.082 -8.289 35.556 1.00 15.51 ? 227 ILE A CG1 1 ATOM 1347 C CG2 . ILE A 1 192 ? 21.889 -6.516 36.866 1.00 15.57 ? 227 ILE A CG2 1 ATOM 1348 C CD1 . ILE A 1 192 ? 24.434 -8.274 36.261 1.00 16.26 ? 227 ILE A CD1 1 ATOM 1349 N N . VAL A 1 193 ? 20.509 -9.181 39.621 1.00 15.04 ? 228 VAL A N 1 ATOM 1350 C CA . VAL A 1 193 ? 19.315 -9.278 40.493 1.00 14.58 ? 228 VAL A CA 1 ATOM 1351 C C . VAL A 1 193 ? 18.926 -7.962 41.150 1.00 14.58 ? 228 VAL A C 1 ATOM 1352 O O . VAL A 1 193 ? 17.877 -7.876 41.783 1.00 15.57 ? 228 VAL A O 1 ATOM 1353 C CB . VAL A 1 193 ? 19.450 -10.383 41.578 1.00 15.15 ? 228 VAL A CB 1 ATOM 1354 C CG1 . VAL A 1 193 ? 19.767 -11.715 40.934 1.00 16.05 ? 228 VAL A CG1 1 ATOM 1355 C CG2 . VAL A 1 193 ? 20.482 -10.045 42.655 1.00 15.88 ? 228 VAL A CG2 1 ATOM 1356 N N . GLY A 1 194 ? 19.774 -6.957 41.003 1.00 15.86 ? 229 GLY A N 1 ATOM 1357 C CA . GLY A 1 194 ? 19.474 -5.600 41.442 1.00 15.47 ? 229 GLY A CA 1 ATOM 1358 C C . GLY A 1 194 ? 20.403 -4.597 40.782 1.00 17.09 ? 229 GLY A C 1 ATOM 1359 O O . GLY A 1 194 ? 21.426 -4.980 40.179 1.00 15.91 ? 229 GLY A O 1 ATOM 1360 N N . ASN A 1 195 ? 20.045 -3.320 40.918 1.00 16.44 ? 230 ASN A N 1 ATOM 1361 C CA . ASN A 1 195 ? 20.988 -2.224 40.679 1.00 18.16 ? 230 ASN A CA 1 ATOM 1362 C C . ASN A 1 195 ? 22.172 -2.263 41.637 1.00 18.76 ? 230 ASN A C 1 ATOM 1363 O O . ASN A 1 195 ? 23.247 -1.815 41.287 1.00 19.16 ? 230 ASN A O 1 ATOM 1364 C CB . ASN A 1 195 ? 20.314 -0.854 40.820 1.00 18.04 ? 230 ASN A CB 1 ATOM 1365 C CG . ASN A 1 195 ? 19.407 -0.507 39.656 1.00 18.08 ? 230 ASN A CG 1 ATOM 1366 O OD1 . ASN A 1 195 ? 19.419 -1.150 38.599 1.00 17.12 ? 230 ASN A OD1 1 ATOM 1367 N ND2 . ASN A 1 195 ? 18.586 0.514 39.862 1.00 18.19 ? 230 ASN A ND2 1 ATOM 1368 N N . SER A 1 196 ? 21.941 -2.735 42.851 1.00 17.72 ? 231 SER A N 1 ATOM 1369 C CA . SER A 1 196 ? 22.977 -3.020 43.825 1.00 20.24 ? 231 SER A CA 1 ATOM 1370 C C . SER A 1 196 ? 22.909 -4.475 44.235 1.00 19.52 ? 231 SER A C 1 ATOM 1371 O O . SER A 1 196 ? 21.819 -5.006 44.406 1.00 20.39 ? 231 SER A O 1 ATOM 1372 C CB . SER A 1 196 ? 22.794 -2.139 45.066 1.00 21.86 ? 231 SER A CB 1 ATOM 1373 O OG . SER A 1 196 ? 23.230 -0.831 44.778 1.00 24.82 ? 231 SER A OG 1 ATOM 1374 N N . MET A 1 197 ? 24.070 -5.115 44.354 1.00 18.49 ? 232 MET A N 1 ATOM 1375 C CA . MET A 1 197 ? 24.168 -6.517 44.744 1.00 19.93 ? 232 MET A CA 1 ATOM 1376 C C . MET A 1 197 ? 25.449 -6.838 45.458 1.00 20.90 ? 232 MET A C 1 ATOM 1377 O O . MET A 1 197 ? 26.472 -6.189 45.232 1.00 20.88 ? 232 MET A O 1 ATOM 1378 C CB . MET A 1 197 ? 24.155 -7.444 43.516 1.00 21.53 ? 232 MET A CB 1 ATOM 1379 C CG . MET A 1 197 ? 23.256 -7.094 42.375 1.00 22.45 ? 232 MET A CG 1 ATOM 1380 S SD . MET A 1 197 ? 23.481 -8.392 41.146 1.00 19.77 ? 232 MET A SD 1 ATOM 1381 C CE . MET A 1 197 ? 24.765 -7.794 40.036 1.00 20.43 ? 232 MET A CE 1 ATOM 1382 N N . TYR A 1 198 ? 25.399 -7.859 46.312 1.00 20.01 ? 233 TYR A N 1 ATOM 1383 C CA . TYR A 1 198 ? 26.581 -8.419 46.931 1.00 20.66 ? 233 TYR A CA 1 ATOM 1384 C C . TYR A 1 198 ? 26.690 -9.901 46.545 1.00 20.60 ? 233 TYR A C 1 ATOM 1385 O O . TYR A 1 198 ? 25.720 -10.674 46.677 1.00 19.44 ? 233 TYR A O 1 ATOM 1386 C CB . TYR A 1 198 ? 26.517 -8.285 48.466 1.00 21.31 ? 233 TYR A CB 1 ATOM 1387 C CG . TYR A 1 198 ? 27.647 -9.016 49.162 1.00 22.06 ? 233 TYR A CG 1 ATOM 1388 C CD1 . TYR A 1 198 ? 28.946 -8.524 49.114 1.00 23.97 ? 233 TYR A CD1 1 ATOM 1389 C CD2 . TYR A 1 198 ? 27.424 -10.223 49.831 1.00 22.90 ? 233 TYR A CD2 1 ATOM 1390 C CE1 . TYR A 1 198 ? 29.993 -9.203 49.712 1.00 25.22 ? 233 TYR A CE1 1 ATOM 1391 C CE2 . TYR A 1 198 ? 28.463 -10.907 50.431 1.00 24.11 ? 233 TYR A CE2 1 ATOM 1392 C CZ . TYR A 1 198 ? 29.747 -10.386 50.373 1.00 25.79 ? 233 TYR A CZ 1 ATOM 1393 O OH . TYR A 1 198 ? 30.796 -11.039 50.976 1.00 28.72 ? 233 TYR A OH 1 ATOM 1394 N N . ASP A 1 199 ? 27.870 -10.301 46.065 1.00 19.83 ? 234 ASP A N 1 ATOM 1395 C CA . ASP A 1 199 ? 28.107 -11.697 45.701 1.00 19.59 ? 234 ASP A CA 1 ATOM 1396 C C . ASP A 1 199 ? 29.063 -12.312 46.723 1.00 21.52 ? 234 ASP A C 1 ATOM 1397 O O . ASP A 1 199 ? 30.217 -11.887 46.828 1.00 20.28 ? 234 ASP A O 1 ATOM 1398 C CB . ASP A 1 199 ? 28.648 -11.777 44.275 1.00 19.58 ? 234 ASP A CB 1 ATOM 1399 C CG . ASP A 1 199 ? 28.763 -13.198 43.776 1.00 19.69 ? 234 ASP A CG 1 ATOM 1400 O OD1 . ASP A 1 199 ? 29.292 -14.054 44.518 1.00 21.26 ? 234 ASP A OD1 1 ATOM 1401 O OD2 . ASP A 1 199 ? 28.339 -13.470 42.636 1.00 19.81 ? 234 ASP A OD2 1 ATOM 1402 N N . PRO A 1 200 ? 28.592 -13.303 47.504 1.00 22.90 ? 235 PRO A N 1 ATOM 1403 C CA . PRO A 1 200 ? 29.457 -13.866 48.553 1.00 25.18 ? 235 PRO A CA 1 ATOM 1404 C C . PRO A 1 200 ? 30.617 -14.738 48.053 1.00 25.75 ? 235 PRO A C 1 ATOM 1405 O O . PRO A 1 200 ? 31.579 -14.922 48.778 1.00 26.75 ? 235 PRO A O 1 ATOM 1406 C CB . PRO A 1 200 ? 28.494 -14.676 49.444 1.00 25.84 ? 235 PRO A CB 1 ATOM 1407 C CG . PRO A 1 200 ? 27.240 -14.816 48.684 1.00 26.06 ? 235 PRO A CG 1 ATOM 1408 C CD . PRO A 1 200 ? 27.223 -13.840 47.538 1.00 23.45 ? 235 PRO A CD 1 ATOM 1409 N N . VAL A 1 201 ? 30.528 -15.243 46.822 1.00 24.47 ? 236 VAL A N 1 ATOM 1410 C CA . VAL A 1 201 ? 31.629 -15.980 46.194 1.00 24.72 ? 236 VAL A CA 1 ATOM 1411 C C . VAL A 1 201 ? 32.712 -14.973 45.760 1.00 25.62 ? 236 VAL A C 1 ATOM 1412 O O . VAL A 1 201 ? 33.902 -15.208 45.996 1.00 25.49 ? 236 VAL A O 1 ATOM 1413 C CB . VAL A 1 201 ? 31.131 -16.844 45.010 1.00 24.26 ? 236 VAL A CB 1 ATOM 1414 C CG1 . VAL A 1 201 ? 32.285 -17.411 44.180 1.00 24.99 ? 236 VAL A CG1 1 ATOM 1415 C CG2 . VAL A 1 201 ? 30.230 -17.975 45.501 1.00 25.32 ? 236 VAL A CG2 1 ATOM 1416 N N . PHE A 1 202 ? 32.313 -13.857 45.142 1.00 23.47 ? 237 PHE A N 1 ATOM 1417 C CA . PHE A 1 202 ? 33.298 -12.813 44.784 1.00 25.37 ? 237 PHE A CA 1 ATOM 1418 C C . PHE A 1 202 ? 33.751 -12.033 46.004 1.00 27.49 ? 237 PHE A C 1 ATOM 1419 O O . PHE A 1 202 ? 34.869 -11.505 46.007 1.00 27.92 ? 237 PHE A O 1 ATOM 1420 C CB . PHE A 1 202 ? 32.735 -11.779 43.807 1.00 24.30 ? 237 PHE A CB 1 ATOM 1421 C CG . PHE A 1 202 ? 32.190 -12.338 42.535 1.00 22.06 ? 237 PHE A CG 1 ATOM 1422 C CD1 . PHE A 1 202 ? 32.543 -13.612 42.073 1.00 22.70 ? 237 PHE A CD1 1 ATOM 1423 C CD2 . PHE A 1 202 ? 31.345 -11.557 41.764 1.00 20.99 ? 237 PHE A CD2 1 ATOM 1424 C CE1 . PHE A 1 202 ? 32.026 -14.087 40.883 1.00 21.81 ? 237 PHE A CE1 1 ATOM 1425 C CE2 . PHE A 1 202 ? 30.827 -12.035 40.583 1.00 21.13 ? 237 PHE A CE2 1 ATOM 1426 C CZ . PHE A 1 202 ? 31.174 -13.301 40.142 1.00 21.30 ? 237 PHE A CZ 1 ATOM 1427 N N . ASP A 1 203 ? 32.880 -11.955 47.024 1.00 27.33 ? 238 ASP A N 1 ATOM 1428 C CA . ASP A 1 203 ? 33.046 -11.071 48.173 1.00 27.91 ? 238 ASP A CA 1 ATOM 1429 C C . ASP A 1 203 ? 33.289 -9.664 47.667 1.00 27.24 ? 238 ASP A C 1 ATOM 1430 O O . ASP A 1 203 ? 34.325 -9.041 47.951 1.00 28.04 ? 238 ASP A O 1 ATOM 1431 C CB . ASP A 1 203 ? 34.160 -11.535 49.127 1.00 31.22 ? 238 ASP A CB 1 ATOM 1432 C CG . ASP A 1 203 ? 34.256 -10.671 50.385 1.00 33.57 ? 238 ASP A CG 1 ATOM 1433 O OD1 . ASP A 1 203 ? 33.229 -10.106 50.826 1.00 35.51 ? 238 ASP A OD1 1 ATOM 1434 O OD2 . ASP A 1 203 ? 35.368 -10.521 50.915 1.00 38.07 ? 238 ASP A OD2 1 ATOM 1435 N N . ALA A 1 204 ? 32.321 -9.197 46.897 1.00 24.12 ? 239 ALA A N 1 ATOM 1436 C CA . ALA A 1 204 ? 32.345 -7.905 46.251 1.00 23.54 ? 239 ALA A CA 1 ATOM 1437 C C . ALA A 1 204 ? 30.919 -7.443 46.028 1.00 23.95 ? 239 ALA A C 1 ATOM 1438 O O . ALA A 1 204 ? 29.992 -8.262 46.011 1.00 21.37 ? 239 ALA A O 1 ATOM 1439 C CB . ALA A 1 204 ? 33.070 -7.996 44.922 1.00 23.50 ? 239 ALA A CB 1 ATOM 1440 N N . SER A 1 205 ? 30.769 -6.132 45.857 1.00 24.05 ? 240 SER A N 1 ATOM 1441 C CA . SER A 1 205 ? 29.486 -5.491 45.665 1.00 24.59 ? 240 SER A CA 1 ATOM 1442 C C . SER A 1 205 ? 29.462 -4.792 44.314 1.00 23.98 ? 240 SER A C 1 ATOM 1443 O O . SER A 1 205 ? 30.461 -4.204 43.903 1.00 25.03 ? 240 SER A O 1 ATOM 1444 C CB . SER A 1 205 ? 29.237 -4.462 46.775 1.00 26.32 ? 240 SER A CB 1 ATOM 1445 O OG . SER A 1 205 ? 29.075 -5.124 48.023 1.00 28.49 ? 240 SER A OG 1 ATOM 1446 N N . PHE A 1 206 ? 28.309 -4.868 43.652 1.00 22.02 ? 241 PHE A N 1 ATOM 1447 C CA . PHE A 1 206 ? 28.030 -4.280 42.345 1.00 21.97 ? 241 PHE A CA 1 ATOM 1448 C C . PHE A 1 206 ? 27.121 -3.074 42.601 1.00 24.30 ? 241 PHE A C 1 ATOM 1449 O O . PHE A 1 206 ? 26.190 -3.190 43.405 1.00 21.80 ? 241 PHE A O 1 ATOM 1450 C CB . PHE A 1 206 ? 27.270 -5.352 41.554 1.00 21.57 ? 241 PHE A CB 1 ATOM 1451 C CG . PHE A 1 206 ? 26.770 -4.935 40.204 1.00 19.16 ? 241 PHE A CG 1 ATOM 1452 C CD1 . PHE A 1 206 ? 25.603 -4.184 40.068 1.00 19.11 ? 241 PHE A CD1 1 ATOM 1453 C CD2 . PHE A 1 206 ? 27.389 -5.423 39.058 1.00 19.00 ? 241 PHE A CD2 1 ATOM 1454 C CE1 . PHE A 1 206 ? 25.099 -3.874 38.813 1.00 19.42 ? 241 PHE A CE1 1 ATOM 1455 C CE2 . PHE A 1 206 ? 26.905 -5.108 37.816 1.00 18.42 ? 241 PHE A CE2 1 ATOM 1456 C CZ . PHE A 1 206 ? 25.745 -4.338 37.689 1.00 18.36 ? 241 PHE A CZ 1 ATOM 1457 N N . HIS A 1 207 ? 27.371 -1.945 41.928 1.00 24.98 ? 242 HIS A N 1 ATOM 1458 C CA . HIS A 1 207 ? 26.535 -0.736 42.041 1.00 27.62 ? 242 HIS A CA 1 ATOM 1459 C C . HIS A 1 207 ? 26.361 -0.053 40.694 1.00 28.35 ? 242 HIS A C 1 ATOM 1460 O O . HIS A 1 207 ? 27.179 -0.206 39.787 1.00 27.47 ? 242 HIS A O 1 ATOM 1461 C CB . HIS A 1 207 ? 27.133 0.279 43.024 1.00 29.32 ? 242 HIS A CB 1 ATOM 1462 C CG . HIS A 1 207 ? 27.181 -0.204 44.435 1.00 31.37 ? 242 HIS A CG 1 ATOM 1463 N ND1 . HIS A 1 207 ? 26.043 -0.488 45.170 1.00 33.17 ? 242 HIS A ND1 1 ATOM 1464 C CD2 . HIS A 1 207 ? 28.231 -0.474 45.245 1.00 31.01 ? 242 HIS A CD2 1 ATOM 1465 C CE1 . HIS A 1 207 ? 26.396 -0.916 46.367 1.00 31.63 ? 242 HIS A CE1 1 ATOM 1466 N NE2 . HIS A 1 207 ? 27.716 -0.902 46.443 1.00 32.03 ? 242 HIS A NE2 1 ATOM 1467 N N . LEU A 1 208 ? 25.281 0.702 40.563 1.00 31.08 ? 243 LEU A N 1 ATOM 1468 C CA . LEU A 1 208 ? 24.981 1.408 39.309 1.00 35.69 ? 243 LEU A CA 1 ATOM 1469 C C . LEU A 1 208 ? 26.072 2.453 39.016 1.00 37.75 ? 243 LEU A C 1 ATOM 1470 O O . LEU A 1 208 ? 26.416 2.677 37.862 1.00 37.23 ? 243 LEU A O 1 ATOM 1471 C CB . LEU A 1 208 ? 23.572 2.029 39.354 1.00 37.85 ? 243 LEU A CB 1 ATOM 1472 C CG . LEU A 1 208 ? 22.994 2.434 37.990 1.00 43.71 ? 243 LEU A CG 1 ATOM 1473 C CD1 . LEU A 1 208 ? 21.515 2.076 37.864 1.00 44.89 ? 243 LEU A CD1 1 ATOM 1474 C CD2 . LEU A 1 208 ? 23.217 3.916 37.706 1.00 44.95 ? 243 LEU A CD2 1 ATOM 1475 N N . ARG A 1 209 ? 26.638 3.055 40.060 1.00 39.37 ? 244 ARG A N 1 ATOM 1476 C CA . ARG A 1 209 ? 27.802 3.936 39.924 1.00 42.82 ? 244 ARG A CA 1 ATOM 1477 C C . ARG A 1 209 ? 29.064 3.178 40.326 1.00 41.78 ? 244 ARG A C 1 ATOM 1478 O O . ARG A 1 209 ? 29.030 2.352 41.234 1.00 41.15 ? 244 ARG A O 1 ATOM 1479 C CB . ARG A 1 209 ? 27.636 5.196 40.787 1.00 49.90 ? 244 ARG A CB 1 ATOM 1480 C CG . ARG A 1 209 ? 26.531 6.138 40.310 1.00 55.49 ? 244 ARG A CG 1 ATOM 1481 C CD . ARG A 1 209 ? 26.414 7.372 41.202 1.00 61.29 ? 244 ARG A CD 1 ATOM 1482 N NE . ARG A 1 209 ? 25.144 8.090 41.015 1.00 68.30 ? 244 ARG A NE 1 ATOM 1483 C CZ . ARG A 1 209 ? 24.902 9.066 40.128 1.00 73.02 ? 244 ARG A CZ 1 ATOM 1484 N NH1 . ARG A 1 209 ? 25.835 9.507 39.284 1.00 74.63 ? 244 ARG A NH1 1 ATOM 1485 N NH2 . ARG A 1 209 ? 23.693 9.621 40.086 1.00 74.49 ? 244 ARG A NH2 1 ATOM 1486 N N . GLY A 1 210 ? 30.170 3.467 39.643 1.00 39.65 ? 245 GLY A N 1 ATOM 1487 C CA . GLY A 1 210 ? 31.459 2.814 39.896 1.00 38.79 ? 245 GLY A CA 1 ATOM 1488 C C . GLY A 1 210 ? 31.900 1.870 38.788 1.00 37.87 ? 245 GLY A C 1 ATOM 1489 O O . GLY A 1 210 ? 31.174 1.646 37.811 1.00 34.20 ? 245 GLY A O 1 ATOM 1490 N N . ARG A 1 211 ? 33.095 1.314 38.979 1.00 37.50 ? 246 ARG A N 1 ATOM 1491 C CA . ARG A 1 211 ? 33.816 0.535 37.974 1.00 38.99 ? 246 ARG A CA 1 ATOM 1492 C C . ARG A 1 211 ? 33.489 -0.976 38.063 1.00 33.01 ? 246 ARG A C 1 ATOM 1493 O O . ARG A 1 211 ? 33.689 -1.723 37.107 1.00 30.79 ? 246 ARG A O 1 ATOM 1494 C CB . ARG A 1 211 ? 35.337 0.812 38.122 1.00 45.97 ? 246 ARG A CB 1 ATOM 1495 C CG . ARG A 1 211 ? 36.323 -0.162 37.468 1.00 54.47 ? 246 ARG A CG 1 ATOM 1496 C CD . ARG A 1 211 ? 36.227 -0.238 35.939 1.00 61.30 ? 246 ARG A CD 1 ATOM 1497 N NE . ARG A 1 211 ? 36.777 0.941 35.256 1.00 68.95 ? 246 ARG A NE 1 ATOM 1498 C CZ . ARG A 1 211 ? 38.075 1.197 35.057 1.00 72.40 ? 246 ARG A CZ 1 ATOM 1499 N NH1 . ARG A 1 211 ? 39.028 0.368 35.493 1.00 76.13 ? 246 ARG A NH1 1 ATOM 1500 N NH2 . ARG A 1 211 ? 38.428 2.311 34.415 1.00 71.07 ? 246 ARG A NH2 1 ATOM 1501 N N . GLU A 1 212 ? 32.993 -1.423 39.210 1.00 28.31 ? 247 GLU A N 1 ATOM 1502 C CA . GLU A 1 212 ? 32.834 -2.847 39.467 1.00 27.01 ? 247 GLU A CA 1 ATOM 1503 C C . GLU A 1 212 ? 31.910 -3.515 38.457 1.00 24.64 ? 247 GLU A C 1 ATOM 1504 O O . GLU A 1 212 ? 32.184 -4.620 37.991 1.00 24.11 ? 247 GLU A O 1 ATOM 1505 C CB . GLU A 1 212 ? 32.318 -3.078 40.880 1.00 26.63 ? 247 GLU A CB 1 ATOM 1506 C CG . GLU A 1 212 ? 32.163 -4.544 41.251 1.00 26.88 ? 247 GLU A CG 1 ATOM 1507 C CD . GLU A 1 212 ? 33.444 -5.333 41.088 1.00 28.67 ? 247 GLU A CD 1 ATOM 1508 O OE1 . GLU A 1 212 ? 34.492 -4.835 41.536 1.00 30.68 ? 247 GLU A OE1 1 ATOM 1509 O OE2 . GLU A 1 212 ? 33.420 -6.449 40.521 1.00 26.00 ? 247 GLU A OE2 1 ATOM 1510 N N . LYS A 1 213 ? 30.833 -2.820 38.119 1.00 23.31 ? 248 LYS A N 1 ATOM 1511 C CA . LYS A 1 213 ? 29.852 -3.304 37.139 1.00 22.50 ? 248 LYS A CA 1 ATOM 1512 C C . LYS A 1 213 ? 30.410 -3.643 35.752 1.00 22.50 ? 248 LYS A C 1 ATOM 1513 O O . LYS A 1 213 ? 29.793 -4.438 35.026 1.00 21.30 ? 248 LYS A O 1 ATOM 1514 C CB . LYS A 1 213 ? 28.695 -2.305 36.995 1.00 22.77 ? 248 LYS A CB 1 ATOM 1515 C CG . LYS A 1 213 ? 29.083 -0.938 36.438 1.00 23.12 ? 248 LYS A CG 1 ATOM 1516 C CD . LYS A 1 213 ? 27.853 -0.100 36.198 1.00 24.91 ? 248 LYS A CD 1 ATOM 1517 C CE . LYS A 1 213 ? 28.162 1.171 35.430 1.00 27.83 ? 248 LYS A CE 1 ATOM 1518 N NZ . LYS A 1 213 ? 28.800 2.182 36.294 1.00 28.70 ? 248 LYS A NZ 1 ATOM 1519 N N . PHE A 1 214 ? 31.535 -3.035 35.375 1.00 23.44 ? 249 PHE A N 1 ATOM 1520 C CA . PHE A 1 214 ? 32.191 -3.334 34.107 1.00 25.86 ? 249 PHE A CA 1 ATOM 1521 C C . PHE A 1 214 ? 32.927 -4.663 34.076 1.00 25.50 ? 249 PHE A C 1 ATOM 1522 O O . PHE A 1 214 ? 33.340 -5.118 32.997 1.00 26.29 ? 249 PHE A O 1 ATOM 1523 C CB . PHE A 1 214 ? 33.186 -2.224 33.726 1.00 29.21 ? 249 PHE A CB 1 ATOM 1524 C CG . PHE A 1 214 ? 32.538 -0.896 33.473 1.00 31.63 ? 249 PHE A CG 1 ATOM 1525 C CD1 . PHE A 1 214 ? 31.806 -0.677 32.318 1.00 36.14 ? 249 PHE A CD1 1 ATOM 1526 C CD2 . PHE A 1 214 ? 32.646 0.129 34.395 1.00 36.60 ? 249 PHE A CD2 1 ATOM 1527 C CE1 . PHE A 1 214 ? 31.213 0.555 32.076 1.00 35.44 ? 249 PHE A CE1 1 ATOM 1528 C CE2 . PHE A 1 214 ? 32.040 1.355 34.169 1.00 36.06 ? 249 PHE A CE2 1 ATOM 1529 C CZ . PHE A 1 214 ? 31.319 1.561 33.015 1.00 35.97 ? 249 PHE A CZ 1 ATOM 1530 N N . ASN A 1 215 ? 33.159 -5.270 35.231 1.00 23.38 ? 250 ASN A N 1 ATOM 1531 C CA . ASN A 1 215 ? 33.764 -6.593 35.267 1.00 22.82 ? 250 ASN A CA 1 ATOM 1532 C C . ASN A 1 215 ? 32.787 -7.646 34.708 1.00 21.36 ? 250 ASN A C 1 ATOM 1533 O O . ASN A 1 215 ? 31.652 -7.753 35.147 1.00 20.12 ? 250 ASN A O 1 ATOM 1534 C CB . ASN A 1 215 ? 34.222 -6.914 36.681 1.00 23.94 ? 250 ASN A CB 1 ATOM 1535 C CG . ASN A 1 215 ? 35.388 -6.019 37.123 1.00 28.26 ? 250 ASN A CG 1 ATOM 1536 O OD1 . ASN A 1 215 ? 36.208 -5.575 36.299 1.00 29.60 ? 250 ASN A OD1 1 ATOM 1537 N ND2 . ASN A 1 215 ? 35.472 -5.757 38.421 1.00 32.42 ? 250 ASN A ND2 1 ATOM 1538 N N . HIS A 1 216 ? 33.238 -8.411 33.730 1.00 21.11 ? 251 HIS A N 1 ATOM 1539 C CA . HIS A 1 216 ? 32.371 -9.409 33.111 1.00 20.75 ? 251 HIS A CA 1 ATOM 1540 C C . HIS A 1 216 ? 31.853 -10.509 34.045 1.00 19.53 ? 251 HIS A C 1 ATOM 1541 O O . HIS A 1 216 ? 30.816 -11.098 33.755 1.00 18.28 ? 251 HIS A O 1 ATOM 1542 C CB . HIS A 1 216 ? 33.042 -10.030 31.887 1.00 21.97 ? 251 HIS A CB 1 ATOM 1543 C CG . HIS A 1 216 ? 34.307 -10.778 32.178 1.00 22.76 ? 251 HIS A CG 1 ATOM 1544 N ND1 . HIS A 1 216 ? 34.323 -12.074 32.654 1.00 23.46 ? 251 HIS A ND1 1 ATOM 1545 C CD2 . HIS A 1 216 ? 35.606 -10.424 32.011 1.00 24.57 ? 251 HIS A CD2 1 ATOM 1546 C CE1 . HIS A 1 216 ? 35.570 -12.481 32.777 1.00 24.64 ? 251 HIS A CE1 1 ATOM 1547 N NE2 . HIS A 1 216 ? 36.369 -11.498 32.391 1.00 25.00 ? 251 HIS A NE2 1 ATOM 1548 N N . ARG A 1 217 ? 32.547 -10.747 35.158 1.00 18.65 ? 252 ARG A N 1 ATOM 1549 C CA . ARG A 1 217 ? 32.172 -11.806 36.086 1.00 19.39 ? 252 ARG A CA 1 ATOM 1550 C C . ARG A 1 217 ? 30.701 -11.769 36.507 1.00 18.51 ? 252 ARG A C 1 ATOM 1551 O O . ARG A 1 217 ? 30.141 -12.795 36.823 1.00 19.36 ? 252 ARG A O 1 ATOM 1552 C CB . ARG A 1 217 ? 33.047 -11.818 37.325 1.00 19.71 ? 252 ARG A CB 1 ATOM 1553 C CG . ARG A 1 217 ? 33.062 -10.535 38.146 1.00 19.64 ? 252 ARG A CG 1 ATOM 1554 C CD . ARG A 1 217 ? 34.030 -10.726 39.311 1.00 21.06 ? 252 ARG A CD 1 ATOM 1555 N NE . ARG A 1 217 ? 34.120 -9.560 40.192 1.00 21.26 ? 252 ARG A NE 1 ATOM 1556 C CZ . ARG A 1 217 ? 34.837 -9.521 41.318 1.00 22.79 ? 252 ARG A CZ 1 ATOM 1557 N NH1 . ARG A 1 217 ? 35.558 -10.569 41.739 1.00 23.44 ? 252 ARG A NH1 1 ATOM 1558 N NH2 . ARG A 1 217 ? 34.841 -8.420 42.039 1.00 23.72 ? 252 ARG A NH2 1 ATOM 1559 N N . TRP A 1 218 ? 30.106 -10.583 36.531 1.00 18.28 ? 253 TRP A N 1 ATOM 1560 C CA . TRP A 1 218 ? 28.754 -10.396 37.048 1.00 16.97 ? 253 TRP A CA 1 ATOM 1561 C C . TRP A 1 218 ? 27.652 -10.856 36.102 1.00 17.45 ? 253 TRP A C 1 ATOM 1562 O O . TRP A 1 218 ? 26.549 -11.149 36.548 1.00 17.11 ? 253 TRP A O 1 ATOM 1563 C CB . TRP A 1 218 ? 28.496 -8.928 37.372 1.00 17.36 ? 253 TRP A CB 1 ATOM 1564 C CG . TRP A 1 218 ? 29.327 -8.409 38.472 1.00 17.77 ? 253 TRP A CG 1 ATOM 1565 C CD1 . TRP A 1 218 ? 30.485 -7.717 38.353 1.00 19.36 ? 253 TRP A CD1 1 ATOM 1566 C CD2 . TRP A 1 218 ? 29.071 -8.528 39.885 1.00 18.41 ? 253 TRP A CD2 1 ATOM 1567 N NE1 . TRP A 1 218 ? 30.978 -7.398 39.582 1.00 19.85 ? 253 TRP A NE1 1 ATOM 1568 C CE2 . TRP A 1 218 ? 30.133 -7.883 40.546 1.00 19.27 ? 253 TRP A CE2 1 ATOM 1569 C CE3 . TRP A 1 218 ? 28.041 -9.104 40.645 1.00 18.85 ? 253 TRP A CE3 1 ATOM 1570 C CZ2 . TRP A 1 218 ? 30.205 -7.795 41.933 1.00 19.83 ? 253 TRP A CZ2 1 ATOM 1571 C CZ3 . TRP A 1 218 ? 28.117 -9.031 42.024 1.00 19.32 ? 253 TRP A CZ3 1 ATOM 1572 C CH2 . TRP A 1 218 ? 29.175 -8.352 42.651 1.00 19.49 ? 253 TRP A CH2 1 ATOM 1573 N N . TRP A 1 219 ? 27.963 -10.896 34.809 1.00 16.13 ? 254 TRP A N 1 ATOM 1574 C CA . TRP A 1 219 ? 26.937 -10.925 33.774 1.00 16.13 ? 254 TRP A CA 1 ATOM 1575 C C . TRP A 1 219 ? 26.841 -12.302 33.153 1.00 16.57 ? 254 TRP A C 1 ATOM 1576 O O . TRP A 1 219 ? 27.784 -12.762 32.518 1.00 17.45 ? 254 TRP A O 1 ATOM 1577 C CB . TRP A 1 219 ? 27.286 -9.902 32.709 1.00 16.09 ? 254 TRP A CB 1 ATOM 1578 C CG . TRP A 1 219 ? 27.519 -8.516 33.238 1.00 16.14 ? 254 TRP A CG 1 ATOM 1579 C CD1 . TRP A 1 219 ? 28.672 -8.027 33.777 1.00 17.20 ? 254 TRP A CD1 1 ATOM 1580 C CD2 . TRP A 1 219 ? 26.574 -7.455 33.276 1.00 15.49 ? 254 TRP A CD2 1 ATOM 1581 N NE1 . TRP A 1 219 ? 28.495 -6.719 34.168 1.00 17.22 ? 254 TRP A NE1 1 ATOM 1582 C CE2 . TRP A 1 219 ? 27.216 -6.342 33.862 1.00 15.30 ? 254 TRP A CE2 1 ATOM 1583 C CE3 . TRP A 1 219 ? 25.239 -7.334 32.880 1.00 14.74 ? 254 TRP A CE3 1 ATOM 1584 C CZ2 . TRP A 1 219 ? 26.568 -5.108 34.040 1.00 16.07 ? 254 TRP A CZ2 1 ATOM 1585 C CZ3 . TRP A 1 219 ? 24.591 -6.104 33.041 1.00 15.28 ? 254 TRP A CZ3 1 ATOM 1586 C CH2 . TRP A 1 219 ? 25.259 -5.009 33.638 1.00 15.32 ? 254 TRP A CH2 1 ATOM 1587 N N . GLY A 1 220 ? 25.684 -12.939 33.299 1.00 15.36 ? 255 GLY A N 1 ATOM 1588 C CA . GLY A 1 220 ? 25.450 -14.281 32.770 1.00 15.86 ? 255 GLY A CA 1 ATOM 1589 C C . GLY A 1 220 ? 24.575 -14.253 31.533 1.00 15.20 ? 255 GLY A C 1 ATOM 1590 O O . GLY A 1 220 ? 24.310 -13.196 30.977 1.00 16.50 ? 255 GLY A O 1 ATOM 1591 N N . GLY A 1 221 ? 24.113 -15.425 31.104 1.00 15.35 ? 256 GLY A N 1 ATOM 1592 C CA . GLY A 1 221 ? 23.306 -15.527 29.898 1.00 15.18 ? 256 GLY A CA 1 ATOM 1593 C C . GLY A 1 221 ? 24.076 -15.066 28.676 1.00 15.78 ? 256 GLY A C 1 ATOM 1594 O O . GLY A 1 221 ? 25.335 -15.077 28.666 1.00 16.98 ? 256 GLY A O 1 ATOM 1595 N N . GLN A 1 222 ? 23.334 -14.708 27.634 1.00 14.17 ? 257 GLN A N 1 ATOM 1596 C CA . GLN A 1 222 ? 23.921 -14.293 26.380 1.00 14.94 ? 257 GLN A CA 1 ATOM 1597 C C . GLN A 1 222 ? 23.095 -13.164 25.795 1.00 13.42 ? 257 GLN A C 1 ATOM 1598 O O . GLN A 1 222 ? 22.020 -13.393 25.279 1.00 15.19 ? 257 GLN A O 1 ATOM 1599 C CB . GLN A 1 222 ? 24.036 -15.453 25.393 1.00 16.25 ? 257 GLN A CB 1 ATOM 1600 C CG . GLN A 1 222 ? 24.804 -15.032 24.160 1.00 17.07 ? 257 GLN A CG 1 ATOM 1601 C CD . GLN A 1 222 ? 24.888 -16.138 23.152 1.00 18.67 ? 257 GLN A CD 1 ATOM 1602 O OE1 . GLN A 1 222 ? 24.140 -16.154 22.162 1.00 17.68 ? 257 GLN A OE1 1 ATOM 1603 N NE2 . GLN A 1 222 ? 25.770 -17.102 23.414 1.00 20.63 ? 257 GLN A NE2 1 ATOM 1604 N N . PRO A 1 223 ? 23.562 -11.932 25.917 1.00 13.15 ? 258 PRO A N 1 ATOM 1605 C CA . PRO A 1 223 ? 22.752 -10.814 25.467 1.00 12.81 ? 258 PRO A CA 1 ATOM 1606 C C . PRO A 1 223 ? 22.749 -10.685 23.948 1.00 13.62 ? 258 PRO A C 1 ATOM 1607 O O . PRO A 1 223 ? 23.659 -11.232 23.253 1.00 13.90 ? 258 PRO A O 1 ATOM 1608 C CB . PRO A 1 223 ? 23.427 -9.604 26.134 1.00 13.79 ? 258 PRO A CB 1 ATOM 1609 C CG . PRO A 1 223 ? 24.835 -10.036 26.316 1.00 13.78 ? 258 PRO A CG 1 ATOM 1610 C CD . PRO A 1 223 ? 24.805 -11.494 26.587 1.00 13.80 ? 258 PRO A CD 1 ATOM 1611 N N . LEU A 1 224 ? 21.765 -9.949 23.453 1.00 13.18 ? 259 LEU A N 1 ATOM 1612 C CA . LEU A 1 224 ? 21.494 -9.871 22.014 1.00 14.62 ? 259 LEU A CA 1 ATOM 1613 C C . LEU A 1 224 ? 22.716 -9.483 21.184 1.00 15.33 ? 259 LEU A C 1 ATOM 1614 O O . LEU A 1 224 ? 22.945 -10.039 20.131 1.00 15.88 ? 259 LEU A O 1 ATOM 1615 C CB . LEU A 1 224 ? 20.386 -8.856 21.746 1.00 15.29 ? 259 LEU A CB 1 ATOM 1616 C CG . LEU A 1 224 ? 19.900 -8.738 20.294 1.00 16.28 ? 259 LEU A CG 1 ATOM 1617 C CD1 . LEU A 1 224 ? 19.270 -10.059 19.870 1.00 17.32 ? 259 LEU A CD1 1 ATOM 1618 C CD2 . LEU A 1 224 ? 18.900 -7.616 20.183 1.00 16.50 ? 259 LEU A CD2 1 ATOM 1619 N N . TRP A 1 225 ? 23.509 -8.533 21.665 1.00 15.44 ? 260 TRP A N 1 ATOM 1620 C CA . TRP A 1 225 ? 24.668 -8.082 20.891 1.00 16.31 ? 260 TRP A CA 1 ATOM 1621 C C . TRP A 1 225 ? 25.723 -9.194 20.716 1.00 17.05 ? 260 TRP A C 1 ATOM 1622 O O . TRP A 1 225 ? 26.411 -9.244 19.693 1.00 17.04 ? 260 TRP A O 1 ATOM 1623 C CB . TRP A 1 225 ? 25.288 -6.802 21.478 1.00 16.51 ? 260 TRP A CB 1 ATOM 1624 C CG . TRP A 1 225 ? 25.706 -6.845 22.949 1.00 16.09 ? 260 TRP A CG 1 ATOM 1625 C CD1 . TRP A 1 225 ? 26.953 -7.116 23.439 1.00 18.67 ? 260 TRP A CD1 1 ATOM 1626 C CD2 . TRP A 1 225 ? 24.877 -6.559 24.090 1.00 16.64 ? 260 TRP A CD2 1 ATOM 1627 N NE1 . TRP A 1 225 ? 26.951 -7.038 24.826 1.00 18.77 ? 260 TRP A NE1 1 ATOM 1628 C CE2 . TRP A 1 225 ? 25.694 -6.691 25.249 1.00 16.92 ? 260 TRP A CE2 1 ATOM 1629 C CE3 . TRP A 1 225 ? 23.539 -6.162 24.245 1.00 16.72 ? 260 TRP A CE3 1 ATOM 1630 C CZ2 . TRP A 1 225 ? 25.196 -6.475 26.546 1.00 17.25 ? 260 TRP A CZ2 1 ATOM 1631 C CZ3 . TRP A 1 225 ? 23.045 -5.964 25.532 1.00 17.03 ? 260 TRP A CZ3 1 ATOM 1632 C CH2 . TRP A 1 225 ? 23.876 -6.121 26.665 1.00 16.82 ? 260 TRP A CH2 1 ATOM 1633 N N . ILE A 1 226 ? 25.825 -10.084 21.697 1.00 15.39 ? 261 ILE A N 1 ATOM 1634 C CA . ILE A 1 226 ? 26.721 -11.232 21.630 1.00 15.58 ? 261 ILE A CA 1 ATOM 1635 C C . ILE A 1 226 ? 26.123 -12.349 20.782 1.00 15.41 ? 261 ILE A C 1 ATOM 1636 O O . ILE A 1 226 ? 26.813 -12.927 19.946 1.00 16.01 ? 261 ILE A O 1 ATOM 1637 C CB . ILE A 1 226 ? 27.077 -11.746 23.033 1.00 16.37 ? 261 ILE A CB 1 ATOM 1638 C CG1 . ILE A 1 226 ? 27.848 -10.672 23.832 1.00 17.72 ? 261 ILE A CG1 1 ATOM 1639 C CG2 . ILE A 1 226 ? 27.854 -13.059 22.950 1.00 16.76 ? 261 ILE A CG2 1 ATOM 1640 C CD1 . ILE A 1 226 ? 29.130 -10.156 23.212 1.00 18.57 ? 261 ILE A CD1 1 ATOM 1641 N N . THR A 1 227 ? 24.846 -12.642 20.961 1.00 14.85 ? 262 THR A N 1 ATOM 1642 C CA . THR A 1 227 ? 24.156 -13.592 20.081 1.00 15.12 ? 262 THR A CA 1 ATOM 1643 C C . THR A 1 227 ? 24.344 -13.199 18.616 1.00 15.22 ? 262 THR A C 1 ATOM 1644 O O . THR A 1 227 ? 24.644 -14.050 17.787 1.00 15.25 ? 262 THR A O 1 ATOM 1645 C CB . THR A 1 227 ? 22.662 -13.653 20.417 1.00 15.54 ? 262 THR A CB 1 ATOM 1646 O OG1 . THR A 1 227 ? 22.530 -13.970 21.806 1.00 14.31 ? 262 THR A OG1 1 ATOM 1647 C CG2 . THR A 1 227 ? 21.966 -14.695 19.609 1.00 15.96 ? 262 THR A CG2 1 ATOM 1648 N N . ALA A 1 228 ? 24.190 -11.914 18.323 1.00 15.51 ? 263 ALA A N 1 ATOM 1649 C CA . ALA A 1 228 ? 24.352 -11.429 16.957 1.00 16.25 ? 263 ALA A CA 1 ATOM 1650 C C . ALA A 1 228 ? 25.794 -11.646 16.461 1.00 17.42 ? 263 ALA A C 1 ATOM 1651 O O . ALA A 1 228 ? 26.012 -12.275 15.416 1.00 18.37 ? 263 ALA A O 1 ATOM 1652 C CB . ALA A 1 228 ? 23.928 -9.968 16.880 1.00 15.70 ? 263 ALA A CB 1 ATOM 1653 N N . THR A 1 229 ? 26.785 -11.166 17.211 1.00 17.66 ? 264 THR A N 1 ATOM 1654 C CA . THR A 1 229 ? 28.186 -11.293 16.790 1.00 20.04 ? 264 THR A CA 1 ATOM 1655 C C . THR A 1 229 ? 28.623 -12.754 16.584 1.00 20.47 ? 264 THR A C 1 ATOM 1656 O O . THR A 1 229 ? 29.316 -13.074 15.608 1.00 19.88 ? 264 THR A O 1 ATOM 1657 C CB . THR A 1 229 ? 29.145 -10.627 17.793 1.00 21.64 ? 264 THR A CB 1 ATOM 1658 O OG1 . THR A 1 229 ? 28.720 -9.281 18.048 1.00 24.74 ? 264 THR A OG1 1 ATOM 1659 C CG2 . THR A 1 229 ? 30.539 -10.592 17.224 1.00 23.73 ? 264 THR A CG2 1 ATOM 1660 N N . LYS A 1 230 ? 28.212 -13.641 17.478 1.00 18.05 ? 265 LYS A N 1 ATOM 1661 C CA . LYS A 1 230 ? 28.534 -15.056 17.357 1.00 20.15 ? 265 LYS A CA 1 ATOM 1662 C C . LYS A 1 230 ? 27.938 -15.673 16.093 1.00 20.49 ? 265 LYS A C 1 ATOM 1663 O O . LYS A 1 230 ? 28.471 -16.652 15.594 1.00 21.43 ? 265 LYS A O 1 ATOM 1664 C CB . LYS A 1 230 ? 28.041 -15.839 18.574 1.00 20.76 ? 265 LYS A CB 1 ATOM 1665 C CG . LYS A 1 230 ? 28.819 -15.575 19.863 1.00 21.65 ? 265 LYS A CG 1 ATOM 1666 C CD . LYS A 1 230 ? 28.227 -16.362 21.014 1.00 23.42 ? 265 LYS A CD 1 ATOM 1667 C CE . LYS A 1 230 ? 29.016 -16.223 22.318 1.00 24.63 ? 265 LYS A CE 1 ATOM 1668 N NZ . LYS A 1 230 ? 30.329 -16.900 22.253 1.00 25.52 ? 265 LYS A NZ 1 ATOM 1669 N N . GLN A 1 231 ? 26.863 -15.079 15.567 1.00 19.07 ? 266 GLN A N 1 ATOM 1670 C CA . GLN A 1 231 ? 26.200 -15.616 14.393 1.00 18.98 ? 266 GLN A CA 1 ATOM 1671 C C . GLN A 1 231 ? 26.470 -14.785 13.147 1.00 20.34 ? 266 GLN A C 1 ATOM 1672 O O . GLN A 1 231 ? 25.778 -14.945 12.146 1.00 20.42 ? 266 GLN A O 1 ATOM 1673 C CB . GLN A 1 231 ? 24.708 -15.765 14.662 1.00 18.64 ? 266 GLN A CB 1 ATOM 1674 C CG . GLN A 1 231 ? 24.468 -16.836 15.710 1.00 20.06 ? 266 GLN A CG 1 ATOM 1675 C CD . GLN A 1 231 ? 23.015 -17.048 16.079 1.00 19.16 ? 266 GLN A CD 1 ATOM 1676 O OE1 . GLN A 1 231 ? 22.142 -17.146 15.205 1.00 19.69 ? 266 GLN A OE1 1 ATOM 1677 N NE2 . GLN A 1 231 ? 22.751 -17.169 17.384 1.00 18.23 ? 266 GLN A NE2 1 ATOM 1678 N N . GLY A 1 232 ? 27.469 -13.908 13.217 1.00 20.11 ? 267 GLY A N 1 ATOM 1679 C CA . GLY A 1 232 ? 27.916 -13.144 12.049 1.00 21.18 ? 267 GLY A CA 1 ATOM 1680 C C . GLY A 1 232 ? 27.043 -11.959 11.700 1.00 21.63 ? 267 GLY A C 1 ATOM 1681 O O . GLY A 1 232 ? 27.035 -11.534 10.544 1.00 22.46 ? 267 GLY A O 1 ATOM 1682 N N . VAL A 1 233 ? 26.312 -11.423 12.678 1.00 20.48 ? 268 VAL A N 1 ATOM 1683 C CA . VAL A 1 233 ? 25.502 -10.223 12.500 1.00 19.32 ? 268 VAL A CA 1 ATOM 1684 C C . VAL A 1 233 ? 26.140 -9.114 13.332 1.00 21.27 ? 268 VAL A C 1 ATOM 1685 O O . VAL A 1 233 ? 26.231 -9.225 14.562 1.00 21.26 ? 268 VAL A O 1 ATOM 1686 C CB . VAL A 1 233 ? 24.047 -10.464 12.897 1.00 19.40 ? 268 VAL A CB 1 ATOM 1687 C CG1 . VAL A 1 233 ? 23.238 -9.174 12.866 1.00 20.21 ? 268 VAL A CG1 1 ATOM 1688 C CG2 . VAL A 1 233 ? 23.423 -11.492 11.978 1.00 20.39 ? 268 VAL A CG2 1 ATOM 1689 N N A ARG A 1 234 ? 26.545 -8.035 12.672 0.50 20.83 ? 269 ARG A N 1 ATOM 1690 N N B ARG A 1 234 ? 26.576 -8.044 12.672 0.50 19.85 ? 269 ARG A N 1 ATOM 1691 C CA A ARG A 1 234 ? 27.314 -6.981 13.330 0.50 21.95 ? 269 ARG A CA 1 ATOM 1692 C CA B ARG A 1 234 ? 27.322 -6.991 13.362 0.50 20.08 ? 269 ARG A CA 1 ATOM 1693 C C A ARG A 1 234 ? 26.413 -6.125 14.234 0.50 20.62 ? 269 ARG A C 1 ATOM 1694 C C B ARG A 1 234 ? 26.407 -6.140 14.243 0.50 19.58 ? 269 ARG A C 1 ATOM 1695 O O A ARG A 1 234 ? 25.322 -5.705 13.824 0.50 19.57 ? 269 ARG A O 1 ATOM 1696 O O B ARG A 1 234 ? 25.311 -5.737 13.829 0.50 18.63 ? 269 ARG A O 1 ATOM 1697 C CB A ARG A 1 234 ? 28.004 -6.135 12.262 0.50 24.38 ? 269 ARG A CB 1 ATOM 1698 C CB B ARG A 1 234 ? 28.072 -6.119 12.361 0.50 20.87 ? 269 ARG A CB 1 ATOM 1699 C CG A ARG A 1 234 ? 29.490 -5.944 12.472 0.50 28.24 ? 269 ARG A CG 1 ATOM 1700 C CG B ARG A 1 234 ? 28.967 -5.081 13.008 0.50 22.05 ? 269 ARG A CG 1 ATOM 1701 C CD A ARG A 1 234 ? 30.258 -6.045 11.159 0.50 30.62 ? 269 ARG A CD 1 ATOM 1702 C CD B ARG A 1 234 ? 29.806 -4.360 11.957 0.50 23.47 ? 269 ARG A CD 1 ATOM 1703 N NE A ARG A 1 234 ? 29.576 -5.384 10.049 0.50 32.19 ? 269 ARG A NE 1 ATOM 1704 N NE B ARG A 1 234 ? 30.508 -5.266 11.041 0.50 25.56 ? 269 ARG A NE 1 ATOM 1705 C CZ A ARG A 1 234 ? 29.230 -5.985 8.920 0.50 32.67 ? 269 ARG A CZ 1 ATOM 1706 C CZ B ARG A 1 234 ? 31.711 -5.805 11.247 0.50 27.19 ? 269 ARG A CZ 1 ATOM 1707 N NH1 A ARG A 1 234 ? 29.511 -7.264 8.732 0.50 35.28 ? 269 ARG A NH1 1 ATOM 1708 N NH1 B ARG A 1 234 ? 32.231 -6.601 10.327 0.50 28.48 ? 269 ARG A NH1 1 ATOM 1709 N NH2 A ARG A 1 234 ? 28.617 -5.304 7.973 0.50 32.68 ? 269 ARG A NH2 1 ATOM 1710 N NH2 B ARG A 1 234 ? 32.398 -5.550 12.349 0.50 27.63 ? 269 ARG A NH2 1 ATOM 1711 N N . ALA A 1 235 ? 26.854 -5.905 15.474 1.00 19.87 ? 270 ALA A N 1 ATOM 1712 C CA . ALA A 1 235 ? 26.111 -5.114 16.429 1.00 21.33 ? 270 ALA A CA 1 ATOM 1713 C C . ALA A 1 235 ? 26.836 -3.804 16.656 1.00 22.92 ? 270 ALA A C 1 ATOM 1714 O O . ALA A 1 235 ? 28.060 -3.772 16.774 1.00 24.46 ? 270 ALA A O 1 ATOM 1715 C CB . ALA A 1 235 ? 25.959 -5.876 17.751 1.00 21.79 ? 270 ALA A CB 1 ATOM 1716 N N . GLY A 1 236 ? 26.077 -2.718 16.718 1.00 23.07 ? 271 GLY A N 1 ATOM 1717 C CA . GLY A 1 236 ? 26.598 -1.441 17.165 1.00 25.69 ? 271 GLY A CA 1 ATOM 1718 C C . GLY A 1 236 ? 26.799 -1.531 18.660 1.00 26.53 ? 271 GLY A C 1 ATOM 1719 O O . GLY A 1 236 ? 26.336 -2.481 19.292 1.00 27.22 ? 271 GLY A O 1 ATOM 1720 N N . THR A 1 237 ? 27.529 -0.584 19.225 1.00 25.83 ? 272 THR A N 1 ATOM 1721 C CA . THR A 1 237 ? 27.705 -0.534 20.677 1.00 25.87 ? 272 THR A CA 1 ATOM 1722 C C . THR A 1 237 ? 26.416 -0.019 21.257 1.00 25.58 ? 272 THR A C 1 ATOM 1723 O O . THR A 1 237 ? 25.985 1.083 20.923 1.00 26.32 ? 272 THR A O 1 ATOM 1724 C CB . THR A 1 237 ? 28.868 0.385 21.042 1.00 28.14 ? 272 THR A CB 1 ATOM 1725 O OG1 . THR A 1 237 ? 30.041 -0.107 20.399 1.00 30.15 ? 272 THR A OG1 1 ATOM 1726 C CG2 . THR A 1 237 ? 29.109 0.405 22.550 1.00 30.63 ? 272 THR A CG2 1 ATOM 1727 N N . PHE A 1 238 ? 25.823 -0.806 22.147 1.00 25.65 ? 273 PHE A N 1 ATOM 1728 C CA . PHE A 1 238 ? 24.495 -0.560 22.690 1.00 25.95 ? 273 PHE A CA 1 ATOM 1729 C C . PHE A 1 238 ? 24.462 0.537 23.757 1.00 28.00 ? 273 PHE A C 1 ATOM 1730 O O . PHE A 1 238 ? 23.418 1.128 23.985 1.00 29.39 ? 273 PHE A O 1 ATOM 1731 C CB . PHE A 1 238 ? 23.928 -1.848 23.311 1.00 25.43 ? 273 PHE A CB 1 ATOM 1732 C CG . PHE A 1 238 ? 23.186 -2.741 22.345 1.00 23.99 ? 273 PHE A CG 1 ATOM 1733 C CD1 . PHE A 1 238 ? 23.593 -2.880 21.029 1.00 23.26 ? 273 PHE A CD1 1 ATOM 1734 C CD2 . PHE A 1 238 ? 22.069 -3.443 22.772 1.00 22.58 ? 273 PHE A CD2 1 ATOM 1735 C CE1 . PHE A 1 238 ? 22.906 -3.709 20.174 1.00 21.75 ? 273 PHE A CE1 1 ATOM 1736 C CE2 . PHE A 1 238 ? 21.380 -4.284 21.917 1.00 22.73 ? 273 PHE A CE2 1 ATOM 1737 C CZ . PHE A 1 238 ? 21.815 -4.417 20.618 1.00 21.14 ? 273 PHE A CZ 1 ATOM 1738 N N . PHE A 1 239 ? 25.600 0.792 24.401 1.00 28.79 ? 274 PHE A N 1 ATOM 1739 C CA . PHE A 1 239 ? 25.654 1.655 25.574 1.00 28.35 ? 274 PHE A CA 1 ATOM 1740 C C . PHE A 1 239 ? 26.359 2.957 25.313 1.00 26.59 ? 274 PHE A C 1 ATOM 1741 O O . PHE A 1 239 ? 27.235 3.023 24.462 1.00 24.75 ? 274 PHE A O 1 ATOM 1742 C CB . PHE A 1 239 ? 26.329 0.905 26.696 1.00 33.42 ? 274 PHE A CB 1 ATOM 1743 C CG . PHE A 1 239 ? 25.673 -0.399 26.965 1.00 35.04 ? 274 PHE A CG 1 ATOM 1744 C CD1 . PHE A 1 239 ? 24.513 -0.446 27.730 1.00 40.93 ? 274 PHE A CD1 1 ATOM 1745 C CD2 . PHE A 1 239 ? 26.159 -1.552 26.399 1.00 36.52 ? 274 PHE A CD2 1 ATOM 1746 C CE1 . PHE A 1 239 ? 23.870 -1.648 27.959 1.00 44.80 ? 274 PHE A CE1 1 ATOM 1747 C CE2 . PHE A 1 239 ? 25.527 -2.765 26.620 1.00 37.40 ? 274 PHE A CE2 1 ATOM 1748 C CZ . PHE A 1 239 ? 24.377 -2.809 27.395 1.00 40.17 ? 274 PHE A CZ 1 ATOM 1749 N N . TRP A 1 240 ? 25.934 3.982 26.056 1.00 22.71 ? 275 TRP A N 1 ATOM 1750 C CA . TRP A 1 240 ? 26.346 5.363 25.824 1.00 22.88 ? 275 TRP A CA 1 ATOM 1751 C C . TRP A 1 240 ? 26.735 5.989 27.148 1.00 21.80 ? 275 TRP A C 1 ATOM 1752 O O . TRP A 1 240 ? 25.937 6.004 28.077 1.00 22.18 ? 275 TRP A O 1 ATOM 1753 C CB . TRP A 1 240 ? 25.195 6.175 25.213 1.00 22.32 ? 275 TRP A CB 1 ATOM 1754 C CG . TRP A 1 240 ? 24.662 5.559 23.972 1.00 21.01 ? 275 TRP A CG 1 ATOM 1755 C CD1 . TRP A 1 240 ? 23.662 4.630 23.878 1.00 21.45 ? 275 TRP A CD1 1 ATOM 1756 C CD2 . TRP A 1 240 ? 25.106 5.808 22.647 1.00 20.82 ? 275 TRP A CD2 1 ATOM 1757 N NE1 . TRP A 1 240 ? 23.459 4.287 22.557 1.00 20.49 ? 275 TRP A NE1 1 ATOM 1758 C CE2 . TRP A 1 240 ? 24.322 5.009 21.783 1.00 20.27 ? 275 TRP A CE2 1 ATOM 1759 C CE3 . TRP A 1 240 ? 26.080 6.642 22.097 1.00 20.43 ? 275 TRP A CE3 1 ATOM 1760 C CZ2 . TRP A 1 240 ? 24.502 5.015 20.410 1.00 20.87 ? 275 TRP A CZ2 1 ATOM 1761 C CZ3 . TRP A 1 240 ? 26.243 6.660 20.756 1.00 20.98 ? 275 TRP A CZ3 1 ATOM 1762 C CH2 . TRP A 1 240 ? 25.478 5.838 19.915 1.00 21.09 ? 275 TRP A CH2 1 ATOM 1763 N N . SER A 1 241 ? 27.972 6.460 27.250 1.00 23.51 ? 276 SER A N 1 ATOM 1764 C CA . SER A 1 241 ? 28.373 7.268 28.392 1.00 23.70 ? 276 SER A CA 1 ATOM 1765 C C . SER A 1 241 ? 27.372 8.396 28.593 1.00 25.03 ? 276 SER A C 1 ATOM 1766 O O . SER A 1 241 ? 26.867 8.977 27.637 1.00 23.81 ? 276 SER A O 1 ATOM 1767 C CB . SER A 1 241 ? 29.776 7.825 28.184 1.00 25.61 ? 276 SER A CB 1 ATOM 1768 O OG . SER A 1 241 ? 30.705 6.767 28.318 1.00 27.16 ? 276 SER A OG 1 ATOM 1769 N N . VAL A 1 242 ? 27.089 8.698 29.857 1.00 26.50 ? 277 VAL A N 1 ATOM 1770 C CA . VAL A 1 242 ? 26.005 9.617 30.184 1.00 28.59 ? 277 VAL A CA 1 ATOM 1771 C C . VAL A 1 242 ? 26.244 11.040 29.685 1.00 27.82 ? 277 VAL A C 1 ATOM 1772 O O . VAL A 1 242 ? 25.289 11.747 29.432 1.00 28.87 ? 277 VAL A O 1 ATOM 1773 C CB . VAL A 1 242 ? 25.674 9.623 31.702 1.00 30.75 ? 277 VAL A CB 1 ATOM 1774 C CG1 . VAL A 1 242 ? 25.161 8.254 32.135 1.00 32.43 ? 277 VAL A CG1 1 ATOM 1775 C CG2 . VAL A 1 242 ? 26.874 10.064 32.548 1.00 30.66 ? 277 VAL A CG2 1 ATOM 1776 N N . SER A 1 243 ? 27.508 11.421 29.519 1.00 28.46 ? 278 SER A N 1 ATOM 1777 C CA . SER A 1 243 ? 27.890 12.718 28.934 1.00 29.40 ? 278 SER A CA 1 ATOM 1778 C C . SER A 1 243 ? 27.457 12.924 27.484 1.00 29.14 ? 278 SER A C 1 ATOM 1779 O O . SER A 1 243 ? 27.346 14.067 27.053 1.00 31.45 ? 278 SER A O 1 ATOM 1780 C CB . SER A 1 243 ? 29.416 12.891 28.968 1.00 32.04 ? 278 SER A CB 1 ATOM 1781 O OG . SER A 1 243 ? 29.884 13.010 30.287 1.00 38.72 ? 278 SER A OG 1 ATOM 1782 N N . ILE A 1 244 ? 27.226 11.843 26.732 1.00 25.39 ? 279 ILE A N 1 ATOM 1783 C CA . ILE A 1 244 ? 26.915 11.967 25.309 1.00 23.96 ? 279 ILE A CA 1 ATOM 1784 C C . ILE A 1 244 ? 25.461 12.455 25.196 1.00 24.17 ? 279 ILE A C 1 ATOM 1785 O O . ILE A 1 244 ? 24.549 11.768 25.653 1.00 23.21 ? 279 ILE A O 1 ATOM 1786 C CB . ILE A 1 244 ? 27.115 10.641 24.531 1.00 24.48 ? 279 ILE A CB 1 ATOM 1787 C CG1 . ILE A 1 244 ? 28.552 10.136 24.692 1.00 25.11 ? 279 ILE A CG1 1 ATOM 1788 C CG2 . ILE A 1 244 ? 26.794 10.820 23.040 1.00 23.46 ? 279 ILE A CG2 1 ATOM 1789 C CD1 . ILE A 1 244 ? 28.730 8.678 24.358 1.00 26.15 ? 279 ILE A CD1 1 ATOM 1790 N N . PRO A 1 245 ? 25.247 13.649 24.613 1.00 25.63 ? 280 PRO A N 1 ATOM 1791 C CA . PRO A 1 245 ? 23.877 14.156 24.476 1.00 26.17 ? 280 PRO A CA 1 ATOM 1792 C C . PRO A 1 245 ? 23.030 13.237 23.618 1.00 25.07 ? 280 PRO A C 1 ATOM 1793 O O . PRO A 1 245 ? 23.554 12.578 22.700 1.00 23.23 ? 280 PRO A O 1 ATOM 1794 C CB . PRO A 1 245 ? 24.051 15.516 23.774 1.00 27.40 ? 280 PRO A CB 1 ATOM 1795 C CG . PRO A 1 245 ? 25.490 15.828 23.815 1.00 28.01 ? 280 PRO A CG 1 ATOM 1796 C CD . PRO A 1 245 ? 26.228 14.541 23.973 1.00 26.70 ? 280 PRO A CD 1 ATOM 1797 N N . HIS A 1 246 ? 21.740 13.171 23.913 1.00 24.25 ? 281 HIS A N 1 ATOM 1798 C CA . HIS A 1 246 ? 20.831 12.346 23.107 1.00 25.52 ? 281 HIS A CA 1 ATOM 1799 C C . HIS A 1 246 ? 20.878 12.622 21.616 1.00 24.82 ? 281 HIS A C 1 ATOM 1800 O O . HIS A 1 246 ? 20.850 11.684 20.827 1.00 24.44 ? 281 HIS A O 1 ATOM 1801 C CB . HIS A 1 246 ? 19.413 12.463 23.612 1.00 26.68 ? 281 HIS A CB 1 ATOM 1802 C CG . HIS A 1 246 ? 19.251 11.963 24.998 1.00 29.64 ? 281 HIS A CG 1 ATOM 1803 N ND1 . HIS A 1 246 ? 18.222 12.372 25.811 1.00 37.33 ? 281 HIS A ND1 1 ATOM 1804 C CD2 . HIS A 1 246 ? 20.014 11.131 25.742 1.00 31.57 ? 281 HIS A CD2 1 ATOM 1805 C CE1 . HIS A 1 246 ? 18.333 11.780 26.986 1.00 35.99 ? 281 HIS A CE1 1 ATOM 1806 N NE2 . HIS A 1 246 ? 19.410 11.019 26.968 1.00 32.44 ? 281 HIS A NE2 1 ATOM 1807 N N . GLU A 1 247 ? 21.003 13.892 21.226 1.00 25.99 ? 282 GLU A N 1 ATOM 1808 C CA . GLU A 1 247 ? 21.069 14.258 19.819 1.00 25.78 ? 282 GLU A CA 1 ATOM 1809 C C . GLU A 1 247 ? 22.273 13.605 19.133 1.00 24.63 ? 282 GLU A C 1 ATOM 1810 O O . GLU A 1 247 ? 22.183 13.203 17.971 1.00 24.13 ? 282 GLU A O 1 ATOM 1811 C CB . GLU A 1 247 ? 21.136 15.778 19.638 1.00 27.61 ? 282 GLU A CB 1 ATOM 1812 C CG . GLU A 1 247 ? 19.888 16.530 20.130 1.00 29.03 ? 282 GLU A CG 1 ATOM 1813 C CD . GLU A 1 247 ? 19.940 16.933 21.608 1.00 30.63 ? 282 GLU A CD 1 ATOM 1814 O OE1 . GLU A 1 247 ? 20.667 16.311 22.415 1.00 27.33 ? 282 GLU A OE1 1 ATOM 1815 O OE2 . GLU A 1 247 ? 19.235 17.900 21.955 1.00 31.95 ? 282 GLU A OE2 1 ATOM 1816 N N . ARG A 1 248 ? 23.384 13.512 19.861 1.00 23.37 ? 283 ARG A N 1 ATOM 1817 C CA . ARG A 1 248 ? 24.636 12.913 19.354 1.00 23.74 ? 283 ARG A CA 1 ATOM 1818 C C . ARG A 1 248 ? 24.518 11.385 19.289 1.00 22.69 ? 283 ARG A C 1 ATOM 1819 O O . ARG A 1 248 ? 25.095 10.770 18.397 1.00 24.16 ? 283 ARG A O 1 ATOM 1820 C CB . ARG A 1 248 ? 25.825 13.356 20.229 1.00 24.83 ? 283 ARG A CB 1 ATOM 1821 C CG . ARG A 1 248 ? 27.179 12.719 19.955 1.00 25.47 ? 283 ARG A CG 1 ATOM 1822 C CD . ARG A 1 248 ? 27.687 13.076 18.586 1.00 27.54 ? 283 ARG A CD 1 ATOM 1823 N NE . ARG A 1 248 ? 27.889 14.514 18.410 1.00 30.27 ? 283 ARG A NE 1 ATOM 1824 C CZ . ARG A 1 248 ? 28.004 15.110 17.224 1.00 30.47 ? 283 ARG A CZ 1 ATOM 1825 N NH1 . ARG A 1 248 ? 27.931 14.398 16.106 1.00 32.10 ? 283 ARG A NH1 1 ATOM 1826 N NH2 . ARG A 1 248 ? 28.174 16.431 17.143 1.00 30.57 ? 283 ARG A NH2 1 ATOM 1827 N N . ARG A 1 249 ? 23.789 10.780 20.227 1.00 21.28 ? 284 ARG A N 1 ATOM 1828 C CA . ARG A 1 249 ? 23.509 9.329 20.173 1.00 20.56 ? 284 ARG A CA 1 ATOM 1829 C C . ARG A 1 249 ? 22.750 8.973 18.896 1.00 21.17 ? 284 ARG A C 1 ATOM 1830 O O . ARG A 1 249 ? 23.089 7.982 18.228 1.00 20.68 ? 284 ARG A O 1 ATOM 1831 C CB . ARG A 1 249 ? 22.728 8.832 21.382 1.00 20.40 ? 284 ARG A CB 1 ATOM 1832 C CG . ARG A 1 249 ? 23.453 9.056 22.709 1.00 21.03 ? 284 ARG A CG 1 ATOM 1833 C CD . ARG A 1 249 ? 22.638 8.621 23.906 1.00 21.84 ? 284 ARG A CD 1 ATOM 1834 N NE . ARG A 1 249 ? 23.174 9.300 25.080 1.00 22.65 ? 284 ARG A NE 1 ATOM 1835 C CZ . ARG A 1 249 ? 22.873 9.036 26.337 1.00 24.19 ? 284 ARG A CZ 1 ATOM 1836 N NH1 . ARG A 1 249 ? 22.012 8.083 26.646 1.00 24.76 ? 284 ARG A NH1 1 ATOM 1837 N NH2 . ARG A 1 249 ? 23.448 9.758 27.294 1.00 25.94 ? 284 ARG A NH2 1 ATOM 1838 N N . ILE A 1 250 ? 21.766 9.803 18.543 1.00 21.00 ? 285 ILE A N 1 ATOM 1839 C CA . ILE A 1 250 ? 20.983 9.611 17.318 1.00 21.41 ? 285 ILE A CA 1 ATOM 1840 C C . ILE A 1 250 ? 21.852 9.819 16.092 1.00 21.52 ? 285 ILE A C 1 ATOM 1841 O O . ILE A 1 250 ? 21.837 8.979 15.209 1.00 20.83 ? 285 ILE A O 1 ATOM 1842 C CB . ILE A 1 250 ? 19.718 10.502 17.258 1.00 21.42 ? 285 ILE A CB 1 ATOM 1843 C CG1 . ILE A 1 250 ? 18.761 10.155 18.407 1.00 21.38 ? 285 ILE A CG1 1 ATOM 1844 C CG2 . ILE A 1 250 ? 19.011 10.368 15.911 1.00 22.22 ? 285 ILE A CG2 1 ATOM 1845 C CD1 . ILE A 1 250 ? 18.243 8.735 18.441 1.00 21.02 ? 285 ILE A CD1 1 ATOM 1846 N N . LEU A 1 251 ? 22.599 10.919 16.046 1.00 21.92 ? 286 LEU A N 1 ATOM 1847 C CA . LEU A 1 251 ? 23.501 11.191 14.928 1.00 23.20 ? 286 LEU A CA 1 ATOM 1848 C C . LEU A 1 251 ? 24.568 10.108 14.747 1.00 22.81 ? 286 LEU A C 1 ATOM 1849 O O . LEU A 1 251 ? 24.926 9.795 13.621 1.00 22.31 ? 286 LEU A O 1 ATOM 1850 C CB . LEU A 1 251 ? 24.166 12.559 15.066 1.00 25.55 ? 286 LEU A CB 1 ATOM 1851 C CG . LEU A 1 251 ? 23.242 13.735 14.735 1.00 27.85 ? 286 LEU A CG 1 ATOM 1852 C CD1 . LEU A 1 251 ? 23.807 15.029 15.286 1.00 29.16 ? 286 LEU A CD1 1 ATOM 1853 C CD2 . LEU A 1 251 ? 23.013 13.835 13.235 1.00 30.46 ? 286 LEU A CD2 1 ATOM 1854 N N . THR A 1 252 ? 25.044 9.519 15.839 1.00 20.91 ? 287 THR A N 1 ATOM 1855 C CA . THR A 1 252 ? 26.013 8.427 15.775 1.00 21.62 ? 287 THR A CA 1 ATOM 1856 C C . THR A 1 252 ? 25.433 7.138 15.182 1.00 20.69 ? 287 THR A C 1 ATOM 1857 O O . THR A 1 252 ? 26.092 6.487 14.371 1.00 20.84 ? 287 THR A O 1 ATOM 1858 C CB . THR A 1 252 ? 26.602 8.145 17.165 1.00 20.95 ? 287 THR A CB 1 ATOM 1859 O OG1 . THR A 1 252 ? 27.293 9.331 17.603 1.00 22.24 ? 287 THR A OG1 1 ATOM 1860 C CG2 . THR A 1 252 ? 27.556 6.952 17.119 1.00 20.35 ? 287 THR A CG2 1 ATOM 1861 N N . ILE A 1 253 ? 24.215 6.781 15.576 1.00 20.41 ? 288 ILE A N 1 ATOM 1862 C CA . ILE A 1 253 ? 23.528 5.649 14.954 1.00 20.54 ? 288 ILE A CA 1 ATOM 1863 C C . ILE A 1 253 ? 23.365 5.880 13.447 1.00 21.16 ? 288 ILE A C 1 ATOM 1864 O O . ILE A 1 253 ? 23.650 4.979 12.643 1.00 20.67 ? 288 ILE A O 1 ATOM 1865 C CB . ILE A 1 253 ? 22.182 5.375 15.639 1.00 22.03 ? 288 ILE A CB 1 ATOM 1866 C CG1 . ILE A 1 253 ? 22.451 4.834 17.050 1.00 20.99 ? 288 ILE A CG1 1 ATOM 1867 C CG2 . ILE A 1 253 ? 21.340 4.385 14.826 1.00 23.33 ? 288 ILE A CG2 1 ATOM 1868 C CD1 . ILE A 1 253 ? 21.250 4.911 17.995 1.00 21.91 ? 288 ILE A CD1 1 ATOM 1869 N N . LEU A 1 254 ? 22.950 7.088 13.071 1.00 21.56 ? 289 LEU A N 1 ATOM 1870 C CA . LEU A 1 254 ? 22.782 7.427 11.652 1.00 21.24 ? 289 LEU A CA 1 ATOM 1871 C C . LEU A 1 254 ? 24.101 7.394 10.895 1.00 22.11 ? 289 LEU A C 1 ATOM 1872 O O . LEU A 1 254 ? 24.129 6.988 9.742 1.00 21.61 ? 289 LEU A O 1 ATOM 1873 C CB . LEU A 1 254 ? 22.092 8.773 11.475 1.00 21.93 ? 289 LEU A CB 1 ATOM 1874 C CG . LEU A 1 254 ? 20.667 8.819 12.061 1.00 21.06 ? 289 LEU A CG 1 ATOM 1875 C CD1 . LEU A 1 254 ? 20.163 10.242 12.169 1.00 21.11 ? 289 LEU A CD1 1 ATOM 1876 C CD2 . LEU A 1 254 ? 19.709 7.979 11.230 1.00 22.63 ? 289 LEU A CD2 1 ATOM 1877 N N . GLN A 1 255 ? 25.176 7.830 11.546 1.00 21.80 ? 290 GLN A N 1 ATOM 1878 C CA . GLN A 1 255 ? 26.510 7.765 10.943 1.00 24.11 ? 290 GLN A CA 1 ATOM 1879 C C . GLN A 1 255 ? 26.936 6.308 10.702 1.00 20.22 ? 290 GLN A C 1 ATOM 1880 O O . GLN A 1 255 ? 27.434 5.966 9.617 1.00 19.63 ? 290 GLN A O 1 ATOM 1881 C CB . GLN A 1 255 ? 27.512 8.474 11.849 1.00 28.01 ? 290 GLN A CB 1 ATOM 1882 C CG . GLN A 1 255 ? 28.874 8.704 11.235 1.00 36.37 ? 290 GLN A CG 1 ATOM 1883 C CD . GLN A 1 255 ? 29.704 9.625 12.104 1.00 42.07 ? 290 GLN A CD 1 ATOM 1884 O OE1 . GLN A 1 255 ? 30.593 9.172 12.830 1.00 47.67 ? 290 GLN A OE1 1 ATOM 1885 N NE2 . GLN A 1 255 ? 29.369 10.914 12.090 1.00 41.78 ? 290 GLN A NE2 1 ATOM 1886 N N . TRP A 1 256 ? 26.701 5.442 11.687 1.00 18.90 ? 291 TRP A N 1 ATOM 1887 C CA . TRP A 1 256 ? 27.031 4.033 11.532 1.00 18.45 ? 291 TRP A CA 1 ATOM 1888 C C . TRP A 1 256 ? 26.189 3.383 10.413 1.00 18.83 ? 291 TRP A C 1 ATOM 1889 O O . TRP A 1 256 ? 26.694 2.529 9.674 1.00 18.00 ? 291 TRP A O 1 ATOM 1890 C CB . TRP A 1 256 ? 26.824 3.284 12.828 1.00 18.02 ? 291 TRP A CB 1 ATOM 1891 C CG . TRP A 1 256 ? 27.759 3.636 13.949 1.00 18.51 ? 291 TRP A CG 1 ATOM 1892 C CD1 . TRP A 1 256 ? 28.984 4.220 13.874 1.00 19.58 ? 291 TRP A CD1 1 ATOM 1893 C CD2 . TRP A 1 256 ? 27.520 3.379 15.339 1.00 18.99 ? 291 TRP A CD2 1 ATOM 1894 N NE1 . TRP A 1 256 ? 29.526 4.364 15.154 1.00 20.09 ? 291 TRP A NE1 1 ATOM 1895 C CE2 . TRP A 1 256 ? 28.644 3.844 16.059 1.00 19.49 ? 291 TRP A CE2 1 ATOM 1896 C CE3 . TRP A 1 256 ? 26.466 2.788 16.040 1.00 20.01 ? 291 TRP A CE3 1 ATOM 1897 C CZ2 . TRP A 1 256 ? 28.743 3.726 17.448 1.00 20.03 ? 291 TRP A CZ2 1 ATOM 1898 C CZ3 . TRP A 1 256 ? 26.565 2.683 17.431 1.00 20.58 ? 291 TRP A CZ3 1 ATOM 1899 C CH2 . TRP A 1 256 ? 27.699 3.162 18.105 1.00 19.76 ? 291 TRP A CH2 1 ATOM 1900 N N . LEU A 1 257 ? 24.928 3.797 10.293 1.00 18.62 ? 292 LEU A N 1 ATOM 1901 C CA . LEU A 1 257 ? 24.042 3.304 9.219 1.00 18.89 ? 292 LEU A CA 1 ATOM 1902 C C . LEU A 1 257 ? 24.487 3.731 7.832 1.00 19.67 ? 292 LEU A C 1 ATOM 1903 O O . LEU A 1 257 ? 24.036 3.135 6.847 1.00 19.37 ? 292 LEU A O 1 ATOM 1904 C CB . LEU A 1 257 ? 22.586 3.704 9.450 1.00 20.25 ? 292 LEU A CB 1 ATOM 1905 C CG . LEU A 1 257 ? 21.850 2.854 10.487 1.00 20.14 ? 292 LEU A CG 1 ATOM 1906 C CD1 . LEU A 1 257 ? 20.592 3.551 11.014 1.00 21.66 ? 292 LEU A CD1 1 ATOM 1907 C CD2 . LEU A 1 257 ? 21.493 1.515 9.866 1.00 20.55 ? 292 LEU A CD2 1 ATOM 1908 N N . SER A 1 258 ? 25.373 4.730 7.766 1.00 18.99 ? 293 SER A N 1 ATOM 1909 C CA . SER A 1 258 ? 25.971 5.207 6.519 1.00 21.35 ? 293 SER A CA 1 ATOM 1910 C C . SER A 1 258 ? 27.292 4.546 6.161 1.00 21.72 ? 293 SER A C 1 ATOM 1911 O O . SER A 1 258 ? 27.873 4.854 5.105 1.00 22.27 ? 293 SER A O 1 ATOM 1912 C CB . SER A 1 258 ? 26.168 6.729 6.605 1.00 21.76 ? 293 SER A CB 1 ATOM 1913 O OG . SER A 1 258 ? 24.930 7.321 6.983 1.00 23.50 ? 293 SER A OG 1 ATOM 1914 N N . LEU A 1 259 ? 27.793 3.667 7.026 1.00 21.80 ? 294 LEU A N 1 ATOM 1915 C CA . LEU A 1 259 ? 29.075 2.978 6.794 1.00 22.67 ? 294 LEU A CA 1 ATOM 1916 C C . LEU A 1 259 ? 28.999 2.021 5.628 1.00 23.54 ? 294 LEU A C 1 ATOM 1917 O O . LEU A 1 259 ? 27.907 1.566 5.262 1.00 22.26 ? 294 LEU A O 1 ATOM 1918 C CB . LEU A 1 259 ? 29.486 2.189 8.043 1.00 22.53 ? 294 LEU A CB 1 ATOM 1919 C CG . LEU A 1 259 ? 30.003 3.065 9.175 1.00 22.40 ? 294 LEU A CG 1 ATOM 1920 C CD1 . LEU A 1 259 ? 30.051 2.209 10.433 1.00 21.51 ? 294 LEU A CD1 1 ATOM 1921 C CD2 . LEU A 1 259 ? 31.366 3.622 8.798 1.00 24.16 ? 294 LEU A CD2 1 ATOM 1922 N N . PRO A 1 260 ? 30.166 1.695 5.038 1.00 23.45 ? 295 PRO A N 1 ATOM 1923 C CA . PRO A 1 260 ? 30.138 0.670 4.014 1.00 24.43 ? 295 PRO A CA 1 ATOM 1924 C C . PRO A 1 260 ? 29.568 -0.660 4.491 1.00 24.17 ? 295 PRO A C 1 ATOM 1925 O O . PRO A 1 260 ? 29.550 -0.957 5.694 1.00 23.09 ? 295 PRO A O 1 ATOM 1926 C CB . PRO A 1 260 ? 31.609 0.512 3.598 1.00 25.18 ? 295 PRO A CB 1 ATOM 1927 C CG . PRO A 1 260 ? 32.413 1.441 4.421 1.00 26.59 ? 295 PRO A CG 1 ATOM 1928 C CD . PRO A 1 260 ? 31.532 2.103 5.427 1.00 24.36 ? 295 PRO A CD 1 ATOM 1929 N N . ASP A 1 261 ? 29.152 -1.472 3.525 1.00 25.81 ? 296 ASP A N 1 ATOM 1930 C CA . ASP A 1 261 ? 28.395 -2.704 3.789 1.00 27.33 ? 296 ASP A CA 1 ATOM 1931 C C . ASP A 1 261 ? 29.112 -3.656 4.770 1.00 27.03 ? 296 ASP A C 1 ATOM 1932 O O . ASP A 1 261 ? 28.469 -4.247 5.641 1.00 28.88 ? 296 ASP A O 1 ATOM 1933 C CB . ASP A 1 261 ? 28.092 -3.441 2.469 1.00 30.21 ? 296 ASP A CB 1 ATOM 1934 C CG . ASP A 1 261 ? 27.296 -2.582 1.459 1.00 32.10 ? 296 ASP A CG 1 ATOM 1935 O OD1 . ASP A 1 261 ? 26.475 -1.734 1.866 1.00 31.01 ? 296 ASP A OD1 1 ATOM 1936 O OD2 . ASP A 1 261 ? 27.499 -2.756 0.232 1.00 35.66 ? 296 ASP A OD2 1 ATOM 1937 N N . ASN A 1 262 ? 30.437 -3.761 4.670 1.00 29.12 ? 297 ASN A N 1 ATOM 1938 C CA . ASN A 1 262 ? 31.167 -4.699 5.528 1.00 30.13 ? 297 ASN A CA 1 ATOM 1939 C C . ASN A 1 262 ? 31.532 -4.169 6.910 1.00 29.67 ? 297 ASN A C 1 ATOM 1940 O O . ASN A 1 262 ? 32.059 -4.931 7.725 1.00 29.88 ? 297 ASN A O 1 ATOM 1941 C CB . ASN A 1 262 ? 32.378 -5.326 4.802 1.00 35.27 ? 297 ASN A CB 1 ATOM 1942 C CG . ASN A 1 262 ? 33.485 -4.341 4.476 1.00 38.87 ? 297 ASN A CG 1 ATOM 1943 O OD1 . ASN A 1 262 ? 33.477 -3.189 4.894 1.00 41.17 ? 297 ASN A OD1 1 ATOM 1944 N ND2 . ASN A 1 262 ? 34.453 -4.804 3.688 1.00 46.61 ? 297 ASN A ND2 1 ATOM 1945 N N . GLU A 1 263 ? 31.263 -2.876 7.157 1.00 25.90 ? 298 GLU A N 1 ATOM 1946 C CA . GLU A 1 263 ? 31.461 -2.234 8.463 1.00 25.07 ? 298 GLU A CA 1 ATOM 1947 C C . GLU A 1 263 ? 30.155 -1.913 9.184 1.00 22.81 ? 298 GLU A C 1 ATOM 1948 O O . GLU A 1 263 ? 30.179 -1.705 10.391 1.00 21.27 ? 298 GLU A O 1 ATOM 1949 C CB . GLU A 1 263 ? 32.212 -0.915 8.324 1.00 27.40 ? 298 GLU A CB 1 ATOM 1950 C CG . GLU A 1 263 ? 33.678 -1.062 7.989 1.00 32.74 ? 298 GLU A CG 1 ATOM 1951 C CD . GLU A 1 263 ? 34.342 0.276 7.797 1.00 36.24 ? 298 GLU A CD 1 ATOM 1952 O OE1 . GLU A 1 263 ? 34.286 1.125 8.712 1.00 44.73 ? 298 GLU A OE1 1 ATOM 1953 O OE2 . GLU A 1 263 ? 34.924 0.481 6.726 1.00 43.01 ? 298 GLU A OE2 1 ATOM 1954 N N . ARG A 1 264 ? 29.040 -1.833 8.451 1.00 21.56 ? 299 ARG A N 1 ATOM 1955 C CA . ARG A 1 264 ? 27.778 -1.314 8.989 1.00 21.31 ? 299 ARG A CA 1 ATOM 1956 C C . ARG A 1 264 ? 27.102 -2.355 9.883 1.00 20.85 ? 299 ARG A C 1 ATOM 1957 O O . ARG A 1 264 ? 26.884 -3.488 9.460 1.00 20.65 ? 299 ARG A O 1 ATOM 1958 C CB . ARG A 1 264 ? 26.844 -0.938 7.828 1.00 21.56 ? 299 ARG A CB 1 ATOM 1959 C CG . ARG A 1 264 ? 25.509 -0.339 8.239 1.00 20.83 ? 299 ARG A CG 1 ATOM 1960 C CD . ARG A 1 264 ? 24.643 -0.028 7.036 1.00 21.83 ? 299 ARG A CD 1 ATOM 1961 N NE . ARG A 1 264 ? 24.407 -1.233 6.252 1.00 23.14 ? 299 ARG A NE 1 ATOM 1962 C CZ . ARG A 1 264 ? 24.822 -1.466 4.996 1.00 25.35 ? 299 ARG A CZ 1 ATOM 1963 N NH1 . ARG A 1 264 ? 25.520 -0.581 4.278 1.00 25.79 ? 299 ARG A NH1 1 ATOM 1964 N NH2 . ARG A 1 264 ? 24.525 -2.631 4.443 1.00 26.64 ? 299 ARG A NH2 1 ATOM 1965 N N . PRO A 1 265 ? 26.745 -1.978 11.126 1.00 19.69 ? 300 PRO A N 1 ATOM 1966 C CA . PRO A 1 265 ? 25.963 -2.906 11.940 1.00 18.74 ? 300 PRO A CA 1 ATOM 1967 C C . PRO A 1 265 ? 24.540 -3.147 11.470 1.00 18.41 ? 300 PRO A C 1 ATOM 1968 O O . PRO A 1 265 ? 23.993 -2.358 10.721 1.00 18.04 ? 300 PRO A O 1 ATOM 1969 C CB . PRO A 1 265 ? 25.947 -2.253 13.308 1.00 18.28 ? 300 PRO A CB 1 ATOM 1970 C CG . PRO A 1 265 ? 27.115 -1.340 13.324 1.00 18.88 ? 300 PRO A CG 1 ATOM 1971 C CD . PRO A 1 265 ? 27.249 -0.843 11.916 1.00 19.64 ? 300 PRO A CD 1 ATOM 1972 N N . SER A 1 266 ? 23.977 -4.271 11.882 1.00 17.54 ? 301 SER A N 1 ATOM 1973 C CA . SER A 1 266 ? 22.549 -4.570 11.625 1.00 18.15 ? 301 SER A CA 1 ATOM 1974 C C . SER A 1 266 ? 21.677 -4.358 12.852 1.00 17.61 ? 301 SER A C 1 ATOM 1975 O O . SER A 1 266 ? 20.479 -4.336 12.702 1.00 16.90 ? 301 SER A O 1 ATOM 1976 C CB . SER A 1 266 ? 22.359 -6.009 11.158 1.00 19.07 ? 301 SER A CB 1 ATOM 1977 O OG . SER A 1 266 ? 22.789 -6.182 9.813 1.00 20.19 ? 301 SER A OG 1 ATOM 1978 N N . VAL A 1 267 ? 22.269 -4.202 14.034 1.00 16.71 ? 302 VAL A N 1 ATOM 1979 C CA . VAL A 1 267 ? 21.479 -3.994 15.256 1.00 17.08 ? 302 VAL A CA 1 ATOM 1980 C C . VAL A 1 267 ? 22.090 -2.864 16.062 1.00 16.70 ? 302 VAL A C 1 ATOM 1981 O O . VAL A 1 267 ? 23.319 -2.786 16.205 1.00 16.32 ? 302 VAL A O 1 ATOM 1982 C CB . VAL A 1 267 ? 21.263 -5.287 16.092 1.00 17.72 ? 302 VAL A CB 1 ATOM 1983 C CG1 . VAL A 1 267 ? 22.565 -5.897 16.573 1.00 18.12 ? 302 VAL A CG1 1 ATOM 1984 C CG2 . VAL A 1 267 ? 20.321 -5.006 17.259 1.00 17.05 ? 302 VAL A CG2 1 ATOM 1985 N N . TYR A 1 268 ? 21.205 -1.992 16.553 1.00 15.87 ? 303 TYR A N 1 ATOM 1986 C CA . TYR A 1 268 ? 21.559 -0.799 17.270 1.00 17.19 ? 303 TYR A CA 1 ATOM 1987 C C . TYR A 1 268 ? 20.662 -0.624 18.487 1.00 16.76 ? 303 TYR A C 1 ATOM 1988 O O . TYR A 1 268 ? 19.510 -1.086 18.495 1.00 17.29 ? 303 TYR A O 1 ATOM 1989 C CB . TYR A 1 268 ? 21.363 0.449 16.398 1.00 17.11 ? 303 TYR A CB 1 ATOM 1990 C CG . TYR A 1 268 ? 22.094 0.390 15.083 1.00 17.48 ? 303 TYR A CG 1 ATOM 1991 C CD1 . TYR A 1 268 ? 21.564 -0.312 14.010 1.00 17.58 ? 303 TYR A CD1 1 ATOM 1992 C CD2 . TYR A 1 268 ? 23.290 1.066 14.909 1.00 18.47 ? 303 TYR A CD2 1 ATOM 1993 C CE1 . TYR A 1 268 ? 22.237 -0.364 12.790 1.00 18.53 ? 303 TYR A CE1 1 ATOM 1994 C CE2 . TYR A 1 268 ? 23.976 1.018 13.695 1.00 17.87 ? 303 TYR A CE2 1 ATOM 1995 C CZ . TYR A 1 268 ? 23.440 0.311 12.643 1.00 18.41 ? 303 TYR A CZ 1 ATOM 1996 O OH . TYR A 1 268 ? 24.114 0.260 11.432 1.00 19.00 ? 303 TYR A OH 1 ATOM 1997 N N . ALA A 1 269 ? 21.182 0.103 19.473 1.00 16.73 ? 304 ALA A N 1 ATOM 1998 C CA . ALA A 1 269 ? 20.356 0.583 20.560 1.00 16.43 ? 304 ALA A CA 1 ATOM 1999 C C . ALA A 1 269 ? 20.638 2.040 20.934 1.00 17.36 ? 304 ALA A C 1 ATOM 2000 O O . ALA A 1 269 ? 21.782 2.483 20.989 1.00 17.32 ? 304 ALA A O 1 ATOM 2001 C CB . ALA A 1 269 ? 20.537 -0.287 21.769 1.00 17.83 ? 304 ALA A CB 1 ATOM 2002 N N . PHE A 1 270 ? 19.557 2.757 21.198 1.00 17.82 ? 305 PHE A N 1 ATOM 2003 C CA . PHE A 1 270 ? 19.566 4.079 21.788 1.00 17.77 ? 305 PHE A CA 1 ATOM 2004 C C . PHE A 1 270 ? 19.000 3.930 23.199 1.00 17.54 ? 305 PHE A C 1 ATOM 2005 O O . PHE A 1 270 ? 18.051 3.174 23.425 1.00 17.19 ? 305 PHE A O 1 ATOM 2006 C CB . PHE A 1 270 ? 18.697 5.050 20.981 1.00 18.26 ? 305 PHE A CB 1 ATOM 2007 C CG . PHE A 1 270 ? 18.447 6.354 21.684 1.00 18.53 ? 305 PHE A CG 1 ATOM 2008 C CD1 . PHE A 1 270 ? 17.356 6.482 22.547 1.00 18.07 ? 305 PHE A CD1 1 ATOM 2009 C CD2 . PHE A 1 270 ? 19.284 7.438 21.515 1.00 18.68 ? 305 PHE A CD2 1 ATOM 2010 C CE1 . PHE A 1 270 ? 17.117 7.657 23.230 1.00 18.29 ? 305 PHE A CE1 1 ATOM 2011 C CE2 . PHE A 1 270 ? 19.049 8.636 22.200 1.00 19.03 ? 305 PHE A CE2 1 ATOM 2012 C CZ . PHE A 1 270 ? 17.963 8.735 23.066 1.00 18.78 ? 305 PHE A CZ 1 ATOM 2013 N N . TYR A 1 271 ? 19.599 4.638 24.146 1.00 17.38 ? 306 TYR A N 1 ATOM 2014 C CA . TYR A 1 271 ? 19.064 4.678 25.503 1.00 18.52 ? 306 TYR A CA 1 ATOM 2015 C C . TYR A 1 271 ? 18.883 6.123 25.957 1.00 18.91 ? 306 TYR A C 1 ATOM 2016 O O . TYR A 1 271 ? 19.754 6.959 25.711 1.00 19.91 ? 306 TYR A O 1 ATOM 2017 C CB . TYR A 1 271 ? 19.983 3.921 26.456 1.00 20.04 ? 306 TYR A CB 1 ATOM 2018 C CG . TYR A 1 271 ? 19.660 4.145 27.906 1.00 22.19 ? 306 TYR A CG 1 ATOM 2019 C CD1 . TYR A 1 271 ? 18.581 3.494 28.537 1.00 23.61 ? 306 TYR A CD1 1 ATOM 2020 C CD2 . TYR A 1 271 ? 20.435 5.006 28.659 1.00 24.92 ? 306 TYR A CD2 1 ATOM 2021 C CE1 . TYR A 1 271 ? 18.312 3.711 29.895 1.00 22.98 ? 306 TYR A CE1 1 ATOM 2022 C CE2 . TYR A 1 271 ? 20.161 5.240 29.990 1.00 24.40 ? 306 TYR A CE2 1 ATOM 2023 C CZ . TYR A 1 271 ? 19.122 4.597 30.607 1.00 24.12 ? 306 TYR A CZ 1 ATOM 2024 O OH . TYR A 1 271 ? 18.932 4.896 31.926 1.00 25.94 ? 306 TYR A OH 1 ATOM 2025 N N . SER A 1 272 ? 17.756 6.400 26.624 1.00 17.95 ? 307 SER A N 1 ATOM 2026 C CA . SER A 1 272 ? 17.505 7.705 27.259 1.00 18.83 ? 307 SER A CA 1 ATOM 2027 C C . SER A 1 272 ? 17.286 7.468 28.735 1.00 19.41 ? 307 SER A C 1 ATOM 2028 O O . SER A 1 272 ? 16.479 6.603 29.103 1.00 18.49 ? 307 SER A O 1 ATOM 2029 C CB . SER A 1 272 ? 16.244 8.395 26.711 1.00 20.94 ? 307 SER A CB 1 ATOM 2030 O OG . SER A 1 272 ? 15.964 9.603 27.415 1.00 22.71 ? 307 SER A OG 1 ATOM 2031 N N . GLU A 1 273 ? 17.916 8.327 29.534 1.00 19.15 ? 308 GLU A N 1 ATOM 2032 C CA A GLU A 1 273 ? 17.777 8.363 30.980 0.50 20.24 ? 308 GLU A CA 1 ATOM 2033 C CA B GLU A 1 273 ? 17.734 8.305 30.991 0.50 20.44 ? 308 GLU A CA 1 ATOM 2034 C C . GLU A 1 273 ? 16.406 8.936 31.392 1.00 20.75 ? 308 GLU A C 1 ATOM 2035 O O . GLU A 1 273 ? 16.037 8.862 32.554 1.00 21.65 ? 308 GLU A O 1 ATOM 2036 C CB A GLU A 1 273 ? 18.907 9.226 31.589 0.50 20.78 ? 308 GLU A CB 1 ATOM 2037 C CB B GLU A 1 273 ? 18.893 8.991 31.748 0.50 21.27 ? 308 GLU A CB 1 ATOM 2038 C CG A GLU A 1 273 ? 20.343 8.723 31.359 0.50 21.03 ? 308 GLU A CG 1 ATOM 2039 C CG B GLU A 1 273 ? 18.843 10.515 31.842 0.50 22.47 ? 308 GLU A CG 1 ATOM 2040 C CD A GLU A 1 273 ? 20.970 9.139 30.025 0.50 20.80 ? 308 GLU A CD 1 ATOM 2041 C CD B GLU A 1 273 ? 18.959 11.171 30.490 0.50 22.83 ? 308 GLU A CD 1 ATOM 2042 O OE1 A GLU A 1 273 ? 20.301 9.833 29.232 0.50 20.36 ? 308 GLU A OE1 1 ATOM 2043 O OE1 B GLU A 1 273 ? 19.485 10.501 29.586 0.50 22.02 ? 308 GLU A OE1 1 ATOM 2044 O OE2 A GLU A 1 273 ? 22.130 8.755 29.758 0.50 20.32 ? 308 GLU A OE2 1 ATOM 2045 O OE2 B GLU A 1 273 ? 18.529 12.335 30.326 0.50 25.11 ? 308 GLU A OE2 1 ATOM 2046 N N . GLN A 1 274 ? 15.694 9.562 30.440 1.00 19.98 ? 309 GLN A N 1 ATOM 2047 C CA . GLN A 1 274 ? 14.362 10.164 30.671 1.00 19.79 ? 309 GLN A CA 1 ATOM 2048 C C . GLN A 1 274 ? 13.298 9.211 30.130 1.00 19.30 ? 309 GLN A C 1 ATOM 2049 O O . GLN A 1 274 ? 13.588 8.455 29.211 1.00 19.19 ? 309 GLN A O 1 ATOM 2050 C CB . GLN A 1 274 ? 14.259 11.582 30.045 1.00 21.34 ? 309 GLN A CB 1 ATOM 2051 C CG . GLN A 1 274 ? 15.028 12.667 30.799 1.00 23.01 ? 309 GLN A CG 1 ATOM 2052 C CD . GLN A 1 274 ? 14.317 13.176 32.065 1.00 23.67 ? 309 GLN A CD 1 ATOM 2053 O OE1 . GLN A 1 274 ? 13.676 12.422 32.791 1.00 23.87 ? 309 GLN A OE1 1 ATOM 2054 N NE2 . GLN A 1 274 ? 14.456 14.461 32.336 1.00 25.09 ? 309 GLN A NE2 1 ATOM 2055 N N . PRO A 1 275 ? 12.071 9.208 30.681 1.00 17.52 ? 310 PRO A N 1 ATOM 2056 C CA . PRO A 1 275 ? 11.572 10.174 31.640 1.00 19.40 ? 310 PRO A CA 1 ATOM 2057 C C . PRO A 1 275 ? 11.778 9.774 33.107 1.00 19.16 ? 310 PRO A C 1 ATOM 2058 O O . PRO A 1 275 ? 11.124 10.351 33.979 1.00 19.64 ? 310 PRO A O 1 ATOM 2059 C CB . PRO A 1 275 ? 10.072 10.202 31.315 1.00 19.04 ? 310 PRO A CB 1 ATOM 2060 C CG . PRO A 1 275 ? 9.789 8.814 30.915 1.00 18.30 ? 310 PRO A CG 1 ATOM 2061 C CD . PRO A 1 275 ? 10.961 8.465 30.064 1.00 18.26 ? 310 PRO A CD 1 ATOM 2062 N N . ASP A 1 276 ? 12.666 8.814 33.377 1.00 19.01 ? 311 ASP A N 1 ATOM 2063 C CA . ASP A 1 276 ? 12.886 8.322 34.756 1.00 17.54 ? 311 ASP A CA 1 ATOM 2064 C C . ASP A 1 276 ? 13.265 9.454 35.706 1.00 18.62 ? 311 ASP A C 1 ATOM 2065 O O . ASP A 1 276 ? 12.702 9.585 36.775 1.00 18.51 ? 311 ASP A O 1 ATOM 2066 C CB . ASP A 1 276 ? 13.991 7.248 34.771 1.00 17.87 ? 311 ASP A CB 1 ATOM 2067 C CG . ASP A 1 276 ? 14.038 6.458 36.063 1.00 17.73 ? 311 ASP A CG 1 ATOM 2068 O OD1 . ASP A 1 276 ? 13.020 5.864 36.421 1.00 18.89 ? 311 ASP A OD1 1 ATOM 2069 O OD2 . ASP A 1 276 ? 15.085 6.473 36.730 1.00 19.19 ? 311 ASP A OD2 1 ATOM 2070 N N . PHE A 1 277 ? 14.200 10.304 35.305 1.00 20.92 ? 312 PHE A N 1 ATOM 2071 C CA . PHE A 1 277 ? 14.697 11.324 36.220 1.00 24.16 ? 312 PHE A CA 1 ATOM 2072 C C . PHE A 1 277 ? 13.626 12.332 36.616 1.00 23.36 ? 312 PHE A C 1 ATOM 2073 O O . PHE A 1 277 ? 13.447 12.621 37.802 1.00 22.63 ? 312 PHE A O 1 ATOM 2074 C CB . PHE A 1 277 ? 15.910 12.068 35.672 1.00 27.96 ? 312 PHE A CB 1 ATOM 2075 C CG . PHE A 1 277 ? 16.405 13.108 36.635 1.00 33.81 ? 312 PHE A CG 1 ATOM 2076 C CD1 . PHE A 1 277 ? 16.762 12.733 37.938 1.00 37.12 ? 312 PHE A CD1 1 ATOM 2077 C CD2 . PHE A 1 277 ? 16.410 14.452 36.303 1.00 37.98 ? 312 PHE A CD2 1 ATOM 2078 C CE1 . PHE A 1 277 ? 17.166 13.680 38.865 1.00 41.02 ? 312 PHE A CE1 1 ATOM 2079 C CE2 . PHE A 1 277 ? 16.826 15.399 37.224 1.00 40.47 ? 312 PHE A CE2 1 ATOM 2080 C CZ . PHE A 1 277 ? 17.199 15.016 38.506 1.00 40.77 ? 312 PHE A CZ 1 ATOM 2081 N N . SER A 1 278 ? 12.879 12.827 35.632 1.00 21.95 ? 313 SER A N 1 ATOM 2082 C CA . SER A 1 278 ? 11.765 13.718 35.917 1.00 22.74 ? 313 SER A CA 1 ATOM 2083 C C . SER A 1 278 ? 10.685 13.031 36.754 1.00 21.25 ? 313 SER A C 1 ATOM 2084 O O . SER A 1 278 ? 10.108 13.651 37.640 1.00 22.77 ? 313 SER A O 1 ATOM 2085 C CB . SER A 1 278 ? 11.168 14.299 34.636 1.00 24.37 ? 313 SER A CB 1 ATOM 2086 O OG . SER A 1 278 ? 12.096 15.198 34.081 1.00 26.69 ? 313 SER A OG 1 ATOM 2087 N N . GLY A 1 279 ? 10.420 11.754 36.486 1.00 19.67 ? 314 GLY A N 1 ATOM 2088 C CA . GLY A 1 279 ? 9.492 10.985 37.345 1.00 19.77 ? 314 GLY A CA 1 ATOM 2089 C C . GLY A 1 279 ? 9.950 10.953 38.795 1.00 19.51 ? 314 GLY A C 1 ATOM 2090 O O . GLY A 1 279 ? 9.138 11.138 39.686 1.00 20.32 ? 314 GLY A O 1 ATOM 2091 N N . HIS A 1 280 ? 11.245 10.736 39.042 1.00 19.30 ? 315 HIS A N 1 ATOM 2092 C CA . HIS A 1 280 ? 11.764 10.725 40.425 1.00 19.08 ? 315 HIS A CA 1 ATOM 2093 C C . HIS A 1 280 ? 11.611 12.077 41.091 1.00 21.04 ? 315 HIS A C 1 ATOM 2094 O O . HIS A 1 280 ? 11.268 12.172 42.277 1.00 20.65 ? 315 HIS A O 1 ATOM 2095 C CB . HIS A 1 280 ? 13.238 10.365 40.482 1.00 19.44 ? 315 HIS A CB 1 ATOM 2096 C CG . HIS A 1 280 ? 13.513 8.920 40.274 1.00 19.14 ? 315 HIS A CG 1 ATOM 2097 N ND1 . HIS A 1 280 ? 13.129 7.964 41.190 1.00 19.39 ? 315 HIS A ND1 1 ATOM 2098 C CD2 . HIS A 1 280 ? 14.141 8.258 39.274 1.00 18.43 ? 315 HIS A CD2 1 ATOM 2099 C CE1 . HIS A 1 280 ? 13.509 6.772 40.757 1.00 19.23 ? 315 HIS A CE1 1 ATOM 2100 N NE2 . HIS A 1 280 ? 14.107 6.918 39.586 1.00 18.31 ? 315 HIS A NE2 1 ATOM 2101 N N . LYS A 1 281 ? 11.862 13.128 40.328 1.00 21.43 ? 316 LYS A N 1 ATOM 2102 C CA . LYS A 1 281 ? 11.846 14.466 40.889 1.00 24.91 ? 316 LYS A CA 1 ATOM 2103 C C . LYS A 1 281 ? 10.429 14.987 41.155 1.00 25.53 ? 316 LYS A C 1 ATOM 2104 O O . LYS A 1 281 ? 10.162 15.539 42.226 1.00 27.06 ? 316 LYS A O 1 ATOM 2105 C CB . LYS A 1 281 ? 12.625 15.431 39.993 1.00 27.13 ? 316 LYS A CB 1 ATOM 2106 C CG . LYS A 1 281 ? 12.843 16.790 40.655 1.00 30.89 ? 316 LYS A CG 1 ATOM 2107 C CD . LYS A 1 281 ? 13.829 17.650 39.880 1.00 35.19 ? 316 LYS A CD 1 ATOM 2108 C CE . LYS A 1 281 ? 14.244 18.869 40.693 1.00 38.70 ? 316 LYS A CE 1 ATOM 2109 N NZ . LYS A 1 281 ? 15.439 19.508 40.080 1.00 42.49 ? 316 LYS A NZ 1 ATOM 2110 N N . TYR A 1 282 ? 9.536 14.801 40.194 1.00 25.75 ? 317 TYR A N 1 ATOM 2111 C CA . TYR A 1 282 ? 8.196 15.393 40.239 1.00 27.86 ? 317 TYR A CA 1 ATOM 2112 C C . TYR A 1 282 ? 7.068 14.402 40.461 1.00 27.12 ? 317 TYR A C 1 ATOM 2113 O O . TYR A 1 282 ? 5.932 14.809 40.678 1.00 27.20 ? 317 TYR A O 1 ATOM 2114 C CB . TYR A 1 282 ? 7.953 16.193 38.952 1.00 31.37 ? 317 TYR A CB 1 ATOM 2115 C CG . TYR A 1 282 ? 8.969 17.293 38.798 1.00 33.61 ? 317 TYR A CG 1 ATOM 2116 C CD1 . TYR A 1 282 ? 9.060 18.312 39.759 1.00 38.43 ? 317 TYR A CD1 1 ATOM 2117 C CD2 . TYR A 1 282 ? 9.869 17.313 37.735 1.00 35.33 ? 317 TYR A CD2 1 ATOM 2118 C CE1 . TYR A 1 282 ? 10.005 19.334 39.653 1.00 39.76 ? 317 TYR A CE1 1 ATOM 2119 C CE2 . TYR A 1 282 ? 10.814 18.336 37.621 1.00 36.97 ? 317 TYR A CE2 1 ATOM 2120 C CZ . TYR A 1 282 ? 10.869 19.338 38.592 1.00 39.51 ? 317 TYR A CZ 1 ATOM 2121 O OH . TYR A 1 282 ? 11.786 20.356 38.521 1.00 45.64 ? 317 TYR A OH 1 ATOM 2122 N N . GLY A 1 283 ? 7.366 13.108 40.465 1.00 25.30 ? 318 GLY A N 1 ATOM 2123 C CA . GLY A 1 283 ? 6.323 12.087 40.485 1.00 24.72 ? 318 GLY A CA 1 ATOM 2124 C C . GLY A 1 283 ? 5.702 11.905 39.113 1.00 25.54 ? 318 GLY A C 1 ATOM 2125 O O . GLY A 1 283 ? 5.775 12.817 38.264 1.00 27.16 ? 318 GLY A O 1 ATOM 2126 N N . PRO A 1 284 ? 5.072 10.744 38.878 1.00 24.00 ? 319 PRO A N 1 ATOM 2127 C CA . PRO A 1 284 ? 4.525 10.415 37.555 1.00 25.11 ? 319 PRO A CA 1 ATOM 2128 C C . PRO A 1 284 ? 3.365 11.286 37.037 1.00 28.70 ? 319 PRO A C 1 ATOM 2129 O O . PRO A 1 284 ? 3.166 11.347 35.829 1.00 29.70 ? 319 PRO A O 1 ATOM 2130 C CB . PRO A 1 284 ? 4.025 8.986 37.742 1.00 23.54 ? 319 PRO A CB 1 ATOM 2131 C CG . PRO A 1 284 ? 3.734 8.863 39.199 1.00 23.12 ? 319 PRO A CG 1 ATOM 2132 C CD . PRO A 1 284 ? 4.820 9.658 39.853 1.00 22.84 ? 319 PRO A CD 1 ATOM 2133 N N . PHE A 1 285 ? 2.590 11.890 37.927 1.00 30.61 ? 320 PHE A N 1 ATOM 2134 C CA . PHE A 1 285 ? 1.412 12.666 37.541 1.00 36.83 ? 320 PHE A CA 1 ATOM 2135 C C . PHE A 1 285 ? 1.645 14.181 37.574 1.00 36.46 ? 320 PHE A C 1 ATOM 2136 O O . PHE A 1 285 ? 0.695 14.953 37.400 1.00 39.69 ? 320 PHE A O 1 ATOM 2137 C CB . PHE A 1 285 ? 0.236 12.312 38.454 1.00 42.31 ? 320 PHE A CB 1 ATOM 2138 C CG . PHE A 1 285 ? -0.089 10.853 38.472 1.00 49.39 ? 320 PHE A CG 1 ATOM 2139 C CD1 . PHE A 1 285 ? -0.425 10.191 37.295 1.00 52.06 ? 320 PHE A CD1 1 ATOM 2140 C CD2 . PHE A 1 285 ? -0.063 10.135 39.658 1.00 55.53 ? 320 PHE A CD2 1 ATOM 2141 C CE1 . PHE A 1 285 ? -0.724 8.839 37.302 1.00 54.74 ? 320 PHE A CE1 1 ATOM 2142 C CE2 . PHE A 1 285 ? -0.362 8.780 39.673 1.00 57.82 ? 320 PHE A CE2 1 ATOM 2143 C CZ . PHE A 1 285 ? -0.697 8.135 38.493 1.00 57.64 ? 320 PHE A CZ 1 ATOM 2144 N N . GLY A 1 286 ? 2.886 14.615 37.779 1.00 34.57 ? 321 GLY A N 1 ATOM 2145 C CA . GLY A 1 286 ? 3.183 16.035 37.813 1.00 38.78 ? 321 GLY A CA 1 ATOM 2146 C C . GLY A 1 286 ? 2.948 16.656 36.442 1.00 36.77 ? 321 GLY A C 1 ATOM 2147 O O . GLY A 1 286 ? 3.197 15.997 35.429 1.00 35.21 ? 321 GLY A O 1 ATOM 2148 N N . PRO A 1 287 ? 2.476 17.924 36.397 1.00 36.76 ? 322 PRO A N 1 ATOM 2149 C CA . PRO A 1 287 ? 2.436 18.637 35.110 1.00 35.96 ? 322 PRO A CA 1 ATOM 2150 C C . PRO A 1 287 ? 3.833 18.851 34.528 1.00 34.05 ? 322 PRO A C 1 ATOM 2151 O O . PRO A 1 287 ? 3.964 19.045 33.325 1.00 33.13 ? 322 PRO A O 1 ATOM 2152 C CB . PRO A 1 287 ? 1.800 19.981 35.472 1.00 37.36 ? 322 PRO A CB 1 ATOM 2153 C CG . PRO A 1 287 ? 2.167 20.183 36.895 1.00 37.99 ? 322 PRO A CG 1 ATOM 2154 C CD . PRO A 1 287 ? 2.083 18.812 37.508 1.00 38.02 ? 322 PRO A CD 1 ATOM 2155 N N . GLU A 1 288 ? 4.857 18.797 35.380 1.00 33.71 ? 323 GLU A N 1 ATOM 2156 C CA . GLU A 1 288 ? 6.265 18.839 34.937 1.00 35.45 ? 323 GLU A CA 1 ATOM 2157 C C . GLU A 1 288 ? 6.684 17.670 34.051 1.00 30.91 ? 323 GLU A C 1 ATOM 2158 O O . GLU A 1 288 ? 7.740 17.748 33.463 1.00 32.19 ? 323 GLU A O 1 ATOM 2159 C CB . GLU A 1 288 ? 7.240 18.847 36.123 1.00 36.64 ? 323 GLU A CB 1 ATOM 2160 C CG . GLU A 1 288 ? 7.037 19.983 37.104 1.00 40.76 ? 323 GLU A CG 1 ATOM 2161 C CD . GLU A 1 288 ? 6.071 19.665 38.230 1.00 39.77 ? 323 GLU A CD 1 ATOM 2162 O OE1 . GLU A 1 288 ? 5.319 18.669 38.154 1.00 35.76 ? 323 GLU A OE1 1 ATOM 2163 O OE2 . GLU A 1 288 ? 6.052 20.451 39.197 1.00 46.68 ? 323 GLU A OE2 1 ATOM 2164 N N . MET A 1 289 ? 5.924 16.577 34.010 1.00 27.75 ? 324 MET A N 1 ATOM 2165 C CA . MET A 1 289 ? 6.250 15.442 33.131 1.00 27.25 ? 324 MET A CA 1 ATOM 2166 C C . MET A 1 289 ? 6.070 15.756 31.647 1.00 27.42 ? 324 MET A C 1 ATOM 2167 O O . MET A 1 289 ? 6.644 15.070 30.811 1.00 25.90 ? 324 MET A O 1 ATOM 2168 C CB . MET A 1 289 ? 5.425 14.204 33.480 1.00 27.13 ? 324 MET A CB 1 ATOM 2169 C CG . MET A 1 289 ? 5.768 13.590 34.832 1.00 27.45 ? 324 MET A CG 1 ATOM 2170 S SD . MET A 1 289 ? 7.530 13.208 35.029 1.00 28.33 ? 324 MET A SD 1 ATOM 2171 C CE . MET A 1 289 ? 7.742 12.105 33.657 1.00 26.77 ? 324 MET A CE 1 ATOM 2172 N N . THR A 1 290 ? 5.289 16.787 31.324 1.00 27.81 ? 325 THR A N 1 ATOM 2173 C CA . THR A 1 290 ? 4.971 17.100 29.935 1.00 28.56 ? 325 THR A CA 1 ATOM 2174 C C . THR A 1 290 ? 6.217 17.438 29.132 1.00 27.76 ? 325 THR A C 1 ATOM 2175 O O . THR A 1 290 ? 6.423 16.889 28.050 1.00 25.94 ? 325 THR A O 1 ATOM 2176 C CB . THR A 1 290 ? 3.965 18.257 29.867 1.00 31.17 ? 325 THR A CB 1 ATOM 2177 O OG1 . THR A 1 290 ? 2.783 17.852 30.561 1.00 34.48 ? 325 THR A OG1 1 ATOM 2178 C CG2 . THR A 1 290 ? 3.620 18.625 28.418 1.00 31.92 ? 325 THR A CG2 1 ATOM 2179 N N . ASN A 1 291 ? 7.057 18.311 29.673 1.00 29.29 ? 326 ASN A N 1 ATOM 2180 C CA . ASN A 1 291 ? 8.253 18.749 28.947 1.00 32.18 ? 326 ASN A CA 1 ATOM 2181 C C . ASN A 1 291 ? 9.258 17.603 28.654 1.00 29.61 ? 326 ASN A C 1 ATOM 2182 O O . ASN A 1 291 ? 9.715 17.488 27.518 1.00 27.25 ? 326 ASN A O 1 ATOM 2183 C CB . ASN A 1 291 ? 8.919 19.953 29.626 1.00 37.57 ? 326 ASN A CB 1 ATOM 2184 C CG . ASN A 1 291 ? 8.117 21.251 29.451 1.00 43.37 ? 326 ASN A CG 1 ATOM 2185 O OD1 . ASN A 1 291 ? 7.363 21.428 28.481 1.00 46.73 ? 326 ASN A OD1 1 ATOM 2186 N ND2 . ASN A 1 291 ? 8.290 22.172 30.389 1.00 48.49 ? 326 ASN A ND2 1 ATOM 2187 N N . PRO A 1 292 ? 9.570 16.737 29.647 1.00 27.45 ? 327 PRO A N 1 ATOM 2188 C CA . PRO A 1 292 ? 10.455 15.592 29.334 1.00 25.92 ? 327 PRO A CA 1 ATOM 2189 C C . PRO A 1 292 ? 9.882 14.666 28.258 1.00 23.22 ? 327 PRO A C 1 ATOM 2190 O O . PRO A 1 292 ? 10.620 14.174 27.400 1.00 22.15 ? 327 PRO A O 1 ATOM 2191 C CB . PRO A 1 292 ? 10.631 14.864 30.683 1.00 27.75 ? 327 PRO A CB 1 ATOM 2192 C CG . PRO A 1 292 ? 9.915 15.677 31.707 1.00 30.46 ? 327 PRO A CG 1 ATOM 2193 C CD . PRO A 1 292 ? 9.422 16.945 31.094 1.00 28.87 ? 327 PRO A CD 1 ATOM 2194 N N . LEU A 1 293 ? 8.572 14.465 28.270 1.00 21.63 ? 328 LEU A N 1 ATOM 2195 C CA . LEU A 1 293 ? 7.927 13.636 27.252 1.00 21.94 ? 328 LEU A CA 1 ATOM 2196 C C . LEU A 1 293 ? 7.978 14.289 25.871 1.00 22.94 ? 328 LEU A C 1 ATOM 2197 O O . LEU A 1 293 ? 8.205 13.603 24.876 1.00 21.91 ? 328 LEU A O 1 ATOM 2198 C CB . LEU A 1 293 ? 6.494 13.314 27.639 1.00 22.24 ? 328 LEU A CB 1 ATOM 2199 C CG . LEU A 1 293 ? 6.384 12.385 28.859 1.00 22.27 ? 328 LEU A CG 1 ATOM 2200 C CD1 . LEU A 1 293 ? 4.926 12.314 29.275 1.00 24.28 ? 328 LEU A CD1 1 ATOM 2201 C CD2 . LEU A 1 293 ? 6.967 10.989 28.621 1.00 21.44 ? 328 LEU A CD2 1 ATOM 2202 N N . ARG A 1 294 ? 7.778 15.606 25.806 1.00 22.86 ? 329 ARG A N 1 ATOM 2203 C CA . ARG A 1 294 ? 8.005 16.340 24.547 1.00 24.08 ? 329 ARG A CA 1 ATOM 2204 C C . ARG A 1 294 ? 9.435 16.188 24.028 1.00 23.90 ? 329 ARG A C 1 ATOM 2205 O O . ARG A 1 294 ? 9.658 16.044 22.815 1.00 22.78 ? 329 ARG A O 1 ATOM 2206 C CB . ARG A 1 294 ? 7.723 17.830 24.720 1.00 25.87 ? 329 ARG A CB 1 ATOM 2207 C CG . ARG A 1 294 ? 6.263 18.190 24.906 1.00 28.63 ? 329 ARG A CG 1 ATOM 2208 C CD . ARG A 1 294 ? 6.071 19.683 24.669 1.00 33.29 ? 329 ARG A CD 1 ATOM 2209 N NE . ARG A 1 294 ? 4.714 20.085 25.009 1.00 37.09 ? 329 ARG A NE 1 ATOM 2210 C CZ . ARG A 1 294 ? 3.630 19.857 24.261 1.00 42.12 ? 329 ARG A CZ 1 ATOM 2211 N NH1 . ARG A 1 294 ? 3.710 19.214 23.097 1.00 43.10 ? 329 ARG A NH1 1 ATOM 2212 N NH2 . ARG A 1 294 ? 2.435 20.278 24.686 1.00 44.83 ? 329 ARG A NH2 1 ATOM 2213 N N . GLU A 1 295 ? 10.407 16.236 24.935 1.00 23.92 ? 330 GLU A N 1 ATOM 2214 C CA . GLU A 1 295 ? 11.814 16.141 24.548 1.00 25.09 ? 330 GLU A CA 1 ATOM 2215 C C . GLU A 1 295 ? 12.150 14.754 23.992 1.00 22.84 ? 330 GLU A C 1 ATOM 2216 O O . GLU A 1 295 ? 12.869 14.637 23.001 1.00 21.78 ? 330 GLU A O 1 ATOM 2217 C CB . GLU A 1 295 ? 12.745 16.471 25.721 1.00 27.60 ? 330 GLU A CB 1 ATOM 2218 C CG . GLU A 1 295 ? 12.760 17.936 26.130 1.00 32.15 ? 330 GLU A CG 1 ATOM 2219 C CD . GLU A 1 295 ? 13.361 18.881 25.081 1.00 36.69 ? 330 GLU A CD 1 ATOM 2220 O OE1 . GLU A 1 295 ? 14.039 18.427 24.141 1.00 37.79 ? 330 GLU A OE1 1 ATOM 2221 O OE2 . GLU A 1 295 ? 13.136 20.101 25.196 1.00 46.08 ? 330 GLU A OE2 1 ATOM 2222 N N . ILE A 1 296 ? 11.619 13.702 24.607 1.00 21.21 ? 331 ILE A N 1 ATOM 2223 C CA . ILE A 1 296 ? 11.825 12.360 24.081 1.00 20.48 ? 331 ILE A CA 1 ATOM 2224 C C . ILE A 1 296 ? 11.199 12.236 22.695 1.00 20.41 ? 331 ILE A C 1 ATOM 2225 O O . ILE A 1 296 ? 11.819 11.675 21.766 1.00 20.05 ? 331 ILE A O 1 ATOM 2226 C CB . ILE A 1 296 ? 11.271 11.274 25.007 1.00 21.13 ? 331 ILE A CB 1 ATOM 2227 C CG1 . ILE A 1 296 ? 12.044 11.268 26.319 1.00 22.30 ? 331 ILE A CG1 1 ATOM 2228 C CG2 . ILE A 1 296 ? 11.381 9.897 24.369 1.00 21.66 ? 331 ILE A CG2 1 ATOM 2229 C CD1 . ILE A 1 296 ? 11.244 10.663 27.427 1.00 23.48 ? 331 ILE A CD1 1 ATOM 2230 N N . ASP A 1 297 ? 9.996 12.762 22.538 1.00 20.18 ? 332 ASP A N 1 ATOM 2231 C CA . ASP A 1 297 ? 9.337 12.690 21.234 1.00 20.73 ? 332 ASP A CA 1 ATOM 2232 C C . ASP A 1 297 ? 10.152 13.430 20.178 1.00 20.79 ? 332 ASP A C 1 ATOM 2233 O O . ASP A 1 297 ? 10.242 12.983 19.027 1.00 19.37 ? 332 ASP A O 1 ATOM 2234 C CB . ASP A 1 297 ? 7.935 13.285 21.261 1.00 21.17 ? 332 ASP A CB 1 ATOM 2235 C CG . ASP A 1 297 ? 7.150 12.899 20.044 1.00 22.36 ? 332 ASP A CG 1 ATOM 2236 O OD1 . ASP A 1 297 ? 6.699 11.740 20.029 1.00 22.45 ? 332 ASP A OD1 1 ATOM 2237 O OD2 . ASP A 1 297 ? 7.013 13.719 19.093 1.00 22.97 ? 332 ASP A OD2 1 ATOM 2238 N N . LYS A 1 298 ? 10.729 14.561 20.564 1.00 22.03 ? 333 LYS A N 1 ATOM 2239 C CA . LYS A 1 298 ? 11.622 15.303 19.653 1.00 23.58 ? 333 LYS A CA 1 ATOM 2240 C C . LYS A 1 298 ? 12.804 14.426 19.191 1.00 22.57 ? 333 LYS A C 1 ATOM 2241 O O . LYS A 1 298 ? 13.152 14.411 18.008 1.00 21.40 ? 333 LYS A O 1 ATOM 2242 C CB . LYS A 1 298 ? 12.107 16.604 20.312 1.00 26.43 ? 333 LYS A CB 1 ATOM 2243 C CG . LYS A 1 298 ? 12.908 17.554 19.432 1.00 31.77 ? 333 LYS A CG 1 ATOM 2244 C CD . LYS A 1 298 ? 13.206 18.851 20.190 1.00 34.83 ? 333 LYS A CD 1 ATOM 2245 C CE . LYS A 1 298 ? 14.322 19.669 19.560 1.00 38.98 ? 333 LYS A CE 1 ATOM 2246 N NZ . LYS A 1 298 ? 13.835 20.634 18.543 1.00 41.32 ? 333 LYS A NZ 1 ATOM 2247 N N . THR A 1 299 ? 13.381 13.655 20.107 1.00 22.52 ? 334 THR A N 1 ATOM 2248 C CA . THR A 1 299 ? 14.476 12.737 19.764 1.00 21.85 ? 334 THR A CA 1 ATOM 2249 C C . THR A 1 299 ? 14.001 11.619 18.838 1.00 20.71 ? 334 THR A C 1 ATOM 2250 O O . THR A 1 299 ? 14.705 11.259 17.889 1.00 19.47 ? 334 THR A O 1 ATOM 2251 C CB . THR A 1 299 ? 15.107 12.146 21.037 1.00 22.66 ? 334 THR A CB 1 ATOM 2252 O OG1 . THR A 1 299 ? 15.512 13.226 21.879 1.00 24.11 ? 334 THR A OG1 1 ATOM 2253 C CG2 . THR A 1 299 ? 16.340 11.274 20.706 1.00 21.69 ? 334 THR A CG2 1 ATOM 2254 N N . VAL A 1 300 ? 12.815 11.072 19.100 1.00 19.45 ? 335 VAL A N 1 ATOM 2255 C CA . VAL A 1 300 ? 12.217 10.065 18.182 1.00 19.70 ? 335 VAL A CA 1 ATOM 2256 C C . VAL A 1 300 ? 12.037 10.658 16.778 1.00 21.09 ? 335 VAL A C 1 ATOM 2257 O O . VAL A 1 300 ? 12.367 10.003 15.773 1.00 21.15 ? 335 VAL A O 1 ATOM 2258 C CB . VAL A 1 300 ? 10.876 9.493 18.713 1.00 20.73 ? 335 VAL A CB 1 ATOM 2259 C CG1 . VAL A 1 300 ? 10.235 8.559 17.689 1.00 20.92 ? 335 VAL A CG1 1 ATOM 2260 C CG2 . VAL A 1 300 ? 11.104 8.732 20.010 1.00 20.27 ? 335 VAL A CG2 1 ATOM 2261 N N . GLY A 1 301 ? 11.520 11.891 16.712 1.00 20.81 ? 336 GLY A N 1 ATOM 2262 C CA . GLY A 1 301 ? 11.394 12.636 15.447 1.00 21.32 ? 336 GLY A CA 1 ATOM 2263 C C . GLY A 1 301 ? 12.721 12.800 14.728 1.00 21.90 ? 336 GLY A C 1 ATOM 2264 O O . GLY A 1 301 ? 12.790 12.608 13.507 1.00 21.86 ? 336 GLY A O 1 ATOM 2265 N N . GLN A 1 302 ? 13.780 13.119 15.474 1.00 21.82 ? 337 GLN A N 1 ATOM 2266 C CA . GLN A 1 302 ? 15.121 13.234 14.862 1.00 23.00 ? 337 GLN A CA 1 ATOM 2267 C C . GLN A 1 302 ? 15.561 11.903 14.249 1.00 22.20 ? 337 GLN A C 1 ATOM 2268 O O . GLN A 1 302 ? 16.065 11.881 13.121 1.00 22.41 ? 337 GLN A O 1 ATOM 2269 C CB . GLN A 1 302 ? 16.168 13.728 15.869 1.00 24.13 ? 337 GLN A CB 1 ATOM 2270 C CG . GLN A 1 302 ? 16.067 15.204 16.191 1.00 25.76 ? 337 GLN A CG 1 ATOM 2271 C CD . GLN A 1 302 ? 16.937 15.626 17.371 1.00 28.36 ? 337 GLN A CD 1 ATOM 2272 O OE1 . GLN A 1 302 ? 17.692 14.829 17.951 1.00 27.14 ? 337 GLN A OE1 1 ATOM 2273 N NE2 . GLN A 1 302 ? 16.828 16.893 17.738 1.00 31.93 ? 337 GLN A NE2 1 ATOM 2274 N N . LEU A 1 303 ? 15.338 10.808 14.962 1.00 20.31 ? 338 LEU A N 1 ATOM 2275 C CA . LEU A 1 303 ? 15.680 9.493 14.440 1.00 19.74 ? 338 LEU A CA 1 ATOM 2276 C C . LEU A 1 303 ? 14.880 9.186 13.193 1.00 19.86 ? 338 LEU A C 1 ATOM 2277 O O . LEU A 1 303 ? 15.441 8.729 12.193 1.00 20.05 ? 338 LEU A O 1 ATOM 2278 C CB . LEU A 1 303 ? 15.396 8.400 15.453 1.00 18.98 ? 338 LEU A CB 1 ATOM 2279 C CG . LEU A 1 303 ? 15.676 6.960 14.992 1.00 18.73 ? 338 LEU A CG 1 ATOM 2280 C CD1 . LEU A 1 303 ? 17.136 6.815 14.626 1.00 18.30 ? 338 LEU A CD1 1 ATOM 2281 C CD2 . LEU A 1 303 ? 15.268 5.916 16.042 1.00 19.02 ? 338 LEU A CD2 1 ATOM 2282 N N . MET A 1 304 ? 13.567 9.396 13.243 1.00 19.55 ? 339 MET A N 1 ATOM 2283 C CA . MET A 1 304 ? 12.743 9.041 12.081 1.00 19.74 ? 339 MET A CA 1 ATOM 2284 C C . MET A 1 304 ? 13.024 9.919 10.845 1.00 20.14 ? 339 MET A C 1 ATOM 2285 O O . MET A 1 304 ? 13.083 9.399 9.719 1.00 20.32 ? 339 MET A O 1 ATOM 2286 C CB . MET A 1 304 ? 11.249 9.043 12.416 1.00 20.42 ? 339 MET A CB 1 ATOM 2287 C CG . MET A 1 304 ? 10.826 7.990 13.458 1.00 19.74 ? 339 MET A CG 1 ATOM 2288 S SD . MET A 1 304 ? 11.533 6.337 13.257 1.00 20.27 ? 339 MET A SD 1 ATOM 2289 C CE . MET A 1 304 ? 10.643 5.798 11.808 1.00 21.28 ? 339 MET A CE 1 ATOM 2290 N N . ASP A 1 305 ? 13.189 11.227 11.053 1.00 21.28 ? 340 ASP A N 1 ATOM 2291 C CA . ASP A 1 305 ? 13.619 12.153 9.977 1.00 22.61 ? 340 ASP A CA 1 ATOM 2292 C C . ASP A 1 305 ? 14.993 11.754 9.466 1.00 22.48 ? 340 ASP A C 1 ATOM 2293 O O . ASP A 1 305 ? 15.230 11.755 8.261 1.00 21.98 ? 340 ASP A O 1 ATOM 2294 C CB . ASP A 1 305 ? 13.725 13.608 10.471 1.00 23.19 ? 340 ASP A CB 1 ATOM 2295 C CG . ASP A 1 305 ? 12.377 14.244 10.824 1.00 25.82 ? 340 ASP A CG 1 ATOM 2296 O OD1 . ASP A 1 305 ? 11.304 13.674 10.558 1.00 28.64 ? 340 ASP A OD1 1 ATOM 2297 O OD2 . ASP A 1 305 ? 12.396 15.357 11.398 1.00 28.64 ? 340 ASP A OD2 1 ATOM 2298 N N . GLY A 1 306 ? 15.904 11.416 10.372 1.00 21.90 ? 341 GLY A N 1 ATOM 2299 C CA . GLY A 1 306 ? 17.231 10.930 9.963 1.00 21.94 ? 341 GLY A CA 1 ATOM 2300 C C . GLY A 1 306 ? 17.209 9.640 9.142 1.00 21.74 ? 341 GLY A C 1 ATOM 2301 O O . GLY A 1 306 ? 17.940 9.503 8.151 1.00 23.11 ? 341 GLY A O 1 ATOM 2302 N N . LEU A 1 307 ? 16.368 8.691 9.535 1.00 20.44 ? 342 LEU A N 1 ATOM 2303 C CA . LEU A 1 307 ? 16.192 7.478 8.743 1.00 21.19 ? 342 LEU A CA 1 ATOM 2304 C C . LEU A 1 307 ? 15.604 7.786 7.374 1.00 22.77 ? 342 LEU A C 1 ATOM 2305 O O . LEU A 1 307 ? 16.038 7.217 6.379 1.00 23.63 ? 342 LEU A O 1 ATOM 2306 C CB . LEU A 1 307 ? 15.299 6.477 9.468 1.00 21.04 ? 342 LEU A CB 1 ATOM 2307 C CG . LEU A 1 307 ? 15.917 5.867 10.729 1.00 20.90 ? 342 LEU A CG 1 ATOM 2308 C CD1 . LEU A 1 307 ? 14.857 5.095 11.504 1.00 21.36 ? 342 LEU A CD1 1 ATOM 2309 C CD2 . LEU A 1 307 ? 17.099 4.965 10.432 1.00 21.62 ? 342 LEU A CD2 1 ATOM 2310 N N . LYS A 1 308 ? 14.614 8.675 7.335 1.00 22.77 ? 343 LYS A N 1 ATOM 2311 C CA . LYS A 1 308 ? 13.978 9.050 6.083 1.00 23.45 ? 343 LYS A CA 1 ATOM 2312 C C . LYS A 1 308 ? 14.978 9.690 5.123 1.00 25.26 ? 343 LYS A C 1 ATOM 2313 O O . LYS A 1 308 ? 14.975 9.351 3.932 1.00 24.69 ? 343 LYS A O 1 ATOM 2314 C CB . LYS A 1 308 ? 12.781 9.967 6.341 1.00 24.60 ? 343 LYS A CB 1 ATOM 2315 C CG . LYS A 1 308 ? 11.909 10.191 5.129 1.00 26.71 ? 343 LYS A CG 1 ATOM 2316 C CD . LYS A 1 308 ? 10.729 11.093 5.457 1.00 28.48 ? 343 LYS A CD 1 ATOM 2317 C CE . LYS A 1 308 ? 10.084 11.597 4.176 1.00 30.97 ? 343 LYS A CE 1 ATOM 2318 N NZ . LYS A 1 308 ? 9.272 12.797 4.451 1.00 32.23 ? 343 LYS A NZ 1 ATOM 2319 N N . GLN A 1 309 ? 15.847 10.574 5.628 1.00 24.82 ? 344 GLN A N 1 ATOM 2320 C CA . GLN A 1 309 ? 16.949 11.135 4.844 1.00 27.85 ? 344 GLN A CA 1 ATOM 2321 C C . GLN A 1 309 ? 17.860 10.093 4.233 1.00 26.36 ? 344 GLN A C 1 ATOM 2322 O O . GLN A 1 309 ? 18.343 10.301 3.125 1.00 28.03 ? 344 GLN A O 1 ATOM 2323 C CB . GLN A 1 309 ? 17.878 12.028 5.676 1.00 30.44 ? 344 GLN A CB 1 ATOM 2324 C CG . GLN A 1 309 ? 17.260 13.282 6.196 1.00 35.64 ? 344 GLN A CG 1 ATOM 2325 C CD . GLN A 1 309 ? 18.285 14.347 6.556 1.00 36.65 ? 344 GLN A CD 1 ATOM 2326 O OE1 . GLN A 1 309 ? 18.089 15.491 6.203 1.00 41.55 ? 344 GLN A OE1 1 ATOM 2327 N NE2 . GLN A 1 309 ? 19.360 13.978 7.278 1.00 35.43 ? 344 GLN A NE2 1 ATOM 2328 N N . LEU A 1 310 ? 18.116 9.002 4.951 1.00 26.21 ? 345 LEU A N 1 ATOM 2329 C CA . LEU A 1 310 ? 18.921 7.890 4.428 1.00 26.62 ? 345 LEU A CA 1 ATOM 2330 C C . LEU A 1 310 ? 18.100 6.860 3.651 1.00 25.19 ? 345 LEU A C 1 ATOM 2331 O O . LEU A 1 310 ? 18.625 5.811 3.313 1.00 25.44 ? 345 LEU A O 1 ATOM 2332 C CB . LEU A 1 310 ? 19.669 7.183 5.558 1.00 27.47 ? 345 LEU A CB 1 ATOM 2333 C CG . LEU A 1 310 ? 20.593 8.043 6.420 1.00 29.95 ? 345 LEU A CG 1 ATOM 2334 C CD1 . LEU A 1 310 ? 21.135 7.168 7.550 1.00 30.59 ? 345 LEU A CD1 1 ATOM 2335 C CD2 . LEU A 1 310 ? 21.720 8.657 5.600 1.00 32.14 ? 345 LEU A CD2 1 ATOM 2336 N N . ARG A 1 311 ? 16.826 7.150 3.379 1.00 24.86 ? 346 ARG A N 1 ATOM 2337 C CA . ARG A 1 311 ? 15.893 6.201 2.758 1.00 24.70 ? 346 ARG A CA 1 ATOM 2338 C C . ARG A 1 311 ? 15.780 4.855 3.471 1.00 22.94 ? 346 ARG A C 1 ATOM 2339 O O . ARG A 1 311 ? 15.622 3.793 2.846 1.00 20.70 ? 346 ARG A O 1 ATOM 2340 C CB . ARG A 1 311 ? 16.229 6.059 1.257 1.00 27.63 ? 346 ARG A CB 1 ATOM 2341 C CG . ARG A 1 311 ? 16.105 7.390 0.527 1.00 33.81 ? 346 ARG A CG 1 ATOM 2342 C CD . ARG A 1 311 ? 14.671 7.943 0.550 1.00 40.46 ? 346 ARG A CD 1 ATOM 2343 N NE . ARG A 1 311 ? 14.657 9.399 0.743 1.00 47.77 ? 346 ARG A NE 1 ATOM 2344 C CZ . ARG A 1 311 ? 14.592 10.320 -0.225 1.00 48.69 ? 346 ARG A CZ 1 ATOM 2345 N NH1 . ARG A 1 311 ? 14.503 9.986 -1.516 1.00 58.29 ? 346 ARG A NH1 1 ATOM 2346 N NH2 . ARG A 1 311 ? 14.604 11.611 0.106 1.00 51.78 ? 346 ARG A NH2 1 ATOM 2347 N N . LEU A 1 312 ? 15.810 4.918 4.803 1.00 21.43 ? 347 LEU A N 1 ATOM 2348 C CA . LEU A 1 312 ? 15.746 3.720 5.652 1.00 21.42 ? 347 LEU A CA 1 ATOM 2349 C C . LEU A 1 312 ? 14.460 3.612 6.481 1.00 20.51 ? 347 LEU A C 1 ATOM 2350 O O . LEU A 1 312 ? 14.260 2.625 7.219 1.00 19.44 ? 347 LEU A O 1 ATOM 2351 C CB . LEU A 1 312 ? 16.935 3.725 6.605 1.00 22.65 ? 347 LEU A CB 1 ATOM 2352 C CG . LEU A 1 312 ? 18.295 3.360 6.025 1.00 24.09 ? 347 LEU A CG 1 ATOM 2353 C CD1 . LEU A 1 312 ? 19.401 3.671 7.027 1.00 23.32 ? 347 LEU A CD1 1 ATOM 2354 C CD2 . LEU A 1 312 ? 18.326 1.900 5.621 1.00 24.96 ? 347 LEU A CD2 1 ATOM 2355 N N . HIS A 1 313 ? 13.602 4.615 6.360 1.00 20.07 ? 348 HIS A N 1 ATOM 2356 C CA . HIS A 1 313 ? 12.354 4.689 7.140 1.00 20.05 ? 348 HIS A CA 1 ATOM 2357 C C . HIS A 1 313 ? 11.319 3.626 6.820 1.00 20.31 ? 348 HIS A C 1 ATOM 2358 O O . HIS A 1 313 ? 10.369 3.462 7.582 1.00 20.94 ? 348 HIS A O 1 ATOM 2359 C CB . HIS A 1 313 ? 11.726 6.094 7.034 1.00 20.30 ? 348 HIS A CB 1 ATOM 2360 C CG . HIS A 1 313 ? 11.203 6.433 5.672 1.00 21.72 ? 348 HIS A CG 1 ATOM 2361 N ND1 . HIS A 1 313 ? 12.008 6.481 4.557 1.00 22.37 ? 348 HIS A ND1 1 ATOM 2362 C CD2 . HIS A 1 313 ? 9.958 6.764 5.254 1.00 22.31 ? 348 HIS A CD2 1 ATOM 2363 C CE1 . HIS A 1 313 ? 11.276 6.785 3.505 1.00 24.11 ? 348 HIS A CE1 1 ATOM 2364 N NE2 . HIS A 1 313 ? 10.031 6.975 3.902 1.00 23.92 ? 348 HIS A NE2 1 ATOM 2365 N N . ARG A 1 314 ? 11.469 2.926 5.700 1.00 20.41 ? 349 ARG A N 1 ATOM 2366 C CA . ARG A 1 314 ? 10.633 1.783 5.371 1.00 20.87 ? 349 ARG A CA 1 ATOM 2367 C C . ARG A 1 314 ? 11.472 0.504 5.241 1.00 22.04 ? 349 ARG A C 1 ATOM 2368 O O . ARG A 1 314 ? 11.063 -0.439 4.575 1.00 22.62 ? 349 ARG A O 1 ATOM 2369 C CB . ARG A 1 314 ? 9.824 2.073 4.096 1.00 22.12 ? 349 ARG A CB 1 ATOM 2370 C CG . ARG A 1 314 ? 8.815 3.204 4.274 1.00 22.85 ? 349 ARG A CG 1 ATOM 2371 C CD . ARG A 1 314 ? 8.191 3.617 2.951 1.00 24.25 ? 349 ARG A CD 1 ATOM 2372 N NE . ARG A 1 314 ? 7.422 2.526 2.340 1.00 24.94 ? 349 ARG A NE 1 ATOM 2373 C CZ . ARG A 1 314 ? 6.215 2.117 2.753 1.00 26.64 ? 349 ARG A CZ 1 ATOM 2374 N NH1 . ARG A 1 314 ? 5.589 2.707 3.765 1.00 27.81 ? 349 ARG A NH1 1 ATOM 2375 N NH2 . ARG A 1 314 ? 5.616 1.096 2.135 1.00 28.86 ? 349 ARG A NH2 1 ATOM 2376 N N . CYS A 1 315 ? 12.617 0.494 5.923 1.00 21.70 ? 350 CYS A N 1 ATOM 2377 C CA . CYS A 1 315 ? 13.600 -0.583 5.922 1.00 23.24 ? 350 CYS A CA 1 ATOM 2378 C C . CYS A 1 315 ? 13.890 -1.096 7.346 1.00 22.48 ? 350 CYS A C 1 ATOM 2379 O O . CYS A 1 315 ? 13.909 -2.289 7.578 1.00 25.77 ? 350 CYS A O 1 ATOM 2380 C CB . CYS A 1 315 ? 14.895 -0.051 5.285 1.00 26.23 ? 350 CYS A CB 1 ATOM 2381 S SG . CYS A 1 315 ? 16.347 -1.098 5.432 1.00 30.07 ? 350 CYS A SG 1 ATOM 2382 N N . VAL A 1 316 ? 14.112 -0.188 8.283 1.00 20.98 ? 351 VAL A N 1 ATOM 2383 C CA . VAL A 1 316 ? 14.478 -0.525 9.668 1.00 20.63 ? 351 VAL A CA 1 ATOM 2384 C C . VAL A 1 316 ? 13.264 -0.927 10.496 1.00 20.10 ? 351 VAL A C 1 ATOM 2385 O O . VAL A 1 316 ? 12.192 -0.336 10.371 1.00 21.25 ? 351 VAL A O 1 ATOM 2386 C CB . VAL A 1 316 ? 15.199 0.691 10.317 1.00 21.85 ? 351 VAL A CB 1 ATOM 2387 C CG1 . VAL A 1 316 ? 15.412 0.519 11.796 1.00 23.97 ? 351 VAL A CG1 1 ATOM 2388 C CG2 . VAL A 1 316 ? 16.527 0.930 9.605 1.00 21.56 ? 351 VAL A CG2 1 ATOM 2389 N N . ASN A 1 317 ? 13.435 -1.946 11.328 1.00 18.28 ? 352 ASN A N 1 ATOM 2390 C CA . ASN A 1 317 ? 12.474 -2.210 12.402 1.00 17.09 ? 352 ASN A CA 1 ATOM 2391 C C . ASN A 1 317 ? 12.892 -1.404 13.634 1.00 17.02 ? 352 ASN A C 1 ATOM 2392 O O . ASN A 1 317 ? 14.060 -1.413 14.014 1.00 17.39 ? 352 ASN A O 1 ATOM 2393 C CB . ASN A 1 317 ? 12.387 -3.704 12.696 1.00 16.89 ? 352 ASN A CB 1 ATOM 2394 C CG . ASN A 1 317 ? 11.748 -4.483 11.558 1.00 18.01 ? 352 ASN A CG 1 ATOM 2395 O OD1 . ASN A 1 317 ? 10.579 -4.247 11.185 1.00 18.08 ? 352 ASN A OD1 1 ATOM 2396 N ND2 . ASN A 1 317 ? 12.493 -5.442 11.008 1.00 17.32 ? 352 ASN A ND2 1 ATOM 2397 N N . VAL A 1 318 ? 11.940 -0.688 14.229 1.00 16.91 ? 353 VAL A N 1 ATOM 2398 C CA . VAL A 1 318 ? 12.186 0.113 15.411 1.00 17.78 ? 353 VAL A CA 1 ATOM 2399 C C . VAL A 1 318 ? 11.363 -0.464 16.563 1.00 17.80 ? 353 VAL A C 1 ATOM 2400 O O . VAL A 1 318 ? 10.154 -0.703 16.416 1.00 18.54 ? 353 VAL A O 1 ATOM 2401 C CB . VAL A 1 318 ? 11.854 1.598 15.186 1.00 18.49 ? 353 VAL A CB 1 ATOM 2402 C CG1 . VAL A 1 318 ? 12.123 2.421 16.456 1.00 19.15 ? 353 VAL A CG1 1 ATOM 2403 C CG2 . VAL A 1 318 ? 12.669 2.144 14.032 1.00 19.28 ? 353 VAL A CG2 1 ATOM 2404 N N . ILE A 1 319 ? 12.019 -0.672 17.701 1.00 16.23 ? 354 ILE A N 1 ATOM 2405 C CA . ILE A 1 319 ? 11.327 -1.074 18.935 1.00 17.06 ? 354 ILE A CA 1 ATOM 2406 C C . ILE A 1 319 ? 11.443 0.090 19.909 1.00 18.01 ? 354 ILE A C 1 ATOM 2407 O O . ILE A 1 319 ? 12.546 0.549 20.193 1.00 18.24 ? 354 ILE A O 1 ATOM 2408 C CB . ILE A 1 319 ? 11.919 -2.350 19.532 1.00 17.62 ? 354 ILE A CB 1 ATOM 2409 C CG1 . ILE A 1 319 ? 11.540 -3.534 18.647 1.00 17.37 ? 354 ILE A CG1 1 ATOM 2410 C CG2 . ILE A 1 319 ? 11.435 -2.566 20.969 1.00 18.05 ? 354 ILE A CG2 1 ATOM 2411 C CD1 . ILE A 1 319 ? 12.235 -4.845 18.991 1.00 17.33 ? 354 ILE A CD1 1 ATOM 2412 N N . PHE A 1 320 ? 10.299 0.562 20.390 1.00 16.92 ? 355 PHE A N 1 ATOM 2413 C CA . PHE A 1 320 ? 10.234 1.614 21.400 1.00 16.88 ? 355 PHE A CA 1 ATOM 2414 C C . PHE A 1 320 ? 9.767 0.923 22.657 1.00 15.77 ? 355 PHE A C 1 ATOM 2415 O O . PHE A 1 320 ? 8.642 0.425 22.695 1.00 16.93 ? 355 PHE A O 1 ATOM 2416 C CB . PHE A 1 320 ? 9.250 2.712 20.987 1.00 16.93 ? 355 PHE A CB 1 ATOM 2417 C CG . PHE A 1 320 ? 9.200 3.887 21.923 1.00 17.94 ? 355 PHE A CG 1 ATOM 2418 C CD1 . PHE A 1 320 ? 10.106 4.932 21.807 1.00 18.03 ? 355 PHE A CD1 1 ATOM 2419 C CD2 . PHE A 1 320 ? 8.205 3.975 22.914 1.00 17.46 ? 355 PHE A CD2 1 ATOM 2420 C CE1 . PHE A 1 320 ? 10.063 6.024 22.662 1.00 18.70 ? 355 PHE A CE1 1 ATOM 2421 C CE2 . PHE A 1 320 ? 8.162 5.074 23.773 1.00 17.40 ? 355 PHE A CE2 1 ATOM 2422 C CZ . PHE A 1 320 ? 9.087 6.094 23.645 1.00 18.14 ? 355 PHE A CZ 1 ATOM 2423 N N . VAL A 1 321 ? 10.615 0.927 23.680 1.00 15.50 ? 356 VAL A N 1 ATOM 2424 C CA . VAL A 1 321 ? 10.401 0.106 24.834 1.00 16.77 ? 356 VAL A CA 1 ATOM 2425 C C . VAL A 1 321 ? 10.952 0.771 26.096 1.00 16.91 ? 356 VAL A C 1 ATOM 2426 O O . VAL A 1 321 ? 11.984 1.436 26.084 1.00 16.68 ? 356 VAL A O 1 ATOM 2427 C CB . VAL A 1 321 ? 11.032 -1.294 24.561 1.00 19.26 ? 356 VAL A CB 1 ATOM 2428 C CG1 . VAL A 1 321 ? 12.568 -1.251 24.530 1.00 19.37 ? 356 VAL A CG1 1 ATOM 2429 C CG2 . VAL A 1 321 ? 10.560 -2.321 25.526 1.00 23.68 ? 356 VAL A CG2 1 ATOM 2430 N N . GLY A 1 322 ? 10.248 0.575 27.201 1.00 16.09 ? 357 GLY A N 1 ATOM 2431 C CA . GLY A 1 322 ? 10.732 1.040 28.486 1.00 16.61 ? 357 GLY A CA 1 ATOM 2432 C C . GLY A 1 322 ? 11.184 -0.072 29.373 1.00 16.91 ? 357 GLY A C 1 ATOM 2433 O O . GLY A 1 322 ? 10.939 -1.231 29.080 1.00 15.99 ? 357 GLY A O 1 ATOM 2434 N N . ASP A 1 323 ? 11.852 0.284 30.471 1.00 17.27 ? 358 ASP A N 1 ATOM 2435 C CA . ASP A 1 323 ? 12.378 -0.731 31.411 1.00 15.92 ? 358 ASP A CA 1 ATOM 2436 C C . ASP A 1 323 ? 11.453 -0.992 32.589 1.00 15.41 ? 358 ASP A C 1 ATOM 2437 O O . ASP A 1 323 ? 11.408 -2.122 33.096 1.00 14.23 ? 358 ASP A O 1 ATOM 2438 C CB . ASP A 1 323 ? 13.806 -0.399 31.860 1.00 17.06 ? 358 ASP A CB 1 ATOM 2439 C CG . ASP A 1 323 ? 13.931 0.918 32.581 1.00 17.17 ? 358 ASP A CG 1 ATOM 2440 O OD1 . ASP A 1 323 ? 13.033 1.789 32.483 1.00 15.12 ? 358 ASP A OD1 1 ATOM 2441 O OD2 . ASP A 1 323 ? 14.972 1.083 33.280 1.00 20.84 ? 358 ASP A OD2 1 ATOM 2442 N N . HIS A 1 324 ? 10.684 0.030 32.967 1.00 14.74 ? 359 HIS A N 1 ATOM 2443 C CA . HIS A 1 324 ? 9.737 -0.045 34.068 1.00 15.05 ? 359 HIS A CA 1 ATOM 2444 C C . HIS A 1 324 ? 8.965 1.292 34.117 1.00 15.54 ? 359 HIS A C 1 ATOM 2445 O O . HIS A 1 324 ? 9.281 2.246 33.426 1.00 14.75 ? 359 HIS A O 1 ATOM 2446 C CB . HIS A 1 324 ? 10.485 -0.242 35.408 1.00 14.18 ? 359 HIS A CB 1 ATOM 2447 C CG . HIS A 1 324 ? 11.524 0.798 35.652 1.00 14.64 ? 359 HIS A CG 1 ATOM 2448 N ND1 . HIS A 1 324 ? 11.221 2.104 35.969 1.00 14.81 ? 359 HIS A ND1 1 ATOM 2449 C CD2 . HIS A 1 324 ? 12.868 0.752 35.490 1.00 15.60 ? 359 HIS A CD2 1 ATOM 2450 C CE1 . HIS A 1 324 ? 12.339 2.803 36.039 1.00 15.35 ? 359 HIS A CE1 1 ATOM 2451 N NE2 . HIS A 1 324 ? 13.356 2.003 35.763 1.00 15.37 ? 359 HIS A NE2 1 ATOM 2452 N N . GLY A 1 325 ? 7.986 1.354 35.012 1.00 15.83 ? 360 GLY A N 1 ATOM 2453 C CA . GLY A 1 325 ? 7.208 2.553 35.239 1.00 16.12 ? 360 GLY A CA 1 ATOM 2454 C C . GLY A 1 325 ? 7.707 3.408 36.395 1.00 15.84 ? 360 GLY A C 1 ATOM 2455 O O . GLY A 1 325 ? 8.910 3.469 36.680 1.00 16.33 ? 360 GLY A O 1 ATOM 2456 N N . MET A 1 326 ? 6.763 4.104 37.026 1.00 16.72 ? 361 MET A N 1 ATOM 2457 C CA . MET A 1 326 ? 7.049 5.067 38.065 1.00 16.61 ? 361 MET A CA 1 ATOM 2458 C C . MET A 1 326 ? 5.826 5.248 38.963 1.00 17.23 ? 361 MET A C 1 ATOM 2459 O O . MET A 1 326 ? 4.712 5.391 38.473 1.00 16.99 ? 361 MET A O 1 ATOM 2460 C CB . MET A 1 326 ? 7.393 6.411 37.421 1.00 16.66 ? 361 MET A CB 1 ATOM 2461 C CG . MET A 1 326 ? 7.842 7.475 38.397 1.00 18.13 ? 361 MET A CG 1 ATOM 2462 S SD . MET A 1 326 ? 9.425 7.159 39.196 1.00 18.15 ? 361 MET A SD 1 ATOM 2463 C CE . MET A 1 326 ? 10.511 7.232 37.808 1.00 16.63 ? 361 MET A CE 1 ATOM 2464 N N . GLU A 1 327 ? 6.046 5.275 40.276 1.00 18.41 ? 362 GLU A N 1 ATOM 2465 C CA . GLU A 1 327 ? 4.969 5.425 41.261 1.00 19.61 ? 362 GLU A CA 1 ATOM 2466 C C . GLU A 1 327 ? 5.193 6.699 42.055 1.00 20.80 ? 362 GLU A C 1 ATOM 2467 O O . GLU A 1 327 ? 6.306 7.210 42.118 1.00 20.00 ? 362 GLU A O 1 ATOM 2468 C CB . GLU A 1 327 ? 4.963 4.198 42.181 1.00 18.97 ? 362 GLU A CB 1 ATOM 2469 C CG . GLU A 1 327 ? 3.924 4.131 43.287 1.00 19.36 ? 362 GLU A CG 1 ATOM 2470 C CD . GLU A 1 327 ? 2.502 4.138 42.753 1.00 20.54 ? 362 GLU A CD 1 ATOM 2471 O OE1 . GLU A 1 327 ? 1.990 5.231 42.447 1.00 22.26 ? 362 GLU A OE1 1 ATOM 2472 O OE2 . GLU A 1 327 ? 1.913 3.061 42.613 1.00 22.32 ? 362 GLU A OE2 1 ATOM 2473 N N . ASP A 1 328 ? 4.126 7.207 42.670 1.00 21.29 ? 363 ASP A N 1 ATOM 2474 C CA . ASP A 1 328 ? 4.228 8.280 43.660 1.00 23.15 ? 363 ASP A CA 1 ATOM 2475 C C . ASP A 1 328 ? 4.819 7.754 44.946 1.00 21.94 ? 363 ASP A C 1 ATOM 2476 O O . ASP A 1 328 ? 4.194 6.933 45.606 1.00 19.39 ? 363 ASP A O 1 ATOM 2477 C CB . ASP A 1 328 ? 2.839 8.825 43.974 1.00 26.99 ? 363 ASP A CB 1 ATOM 2478 C CG . ASP A 1 328 ? 2.300 9.662 42.866 1.00 30.82 ? 363 ASP A CG 1 ATOM 2479 O OD1 . ASP A 1 328 ? 2.935 10.702 42.560 1.00 37.71 ? 363 ASP A OD1 1 ATOM 2480 O OD2 . ASP A 1 328 ? 1.250 9.291 42.314 1.00 38.20 ? 363 ASP A OD2 1 ATOM 2481 N N . VAL A 1 329 ? 6.012 8.227 45.296 1.00 21.51 ? 364 VAL A N 1 ATOM 2482 C CA . VAL A 1 329 ? 6.703 7.833 46.515 1.00 22.93 ? 364 VAL A CA 1 ATOM 2483 C C . VAL A 1 329 ? 7.393 9.091 47.046 1.00 25.23 ? 364 VAL A C 1 ATOM 2484 O O . VAL A 1 329 ? 8.154 9.729 46.325 1.00 25.33 ? 364 VAL A O 1 ATOM 2485 C CB . VAL A 1 329 ? 7.765 6.744 46.241 1.00 22.22 ? 364 VAL A CB 1 ATOM 2486 C CG1 . VAL A 1 329 ? 8.379 6.239 47.542 1.00 24.38 ? 364 VAL A CG1 1 ATOM 2487 C CG2 . VAL A 1 329 ? 7.154 5.583 45.474 1.00 20.61 ? 364 VAL A CG2 1 ATOM 2488 N N . THR A 1 330 ? 7.120 9.436 48.291 1.00 25.68 ? 365 THR A N 1 ATOM 2489 C CA . THR A 1 330 ? 7.759 10.583 48.932 1.00 28.53 ? 365 THR A CA 1 ATOM 2490 C C . THR A 1 330 ? 8.407 10.145 50.236 1.00 31.53 ? 365 THR A C 1 ATOM 2491 O O . THR A 1 330 ? 8.051 9.099 50.797 1.00 28.54 ? 365 THR A O 1 ATOM 2492 C CB . THR A 1 330 ? 6.717 11.671 49.235 1.00 29.52 ? 365 THR A CB 1 ATOM 2493 O OG1 . THR A 1 330 ? 5.795 11.172 50.180 1.00 29.27 ? 365 THR A OG1 1 ATOM 2494 C CG2 . THR A 1 330 ? 5.965 12.047 47.965 1.00 29.78 ? 365 THR A CG2 1 ATOM 2495 N N . CYS A 1 331 ? 9.345 10.957 50.719 1.00 32.72 ? 366 CYS A N 1 ATOM 2496 C CA . CYS A 1 331 ? 10.096 10.637 51.928 1.00 35.14 ? 366 CYS A CA 1 ATOM 2497 C C . CYS A 1 331 ? 9.213 10.495 53.190 1.00 34.85 ? 366 CYS A C 1 ATOM 2498 O O . CYS A 1 331 ? 9.586 9.794 54.127 1.00 35.04 ? 366 CYS A O 1 ATOM 2499 C CB . CYS A 1 331 ? 11.204 11.679 52.124 1.00 42.07 ? 366 CYS A CB 1 ATOM 2500 S SG . CYS A 1 331 ? 10.648 13.312 52.625 1.00 50.03 ? 366 CYS A SG 1 ATOM 2501 N N . ASP A 1 332 ? 8.040 11.128 53.187 1.00 32.97 ? 367 ASP A N 1 ATOM 2502 C CA . ASP A 1 332 ? 7.046 10.967 54.245 1.00 34.18 ? 367 ASP A CA 1 ATOM 2503 C C . ASP A 1 332 ? 6.480 9.554 54.400 1.00 32.00 ? 367 ASP A C 1 ATOM 2504 O O . ASP A 1 332 ? 5.999 9.200 55.469 1.00 31.80 ? 367 ASP A O 1 ATOM 2505 C CB . ASP A 1 332 ? 5.896 11.960 54.036 1.00 38.70 ? 367 ASP A CB 1 ATOM 2506 C CG . ASP A 1 332 ? 6.312 13.404 54.341 1.00 45.38 ? 367 ASP A CG 1 ATOM 2507 O OD1 . ASP A 1 332 ? 6.718 13.687 55.492 1.00 50.62 ? 367 ASP A OD1 1 ATOM 2508 O OD2 . ASP A 1 332 ? 6.242 14.256 53.428 1.00 52.98 ? 367 ASP A OD2 1 ATOM 2509 N N . ARG A 1 333 ? 6.511 8.758 53.342 1.00 29.28 ? 368 ARG A N 1 ATOM 2510 C CA . ARG A 1 333 ? 6.010 7.383 53.383 1.00 26.64 ? 368 ARG A CA 1 ATOM 2511 C C . ARG A 1 333 ? 7.203 6.439 53.434 1.00 25.24 ? 368 ARG A C 1 ATOM 2512 O O . ARG A 1 333 ? 7.489 5.717 52.489 1.00 23.78 ? 368 ARG A O 1 ATOM 2513 C CB . ARG A 1 333 ? 5.116 7.116 52.175 1.00 25.31 ? 368 ARG A CB 1 ATOM 2514 C CG . ARG A 1 333 ? 3.854 7.957 52.196 1.00 26.71 ? 368 ARG A CG 1 ATOM 2515 C CD . ARG A 1 333 ? 2.820 7.401 51.247 1.00 26.29 ? 368 ARG A CD 1 ATOM 2516 N NE . ARG A 1 333 ? 3.214 7.582 49.852 1.00 23.85 ? 368 ARG A NE 1 ATOM 2517 C CZ . ARG A 1 333 ? 3.036 8.692 49.140 1.00 25.42 ? 368 ARG A CZ 1 ATOM 2518 N NH1 . ARG A 1 333 ? 2.496 9.800 49.673 1.00 26.50 ? 368 ARG A NH1 1 ATOM 2519 N NH2 . ARG A 1 333 ? 3.401 8.703 47.868 1.00 25.48 ? 368 ARG A NH2 1 ATOM 2520 N N . THR A 1 334 ? 7.918 6.487 54.552 1.00 23.37 ? 369 THR A N 1 ATOM 2521 C CA . THR A 1 334 ? 9.044 5.617 54.792 1.00 23.13 ? 369 THR A CA 1 ATOM 2522 C C . THR A 1 334 ? 8.852 4.834 56.099 1.00 23.21 ? 369 THR A C 1 ATOM 2523 O O . THR A 1 334 ? 8.619 5.421 57.151 1.00 24.50 ? 369 THR A O 1 ATOM 2524 C CB . THR A 1 334 ? 10.335 6.414 54.852 1.00 24.51 ? 369 THR A CB 1 ATOM 2525 O OG1 . THR A 1 334 ? 10.474 7.179 53.632 1.00 24.62 ? 369 THR A OG1 1 ATOM 2526 C CG2 . THR A 1 334 ? 11.546 5.471 55.029 1.00 23.92 ? 369 THR A CG2 1 ATOM 2527 N N . GLU A 1 335 ? 8.939 3.514 56.004 1.00 23.46 ? 370 GLU A N 1 ATOM 2528 C CA . GLU A 1 335 ? 9.018 2.632 57.166 1.00 23.52 ? 370 GLU A CA 1 ATOM 2529 C C . GLU A 1 335 ? 10.475 2.458 57.559 1.00 23.24 ? 370 GLU A C 1 ATOM 2530 O O . GLU A 1 335 ? 11.352 2.327 56.698 1.00 22.56 ? 370 GLU A O 1 ATOM 2531 C CB . GLU A 1 335 ? 8.444 1.253 56.825 1.00 24.77 ? 370 GLU A CB 1 ATOM 2532 C CG . GLU A 1 335 ? 6.933 1.220 56.637 1.00 26.00 ? 370 GLU A CG 1 ATOM 2533 C CD . GLU A 1 335 ? 6.168 0.736 57.857 1.00 27.38 ? 370 GLU A CD 1 ATOM 2534 O OE1 . GLU A 1 335 ? 6.716 0.680 58.980 1.00 30.10 ? 370 GLU A OE1 1 ATOM 2535 O OE2 . GLU A 1 335 ? 4.985 0.402 57.686 1.00 28.86 ? 370 GLU A OE2 1 ATOM 2536 N N . PHE A 1 336 ? 10.745 2.404 58.859 1.00 22.75 ? 371 PHE A N 1 ATOM 2537 C CA . PHE A 1 336 ? 12.109 2.202 59.312 1.00 23.95 ? 371 PHE A CA 1 ATOM 2538 C C . PHE A 1 336 ? 12.279 0.889 60.048 1.00 23.68 ? 371 PHE A C 1 ATOM 2539 O O . PHE A 1 336 ? 11.569 0.645 61.017 1.00 22.81 ? 371 PHE A O 1 ATOM 2540 C CB . PHE A 1 336 ? 12.514 3.362 60.209 1.00 24.83 ? 371 PHE A CB 1 ATOM 2541 C CG . PHE A 1 336 ? 12.486 4.692 59.508 1.00 26.35 ? 371 PHE A CG 1 ATOM 2542 C CD1 . PHE A 1 336 ? 13.499 5.034 58.630 1.00 26.33 ? 371 PHE A CD1 1 ATOM 2543 C CD2 . PHE A 1 336 ? 11.440 5.585 59.699 1.00 27.54 ? 371 PHE A CD2 1 ATOM 2544 C CE1 . PHE A 1 336 ? 13.479 6.237 57.942 1.00 27.41 ? 371 PHE A CE1 1 ATOM 2545 C CE2 . PHE A 1 336 ? 11.413 6.799 59.012 1.00 28.21 ? 371 PHE A CE2 1 ATOM 2546 C CZ . PHE A 1 336 ? 12.436 7.117 58.130 1.00 27.47 ? 371 PHE A CZ 1 ATOM 2547 N N . LEU A 1 337 ? 13.266 0.083 59.657 1.00 23.27 ? 372 LEU A N 1 ATOM 2548 C CA . LEU A 1 337 ? 13.540 -1.180 60.360 1.00 24.86 ? 372 LEU A CA 1 ATOM 2549 C C . LEU A 1 337 ? 13.845 -0.999 61.836 1.00 25.50 ? 372 LEU A C 1 ATOM 2550 O O . LEU A 1 337 ? 13.489 -1.866 62.652 1.00 27.15 ? 372 LEU A O 1 ATOM 2551 C CB . LEU A 1 337 ? 14.691 -1.954 59.722 1.00 25.55 ? 372 LEU A CB 1 ATOM 2552 C CG . LEU A 1 337 ? 14.449 -2.482 58.311 1.00 26.79 ? 372 LEU A CG 1 ATOM 2553 C CD1 . LEU A 1 337 ? 15.625 -3.345 57.903 1.00 26.83 ? 372 LEU A CD1 1 ATOM 2554 C CD2 . LEU A 1 337 ? 13.133 -3.243 58.221 1.00 27.01 ? 372 LEU A CD2 1 ATOM 2555 N N . SER A 1 338 ? 14.482 0.129 62.182 1.00 25.95 ? 373 SER A N 1 ATOM 2556 C CA . SER A 1 338 ? 14.746 0.482 63.589 1.00 27.48 ? 373 SER A CA 1 ATOM 2557 C C . SER A 1 338 ? 13.490 0.582 64.464 1.00 28.16 ? 373 SER A C 1 ATOM 2558 O O . SER A 1 338 ? 13.604 0.476 65.683 1.00 28.41 ? 373 SER A O 1 ATOM 2559 C CB . SER A 1 338 ? 15.562 1.769 63.698 1.00 27.29 ? 373 SER A CB 1 ATOM 2560 O OG . SER A 1 338 ? 14.924 2.834 63.014 1.00 27.12 ? 373 SER A OG 1 ATOM 2561 N N . ASN A 1 339 ? 12.317 0.774 63.858 1.00 26.57 ? 374 ASN A N 1 ATOM 2562 C CA . ASN A 1 339 ? 11.027 0.677 64.557 1.00 27.10 ? 374 ASN A CA 1 ATOM 2563 C C . ASN A 1 339 ? 10.473 -0.732 64.782 1.00 26.11 ? 374 ASN A C 1 ATOM 2564 O O . ASN A 1 339 ? 9.409 -0.885 65.400 1.00 27.11 ? 374 ASN A O 1 ATOM 2565 C CB . ASN A 1 339 ? 9.961 1.507 63.828 1.00 27.87 ? 374 ASN A CB 1 ATOM 2566 C CG . ASN A 1 339 ? 10.201 2.997 63.941 1.00 30.40 ? 374 ASN A CG 1 ATOM 2567 O OD1 . ASN A 1 339 ? 10.836 3.479 64.877 1.00 29.37 ? 374 ASN A OD1 1 ATOM 2568 N ND2 . ASN A 1 339 ? 9.672 3.743 62.982 1.00 32.57 ? 374 ASN A ND2 1 ATOM 2569 N N . TYR A 1 340 ? 11.166 -1.744 64.274 1.00 24.30 ? 375 TYR A N 1 ATOM 2570 C CA . TYR A 1 340 ? 10.811 -3.158 64.424 1.00 24.32 ? 375 TYR A CA 1 ATOM 2571 C C . TYR A 1 340 ? 11.931 -3.989 65.038 1.00 25.33 ? 375 TYR A C 1 ATOM 2572 O O . TYR A 1 340 ? 11.654 -4.924 65.781 1.00 26.78 ? 375 TYR A O 1 ATOM 2573 C CB . TYR A 1 340 ? 10.482 -3.766 63.047 1.00 22.67 ? 375 TYR A CB 1 ATOM 2574 C CG . TYR A 1 340 ? 9.317 -3.113 62.346 1.00 23.29 ? 375 TYR A CG 1 ATOM 2575 C CD1 . TYR A 1 340 ? 9.470 -1.906 61.669 1.00 23.20 ? 375 TYR A CD1 1 ATOM 2576 C CD2 . TYR A 1 340 ? 8.062 -3.714 62.339 1.00 24.24 ? 375 TYR A CD2 1 ATOM 2577 C CE1 . TYR A 1 340 ? 8.402 -1.291 61.041 1.00 24.10 ? 375 TYR A CE1 1 ATOM 2578 C CE2 . TYR A 1 340 ? 6.987 -3.116 61.712 1.00 24.45 ? 375 TYR A CE2 1 ATOM 2579 C CZ . TYR A 1 340 ? 7.153 -1.909 61.064 1.00 25.13 ? 375 TYR A CZ 1 ATOM 2580 O OH . TYR A 1 340 ? 6.070 -1.332 60.453 1.00 26.71 ? 375 TYR A OH 1 ATOM 2581 N N . LEU A 1 341 ? 13.183 -3.680 64.695 1.00 27.36 ? 376 LEU A N 1 ATOM 2582 C CA . LEU A 1 341 ? 14.334 -4.463 65.122 1.00 30.07 ? 376 LEU A CA 1 ATOM 2583 C C . LEU A 1 341 ? 15.129 -3.670 66.134 1.00 32.77 ? 376 LEU A C 1 ATOM 2584 O O . LEU A 1 341 ? 15.495 -2.533 65.879 1.00 34.09 ? 376 LEU A O 1 ATOM 2585 C CB . LEU A 1 341 ? 15.234 -4.782 63.926 1.00 29.39 ? 376 LEU A CB 1 ATOM 2586 C CG . LEU A 1 341 ? 14.594 -5.462 62.720 1.00 28.71 ? 376 LEU A CG 1 ATOM 2587 C CD1 . LEU A 1 341 ? 15.609 -5.658 61.606 1.00 28.63 ? 376 LEU A CD1 1 ATOM 2588 C CD2 . LEU A 1 341 ? 13.982 -6.784 63.107 1.00 29.05 ? 376 LEU A CD2 1 ATOM 2589 N N . THR A 1 342 ? 15.403 -4.281 67.273 1.00 36.67 ? 377 THR A N 1 ATOM 2590 C CA . THR A 1 342 ? 16.209 -3.641 68.296 1.00 41.36 ? 377 THR A CA 1 ATOM 2591 C C . THR A 1 342 ? 17.701 -3.644 67.944 1.00 45.73 ? 377 THR A C 1 ATOM 2592 O O . THR A 1 342 ? 18.422 -2.740 68.355 1.00 50.35 ? 377 THR A O 1 ATOM 2593 C CB . THR A 1 342 ? 15.972 -4.323 69.639 1.00 43.47 ? 377 THR A CB 1 ATOM 2594 O OG1 . THR A 1 342 ? 16.246 -5.723 69.508 1.00 44.46 ? 377 THR A OG1 1 ATOM 2595 C CG2 . THR A 1 342 ? 14.524 -4.134 70.058 1.00 43.59 ? 377 THR A CG2 1 ATOM 2596 N N . ASN A 1 343 ? 18.147 -4.640 67.173 1.00 48.03 ? 378 ASN A N 1 ATOM 2597 C CA . ASN A 1 343 ? 19.550 -4.780 66.760 1.00 49.99 ? 378 ASN A CA 1 ATOM 2598 C C . ASN A 1 343 ? 19.761 -4.471 65.262 1.00 48.08 ? 378 ASN A C 1 ATOM 2599 O O . ASN A 1 343 ? 20.345 -5.279 64.542 1.00 48.31 ? 378 ASN A O 1 ATOM 2600 C CB . ASN A 1 343 ? 20.050 -6.204 67.095 1.00 53.87 ? 378 ASN A CB 1 ATOM 2601 C CG . ASN A 1 343 ? 20.156 -6.467 68.599 1.00 61.27 ? 378 ASN A CG 1 ATOM 2602 O OD1 . ASN A 1 343 ? 19.405 -7.270 69.162 1.00 65.45 ? 378 ASN A OD1 1 ATOM 2603 N ND2 . ASN A 1 343 ? 21.102 -5.801 69.252 1.00 63.75 ? 378 ASN A ND2 1 ATOM 2604 N N . VAL A 1 344 ? 19.318 -3.296 64.798 1.00 45.37 ? 379 VAL A N 1 ATOM 2605 C CA . VAL A 1 344 ? 19.501 -2.901 63.380 1.00 44.62 ? 379 VAL A CA 1 ATOM 2606 C C . VAL A 1 344 ? 20.938 -2.671 62.922 1.00 44.21 ? 379 VAL A C 1 ATOM 2607 O O . VAL A 1 344 ? 21.202 -2.641 61.719 1.00 40.68 ? 379 VAL A O 1 ATOM 2608 C CB . VAL A 1 344 ? 18.709 -1.636 62.955 1.00 46.80 ? 379 VAL A CB 1 ATOM 2609 C CG1 . VAL A 1 344 ? 17.228 -1.927 62.886 1.00 46.78 ? 379 VAL A CG1 1 ATOM 2610 C CG2 . VAL A 1 344 ? 18.997 -0.451 63.861 1.00 49.16 ? 379 VAL A CG2 1 ATOM 2611 N N . ASP A 1 345 ? 21.854 -2.459 63.859 1.00 42.05 ? 380 ASP A N 1 ATOM 2612 C CA . ASP A 1 345 ? 23.262 -2.265 63.510 1.00 43.63 ? 380 ASP A CA 1 ATOM 2613 C C . ASP A 1 345 ? 23.952 -3.568 63.110 1.00 39.94 ? 380 ASP A C 1 ATOM 2614 O O . ASP A 1 345 ? 25.015 -3.525 62.526 1.00 38.94 ? 380 ASP A O 1 ATOM 2615 C CB . ASP A 1 345 ? 24.014 -1.593 64.668 1.00 47.90 ? 380 ASP A CB 1 ATOM 2616 C CG . ASP A 1 345 ? 23.492 -0.200 64.969 1.00 51.09 ? 380 ASP A CG 1 ATOM 2617 O OD1 . ASP A 1 345 ? 23.082 0.515 64.025 1.00 54.07 ? 380 ASP A OD1 1 ATOM 2618 O OD2 . ASP A 1 345 ? 23.491 0.188 66.152 1.00 59.32 ? 380 ASP A OD2 1 ATOM 2619 N N . ASP A 1 346 ? 23.357 -4.715 63.423 1.00 37.01 ? 381 ASP A N 1 ATOM 2620 C CA . ASP A 1 346 ? 23.905 -5.999 62.993 1.00 37.59 ? 381 ASP A CA 1 ATOM 2621 C C . ASP A 1 346 ? 23.470 -6.423 61.585 1.00 35.38 ? 381 ASP A C 1 ATOM 2622 O O . ASP A 1 346 ? 23.862 -7.488 61.138 1.00 34.60 ? 381 ASP A O 1 ATOM 2623 C CB . ASP A 1 346 ? 23.501 -7.100 63.968 1.00 40.27 ? 381 ASP A CB 1 ATOM 2624 C CG . ASP A 1 346 ? 23.999 -6.846 65.377 1.00 43.89 ? 381 ASP A CG 1 ATOM 2625 O OD1 . ASP A 1 346 ? 24.824 -5.927 65.573 1.00 46.45 ? 381 ASP A OD1 1 ATOM 2626 O OD2 . ASP A 1 346 ? 23.541 -7.571 66.282 1.00 46.91 ? 381 ASP A OD2 1 ATOM 2627 N N . ILE A 1 347 ? 22.666 -5.625 60.895 1.00 33.31 ? 382 ILE A N 1 ATOM 2628 C CA . ILE A 1 347 ? 22.208 -6.012 59.562 1.00 33.28 ? 382 ILE A CA 1 ATOM 2629 C C . ILE A 1 347 ? 22.590 -4.995 58.522 1.00 30.57 ? 382 ILE A C 1 ATOM 2630 O O . ILE A 1 347 ? 22.824 -3.831 58.828 1.00 29.78 ? 382 ILE A O 1 ATOM 2631 C CB . ILE A 1 347 ? 20.673 -6.259 59.493 1.00 35.42 ? 382 ILE A CB 1 ATOM 2632 C CG1 . ILE A 1 347 ? 19.867 -4.983 59.765 1.00 37.71 ? 382 ILE A CG1 1 ATOM 2633 C CG2 . ILE A 1 347 ? 20.261 -7.359 60.451 1.00 35.77 ? 382 ILE A CG2 1 ATOM 2634 C CD1 . ILE A 1 347 ? 18.414 -5.101 59.360 1.00 39.94 ? 382 ILE A CD1 1 ATOM 2635 N N . THR A 1 348 ? 22.623 -5.465 57.280 1.00 28.66 ? 383 THR A N 1 ATOM 2636 C CA . THR A 1 348 ? 22.741 -4.624 56.113 1.00 28.12 ? 383 THR A CA 1 ATOM 2637 C C . THR A 1 348 ? 21.417 -4.735 55.365 1.00 25.85 ? 383 THR A C 1 ATOM 2638 O O . THR A 1 348 ? 20.894 -5.812 55.236 1.00 26.27 ? 383 THR A O 1 ATOM 2639 C CB . THR A 1 348 ? 23.905 -5.118 55.227 1.00 28.72 ? 383 THR A CB 1 ATOM 2640 O OG1 . THR A 1 348 ? 25.146 -4.868 55.906 1.00 32.70 ? 383 THR A OG1 1 ATOM 2641 C CG2 . THR A 1 348 ? 23.912 -4.432 53.888 1.00 28.88 ? 383 THR A CG2 1 ATOM 2642 N N . LEU A 1 349 ? 20.906 -3.605 54.892 1.00 25.19 ? 384 LEU A N 1 ATOM 2643 C CA . LEU A 1 349 ? 19.659 -3.529 54.148 1.00 23.63 ? 384 LEU A CA 1 ATOM 2644 C C . LEU A 1 349 ? 19.915 -2.897 52.800 1.00 23.02 ? 384 LEU A C 1 ATOM 2645 O O . LEU A 1 349 ? 20.459 -1.818 52.725 1.00 22.81 ? 384 LEU A O 1 ATOM 2646 C CB . LEU A 1 349 ? 18.644 -2.673 54.905 1.00 24.22 ? 384 LEU A CB 1 ATOM 2647 C CG . LEU A 1 349 ? 17.333 -2.353 54.190 1.00 22.57 ? 384 LEU A CG 1 ATOM 2648 C CD1 . LEU A 1 349 ? 16.502 -3.611 54.052 1.00 22.31 ? 384 LEU A CD1 1 ATOM 2649 C CD2 . LEU A 1 349 ? 16.581 -1.254 54.913 1.00 24.37 ? 384 LEU A CD2 1 ATOM 2650 N N . VAL A 1 350 ? 19.508 -3.583 51.741 1.00 22.63 ? 385 VAL A N 1 ATOM 2651 C CA . VAL A 1 350 ? 19.334 -2.948 50.457 1.00 23.44 ? 385 VAL A CA 1 ATOM 2652 C C . VAL A 1 350 ? 17.931 -2.317 50.540 1.00 23.40 ? 385 VAL A C 1 ATOM 2653 O O . VAL A 1 350 ? 16.945 -3.032 50.593 1.00 22.05 ? 385 VAL A O 1 ATOM 2654 C CB . VAL A 1 350 ? 19.424 -3.952 49.301 1.00 24.08 ? 385 VAL A CB 1 ATOM 2655 C CG1 . VAL A 1 350 ? 19.259 -3.234 47.964 1.00 23.96 ? 385 VAL A CG1 1 ATOM 2656 C CG2 . VAL A 1 350 ? 20.754 -4.714 49.360 1.00 25.37 ? 385 VAL A CG2 1 ATOM 2657 N N . PRO A 1 351 ? 17.842 -0.978 50.583 1.00 23.26 ? 386 PRO A N 1 ATOM 2658 C CA . PRO A 1 351 ? 16.596 -0.319 50.963 1.00 22.26 ? 386 PRO A CA 1 ATOM 2659 C C . PRO A 1 351 ? 15.768 0.214 49.796 1.00 22.14 ? 386 PRO A C 1 ATOM 2660 O O . PRO A 1 351 ? 16.144 0.044 48.642 1.00 21.45 ? 386 PRO A O 1 ATOM 2661 C CB . PRO A 1 351 ? 17.130 0.855 51.767 1.00 23.90 ? 386 PRO A CB 1 ATOM 2662 C CG . PRO A 1 351 ? 18.291 1.287 50.919 1.00 24.50 ? 386 PRO A CG 1 ATOM 2663 C CD . PRO A 1 351 ? 18.896 0.029 50.354 1.00 24.56 ? 386 PRO A CD 1 ATOM 2664 N N . GLY A 1 352 ? 14.653 0.862 50.121 1.00 22.30 ? 387 GLY A N 1 ATOM 2665 C CA . GLY A 1 352 ? 13.822 1.584 49.180 1.00 20.98 ? 387 GLY A CA 1 ATOM 2666 C C . GLY A 1 352 ? 12.507 0.903 48.859 1.00 20.04 ? 387 GLY A C 1 ATOM 2667 O O . GLY A 1 352 ? 11.715 0.588 49.760 1.00 20.10 ? 387 GLY A O 1 ATOM 2668 N N . THR A 1 353 ? 12.278 0.634 47.575 1.00 17.81 ? 388 THR A N 1 ATOM 2669 C CA . THR A 1 353 ? 11.022 0.064 47.107 1.00 17.41 ? 388 THR A CA 1 ATOM 2670 C C . THR A 1 353 ? 11.002 -1.474 47.177 1.00 17.79 ? 388 THR A C 1 ATOM 2671 O O . THR A 1 353 ? 10.004 -2.109 46.783 1.00 15.52 ? 388 THR A O 1 ATOM 2672 C CB . THR A 1 353 ? 10.764 0.519 45.667 1.00 16.68 ? 388 THR A CB 1 ATOM 2673 O OG1 . THR A 1 353 ? 11.901 0.154 44.878 1.00 17.83 ? 388 THR A OG1 1 ATOM 2674 C CG2 . THR A 1 353 ? 10.562 2.047 45.625 1.00 17.54 ? 388 THR A CG2 1 ATOM 2675 N N A LEU A 1 354 ? 12.110 -2.056 47.625 0.50 17.62 ? 389 LEU A N 1 ATOM 2676 N N B LEU A 1 354 ? 12.112 -2.050 47.630 0.50 18.05 ? 389 LEU A N 1 ATOM 2677 C CA A LEU A 1 354 ? 12.177 -3.448 48.046 0.50 17.30 ? 389 LEU A CA 1 ATOM 2678 C CA B LEU A 1 354 ? 12.209 -3.447 48.026 0.50 17.95 ? 389 LEU A CA 1 ATOM 2679 C C A LEU A 1 354 ? 13.201 -3.483 49.174 0.50 18.08 ? 389 LEU A C 1 ATOM 2680 C C B LEU A 1 354 ? 13.117 -3.441 49.249 0.50 18.27 ? 389 LEU A C 1 ATOM 2681 O O A LEU A 1 354 ? 13.948 -2.523 49.365 0.50 19.34 ? 389 LEU A O 1 ATOM 2682 O O B LEU A 1 354 ? 13.670 -2.398 49.600 0.50 18.85 ? 389 LEU A O 1 ATOM 2683 C CB A LEU A 1 354 ? 12.592 -4.360 46.896 0.50 16.81 ? 389 LEU A CB 1 ATOM 2684 C CB B LEU A 1 354 ? 12.807 -4.287 46.901 0.50 18.37 ? 389 LEU A CB 1 ATOM 2685 C CG A LEU A 1 354 ? 13.959 -4.096 46.246 0.50 16.82 ? 389 LEU A CG 1 ATOM 2686 C CG B LEU A 1 354 ? 14.137 -3.785 46.303 0.50 18.85 ? 389 LEU A CG 1 ATOM 2687 C CD1 A LEU A 1 354 ? 14.530 -5.387 45.675 0.50 16.57 ? 389 LEU A CD1 1 ATOM 2688 C CD1 B LEU A 1 354 ? 15.341 -4.266 47.088 0.50 19.49 ? 389 LEU A CD1 1 ATOM 2689 C CD2 A LEU A 1 354 ? 13.834 -3.008 45.181 0.50 16.52 ? 389 LEU A CD2 1 ATOM 2690 C CD2 B LEU A 1 354 ? 14.270 -4.223 44.859 0.50 19.01 ? 389 LEU A CD2 1 ATOM 2691 N N . GLY A 1 355 ? 13.240 -4.585 49.912 1.00 16.97 ? 390 GLY A N 1 ATOM 2692 C CA . GLY A 1 355 ? 14.229 -4.777 50.978 1.00 17.88 ? 390 GLY A CA 1 ATOM 2693 C C . GLY A 1 355 ? 14.924 -6.117 50.816 1.00 17.12 ? 390 GLY A C 1 ATOM 2694 O O . GLY A 1 355 ? 14.261 -7.108 50.559 1.00 17.23 ? 390 GLY A O 1 ATOM 2695 N N . ARG A 1 356 ? 16.244 -6.136 50.962 1.00 17.63 ? 391 ARG A N 1 ATOM 2696 C CA . ARG A 1 356 ? 17.015 -7.374 51.050 1.00 17.72 ? 391 ARG A CA 1 ATOM 2697 C C . ARG A 1 356 ? 17.897 -7.210 52.251 1.00 19.19 ? 391 ARG A C 1 ATOM 2698 O O . ARG A 1 356 ? 18.572 -6.200 52.386 1.00 18.99 ? 391 ARG A O 1 ATOM 2699 C CB . ARG A 1 356 ? 17.839 -7.614 49.787 1.00 18.23 ? 391 ARG A CB 1 ATOM 2700 C CG . ARG A 1 356 ? 16.989 -7.627 48.531 1.00 18.64 ? 391 ARG A CG 1 ATOM 2701 C CD . ARG A 1 356 ? 17.583 -8.460 47.402 1.00 18.99 ? 391 ARG A CD 1 ATOM 2702 N NE . ARG A 1 356 ? 18.928 -8.039 47.045 1.00 19.65 ? 391 ARG A NE 1 ATOM 2703 C CZ . ARG A 1 356 ? 19.252 -7.031 46.231 1.00 21.34 ? 391 ARG A CZ 1 ATOM 2704 N NH1 . ARG A 1 356 ? 18.333 -6.272 45.618 1.00 21.54 ? 391 ARG A NH1 1 ATOM 2705 N NH2 . ARG A 1 356 ? 20.538 -6.788 46.008 1.00 21.90 ? 391 ARG A NH2 1 ATOM 2706 N N . ILE A 1 357 ? 17.847 -8.179 53.151 1.00 19.42 ? 392 ILE A N 1 ATOM 2707 C CA . ILE A 1 357 ? 18.558 -8.094 54.413 1.00 20.13 ? 392 ILE A CA 1 ATOM 2708 C C . ILE A 1 357 ? 19.553 -9.232 54.510 1.00 20.11 ? 392 ILE A C 1 ATOM 2709 O O . ILE A 1 357 ? 19.213 -10.386 54.257 1.00 19.64 ? 392 ILE A O 1 ATOM 2710 C CB . ILE A 1 357 ? 17.584 -8.165 55.617 1.00 20.37 ? 392 ILE A CB 1 ATOM 2711 C CG1 . ILE A 1 357 ? 16.704 -6.912 55.661 1.00 20.07 ? 392 ILE A CG1 1 ATOM 2712 C CG2 . ILE A 1 357 ? 18.353 -8.287 56.925 1.00 21.55 ? 392 ILE A CG2 1 ATOM 2713 C CD1 . ILE A 1 357 ? 15.564 -6.989 56.659 1.00 20.92 ? 392 ILE A CD1 1 ATOM 2714 N N . ARG A 1 358 ? 20.767 -8.901 54.946 1.00 22.92 ? 393 ARG A N 1 ATOM 2715 C CA . ARG A 1 358 ? 21.739 -9.918 55.353 1.00 25.17 ? 393 ARG A CA 1 ATOM 2716 C C . ARG A 1 358 ? 22.523 -9.432 56.582 1.00 26.74 ? 393 ARG A C 1 ATOM 2717 O O . ARG A 1 358 ? 22.395 -8.274 56.996 1.00 27.71 ? 393 ARG A O 1 ATOM 2718 C CB . ARG A 1 358 ? 22.705 -10.242 54.200 1.00 25.70 ? 393 ARG A CB 1 ATOM 2719 C CG . ARG A 1 358 ? 23.563 -9.065 53.767 1.00 25.95 ? 393 ARG A CG 1 ATOM 2720 C CD . ARG A 1 358 ? 24.334 -9.333 52.478 1.00 27.18 ? 393 ARG A CD 1 ATOM 2721 N NE . ARG A 1 358 ? 25.238 -8.218 52.205 1.00 27.80 ? 393 ARG A NE 1 ATOM 2722 C CZ . ARG A 1 358 ? 25.012 -7.190 51.384 1.00 28.46 ? 393 ARG A CZ 1 ATOM 2723 N NH1 . ARG A 1 358 ? 23.894 -7.070 50.650 1.00 26.33 ? 393 ARG A NH1 1 ATOM 2724 N NH2 . ARG A 1 358 ? 25.949 -6.249 51.291 1.00 30.91 ? 393 ARG A NH2 1 ATOM 2725 N N . ALA A 1 359 ? 23.344 -10.314 57.144 1.00 29.81 ? 394 ALA A N 1 ATOM 2726 C CA . ALA A 1 359 ? 24.172 -9.955 58.313 1.00 32.41 ? 394 ALA A CA 1 ATOM 2727 C C . ALA A 1 359 ? 25.223 -8.913 57.933 1.00 36.16 ? 394 ALA A C 1 ATOM 2728 O O . ALA A 1 359 ? 25.841 -9.025 56.873 1.00 36.07 ? 394 ALA A O 1 ATOM 2729 C CB . ALA A 1 359 ? 24.848 -11.186 58.875 1.00 34.31 ? 394 ALA A CB 1 ATOM 2730 N N . LYS A 1 360 ? 25.433 -7.902 58.776 1.00 38.86 ? 395 LYS A N 1 ATOM 2731 C CA . LYS A 1 360 ? 26.514 -6.936 58.514 1.00 45.50 ? 395 LYS A CA 1 ATOM 2732 C C . LYS A 1 360 ? 27.883 -7.630 58.553 1.00 49.42 ? 395 LYS A C 1 ATOM 2733 O O . LYS A 1 360 ? 28.752 -7.331 57.730 1.00 51.91 ? 395 LYS A O 1 ATOM 2734 C CB . LYS A 1 360 ? 26.488 -5.746 59.474 1.00 49.86 ? 395 LYS A CB 1 ATOM 2735 C CG . LYS A 1 360 ? 27.378 -4.602 58.997 1.00 53.03 ? 395 LYS A CG 1 ATOM 2736 C CD . LYS A 1 360 ? 27.384 -3.410 59.936 1.00 57.60 ? 395 LYS A CD 1 ATOM 2737 C CE . LYS A 1 360 ? 26.311 -2.393 59.579 1.00 60.45 ? 395 LYS A CE 1 ATOM 2738 N NZ . LYS A 1 360 ? 26.305 -1.249 60.534 1.00 64.39 ? 395 LYS A NZ 1 ATOM 2739 N N . SER A 1 361 ? 28.066 -8.553 59.497 1.00 53.17 ? 396 SER A N 1 ATOM 2740 C CA . SER A 1 361 ? 29.280 -9.357 59.562 1.00 59.81 ? 396 SER A CA 1 ATOM 2741 C C . SER A 1 361 ? 28.942 -10.842 59.547 1.00 62.58 ? 396 SER A C 1 ATOM 2742 O O . SER A 1 361 ? 28.061 -11.292 60.284 1.00 59.99 ? 396 SER A O 1 ATOM 2743 C CB . SER A 1 361 ? 30.078 -9.015 60.819 1.00 63.09 ? 396 SER A CB 1 ATOM 2744 O OG . SER A 1 361 ? 31.239 -9.821 60.911 1.00 67.23 ? 396 SER A OG 1 ATOM 2745 N N . ILE A 1 362 ? 29.657 -11.592 58.706 1.00 71.67 ? 397 ILE A N 1 ATOM 2746 C CA . ILE A 1 362 ? 29.606 -13.069 58.714 1.00 80.01 ? 397 ILE A CA 1 ATOM 2747 C C . ILE A 1 362 ? 30.061 -13.670 60.055 1.00 86.03 ? 397 ILE A C 1 ATOM 2748 O O . ILE A 1 362 ? 29.592 -14.741 60.443 1.00 90.54 ? 397 ILE A O 1 ATOM 2749 C CB . ILE A 1 362 ? 30.424 -13.713 57.552 1.00 81.50 ? 397 ILE A CB 1 ATOM 2750 C CG1 . ILE A 1 362 ? 31.928 -13.373 57.636 1.00 84.21 ? 397 ILE A CG1 1 ATOM 2751 C CG2 . ILE A 1 362 ? 29.846 -13.306 56.201 1.00 79.98 ? 397 ILE A CG2 1 ATOM 2752 C CD1 . ILE A 1 362 ? 32.792 -14.131 56.647 1.00 85.74 ? 397 ILE A CD1 1 ATOM 2753 N N . ASN A 1 363 ? 30.955 -12.968 60.757 1.00 88.38 ? 398 ASN A N 1 ATOM 2754 C CA . ASN A 1 363 ? 31.449 -13.392 62.077 1.00 93.11 ? 398 ASN A CA 1 ATOM 2755 C C . ASN A 1 363 ? 30.428 -13.267 63.217 1.00 96.40 ? 398 ASN A C 1 ATOM 2756 O O . ASN A 1 363 ? 30.675 -13.748 64.328 1.00 96.15 ? 398 ASN A O 1 ATOM 2757 C CB . ASN A 1 363 ? 32.711 -12.603 62.447 1.00 95.69 ? 398 ASN A CB 1 ATOM 2758 C CG . ASN A 1 363 ? 33.830 -12.772 61.431 1.00 100.04 ? 398 ASN A CG 1 ATOM 2759 O OD1 . ASN A 1 363 ? 33.919 -13.796 60.751 1.00 100.37 ? 398 ASN A OD1 1 ATOM 2760 N ND2 . ASN A 1 363 ? 34.689 -11.762 61.319 1.00 103.32 ? 398 ASN A ND2 1 ATOM 2761 N N . ASN A 1 364 ? 29.302 -12.608 62.947 1.00 94.77 ? 399 ASN A N 1 ATOM 2762 C CA . ASN A 1 364 ? 28.196 -12.501 63.897 1.00 91.91 ? 399 ASN A CA 1 ATOM 2763 C C . ASN A 1 364 ? 27.606 -13.883 64.228 1.00 89.42 ? 399 ASN A C 1 ATOM 2764 O O . ASN A 1 364 ? 27.300 -14.661 63.321 1.00 85.66 ? 399 ASN A O 1 ATOM 2765 C CB . ASN A 1 364 ? 27.118 -11.569 63.317 1.00 88.37 ? 399 ASN A CB 1 ATOM 2766 C CG . ASN A 1 364 ? 26.146 -11.053 64.367 1.00 84.35 ? 399 ASN A CG 1 ATOM 2767 O OD1 . ASN A 1 364 ? 25.425 -11.830 64.981 1.00 79.45 ? 399 ASN A OD1 1 ATOM 2768 N ND2 . ASN A 1 364 ? 26.099 -9.735 64.557 1.00 83.81 ? 399 ASN A ND2 1 ATOM 2769 N N . SER A 1 365 ? 27.496 -14.184 65.526 1.00 88.69 ? 400 SER A N 1 ATOM 2770 C CA . SER A 1 365 ? 26.786 -15.373 66.033 1.00 85.86 ? 400 SER A CA 1 ATOM 2771 C C . SER A 1 365 ? 25.395 -15.052 66.625 1.00 82.13 ? 400 SER A C 1 ATOM 2772 O O . SER A 1 365 ? 24.651 -15.967 66.984 1.00 77.04 ? 400 SER A O 1 ATOM 2773 C CB . SER A 1 365 ? 27.644 -16.082 67.088 1.00 85.98 ? 400 SER A CB 1 ATOM 2774 O OG . SER A 1 365 ? 27.809 -15.286 68.250 1.00 84.28 ? 400 SER A OG 1 ATOM 2775 N N . LYS A 1 366 ? 25.065 -13.760 66.716 1.00 80.09 ? 401 LYS A N 1 ATOM 2776 C CA . LYS A 1 366 ? 23.801 -13.259 67.285 1.00 76.88 ? 401 LYS A CA 1 ATOM 2777 C C . LYS A 1 366 ? 22.670 -13.226 66.230 1.00 76.35 ? 401 LYS A C 1 ATOM 2778 O O . LYS A 1 366 ? 21.499 -13.458 66.551 1.00 74.59 ? 401 LYS A O 1 ATOM 2779 C CB . LYS A 1 366 ? 24.028 -11.845 67.867 1.00 74.88 ? 401 LYS A CB 1 ATOM 2780 C CG . LYS A 1 366 ? 23.320 -11.546 69.181 1.00 76.35 ? 401 LYS A CG 1 ATOM 2781 C CD . LYS A 1 366 ? 21.884 -11.087 68.983 1.00 77.02 ? 401 LYS A CD 1 ATOM 2782 C CE . LYS A 1 366 ? 21.153 -10.967 70.311 1.00 78.70 ? 401 LYS A CE 1 ATOM 2783 N NZ . LYS A 1 366 ? 20.843 -12.292 70.922 1.00 79.93 ? 401 LYS A NZ 1 ATOM 2784 N N . TYR A 1 367 ? 23.041 -12.937 64.980 1.00 71.38 ? 402 TYR A N 1 ATOM 2785 C CA . TYR A 1 367 ? 22.109 -12.801 63.854 1.00 65.04 ? 402 TYR A CA 1 ATOM 2786 C C . TYR A 1 367 ? 21.399 -14.125 63.558 1.00 62.37 ? 402 TYR A C 1 ATOM 2787 O O . TYR A 1 367 ? 22.042 -15.088 63.128 1.00 68.98 ? 402 TYR A O 1 ATOM 2788 C CB . TYR A 1 367 ? 22.887 -12.310 62.613 1.00 62.58 ? 402 TYR A CB 1 ATOM 2789 C CG . TYR A 1 367 ? 22.109 -12.213 61.310 1.00 58.76 ? 402 TYR A CG 1 ATOM 2790 C CD1 . TYR A 1 367 ? 21.441 -11.037 60.956 1.00 59.12 ? 402 TYR A CD1 1 ATOM 2791 C CD2 . TYR A 1 367 ? 22.075 -13.283 60.410 1.00 55.83 ? 402 TYR A CD2 1 ATOM 2792 C CE1 . TYR A 1 367 ? 20.744 -10.940 59.756 1.00 54.62 ? 402 TYR A CE1 1 ATOM 2793 C CE2 . TYR A 1 367 ? 21.378 -13.197 59.212 1.00 52.74 ? 402 TYR A CE2 1 ATOM 2794 C CZ . TYR A 1 367 ? 20.719 -12.022 58.890 1.00 51.93 ? 402 TYR A CZ 1 ATOM 2795 O OH . TYR A 1 367 ? 20.034 -11.920 57.712 1.00 43.97 ? 402 TYR A OH 1 ATOM 2796 N N . ASP A 1 368 ? 20.086 -14.163 63.804 1.00 51.89 ? 403 ASP A N 1 ATOM 2797 C CA . ASP A 1 368 ? 19.243 -15.319 63.495 1.00 49.40 ? 403 ASP A CA 1 ATOM 2798 C C . ASP A 1 368 ? 18.167 -14.842 62.511 1.00 46.72 ? 403 ASP A C 1 ATOM 2799 O O . ASP A 1 368 ? 17.288 -14.054 62.882 1.00 41.88 ? 403 ASP A O 1 ATOM 2800 C CB . ASP A 1 368 ? 18.598 -15.883 64.766 1.00 50.69 ? 403 ASP A CB 1 ATOM 2801 C CG . ASP A 1 368 ? 17.794 -17.167 64.526 1.00 52.58 ? 403 ASP A CG 1 ATOM 2802 O OD1 . ASP A 1 368 ? 17.598 -17.604 63.370 1.00 56.31 ? 403 ASP A OD1 1 ATOM 2803 O OD2 . ASP A 1 368 ? 17.346 -17.762 65.526 1.00 61.12 ? 403 ASP A OD2 1 ATOM 2804 N N . PRO A 1 369 ? 18.214 -15.329 61.263 1.00 43.45 ? 404 PRO A N 1 ATOM 2805 C CA . PRO A 1 369 ? 17.266 -14.829 60.271 1.00 42.27 ? 404 PRO A CA 1 ATOM 2806 C C . PRO A 1 369 ? 15.802 -15.177 60.580 1.00 40.33 ? 404 PRO A C 1 ATOM 2807 O O . PRO A 1 369 ? 14.908 -14.469 60.124 1.00 37.38 ? 404 PRO A O 1 ATOM 2808 C CB . PRO A 1 369 ? 17.744 -15.480 58.976 1.00 43.25 ? 404 PRO A CB 1 ATOM 2809 C CG . PRO A 1 369 ? 18.365 -16.748 59.413 1.00 43.89 ? 404 PRO A CG 1 ATOM 2810 C CD . PRO A 1 369 ? 19.019 -16.441 60.730 1.00 46.45 ? 404 PRO A CD 1 ATOM 2811 N N . LYS A 1 370 ? 15.569 -16.232 61.364 1.00 40.21 ? 405 LYS A N 1 ATOM 2812 C CA . LYS A 1 370 ? 14.223 -16.555 61.847 1.00 39.34 ? 405 LYS A CA 1 ATOM 2813 C C . LYS A 1 370 ? 13.697 -15.506 62.806 1.00 36.22 ? 405 LYS A C 1 ATOM 2814 O O . LYS A 1 370 ? 12.502 -15.198 62.769 1.00 33.01 ? 405 LYS A O 1 ATOM 2815 C CB . LYS A 1 370 ? 14.179 -17.922 62.541 1.00 43.76 ? 405 LYS A CB 1 ATOM 2816 C CG . LYS A 1 370 ? 14.338 -19.095 61.594 1.00 46.20 ? 405 LYS A CG 1 ATOM 2817 C CD . LYS A 1 370 ? 14.277 -20.414 62.357 1.00 50.45 ? 405 LYS A CD 1 ATOM 2818 C CE . LYS A 1 370 ? 14.600 -21.594 61.458 1.00 53.26 ? 405 LYS A CE 1 ATOM 2819 N NZ . LYS A 1 370 ? 15.998 -21.551 60.940 1.00 55.54 ? 405 LYS A NZ 1 ATOM 2820 N N . THR A 1 371 ? 14.569 -14.980 63.673 1.00 35.53 ? 406 THR A N 1 ATOM 2821 C CA . THR A 1 371 ? 14.147 -13.941 64.619 1.00 36.00 ? 406 THR A CA 1 ATOM 2822 C C . THR A 1 371 ? 13.865 -12.633 63.868 1.00 31.40 ? 406 THR A C 1 ATOM 2823 O O . THR A 1 371 ? 12.956 -11.908 64.235 1.00 28.96 ? 406 THR A O 1 ATOM 2824 C CB . THR A 1 371 ? 15.134 -13.722 65.792 1.00 39.32 ? 406 THR A CB 1 ATOM 2825 O OG1 . THR A 1 371 ? 16.398 -13.274 65.299 1.00 44.78 ? 406 THR A OG1 1 ATOM 2826 C CG2 . THR A 1 371 ? 15.330 -15.007 66.567 1.00 40.79 ? 406 THR A CG2 1 ATOM 2827 N N . ILE A 1 372 ? 14.612 -12.371 62.792 1.00 28.81 ? 407 ILE A N 1 ATOM 2828 C CA . ILE A 1 372 ? 14.405 -11.164 61.999 1.00 26.33 ? 407 ILE A CA 1 ATOM 2829 C C . ILE A 1 372 ? 13.047 -11.202 61.341 1.00 23.64 ? 407 ILE A C 1 ATOM 2830 O O . ILE A 1 372 ? 12.280 -10.247 61.453 1.00 23.55 ? 407 ILE A O 1 ATOM 2831 C CB . ILE A 1 372 ? 15.483 -10.971 60.920 1.00 27.07 ? 407 ILE A CB 1 ATOM 2832 C CG1 . ILE A 1 372 ? 16.873 -10.864 61.552 1.00 30.16 ? 407 ILE A CG1 1 ATOM 2833 C CG2 . ILE A 1 372 ? 15.185 -9.732 60.081 1.00 26.28 ? 407 ILE A CG2 1 ATOM 2834 C CD1 . ILE A 1 372 ? 16.956 -9.899 62.703 1.00 32.89 ? 407 ILE A CD1 1 ATOM 2835 N N . ILE A 1 373 ? 12.745 -12.315 60.680 1.00 23.42 ? 408 ILE A N 1 ATOM 2836 C CA . ILE A 1 373 ? 11.468 -12.466 59.959 1.00 23.34 ? 408 ILE A CA 1 ATOM 2837 C C . ILE A 1 373 ? 10.308 -12.320 60.942 1.00 22.49 ? 408 ILE A C 1 ATOM 2838 O O . ILE A 1 373 ? 9.375 -11.552 60.705 1.00 20.73 ? 408 ILE A O 1 ATOM 2839 C CB . ILE A 1 373 ? 11.371 -13.830 59.249 1.00 26.08 ? 408 ILE A CB 1 ATOM 2840 C CG1 . ILE A 1 373 ? 12.395 -13.910 58.104 1.00 27.23 ? 408 ILE A CG1 1 ATOM 2841 C CG2 . ILE A 1 373 ? 9.957 -14.090 58.726 1.00 26.33 ? 408 ILE A CG2 1 ATOM 2842 C CD1 . ILE A 1 373 ? 12.046 -13.138 56.855 1.00 28.38 ? 408 ILE A CD1 1 ATOM 2843 N N . ALA A 1 374 ? 10.425 -13.014 62.068 1.00 22.90 ? 409 ALA A N 1 ATOM 2844 C CA . ALA A 1 374 ? 9.407 -12.962 63.117 1.00 23.28 ? 409 ALA A CA 1 ATOM 2845 C C . ALA A 1 374 ? 9.195 -11.541 63.644 1.00 22.59 ? 409 ALA A C 1 ATOM 2846 O O . ALA A 1 374 ? 8.045 -11.114 63.844 1.00 21.53 ? 409 ALA A O 1 ATOM 2847 C CB . ALA A 1 374 ? 9.750 -13.916 64.254 1.00 24.25 ? 409 ALA A CB 1 ATOM 2848 N N . ALA A 1 375 ? 10.290 -10.794 63.807 1.00 21.55 ? 410 ALA A N 1 ATOM 2849 C CA . ALA A 1 375 ? 10.200 -9.413 64.304 1.00 21.76 ? 410 ALA A CA 1 ATOM 2850 C C . ALA A 1 375 ? 9.607 -8.447 63.291 1.00 20.76 ? 410 ALA A C 1 ATOM 2851 O O . ALA A 1 375 ? 9.226 -7.341 63.663 1.00 20.80 ? 410 ALA A O 1 ATOM 2852 C CB . ALA A 1 375 ? 11.565 -8.914 64.731 1.00 23.01 ? 410 ALA A CB 1 ATOM 2853 N N . LEU A 1 376 ? 9.583 -8.837 62.013 1.00 18.68 ? 411 LEU A N 1 ATOM 2854 C CA . LEU A 1 376 ? 8.992 -8.029 60.969 1.00 19.24 ? 411 LEU A CA 1 ATOM 2855 C C . LEU A 1 376 ? 7.594 -8.490 60.526 1.00 19.00 ? 411 LEU A C 1 ATOM 2856 O O . LEU A 1 376 ? 7.024 -7.931 59.599 1.00 19.17 ? 411 LEU A O 1 ATOM 2857 C CB . LEU A 1 376 ? 9.963 -8.015 59.784 1.00 18.28 ? 411 LEU A CB 1 ATOM 2858 C CG . LEU A 1 376 ? 11.335 -7.411 60.087 1.00 18.59 ? 411 LEU A CG 1 ATOM 2859 C CD1 . LEU A 1 376 ? 12.265 -7.654 58.923 1.00 19.02 ? 411 LEU A CD1 1 ATOM 2860 C CD2 . LEU A 1 376 ? 11.223 -5.924 60.384 1.00 19.23 ? 411 LEU A CD2 1 ATOM 2861 N N . THR A 1 377 ? 7.022 -9.482 61.204 1.00 19.06 ? 412 THR A N 1 ATOM 2862 C CA . THR A 1 377 ? 5.770 -10.083 60.746 1.00 19.33 ? 412 THR A CA 1 ATOM 2863 C C . THR A 1 377 ? 4.570 -9.490 61.488 1.00 20.37 ? 412 THR A C 1 ATOM 2864 O O . THR A 1 377 ? 4.421 -9.692 62.712 1.00 20.01 ? 412 THR A O 1 ATOM 2865 C CB . THR A 1 377 ? 5.809 -11.609 60.936 1.00 19.96 ? 412 THR A CB 1 ATOM 2866 O OG1 . THR A 1 377 ? 6.834 -12.133 60.085 1.00 20.45 ? 412 THR A OG1 1 ATOM 2867 C CG2 . THR A 1 377 ? 4.483 -12.258 60.587 1.00 20.03 ? 412 THR A CG2 1 ATOM 2868 N N . CYS A 1 378 ? 3.744 -8.762 60.737 1.00 19.99 ? 413 CYS A N 1 ATOM 2869 C CA . CYS A 1 378 ? 2.469 -8.214 61.196 1.00 21.30 ? 413 CYS A CA 1 ATOM 2870 C C . CYS A 1 378 ? 2.568 -7.506 62.546 1.00 22.92 ? 413 CYS A C 1 ATOM 2871 O O . CYS A 1 378 ? 1.769 -7.776 63.445 1.00 22.95 ? 413 CYS A O 1 ATOM 2872 C CB . CYS A 1 378 ? 1.392 -9.331 61.250 1.00 21.84 ? 413 CYS A CB 1 ATOM 2873 S SG . CYS A 1 378 ? 1.235 -10.359 59.774 1.00 25.29 ? 413 CYS A SG 1 ATOM 2874 N N . LYS A 1 379 ? 3.555 -6.620 62.696 1.00 23.94 ? 414 LYS A N 1 ATOM 2875 C CA . LYS A 1 379 ? 3.808 -5.956 63.982 1.00 25.68 ? 414 LYS A CA 1 ATOM 2876 C C . LYS A 1 379 ? 3.080 -4.645 64.186 1.00 26.95 ? 414 LYS A C 1 ATOM 2877 O O . LYS A 1 379 ? 2.824 -4.272 65.324 1.00 29.07 ? 414 LYS A O 1 ATOM 2878 C CB . LYS A 1 379 ? 5.298 -5.765 64.208 1.00 26.57 ? 414 LYS A CB 1 ATOM 2879 C CG . LYS A 1 379 ? 6.054 -7.060 64.396 1.00 27.67 ? 414 LYS A CG 1 ATOM 2880 C CD . LYS A 1 379 ? 5.639 -7.786 65.657 1.00 29.61 ? 414 LYS A CD 1 ATOM 2881 C CE . LYS A 1 379 ? 6.357 -9.102 65.807 1.00 30.43 ? 414 LYS A CE 1 ATOM 2882 N NZ . LYS A 1 379 ? 6.107 -9.618 67.163 1.00 31.20 ? 414 LYS A NZ 1 ATOM 2883 N N . LYS A 1 380 ? 2.739 -3.953 63.113 1.00 27.17 ? 415 LYS A N 1 ATOM 2884 C CA . LYS A 1 380 ? 1.911 -2.753 63.180 1.00 28.30 ? 415 LYS A CA 1 ATOM 2885 C C . LYS A 1 380 ? 0.709 -2.948 62.278 1.00 28.41 ? 415 LYS A C 1 ATOM 2886 O O . LYS A 1 380 ? 0.851 -3.507 61.197 1.00 25.02 ? 415 LYS A O 1 ATOM 2887 C CB . LYS A 1 380 ? 2.725 -1.553 62.727 1.00 30.57 ? 415 LYS A CB 1 ATOM 2888 C CG . LYS A 1 380 ? 3.928 -1.309 63.623 1.00 33.71 ? 415 LYS A CG 1 ATOM 2889 C CD . LYS A 1 380 ? 4.559 0.035 63.335 1.00 37.59 ? 415 LYS A CD 1 ATOM 2890 C CE . LYS A 1 380 ? 5.594 0.394 64.379 1.00 43.08 ? 415 LYS A CE 1 ATOM 2891 N NZ . LYS A 1 380 ? 5.878 1.851 64.314 1.00 46.71 ? 415 LYS A NZ 1 ATOM 2892 N N . PRO A 1 381 ? -0.486 -2.497 62.695 1.00 29.74 ? 416 PRO A N 1 ATOM 2893 C CA . PRO A 1 381 ? -1.689 -2.756 61.873 1.00 31.52 ? 416 PRO A CA 1 ATOM 2894 C C . PRO A 1 381 ? -1.652 -2.262 60.426 1.00 35.15 ? 416 PRO A C 1 ATOM 2895 O O . PRO A 1 381 ? -2.221 -2.904 59.549 1.00 36.96 ? 416 PRO A O 1 ATOM 2896 C CB . PRO A 1 381 ? -2.814 -2.031 62.642 1.00 33.52 ? 416 PRO A CB 1 ATOM 2897 C CG . PRO A 1 381 ? -2.276 -1.820 64.012 1.00 33.44 ? 416 PRO A CG 1 ATOM 2898 C CD . PRO A 1 381 ? -0.798 -1.638 63.856 1.00 32.40 ? 416 PRO A CD 1 ATOM 2899 N N . ASP A 1 382 ? -0.997 -1.132 60.178 1.00 34.09 ? 417 ASP A N 1 ATOM 2900 C CA . ASP A 1 382 ? -0.932 -0.572 58.827 1.00 36.20 ? 417 ASP A CA 1 ATOM 2901 C C . ASP A 1 382 ? 0.468 -0.751 58.205 1.00 32.22 ? 417 ASP A C 1 ATOM 2902 O O . ASP A 1 382 ? 0.829 -0.012 57.295 1.00 34.61 ? 417 ASP A O 1 ATOM 2903 C CB . ASP A 1 382 ? -1.364 0.905 58.849 1.00 41.48 ? 417 ASP A CB 1 ATOM 2904 C CG . ASP A 1 382 ? -0.494 1.767 59.754 1.00 48.03 ? 417 ASP A CG 1 ATOM 2905 O OD1 . ASP A 1 382 ? 0.196 1.217 60.651 1.00 50.84 ? 417 ASP A OD1 1 ATOM 2906 O OD2 . ASP A 1 382 ? -0.510 3.007 59.573 1.00 58.27 ? 417 ASP A OD2 1 ATOM 2907 N N . GLN A 1 383 ? 1.230 -1.746 58.675 1.00 27.25 ? 418 GLN A N 1 ATOM 2908 C CA . GLN A 1 383 ? 2.596 -2.025 58.183 1.00 24.68 ? 418 GLN A CA 1 ATOM 2909 C C . GLN A 1 383 ? 2.627 -2.054 56.661 1.00 21.91 ? 418 GLN A C 1 ATOM 2910 O O . GLN A 1 383 ? 1.840 -2.760 56.039 1.00 23.18 ? 418 GLN A O 1 ATOM 2911 C CB . GLN A 1 383 ? 3.031 -3.382 58.704 1.00 24.03 ? 418 GLN A CB 1 ATOM 2912 C CG . GLN A 1 383 ? 4.476 -3.721 58.569 1.00 23.57 ? 418 GLN A CG 1 ATOM 2913 C CD . GLN A 1 383 ? 4.780 -5.020 59.271 1.00 22.90 ? 418 GLN A CD 1 ATOM 2914 O OE1 . GLN A 1 383 ? 4.480 -5.184 60.468 1.00 25.14 ? 418 GLN A OE1 1 ATOM 2915 N NE2 . GLN A 1 383 ? 5.370 -5.943 58.557 1.00 23.30 ? 418 GLN A NE2 1 ATOM 2916 N N . HIS A 1 384 ? 3.547 -1.306 56.067 1.00 20.76 ? 419 HIS A N 1 ATOM 2917 C CA . HIS A 1 384 ? 3.574 -1.108 54.603 1.00 19.36 ? 419 HIS A CA 1 ATOM 2918 C C . HIS A 1 384 ? 4.622 -1.930 53.895 1.00 18.58 ? 419 HIS A C 1 ATOM 2919 O O . HIS A 1 384 ? 5.081 -1.554 52.815 1.00 17.79 ? 419 HIS A O 1 ATOM 2920 C CB . HIS A 1 384 ? 3.746 0.381 54.291 1.00 20.04 ? 419 HIS A CB 1 ATOM 2921 C CG . HIS A 1 384 ? 2.686 1.230 54.903 1.00 23.22 ? 419 HIS A CG 1 ATOM 2922 N ND1 . HIS A 1 384 ? 1.439 1.382 54.333 1.00 24.14 ? 419 HIS A ND1 1 ATOM 2923 C CD2 . HIS A 1 384 ? 2.665 1.937 56.056 1.00 24.38 ? 419 HIS A CD2 1 ATOM 2924 C CE1 . HIS A 1 384 ? 0.703 2.163 55.101 1.00 24.61 ? 419 HIS A CE1 1 ATOM 2925 N NE2 . HIS A 1 384 ? 1.424 2.517 56.148 1.00 25.47 ? 419 HIS A NE2 1 ATOM 2926 N N . PHE A 1 385 ? 4.986 -3.069 54.476 1.00 18.03 ? 420 PHE A N 1 ATOM 2927 C CA . PHE A 1 385 ? 5.803 -4.061 53.819 1.00 17.23 ? 420 PHE A CA 1 ATOM 2928 C C . PHE A 1 385 ? 5.540 -5.428 54.455 1.00 16.88 ? 420 PHE A C 1 ATOM 2929 O O . PHE A 1 385 ? 4.944 -5.519 55.520 1.00 15.81 ? 420 PHE A O 1 ATOM 2930 C CB . PHE A 1 385 ? 7.283 -3.711 53.958 1.00 17.90 ? 420 PHE A CB 1 ATOM 2931 C CG . PHE A 1 385 ? 7.758 -3.747 55.381 1.00 18.83 ? 420 PHE A CG 1 ATOM 2932 C CD1 . PHE A 1 385 ? 7.623 -2.633 56.191 1.00 20.39 ? 420 PHE A CD1 1 ATOM 2933 C CD2 . PHE A 1 385 ? 8.334 -4.895 55.908 1.00 19.43 ? 420 PHE A CD2 1 ATOM 2934 C CE1 . PHE A 1 385 ? 8.027 -2.676 57.523 1.00 21.42 ? 420 PHE A CE1 1 ATOM 2935 C CE2 . PHE A 1 385 ? 8.723 -4.949 57.242 1.00 20.30 ? 420 PHE A CE2 1 ATOM 2936 C CZ . PHE A 1 385 ? 8.586 -3.830 58.038 1.00 20.70 ? 420 PHE A CZ 1 ATOM 2937 N N . LYS A 1 386 ? 5.994 -6.489 53.796 1.00 16.30 ? 421 LYS A N 1 ATOM 2938 C CA . LYS A 1 386 ? 5.805 -7.840 54.312 1.00 15.91 ? 421 LYS A CA 1 ATOM 2939 C C . LYS A 1 386 ? 7.117 -8.574 54.099 1.00 15.48 ? 421 LYS A C 1 ATOM 2940 O O . LYS A 1 386 ? 7.645 -8.566 52.982 1.00 16.19 ? 421 LYS A O 1 ATOM 2941 C CB . LYS A 1 386 ? 4.636 -8.557 53.602 1.00 16.21 ? 421 LYS A CB 1 ATOM 2942 C CG . LYS A 1 386 ? 4.400 -9.991 54.079 1.00 16.01 ? 421 LYS A CG 1 ATOM 2943 C CD . LYS A 1 386 ? 3.201 -10.721 53.486 1.00 15.90 ? 421 LYS A CD 1 ATOM 2944 C CE . LYS A 1 386 ? 1.879 -10.000 53.582 1.00 17.14 ? 421 LYS A CE 1 ATOM 2945 N NZ . LYS A 1 386 ? 1.531 -9.720 54.997 1.00 17.83 ? 421 LYS A NZ 1 ATOM 2946 N N . PRO A 1 387 ? 7.659 -9.207 55.162 1.00 16.40 ? 422 PRO A N 1 ATOM 2947 C CA . PRO A 1 387 ? 8.879 -10.008 55.017 1.00 16.38 ? 422 PRO A CA 1 ATOM 2948 C C . PRO A 1 387 ? 8.587 -11.408 54.482 1.00 16.67 ? 422 PRO A C 1 ATOM 2949 O O . PRO A 1 387 ? 7.530 -12.011 54.777 1.00 16.66 ? 422 PRO A O 1 ATOM 2950 C CB . PRO A 1 387 ? 9.393 -10.107 56.456 1.00 17.29 ? 422 PRO A CB 1 ATOM 2951 C CG . PRO A 1 387 ? 8.128 -10.176 57.255 1.00 17.90 ? 422 PRO A CG 1 ATOM 2952 C CD . PRO A 1 387 ? 7.148 -9.277 56.551 1.00 17.86 ? 422 PRO A CD 1 ATOM 2953 N N . TYR A 1 388 ? 9.534 -11.938 53.723 1.00 16.15 ? 423 TYR A N 1 ATOM 2954 C CA . TYR A 1 388 ? 9.475 -13.290 53.207 1.00 16.34 ? 423 TYR A CA 1 ATOM 2955 C C . TYR A 1 388 ? 10.864 -13.889 53.226 1.00 17.35 ? 423 TYR A C 1 ATOM 2956 O O . TYR A 1 388 ? 11.837 -13.215 52.869 1.00 18.16 ? 423 TYR A O 1 ATOM 2957 C CB . TYR A 1 388 ? 9.079 -13.274 51.720 1.00 15.77 ? 423 TYR A CB 1 ATOM 2958 C CG . TYR A 1 388 ? 7.650 -12.968 51.386 1.00 15.31 ? 423 TYR A CG 1 ATOM 2959 C CD1 . TYR A 1 388 ? 7.184 -11.661 51.317 1.00 15.36 ? 423 TYR A CD1 1 ATOM 2960 C CD2 . TYR A 1 388 ? 6.763 -13.983 51.095 1.00 16.15 ? 423 TYR A CD2 1 ATOM 2961 C CE1 . TYR A 1 388 ? 5.863 -11.389 50.989 1.00 16.33 ? 423 TYR A CE1 1 ATOM 2962 C CE2 . TYR A 1 388 ? 5.442 -13.729 50.762 1.00 16.10 ? 423 TYR A CE2 1 ATOM 2963 C CZ . TYR A 1 388 ? 4.987 -12.428 50.705 1.00 15.95 ? 423 TYR A CZ 1 ATOM 2964 O OH . TYR A 1 388 ? 3.672 -12.193 50.354 1.00 17.15 ? 423 TYR A OH 1 ATOM 2965 N N . MET A 1 389 ? 10.977 -15.163 53.568 1.00 17.35 ? 424 MET A N 1 ATOM 2966 C CA . MET A 1 389 ? 12.142 -15.915 53.106 1.00 18.26 ? 424 MET A CA 1 ATOM 2967 C C . MET A 1 389 ? 11.985 -16.042 51.576 1.00 16.99 ? 424 MET A C 1 ATOM 2968 O O . MET A 1 389 ? 10.860 -16.256 51.070 1.00 16.74 ? 424 MET A O 1 ATOM 2969 C CB . MET A 1 389 ? 12.214 -17.271 53.778 1.00 19.38 ? 424 MET A CB 1 ATOM 2970 C CG . MET A 1 389 ? 12.614 -17.173 55.248 1.00 22.39 ? 424 MET A CG 1 ATOM 2971 S SD . MET A 1 389 ? 14.310 -16.596 55.521 1.00 26.56 ? 424 MET A SD 1 ATOM 2972 C CE . MET A 1 389 ? 15.176 -18.051 54.950 1.00 27.68 ? 424 MET A CE 1 ATOM 2973 N N . LYS A 1 390 ? 13.082 -15.902 50.827 1.00 16.15 ? 425 LYS A N 1 ATOM 2974 C CA . LYS A 1 390 ? 12.960 -15.800 49.368 1.00 16.12 ? 425 LYS A CA 1 ATOM 2975 C C . LYS A 1 390 ? 12.234 -16.972 48.722 1.00 16.34 ? 425 LYS A C 1 ATOM 2976 O O . LYS A 1 390 ? 11.489 -16.771 47.757 1.00 15.64 ? 425 LYS A O 1 ATOM 2977 C CB . LYS A 1 390 ? 14.303 -15.544 48.714 1.00 15.77 ? 425 LYS A CB 1 ATOM 2978 C CG . LYS A 1 390 ? 15.308 -16.673 48.827 1.00 15.86 ? 425 LYS A CG 1 ATOM 2979 C CD . LYS A 1 390 ? 16.642 -16.286 48.202 1.00 15.81 ? 425 LYS A CD 1 ATOM 2980 C CE . LYS A 1 390 ? 17.625 -17.461 48.180 1.00 16.18 ? 425 LYS A CE 1 ATOM 2981 N NZ . LYS A 1 390 ? 18.806 -17.112 47.325 1.00 16.99 ? 425 LYS A NZ 1 ATOM 2982 N N . GLN A 1 391 ? 12.379 -18.179 49.276 1.00 16.86 ? 426 GLN A N 1 ATOM 2983 C CA . GLN A 1 391 ? 11.649 -19.331 48.731 1.00 18.24 ? 426 GLN A CA 1 ATOM 2984 C C . GLN A 1 391 ? 10.131 -19.201 48.871 1.00 17.32 ? 426 GLN A C 1 ATOM 2985 O O . GLN A 1 391 ? 9.387 -19.868 48.147 1.00 16.39 ? 426 GLN A O 1 ATOM 2986 C CB . GLN A 1 391 ? 12.138 -20.672 49.309 1.00 20.78 ? 426 GLN A CB 1 ATOM 2987 C CG . GLN A 1 391 ? 11.900 -20.898 50.790 1.00 24.32 ? 426 GLN A CG 1 ATOM 2988 C CD . GLN A 1 391 ? 13.015 -20.386 51.704 1.00 30.17 ? 426 GLN A CD 1 ATOM 2989 O OE1 . GLN A 1 391 ? 13.868 -19.516 51.335 1.00 29.61 ? 426 GLN A OE1 1 ATOM 2990 N NE2 . GLN A 1 391 ? 13.007 -20.914 52.948 1.00 33.95 ? 426 GLN A NE2 1 ATOM 2991 N N . HIS A 1 392 ? 9.669 -18.371 49.798 1.00 16.16 ? 427 HIS A N 1 ATOM 2992 C CA . HIS A 1 392 ? 8.243 -18.113 49.973 1.00 16.83 ? 427 HIS A CA 1 ATOM 2993 C C . HIS A 1 392 ? 7.651 -16.955 49.184 1.00 15.48 ? 427 HIS A C 1 ATOM 2994 O O . HIS A 1 392 ? 6.428 -16.758 49.220 1.00 15.73 ? 427 HIS A O 1 ATOM 2995 C CB . HIS A 1 392 ? 7.941 -17.970 51.469 1.00 18.15 ? 427 HIS A CB 1 ATOM 2996 C CG . HIS A 1 392 ? 8.265 -19.205 52.249 1.00 21.91 ? 427 HIS A CG 1 ATOM 2997 N ND1 . HIS A 1 392 ? 8.618 -19.176 53.579 1.00 24.57 ? 427 HIS A ND1 1 ATOM 2998 C CD2 . HIS A 1 392 ? 8.310 -20.508 51.875 1.00 23.76 ? 427 HIS A CD2 1 ATOM 2999 C CE1 . HIS A 1 392 ? 8.862 -20.406 53.996 1.00 26.59 ? 427 HIS A CE1 1 ATOM 3000 N NE2 . HIS A 1 392 ? 8.677 -21.235 52.984 1.00 27.32 ? 427 HIS A NE2 1 ATOM 3001 N N . LEU A 1 393 ? 8.475 -16.192 48.458 1.00 14.11 ? 428 LEU A N 1 ATOM 3002 C CA . LEU A 1 393 ? 7.937 -15.180 47.572 1.00 14.17 ? 428 LEU A CA 1 ATOM 3003 C C . LEU A 1 393 ? 7.045 -15.810 46.524 1.00 13.99 ? 428 LEU A C 1 ATOM 3004 O O . LEU A 1 393 ? 7.288 -16.950 46.128 1.00 14.73 ? 428 LEU A O 1 ATOM 3005 C CB . LEU A 1 393 ? 9.039 -14.415 46.849 1.00 13.84 ? 428 LEU A CB 1 ATOM 3006 C CG . LEU A 1 393 ? 9.859 -13.499 47.744 1.00 14.24 ? 428 LEU A CG 1 ATOM 3007 C CD1 . LEU A 1 393 ? 11.110 -13.063 46.971 1.00 14.92 ? 428 LEU A CD1 1 ATOM 3008 C CD2 . LEU A 1 393 ? 9.034 -12.299 48.190 1.00 13.75 ? 428 LEU A CD2 1 ATOM 3009 N N . PRO A 1 394 ? 6.043 -15.063 46.055 1.00 14.65 ? 429 PRO A N 1 ATOM 3010 C CA . PRO A 1 394 ? 5.238 -15.560 44.910 1.00 14.16 ? 429 PRO A CA 1 ATOM 3011 C C . PRO A 1 394 ? 6.107 -16.109 43.788 1.00 13.68 ? 429 PRO A C 1 ATOM 3012 O O . PRO A 1 394 ? 7.068 -15.459 43.352 1.00 14.32 ? 429 PRO A O 1 ATOM 3013 C CB . PRO A 1 394 ? 4.482 -14.324 44.448 1.00 14.36 ? 429 PRO A CB 1 ATOM 3014 C CG . PRO A 1 394 ? 4.344 -13.514 45.696 1.00 15.38 ? 429 PRO A CG 1 ATOM 3015 C CD . PRO A 1 394 ? 5.568 -13.742 46.522 1.00 14.82 ? 429 PRO A CD 1 ATOM 3016 N N . LYS A 1 395 ? 5.745 -17.286 43.317 1.00 13.23 ? 430 LYS A N 1 ATOM 3017 C CA . LYS A 1 395 ? 6.556 -17.983 42.337 1.00 13.29 ? 430 LYS A CA 1 ATOM 3018 C C . LYS A 1 395 ? 6.604 -17.230 41.030 1.00 13.28 ? 430 LYS A C 1 ATOM 3019 O O . LYS A 1 395 ? 7.630 -17.308 40.335 1.00 12.40 ? 430 LYS A O 1 ATOM 3020 C CB . LYS A 1 395 ? 6.055 -19.403 42.133 1.00 13.26 ? 430 LYS A CB 1 ATOM 3021 C CG . LYS A 1 395 ? 6.140 -20.260 43.402 1.00 13.47 ? 430 LYS A CG 1 ATOM 3022 C CD . LYS A 1 395 ? 7.581 -20.470 43.903 1.00 13.42 ? 430 LYS A CD 1 ATOM 3023 C CE . LYS A 1 395 ? 8.270 -21.627 43.202 1.00 14.45 ? 430 LYS A CE 1 ATOM 3024 N NZ . LYS A 1 395 ? 9.614 -21.824 43.769 1.00 14.99 ? 430 LYS A NZ 1 ATOM 3025 N N . ARG A 1 396 ? 5.549 -16.460 40.718 1.00 12.60 ? 431 ARG A N 1 ATOM 3026 C CA . ARG A 1 396 ? 5.544 -15.622 39.500 1.00 13.16 ? 431 ARG A CA 1 ATOM 3027 C C . ARG A 1 396 ? 6.706 -14.631 39.441 1.00 13.75 ? 431 ARG A C 1 ATOM 3028 O O . ARG A 1 396 ? 7.040 -14.159 38.347 1.00 15.04 ? 431 ARG A O 1 ATOM 3029 C CB . ARG A 1 396 ? 4.229 -14.821 39.365 1.00 13.64 ? 431 ARG A CB 1 ATOM 3030 C CG . ARG A 1 396 ? 3.989 -13.809 40.475 1.00 13.32 ? 431 ARG A CG 1 ATOM 3031 C CD . ARG A 1 396 ? 2.599 -13.196 40.399 1.00 13.99 ? 431 ARG A CD 1 ATOM 3032 N NE . ARG A 1 396 ? 2.346 -12.503 41.636 1.00 13.60 ? 431 ARG A NE 1 ATOM 3033 C CZ . ARG A 1 396 ? 2.832 -11.308 41.963 1.00 15.25 ? 431 ARG A CZ 1 ATOM 3034 N NH1 . ARG A 1 396 ? 3.585 -10.599 41.113 1.00 15.46 ? 431 ARG A NH1 1 ATOM 3035 N NH2 . ARG A 1 396 ? 2.576 -10.812 43.155 1.00 15.92 ? 431 ARG A NH2 1 ATOM 3036 N N . LEU A 1 397 ? 7.264 -14.238 40.587 1.00 13.26 ? 432 LEU A N 1 ATOM 3037 C CA . LEU A 1 397 ? 8.395 -13.317 40.595 1.00 14.18 ? 432 LEU A CA 1 ATOM 3038 C C . LEU A 1 397 ? 9.715 -13.944 40.146 1.00 14.56 ? 432 LEU A C 1 ATOM 3039 O O . LEU A 1 397 ? 10.646 -13.221 39.807 1.00 15.12 ? 432 LEU A O 1 ATOM 3040 C CB . LEU A 1 397 ? 8.572 -12.678 41.956 1.00 14.79 ? 432 LEU A CB 1 ATOM 3041 C CG . LEU A 1 397 ? 7.396 -11.846 42.478 1.00 14.98 ? 432 LEU A CG 1 ATOM 3042 C CD1 . LEU A 1 397 ? 7.643 -11.529 43.947 1.00 17.00 ? 432 LEU A CD1 1 ATOM 3043 C CD2 . LEU A 1 397 ? 7.134 -10.582 41.677 1.00 15.08 ? 432 LEU A CD2 1 ATOM 3044 N N . HIS A 1 398 ? 9.803 -15.274 40.198 1.00 14.07 ? 433 HIS A N 1 ATOM 3045 C CA . HIS A 1 398 ? 10.979 -16.033 39.834 1.00 13.50 ? 433 HIS A CA 1 ATOM 3046 C C . HIS A 1 398 ? 12.236 -15.437 40.443 1.00 13.70 ? 433 HIS A C 1 ATOM 3047 O O . HIS A 1 398 ? 13.206 -15.204 39.742 1.00 13.99 ? 433 HIS A O 1 ATOM 3048 C CB . HIS A 1 398 ? 11.096 -16.112 38.305 1.00 13.21 ? 433 HIS A CB 1 ATOM 3049 C CG . HIS A 1 398 ? 9.990 -16.884 37.656 1.00 13.66 ? 433 HIS A CG 1 ATOM 3050 N ND1 . HIS A 1 398 ? 9.966 -18.259 37.639 1.00 15.10 ? 433 HIS A ND1 1 ATOM 3051 C CD2 . HIS A 1 398 ? 8.856 -16.474 37.042 1.00 14.32 ? 433 HIS A CD2 1 ATOM 3052 C CE1 . HIS A 1 398 ? 8.865 -18.666 37.034 1.00 14.98 ? 433 HIS A CE1 1 ATOM 3053 N NE2 . HIS A 1 398 ? 8.167 -17.601 36.676 1.00 15.06 ? 433 HIS A NE2 1 ATOM 3054 N N . TYR A 1 399 ? 12.170 -15.117 41.734 1.00 13.26 ? 434 TYR A N 1 ATOM 3055 C CA . TYR A 1 399 ? 13.191 -14.267 42.388 1.00 13.45 ? 434 TYR A CA 1 ATOM 3056 C C . TYR A 1 399 ? 13.778 -14.968 43.613 1.00 14.20 ? 434 TYR A C 1 ATOM 3057 O O . TYR A 1 399 ? 13.611 -14.538 44.771 1.00 14.87 ? 434 TYR A O 1 ATOM 3058 C CB . TYR A 1 399 ? 12.626 -12.878 42.734 1.00 13.66 ? 434 TYR A CB 1 ATOM 3059 C CG . TYR A 1 399 ? 13.703 -11.854 43.030 1.00 13.46 ? 434 TYR A CG 1 ATOM 3060 C CD1 . TYR A 1 399 ? 14.490 -11.333 42.009 1.00 14.48 ? 434 TYR A CD1 1 ATOM 3061 C CD2 . TYR A 1 399 ? 13.945 -11.420 44.318 1.00 14.60 ? 434 TYR A CD2 1 ATOM 3062 C CE1 . TYR A 1 399 ? 15.494 -10.405 42.275 1.00 14.99 ? 434 TYR A CE1 1 ATOM 3063 C CE2 . TYR A 1 399 ? 14.953 -10.499 44.600 1.00 14.93 ? 434 TYR A CE2 1 ATOM 3064 C CZ . TYR A 1 399 ? 15.732 -10.003 43.573 1.00 14.67 ? 434 TYR A CZ 1 ATOM 3065 O OH . TYR A 1 399 ? 16.696 -9.062 43.876 1.00 15.22 ? 434 TYR A OH 1 ATOM 3066 N N . ALA A 1 400 ? 14.524 -16.045 43.366 1.00 13.71 ? 435 ALA A N 1 ATOM 3067 C CA . ALA A 1 400 ? 15.094 -16.806 44.484 1.00 14.62 ? 435 ALA A CA 1 ATOM 3068 C C . ALA A 1 400 ? 16.361 -17.564 44.172 1.00 15.34 ? 435 ALA A C 1 ATOM 3069 O O . ALA A 1 400 ? 17.239 -17.661 45.032 1.00 15.71 ? 435 ALA A O 1 ATOM 3070 C CB . ALA A 1 400 ? 14.071 -17.758 45.087 1.00 15.18 ? 435 ALA A CB 1 ATOM 3071 N N . ASN A 1 401 ? 16.471 -18.089 42.954 1.00 13.96 ? 436 ASN A N 1 ATOM 3072 C CA . ASN A 1 401 ? 17.546 -19.012 42.642 1.00 15.14 ? 436 ASN A CA 1 ATOM 3073 C C . ASN A 1 401 ? 18.824 -18.316 42.199 1.00 15.73 ? 436 ASN A C 1 ATOM 3074 O O . ASN A 1 401 ? 19.264 -18.484 41.083 1.00 15.08 ? 436 ASN A O 1 ATOM 3075 C CB . ASN A 1 401 ? 17.099 -20.058 41.600 1.00 15.35 ? 436 ASN A CB 1 ATOM 3076 C CG . ASN A 1 401 ? 18.136 -21.158 41.395 1.00 17.35 ? 436 ASN A CG 1 ATOM 3077 O OD1 . ASN A 1 401 ? 18.879 -21.510 42.311 1.00 17.45 ? 436 ASN A OD1 1 ATOM 3078 N ND2 . ASN A 1 401 ? 18.211 -21.672 40.181 1.00 17.96 ? 436 ASN A ND2 1 ATOM 3079 N N . ASN A 1 402 ? 19.436 -17.580 43.113 1.00 15.39 ? 437 ASN A N 1 ATOM 3080 C CA . ASN A 1 402 ? 20.693 -16.929 42.853 1.00 15.80 ? 437 ASN A CA 1 ATOM 3081 C C . ASN A 1 402 ? 21.344 -16.615 44.176 1.00 16.95 ? 437 ASN A C 1 ATOM 3082 O O . ASN A 1 402 ? 20.658 -16.157 45.088 1.00 16.08 ? 437 ASN A O 1 ATOM 3083 C CB . ASN A 1 402 ? 20.457 -15.651 42.026 1.00 16.49 ? 437 ASN A CB 1 ATOM 3084 C CG . ASN A 1 402 ? 21.736 -15.098 41.460 1.00 16.82 ? 437 ASN A CG 1 ATOM 3085 O OD1 . ASN A 1 402 ? 22.557 -14.568 42.193 1.00 18.03 ? 437 ASN A OD1 1 ATOM 3086 N ND2 . ASN A 1 402 ? 21.936 -15.243 40.152 1.00 16.63 ? 437 ASN A ND2 1 ATOM 3087 N N . ARG A 1 403 ? 22.658 -16.856 44.303 1.00 16.94 ? 438 ARG A N 1 ATOM 3088 C CA . ARG A 1 403 ? 23.377 -16.563 45.565 1.00 17.10 ? 438 ARG A CA 1 ATOM 3089 C C . ARG A 1 403 ? 23.437 -15.060 45.929 1.00 16.97 ? 438 ARG A C 1 ATOM 3090 O O . ARG A 1 403 ? 23.758 -14.706 47.069 1.00 17.11 ? 438 ARG A O 1 ATOM 3091 C CB . ARG A 1 403 ? 24.786 -17.151 45.549 1.00 18.32 ? 438 ARG A CB 1 ATOM 3092 C CG . ARG A 1 403 ? 25.732 -16.455 44.588 1.00 19.26 ? 438 ARG A CG 1 ATOM 3093 C CD . ARG A 1 403 ? 27.056 -17.190 44.488 1.00 22.20 ? 438 ARG A CD 1 ATOM 3094 N NE . ARG A 1 403 ? 27.904 -16.491 43.527 1.00 22.47 ? 438 ARG A NE 1 ATOM 3095 C CZ . ARG A 1 403 ? 28.341 -16.961 42.354 1.00 26.39 ? 438 ARG A CZ 1 ATOM 3096 N NH1 . ARG A 1 403 ? 28.111 -18.221 41.944 1.00 27.24 ? 438 ARG A NH1 1 ATOM 3097 N NH2 . ARG A 1 403 ? 29.080 -16.142 41.581 1.00 25.28 ? 438 ARG A NH2 1 ATOM 3098 N N . ARG A 1 404 ? 23.163 -14.199 44.966 1.00 16.26 ? 439 ARG A N 1 ATOM 3099 C CA . ARG A 1 404 ? 23.093 -12.762 45.196 1.00 16.35 ? 439 ARG A CA 1 ATOM 3100 C C . ARG A 1 404 ? 21.774 -12.278 45.765 1.00 16.39 ? 439 ARG A C 1 ATOM 3101 O O . ARG A 1 404 ? 21.670 -11.099 46.088 1.00 17.63 ? 439 ARG A O 1 ATOM 3102 C CB . ARG A 1 404 ? 23.343 -12.007 43.886 1.00 16.28 ? 439 ARG A CB 1 ATOM 3103 C CG . ARG A 1 404 ? 24.715 -12.290 43.320 1.00 16.16 ? 439 ARG A CG 1 ATOM 3104 C CD . ARG A 1 404 ? 24.820 -11.919 41.856 1.00 16.30 ? 439 ARG A CD 1 ATOM 3105 N NE . ARG A 1 404 ? 26.119 -12.332 41.361 1.00 17.53 ? 439 ARG A NE 1 ATOM 3106 C CZ . ARG A 1 404 ? 26.498 -12.252 40.092 1.00 17.63 ? 439 ARG A CZ 1 ATOM 3107 N NH1 . ARG A 1 404 ? 25.675 -11.788 39.161 1.00 17.49 ? 439 ARG A NH1 1 ATOM 3108 N NH2 . ARG A 1 404 ? 27.724 -12.660 39.769 1.00 18.55 ? 439 ARG A NH2 1 ATOM 3109 N N . ILE A 1 405 ? 20.761 -13.142 45.811 1.00 15.70 ? 440 ILE A N 1 ATOM 3110 C CA . ILE A 1 405 ? 19.473 -12.779 46.420 1.00 15.37 ? 440 ILE A CA 1 ATOM 3111 C C . ILE A 1 405 ? 19.494 -13.221 47.876 1.00 16.39 ? 440 ILE A C 1 ATOM 3112 O O . ILE A 1 405 ? 19.528 -14.425 48.178 1.00 16.52 ? 440 ILE A O 1 ATOM 3113 C CB . ILE A 1 405 ? 18.266 -13.411 45.687 1.00 14.89 ? 440 ILE A CB 1 ATOM 3114 C CG1 . ILE A 1 405 ? 18.223 -12.931 44.233 1.00 14.44 ? 440 ILE A CG1 1 ATOM 3115 C CG2 . ILE A 1 405 ? 16.958 -13.051 46.389 1.00 15.48 ? 440 ILE A CG2 1 ATOM 3116 C CD1 . ILE A 1 405 ? 17.305 -13.719 43.341 1.00 14.61 ? 440 ILE A CD1 1 ATOM 3117 N N . GLU A 1 406 ? 19.437 -12.242 48.769 1.00 16.36 ? 441 GLU A N 1 ATOM 3118 C CA . GLU A 1 406 ? 19.489 -12.508 50.204 1.00 18.53 ? 441 GLU A CA 1 ATOM 3119 C C . GLU A 1 406 ? 18.295 -13.357 50.592 1.00 18.74 ? 441 GLU A C 1 ATOM 3120 O O . GLU A 1 406 ? 17.221 -13.259 49.990 1.00 18.90 ? 441 GLU A O 1 ATOM 3121 C CB . GLU A 1 406 ? 19.496 -11.212 51.010 1.00 19.29 ? 441 GLU A CB 1 ATOM 3122 C CG . GLU A 1 406 ? 20.825 -10.449 50.971 1.00 20.30 ? 441 GLU A CG 1 ATOM 3123 C CD . GLU A 1 406 ? 21.055 -9.648 49.695 1.00 21.04 ? 441 GLU A CD 1 ATOM 3124 O OE1 . GLU A 1 406 ? 20.181 -9.652 48.799 1.00 20.65 ? 441 GLU A OE1 1 ATOM 3125 O OE2 . GLU A 1 406 ? 22.122 -9.011 49.606 1.00 22.40 ? 441 GLU A OE2 1 ATOM 3126 N N . ASP A 1 407 ? 18.491 -14.211 51.593 1.00 20.08 ? 442 ASP A N 1 ATOM 3127 C CA . ASP A 1 407 ? 17.411 -15.089 52.063 1.00 20.71 ? 442 ASP A CA 1 ATOM 3128 C C . ASP A 1 407 ? 16.198 -14.289 52.507 1.00 19.25 ? 442 ASP A C 1 ATOM 3129 O O . ASP A 1 407 ? 15.068 -14.681 52.230 1.00 19.25 ? 442 ASP A O 1 ATOM 3130 C CB . ASP A 1 407 ? 17.854 -15.974 53.228 1.00 21.99 ? 442 ASP A CB 1 ATOM 3131 C CG . ASP A 1 407 ? 18.816 -17.078 52.824 1.00 25.49 ? 442 ASP A CG 1 ATOM 3132 O OD1 . ASP A 1 407 ? 19.018 -17.345 51.618 1.00 28.41 ? 442 ASP A OD1 1 ATOM 3133 O OD2 . ASP A 1 407 ? 19.369 -17.716 53.752 1.00 29.69 ? 442 ASP A OD2 1 ATOM 3134 N N . ILE A 1 408 ? 16.444 -13.161 53.164 1.00 18.71 ? 443 ILE A N 1 ATOM 3135 C CA . ILE A 1 408 ? 15.372 -12.330 53.699 1.00 18.47 ? 443 ILE A CA 1 ATOM 3136 C C . ILE A 1 408 ? 15.027 -11.253 52.705 1.00 18.22 ? 443 ILE A C 1 ATOM 3137 O O . ILE A 1 408 ? 15.890 -10.463 52.314 1.00 18.75 ? 443 ILE A O 1 ATOM 3138 C CB . ILE A 1 408 ? 15.738 -11.691 55.054 1.00 19.57 ? 443 ILE A CB 1 ATOM 3139 C CG1 . ILE A 1 408 ? 15.978 -12.766 56.089 1.00 21.04 ? 443 ILE A CG1 1 ATOM 3140 C CG2 . ILE A 1 408 ? 14.621 -10.747 55.495 1.00 20.02 ? 443 ILE A CG2 1 ATOM 3141 C CD1 . ILE A 1 408 ? 16.514 -12.263 57.415 1.00 23.08 ? 443 ILE A CD1 1 ATOM 3142 N N . HIS A 1 409 ? 13.763 -11.245 52.288 1.00 17.28 ? 444 HIS A N 1 ATOM 3143 C CA . HIS A 1 409 ? 13.246 -10.253 51.381 1.00 16.70 ? 444 HIS A CA 1 ATOM 3144 C C . HIS A 1 409 ? 12.057 -9.489 51.974 1.00 17.53 ? 444 HIS A C 1 ATOM 3145 O O . HIS A 1 409 ? 11.227 -10.082 52.648 1.00 18.55 ? 444 HIS A O 1 ATOM 3146 C CB . HIS A 1 409 ? 12.810 -10.916 50.063 1.00 16.41 ? 444 HIS A CB 1 ATOM 3147 C CG . HIS A 1 409 ? 12.693 -9.957 48.935 1.00 16.05 ? 444 HIS A CG 1 ATOM 3148 N ND1 . HIS A 1 409 ? 13.793 -9.526 48.225 1.00 17.12 ? 444 HIS A ND1 1 ATOM 3149 C CD2 . HIS A 1 409 ? 11.632 -9.277 48.440 1.00 16.08 ? 444 HIS A CD2 1 ATOM 3150 C CE1 . HIS A 1 409 ? 13.412 -8.649 47.316 1.00 18.04 ? 444 HIS A CE1 1 ATOM 3151 N NE2 . HIS A 1 409 ? 12.107 -8.488 47.418 1.00 17.12 ? 444 HIS A NE2 1 ATOM 3152 N N . LEU A 1 410 ? 11.972 -8.186 51.676 1.00 16.17 ? 445 LEU A N 1 ATOM 3153 C CA . LEU A 1 410 ? 10.794 -7.357 52.017 1.00 15.45 ? 445 LEU A CA 1 ATOM 3154 C C . LEU A 1 410 ? 10.077 -6.905 50.752 1.00 16.27 ? 445 LEU A C 1 ATOM 3155 O O . LEU A 1 410 ? 10.683 -6.218 49.878 1.00 14.95 ? 445 LEU A O 1 ATOM 3156 C CB . LEU A 1 410 ? 11.183 -6.136 52.836 1.00 16.76 ? 445 LEU A CB 1 ATOM 3157 C CG . LEU A 1 410 ? 12.112 -6.369 54.013 1.00 17.48 ? 445 LEU A CG 1 ATOM 3158 C CD1 . LEU A 1 410 ? 12.352 -5.050 54.742 1.00 18.86 ? 445 LEU A CD1 1 ATOM 3159 C CD2 . LEU A 1 410 ? 11.575 -7.404 54.985 1.00 17.50 ? 445 LEU A CD2 1 ATOM 3160 N N . LEU A 1 411 ? 8.815 -7.308 50.621 1.00 15.98 ? 446 LEU A N 1 ATOM 3161 C CA . LEU A 1 411 ? 7.975 -6.815 49.541 1.00 16.68 ? 446 LEU A CA 1 ATOM 3162 C C . LEU A 1 411 ? 7.312 -5.559 50.067 1.00 16.73 ? 446 LEU A C 1 ATOM 3163 O O . LEU A 1 411 ? 6.502 -5.611 50.992 1.00 16.56 ? 446 LEU A O 1 ATOM 3164 C CB . LEU A 1 411 ? 6.900 -7.818 49.115 1.00 18.46 ? 446 LEU A CB 1 ATOM 3165 C CG . LEU A 1 411 ? 7.168 -8.854 48.062 1.00 20.69 ? 446 LEU A CG 1 ATOM 3166 C CD1 . LEU A 1 411 ? 5.856 -9.578 47.753 1.00 20.89 ? 446 LEU A CD1 1 ATOM 3167 C CD2 . LEU A 1 411 ? 7.750 -8.221 46.806 1.00 19.84 ? 446 LEU A CD2 1 ATOM 3168 N N . VAL A 1 412 ? 7.676 -4.434 49.497 1.00 15.90 ? 447 VAL A N 1 ATOM 3169 C CA . VAL A 1 412 ? 7.209 -3.143 49.980 1.00 16.26 ? 447 VAL A CA 1 ATOM 3170 C C . VAL A 1 412 ? 5.922 -2.742 49.277 1.00 16.86 ? 447 VAL A C 1 ATOM 3171 O O . VAL A 1 412 ? 5.791 -2.898 48.060 1.00 16.36 ? 447 VAL A O 1 ATOM 3172 C CB . VAL A 1 412 ? 8.296 -2.091 49.804 1.00 16.82 ? 447 VAL A CB 1 ATOM 3173 C CG1 . VAL A 1 412 ? 7.843 -0.708 50.271 1.00 17.03 ? 447 VAL A CG1 1 ATOM 3174 C CG2 . VAL A 1 412 ? 9.571 -2.545 50.505 1.00 17.67 ? 447 VAL A CG2 1 ATOM 3175 N N . ASP A 1 413 ? 4.962 -2.219 50.019 1.00 16.86 ? 448 ASP A N 1 ATOM 3176 C CA . ASP A 1 413 ? 3.715 -1.727 49.396 1.00 17.39 ? 448 ASP A CA 1 ATOM 3177 C C . ASP A 1 413 ? 4.002 -0.594 48.385 1.00 17.13 ? 448 ASP A C 1 ATOM 3178 O O . ASP A 1 413 ? 4.848 0.254 48.649 1.00 16.18 ? 448 ASP A O 1 ATOM 3179 C CB . ASP A 1 413 ? 2.748 -1.168 50.443 1.00 19.94 ? 448 ASP A CB 1 ATOM 3180 C CG . ASP A 1 413 ? 2.140 -2.228 51.318 1.00 21.81 ? 448 ASP A CG 1 ATOM 3181 O OD1 . ASP A 1 413 ? 2.373 -3.424 51.093 1.00 23.12 ? 448 ASP A OD1 1 ATOM 3182 O OD2 . ASP A 1 413 ? 1.411 -1.849 52.256 1.00 22.98 ? 448 ASP A OD2 1 ATOM 3183 N N . ARG A 1 414 ? 3.258 -0.565 47.278 1.00 17.34 ? 449 ARG A N 1 ATOM 3184 C CA A ARG A 1 414 ? 3.376 0.556 46.342 0.60 18.11 ? 449 ARG A CA 1 ATOM 3185 C CA B ARG A 1 414 ? 3.306 0.556 46.325 0.40 18.05 ? 449 ARG A CA 1 ATOM 3186 C C . ARG A 1 414 ? 3.150 1.868 47.092 1.00 18.78 ? 449 ARG A C 1 ATOM 3187 O O . ARG A 1 414 ? 2.333 1.941 48.020 1.00 17.81 ? 449 ARG A O 1 ATOM 3188 C CB A ARG A 1 414 ? 2.410 0.410 45.171 0.60 19.31 ? 449 ARG A CB 1 ATOM 3189 C CB B ARG A 1 414 ? 2.208 0.423 45.246 0.40 19.08 ? 449 ARG A CB 1 ATOM 3190 C CG A ARG A 1 414 ? 0.948 0.595 45.515 0.60 20.87 ? 449 ARG A CG 1 ATOM 3191 C CG B ARG A 1 414 ? 0.767 0.584 45.734 0.40 20.55 ? 449 ARG A CG 1 ATOM 3192 C CD A ARG A 1 414 ? 0.056 0.146 44.377 0.60 21.82 ? 449 ARG A CD 1 ATOM 3193 C CD B ARG A 1 414 ? -0.279 0.302 44.658 0.40 21.46 ? 449 ARG A CD 1 ATOM 3194 N NE A ARG A 1 414 ? -0.256 -1.276 44.463 0.60 23.13 ? 449 ARG A NE 1 ATOM 3195 N NE B ARG A 1 414 ? -0.002 0.998 43.407 0.40 22.09 ? 449 ARG A NE 1 ATOM 3196 C CZ A ARG A 1 414 ? -0.912 -1.968 43.534 0.60 23.72 ? 449 ARG A CZ 1 ATOM 3197 C CZ B ARG A 1 414 ? -0.716 0.844 42.290 0.40 23.54 ? 449 ARG A CZ 1 ATOM 3198 N NH1 A ARG A 1 414 ? -1.319 -1.388 42.394 0.60 24.70 ? 449 ARG A NH1 1 ATOM 3199 N NH1 B ARG A 1 414 ? -0.379 1.493 41.183 0.40 22.06 ? 449 ARG A NH1 1 ATOM 3200 N NH2 A ARG A 1 414 ? -1.137 -3.256 43.742 0.60 24.11 ? 449 ARG A NH2 1 ATOM 3201 N NH2 B ARG A 1 414 ? -1.765 0.027 42.274 0.40 23.40 ? 449 ARG A NH2 1 ATOM 3202 N N . ARG A 1 415 ? 3.923 2.878 46.709 1.00 17.93 ? 450 ARG A N 1 ATOM 3203 C CA . ARG A 1 415 ? 3.898 4.243 47.245 1.00 19.87 ? 450 ARG A CA 1 ATOM 3204 C C . ARG A 1 415 ? 4.787 4.435 48.471 1.00 19.37 ? 450 ARG A C 1 ATOM 3205 O O . ARG A 1 415 ? 4.900 5.567 48.940 1.00 19.52 ? 450 ARG A O 1 ATOM 3206 C CB . ARG A 1 415 ? 2.465 4.768 47.501 1.00 21.35 ? 450 ARG A CB 1 ATOM 3207 C CG . ARG A 1 415 ? 1.521 4.649 46.300 1.00 23.27 ? 450 ARG A CG 1 ATOM 3208 C CD . ARG A 1 415 ? 0.142 5.242 46.573 1.00 28.84 ? 450 ARG A CD 1 ATOM 3209 N NE . ARG A 1 415 ? 0.178 6.714 46.714 1.00 35.02 ? 450 ARG A NE 1 ATOM 3210 C CZ . ARG A 1 415 ? -0.075 7.424 47.824 1.00 40.16 ? 450 ARG A CZ 1 ATOM 3211 N NH1 . ARG A 1 415 ? -0.419 6.860 48.985 1.00 40.64 ? 450 ARG A NH1 1 ATOM 3212 N NH2 . ARG A 1 415 ? 0.010 8.748 47.771 1.00 43.56 ? 450 ARG A NH2 1 ATOM 3213 N N . TRP A 1 416 ? 5.445 3.357 48.939 1.00 17.93 ? 451 TRP A N 1 ATOM 3214 C CA . TRP A 1 416 ? 6.229 3.355 50.185 1.00 18.29 ? 451 TRP A CA 1 ATOM 3215 C C . TRP A 1 416 ? 7.713 3.031 49.979 1.00 18.12 ? 451 TRP A C 1 ATOM 3216 O O . TRP A 1 416 ? 8.123 2.446 48.955 1.00 17.92 ? 451 TRP A O 1 ATOM 3217 C CB . TRP A 1 416 ? 5.590 2.388 51.237 1.00 19.47 ? 451 TRP A CB 1 ATOM 3218 C CG . TRP A 1 416 ? 4.403 2.985 51.847 1.00 20.14 ? 451 TRP A CG 1 ATOM 3219 C CD1 . TRP A 1 416 ? 3.159 3.080 51.304 1.00 20.31 ? 451 TRP A CD1 1 ATOM 3220 C CD2 . TRP A 1 416 ? 4.350 3.667 53.101 1.00 21.51 ? 451 TRP A CD2 1 ATOM 3221 N NE1 . TRP A 1 416 ? 2.329 3.780 52.140 1.00 22.07 ? 451 TRP A NE1 1 ATOM 3222 C CE2 . TRP A 1 416 ? 3.038 4.155 53.255 1.00 22.51 ? 451 TRP A CE2 1 ATOM 3223 C CE3 . TRP A 1 416 ? 5.290 3.907 54.113 1.00 22.43 ? 451 TRP A CE3 1 ATOM 3224 C CZ2 . TRP A 1 416 ? 2.638 4.860 54.390 1.00 24.65 ? 451 TRP A CZ2 1 ATOM 3225 C CZ3 . TRP A 1 416 ? 4.903 4.609 55.216 1.00 22.73 ? 451 TRP A CZ3 1 ATOM 3226 C CH2 . TRP A 1 416 ? 3.582 5.081 55.354 1.00 24.46 ? 451 TRP A CH2 1 ATOM 3227 N N . HIS A 1 417 ? 8.525 3.438 50.953 1.00 18.25 ? 452 HIS A N 1 ATOM 3228 C CA . HIS A 1 417 ? 9.924 3.001 51.070 1.00 18.46 ? 452 HIS A CA 1 ATOM 3229 C C . HIS A 1 417 ? 10.116 2.262 52.380 1.00 18.73 ? 452 HIS A C 1 ATOM 3230 O O . HIS A 1 417 ? 9.368 2.491 53.319 1.00 18.95 ? 452 HIS A O 1 ATOM 3231 C CB . HIS A 1 417 ? 10.888 4.206 51.107 1.00 20.34 ? 452 HIS A CB 1 ATOM 3232 C CG . HIS A 1 417 ? 11.306 4.711 49.759 1.00 20.36 ? 452 HIS A CG 1 ATOM 3233 N ND1 . HIS A 1 417 ? 11.863 5.957 49.581 1.00 21.91 ? 452 HIS A ND1 1 ATOM 3234 C CD2 . HIS A 1 417 ? 11.272 4.135 48.534 1.00 20.92 ? 452 HIS A CD2 1 ATOM 3235 C CE1 . HIS A 1 417 ? 12.141 6.133 48.300 1.00 21.14 ? 452 HIS A CE1 1 ATOM 3236 N NE2 . HIS A 1 417 ? 11.794 5.040 47.646 1.00 20.75 ? 452 HIS A NE2 1 ATOM 3237 N N . VAL A 1 418 ? 11.126 1.397 52.422 1.00 18.98 ? 453 VAL A N 1 ATOM 3238 C CA A VAL A 1 418 ? 11.653 0.858 53.672 0.50 19.83 ? 453 VAL A CA 1 ATOM 3239 C CA B VAL A 1 418 ? 11.654 0.859 53.671 0.50 19.71 ? 453 VAL A CA 1 ATOM 3240 C C . VAL A 1 418 ? 13.123 1.248 53.767 1.00 20.64 ? 453 VAL A C 1 ATOM 3241 O O . VAL A 1 418 ? 13.885 1.045 52.826 1.00 21.32 ? 453 VAL A O 1 ATOM 3242 C CB A VAL A 1 418 ? 11.479 -0.671 53.765 0.50 19.83 ? 453 VAL A CB 1 ATOM 3243 C CB B VAL A 1 418 ? 11.463 -0.675 53.822 0.50 19.60 ? 453 VAL A CB 1 ATOM 3244 C CG1 A VAL A 1 418 ? 12.265 -1.247 54.944 0.50 20.22 ? 453 VAL A CG1 1 ATOM 3245 C CG1 B VAL A 1 418 ? 12.328 -1.486 52.852 0.50 18.92 ? 453 VAL A CG1 1 ATOM 3246 C CG2 A VAL A 1 418 ? 10.004 -1.012 53.913 0.50 19.97 ? 453 VAL A CG2 1 ATOM 3247 C CG2 B VAL A 1 418 ? 11.756 -1.084 55.261 0.50 20.24 ? 453 VAL A CG2 1 ATOM 3248 N N . ALA A 1 419 ? 13.501 1.840 54.895 1.00 21.80 ? 454 ALA A N 1 ATOM 3249 C CA . ALA A 1 419 ? 14.873 2.233 55.184 1.00 23.81 ? 454 ALA A CA 1 ATOM 3250 C C . ALA A 1 419 ? 15.280 1.624 56.516 1.00 25.77 ? 454 ALA A C 1 ATOM 3251 O O . ALA A 1 419 ? 14.444 1.100 57.267 1.00 24.48 ? 454 ALA A O 1 ATOM 3252 C CB . ALA A 1 419 ? 14.990 3.755 55.225 1.00 24.88 ? 454 ALA A CB 1 ATOM 3253 N N . ARG A 1 420 ? 16.567 1.704 56.811 1.00 27.61 ? 455 ARG A N 1 ATOM 3254 C CA . ARG A 1 420 ? 17.110 1.042 57.981 1.00 32.02 ? 455 ARG A CA 1 ATOM 3255 C C . ARG A 1 420 ? 16.840 1.853 59.243 1.00 32.72 ? 455 ARG A C 1 ATOM 3256 O O . ARG A 1 420 ? 16.377 1.277 60.230 1.00 29.70 ? 455 ARG A O 1 ATOM 3257 C CB . ARG A 1 420 ? 18.614 0.752 57.820 1.00 34.21 ? 455 ARG A CB 1 ATOM 3258 C CG . ARG A 1 420 ? 19.102 -0.341 58.777 1.00 37.99 ? 455 ARG A CG 1 ATOM 3259 C CD . ARG A 1 420 ? 20.511 -0.800 58.439 1.00 40.88 ? 455 ARG A CD 1 ATOM 3260 N NE . ARG A 1 420 ? 21.450 0.325 58.469 1.00 42.60 ? 455 ARG A NE 1 ATOM 3261 C CZ . ARG A 1 420 ? 22.350 0.582 59.423 1.00 46.73 ? 455 ARG A CZ 1 ATOM 3262 N NH1 . ARG A 1 420 ? 22.509 -0.210 60.485 1.00 47.96 ? 455 ARG A NH1 1 ATOM 3263 N NH2 . ARG A 1 420 ? 23.124 1.653 59.296 1.00 48.05 ? 455 ARG A NH2 1 ATOM 3264 N N . LYS A 1 421 ? 17.106 3.168 59.176 1.00 35.60 ? 456 LYS A N 1 ATOM 3265 C CA . LYS A 1 421 ? 17.022 4.118 60.310 1.00 40.90 ? 456 LYS A CA 1 ATOM 3266 C C . LYS A 1 421 ? 16.496 5.502 59.861 1.00 39.30 ? 456 LYS A C 1 ATOM 3267 O O . LYS A 1 421 ? 16.698 5.879 58.712 1.00 36.11 ? 456 LYS A O 1 ATOM 3268 C CB . LYS A 1 421 ? 18.409 4.387 60.904 1.00 45.24 ? 456 LYS A CB 1 ATOM 3269 C CG . LYS A 1 421 ? 19.141 3.197 61.487 1.00 48.02 ? 456 LYS A CG 1 ATOM 3270 C CD . LYS A 1 421 ? 20.273 3.683 62.391 1.00 51.40 ? 456 LYS A CD 1 ATOM 3271 C CE . LYS A 1 421 ? 20.893 2.546 63.176 1.00 54.74 ? 456 LYS A CE 1 ATOM 3272 N NZ . LYS A 1 421 ? 21.550 2.978 64.442 1.00 57.79 ? 456 LYS A NZ 1 ATOM 3273 N N . PRO A 1 422 ? 15.871 6.281 60.770 1.00 39.18 ? 457 PRO A N 1 ATOM 3274 C CA . PRO A 1 422 ? 15.366 7.611 60.375 1.00 41.40 ? 457 PRO A CA 1 ATOM 3275 C C . PRO A 1 422 ? 16.392 8.639 59.890 1.00 47.52 ? 457 PRO A C 1 ATOM 3276 O O . PRO A 1 422 ? 16.014 9.560 59.158 1.00 51.37 ? 457 PRO A O 1 ATOM 3277 C CB . PRO A 1 422 ? 14.659 8.112 61.633 1.00 41.59 ? 457 PRO A CB 1 ATOM 3278 C CG . PRO A 1 422 ? 14.252 6.871 62.345 1.00 40.32 ? 457 PRO A CG 1 ATOM 3279 C CD . PRO A 1 422 ? 15.366 5.899 62.105 1.00 40.00 ? 457 PRO A CD 1 ATOM 3280 N N . LEU A 1 423 ? 17.660 8.489 60.264 1.00 50.01 ? 458 LEU A N 1 ATOM 3281 C CA . LEU A 1 423 ? 18.719 9.338 59.700 1.00 57.68 ? 458 LEU A CA 1 ATOM 3282 C C . LEU A 1 423 ? 18.808 9.219 58.167 1.00 58.40 ? 458 LEU A C 1 ATOM 3283 O O . LEU A 1 423 ? 19.182 10.179 57.489 1.00 56.26 ? 458 LEU A O 1 ATOM 3284 C CB . LEU A 1 423 ? 20.078 9.055 60.371 1.00 61.50 ? 458 LEU A CB 1 ATOM 3285 C CG . LEU A 1 423 ? 20.279 9.884 61.652 1.00 66.02 ? 458 LEU A CG 1 ATOM 3286 C CD1 . LEU A 1 423 ? 21.150 9.195 62.699 1.00 66.33 ? 458 LEU A CD1 1 ATOM 3287 C CD2 . LEU A 1 423 ? 20.842 11.253 61.291 1.00 67.54 ? 458 LEU A CD2 1 ATOM 3288 N N . ASP A 1 424 ? 18.436 8.052 57.638 1.00 58.40 ? 459 ASP A N 1 ATOM 3289 C CA . ASP A 1 424 ? 18.327 7.836 56.192 1.00 59.00 ? 459 ASP A CA 1 ATOM 3290 C C . ASP A 1 424 ? 17.052 8.515 55.693 1.00 60.81 ? 459 ASP A C 1 ATOM 3291 O O . ASP A 1 424 ? 17.065 9.218 54.686 1.00 61.95 ? 459 ASP A O 1 ATOM 3292 C CB . ASP A 1 424 ? 18.284 6.333 55.851 1.00 55.43 ? 459 ASP A CB 1 ATOM 3293 C CG . ASP A 1 424 ? 19.398 5.530 56.531 1.00 55.47 ? 459 ASP A CG 1 ATOM 3294 O OD1 . ASP A 1 424 ? 20.494 6.086 56.738 1.00 58.43 ? 459 ASP A OD1 1 ATOM 3295 O OD2 . ASP A 1 424 ? 19.178 4.339 56.863 1.00 49.51 ? 459 ASP A OD2 1 ATOM 3296 N N . LYS A 1 432 ? 9.012 18.886 53.103 1.00 60.51 ? 467 LYS A N 1 ATOM 3297 C CA . LYS A 1 432 ? 8.995 18.831 51.640 1.00 59.95 ? 467 LYS A CA 1 ATOM 3298 C C . LYS A 1 432 ? 10.209 18.046 51.106 1.00 57.27 ? 467 LYS A C 1 ATOM 3299 O O . LYS A 1 432 ? 11.356 18.447 51.332 1.00 56.31 ? 467 LYS A O 1 ATOM 3300 C CB . LYS A 1 432 ? 8.943 20.264 51.079 1.00 61.65 ? 467 LYS A CB 1 ATOM 3301 C CG . LYS A 1 432 ? 9.161 20.416 49.576 1.00 62.85 ? 467 LYS A CG 1 ATOM 3302 C CD . LYS A 1 432 ? 8.231 19.544 48.748 1.00 62.77 ? 467 LYS A CD 1 ATOM 3303 C CE . LYS A 1 432 ? 8.354 19.863 47.266 1.00 61.50 ? 467 LYS A CE 1 ATOM 3304 N NZ . LYS A 1 432 ? 7.339 19.124 46.464 1.00 61.75 ? 467 LYS A NZ 1 ATOM 3305 N N . CYS A 1 433 ? 9.950 16.938 50.396 1.00 52.22 ? 468 CYS A N 1 ATOM 3306 C CA . CYS A 1 433 ? 11.005 15.994 49.984 1.00 46.68 ? 468 CYS A CA 1 ATOM 3307 C C . CYS A 1 433 ? 11.684 16.394 48.671 1.00 42.17 ? 468 CYS A C 1 ATOM 3308 O O . CYS A 1 433 ? 11.089 17.064 47.834 1.00 44.10 ? 468 CYS A O 1 ATOM 3309 C CB . CYS A 1 433 ? 10.433 14.565 49.836 1.00 48.65 ? 468 CYS A CB 1 ATOM 3310 S SG . CYS A 1 433 ? 9.359 14.031 51.195 1.00 55.33 ? 468 CYS A SG 1 ATOM 3311 N N . PHE A 1 434 ? 12.919 15.930 48.492 1.00 36.39 ? 469 PHE A N 1 ATOM 3312 C CA . PHE A 1 434 ? 13.666 16.124 47.253 1.00 35.59 ? 469 PHE A CA 1 ATOM 3313 C C . PHE A 1 434 ? 13.157 15.254 46.093 1.00 33.07 ? 469 PHE A C 1 ATOM 3314 O O . PHE A 1 434 ? 13.408 15.571 44.932 1.00 31.89 ? 469 PHE A O 1 ATOM 3315 C CB . PHE A 1 434 ? 15.156 15.833 47.476 1.00 37.43 ? 469 PHE A CB 1 ATOM 3316 C CG . PHE A 1 434 ? 15.880 16.897 48.255 1.00 40.52 ? 469 PHE A CG 1 ATOM 3317 C CD1 . PHE A 1 434 ? 16.353 18.042 47.617 1.00 41.23 ? 469 PHE A CD1 1 ATOM 3318 C CD2 . PHE A 1 434 ? 16.096 16.753 49.628 1.00 41.80 ? 469 PHE A CD2 1 ATOM 3319 C CE1 . PHE A 1 434 ? 17.031 19.025 48.324 1.00 44.12 ? 469 PHE A CE1 1 ATOM 3320 C CE2 . PHE A 1 434 ? 16.775 17.730 50.341 1.00 43.34 ? 469 PHE A CE2 1 ATOM 3321 C CZ . PHE A 1 434 ? 17.238 18.870 49.692 1.00 44.42 ? 469 PHE A CZ 1 ATOM 3322 N N . PHE A 1 435 ? 12.498 14.141 46.407 1.00 29.54 ? 470 PHE A N 1 ATOM 3323 C CA . PHE A 1 435 ? 11.963 13.224 45.399 1.00 28.92 ? 470 PHE A CA 1 ATOM 3324 C C . PHE A 1 435 ? 10.470 12.953 45.652 1.00 26.51 ? 470 PHE A C 1 ATOM 3325 O O . PHE A 1 435 ? 9.976 13.031 46.795 1.00 25.72 ? 470 PHE A O 1 ATOM 3326 C CB . PHE A 1 435 ? 12.764 11.921 45.390 1.00 29.82 ? 470 PHE A CB 1 ATOM 3327 C CG . PHE A 1 435 ? 12.466 11.035 46.559 1.00 31.50 ? 470 PHE A CG 1 ATOM 3328 C CD1 . PHE A 1 435 ? 11.381 10.152 46.522 1.00 32.45 ? 470 PHE A CD1 1 ATOM 3329 C CD2 . PHE A 1 435 ? 13.241 11.097 47.721 1.00 33.95 ? 470 PHE A CD2 1 ATOM 3330 C CE1 . PHE A 1 435 ? 11.076 9.356 47.626 1.00 32.12 ? 470 PHE A CE1 1 ATOM 3331 C CE2 . PHE A 1 435 ? 12.940 10.290 48.820 1.00 35.06 ? 470 PHE A CE2 1 ATOM 3332 C CZ . PHE A 1 435 ? 11.860 9.425 48.769 1.00 31.71 ? 470 PHE A CZ 1 ATOM 3333 N N . GLN A 1 436 ? 9.761 12.690 44.562 1.00 24.28 ? 471 GLN A N 1 ATOM 3334 C CA . GLN A 1 436 ? 8.328 12.422 44.579 1.00 24.70 ? 471 GLN A CA 1 ATOM 3335 C C . GLN A 1 436 ? 7.918 11.169 43.807 1.00 22.29 ? 471 GLN A C 1 ATOM 3336 O O . GLN A 1 436 ? 6.731 10.849 43.747 1.00 22.52 ? 471 GLN A O 1 ATOM 3337 C CB . GLN A 1 436 ? 7.602 13.612 43.971 1.00 27.91 ? 471 GLN A CB 1 ATOM 3338 C CG . GLN A 1 436 ? 7.835 14.902 44.722 1.00 31.76 ? 471 GLN A CG 1 ATOM 3339 C CD . GLN A 1 436 ? 6.947 16.002 44.205 1.00 38.25 ? 471 GLN A CD 1 ATOM 3340 O OE1 . GLN A 1 436 ? 5.738 16.003 44.460 1.00 41.94 ? 471 GLN A OE1 1 ATOM 3341 N NE2 . GLN A 1 436 ? 7.531 16.952 43.482 1.00 41.58 ? 471 GLN A NE2 1 ATOM 3342 N N . GLY A 1 437 ? 8.878 10.473 43.196 1.00 20.52 ? 472 GLY A N 1 ATOM 3343 C CA . GLY A 1 437 ? 8.582 9.234 42.488 1.00 19.04 ? 472 GLY A CA 1 ATOM 3344 C C . GLY A 1 437 ? 9.640 8.180 42.721 1.00 18.33 ? 472 GLY A C 1 ATOM 3345 O O . GLY A 1 437 ? 10.817 8.498 42.961 1.00 18.18 ? 472 GLY A O 1 ATOM 3346 N N . ASP A 1 438 ? 9.230 6.919 42.669 1.00 16.67 ? 473 ASP A N 1 ATOM 3347 C CA . ASP A 1 438 ? 10.195 5.830 42.629 1.00 16.00 ? 473 ASP A CA 1 ATOM 3348 C C . ASP A 1 438 ? 9.522 4.598 42.011 1.00 15.17 ? 473 ASP A C 1 ATOM 3349 O O . ASP A 1 438 ? 8.295 4.580 41.738 1.00 14.66 ? 473 ASP A O 1 ATOM 3350 C CB . ASP A 1 438 ? 10.748 5.559 44.047 1.00 16.73 ? 473 ASP A CB 1 ATOM 3351 C CG . ASP A 1 438 ? 12.167 4.950 44.073 1.00 16.93 ? 473 ASP A CG 1 ATOM 3352 O OD1 . ASP A 1 438 ? 12.732 4.571 43.014 1.00 17.19 ? 473 ASP A OD1 1 ATOM 3353 O OD2 . ASP A 1 438 ? 12.730 4.808 45.192 1.00 17.48 ? 473 ASP A OD2 1 ATOM 3354 N N . HIS A 1 439 ? 10.332 3.563 41.832 1.00 15.02 ? 474 HIS A N 1 ATOM 3355 C CA . HIS A 1 439 ? 9.931 2.303 41.221 1.00 14.77 ? 474 HIS A CA 1 ATOM 3356 C C . HIS A 1 439 ? 10.801 1.191 41.819 1.00 14.32 ? 474 HIS A C 1 ATOM 3357 O O . HIS A 1 439 ? 11.808 1.465 42.501 1.00 15.16 ? 474 HIS A O 1 ATOM 3358 C CB . HIS A 1 439 ? 10.123 2.394 39.689 1.00 14.43 ? 474 HIS A CB 1 ATOM 3359 C CG . HIS A 1 439 ? 11.514 2.818 39.303 1.00 15.15 ? 474 HIS A CG 1 ATOM 3360 N ND1 . HIS A 1 439 ? 12.536 1.913 39.112 1.00 15.27 ? 474 HIS A ND1 1 ATOM 3361 C CD2 . HIS A 1 439 ? 12.060 4.045 39.138 1.00 15.11 ? 474 HIS A CD2 1 ATOM 3362 C CE1 . HIS A 1 439 ? 13.655 2.565 38.854 1.00 15.74 ? 474 HIS A CE1 1 ATOM 3363 N NE2 . HIS A 1 439 ? 13.393 3.863 38.865 1.00 15.40 ? 474 HIS A NE2 1 ATOM 3364 N N . GLY A 1 440 ? 10.434 -0.059 41.543 1.00 14.22 ? 475 GLY A N 1 ATOM 3365 C CA . GLY A 1 440 ? 11.132 -1.244 42.077 1.00 14.09 ? 475 GLY A CA 1 ATOM 3366 C C . GLY A 1 440 ? 10.173 -2.281 42.661 1.00 14.41 ? 475 GLY A C 1 ATOM 3367 O O . GLY A 1 440 ? 10.539 -3.456 42.808 1.00 15.91 ? 475 GLY A O 1 ATOM 3368 N N . PHE A 1 441 ? 8.929 -1.849 42.889 1.00 14.54 ? 476 PHE A N 1 ATOM 3369 C CA . PHE A 1 441 ? 7.864 -2.687 43.431 1.00 14.03 ? 476 PHE A CA 1 ATOM 3370 C C . PHE A 1 441 ? 7.527 -3.925 42.578 1.00 13.49 ? 476 PHE A C 1 ATOM 3371 O O . PHE A 1 441 ? 7.885 -4.006 41.402 1.00 13.14 ? 476 PHE A O 1 ATOM 3372 C CB . PHE A 1 441 ? 6.583 -1.864 43.578 1.00 14.82 ? 476 PHE A CB 1 ATOM 3373 C CG . PHE A 1 441 ? 6.765 -0.594 44.357 1.00 15.13 ? 476 PHE A CG 1 ATOM 3374 C CD1 . PHE A 1 441 ? 6.958 -0.648 45.715 1.00 15.08 ? 476 PHE A CD1 1 ATOM 3375 C CD2 . PHE A 1 441 ? 6.744 0.641 43.730 1.00 15.02 ? 476 PHE A CD2 1 ATOM 3376 C CE1 . PHE A 1 441 ? 7.130 0.490 46.440 1.00 15.89 ? 476 PHE A CE1 1 ATOM 3377 C CE2 . PHE A 1 441 ? 6.915 1.799 44.441 1.00 15.57 ? 476 PHE A CE2 1 ATOM 3378 C CZ . PHE A 1 441 ? 7.116 1.725 45.810 1.00 15.92 ? 476 PHE A CZ 1 ATOM 3379 N N . ASP A 1 442 ? 6.814 -4.853 43.206 1.00 14.32 ? 477 ASP A N 1 ATOM 3380 C CA . ASP A 1 442 ? 6.170 -6.003 42.559 1.00 13.43 ? 477 ASP A CA 1 ATOM 3381 C C . ASP A 1 442 ? 5.784 -5.665 41.100 1.00 13.09 ? 477 ASP A C 1 ATOM 3382 O O . ASP A 1 442 ? 5.094 -4.688 40.846 1.00 12.59 ? 477 ASP A O 1 ATOM 3383 C CB . ASP A 1 442 ? 4.924 -6.362 43.386 1.00 14.34 ? 477 ASP A CB 1 ATOM 3384 C CG . ASP A 1 442 ? 4.225 -7.642 42.937 1.00 14.54 ? 477 ASP A CG 1 ATOM 3385 O OD1 . ASP A 1 442 ? 4.364 -8.062 41.776 1.00 13.85 ? 477 ASP A OD1 1 ATOM 3386 O OD2 . ASP A 1 442 ? 3.466 -8.224 43.770 1.00 15.48 ? 477 ASP A OD2 1 ATOM 3387 N N . ASN A 1 443 ? 6.247 -6.505 40.166 1.00 12.96 ? 478 ASN A N 1 ATOM 3388 C CA . ASN A 1 443 ? 6.043 -6.238 38.746 1.00 13.89 ? 478 ASN A CA 1 ATOM 3389 C C . ASN A 1 443 ? 4.623 -6.388 38.208 1.00 14.28 ? 478 ASN A C 1 ATOM 3390 O O . ASN A 1 443 ? 4.380 -6.058 37.045 1.00 15.32 ? 478 ASN A O 1 ATOM 3391 C CB . ASN A 1 443 ? 7.006 -7.042 37.899 1.00 13.74 ? 478 ASN A CB 1 ATOM 3392 C CG . ASN A 1 443 ? 6.701 -8.523 37.901 1.00 14.25 ? 478 ASN A CG 1 ATOM 3393 O OD1 . ASN A 1 443 ? 6.217 -9.056 38.894 1.00 14.69 ? 478 ASN A OD1 1 ATOM 3394 N ND2 . ASN A 1 443 ? 7.074 -9.215 36.833 1.00 14.26 ? 478 ASN A ND2 1 ATOM 3395 N N . LYS A 1 444 ? 3.679 -6.833 39.024 1.00 16.44 ? 479 LYS A N 1 ATOM 3396 C CA . LYS A 1 444 ? 2.275 -6.770 38.617 1.00 17.90 ? 479 LYS A CA 1 ATOM 3397 C C . LYS A 1 444 ? 1.550 -5.475 38.975 1.00 17.47 ? 479 LYS A C 1 ATOM 3398 O O . LYS A 1 444 ? 0.455 -5.264 38.492 1.00 20.01 ? 479 LYS A O 1 ATOM 3399 C CB . LYS A 1 444 ? 1.504 -8.007 39.062 1.00 19.64 ? 479 LYS A CB 1 ATOM 3400 C CG . LYS A 1 444 ? 1.080 -8.040 40.512 1.00 22.89 ? 479 LYS A CG 1 ATOM 3401 C CD . LYS A 1 444 ? 0.265 -9.318 40.700 1.00 25.73 ? 479 LYS A CD 1 ATOM 3402 C CE . LYS A 1 444 ? -0.196 -9.469 42.132 1.00 28.37 ? 479 LYS A CE 1 ATOM 3403 N NZ . LYS A 1 444 ? -1.548 -8.889 42.261 1.00 30.95 ? 479 LYS A NZ 1 ATOM 3404 N N . VAL A 1 445 ? 2.185 -4.605 39.758 1.00 17.38 ? 480 VAL A N 1 ATOM 3405 C CA . VAL A 1 445 ? 1.623 -3.316 40.150 1.00 18.68 ? 480 VAL A CA 1 ATOM 3406 C C . VAL A 1 445 ? 1.423 -2.421 38.908 1.00 18.19 ? 480 VAL A C 1 ATOM 3407 O O . VAL A 1 445 ? 2.335 -2.287 38.084 1.00 16.96 ? 480 VAL A O 1 ATOM 3408 C CB . VAL A 1 445 ? 2.532 -2.634 41.208 1.00 18.48 ? 480 VAL A CB 1 ATOM 3409 C CG1 . VAL A 1 445 ? 2.163 -1.172 41.409 1.00 20.50 ? 480 VAL A CG1 1 ATOM 3410 C CG2 . VAL A 1 445 ? 2.417 -3.378 42.525 1.00 19.79 ? 480 VAL A CG2 1 ATOM 3411 N N . ASN A 1 446 ? 0.241 -1.818 38.788 1.00 18.98 ? 481 ASN A N 1 ATOM 3412 C CA . ASN A 1 446 ? -0.087 -0.972 37.603 1.00 21.07 ? 481 ASN A CA 1 ATOM 3413 C C . ASN A 1 446 ? 0.941 0.115 37.274 1.00 19.38 ? 481 ASN A C 1 ATOM 3414 O O . ASN A 1 446 ? 1.357 0.275 36.114 1.00 18.29 ? 481 ASN A O 1 ATOM 3415 C CB . ASN A 1 446 ? -1.447 -0.300 37.797 1.00 28.18 ? 481 ASN A CB 1 ATOM 3416 C CG . ASN A 1 446 ? -2.588 -1.179 37.372 1.00 35.61 ? 481 ASN A CG 1 ATOM 3417 O OD1 . ASN A 1 446 ? -2.389 -2.275 36.833 1.00 46.62 ? 481 ASN A OD1 1 ATOM 3418 N ND2 . ASN A 1 446 ? -3.809 -0.701 37.596 1.00 42.31 ? 481 ASN A ND2 1 ATOM 3419 N N . SER A 1 447 ? 1.380 0.838 38.297 1.00 16.92 ? 482 SER A N 1 ATOM 3420 C CA . SER A 1 447 ? 2.307 1.951 38.106 1.00 17.45 ? 482 SER A CA 1 ATOM 3421 C C . SER A 1 447 ? 3.665 1.496 37.555 1.00 16.35 ? 482 SER A C 1 ATOM 3422 O O . SER A 1 447 ? 4.388 2.296 36.975 1.00 16.04 ? 482 SER A O 1 ATOM 3423 C CB . SER A 1 447 ? 2.484 2.719 39.422 1.00 18.21 ? 482 SER A CB 1 ATOM 3424 O OG . SER A 1 447 ? 2.901 1.848 40.458 1.00 18.24 ? 482 SER A OG 1 ATOM 3425 N N . MET A 1 448 ? 3.999 0.209 37.722 1.00 16.12 ? 483 MET A N 1 ATOM 3426 C CA . MET A 1 448 ? 5.280 -0.342 37.283 1.00 15.04 ? 483 MET A CA 1 ATOM 3427 C C . MET A 1 448 ? 5.296 -0.765 35.806 1.00 14.71 ? 483 MET A C 1 ATOM 3428 O O . MET A 1 448 ? 6.379 -0.998 35.250 1.00 13.77 ? 483 MET A O 1 ATOM 3429 C CB . MET A 1 448 ? 5.670 -1.526 38.185 1.00 16.17 ? 483 MET A CB 1 ATOM 3430 C CG . MET A 1 448 ? 6.079 -1.152 39.611 1.00 16.11 ? 483 MET A CG 1 ATOM 3431 S SD . MET A 1 448 ? 7.373 0.126 39.774 1.00 16.53 ? 483 MET A SD 1 ATOM 3432 C CE . MET A 1 448 ? 6.418 1.646 39.931 1.00 17.26 ? 483 MET A CE 1 ATOM 3433 N N . GLN A 1 449 ? 4.125 -0.851 35.177 1.00 14.30 ? 484 GLN A N 1 ATOM 3434 C CA . GLN A 1 449 ? 4.040 -1.268 33.776 1.00 15.58 ? 484 GLN A CA 1 ATOM 3435 C C . GLN A 1 449 ? 4.676 -0.243 32.881 1.00 15.49 ? 484 GLN A C 1 ATOM 3436 O O . GLN A 1 449 ? 4.657 0.957 33.161 1.00 17.45 ? 484 GLN A O 1 ATOM 3437 C CB . GLN A 1 449 ? 2.581 -1.523 33.341 1.00 16.48 ? 484 GLN A CB 1 ATOM 3438 C CG . GLN A 1 449 ? 1.831 -2.513 34.242 1.00 16.68 ? 484 GLN A CG 1 ATOM 3439 C CD . GLN A 1 449 ? 2.648 -3.756 34.615 1.00 17.93 ? 484 GLN A CD 1 ATOM 3440 O OE1 . GLN A 1 449 ? 2.961 -4.587 33.764 1.00 18.04 ? 484 GLN A OE1 1 ATOM 3441 N NE2 . GLN A 1 449 ? 2.967 -3.898 35.885 1.00 15.54 ? 484 GLN A NE2 1 ATOM 3442 N N . THR A 1 450 ? 5.217 -0.737 31.778 1.00 15.70 ? 485 THR A N 1 ATOM 3443 C CA . THR A 1 450 ? 5.940 0.092 30.844 1.00 15.92 ? 485 THR A CA 1 ATOM 3444 C C . THR A 1 450 ? 5.388 -0.093 29.442 1.00 16.21 ? 485 THR A C 1 ATOM 3445 O O . THR A 1 450 ? 4.278 -0.604 29.281 1.00 17.24 ? 485 THR A O 1 ATOM 3446 C CB . THR A 1 450 ? 7.457 -0.123 30.990 1.00 15.64 ? 485 THR A CB 1 ATOM 3447 O OG1 . THR A 1 450 ? 8.146 0.873 30.212 1.00 17.19 ? 485 THR A OG1 1 ATOM 3448 C CG2 . THR A 1 450 ? 7.875 -1.497 30.563 1.00 16.50 ? 485 THR A CG2 1 ATOM 3449 N N . VAL A 1 451 ? 6.137 0.376 28.432 1.00 16.41 ? 486 VAL A N 1 ATOM 3450 C CA . VAL A 1 451 ? 5.608 0.457 27.053 1.00 18.16 ? 486 VAL A CA 1 ATOM 3451 C C . VAL A 1 451 ? 6.297 -0.467 26.055 1.00 16.34 ? 486 VAL A C 1 ATOM 3452 O O . VAL A 1 451 ? 7.454 -0.841 26.233 1.00 15.78 ? 486 VAL A O 1 ATOM 3453 C CB . VAL A 1 451 ? 5.666 1.885 26.506 1.00 18.89 ? 486 VAL A CB 1 ATOM 3454 C CG1 . VAL A 1 451 ? 4.721 2.754 27.312 1.00 21.04 ? 486 VAL A CG1 1 ATOM 3455 C CG2 . VAL A 1 451 ? 7.090 2.426 26.535 1.00 19.89 ? 486 VAL A CG2 1 ATOM 3456 N N . PHE A 1 452 ? 5.541 -0.843 25.021 1.00 16.34 ? 487 PHE A N 1 ATOM 3457 C CA . PHE A 1 452 ? 6.103 -1.482 23.856 1.00 15.52 ? 487 PHE A CA 1 ATOM 3458 C C . PHE A 1 452 ? 5.417 -1.006 22.582 1.00 14.90 ? 487 PHE A C 1 ATOM 3459 O O . PHE A 1 452 ? 4.180 -1.034 22.478 1.00 15.60 ? 487 PHE A O 1 ATOM 3460 C CB . PHE A 1 452 ? 6.000 -3.019 23.925 1.00 14.35 ? 487 PHE A CB 1 ATOM 3461 C CG . PHE A 1 452 ? 6.401 -3.660 22.645 1.00 16.15 ? 487 PHE A CG 1 ATOM 3462 C CD1 . PHE A 1 452 ? 7.742 -3.835 22.352 1.00 17.17 ? 487 PHE A CD1 1 ATOM 3463 C CD2 . PHE A 1 452 ? 5.458 -3.975 21.691 1.00 17.40 ? 487 PHE A CD2 1 ATOM 3464 C CE1 . PHE A 1 452 ? 8.128 -4.366 21.146 1.00 18.16 ? 487 PHE A CE1 1 ATOM 3465 C CE2 . PHE A 1 452 ? 5.844 -4.486 20.461 1.00 18.58 ? 487 PHE A CE2 1 ATOM 3466 C CZ . PHE A 1 452 ? 7.168 -4.698 20.205 1.00 18.28 ? 487 PHE A CZ 1 ATOM 3467 N N . VAL A 1 453 ? 6.219 -0.567 21.612 1.00 15.22 ? 488 VAL A N 1 ATOM 3468 C CA . VAL A 1 453 ? 5.766 -0.369 20.235 1.00 16.36 ? 488 VAL A CA 1 ATOM 3469 C C . VAL A 1 453 ? 6.809 -1.005 19.327 1.00 15.72 ? 488 VAL A C 1 ATOM 3470 O O . VAL A 1 453 ? 7.998 -0.835 19.538 1.00 16.30 ? 488 VAL A O 1 ATOM 3471 C CB . VAL A 1 453 ? 5.639 1.132 19.867 1.00 18.00 ? 488 VAL A CB 1 ATOM 3472 C CG1 . VAL A 1 453 ? 5.211 1.343 18.411 1.00 19.63 ? 488 VAL A CG1 1 ATOM 3473 C CG2 . VAL A 1 453 ? 4.683 1.834 20.810 1.00 17.54 ? 488 VAL A CG2 1 ATOM 3474 N N . GLY A 1 454 ? 6.338 -1.721 18.315 1.00 16.06 ? 489 GLY A N 1 ATOM 3475 C CA . GLY A 1 454 ? 7.179 -2.168 17.204 1.00 16.80 ? 489 GLY A CA 1 ATOM 3476 C C . GLY A 1 454 ? 6.700 -1.531 15.909 1.00 17.92 ? 489 GLY A C 1 ATOM 3477 O O . GLY A 1 454 ? 5.492 -1.534 15.616 1.00 19.44 ? 489 GLY A O 1 ATOM 3478 N N . TYR A 1 455 ? 7.630 -0.995 15.122 1.00 18.01 ? 490 TYR A N 1 ATOM 3479 C CA . TYR A 1 455 ? 7.270 -0.337 13.869 1.00 17.88 ? 490 TYR A CA 1 ATOM 3480 C C . TYR A 1 455 ? 8.299 -0.743 12.820 1.00 18.40 ? 490 TYR A C 1 ATOM 3481 O O . TYR A 1 455 ? 9.493 -0.653 13.069 1.00 18.21 ? 490 TYR A O 1 ATOM 3482 C CB . TYR A 1 455 ? 7.293 1.170 14.042 1.00 19.08 ? 490 TYR A CB 1 ATOM 3483 C CG . TYR A 1 455 ? 7.004 1.943 12.767 1.00 19.48 ? 490 TYR A CG 1 ATOM 3484 C CD1 . TYR A 1 455 ? 8.021 2.273 11.882 1.00 20.09 ? 490 TYR A CD1 1 ATOM 3485 C CD2 . TYR A 1 455 ? 5.708 2.332 12.445 1.00 20.34 ? 490 TYR A CD2 1 ATOM 3486 C CE1 . TYR A 1 455 ? 7.758 2.980 10.715 1.00 21.11 ? 490 TYR A CE1 1 ATOM 3487 C CE2 . TYR A 1 455 ? 5.436 3.051 11.277 1.00 21.94 ? 490 TYR A CE2 1 ATOM 3488 C CZ . TYR A 1 455 ? 6.465 3.369 10.426 1.00 21.77 ? 490 TYR A CZ 1 ATOM 3489 O OH . TYR A 1 455 ? 6.190 4.081 9.276 1.00 24.66 ? 490 TYR A OH 1 ATOM 3490 N N . GLY A 1 456 ? 7.820 -1.169 11.656 1.00 18.50 ? 491 GLY A N 1 ATOM 3491 C CA . GLY A 1 456 ? 8.710 -1.515 10.557 1.00 19.08 ? 491 GLY A CA 1 ATOM 3492 C C . GLY A 1 456 ? 8.151 -2.596 9.683 1.00 19.60 ? 491 GLY A C 1 ATOM 3493 O O . GLY A 1 456 ? 7.040 -3.073 9.905 1.00 18.96 ? 491 GLY A O 1 ATOM 3494 N N . PRO A 1 457 ? 8.919 -3.013 8.677 1.00 19.48 ? 492 PRO A N 1 ATOM 3495 C CA . PRO A 1 457 ? 8.386 -4.017 7.766 1.00 21.02 ? 492 PRO A CA 1 ATOM 3496 C C . PRO A 1 457 ? 8.005 -5.364 8.388 1.00 20.55 ? 492 PRO A C 1 ATOM 3497 O O . PRO A 1 457 ? 7.104 -6.019 7.874 1.00 19.38 ? 492 PRO A O 1 ATOM 3498 C CB . PRO A 1 457 ? 9.544 -4.227 6.759 1.00 21.60 ? 492 PRO A CB 1 ATOM 3499 C CG . PRO A 1 457 ? 10.767 -3.808 7.477 1.00 20.77 ? 492 PRO A CG 1 ATOM 3500 C CD . PRO A 1 457 ? 10.318 -2.659 8.352 1.00 21.12 ? 492 PRO A CD 1 ATOM 3501 N N . THR A 1 458 ? 8.676 -5.769 9.474 1.00 20.09 ? 493 THR A N 1 ATOM 3502 C CA . THR A 1 458 ? 8.477 -7.107 10.022 1.00 19.51 ? 493 THR A CA 1 ATOM 3503 C C . THR A 1 458 ? 7.370 -7.142 11.062 1.00 19.35 ? 493 THR A C 1 ATOM 3504 O O . THR A 1 458 ? 6.791 -8.176 11.301 1.00 20.14 ? 493 THR A O 1 ATOM 3505 C CB . THR A 1 458 ? 9.790 -7.697 10.578 1.00 19.53 ? 493 THR A CB 1 ATOM 3506 O OG1 . THR A 1 458 ? 10.822 -7.470 9.620 1.00 20.58 ? 493 THR A OG1 1 ATOM 3507 C CG2 . THR A 1 458 ? 9.651 -9.228 10.785 1.00 20.37 ? 493 THR A CG2 1 ATOM 3508 N N . PHE A 1 459 ? 7.064 -5.993 11.643 1.00 19.05 ? 494 PHE A N 1 ATOM 3509 C CA . PHE A 1 459 ? 5.947 -5.852 12.564 1.00 18.06 ? 494 PHE A CA 1 ATOM 3510 C C . PHE A 1 459 ? 4.659 -5.687 11.787 1.00 19.78 ? 494 PHE A C 1 ATOM 3511 O O . PHE A 1 459 ? 4.679 -5.214 10.635 1.00 19.44 ? 494 PHE A O 1 ATOM 3512 C CB . PHE A 1 459 ? 6.171 -4.659 13.483 1.00 17.91 ? 494 PHE A CB 1 ATOM 3513 C CG . PHE A 1 459 ? 7.152 -4.932 14.574 1.00 17.58 ? 494 PHE A CG 1 ATOM 3514 C CD1 . PHE A 1 459 ? 6.808 -5.800 15.619 1.00 17.42 ? 494 PHE A CD1 1 ATOM 3515 C CD2 . PHE A 1 459 ? 8.422 -4.370 14.565 1.00 16.40 ? 494 PHE A CD2 1 ATOM 3516 C CE1 . PHE A 1 459 ? 7.717 -6.077 16.635 1.00 17.53 ? 494 PHE A CE1 1 ATOM 3517 C CE2 . PHE A 1 459 ? 9.331 -4.660 15.574 1.00 17.66 ? 494 PHE A CE2 1 ATOM 3518 C CZ . PHE A 1 459 ? 8.978 -5.512 16.610 1.00 16.65 ? 494 PHE A CZ 1 ATOM 3519 N N . LYS A 1 460 ? 3.539 -6.071 12.400 1.00 19.31 ? 495 LYS A N 1 ATOM 3520 C CA . LYS A 1 460 ? 2.237 -5.862 11.793 1.00 21.25 ? 495 LYS A CA 1 ATOM 3521 C C . LYS A 1 460 ? 1.882 -4.367 11.682 1.00 21.19 ? 495 LYS A C 1 ATOM 3522 O O . LYS A 1 460 ? 2.470 -3.528 12.353 1.00 20.56 ? 495 LYS A O 1 ATOM 3523 C CB . LYS A 1 460 ? 1.146 -6.620 12.548 1.00 22.25 ? 495 LYS A CB 1 ATOM 3524 C CG . LYS A 1 460 ? 1.282 -8.114 12.393 1.00 23.29 ? 495 LYS A CG 1 ATOM 3525 C CD . LYS A 1 460 ? 0.113 -8.801 13.047 1.00 25.65 ? 495 LYS A CD 1 ATOM 3526 C CE . LYS A 1 460 ? 0.093 -10.277 12.773 1.00 27.84 ? 495 LYS A CE 1 ATOM 3527 N NZ . LYS A 1 460 ? -0.850 -10.937 13.724 1.00 30.46 ? 495 LYS A NZ 1 ATOM 3528 N N . TYR A 1 461 ? 0.936 -4.077 10.793 1.00 22.89 ? 496 TYR A N 1 ATOM 3529 C CA . TYR A 1 461 ? 0.438 -2.734 10.490 1.00 21.85 ? 496 TYR A CA 1 ATOM 3530 C C . TYR A 1 461 ? -0.799 -2.463 11.357 1.00 21.79 ? 496 TYR A C 1 ATOM 3531 O O . TYR A 1 461 ? -1.688 -3.304 11.430 1.00 21.17 ? 496 TYR A O 1 ATOM 3532 C CB . TYR A 1 461 ? 0.065 -2.684 9.005 1.00 24.10 ? 496 TYR A CB 1 ATOM 3533 C CG . TYR A 1 461 ? -0.563 -1.389 8.504 1.00 24.23 ? 496 TYR A CG 1 ATOM 3534 C CD1 . TYR A 1 461 ? 0.145 -0.207 8.524 1.00 25.05 ? 496 TYR A CD1 1 ATOM 3535 C CD2 . TYR A 1 461 ? -1.860 -1.369 7.970 1.00 26.26 ? 496 TYR A CD2 1 ATOM 3536 C CE1 . TYR A 1 461 ? -0.411 0.970 8.038 1.00 25.71 ? 496 TYR A CE1 1 ATOM 3537 C CE2 . TYR A 1 461 ? -2.426 -0.193 7.482 1.00 27.67 ? 496 TYR A CE2 1 ATOM 3538 C CZ . TYR A 1 461 ? -1.695 0.971 7.530 1.00 27.47 ? 496 TYR A CZ 1 ATOM 3539 O OH . TYR A 1 461 ? -2.235 2.151 7.058 1.00 31.76 ? 496 TYR A OH 1 ATOM 3540 N N . ARG A 1 462 ? -0.830 -1.301 12.018 1.00 22.51 ? 497 ARG A N 1 ATOM 3541 C CA . ARG A 1 462 ? -1.990 -0.805 12.787 1.00 24.00 ? 497 ARG A CA 1 ATOM 3542 C C . ARG A 1 462 ? -2.622 -1.900 13.648 1.00 23.72 ? 497 ARG A C 1 ATOM 3543 O O . ARG A 1 462 ? -3.821 -2.175 13.536 1.00 23.59 ? 497 ARG A O 1 ATOM 3544 C CB . ARG A 1 462 ? -3.057 -0.206 11.861 1.00 26.55 ? 497 ARG A CB 1 ATOM 3545 C CG . ARG A 1 462 ? -2.630 1.014 11.062 1.00 28.87 ? 497 ARG A CG 1 ATOM 3546 C CD . ARG A 1 462 ? -3.827 1.560 10.289 1.00 32.85 ? 497 ARG A CD 1 ATOM 3547 N NE . ARG A 1 462 ? -3.587 2.867 9.679 1.00 39.02 ? 497 ARG A NE 1 ATOM 3548 C CZ . ARG A 1 462 ? -3.623 4.043 10.317 1.00 44.80 ? 497 ARG A CZ 1 ATOM 3549 N NH1 . ARG A 1 462 ? -3.854 4.121 11.626 1.00 47.16 ? 497 ARG A NH1 1 ATOM 3550 N NH2 . ARG A 1 462 ? -3.407 5.166 9.636 1.00 47.74 ? 497 ARG A NH2 1 ATOM 3551 N N . THR A 1 463 ? -1.804 -2.508 14.494 1.00 21.71 ? 498 THR A N 1 ATOM 3552 C CA . THR A 1 463 ? -2.193 -3.702 15.232 1.00 21.20 ? 498 THR A CA 1 ATOM 3553 C C . THR A 1 463 ? -1.941 -3.541 16.725 1.00 20.61 ? 498 THR A C 1 ATOM 3554 O O . THR A 1 463 ? -0.847 -3.172 17.139 1.00 19.31 ? 498 THR A O 1 ATOM 3555 C CB . THR A 1 463 ? -1.457 -4.944 14.678 1.00 22.09 ? 498 THR A CB 1 ATOM 3556 O OG1 . THR A 1 463 ? -1.860 -5.181 13.324 1.00 22.97 ? 498 THR A OG1 1 ATOM 3557 C CG2 . THR A 1 463 ? -1.791 -6.210 15.492 1.00 22.81 ? 498 THR A CG2 1 ATOM 3558 N N . LYS A 1 464 ? -2.983 -3.825 17.509 1.00 21.02 ? 499 LYS A N 1 ATOM 3559 C CA . LYS A 1 464 ? -2.917 -3.860 18.953 1.00 21.70 ? 499 LYS A CA 1 ATOM 3560 C C . LYS A 1 464 ? -2.812 -5.327 19.385 1.00 20.97 ? 499 LYS A C 1 ATOM 3561 O O . LYS A 1 464 ? -3.486 -6.188 18.840 1.00 21.21 ? 499 LYS A O 1 ATOM 3562 C CB . LYS A 1 464 ? -4.166 -3.225 19.525 1.00 24.53 ? 499 LYS A CB 1 ATOM 3563 C CG . LYS A 1 464 ? -4.189 -3.136 21.025 1.00 26.68 ? 499 LYS A CG 1 ATOM 3564 C CD . LYS A 1 464 ? -5.501 -2.529 21.457 1.00 31.83 ? 499 LYS A CD 1 ATOM 3565 C CE . LYS A 1 464 ? -5.600 -2.379 22.956 1.00 34.89 ? 499 LYS A CE 1 ATOM 3566 N NZ . LYS A 1 464 ? -6.952 -1.857 23.300 1.00 37.57 ? 499 LYS A NZ 1 ATOM 3567 N N . VAL A 1 465 ? -1.949 -5.601 20.345 1.00 18.82 ? 500 VAL A N 1 ATOM 3568 C CA . VAL A 1 465 ? -1.726 -6.955 20.835 1.00 19.36 ? 500 VAL A CA 1 ATOM 3569 C C . VAL A 1 465 ? -1.882 -6.913 22.343 1.00 19.01 ? 500 VAL A C 1 ATOM 3570 O O . VAL A 1 465 ? -1.713 -5.859 22.936 1.00 18.92 ? 500 VAL A O 1 ATOM 3571 C CB . VAL A 1 465 ? -0.336 -7.501 20.442 1.00 20.16 ? 500 VAL A CB 1 ATOM 3572 C CG1 . VAL A 1 465 ? -0.168 -7.452 18.939 1.00 21.75 ? 500 VAL A CG1 1 ATOM 3573 C CG2 . VAL A 1 465 ? 0.803 -6.751 21.122 1.00 19.08 ? 500 VAL A CG2 1 ATOM 3574 N N . PRO A 1 466 ? -2.183 -8.049 22.961 1.00 19.40 ? 501 PRO A N 1 ATOM 3575 C CA . PRO A 1 466 ? -2.354 -8.006 24.407 1.00 18.92 ? 501 PRO A CA 1 ATOM 3576 C C . PRO A 1 466 ? -1.070 -7.669 25.167 1.00 17.29 ? 501 PRO A C 1 ATOM 3577 O O . PRO A 1 466 ? 0.042 -7.834 24.641 1.00 16.09 ? 501 PRO A O 1 ATOM 3578 C CB . PRO A 1 466 ? -2.801 -9.423 24.754 1.00 21.02 ? 501 PRO A CB 1 ATOM 3579 C CG . PRO A 1 466 ? -3.340 -9.994 23.504 1.00 22.27 ? 501 PRO A CG 1 ATOM 3580 C CD . PRO A 1 466 ? -2.581 -9.350 22.394 1.00 20.30 ? 501 PRO A CD 1 ATOM 3581 N N . PRO A 1 467 ? -1.208 -7.216 26.414 1.00 17.55 ? 502 PRO A N 1 ATOM 3582 C CA . PRO A 1 467 ? 0.005 -7.009 27.221 1.00 16.75 ? 502 PRO A CA 1 ATOM 3583 C C . PRO A 1 467 ? 0.828 -8.281 27.347 1.00 16.56 ? 502 PRO A C 1 ATOM 3584 O O . PRO A 1 467 ? 0.265 -9.368 27.407 1.00 16.40 ? 502 PRO A O 1 ATOM 3585 C CB . PRO A 1 467 ? -0.542 -6.623 28.593 1.00 17.93 ? 502 PRO A CB 1 ATOM 3586 C CG . PRO A 1 467 ? -1.913 -6.120 28.329 1.00 20.49 ? 502 PRO A CG 1 ATOM 3587 C CD . PRO A 1 467 ? -2.437 -6.915 27.171 1.00 19.31 ? 502 PRO A CD 1 ATOM 3588 N N . PHE A 1 468 ? 2.156 -8.148 27.396 1.00 14.77 ? 503 PHE A N 1 ATOM 3589 C CA . PHE A 1 468 ? 3.029 -9.316 27.497 1.00 14.65 ? 503 PHE A CA 1 ATOM 3590 C C . PHE A 1 468 ? 4.220 -8.940 28.371 1.00 14.08 ? 503 PHE A C 1 ATOM 3591 O O . PHE A 1 468 ? 4.409 -7.755 28.698 1.00 13.93 ? 503 PHE A O 1 ATOM 3592 C CB . PHE A 1 468 ? 3.470 -9.787 26.098 1.00 15.31 ? 503 PHE A CB 1 ATOM 3593 C CG . PHE A 1 468 ? 4.299 -8.777 25.345 1.00 15.42 ? 503 PHE A CG 1 ATOM 3594 C CD1 . PHE A 1 468 ? 5.678 -8.677 25.574 1.00 15.10 ? 503 PHE A CD1 1 ATOM 3595 C CD2 . PHE A 1 468 ? 3.707 -7.885 24.460 1.00 17.23 ? 503 PHE A CD2 1 ATOM 3596 C CE1 . PHE A 1 468 ? 6.447 -7.728 24.927 1.00 15.82 ? 503 PHE A CE1 1 ATOM 3597 C CE2 . PHE A 1 468 ? 4.489 -6.930 23.782 1.00 18.11 ? 503 PHE A CE2 1 ATOM 3598 C CZ . PHE A 1 468 ? 5.855 -6.857 24.026 1.00 17.05 ? 503 PHE A CZ 1 ATOM 3599 N N . GLU A 1 469 ? 5.036 -9.932 28.690 1.00 14.13 ? 504 GLU A N 1 ATOM 3600 C CA . GLU A 1 469 ? 6.206 -9.749 29.549 1.00 14.34 ? 504 GLU A CA 1 ATOM 3601 C C . GLU A 1 469 ? 7.501 -9.473 28.796 1.00 14.63 ? 504 GLU A C 1 ATOM 3602 O O . GLU A 1 469 ? 7.751 -10.035 27.728 1.00 14.90 ? 504 GLU A O 1 ATOM 3603 C CB . GLU A 1 469 ? 6.408 -10.974 30.421 1.00 15.21 ? 504 GLU A CB 1 ATOM 3604 C CG . GLU A 1 469 ? 5.190 -11.276 31.251 1.00 17.25 ? 504 GLU A CG 1 ATOM 3605 C CD . GLU A 1 469 ? 5.412 -12.334 32.321 1.00 18.03 ? 504 GLU A CD 1 ATOM 3606 O OE1 . GLU A 1 469 ? 6.270 -13.245 32.133 1.00 18.34 ? 504 GLU A OE1 1 ATOM 3607 O OE2 . GLU A 1 469 ? 4.673 -12.257 33.337 1.00 20.99 ? 504 GLU A OE2 1 ATOM 3608 N N . ASN A 1 470 ? 8.365 -8.636 29.369 1.00 13.06 ? 505 ASN A N 1 ATOM 3609 C CA . ASN A 1 470 ? 9.593 -8.252 28.629 1.00 13.92 ? 505 ASN A CA 1 ATOM 3610 C C . ASN A 1 470 ? 10.580 -9.424 28.403 1.00 12.97 ? 505 ASN A C 1 ATOM 3611 O O . ASN A 1 470 ? 11.404 -9.352 27.486 1.00 14.08 ? 505 ASN A O 1 ATOM 3612 C CB . ASN A 1 470 ? 10.261 -7.004 29.235 1.00 15.27 ? 505 ASN A CB 1 ATOM 3613 C CG . ASN A 1 470 ? 10.851 -7.236 30.614 1.00 16.77 ? 505 ASN A CG 1 ATOM 3614 O OD1 . ASN A 1 470 ? 10.688 -8.280 31.225 1.00 16.76 ? 505 ASN A OD1 1 ATOM 3615 N ND2 . ASN A 1 470 ? 11.572 -6.230 31.104 1.00 18.62 ? 505 ASN A ND2 1 ATOM 3616 N N . ILE A 1 471 ? 10.455 -10.518 29.176 1.00 12.06 ? 506 ILE A N 1 ATOM 3617 C CA . ILE A 1 471 ? 11.274 -11.721 28.964 1.00 13.09 ? 506 ILE A CA 1 ATOM 3618 C C . ILE A 1 471 ? 11.057 -12.322 27.547 1.00 13.97 ? 506 ILE A C 1 ATOM 3619 O O . ILE A 1 471 ? 11.893 -13.094 27.051 1.00 14.60 ? 506 ILE A O 1 ATOM 3620 C CB . ILE A 1 471 ? 11.061 -12.825 30.053 1.00 13.59 ? 506 ILE A CB 1 ATOM 3621 C CG1 . ILE A 1 471 ? 9.614 -13.325 30.077 1.00 13.91 ? 506 ILE A CG1 1 ATOM 3622 C CG2 . ILE A 1 471 ? 11.501 -12.349 31.414 1.00 13.53 ? 506 ILE A CG2 1 ATOM 3623 C CD1 . ILE A 1 471 ? 9.357 -14.555 30.914 1.00 14.18 ? 506 ILE A CD1 1 ATOM 3624 N N . GLU A 1 472 ? 9.932 -11.967 26.918 1.00 13.65 ? 507 GLU A N 1 ATOM 3625 C CA . GLU A 1 472 ? 9.564 -12.547 25.646 1.00 13.85 ? 507 GLU A CA 1 ATOM 3626 C C . GLU A 1 472 ? 10.261 -11.856 24.481 1.00 13.96 ? 507 GLU A C 1 ATOM 3627 O O . GLU A 1 472 ? 10.251 -12.383 23.375 1.00 14.12 ? 507 GLU A O 1 ATOM 3628 C CB . GLU A 1 472 ? 8.053 -12.455 25.414 1.00 13.73 ? 507 GLU A CB 1 ATOM 3629 C CG . GLU A 1 472 ? 7.192 -13.180 26.440 1.00 14.43 ? 507 GLU A CG 1 ATOM 3630 C CD . GLU A 1 472 ? 7.484 -14.661 26.523 1.00 15.06 ? 507 GLU A CD 1 ATOM 3631 O OE1 . GLU A 1 472 ? 7.866 -15.284 25.503 1.00 16.37 ? 507 GLU A OE1 1 ATOM 3632 O OE2 . GLU A 1 472 ? 7.319 -15.221 27.648 1.00 17.83 ? 507 GLU A OE2 1 ATOM 3633 N N . LEU A 1 473 ? 10.831 -10.679 24.708 1.00 14.64 ? 508 LEU A N 1 ATOM 3634 C CA . LEU A 1 473 ? 11.287 -9.848 23.582 1.00 14.94 ? 508 LEU A CA 1 ATOM 3635 C C . LEU A 1 473 ? 12.584 -10.320 22.944 1.00 15.21 ? 508 LEU A C 1 ATOM 3636 O O . LEU A 1 473 ? 12.771 -10.168 21.727 1.00 16.98 ? 508 LEU A O 1 ATOM 3637 C CB . LEU A 1 473 ? 11.382 -8.375 23.979 1.00 18.75 ? 508 LEU A CB 1 ATOM 3638 C CG . LEU A 1 473 ? 10.056 -7.613 23.823 1.00 20.94 ? 508 LEU A CG 1 ATOM 3639 C CD1 . LEU A 1 473 ? 10.235 -6.142 24.192 1.00 22.12 ? 508 LEU A CD1 1 ATOM 3640 C CD2 . LEU A 1 473 ? 9.491 -7.750 22.404 1.00 21.95 ? 508 LEU A CD2 1 ATOM 3641 N N . TYR A 1 474 ? 13.488 -10.876 23.733 1.00 14.29 ? 509 TYR A N 1 ATOM 3642 C CA . TYR A 1 474 ? 14.739 -11.424 23.169 1.00 13.85 ? 509 TYR A CA 1 ATOM 3643 C C . TYR A 1 474 ? 14.495 -12.396 21.998 1.00 13.61 ? 509 TYR A C 1 ATOM 3644 O O . TYR A 1 474 ? 15.133 -12.273 20.935 1.00 15.14 ? 509 TYR A O 1 ATOM 3645 C CB . TYR A 1 474 ? 15.554 -12.070 24.267 1.00 13.88 ? 509 TYR A CB 1 ATOM 3646 C CG . TYR A 1 474 ? 16.786 -12.820 23.828 1.00 13.07 ? 509 TYR A CG 1 ATOM 3647 C CD1 . TYR A 1 474 ? 17.949 -12.157 23.460 1.00 14.18 ? 509 TYR A CD1 1 ATOM 3648 C CD2 . TYR A 1 474 ? 16.794 -14.194 23.793 1.00 12.84 ? 509 TYR A CD2 1 ATOM 3649 C CE1 . TYR A 1 474 ? 19.094 -12.859 23.069 1.00 13.05 ? 509 TYR A CE1 1 ATOM 3650 C CE2 . TYR A 1 474 ? 17.919 -14.903 23.434 1.00 12.89 ? 509 TYR A CE2 1 ATOM 3651 C CZ . TYR A 1 474 ? 19.072 -14.252 23.066 1.00 13.64 ? 509 TYR A CZ 1 ATOM 3652 O OH . TYR A 1 474 ? 20.168 -15.004 22.678 1.00 13.24 ? 509 TYR A OH 1 ATOM 3653 N N . ASN A 1 475 ? 13.580 -13.355 22.158 1.00 12.69 ? 510 ASN A N 1 ATOM 3654 C CA . ASN A 1 475 ? 13.243 -14.263 21.049 1.00 13.80 ? 510 ASN A CA 1 ATOM 3655 C C . ASN A 1 475 ? 12.800 -13.507 19.793 1.00 14.36 ? 510 ASN A C 1 ATOM 3656 O O . ASN A 1 475 ? 13.193 -13.851 18.695 1.00 14.79 ? 510 ASN A O 1 ATOM 3657 C CB . ASN A 1 475 ? 12.142 -15.269 21.421 1.00 14.02 ? 510 ASN A CB 1 ATOM 3658 C CG . ASN A 1 475 ? 12.629 -16.378 22.330 1.00 14.45 ? 510 ASN A CG 1 ATOM 3659 O OD1 . ASN A 1 475 ? 13.787 -16.804 22.276 1.00 14.23 ? 510 ASN A OD1 1 ATOM 3660 N ND2 . ASN A 1 475 ? 11.718 -16.878 23.178 1.00 13.92 ? 510 ASN A ND2 1 ATOM 3661 N N . VAL A 1 476 ? 11.991 -12.471 19.975 1.00 13.96 ? 511 VAL A N 1 ATOM 3662 C CA . VAL A 1 476 ? 11.450 -11.704 18.848 1.00 15.72 ? 511 VAL A CA 1 ATOM 3663 C C . VAL A 1 476 ? 12.563 -10.903 18.182 1.00 15.25 ? 511 VAL A C 1 ATOM 3664 O O . VAL A 1 476 ? 12.641 -10.826 16.934 1.00 17.58 ? 511 VAL A O 1 ATOM 3665 C CB . VAL A 1 476 ? 10.362 -10.726 19.309 1.00 16.25 ? 511 VAL A CB 1 ATOM 3666 C CG1 . VAL A 1 476 ? 9.958 -9.779 18.162 1.00 17.91 ? 511 VAL A CG1 1 ATOM 3667 C CG2 . VAL A 1 476 ? 9.164 -11.479 19.887 1.00 18.00 ? 511 VAL A CG2 1 ATOM 3668 N N . MET A 1 477 ? 13.421 -10.286 18.994 1.00 14.67 ? 512 MET A N 1 ATOM 3669 C CA . MET A 1 477 ? 14.553 -9.548 18.428 1.00 15.50 ? 512 MET A CA 1 ATOM 3670 C C . MET A 1 477 ? 15.520 -10.476 17.672 1.00 16.32 ? 512 MET A C 1 ATOM 3671 O O . MET A 1 477 ? 16.036 -10.092 16.606 1.00 15.82 ? 512 MET A O 1 ATOM 3672 C CB . MET A 1 477 ? 15.259 -8.715 19.493 1.00 15.75 ? 512 MET A CB 1 ATOM 3673 C CG . MET A 1 477 ? 14.354 -7.647 20.106 1.00 17.06 ? 512 MET A CG 1 ATOM 3674 S SD . MET A 1 477 ? 15.222 -6.560 21.228 1.00 18.92 ? 512 MET A SD 1 ATOM 3675 C CE . MET A 1 477 ? 15.569 -7.654 22.612 1.00 19.51 ? 512 MET A CE 1 ATOM 3676 N N . CYS A 1 478 ? 15.694 -11.712 18.157 1.00 15.34 ? 513 CYS A N 1 ATOM 3677 C CA . CYS A 1 478 ? 16.480 -12.709 17.425 1.00 16.06 ? 513 CYS A CA 1 ATOM 3678 C C . CYS A 1 478 ? 15.790 -13.031 16.106 1.00 16.71 ? 513 CYS A C 1 ATOM 3679 O O . CYS A 1 478 ? 16.441 -13.048 15.055 1.00 17.98 ? 513 CYS A O 1 ATOM 3680 C CB . CYS A 1 478 ? 16.710 -13.979 18.260 1.00 16.42 ? 513 CYS A CB 1 ATOM 3681 S SG . CYS A 1 478 ? 17.908 -13.726 19.573 1.00 16.66 ? 513 CYS A SG 1 ATOM 3682 N N . ASP A 1 479 ? 14.482 -13.255 16.147 1.00 16.54 ? 514 ASP A N 1 ATOM 3683 C CA . ASP A 1 479 ? 13.722 -13.518 14.921 1.00 18.63 ? 514 ASP A CA 1 ATOM 3684 C C . ASP A 1 479 ? 13.893 -12.371 13.917 1.00 17.88 ? 514 ASP A C 1 ATOM 3685 O O . ASP A 1 479 ? 14.083 -12.610 12.705 1.00 18.36 ? 514 ASP A O 1 ATOM 3686 C CB . ASP A 1 479 ? 12.228 -13.723 15.221 1.00 20.74 ? 514 ASP A CB 1 ATOM 3687 C CG . ASP A 1 479 ? 11.921 -15.056 15.950 1.00 23.71 ? 514 ASP A CG 1 ATOM 3688 O OD1 . ASP A 1 479 ? 12.759 -15.980 15.965 1.00 25.22 ? 514 ASP A OD1 1 ATOM 3689 O OD2 . ASP A 1 479 ? 10.816 -15.169 16.526 1.00 26.35 ? 514 ASP A OD2 1 ATOM 3690 N N . LEU A 1 480 ? 13.839 -11.144 14.422 1.00 17.70 ? 515 LEU A N 1 ATOM 3691 C CA . LEU A 1 480 ? 13.907 -9.949 13.576 1.00 18.86 ? 515 LEU A CA 1 ATOM 3692 C C . LEU A 1 480 ? 15.269 -9.813 12.889 1.00 20.08 ? 515 LEU A C 1 ATOM 3693 O O . LEU A 1 480 ? 15.371 -9.097 11.865 1.00 19.68 ? 515 LEU A O 1 ATOM 3694 C CB . LEU A 1 480 ? 13.619 -8.692 14.367 1.00 19.92 ? 515 LEU A CB 1 ATOM 3695 C CG . LEU A 1 480 ? 12.176 -8.464 14.816 1.00 22.06 ? 515 LEU A CG 1 ATOM 3696 C CD1 . LEU A 1 480 ? 12.140 -7.355 15.854 1.00 23.02 ? 515 LEU A CD1 1 ATOM 3697 C CD2 . LEU A 1 480 ? 11.282 -8.116 13.649 1.00 23.41 ? 515 LEU A CD2 1 ATOM 3698 N N . LEU A 1 481 ? 16.293 -10.498 13.422 1.00 17.94 ? 516 LEU A N 1 ATOM 3699 C CA . LEU A 1 481 ? 17.671 -10.445 12.873 1.00 17.10 ? 516 LEU A CA 1 ATOM 3700 C C . LEU A 1 481 ? 18.150 -11.753 12.265 1.00 18.69 ? 516 LEU A C 1 ATOM 3701 O O . LEU A 1 481 ? 19.291 -11.841 11.776 1.00 18.21 ? 516 LEU A O 1 ATOM 3702 C CB . LEU A 1 481 ? 18.642 -10.020 13.986 1.00 17.26 ? 516 LEU A CB 1 ATOM 3703 C CG . LEU A 1 481 ? 18.452 -8.586 14.475 1.00 17.31 ? 516 LEU A CG 1 ATOM 3704 C CD1 . LEU A 1 481 ? 19.185 -8.365 15.782 1.00 17.36 ? 516 LEU A CD1 1 ATOM 3705 C CD2 . LEU A 1 481 ? 18.948 -7.616 13.412 1.00 17.98 ? 516 LEU A CD2 1 ATOM 3706 N N . GLY A 1 482 ? 17.264 -12.745 12.226 1.00 17.76 ? 517 GLY A N 1 ATOM 3707 C CA . GLY A 1 482 ? 17.569 -14.041 11.682 1.00 18.47 ? 517 GLY A CA 1 ATOM 3708 C C . GLY A 1 482 ? 18.504 -14.831 12.557 1.00 18.50 ? 517 GLY A C 1 ATOM 3709 O O . GLY A 1 482 ? 19.253 -15.665 12.065 1.00 19.32 ? 517 GLY A O 1 ATOM 3710 N N . LEU A 1 483 ? 18.445 -14.590 13.864 1.00 17.41 ? 518 LEU A N 1 ATOM 3711 C CA . LEU A 1 483 ? 19.337 -15.237 14.802 1.00 18.21 ? 518 LEU A CA 1 ATOM 3712 C C . LEU A 1 483 ? 18.662 -16.395 15.534 1.00 18.75 ? 518 LEU A C 1 ATOM 3713 O O . LEU A 1 483 ? 17.477 -16.325 15.823 1.00 18.73 ? 518 LEU A O 1 ATOM 3714 C CB . LEU A 1 483 ? 19.785 -14.205 15.820 1.00 17.70 ? 518 LEU A CB 1 ATOM 3715 C CG . LEU A 1 483 ? 20.539 -12.975 15.336 1.00 18.04 ? 518 LEU A CG 1 ATOM 3716 C CD1 . LEU A 1 483 ? 20.715 -11.996 16.494 1.00 17.28 ? 518 LEU A CD1 1 ATOM 3717 C CD2 . LEU A 1 483 ? 21.872 -13.417 14.783 1.00 18.96 ? 518 LEU A CD2 1 ATOM 3718 N N . LYS A 1 484 ? 19.425 -17.446 15.842 1.00 19.22 ? 519 LYS A N 1 ATOM 3719 C CA . LYS A 1 484 ? 18.970 -18.485 16.755 1.00 20.20 ? 519 LYS A CA 1 ATOM 3720 C C . LYS A 1 484 ? 19.134 -17.979 18.197 1.00 19.26 ? 519 LYS A C 1 ATOM 3721 O O . LYS A 1 484 ? 20.258 -17.706 18.627 1.00 17.68 ? 519 LYS A O 1 ATOM 3722 C CB . LYS A 1 484 ? 19.741 -19.792 16.537 1.00 24.13 ? 519 LYS A CB 1 ATOM 3723 C CG . LYS A 1 484 ? 19.152 -20.953 17.321 1.00 28.71 ? 519 LYS A CG 1 ATOM 3724 C CD . LYS A 1 484 ? 20.040 -22.184 17.324 1.00 34.03 ? 519 LYS A CD 1 ATOM 3725 C CE . LYS A 1 484 ? 19.526 -23.238 18.288 1.00 37.62 ? 519 LYS A CE 1 ATOM 3726 N NZ . LYS A 1 484 ? 20.266 -24.514 18.107 1.00 47.25 ? 519 LYS A NZ 1 ATOM 3727 N N . PRO A 1 485 ? 18.017 -17.837 18.952 1.00 17.74 ? 520 PRO A N 1 ATOM 3728 C CA . PRO A 1 485 ? 18.164 -17.397 20.337 1.00 17.22 ? 520 PRO A CA 1 ATOM 3729 C C . PRO A 1 485 ? 18.901 -18.384 21.237 1.00 17.43 ? 520 PRO A C 1 ATOM 3730 O O . PRO A 1 485 ? 18.730 -19.594 21.094 1.00 17.83 ? 520 PRO A O 1 ATOM 3731 C CB . PRO A 1 485 ? 16.711 -17.225 20.831 1.00 17.77 ? 520 PRO A CB 1 ATOM 3732 C CG . PRO A 1 485 ? 15.823 -17.494 19.666 1.00 18.38 ? 520 PRO A CG 1 ATOM 3733 C CD . PRO A 1 485 ? 16.626 -18.168 18.615 1.00 18.57 ? 520 PRO A CD 1 ATOM 3734 N N . ALA A 1 486 ? 19.710 -17.877 22.160 1.00 16.19 ? 521 ALA A N 1 ATOM 3735 C CA . ALA A 1 486 ? 20.284 -18.703 23.213 1.00 16.51 ? 521 ALA A CA 1 ATOM 3736 C C . ALA A 1 486 ? 19.158 -19.135 24.134 1.00 17.50 ? 521 ALA A C 1 ATOM 3737 O O . ALA A 1 486 ? 18.119 -18.489 24.153 1.00 16.63 ? 521 ALA A O 1 ATOM 3738 C CB . ALA A 1 486 ? 21.335 -17.933 23.993 1.00 16.71 ? 521 ALA A CB 1 ATOM 3739 N N . PRO A 1 487 ? 19.353 -20.231 24.881 1.00 17.23 ? 522 PRO A N 1 ATOM 3740 C CA . PRO A 1 487 ? 18.267 -20.689 25.768 1.00 17.54 ? 522 PRO A CA 1 ATOM 3741 C C . PRO A 1 487 ? 17.800 -19.621 26.741 1.00 16.04 ? 522 PRO A C 1 ATOM 3742 O O . PRO A 1 487 ? 18.620 -18.981 27.402 1.00 15.80 ? 522 PRO A O 1 ATOM 3743 C CB . PRO A 1 487 ? 18.911 -21.854 26.516 1.00 18.89 ? 522 PRO A CB 1 ATOM 3744 C CG . PRO A 1 487 ? 20.007 -22.340 25.599 1.00 19.62 ? 522 PRO A CG 1 ATOM 3745 C CD . PRO A 1 487 ? 20.571 -21.058 25.040 1.00 18.66 ? 522 PRO A CD 1 ATOM 3746 N N . ASN A 1 488 ? 16.497 -19.419 26.844 1.00 14.46 ? 523 ASN A N 1 ATOM 3747 C CA . ASN A 1 488 ? 16.020 -18.307 27.643 1.00 13.92 ? 523 ASN A CA 1 ATOM 3748 C C . ASN A 1 488 ? 14.644 -18.584 28.220 1.00 14.61 ? 523 ASN A C 1 ATOM 3749 O O . ASN A 1 488 ? 14.092 -19.674 28.035 1.00 14.48 ? 523 ASN A O 1 ATOM 3750 C CB . ASN A 1 488 ? 16.093 -16.995 26.836 1.00 13.55 ? 523 ASN A CB 1 ATOM 3751 C CG . ASN A 1 488 ? 15.077 -16.930 25.722 1.00 13.71 ? 523 ASN A CG 1 ATOM 3752 O OD1 . ASN A 1 488 ? 13.961 -16.445 25.902 1.00 14.62 ? 523 ASN A OD1 1 ATOM 3753 N ND2 . ASN A 1 488 ? 15.456 -17.421 24.565 1.00 13.94 ? 523 ASN A ND2 1 ATOM 3754 N N . ASN A 1 489 ? 14.108 -17.619 28.955 1.00 14.26 ? 524 ASN A N 1 ATOM 3755 C CA . ASN A 1 489 ? 12.839 -17.827 29.648 1.00 14.35 ? 524 ASN A CA 1 ATOM 3756 C C . ASN A 1 489 ? 11.587 -17.368 28.932 1.00 14.87 ? 524 ASN A C 1 ATOM 3757 O O . ASN A 1 489 ? 10.486 -17.568 29.440 1.00 14.10 ? 524 ASN A O 1 ATOM 3758 C CB . ASN A 1 489 ? 12.899 -17.225 31.043 1.00 13.65 ? 524 ASN A CB 1 ATOM 3759 C CG . ASN A 1 489 ? 14.049 -17.765 31.838 1.00 14.29 ? 524 ASN A CG 1 ATOM 3760 O OD1 . ASN A 1 489 ? 14.875 -17.001 32.363 1.00 14.58 ? 524 ASN A OD1 1 ATOM 3761 N ND2 . ASN A 1 489 ? 14.117 -19.089 31.944 1.00 14.27 ? 524 ASN A ND2 1 ATOM 3762 N N . GLY A 1 490 ? 11.736 -16.794 27.738 1.00 13.97 ? 525 GLY A N 1 ATOM 3763 C CA . GLY A 1 490 ? 10.589 -16.610 26.861 1.00 14.80 ? 525 GLY A CA 1 ATOM 3764 C C . GLY A 1 490 ? 9.996 -17.955 26.434 1.00 15.40 ? 525 GLY A C 1 ATOM 3765 O O . GLY A 1 490 ? 10.587 -19.049 26.634 1.00 17.33 ? 525 GLY A O 1 ATOM 3766 N N . THR A 1 491 ? 8.809 -17.867 25.866 1.00 15.77 ? 526 THR A N 1 ATOM 3767 C CA . THR A 1 491 ? 8.110 -19.005 25.291 1.00 16.00 ? 526 THR A CA 1 ATOM 3768 C C . THR A 1 491 ? 8.058 -18.646 23.806 1.00 16.71 ? 526 THR A C 1 ATOM 3769 O O . THR A 1 491 ? 7.214 -17.848 23.366 1.00 15.25 ? 526 THR A O 1 ATOM 3770 C CB . THR A 1 491 ? 6.730 -19.166 25.936 1.00 17.25 ? 526 THR A CB 1 ATOM 3771 O OG1 . THR A 1 491 ? 6.917 -19.526 27.321 1.00 15.82 ? 526 THR A OG1 1 ATOM 3772 C CG2 . THR A 1 491 ? 5.905 -20.269 25.289 1.00 16.67 ? 526 THR A CG2 1 ATOM 3773 N N . HIS A 1 492 ? 9.015 -19.192 23.053 1.00 15.41 ? 527 HIS A N 1 ATOM 3774 C CA . HIS A 1 492 ? 9.195 -18.778 21.660 1.00 16.22 ? 527 HIS A CA 1 ATOM 3775 C C . HIS A 1 492 ? 7.976 -19.189 20.829 1.00 16.19 ? 527 HIS A C 1 ATOM 3776 O O . HIS A 1 492 ? 7.598 -20.364 20.804 1.00 15.91 ? 527 HIS A O 1 ATOM 3777 C CB . HIS A 1 492 ? 10.452 -19.431 21.108 1.00 16.85 ? 527 HIS A CB 1 ATOM 3778 C CG . HIS A 1 492 ? 11.011 -18.739 19.912 1.00 18.33 ? 527 HIS A CG 1 ATOM 3779 N ND1 . HIS A 1 492 ? 12.163 -19.160 19.302 1.00 20.26 ? 527 HIS A ND1 1 ATOM 3780 C CD2 . HIS A 1 492 ? 10.581 -17.661 19.215 1.00 19.19 ? 527 HIS A CD2 1 ATOM 3781 C CE1 . HIS A 1 492 ? 12.416 -18.380 18.265 1.00 20.93 ? 527 HIS A CE1 1 ATOM 3782 N NE2 . HIS A 1 492 ? 11.481 -17.453 18.203 1.00 20.07 ? 527 HIS A NE2 1 ATOM 3783 N N . GLY A 1 493 ? 7.363 -18.214 20.162 1.00 15.95 ? 528 GLY A N 1 ATOM 3784 C CA . GLY A 1 493 ? 6.108 -18.405 19.484 1.00 16.09 ? 528 GLY A CA 1 ATOM 3785 C C . GLY A 1 493 ? 4.975 -17.664 20.184 1.00 16.50 ? 528 GLY A C 1 ATOM 3786 O O . GLY A 1 493 ? 3.955 -17.404 19.565 1.00 18.65 ? 528 GLY A O 1 ATOM 3787 N N . SER A 1 494 ? 5.112 -17.364 21.472 1.00 15.53 ? 529 SER A N 1 ATOM 3788 C CA . SER A 1 494 ? 4.034 -16.662 22.163 1.00 15.93 ? 529 SER A CA 1 ATOM 3789 C C . SER A 1 494 ? 3.830 -15.232 21.651 1.00 16.81 ? 529 SER A C 1 ATOM 3790 O O . SER A 1 494 ? 2.787 -14.666 21.899 1.00 16.45 ? 529 SER A O 1 ATOM 3791 C CB . SER A 1 494 ? 4.252 -16.641 23.664 1.00 15.36 ? 529 SER A CB 1 ATOM 3792 O OG . SER A 1 494 ? 5.310 -15.762 24.014 1.00 15.89 ? 529 SER A OG 1 ATOM 3793 N N . LEU A 1 495 ? 4.818 -14.657 20.964 1.00 15.57 ? 530 LEU A N 1 ATOM 3794 C CA . LEU A 1 495 ? 4.695 -13.317 20.387 1.00 17.18 ? 530 LEU A CA 1 ATOM 3795 C C . LEU A 1 495 ? 4.727 -13.333 18.864 1.00 17.55 ? 530 LEU A C 1 ATOM 3796 O O . LEU A 1 495 ? 4.904 -12.286 18.240 1.00 20.24 ? 530 LEU A O 1 ATOM 3797 C CB . LEU A 1 495 ? 5.783 -12.395 20.927 1.00 17.28 ? 530 LEU A CB 1 ATOM 3798 C CG . LEU A 1 495 ? 5.727 -12.056 22.423 1.00 16.24 ? 530 LEU A CG 1 ATOM 3799 C CD1 . LEU A 1 495 ? 6.710 -10.948 22.745 1.00 17.95 ? 530 LEU A CD1 1 ATOM 3800 C CD2 . LEU A 1 495 ? 4.342 -11.636 22.831 1.00 17.31 ? 530 LEU A CD2 1 ATOM 3801 N N . ASN A 1 496 ? 4.478 -14.488 18.254 1.00 18.27 ? 531 ASN A N 1 ATOM 3802 C CA . ASN A 1 496 ? 4.400 -14.538 16.792 1.00 20.13 ? 531 ASN A CA 1 ATOM 3803 C C . ASN A 1 496 ? 3.327 -13.611 16.212 1.00 19.74 ? 531 ASN A C 1 ATOM 3804 O O . ASN A 1 496 ? 3.484 -13.084 15.114 1.00 19.74 ? 531 ASN A O 1 ATOM 3805 C CB . ASN A 1 496 ? 4.211 -15.979 16.283 1.00 21.22 ? 531 ASN A CB 1 ATOM 3806 C CG . ASN A 1 496 ? 5.525 -16.757 16.182 1.00 22.34 ? 531 ASN A CG 1 ATOM 3807 O OD1 . ASN A 1 496 ? 6.573 -16.337 16.654 1.00 23.13 ? 531 ASN A OD1 1 ATOM 3808 N ND2 . ASN A 1 496 ? 5.452 -17.921 15.587 1.00 26.38 ? 531 ASN A ND2 1 ATOM 3809 N N . HIS A 1 497 ? 2.257 -13.384 16.960 1.00 19.89 ? 532 HIS A N 1 ATOM 3810 C CA . HIS A 1 497 ? 1.171 -12.501 16.554 1.00 20.54 ? 532 HIS A CA 1 ATOM 3811 C C . HIS A 1 497 ? 1.560 -11.002 16.466 1.00 20.50 ? 532 HIS A C 1 ATOM 3812 O O . HIS A 1 497 ? 0.737 -10.194 16.062 1.00 21.43 ? 532 HIS A O 1 ATOM 3813 C CB . HIS A 1 497 ? -0.047 -12.725 17.460 1.00 22.12 ? 532 HIS A CB 1 ATOM 3814 C CG . HIS A 1 497 ? 0.171 -12.332 18.891 1.00 21.02 ? 532 HIS A CG 1 ATOM 3815 N ND1 . HIS A 1 497 ? 0.784 -13.147 19.822 1.00 21.80 ? 532 HIS A ND1 1 ATOM 3816 C CD2 . HIS A 1 497 ? -0.177 -11.210 19.553 1.00 21.60 ? 532 HIS A CD2 1 ATOM 3817 C CE1 . HIS A 1 497 ? 0.834 -12.524 20.984 1.00 19.81 ? 532 HIS A CE1 1 ATOM 3818 N NE2 . HIS A 1 497 ? 0.246 -11.354 20.851 1.00 19.48 ? 532 HIS A NE2 1 ATOM 3819 N N . LEU A 1 498 ? 2.788 -10.640 16.870 1.00 18.37 ? 533 LEU A N 1 ATOM 3820 C CA . LEU A 1 498 ? 3.303 -9.278 16.679 1.00 19.07 ? 533 LEU A CA 1 ATOM 3821 C C . LEU A 1 498 ? 3.847 -9.049 15.263 1.00 19.69 ? 533 LEU A C 1 ATOM 3822 O O . LEU A 1 498 ? 4.034 -7.903 14.856 1.00 19.62 ? 533 LEU A O 1 ATOM 3823 C CB . LEU A 1 498 ? 4.423 -8.960 17.661 1.00 18.66 ? 533 LEU A CB 1 ATOM 3824 C CG . LEU A 1 498 ? 3.993 -8.496 19.057 1.00 18.90 ? 533 LEU A CG 1 ATOM 3825 C CD1 . LEU A 1 498 ? 3.070 -9.479 19.759 1.00 21.08 ? 533 LEU A CD1 1 ATOM 3826 C CD2 . LEU A 1 498 ? 5.226 -8.223 19.868 1.00 19.22 ? 533 LEU A CD2 1 ATOM 3827 N N . LEU A 1 499 ? 4.130 -10.129 14.541 1.00 20.36 ? 534 LEU A N 1 ATOM 3828 C CA . LEU A 1 499 ? 4.952 -10.027 13.332 1.00 20.56 ? 534 LEU A CA 1 ATOM 3829 C C . LEU A 1 499 ? 4.152 -10.354 12.107 1.00 21.87 ? 534 LEU A C 1 ATOM 3830 O O . LEU A 1 499 ? 3.351 -11.282 12.117 1.00 22.32 ? 534 LEU A O 1 ATOM 3831 C CB . LEU A 1 499 ? 6.148 -10.974 13.420 1.00 22.28 ? 534 LEU A CB 1 ATOM 3832 C CG . LEU A 1 499 ? 7.002 -10.806 14.680 1.00 23.70 ? 534 LEU A CG 1 ATOM 3833 C CD1 . LEU A 1 499 ? 8.116 -11.847 14.692 1.00 26.50 ? 534 LEU A CD1 1 ATOM 3834 C CD2 . LEU A 1 499 ? 7.550 -9.394 14.778 1.00 23.92 ? 534 LEU A CD2 1 ATOM 3835 N N . ARG A 1 500 ? 4.387 -9.575 11.052 1.00 22.62 ? 535 ARG A N 1 ATOM 3836 C CA . ARG A 1 500 ? 3.864 -9.858 9.717 1.00 25.92 ? 535 ARG A CA 1 ATOM 3837 C C . ARG A 1 500 ? 4.464 -11.140 9.142 1.00 27.60 ? 535 ARG A C 1 ATOM 3838 O O . ARG A 1 500 ? 3.754 -11.918 8.499 1.00 27.57 ? 535 ARG A O 1 ATOM 3839 C CB . ARG A 1 500 ? 4.170 -8.680 8.768 1.00 26.43 ? 535 ARG A CB 1 ATOM 3840 C CG . ARG A 1 500 ? 3.900 -8.972 7.298 1.00 28.88 ? 535 ARG A CG 1 ATOM 3841 C CD . ARG A 1 500 ? 4.323 -7.832 6.385 1.00 31.63 ? 535 ARG A CD 1 ATOM 3842 N NE . ARG A 1 500 ? 3.598 -6.625 6.752 1.00 33.14 ? 535 ARG A NE 1 ATOM 3843 C CZ . ARG A 1 500 ? 2.386 -6.272 6.324 1.00 32.70 ? 535 ARG A CZ 1 ATOM 3844 N NH1 . ARG A 1 500 ? 1.683 -7.009 5.456 1.00 33.05 ? 535 ARG A NH1 1 ATOM 3845 N NH2 . ARG A 1 500 ? 1.876 -5.141 6.769 1.00 33.94 ? 535 ARG A NH2 1 ATOM 3846 N N . THR A 1 501 ? 5.767 -11.338 9.312 1.00 27.03 ? 536 THR A N 1 ATOM 3847 C CA . THR A 1 501 ? 6.409 -12.555 8.817 1.00 34.10 ? 536 THR A CA 1 ATOM 3848 C C . THR A 1 501 ? 7.175 -13.199 9.954 1.00 34.96 ? 536 THR A C 1 ATOM 3849 O O . THR A 1 501 ? 7.994 -12.535 10.597 1.00 34.78 ? 536 THR A O 1 ATOM 3850 C CB . THR A 1 501 ? 7.325 -12.284 7.594 1.00 38.37 ? 536 THR A CB 1 ATOM 3851 O OG1 . THR A 1 501 ? 8.153 -11.141 7.834 1.00 41.15 ? 536 THR A OG1 1 ATOM 3852 C CG2 . THR A 1 501 ? 6.491 -12.028 6.356 1.00 43.10 ? 536 THR A CG2 1 ATOM 3853 N N . ASN A 1 502 ? 6.849 -14.471 10.217 1.00 35.56 ? 537 ASN A N 1 ATOM 3854 C CA . ASN A 1 502 ? 7.529 -15.289 11.215 1.00 35.46 ? 537 ASN A CA 1 ATOM 3855 C C . ASN A 1 502 ? 8.476 -16.266 10.562 1.00 40.34 ? 537 ASN A C 1 ATOM 3856 O O . ASN A 1 502 ? 8.151 -16.874 9.548 1.00 41.40 ? 537 ASN A O 1 ATOM 3857 C CB . ASN A 1 502 ? 6.507 -16.056 12.055 1.00 35.15 ? 537 ASN A CB 1 ATOM 3858 C CG . ASN A 1 502 ? 5.859 -15.168 13.079 1.00 36.00 ? 537 ASN A CG 1 ATOM 3859 O OD1 . ASN A 1 502 ? 6.486 -14.822 14.081 1.00 35.75 ? 537 ASN A OD1 1 ATOM 3860 N ND2 . ASN A 1 502 ? 4.641 -14.729 12.811 1.00 33.10 ? 537 ASN A ND2 1 ATOM 3861 N N . THR A 1 503 ? 9.649 -16.411 11.158 1.00 41.84 ? 538 THR A N 1 ATOM 3862 C CA . THR A 1 503 ? 10.614 -17.421 10.738 1.00 46.87 ? 538 THR A CA 1 ATOM 3863 C C . THR A 1 503 ? 10.700 -18.571 11.747 1.00 39.64 ? 538 THR A C 1 ATOM 3864 O O . THR A 1 503 ? 11.296 -19.588 11.446 1.00 41.54 ? 538 THR A O 1 ATOM 3865 C CB . THR A 1 503 ? 12.012 -16.799 10.456 1.00 51.27 ? 538 THR A CB 1 ATOM 3866 O OG1 . THR A 1 503 ? 12.906 -17.816 9.976 1.00 58.48 ? 538 THR A OG1 1 ATOM 3867 C CG2 . THR A 1 503 ? 12.613 -16.099 11.700 1.00 51.40 ? 538 THR A CG2 1 ATOM 3868 N N . PHE A 1 504 ? 10.111 -18.410 12.932 1.00 34.70 ? 539 PHE A N 1 ATOM 3869 C CA . PHE A 1 504 ? 10.024 -19.495 13.895 1.00 32.38 ? 539 PHE A CA 1 ATOM 3870 C C . PHE A 1 504 ? 8.590 -20.039 14.002 1.00 31.84 ? 539 PHE A C 1 ATOM 3871 O O . PHE A 1 504 ? 7.660 -19.292 14.285 1.00 35.50 ? 539 PHE A O 1 ATOM 3872 C CB . PHE A 1 504 ? 10.457 -19.040 15.278 1.00 29.78 ? 539 PHE A CB 1 ATOM 3873 C CG . PHE A 1 504 ? 10.482 -20.157 16.267 1.00 25.69 ? 539 PHE A CG 1 ATOM 3874 C CD1 . PHE A 1 504 ? 11.517 -21.087 16.250 1.00 26.28 ? 539 PHE A CD1 1 ATOM 3875 C CD2 . PHE A 1 504 ? 9.452 -20.317 17.186 1.00 24.32 ? 539 PHE A CD2 1 ATOM 3876 C CE1 . PHE A 1 504 ? 11.542 -22.160 17.148 1.00 27.20 ? 539 PHE A CE1 1 ATOM 3877 C CE2 . PHE A 1 504 ? 9.475 -21.371 18.077 1.00 23.63 ? 539 PHE A CE2 1 ATOM 3878 C CZ . PHE A 1 504 ? 10.517 -22.297 18.068 1.00 24.72 ? 539 PHE A CZ 1 ATOM 3879 N N . ARG A 1 505 ? 8.434 -21.343 13.808 1.00 30.22 ? 540 ARG A N 1 ATOM 3880 C CA . ARG A 1 505 ? 7.144 -21.985 13.950 1.00 31.78 ? 540 ARG A CA 1 ATOM 3881 C C . ARG A 1 505 ? 7.267 -22.953 15.104 1.00 28.74 ? 540 ARG A C 1 ATOM 3882 O O . ARG A 1 505 ? 8.065 -23.867 15.054 1.00 28.15 ? 540 ARG A O 1 ATOM 3883 C CB . ARG A 1 505 ? 6.733 -22.665 12.644 1.00 37.47 ? 540 ARG A CB 1 ATOM 3884 C CG . ARG A 1 505 ? 6.238 -21.652 11.604 1.00 45.00 ? 540 ARG A CG 1 ATOM 3885 C CD . ARG A 1 505 ? 4.712 -21.503 11.577 1.00 52.31 ? 540 ARG A CD 1 ATOM 3886 N NE . ARG A 1 505 ? 4.106 -20.873 12.773 1.00 54.85 ? 540 ARG A NE 1 ATOM 3887 C CZ . ARG A 1 505 ? 3.656 -19.611 12.872 1.00 57.70 ? 540 ARG A CZ 1 ATOM 3888 N NH1 . ARG A 1 505 ? 3.735 -18.752 11.852 1.00 63.18 ? 540 ARG A NH1 1 ATOM 3889 N NH2 . ARG A 1 505 ? 3.115 -19.189 14.021 1.00 52.56 ? 540 ARG A NH2 1 ATOM 3890 N N . PRO A 1 506 ? 6.509 -22.714 16.182 1.00 28.88 ? 541 PRO A N 1 ATOM 3891 C CA . PRO A 1 506 ? 6.619 -23.570 17.343 1.00 28.15 ? 541 PRO A CA 1 ATOM 3892 C C . PRO A 1 506 ? 5.888 -24.885 17.127 1.00 29.63 ? 541 PRO A C 1 ATOM 3893 O O . PRO A 1 506 ? 4.952 -24.963 16.327 1.00 29.10 ? 541 PRO A O 1 ATOM 3894 C CB . PRO A 1 506 ? 5.956 -22.733 18.441 1.00 27.16 ? 541 PRO A CB 1 ATOM 3895 C CG . PRO A 1 506 ? 4.926 -21.918 17.713 1.00 27.36 ? 541 PRO A CG 1 ATOM 3896 C CD . PRO A 1 506 ? 5.470 -21.679 16.347 1.00 28.66 ? 541 PRO A CD 1 ATOM 3897 N N . THR A 1 507 ? 6.326 -25.907 17.843 1.00 29.83 ? 542 THR A N 1 ATOM 3898 C CA . THR A 1 507 ? 5.733 -27.226 17.760 1.00 30.19 ? 542 THR A CA 1 ATOM 3899 C C . THR A 1 507 ? 5.496 -27.751 19.177 1.00 28.47 ? 542 THR A C 1 ATOM 3900 O O . THR A 1 507 ? 6.318 -27.572 20.056 1.00 27.44 ? 542 THR A O 1 ATOM 3901 C CB . THR A 1 507 ? 6.665 -28.173 16.989 1.00 34.35 ? 542 THR A CB 1 ATOM 3902 O OG1 . THR A 1 507 ? 7.961 -28.164 17.588 1.00 36.33 ? 542 THR A OG1 1 ATOM 3903 C CG2 . THR A 1 507 ? 6.807 -27.719 15.546 1.00 35.97 ? 542 THR A CG2 1 ATOM 3904 N N . MET A 1 508 ? 4.363 -28.393 19.383 1.00 27.30 ? 543 MET A N 1 ATOM 3905 C CA . MET A 1 508 ? 3.995 -28.928 20.688 1.00 30.27 ? 543 MET A CA 1 ATOM 3906 C C . MET A 1 508 ? 4.973 -30.047 21.081 1.00 28.51 ? 543 MET A C 1 ATOM 3907 O O . MET A 1 508 ? 5.274 -30.889 20.250 1.00 30.33 ? 543 MET A O 1 ATOM 3908 C CB . MET A 1 508 ? 2.566 -29.433 20.577 1.00 32.61 ? 543 MET A CB 1 ATOM 3909 C CG . MET A 1 508 ? 1.878 -29.846 21.844 1.00 34.44 ? 543 MET A CG 1 ATOM 3910 S SD . MET A 1 508 ? 0.208 -30.345 21.369 1.00 36.90 ? 543 MET A SD 1 ATOM 3911 C CE . MET A 1 508 ? -0.607 -28.761 21.141 1.00 36.86 ? 543 MET A CE 1 ATOM 3912 N N . PRO A 1 509 ? 5.501 -30.044 22.326 1.00 28.68 ? 544 PRO A N 1 ATOM 3913 C CA . PRO A 1 509 ? 6.486 -31.091 22.695 1.00 28.78 ? 544 PRO A CA 1 ATOM 3914 C C . PRO A 1 509 ? 5.877 -32.499 22.740 1.00 29.62 ? 544 PRO A C 1 ATOM 3915 O O . PRO A 1 509 ? 4.687 -32.653 23.011 1.00 25.30 ? 544 PRO A O 1 ATOM 3916 C CB . PRO A 1 509 ? 6.989 -30.654 24.071 1.00 28.73 ? 544 PRO A CB 1 ATOM 3917 C CG . PRO A 1 509 ? 5.955 -29.711 24.590 1.00 28.14 ? 544 PRO A CG 1 ATOM 3918 C CD . PRO A 1 509 ? 5.271 -29.084 23.416 1.00 26.90 ? 544 PRO A CD 1 ATOM 3919 N N . ASP A 1 510 ? 6.680 -33.514 22.432 1.00 30.62 ? 545 ASP A N 1 ATOM 3920 C CA . ASP A 1 510 ? 6.186 -34.888 22.452 1.00 32.03 ? 545 ASP A CA 1 ATOM 3921 C C . ASP A 1 510 ? 5.989 -35.354 23.887 1.00 28.36 ? 545 ASP A C 1 ATOM 3922 O O . ASP A 1 510 ? 6.793 -35.044 24.752 1.00 27.79 ? 545 ASP A O 1 ATOM 3923 C CB . ASP A 1 510 ? 7.138 -35.841 21.713 1.00 37.58 ? 545 ASP A CB 1 ATOM 3924 C CG . ASP A 1 510 ? 6.854 -35.916 20.221 1.00 44.05 ? 545 ASP A CG 1 ATOM 3925 O OD1 . ASP A 1 510 ? 6.404 -34.904 19.635 1.00 46.23 ? 545 ASP A OD1 1 ATOM 3926 O OD2 . ASP A 1 510 ? 7.085 -36.997 19.628 1.00 51.89 ? 545 ASP A OD2 1 ATOM 3927 N N . GLU A 1 511 ? 4.902 -36.075 24.140 1.00 29.85 ? 546 GLU A N 1 ATOM 3928 C CA . GLU A 1 511 ? 4.699 -36.701 25.450 1.00 30.08 ? 546 GLU A CA 1 ATOM 3929 C C . GLU A 1 511 ? 5.829 -37.698 25.702 1.00 29.06 ? 546 GLU A C 1 ATOM 3930 O O . GLU A 1 511 ? 6.237 -38.443 24.795 1.00 30.99 ? 546 GLU A O 1 ATOM 3931 C CB . GLU A 1 511 ? 3.333 -37.395 25.558 1.00 33.55 ? 546 GLU A CB 1 ATOM 3932 C CG . GLU A 1 511 ? 3.158 -38.135 26.882 1.00 37.18 ? 546 GLU A CG 1 ATOM 3933 C CD . GLU A 1 511 ? 1.729 -38.195 27.411 1.00 43.32 ? 546 GLU A CD 1 ATOM 3934 O OE1 . GLU A 1 511 ? 0.811 -38.468 26.594 1.00 46.51 ? 546 GLU A OE1 1 ATOM 3935 O OE2 . GLU A 1 511 ? 1.541 -38.022 28.667 1.00 36.38 ? 546 GLU A OE2 1 ATOM 3936 N N . VAL A 1 512 ? 6.340 -37.701 26.924 1.00 27.01 ? 547 VAL A N 1 ATOM 3937 C CA . VAL A 1 512 ? 7.451 -38.557 27.298 1.00 29.16 ? 547 VAL A CA 1 ATOM 3938 C C . VAL A 1 512 ? 6.945 -39.840 27.962 1.00 28.97 ? 547 VAL A C 1 ATOM 3939 O O . VAL A 1 512 ? 7.364 -40.914 27.584 1.00 30.87 ? 547 VAL A O 1 ATOM 3940 C CB . VAL A 1 512 ? 8.478 -37.824 28.184 1.00 28.32 ? 547 VAL A CB 1 ATOM 3941 C CG1 . VAL A 1 512 ? 9.529 -38.793 28.713 1.00 31.06 ? 547 VAL A CG1 1 ATOM 3942 C CG2 . VAL A 1 512 ? 9.147 -36.703 27.391 1.00 28.74 ? 547 VAL A CG2 1 ATOM 3943 N N . SER A 1 513 ? 6.070 -39.723 28.953 1.00 29.47 ? 548 SER A N 1 ATOM 3944 C CA . SER A 1 513 ? 5.527 -40.888 29.648 1.00 31.36 ? 548 SER A CA 1 ATOM 3945 C C . SER A 1 513 ? 4.108 -41.139 29.199 1.00 32.41 ? 548 SER A C 1 ATOM 3946 O O . SER A 1 513 ? 3.313 -40.229 29.179 1.00 34.87 ? 548 SER A O 1 ATOM 3947 C CB . SER A 1 513 ? 5.559 -40.660 31.152 1.00 31.02 ? 548 SER A CB 1 ATOM 3948 O OG . SER A 1 513 ? 6.896 -40.679 31.591 1.00 32.81 ? 548 SER A OG 1 ATOM 3949 N N . ARG A 1 514 ? 3.793 -42.380 28.859 1.00 34.47 ? 549 ARG A N 1 ATOM 3950 C CA . ARG A 1 514 ? 2.440 -42.748 28.465 1.00 36.68 ? 549 ARG A CA 1 ATOM 3951 C C . ARG A 1 514 ? 1.713 -43.333 29.675 1.00 34.58 ? 549 ARG A C 1 ATOM 3952 O O . ARG A 1 514 ? 2.285 -44.142 30.398 1.00 35.47 ? 549 ARG A O 1 ATOM 3953 C CB . ARG A 1 514 ? 2.472 -43.756 27.321 1.00 40.88 ? 549 ARG A CB 1 ATOM 3954 C CG . ARG A 1 514 ? 2.939 -43.175 25.989 1.00 44.75 ? 549 ARG A CG 1 ATOM 3955 C CD . ARG A 1 514 ? 1.866 -42.308 25.329 1.00 49.74 ? 549 ARG A CD 1 ATOM 3956 N NE . ARG A 1 514 ? 0.793 -43.131 24.743 1.00 53.60 ? 549 ARG A NE 1 ATOM 3957 C CZ . ARG A 1 514 ? 0.271 -43.000 23.518 1.00 59.73 ? 549 ARG A CZ 1 ATOM 3958 N NH1 . ARG A 1 514 ? 0.672 -42.057 22.664 1.00 60.88 ? 549 ARG A NH1 1 ATOM 3959 N NH2 . ARG A 1 514 ? -0.691 -43.836 23.140 1.00 63.68 ? 549 ARG A NH2 1 ATOM 3960 N N . PRO A 1 515 ? 0.445 -42.958 29.881 1.00 33.42 ? 550 PRO A N 1 ATOM 3961 C CA . PRO A 1 515 ? -0.258 -43.463 31.069 1.00 33.16 ? 550 PRO A CA 1 ATOM 3962 C C . PRO A 1 515 ? -0.752 -44.898 30.956 1.00 34.25 ? 550 PRO A C 1 ATOM 3963 O O . PRO A 1 515 ? -0.991 -45.393 29.856 1.00 33.59 ? 550 PRO A O 1 ATOM 3964 C CB . PRO A 1 515 ? -1.485 -42.572 31.146 1.00 33.12 ? 550 PRO A CB 1 ATOM 3965 C CG . PRO A 1 515 ? -1.755 -42.163 29.741 1.00 33.21 ? 550 PRO A CG 1 ATOM 3966 C CD . PRO A 1 515 ? -0.444 -42.166 29.011 1.00 32.18 ? 550 PRO A CD 1 ATOM 3967 N N . ASN A 1 516 ? -0.932 -45.530 32.109 1.00 33.78 ? 551 ASN A N 1 ATOM 3968 C CA . ASN A 1 516 ? -1.699 -46.757 32.217 1.00 35.98 ? 551 ASN A CA 1 ATOM 3969 C C . ASN A 1 516 ? -3.168 -46.392 32.411 1.00 33.88 ? 551 ASN A C 1 ATOM 3970 O O . ASN A 1 516 ? -3.486 -45.288 32.849 1.00 31.63 ? 551 ASN A O 1 ATOM 3971 C CB . ASN A 1 516 ? -1.210 -47.584 33.402 1.00 39.39 ? 551 ASN A CB 1 ATOM 3972 C CG . ASN A 1 516 ? 0.276 -47.871 33.330 1.00 42.63 ? 551 ASN A CG 1 ATOM 3973 O OD1 . ASN A 1 516 ? 0.749 -48.492 32.384 1.00 44.54 ? 551 ASN A OD1 1 ATOM 3974 N ND2 . ASN A 1 516 ? 1.023 -47.400 34.316 1.00 45.10 ? 551 ASN A ND2 1 ATOM 3975 N N . TYR A 1 517 ? -4.062 -47.310 32.070 1.00 33.25 ? 552 TYR A N 1 ATOM 3976 C CA . TYR A 1 517 ? -5.481 -47.098 32.255 1.00 32.91 ? 552 TYR A CA 1 ATOM 3977 C C . TYR A 1 517 ? -6.028 -48.289 33.029 1.00 33.66 ? 552 TYR A C 1 ATOM 3978 O O . TYR A 1 517 ? -6.656 -49.141 32.432 1.00 33.82 ? 552 TYR A O 1 ATOM 3979 C CB . TYR A 1 517 ? -6.167 -46.979 30.903 1.00 34.15 ? 552 TYR A CB 1 ATOM 3980 C CG . TYR A 1 517 ? -5.764 -45.786 30.083 1.00 34.60 ? 552 TYR A CG 1 ATOM 3981 C CD1 . TYR A 1 517 ? -4.596 -45.804 29.311 1.00 36.29 ? 552 TYR A CD1 1 ATOM 3982 C CD2 . TYR A 1 517 ? -6.559 -44.653 30.042 1.00 33.68 ? 552 TYR A CD2 1 ATOM 3983 C CE1 . TYR A 1 517 ? -4.228 -44.707 28.541 1.00 36.51 ? 552 TYR A CE1 1 ATOM 3984 C CE2 . TYR A 1 517 ? -6.202 -43.551 29.277 1.00 34.89 ? 552 TYR A CE2 1 ATOM 3985 C CZ . TYR A 1 517 ? -5.041 -43.585 28.526 1.00 36.38 ? 552 TYR A CZ 1 ATOM 3986 O OH . TYR A 1 517 ? -4.713 -42.481 27.772 1.00 37.92 ? 552 TYR A OH 1 ATOM 3987 N N . PRO A 1 518 ? -5.777 -48.360 34.360 1.00 33.60 ? 553 PRO A N 1 ATOM 3988 C CA . PRO A 1 518 ? -6.141 -49.560 35.121 1.00 35.36 ? 553 PRO A CA 1 ATOM 3989 C C . PRO A 1 518 ? -7.636 -49.699 35.379 1.00 36.87 ? 553 PRO A C 1 ATOM 3990 O O . PRO A 1 518 ? -8.302 -48.721 35.697 1.00 37.46 ? 553 PRO A O 1 ATOM 3991 C CB . PRO A 1 518 ? -5.395 -49.369 36.441 1.00 35.18 ? 553 PRO A CB 1 ATOM 3992 C CG . PRO A 1 518 ? -5.326 -47.897 36.617 1.00 33.29 ? 553 PRO A CG 1 ATOM 3993 C CD . PRO A 1 518 ? -5.132 -47.354 35.226 1.00 32.81 ? 553 PRO A CD 1 ATOM 3994 N N . GLY A 1 519 ? -8.149 -50.918 35.239 1.00 40.77 ? 554 GLY A N 1 ATOM 3995 C CA . GLY A 1 519 ? -9.550 -51.214 35.522 1.00 44.10 ? 554 GLY A CA 1 ATOM 3996 C C . GLY A 1 519 ? -9.752 -51.599 36.977 1.00 47.42 ? 554 GLY A C 1 ATOM 3997 O O . GLY A 1 519 ? -8.774 -51.738 37.739 1.00 46.07 ? 554 GLY A O 1 ATOM 3998 N N . ILE A 1 520 ? -11.026 -51.764 37.353 1.00 50.39 ? 555 ILE A N 1 ATOM 3999 C CA . ILE A 1 520 ? -11.419 -52.284 38.672 1.00 52.31 ? 555 ILE A CA 1 ATOM 4000 C C . ILE A 1 520 ? -10.994 -53.748 38.763 1.00 54.05 ? 555 ILE A C 1 ATOM 4001 O O . ILE A 1 520 ? -11.686 -54.617 38.252 1.00 55.12 ? 555 ILE A O 1 ATOM 4002 C CB . ILE A 1 520 ? -12.948 -52.144 38.917 1.00 53.77 ? 555 ILE A CB 1 ATOM 4003 C CG1 . ILE A 1 520 ? -13.314 -50.658 39.079 1.00 53.86 ? 555 ILE A CG1 1 ATOM 4004 C CG2 . ILE A 1 520 ? -13.397 -52.968 40.133 1.00 53.97 ? 555 ILE A CG2 1 ATOM 4005 C CD1 . ILE A 1 520 ? -14.797 -50.369 39.175 1.00 54.74 ? 555 ILE A CD1 1 ATOM 4006 N N . MET A 1 521 ? -9.851 -53.997 39.398 1.00 55.84 ? 556 MET A N 1 ATOM 4007 C CA . MET A 1 521 ? -9.260 -55.337 39.464 1.00 61.67 ? 556 MET A CA 1 ATOM 4008 C C . MET A 1 521 ? -9.067 -55.909 40.876 1.00 62.39 ? 556 MET A C 1 ATOM 4009 O O . MET A 1 521 ? -9.168 -57.133 41.049 1.00 62.67 ? 556 MET A O 1 ATOM 4010 C CB . MET A 1 521 ? -7.941 -55.381 38.679 1.00 65.99 ? 556 MET A CB 1 ATOM 4011 C CG . MET A 1 521 ? -6.857 -54.417 39.133 1.00 68.05 ? 556 MET A CG 1 ATOM 4012 S SD . MET A 1 521 ? -5.417 -54.503 38.040 1.00 81.88 ? 556 MET A SD 1 ATOM 4013 C CE . MET A 1 521 ? -5.049 -52.766 37.779 1.00 74.70 ? 556 MET A CE 1 ATOM 4014 N N . TYR A 1 522 ? -8.801 -55.059 41.875 1.00 60.65 ? 557 TYR A N 1 ATOM 4015 C CA . TYR A 1 522 ? -8.556 -55.529 43.254 1.00 61.62 ? 557 TYR A CA 1 ATOM 4016 C C . TYR A 1 522 ? -9.831 -55.594 44.101 1.00 61.05 ? 557 TYR A C 1 ATOM 4017 O O . TYR A 1 522 ? -10.833 -54.952 43.795 1.00 60.95 ? 557 TYR A O 1 ATOM 4018 C CB . TYR A 1 522 ? -7.524 -54.650 43.962 1.00 60.96 ? 557 TYR A CB 1 ATOM 4019 C CG . TYR A 1 522 ? -6.185 -54.528 43.251 1.00 62.16 ? 557 TYR A CG 1 ATOM 4020 C CD1 . TYR A 1 522 ? -5.223 -55.529 43.350 1.00 62.89 ? 557 TYR A CD1 1 ATOM 4021 C CD2 . TYR A 1 522 ? -5.867 -53.387 42.507 1.00 61.03 ? 557 TYR A CD2 1 ATOM 4022 C CE1 . TYR A 1 522 ? -3.993 -55.408 42.714 1.00 62.96 ? 557 TYR A CE1 1 ATOM 4023 C CE2 . TYR A 1 522 ? -4.645 -53.260 41.868 1.00 61.08 ? 557 TYR A CE2 1 ATOM 4024 C CZ . TYR A 1 522 ? -3.711 -54.270 41.974 1.00 62.76 ? 557 TYR A CZ 1 ATOM 4025 O OH . TYR A 1 522 ? -2.500 -54.128 41.334 1.00 64.00 ? 557 TYR A OH 1 ATOM 4026 N N . LEU A 1 523 ? -9.783 -56.400 45.159 1.00 61.56 ? 558 LEU A N 1 ATOM 4027 C CA . LEU A 1 523 ? -10.866 -56.481 46.149 1.00 60.84 ? 558 LEU A CA 1 ATOM 4028 C C . LEU A 1 523 ? -10.460 -55.665 47.374 1.00 57.94 ? 558 LEU A C 1 ATOM 4029 O O . LEU A 1 523 ? -9.269 -55.550 47.673 1.00 53.87 ? 558 LEU A O 1 ATOM 4030 C CB . LEU A 1 523 ? -11.128 -57.940 46.563 1.00 63.26 ? 558 LEU A CB 1 ATOM 4031 C CG . LEU A 1 523 ? -11.499 -58.996 45.507 1.00 65.09 ? 558 LEU A CG 1 ATOM 4032 C CD1 . LEU A 1 523 ? -11.577 -60.380 46.148 1.00 65.91 ? 558 LEU A CD1 1 ATOM 4033 C CD2 . LEU A 1 523 ? -12.805 -58.676 44.790 1.00 65.16 ? 558 LEU A CD2 1 ATOM 4034 N N . GLN A 1 524 ? -11.453 -55.117 48.076 1.00 59.85 ? 559 GLN A N 1 ATOM 4035 C CA . GLN A 1 524 ? -11.257 -54.429 49.368 1.00 60.48 ? 559 GLN A CA 1 ATOM 4036 C C . GLN A 1 524 ? -10.296 -55.150 50.325 1.00 59.53 ? 559 GLN A C 1 ATOM 4037 O O . GLN A 1 524 ? -9.413 -54.522 50.909 1.00 57.62 ? 559 GLN A O 1 ATOM 4038 C CB . GLN A 1 524 ? -12.608 -54.231 50.081 1.00 63.63 ? 559 GLN A CB 1 ATOM 4039 C CG . GLN A 1 524 ? -13.466 -53.101 49.531 1.00 65.65 ? 559 GLN A CG 1 ATOM 4040 C CD . GLN A 1 524 ? -12.911 -51.721 49.847 1.00 67.16 ? 559 GLN A CD 1 ATOM 4041 O OE1 . GLN A 1 524 ? -12.583 -50.956 48.941 1.00 70.84 ? 559 GLN A OE1 1 ATOM 4042 N NE2 . GLN A 1 524 ? -12.801 -51.397 51.136 1.00 69.07 ? 559 GLN A NE2 1 ATOM 4043 N N . SER A 1 525 ? -10.466 -56.466 50.457 1.00 59.27 ? 560 SER A N 1 ATOM 4044 C CA . SER A 1 525 ? -9.675 -57.295 51.383 1.00 59.40 ? 560 SER A CA 1 ATOM 4045 C C . SER A 1 525 ? -8.142 -57.221 51.227 1.00 58.60 ? 560 SER A C 1 ATOM 4046 O O . SER A 1 525 ? -7.413 -57.479 52.182 1.00 58.60 ? 560 SER A O 1 ATOM 4047 C CB . SER A 1 525 ? -10.144 -58.761 51.301 1.00 61.22 ? 560 SER A CB 1 ATOM 4048 O OG . SER A 1 525 ? -10.476 -59.124 49.969 1.00 60.96 ? 560 SER A OG 1 ATOM 4049 N N . GLU A 1 526 ? -7.657 -56.848 50.047 1.00 58.98 ? 561 GLU A N 1 ATOM 4050 C CA . GLU A 1 526 ? -6.209 -56.738 49.799 1.00 61.58 ? 561 GLU A CA 1 ATOM 4051 C C . GLU A 1 526 ? -5.527 -55.493 50.427 1.00 58.85 ? 561 GLU A C 1 ATOM 4052 O O . GLU A 1 526 ? -4.296 -55.434 50.495 1.00 59.34 ? 561 GLU A O 1 ATOM 4053 C CB . GLU A 1 526 ? -5.933 -56.770 48.285 1.00 64.01 ? 561 GLU A CB 1 ATOM 4054 C CG . GLU A 1 526 ? -6.465 -58.015 47.570 1.00 68.43 ? 561 GLU A CG 1 ATOM 4055 C CD . GLU A 1 526 ? -6.168 -58.007 46.080 1.00 70.12 ? 561 GLU A CD 1 ATOM 4056 O OE1 . GLU A 1 526 ? -4.971 -57.968 45.716 1.00 71.45 ? 561 GLU A OE1 1 ATOM 4057 O OE2 . GLU A 1 526 ? -7.127 -58.043 45.279 1.00 68.35 ? 561 GLU A OE2 1 ATOM 4058 N N . PHE A 1 527 ? -6.307 -54.515 50.888 1.00 56.02 ? 562 PHE A N 1 ATOM 4059 C CA . PHE A 1 527 ? -5.752 -53.232 51.374 1.00 54.43 ? 562 PHE A CA 1 ATOM 4060 C C . PHE A 1 527 ? -5.614 -53.184 52.906 1.00 55.67 ? 562 PHE A C 1 ATOM 4061 O O . PHE A 1 527 ? -6.546 -53.538 53.621 1.00 54.13 ? 562 PHE A O 1 ATOM 4062 C CB . PHE A 1 527 ? -6.625 -52.076 50.896 1.00 51.38 ? 562 PHE A CB 1 ATOM 4063 C CG . PHE A 1 527 ? -6.630 -51.894 49.400 1.00 49.63 ? 562 PHE A CG 1 ATOM 4064 C CD1 . PHE A 1 527 ? -7.533 -52.592 48.602 1.00 48.67 ? 562 PHE A CD1 1 ATOM 4065 C CD2 . PHE A 1 527 ? -5.752 -50.999 48.790 1.00 46.82 ? 562 PHE A CD2 1 ATOM 4066 C CE1 . PHE A 1 527 ? -7.549 -52.418 47.224 1.00 48.30 ? 562 PHE A CE1 1 ATOM 4067 C CE2 . PHE A 1 527 ? -5.763 -50.825 47.412 1.00 45.79 ? 562 PHE A CE2 1 ATOM 4068 C CZ . PHE A 1 527 ? -6.662 -51.536 46.626 1.00 46.63 ? 562 PHE A CZ 1 ATOM 4069 N N . ASP A 1 528 ? -4.446 -52.741 53.384 1.00 57.28 ? 563 ASP A N 1 ATOM 4070 C CA . ASP A 1 528 ? -4.136 -52.608 54.819 1.00 58.53 ? 563 ASP A CA 1 ATOM 4071 C C . ASP A 1 528 ? -3.557 -51.200 55.055 1.00 56.64 ? 563 ASP A C 1 ATOM 4072 O O . ASP A 1 528 ? -2.440 -51.040 55.553 1.00 56.85 ? 563 ASP A O 1 ATOM 4073 C CB . ASP A 1 528 ? -3.150 -53.712 55.246 1.00 61.42 ? 563 ASP A CB 1 ATOM 4074 C CG . ASP A 1 528 ? -3.140 -53.964 56.760 1.00 63.51 ? 563 ASP A CG 1 ATOM 4075 O OD1 . ASP A 1 528 ? -3.226 -53.001 57.552 1.00 63.56 ? 563 ASP A OD1 1 ATOM 4076 O OD2 . ASP A 1 528 ? -3.036 -55.144 57.161 1.00 66.44 ? 563 ASP A OD2 1 ATOM 4077 N N . LEU A 1 529 ? -4.338 -50.188 54.678 1.00 54.87 ? 564 LEU A N 1 ATOM 4078 C CA . LEU A 1 529 ? -3.904 -48.775 54.705 1.00 52.82 ? 564 LEU A CA 1 ATOM 4079 C C . LEU A 1 529 ? -4.183 -48.044 56.023 1.00 51.11 ? 564 LEU A C 1 ATOM 4080 O O . LEU A 1 529 ? -3.796 -46.886 56.175 1.00 49.99 ? 564 LEU A O 1 ATOM 4081 C CB . LEU A 1 529 ? -4.565 -47.997 53.557 1.00 51.34 ? 564 LEU A CB 1 ATOM 4082 C CG . LEU A 1 529 ? -4.538 -48.617 52.154 1.00 52.21 ? 564 LEU A CG 1 ATOM 4083 C CD1 . LEU A 1 529 ? -5.263 -47.721 51.158 1.00 49.13 ? 564 LEU A CD1 1 ATOM 4084 C CD2 . LEU A 1 529 ? -3.111 -48.897 51.687 1.00 53.32 ? 564 LEU A CD2 1 ATOM 4085 N N . GLY A 1 530 ? -4.853 -48.704 56.970 1.00 50.80 ? 565 GLY A N 1 ATOM 4086 C CA . GLY A 1 530 ? -5.276 -48.059 58.213 1.00 50.98 ? 565 GLY A CA 1 ATOM 4087 C C . GLY A 1 530 ? -6.352 -46.990 58.053 1.00 50.47 ? 565 GLY A C 1 ATOM 4088 O O . GLY A 1 530 ? -6.553 -46.183 58.965 1.00 49.27 ? 565 GLY A O 1 ATOM 4089 N N . CYS A 1 531 ? -7.049 -46.994 56.910 1.00 51.39 ? 566 CYS A N 1 ATOM 4090 C CA . CYS A 1 531 ? -8.097 -46.015 56.603 1.00 54.18 ? 566 CYS A CA 1 ATOM 4091 C C . CYS A 1 531 ? -9.468 -46.517 57.033 1.00 55.82 ? 566 CYS A C 1 ATOM 4092 O O . CYS A 1 531 ? -9.710 -47.726 57.112 1.00 58.20 ? 566 CYS A O 1 ATOM 4093 C CB . CYS A 1 531 ? -8.135 -45.708 55.106 1.00 55.05 ? 566 CYS A CB 1 ATOM 4094 S SG . CYS A 1 531 ? -6.581 -45.096 54.420 1.00 55.87 ? 566 CYS A SG 1 ATOM 4095 N N . THR A 1 532 ? -10.364 -45.572 57.288 1.00 57.14 ? 567 THR A N 1 ATOM 4096 C CA . THR A 1 532 ? -11.695 -45.857 57.825 1.00 61.58 ? 567 THR A CA 1 ATOM 4097 C C . THR A 1 532 ? -12.712 -44.908 57.200 1.00 62.62 ? 567 THR A C 1 ATOM 4098 O O . THR A 1 532 ? -12.386 -43.752 56.921 1.00 61.96 ? 567 THR A O 1 ATOM 4099 C CB . THR A 1 532 ? -11.708 -45.741 59.372 1.00 62.75 ? 567 THR A CB 1 ATOM 4100 O OG1 . THR A 1 532 ? -13.047 -45.873 59.859 1.00 67.78 ? 567 THR A OG1 1 ATOM 4101 C CG2 . THR A 1 532 ? -11.121 -44.414 59.862 1.00 61.68 ? 567 THR A CG2 1 ATOM 4102 N N . CYS A 1 533 ? -13.926 -45.402 56.963 1.00 61.35 ? 568 CYS A N 1 ATOM 4103 C CA . CYS A 1 533 ? -15.006 -44.585 56.411 1.00 62.50 ? 568 CYS A CA 1 ATOM 4104 C C . CYS A 1 533 ? -16.210 -44.603 57.341 1.00 66.17 ? 568 CYS A C 1 ATOM 4105 O O . CYS A 1 533 ? -16.434 -45.572 58.072 1.00 67.54 ? 568 CYS A O 1 ATOM 4106 C CB . CYS A 1 533 ? -15.384 -45.067 55.007 1.00 63.84 ? 568 CYS A CB 1 ATOM 4107 S SG . CYS A 1 533 ? -16.433 -43.922 54.062 1.00 65.14 ? 568 CYS A SG 1 ATOM 4108 N N . LYS A 1 536 ? -17.968 -48.485 62.181 1.00 97.58 ? 571 LYS A N 1 ATOM 4109 C CA . LYS A 1 536 ? -18.950 -48.286 63.251 1.00 96.32 ? 571 LYS A CA 1 ATOM 4110 C C . LYS A 1 536 ? -20.358 -48.163 62.672 1.00 94.46 ? 571 LYS A C 1 ATOM 4111 O O . LYS A 1 536 ? -21.317 -48.699 63.229 1.00 88.82 ? 571 LYS A O 1 ATOM 4112 C CB . LYS A 1 536 ? -18.600 -47.047 64.089 1.00 94.79 ? 571 LYS A CB 1 ATOM 4113 C CG . LYS A 1 536 ? -17.123 -46.923 64.452 1.00 94.78 ? 571 LYS A CG 1 ATOM 4114 C CD . LYS A 1 536 ? -16.614 -48.105 65.278 1.00 97.02 ? 571 LYS A CD 1 ATOM 4115 C CE . LYS A 1 536 ? -15.394 -48.769 64.650 1.00 97.50 ? 571 LYS A CE 1 ATOM 4116 N NZ . LYS A 1 536 ? -14.199 -47.881 64.619 1.00 97.89 ? 571 LYS A NZ 1 ATOM 4117 N N . VAL A 1 537 ? -20.460 -47.417 61.573 1.00 93.32 ? 572 VAL A N 1 ATOM 4118 C CA . VAL A 1 537 ? -21.655 -47.400 60.713 1.00 92.94 ? 572 VAL A CA 1 ATOM 4119 C C . VAL A 1 537 ? -21.408 -48.110 59.365 1.00 91.89 ? 572 VAL A C 1 ATOM 4120 O O . VAL A 1 537 ? -22.343 -48.675 58.787 1.00 96.06 ? 572 VAL A O 1 ATOM 4121 C CB . VAL A 1 537 ? -22.205 -45.959 60.493 1.00 90.61 ? 572 VAL A CB 1 ATOM 4122 C CG1 . VAL A 1 537 ? -22.650 -45.347 61.815 1.00 90.92 ? 572 VAL A CG1 1 ATOM 4123 C CG2 . VAL A 1 537 ? -21.194 -45.050 59.804 1.00 87.03 ? 572 VAL A CG2 1 ATOM 4124 N N . GLU A 1 538 ? -20.157 -48.088 58.887 1.00 87.59 ? 573 GLU A N 1 ATOM 4125 C CA . GLU A 1 538 ? -19.765 -48.627 57.578 1.00 84.59 ? 573 GLU A CA 1 ATOM 4126 C C . GLU A 1 538 ? -20.522 -47.942 56.422 1.00 80.20 ? 573 GLU A C 1 ATOM 4127 O O . GLU A 1 538 ? -21.348 -48.579 55.749 1.00 76.83 ? 573 GLU A O 1 ATOM 4128 C CB . GLU A 1 538 ? -19.904 -50.159 57.537 1.00 87.56 ? 573 GLU A CB 1 ATOM 4129 C CG . GLU A 1 538 ? -19.055 -50.865 58.587 1.00 89.11 ? 573 GLU A CG 1 ATOM 4130 C CD . GLU A 1 538 ? -19.128 -52.380 58.500 1.00 91.94 ? 573 GLU A CD 1 ATOM 4131 O OE1 . GLU A 1 538 ? -18.933 -52.931 57.395 1.00 91.98 ? 573 GLU A OE1 1 ATOM 4132 O OE2 . GLU A 1 538 ? -19.365 -53.023 59.546 1.00 93.65 ? 573 GLU A OE2 1 ATOM 4133 N N . PRO A 1 539 ? -20.241 -46.636 56.192 1.00 71.82 ? 574 PRO A N 1 ATOM 4134 C CA . PRO A 1 539 ? -20.894 -45.913 55.103 1.00 68.24 ? 574 PRO A CA 1 ATOM 4135 C C . PRO A 1 539 ? -20.407 -46.404 53.741 1.00 64.92 ? 574 PRO A C 1 ATOM 4136 O O . PRO A 1 539 ? -19.199 -46.509 53.523 1.00 58.84 ? 574 PRO A O 1 ATOM 4137 C CB . PRO A 1 539 ? -20.474 -44.448 55.329 1.00 67.48 ? 574 PRO A CB 1 ATOM 4138 C CG . PRO A 1 539 ? -19.680 -44.419 56.590 1.00 67.34 ? 574 PRO A CG 1 ATOM 4139 C CD . PRO A 1 539 ? -19.187 -45.814 56.805 1.00 70.12 ? 574 PRO A CD 1 ATOM 4140 N N . LYS A 1 540 ? -21.350 -46.717 52.853 1.00 62.37 ? 575 LYS A N 1 ATOM 4141 C CA . LYS A 1 540 ? -21.025 -47.229 51.526 1.00 62.25 ? 575 LYS A CA 1 ATOM 4142 C C . LYS A 1 540 ? -22.177 -47.062 50.532 1.00 62.24 ? 575 LYS A C 1 ATOM 4143 O O . LYS A 1 540 ? -23.354 -47.157 50.890 1.00 61.12 ? 575 LYS A O 1 ATOM 4144 C CB . LYS A 1 540 ? -20.603 -48.701 51.612 1.00 63.85 ? 575 LYS A CB 1 ATOM 4145 C CG . LYS A 1 540 ? -21.620 -49.639 52.268 1.00 63.99 ? 575 LYS A CG 1 ATOM 4146 C CD . LYS A 1 540 ? -22.469 -50.386 51.246 1.00 64.66 ? 575 LYS A CD 1 ATOM 4147 C CE . LYS A 1 540 ? -23.179 -51.586 51.863 1.00 66.87 ? 575 LYS A CE 1 ATOM 4148 N NZ . LYS A 1 540 ? -24.358 -51.187 52.675 1.00 66.87 ? 575 LYS A NZ 1 ATOM 4149 N N . ASN A 1 541 ? -21.815 -46.796 49.281 1.00 61.80 ? 576 ASN A N 1 ATOM 4150 C CA . ASN A 1 541 ? -22.761 -46.790 48.188 1.00 60.23 ? 576 ASN A CA 1 ATOM 4151 C C . ASN A 1 541 ? -22.906 -48.234 47.725 1.00 60.95 ? 576 ASN A C 1 ATOM 4152 O O . ASN A 1 541 ? -22.136 -48.713 46.886 1.00 57.39 ? 576 ASN A O 1 ATOM 4153 C CB . ASN A 1 541 ? -22.276 -45.868 47.056 1.00 61.67 ? 576 ASN A CB 1 ATOM 4154 C CG . ASN A 1 541 ? -23.267 -45.775 45.901 1.00 62.79 ? 576 ASN A CG 1 ATOM 4155 O OD1 . ASN A 1 541 ? -24.372 -46.312 45.960 1.00 62.68 ? 576 ASN A OD1 1 ATOM 4156 N ND2 . ASN A 1 541 ? -22.872 -45.083 44.845 1.00 63.58 ? 576 ASN A ND2 1 ATOM 4157 N N . LYS A 1 542 ? -23.891 -48.917 48.313 1.00 61.16 ? 577 LYS A N 1 ATOM 4158 C CA . LYS A 1 542 ? -24.278 -50.291 47.950 1.00 62.21 ? 577 LYS A CA 1 ATOM 4159 C C . LYS A 1 542 ? -24.464 -50.511 46.422 1.00 59.51 ? 577 LYS A C 1 ATOM 4160 O O . LYS A 1 542 ? -24.168 -51.590 45.892 1.00 55.25 ? 577 LYS A O 1 ATOM 4161 C CB . LYS A 1 542 ? -25.564 -50.636 48.724 1.00 66.32 ? 577 LYS A CB 1 ATOM 4162 C CG . LYS A 1 542 ? -26.217 -51.968 48.413 1.00 69.40 ? 577 LYS A CG 1 ATOM 4163 C CD . LYS A 1 542 ? -25.294 -53.150 48.623 1.00 71.15 ? 577 LYS A CD 1 ATOM 4164 C CE . LYS A 1 542 ? -26.075 -54.435 48.426 1.00 73.08 ? 577 LYS A CE 1 ATOM 4165 N NZ . LYS A 1 542 ? -25.192 -55.619 48.259 1.00 75.35 ? 577 LYS A NZ 1 ATOM 4166 N N . LEU A 1 543 ? -24.944 -49.469 45.740 1.00 57.02 ? 578 LEU A N 1 ATOM 4167 C CA . LEU A 1 543 ? -25.138 -49.461 44.290 1.00 55.92 ? 578 LEU A CA 1 ATOM 4168 C C . LEU A 1 543 ? -23.866 -49.731 43.458 1.00 53.00 ? 578 LEU A C 1 ATOM 4169 O O . LEU A 1 543 ? -23.976 -50.261 42.349 1.00 49.86 ? 578 LEU A O 1 ATOM 4170 C CB . LEU A 1 543 ? -25.743 -48.118 43.860 1.00 58.01 ? 578 LEU A CB 1 ATOM 4171 C CG . LEU A 1 543 ? -26.412 -47.990 42.497 1.00 60.03 ? 578 LEU A CG 1 ATOM 4172 C CD1 . LEU A 1 543 ? -27.587 -48.949 42.347 1.00 60.78 ? 578 LEU A CD1 1 ATOM 4173 C CD2 . LEU A 1 543 ? -26.850 -46.543 42.313 1.00 60.08 ? 578 LEU A CD2 1 ATOM 4174 N N . GLU A 1 544 ? -22.683 -49.376 43.979 1.00 49.34 ? 579 GLU A N 1 ATOM 4175 C CA . GLU A 1 544 ? -21.399 -49.605 43.269 1.00 49.48 ? 579 GLU A CA 1 ATOM 4176 C C . GLU A 1 544 ? -21.166 -51.075 42.901 1.00 48.25 ? 579 GLU A C 1 ATOM 4177 O O . GLU A 1 544 ? -20.600 -51.368 41.846 1.00 46.62 ? 579 GLU A O 1 ATOM 4178 C CB . GLU A 1 544 ? -20.196 -49.104 44.086 1.00 49.16 ? 579 GLU A CB 1 ATOM 4179 C CG . GLU A 1 544 ? -20.113 -47.591 44.182 1.00 52.24 ? 579 GLU A CG 1 ATOM 4180 C CD . GLU A 1 544 ? -18.844 -47.075 44.865 1.00 52.91 ? 579 GLU A CD 1 ATOM 4181 O OE1 . GLU A 1 544 ? -17.824 -47.802 44.925 1.00 54.50 ? 579 GLU A OE1 1 ATOM 4182 O OE2 . GLU A 1 544 ? -18.872 -45.918 45.338 1.00 51.92 ? 579 GLU A OE2 1 ATOM 4183 N N . GLU A 1 545 ? -21.621 -51.983 43.764 1.00 48.97 ? 580 GLU A N 1 ATOM 4184 C CA . GLU A 1 545 ? -21.506 -53.423 43.529 1.00 49.70 ? 580 GLU A CA 1 ATOM 4185 C C . GLU A 1 545 ? -22.299 -53.885 42.297 1.00 47.75 ? 580 GLU A C 1 ATOM 4186 O O . GLU A 1 545 ? -21.975 -54.914 41.710 1.00 50.76 ? 580 GLU A O 1 ATOM 4187 C CB . GLU A 1 545 ? -21.977 -54.198 44.770 1.00 53.88 ? 580 GLU A CB 1 ATOM 4188 C CG . GLU A 1 545 ? -21.135 -53.950 46.023 1.00 55.59 ? 580 GLU A CG 1 ATOM 4189 C CD . GLU A 1 545 ? -21.903 -54.176 47.319 1.00 60.33 ? 580 GLU A CD 1 ATOM 4190 O OE1 . GLU A 1 545 ? -22.682 -55.153 47.399 1.00 59.69 ? 580 GLU A OE1 1 ATOM 4191 O OE2 . GLU A 1 545 ? -21.721 -53.371 48.267 1.00 63.61 ? 580 GLU A OE2 1 ATOM 4192 N N . PHE A 1 546 ? -23.349 -53.141 41.938 1.00 43.85 ? 581 PHE A N 1 ATOM 4193 C CA . PHE A 1 546 ? -24.178 -53.425 40.754 1.00 42.01 ? 581 PHE A CA 1 ATOM 4194 C C . PHE A 1 546 ? -23.717 -52.662 39.504 1.00 41.12 ? 581 PHE A C 1 ATOM 4195 O O . PHE A 1 546 ? -24.197 -52.938 38.410 1.00 41.23 ? 581 PHE A O 1 ATOM 4196 C CB . PHE A 1 546 ? -25.633 -53.036 41.021 1.00 41.46 ? 581 PHE A CB 1 ATOM 4197 C CG . PHE A 1 546 ? -26.269 -53.785 42.169 1.00 42.31 ? 581 PHE A CG 1 ATOM 4198 C CD1 . PHE A 1 546 ? -26.279 -55.172 42.183 1.00 43.06 ? 581 PHE A CD1 1 ATOM 4199 C CD2 . PHE A 1 546 ? -26.862 -53.100 43.227 1.00 41.62 ? 581 PHE A CD2 1 ATOM 4200 C CE1 . PHE A 1 546 ? -26.857 -55.869 43.229 1.00 44.41 ? 581 PHE A CE1 1 ATOM 4201 C CE2 . PHE A 1 546 ? -27.450 -53.792 44.277 1.00 42.61 ? 581 PHE A CE2 1 ATOM 4202 C CZ . PHE A 1 546 ? -27.449 -55.179 44.275 1.00 44.76 ? 581 PHE A CZ 1 ATOM 4203 N N . ASN A 1 547 ? -22.796 -51.723 39.659 1.00 39.19 ? 582 ASN A N 1 ATOM 4204 C CA . ASN A 1 547 ? -22.411 -50.838 38.553 1.00 39.21 ? 582 ASN A CA 1 ATOM 4205 C C . ASN A 1 547 ? -21.174 -51.358 37.834 1.00 39.27 ? 582 ASN A C 1 ATOM 4206 O O . ASN A 1 547 ? -20.044 -51.044 38.204 1.00 39.36 ? 582 ASN A O 1 ATOM 4207 C CB . ASN A 1 547 ? -22.197 -49.425 39.061 1.00 39.22 ? 582 ASN A CB 1 ATOM 4208 C CG . ASN A 1 547 ? -21.927 -48.417 37.940 1.00 39.40 ? 582 ASN A CG 1 ATOM 4209 O OD1 . ASN A 1 547 ? -21.999 -48.735 36.747 1.00 42.59 ? 582 ASN A OD1 1 ATOM 4210 N ND2 . ASN A 1 547 ? -21.630 -47.202 38.326 1.00 40.36 ? 582 ASN A ND2 1 ATOM 4211 N N . LYS A 1 548 ? -21.410 -52.139 36.787 1.00 40.54 ? 583 LYS A N 1 ATOM 4212 C CA . LYS A 1 548 ? -20.327 -52.742 36.011 1.00 41.53 ? 583 LYS A CA 1 ATOM 4213 C C . LYS A 1 548 ? -19.445 -51.725 35.318 1.00 40.19 ? 583 LYS A C 1 ATOM 4214 O O . LYS A 1 548 ? -18.253 -51.972 35.187 1.00 39.99 ? 583 LYS A O 1 ATOM 4215 C CB . LYS A 1 548 ? -20.886 -53.724 34.985 1.00 43.69 ? 583 LYS A CB 1 ATOM 4216 C CG . LYS A 1 548 ? -21.552 -54.921 35.637 1.00 46.09 ? 583 LYS A CG 1 ATOM 4217 C CD . LYS A 1 548 ? -21.666 -56.095 34.690 1.00 48.57 ? 583 LYS A CD 1 ATOM 4218 C CE . LYS A 1 548 ? -22.343 -57.276 35.365 1.00 51.02 ? 583 LYS A CE 1 ATOM 4219 N NZ . LYS A 1 548 ? -23.744 -57.458 34.916 1.00 52.97 ? 583 LYS A NZ 1 ATOM 4220 N N . ARG A 1 549 ? -20.018 -50.586 34.913 1.00 40.13 ? 584 ARG A N 1 ATOM 4221 C CA . ARG A 1 549 ? -19.287 -49.545 34.172 1.00 41.07 ? 584 ARG A CA 1 ATOM 4222 C C . ARG A 1 549 ? -18.663 -48.501 35.096 1.00 39.06 ? 584 ARG A C 1 ATOM 4223 O O . ARG A 1 549 ? -18.199 -47.464 34.624 1.00 38.72 ? 584 ARG A O 1 ATOM 4224 C CB . ARG A 1 549 ? -20.207 -48.830 33.165 1.00 43.36 ? 584 ARG A CB 1 ATOM 4225 C CG . ARG A 1 549 ? -20.968 -49.712 32.166 1.00 46.39 ? 584 ARG A CG 1 ATOM 4226 C CD . ARG A 1 549 ? -20.324 -49.867 30.784 1.00 50.43 ? 584 ARG A CD 1 ATOM 4227 N NE . ARG A 1 549 ? -19.829 -48.618 30.178 1.00 54.06 ? 584 ARG A NE 1 ATOM 4228 C CZ . ARG A 1 549 ? -19.338 -48.509 28.935 1.00 56.29 ? 584 ARG A CZ 1 ATOM 4229 N NH1 . ARG A 1 549 ? -19.298 -49.556 28.115 1.00 57.10 ? 584 ARG A NH1 1 ATOM 4230 N NH2 . ARG A 1 549 ? -18.897 -47.329 28.497 1.00 57.41 ? 584 ARG A NH2 1 ATOM 4231 N N . LEU A 1 550 ? -18.655 -48.751 36.407 1.00 38.54 ? 585 LEU A N 1 ATOM 4232 C CA . LEU A 1 550 ? -18.051 -47.822 37.358 1.00 38.70 ? 585 LEU A CA 1 ATOM 4233 C C . LEU A 1 550 ? -16.602 -47.546 36.973 1.00 37.15 ? 585 LEU A C 1 ATOM 4234 O O . LEU A 1 550 ? -15.853 -48.473 36.673 1.00 36.69 ? 585 LEU A O 1 ATOM 4235 C CB . LEU A 1 550 ? -18.109 -48.386 38.783 1.00 39.60 ? 585 LEU A CB 1 ATOM 4236 C CG . LEU A 1 550 ? -17.512 -47.554 39.921 1.00 39.87 ? 585 LEU A CG 1 ATOM 4237 C CD1 . LEU A 1 550 ? -18.254 -46.230 40.094 1.00 41.06 ? 585 LEU A CD1 1 ATOM 4238 C CD2 . LEU A 1 550 ? -17.534 -48.354 41.221 1.00 41.40 ? 585 LEU A CD2 1 ATOM 4239 N N . HIS A 1 551 ? -16.241 -46.270 36.952 1.00 36.13 ? 586 HIS A N 1 ATOM 4240 C CA . HIS A 1 551 ? -14.875 -45.815 36.633 1.00 36.06 ? 586 HIS A CA 1 ATOM 4241 C C . HIS A 1 551 ? -14.385 -46.106 35.209 1.00 36.55 ? 586 HIS A C 1 ATOM 4242 O O . HIS A 1 551 ? -13.191 -46.105 34.964 1.00 36.76 ? 586 HIS A O 1 ATOM 4243 C CB . HIS A 1 551 ? -13.871 -46.348 37.673 1.00 37.02 ? 586 HIS A CB 1 ATOM 4244 C CG . HIS A 1 551 ? -14.195 -45.946 39.079 1.00 37.32 ? 586 HIS A CG 1 ATOM 4245 N ND1 . HIS A 1 551 ? -13.937 -46.756 40.166 1.00 39.98 ? 586 HIS A ND1 1 ATOM 4246 C CD2 . HIS A 1 551 ? -14.797 -44.838 39.570 1.00 36.26 ? 586 HIS A CD2 1 ATOM 4247 C CE1 . HIS A 1 551 ? -14.330 -46.147 41.270 1.00 37.84 ? 586 HIS A CE1 1 ATOM 4248 N NE2 . HIS A 1 551 ? -14.871 -44.990 40.935 1.00 37.51 ? 586 HIS A NE2 1 ATOM 4249 N N . THR A 1 552 ? -15.296 -46.359 34.271 1.00 37.51 ? 587 THR A N 1 ATOM 4250 C CA . THR A 1 552 ? -14.920 -46.424 32.855 1.00 37.06 ? 587 THR A CA 1 ATOM 4251 C C . THR A 1 552 ? -14.903 -45.009 32.308 1.00 36.37 ? 587 THR A C 1 ATOM 4252 O O . THR A 1 552 ? -15.565 -44.137 32.851 1.00 35.86 ? 587 THR A O 1 ATOM 4253 C CB . THR A 1 552 ? -15.908 -47.264 32.026 1.00 37.47 ? 587 THR A CB 1 ATOM 4254 O OG1 . THR A 1 552 ? -17.236 -46.736 32.147 1.00 36.66 ? 587 THR A OG1 1 ATOM 4255 C CG2 . THR A 1 552 ? -15.904 -48.704 32.498 1.00 38.96 ? 587 THR A CG2 1 ATOM 4256 N N . LYS A 1 553 ? -14.168 -44.799 31.221 1.00 38.65 ? 588 LYS A N 1 ATOM 4257 C CA . LYS A 1 553 ? -14.130 -43.502 30.544 1.00 40.40 ? 588 LYS A CA 1 ATOM 4258 C C . LYS A 1 553 ? -15.505 -42.876 30.381 1.00 40.23 ? 588 LYS A C 1 ATOM 4259 O O . LYS A 1 553 ? -15.749 -41.806 30.908 1.00 41.25 ? 588 LYS A O 1 ATOM 4260 C CB . LYS A 1 553 ? -13.471 -43.600 29.166 1.00 43.32 ? 588 LYS A CB 1 ATOM 4261 C CG . LYS A 1 553 ? -13.288 -42.225 28.520 1.00 47.19 ? 588 LYS A CG 1 ATOM 4262 C CD . LYS A 1 553 ? -12.894 -42.300 27.053 1.00 51.22 ? 588 LYS A CD 1 ATOM 4263 C CE . LYS A 1 553 ? -11.444 -42.695 26.868 1.00 52.17 ? 588 LYS A CE 1 ATOM 4264 N NZ . LYS A 1 553 ? -10.891 -42.120 25.615 1.00 54.35 ? 588 LYS A NZ 1 ATOM 4265 N N . GLY A 1 554 ? -16.392 -43.535 29.636 1.00 43.50 ? 589 GLY A N 1 ATOM 4266 C CA . GLY A 1 554 ? -17.698 -42.964 29.314 1.00 43.33 ? 589 GLY A CA 1 ATOM 4267 C C . GLY A 1 554 ? -17.534 -41.568 28.730 1.00 42.10 ? 589 GLY A C 1 ATOM 4268 O O . GLY A 1 554 ? -16.711 -41.363 27.840 1.00 41.46 ? 589 GLY A O 1 ATOM 4269 N N . SER A 1 555 ? -18.303 -40.620 29.261 1.00 43.65 ? 590 SER A N 1 ATOM 4270 C CA . SER A 1 555 ? -18.210 -39.204 28.903 1.00 43.76 ? 590 SER A CA 1 ATOM 4271 C C . SER A 1 555 ? -17.356 -38.375 29.891 1.00 43.11 ? 590 SER A C 1 ATOM 4272 O O . SER A 1 555 ? -17.437 -37.147 29.866 1.00 45.76 ? 590 SER A O 1 ATOM 4273 C CB . SER A 1 555 ? -19.620 -38.603 28.849 1.00 43.78 ? 590 SER A CB 1 ATOM 4274 O OG . SER A 1 555 ? -20.129 -38.369 30.158 1.00 44.72 ? 590 SER A OG 1 ATOM 4275 N N . THR A 1 556 ? -16.563 -39.029 30.746 1.00 41.20 ? 591 THR A N 1 ATOM 4276 C CA . THR A 1 556 ? -15.723 -38.340 31.731 1.00 38.37 ? 591 THR A CA 1 ATOM 4277 C C . THR A 1 556 ? -14.718 -37.429 31.042 1.00 37.68 ? 591 THR A C 1 ATOM 4278 O O . THR A 1 556 ? -14.580 -36.263 31.421 1.00 34.13 ? 591 THR A O 1 ATOM 4279 C CB . THR A 1 556 ? -14.944 -39.334 32.627 1.00 38.01 ? 591 THR A CB 1 ATOM 4280 O OG1 . THR A 1 556 ? -15.865 -40.067 33.439 1.00 40.03 ? 591 THR A OG1 1 ATOM 4281 C CG2 . THR A 1 556 ? -13.965 -38.618 33.561 1.00 35.74 ? 591 THR A CG2 1 ATOM 4282 N N . LYS A 1 557 ? -13.997 -37.974 30.065 1.00 38.11 ? 592 LYS A N 1 ATOM 4283 C CA . LYS A 1 557 ? -12.972 -37.208 29.340 1.00 40.27 ? 592 LYS A CA 1 ATOM 4284 C C . LYS A 1 557 ? -13.613 -36.046 28.575 1.00 41.08 ? 592 LYS A C 1 ATOM 4285 O O . LYS A 1 557 ? -13.118 -34.914 28.627 1.00 40.24 ? 592 LYS A O 1 ATOM 4286 C CB . LYS A 1 557 ? -12.185 -38.125 28.399 1.00 42.75 ? 592 LYS A CB 1 ATOM 4287 C CG . LYS A 1 557 ? -11.098 -37.442 27.571 1.00 43.54 ? 592 LYS A CG 1 ATOM 4288 C CD . LYS A 1 557 ? -10.295 -38.422 26.714 1.00 43.01 ? 592 LYS A CD 1 ATOM 4289 C CE . LYS A 1 557 ? -9.563 -39.488 27.538 1.00 44.20 ? 592 LYS A CE 1 ATOM 4290 N NZ . LYS A 1 557 ? -8.761 -38.979 28.700 1.00 39.24 ? 592 LYS A NZ 1 ATOM 4291 N N . GLU A 1 558 ? -14.717 -36.335 27.889 1.00 40.16 ? 593 GLU A N 1 ATOM 4292 C CA . GLU A 1 558 ? -15.523 -35.319 27.208 1.00 42.51 ? 593 GLU A CA 1 ATOM 4293 C C . GLU A 1 558 ? -15.907 -34.142 28.126 1.00 39.52 ? 593 GLU A C 1 ATOM 4294 O O . GLU A 1 558 ? -15.666 -32.991 27.771 1.00 38.42 ? 593 GLU A O 1 ATOM 4295 C CB . GLU A 1 558 ? -16.781 -35.971 26.629 1.00 50.76 ? 593 GLU A CB 1 ATOM 4296 C CG . GLU A 1 558 ? -17.596 -35.128 25.666 1.00 57.60 ? 593 GLU A CG 1 ATOM 4297 C CD . GLU A 1 558 ? -18.746 -35.926 25.070 1.00 67.02 ? 593 GLU A CD 1 ATOM 4298 O OE1 . GLU A 1 558 ? -18.741 -36.163 23.842 1.00 71.05 ? 593 GLU A OE1 1 ATOM 4299 O OE2 . GLU A 1 558 ? -19.645 -36.342 25.837 1.00 71.47 ? 593 GLU A OE2 1 ATOM 4300 N N . ARG A 1 559 ? -16.460 -34.433 29.306 1.00 32.64 ? 594 ARG A N 1 ATOM 4301 C CA . ARG A 1 559 ? -17.030 -33.402 30.188 1.00 32.69 ? 594 ARG A CA 1 ATOM 4302 C C . ARG A 1 559 ? -15.998 -32.669 31.073 1.00 27.63 ? 594 ARG A C 1 ATOM 4303 O O . ARG A 1 559 ? -16.121 -31.475 31.308 1.00 26.77 ? 594 ARG A O 1 ATOM 4304 C CB . ARG A 1 559 ? -18.116 -34.018 31.090 1.00 35.15 ? 594 ARG A CB 1 ATOM 4305 C CG . ARG A 1 559 ? -19.305 -34.525 30.287 1.00 39.55 ? 594 ARG A CG 1 ATOM 4306 C CD . ARG A 1 559 ? -20.419 -35.098 31.150 1.00 43.85 ? 594 ARG A CD 1 ATOM 4307 N NE . ARG A 1 559 ? -20.004 -36.289 31.899 1.00 46.41 ? 594 ARG A NE 1 ATOM 4308 C CZ . ARG A 1 559 ? -19.897 -36.386 33.232 1.00 48.12 ? 594 ARG A CZ 1 ATOM 4309 N NH1 . ARG A 1 559 ? -20.161 -35.356 34.048 1.00 48.31 ? 594 ARG A NH1 1 ATOM 4310 N NH2 . ARG A 1 559 ? -19.518 -37.546 33.764 1.00 46.43 ? 594 ARG A NH2 1 ATOM 4311 N N . HIS A 1 560 ? -14.996 -33.401 31.541 1.00 27.24 ? 595 HIS A N 1 ATOM 4312 C CA . HIS A 1 560 ? -14.047 -32.920 32.545 1.00 27.81 ? 595 HIS A CA 1 ATOM 4313 C C . HIS A 1 560 ? -12.643 -32.595 32.041 1.00 27.58 ? 595 HIS A C 1 ATOM 4314 O O . HIS A 1 560 ? -11.914 -31.872 32.735 1.00 25.47 ? 595 HIS A O 1 ATOM 4315 C CB . HIS A 1 560 ? -14.009 -33.913 33.717 1.00 27.61 ? 595 HIS A CB 1 ATOM 4316 C CG . HIS A 1 560 ? -15.337 -34.086 34.372 1.00 29.78 ? 595 HIS A CG 1 ATOM 4317 N ND1 . HIS A 1 560 ? -16.082 -33.022 34.824 1.00 29.78 ? 595 HIS A ND1 1 ATOM 4318 C CD2 . HIS A 1 560 ? -16.077 -35.191 34.621 1.00 30.08 ? 595 HIS A CD2 1 ATOM 4319 C CE1 . HIS A 1 560 ? -17.224 -33.456 35.317 1.00 30.53 ? 595 HIS A CE1 1 ATOM 4320 N NE2 . HIS A 1 560 ? -17.243 -34.771 35.209 1.00 31.35 ? 595 HIS A NE2 1 ATOM 4321 N N . LEU A 1 561 ? -12.267 -33.087 30.851 1.00 27.59 ? 596 LEU A N 1 ATOM 4322 C CA . LEU A 1 561 ? -11.001 -32.727 30.197 1.00 29.19 ? 596 LEU A CA 1 ATOM 4323 C C . LEU A 1 561 ? -11.297 -31.991 28.892 1.00 29.49 ? 596 LEU A C 1 ATOM 4324 O O . LEU A 1 561 ? -11.233 -32.569 27.800 1.00 29.67 ? 596 LEU A O 1 ATOM 4325 C CB . LEU A 1 561 ? -10.128 -33.947 29.896 1.00 32.52 ? 596 LEU A CB 1 ATOM 4326 C CG . LEU A 1 561 ? -9.115 -34.477 30.900 1.00 34.30 ? 596 LEU A CG 1 ATOM 4327 C CD1 . LEU A 1 561 ? -8.451 -35.673 30.234 1.00 37.57 ? 596 LEU A CD1 1 ATOM 4328 C CD2 . LEU A 1 561 ? -8.068 -33.452 31.280 1.00 32.12 ? 596 LEU A CD2 1 ATOM 4329 N N . LEU A 1 562 ? -11.588 -30.705 29.012 1.00 25.27 ? 597 LEU A N 1 ATOM 4330 C CA . LEU A 1 562 ? -12.036 -29.925 27.855 1.00 25.54 ? 597 LEU A CA 1 ATOM 4331 C C . LEU A 1 562 ? -10.958 -29.644 26.820 1.00 23.86 ? 597 LEU A C 1 ATOM 4332 O O . LEU A 1 562 ? -11.292 -29.414 25.664 1.00 24.69 ? 597 LEU A O 1 ATOM 4333 C CB . LEU A 1 562 ? -12.670 -28.610 28.305 1.00 24.22 ? 597 LEU A CB 1 ATOM 4334 C CG . LEU A 1 562 ? -13.894 -28.746 29.222 1.00 25.54 ? 597 LEU A CG 1 ATOM 4335 C CD1 . LEU A 1 562 ? -14.430 -27.374 29.571 1.00 24.48 ? 597 LEU A CD1 1 ATOM 4336 C CD2 . LEU A 1 562 ? -15.004 -29.586 28.605 1.00 26.42 ? 597 LEU A CD2 1 ATOM 4337 N N . TYR A 1 563 ? -9.691 -29.679 27.234 1.00 23.07 ? 598 TYR A N 1 ATOM 4338 C CA . TYR A 1 563 ? -8.564 -29.260 26.400 1.00 22.74 ? 598 TYR A CA 1 ATOM 4339 C C . TYR A 1 563 ? -7.558 -30.399 26.219 1.00 24.00 ? 598 TYR A C 1 ATOM 4340 O O . TYR A 1 563 ? -6.385 -30.168 25.903 1.00 23.14 ? 598 TYR A O 1 ATOM 4341 C CB . TYR A 1 563 ? -7.902 -27.992 27.006 1.00 22.65 ? 598 TYR A CB 1 ATOM 4342 C CG . TYR A 1 563 ? -8.920 -27.078 27.639 1.00 21.08 ? 598 TYR A CG 1 ATOM 4343 C CD1 . TYR A 1 563 ? -9.834 -26.371 26.860 1.00 21.94 ? 598 TYR A CD1 1 ATOM 4344 C CD2 . TYR A 1 563 ? -9.015 -26.973 29.026 1.00 20.54 ? 598 TYR A CD2 1 ATOM 4345 C CE1 . TYR A 1 563 ? -10.804 -25.569 27.440 1.00 21.45 ? 598 TYR A CE1 1 ATOM 4346 C CE2 . TYR A 1 563 ? -9.984 -26.182 29.609 1.00 19.87 ? 598 TYR A CE2 1 ATOM 4347 C CZ . TYR A 1 563 ? -10.874 -25.478 28.824 1.00 20.17 ? 598 TYR A CZ 1 ATOM 4348 O OH . TYR A 1 563 ? -11.833 -24.699 29.442 1.00 19.78 ? 598 TYR A OH 1 ATOM 4349 N N . GLY A 1 564 ? -8.033 -31.631 26.386 1.00 23.45 ? 599 GLY A N 1 ATOM 4350 C CA . GLY A 1 564 ? -7.186 -32.793 26.269 1.00 24.80 ? 599 GLY A CA 1 ATOM 4351 C C . GLY A 1 564 ? -6.409 -33.092 27.528 1.00 25.91 ? 599 GLY A C 1 ATOM 4352 O O . GLY A 1 564 ? -6.267 -32.270 28.425 1.00 24.13 ? 599 GLY A O 1 ATOM 4353 N N . ARG A 1 565 ? -5.865 -34.285 27.563 1.00 26.28 ? 600 ARG A N 1 ATOM 4354 C CA . ARG A 1 565 ? -5.118 -34.738 28.706 1.00 28.83 ? 600 ARG A CA 1 ATOM 4355 C C . ARG A 1 565 ? -3.789 -33.969 28.731 1.00 25.71 ? 600 ARG A C 1 ATOM 4356 O O . ARG A 1 565 ? -3.147 -33.823 27.700 1.00 23.42 ? 600 ARG A O 1 ATOM 4357 C CB . ARG A 1 565 ? -4.903 -36.236 28.528 1.00 34.61 ? 600 ARG A CB 1 ATOM 4358 C CG . ARG A 1 565 ? -4.270 -36.962 29.677 1.00 39.59 ? 600 ARG A CG 1 ATOM 4359 C CD . ARG A 1 565 ? -4.263 -38.465 29.398 1.00 43.26 ? 600 ARG A CD 1 ATOM 4360 N NE . ARG A 1 565 ? -3.569 -38.822 28.162 1.00 43.53 ? 600 ARG A NE 1 ATOM 4361 C CZ . ARG A 1 565 ? -2.253 -38.755 27.975 1.00 44.09 ? 600 ARG A CZ 1 ATOM 4362 N NH1 . ARG A 1 565 ? -1.438 -38.322 28.939 1.00 46.20 ? 600 ARG A NH1 1 ATOM 4363 N NH2 . ARG A 1 565 ? -1.743 -39.117 26.803 1.00 47.22 ? 600 ARG A NH2 1 ATOM 4364 N N . PRO A 1 566 ? -3.370 -33.462 29.895 1.00 24.34 ? 601 PRO A N 1 ATOM 4365 C CA . PRO A 1 566 ? -2.022 -32.869 29.936 1.00 23.89 ? 601 PRO A CA 1 ATOM 4366 C C . PRO A 1 566 ? -0.958 -33.921 29.565 1.00 25.48 ? 601 PRO A C 1 ATOM 4367 O O . PRO A 1 566 ? -1.121 -35.080 29.931 1.00 28.75 ? 601 PRO A O 1 ATOM 4368 C CB . PRO A 1 566 ? -1.853 -32.464 31.408 1.00 23.53 ? 601 PRO A CB 1 ATOM 4369 C CG . PRO A 1 566 ? -3.225 -32.456 31.986 1.00 23.88 ? 601 PRO A CG 1 ATOM 4370 C CD . PRO A 1 566 ? -4.015 -33.466 31.223 1.00 23.97 ? 601 PRO A CD 1 ATOM 4371 N N . ALA A 1 567 ? 0.079 -33.534 28.828 1.00 23.06 ? 602 ALA A N 1 ATOM 4372 C CA . ALA A 1 567 ? 1.185 -34.442 28.540 1.00 23.92 ? 602 ALA A CA 1 ATOM 4373 C C . ALA A 1 567 ? 2.240 -34.403 29.647 1.00 23.31 ? 602 ALA A C 1 ATOM 4374 O O . ALA A 1 567 ? 2.614 -33.325 30.143 1.00 22.73 ? 602 ALA A O 1 ATOM 4375 C CB . ALA A 1 567 ? 1.822 -34.129 27.203 1.00 24.43 ? 602 ALA A CB 1 ATOM 4376 N N . VAL A 1 568 ? 2.744 -35.576 30.006 1.00 22.15 ? 603 VAL A N 1 ATOM 4377 C CA . VAL A 1 568 ? 3.823 -35.693 30.974 1.00 22.74 ? 603 VAL A CA 1 ATOM 4378 C C . VAL A 1 568 ? 5.159 -35.689 30.218 1.00 22.94 ? 603 VAL A C 1 ATOM 4379 O O . VAL A 1 568 ? 5.426 -36.604 29.439 1.00 23.87 ? 603 VAL A O 1 ATOM 4380 C CB . VAL A 1 568 ? 3.644 -36.955 31.831 1.00 24.55 ? 603 VAL A CB 1 ATOM 4381 C CG1 . VAL A 1 568 ? 4.777 -37.094 32.852 1.00 26.74 ? 603 VAL A CG1 1 ATOM 4382 C CG2 . VAL A 1 568 ? 2.299 -36.914 32.519 1.00 25.14 ? 603 VAL A CG2 1 ATOM 4383 N N . LEU A 1 569 ? 5.979 -34.658 30.460 1.00 20.82 ? 604 LEU A N 1 ATOM 4384 C CA . LEU A 1 569 ? 7.230 -34.408 29.722 1.00 21.73 ? 604 LEU A CA 1 ATOM 4385 C C . LEU A 1 569 ? 8.503 -34.921 30.404 1.00 23.66 ? 604 LEU A C 1 ATOM 4386 O O . LEU A 1 569 ? 9.612 -34.514 30.053 1.00 25.20 ? 604 LEU A O 1 ATOM 4387 C CB . LEU A 1 569 ? 7.360 -32.915 29.411 1.00 21.75 ? 604 LEU A CB 1 ATOM 4388 C CG . LEU A 1 569 ? 6.177 -32.271 28.667 1.00 21.95 ? 604 LEU A CG 1 ATOM 4389 C CD1 . LEU A 1 569 ? 6.632 -30.898 28.161 1.00 22.29 ? 604 LEU A CD1 1 ATOM 4390 C CD2 . LEU A 1 569 ? 5.638 -33.136 27.536 1.00 23.31 ? 604 LEU A CD2 1 ATOM 4391 N N . TYR A 1 570 ? 8.351 -35.841 31.347 1.00 23.06 ? 605 TYR A N 1 ATOM 4392 C CA . TYR A 1 570 ? 9.483 -36.493 31.973 1.00 24.28 ? 605 TYR A CA 1 ATOM 4393 C C . TYR A 1 570 ? 9.142 -37.966 32.139 1.00 25.00 ? 605 TYR A C 1 ATOM 4394 O O . TYR A 1 570 ? 8.004 -38.360 31.894 1.00 24.68 ? 605 TYR A O 1 ATOM 4395 C CB . TYR A 1 570 ? 9.814 -35.830 33.309 1.00 23.56 ? 605 TYR A CB 1 ATOM 4396 C CG . TYR A 1 570 ? 8.736 -35.904 34.380 1.00 23.49 ? 605 TYR A CG 1 ATOM 4397 C CD1 . TYR A 1 570 ? 7.624 -35.043 34.363 1.00 21.79 ? 605 TYR A CD1 1 ATOM 4398 C CD2 . TYR A 1 570 ? 8.846 -36.810 35.436 1.00 24.13 ? 605 TYR A CD2 1 ATOM 4399 C CE1 . TYR A 1 570 ? 6.650 -35.111 35.359 1.00 21.61 ? 605 TYR A CE1 1 ATOM 4400 C CE2 . TYR A 1 570 ? 7.876 -36.879 36.429 1.00 24.11 ? 605 TYR A CE2 1 ATOM 4401 C CZ . TYR A 1 570 ? 6.786 -36.024 36.394 1.00 22.69 ? 605 TYR A CZ 1 ATOM 4402 O OH . TYR A 1 570 ? 5.854 -36.123 37.417 1.00 24.51 ? 605 TYR A OH 1 ATOM 4403 N N . ARG A 1 571 ? 10.123 -38.774 32.521 1.00 27.03 ? 606 ARG A N 1 ATOM 4404 C CA . ARG A 1 571 ? 9.913 -40.219 32.633 1.00 28.59 ? 606 ARG A CA 1 ATOM 4405 C C . ARG A 1 571 ? 9.351 -40.589 33.997 1.00 27.73 ? 606 ARG A C 1 ATOM 4406 O O . ARG A 1 571 ? 9.982 -40.341 35.010 1.00 28.09 ? 606 ARG A O 1 ATOM 4407 C CB . ARG A 1 571 ? 11.215 -40.978 32.356 1.00 33.88 ? 606 ARG A CB 1 ATOM 4408 C CG . ARG A 1 571 ? 11.662 -40.845 30.906 1.00 38.42 ? 606 ARG A CG 1 ATOM 4409 C CD . ARG A 1 571 ? 12.914 -41.652 30.637 1.00 44.72 ? 606 ARG A CD 1 ATOM 4410 N NE . ARG A 1 571 ? 14.027 -41.168 31.457 1.00 49.61 ? 606 ARG A NE 1 ATOM 4411 C CZ . ARG A 1 571 ? 14.991 -40.328 31.064 1.00 57.18 ? 606 ARG A CZ 1 ATOM 4412 N NH1 . ARG A 1 571 ? 15.045 -39.849 29.819 1.00 58.51 ? 606 ARG A NH1 1 ATOM 4413 N NH2 . ARG A 1 571 ? 15.933 -39.971 31.936 1.00 60.35 ? 606 ARG A NH2 1 ATOM 4414 N N . THR A 1 572 ? 8.157 -41.166 34.016 1.00 28.23 ? 607 THR A N 1 ATOM 4415 C CA . THR A 1 572 ? 7.511 -41.585 35.259 1.00 28.88 ? 607 THR A CA 1 ATOM 4416 C C . THR A 1 572 ? 6.436 -42.635 34.983 1.00 30.45 ? 607 THR A C 1 ATOM 4417 O O . THR A 1 572 ? 6.162 -42.958 33.830 1.00 30.44 ? 607 THR A O 1 ATOM 4418 C CB . THR A 1 572 ? 6.912 -40.364 36.005 1.00 28.35 ? 607 THR A CB 1 ATOM 4419 O OG1 . THR A 1 572 ? 6.671 -40.701 37.374 1.00 28.40 ? 607 THR A OG1 1 ATOM 4420 C CG2 . THR A 1 572 ? 5.622 -39.872 35.355 1.00 27.30 ? 607 THR A CG2 1 ATOM 4421 N N . SER A 1 573 ? 5.830 -43.157 36.046 1.00 30.27 ? 608 SER A N 1 ATOM 4422 C CA . SER A 1 573 ? 4.756 -44.141 35.938 1.00 32.08 ? 608 SER A CA 1 ATOM 4423 C C . SER A 1 573 ? 3.510 -43.559 36.538 1.00 30.30 ? 608 SER A C 1 ATOM 4424 O O . SER A 1 573 ? 3.493 -43.236 37.737 1.00 29.82 ? 608 SER A O 1 ATOM 4425 C CB . SER A 1 573 ? 5.116 -45.413 36.694 1.00 33.97 ? 608 SER A CB 1 ATOM 4426 O OG . SER A 1 573 ? 6.192 -46.042 36.037 1.00 41.09 ? 608 SER A OG 1 ATOM 4427 N N . TYR A 1 574 ? 2.465 -43.449 35.722 1.00 29.05 ? 609 TYR A N 1 ATOM 4428 C CA . TYR A 1 574 ? 1.212 -42.870 36.191 1.00 27.64 ? 609 TYR A CA 1 ATOM 4429 C C . TYR A 1 574 ? -0.008 -43.495 35.526 1.00 28.23 ? 609 TYR A C 1 ATOM 4430 O O . TYR A 1 574 ? 0.102 -44.138 34.470 1.00 29.27 ? 609 TYR A O 1 ATOM 4431 C CB . TYR A 1 574 ? 1.266 -41.338 36.030 1.00 26.82 ? 609 TYR A CB 1 ATOM 4432 C CG . TYR A 1 574 ? 0.955 -40.797 34.654 1.00 25.90 ? 609 TYR A CG 1 ATOM 4433 C CD1 . TYR A 1 574 ? 1.903 -40.809 33.639 1.00 26.31 ? 609 TYR A CD1 1 ATOM 4434 C CD2 . TYR A 1 574 ? -0.289 -40.256 34.384 1.00 25.96 ? 609 TYR A CD2 1 ATOM 4435 C CE1 . TYR A 1 574 ? 1.602 -40.288 32.381 1.00 26.29 ? 609 TYR A CE1 1 ATOM 4436 C CE2 . TYR A 1 574 ? -0.596 -39.735 33.149 1.00 25.69 ? 609 TYR A CE2 1 ATOM 4437 C CZ . TYR A 1 574 ? 0.351 -39.741 32.155 1.00 26.68 ? 609 TYR A CZ 1 ATOM 4438 O OH . TYR A 1 574 ? -0.007 -39.228 30.938 1.00 27.17 ? 609 TYR A OH 1 ATOM 4439 N N . ASP A 1 575 ? -1.154 -43.351 36.184 1.00 28.26 ? 610 ASP A N 1 ATOM 4440 C CA . ASP A 1 575 ? -2.412 -43.965 35.763 1.00 29.02 ? 610 ASP A CA 1 ATOM 4441 C C . ASP A 1 575 ? -3.446 -42.891 35.501 1.00 28.32 ? 610 ASP A C 1 ATOM 4442 O O . ASP A 1 575 ? -3.530 -41.924 36.268 1.00 28.07 ? 610 ASP A O 1 ATOM 4443 C CB . ASP A 1 575 ? -3.003 -44.857 36.853 1.00 30.73 ? 610 ASP A CB 1 ATOM 4444 C CG . ASP A 1 575 ? -2.020 -45.829 37.433 1.00 33.43 ? 610 ASP A CG 1 ATOM 4445 O OD1 . ASP A 1 575 ? -1.262 -46.457 36.681 1.00 34.74 ? 610 ASP A OD1 1 ATOM 4446 O OD2 . ASP A 1 575 ? -2.043 -45.989 38.669 1.00 34.07 ? 610 ASP A OD2 1 ATOM 4447 N N . ILE A 1 576 ? -4.256 -43.080 34.464 1.00 27.40 ? 611 ILE A N 1 ATOM 4448 C CA . ILE A 1 576 ? -5.452 -42.270 34.260 1.00 27.24 ? 611 ILE A CA 1 ATOM 4449 C C . ILE A 1 576 ? -6.585 -42.910 35.012 1.00 26.91 ? 611 ILE A C 1 ATOM 4450 O O . ILE A 1 576 ? -6.844 -44.116 34.841 1.00 27.21 ? 611 ILE A O 1 ATOM 4451 C CB . ILE A 1 576 ? -5.844 -42.179 32.770 1.00 27.98 ? 611 ILE A CB 1 ATOM 4452 C CG1 . ILE A 1 576 ? -4.725 -41.523 31.988 1.00 29.43 ? 611 ILE A CG1 1 ATOM 4453 C CG2 . ILE A 1 576 ? -7.150 -41.411 32.573 1.00 27.20 ? 611 ILE A CG2 1 ATOM 4454 C CD1 . ILE A 1 576 ? -4.442 -40.103 32.366 1.00 28.01 ? 611 ILE A CD1 1 ATOM 4455 N N . LEU A 1 577 ? -7.281 -42.102 35.810 1.00 25.06 ? 612 LEU A N 1 ATOM 4456 C CA . LEU A 1 577 ? -8.417 -42.567 36.609 1.00 26.11 ? 612 LEU A CA 1 ATOM 4457 C C . LEU A 1 577 ? -9.643 -41.734 36.249 1.00 25.65 ? 612 LEU A C 1 ATOM 4458 O O . LEU A 1 577 ? -9.630 -40.510 36.362 1.00 24.11 ? 612 LEU A O 1 ATOM 4459 C CB . LEU A 1 577 ? -8.130 -42.445 38.107 1.00 26.47 ? 612 LEU A CB 1 ATOM 4460 C CG . LEU A 1 577 ? -6.877 -43.127 38.642 1.00 26.06 ? 612 LEU A CG 1 ATOM 4461 C CD1 . LEU A 1 577 ? -6.744 -42.829 40.120 1.00 26.78 ? 612 LEU A CD1 1 ATOM 4462 C CD2 . LEU A 1 577 ? -6.873 -44.638 38.403 1.00 28.07 ? 612 LEU A CD2 1 ATOM 4463 N N . TYR A 1 578 ? -10.707 -42.417 35.840 1.00 26.00 ? 613 TYR A N 1 ATOM 4464 C CA . TYR A 1 578 ? -11.952 -41.771 35.452 1.00 26.84 ? 613 TYR A CA 1 ATOM 4465 C C . TYR A 1 578 ? -12.977 -41.842 36.590 1.00 27.48 ? 613 TYR A C 1 ATOM 4466 O O . TYR A 1 578 ? -13.054 -42.844 37.306 1.00 28.04 ? 613 TYR A O 1 ATOM 4467 C CB . TYR A 1 578 ? -12.541 -42.482 34.242 1.00 27.76 ? 613 TYR A CB 1 ATOM 4468 C CG . TYR A 1 578 ? -11.662 -42.464 33.001 1.00 28.51 ? 613 TYR A CG 1 ATOM 4469 C CD1 . TYR A 1 578 ? -11.476 -41.286 32.267 1.00 29.03 ? 613 TYR A CD1 1 ATOM 4470 C CD2 . TYR A 1 578 ? -11.056 -43.631 32.530 1.00 31.14 ? 613 TYR A CD2 1 ATOM 4471 C CE1 . TYR A 1 578 ? -10.690 -41.272 31.111 1.00 28.30 ? 613 TYR A CE1 1 ATOM 4472 C CE2 . TYR A 1 578 ? -10.263 -43.622 31.377 1.00 30.69 ? 613 TYR A CE2 1 ATOM 4473 C CZ . TYR A 1 578 ? -10.083 -42.447 30.680 1.00 29.92 ? 613 TYR A CZ 1 ATOM 4474 O OH . TYR A 1 578 ? -9.314 -42.453 29.531 1.00 30.05 ? 613 TYR A OH 1 ATOM 4475 N N . HIS A 1 579 ? -13.760 -40.776 36.741 1.00 25.51 ? 614 HIS A N 1 ATOM 4476 C CA . HIS A 1 579 ? -14.902 -40.756 37.657 1.00 26.09 ? 614 HIS A CA 1 ATOM 4477 C C . HIS A 1 579 ? -15.993 -39.929 37.040 1.00 25.97 ? 614 HIS A C 1 ATOM 4478 O O . HIS A 1 579 ? -15.746 -39.140 36.132 1.00 27.71 ? 614 HIS A O 1 ATOM 4479 C CB . HIS A 1 579 ? -14.530 -40.132 39.009 1.00 25.22 ? 614 HIS A CB 1 ATOM 4480 C CG . HIS A 1 579 ? -13.151 -40.471 39.478 1.00 25.26 ? 614 HIS A CG 1 ATOM 4481 N ND1 . HIS A 1 579 ? -12.019 -39.969 38.875 1.00 24.49 ? 614 HIS A ND1 1 ATOM 4482 C CD2 . HIS A 1 579 ? -12.718 -41.288 40.465 1.00 26.19 ? 614 HIS A CD2 1 ATOM 4483 C CE1 . HIS A 1 579 ? -10.950 -40.438 39.481 1.00 24.82 ? 614 HIS A CE1 1 ATOM 4484 N NE2 . HIS A 1 579 ? -11.345 -41.245 40.447 1.00 26.41 ? 614 HIS A NE2 1 ATOM 4485 N N . THR A 1 580 ? -17.185 -40.039 37.601 1.00 26.53 ? 615 THR A N 1 ATOM 4486 C CA . THR A 1 580 ? -18.319 -39.221 37.170 1.00 26.96 ? 615 THR A CA 1 ATOM 4487 C C . THR A 1 580 ? -18.004 -37.724 37.152 1.00 25.29 ? 615 THR A C 1 ATOM 4488 O O . THR A 1 580 ? -18.364 -37.022 36.216 1.00 25.46 ? 615 THR A O 1 ATOM 4489 C CB . THR A 1 580 ? -19.525 -39.457 38.084 1.00 27.37 ? 615 THR A CB 1 ATOM 4490 O OG1 . THR A 1 580 ? -19.831 -40.851 38.065 1.00 30.51 ? 615 THR A OG1 1 ATOM 4491 C CG2 . THR A 1 580 ? -20.740 -38.675 37.605 1.00 27.64 ? 615 THR A CG2 1 ATOM 4492 N N . ASP A 1 581 ? -17.355 -37.237 38.195 1.00 25.33 ? 616 ASP A N 1 ATOM 4493 C CA . ASP A 1 581 ? -17.177 -35.801 38.379 1.00 24.60 ? 616 ASP A CA 1 ATOM 4494 C C . ASP A 1 581 ? -15.764 -35.284 38.086 1.00 24.10 ? 616 ASP A C 1 ATOM 4495 O O . ASP A 1 581 ? -15.552 -34.076 38.088 1.00 22.31 ? 616 ASP A O 1 ATOM 4496 C CB . ASP A 1 581 ? -17.542 -35.421 39.819 1.00 24.86 ? 616 ASP A CB 1 ATOM 4497 C CG . ASP A 1 581 ? -18.987 -35.652 40.153 1.00 26.45 ? 616 ASP A CG 1 ATOM 4498 O OD1 . ASP A 1 581 ? -19.837 -35.776 39.238 1.00 27.46 ? 616 ASP A OD1 1 ATOM 4499 O OD2 . ASP A 1 581 ? -19.280 -35.717 41.376 1.00 26.79 ? 616 ASP A OD2 1 ATOM 4500 N N . PHE A 1 582 ? -14.802 -36.176 37.864 1.00 23.54 ? 617 PHE A N 1 ATOM 4501 C CA . PHE A 1 582 ? -13.430 -35.752 37.640 1.00 22.92 ? 617 PHE A CA 1 ATOM 4502 C C . PHE A 1 582 ? -12.560 -36.829 37.037 1.00 23.38 ? 617 PHE A C 1 ATOM 4503 O O . PHE A 1 582 ? -12.880 -38.038 37.098 1.00 23.71 ? 617 PHE A O 1 ATOM 4504 C CB . PHE A 1 582 ? -12.778 -35.234 38.929 1.00 21.85 ? 617 PHE A CB 1 ATOM 4505 C CG . PHE A 1 582 ? -12.601 -36.273 40.009 1.00 23.05 ? 617 PHE A CG 1 ATOM 4506 C CD1 . PHE A 1 582 ? -13.659 -36.638 40.818 1.00 23.25 ? 617 PHE A CD1 1 ATOM 4507 C CD2 . PHE A 1 582 ? -11.347 -36.821 40.265 1.00 23.40 ? 617 PHE A CD2 1 ATOM 4508 C CE1 . PHE A 1 582 ? -13.489 -37.567 41.823 1.00 24.26 ? 617 PHE A CE1 1 ATOM 4509 C CE2 . PHE A 1 582 ? -11.164 -37.746 41.286 1.00 24.23 ? 617 PHE A CE2 1 ATOM 4510 C CZ . PHE A 1 582 ? -12.237 -38.124 42.059 1.00 24.04 ? 617 PHE A CZ 1 ATOM 4511 N N . GLU A 1 583 ? -11.465 -36.379 36.426 1.00 22.10 ? 618 GLU A N 1 ATOM 4512 C CA . GLU A 1 583 ? -10.441 -37.277 35.897 1.00 23.48 ? 618 GLU A CA 1 ATOM 4513 C C . GLU A 1 583 ? -9.098 -36.892 36.480 1.00 22.76 ? 618 GLU A C 1 ATOM 4514 O O . GLU A 1 583 ? -8.825 -35.695 36.662 1.00 22.25 ? 618 GLU A O 1 ATOM 4515 C CB . GLU A 1 583 ? -10.386 -37.169 34.365 1.00 24.83 ? 618 GLU A CB 1 ATOM 4516 C CG . GLU A 1 583 ? -9.347 -38.087 33.702 1.00 26.27 ? 618 GLU A CG 1 ATOM 4517 C CD . GLU A 1 583 ? -9.469 -38.160 32.186 1.00 29.66 ? 618 GLU A CD 1 ATOM 4518 O OE1 . GLU A 1 583 ? -10.575 -37.928 31.644 1.00 30.05 ? 618 GLU A OE1 1 ATOM 4519 O OE2 . GLU A 1 583 ? -8.444 -38.465 31.527 1.00 28.44 ? 618 GLU A OE2 1 ATOM 4520 N N . SER A 1 584 ? -8.237 -37.879 36.711 1.00 22.55 ? 619 SER A N 1 ATOM 4521 C CA . SER A 1 584 ? -6.911 -37.607 37.247 1.00 23.19 ? 619 SER A CA 1 ATOM 4522 C C . SER A 1 584 ? -5.812 -38.418 36.600 1.00 23.35 ? 619 SER A C 1 ATOM 4523 O O . SER A 1 584 ? -6.041 -39.495 36.045 1.00 23.93 ? 619 SER A O 1 ATOM 4524 C CB . SER A 1 584 ? -6.864 -37.838 38.753 1.00 24.55 ? 619 SER A CB 1 ATOM 4525 O OG . SER A 1 584 ? -7.153 -39.194 39.074 1.00 25.25 ? 619 SER A OG 1 ATOM 4526 N N . GLY A 1 585 ? -4.610 -37.870 36.692 1.00 22.76 ? 620 GLY A N 1 ATOM 4527 C CA . GLY A 1 585 ? -3.368 -38.550 36.344 1.00 23.71 ? 620 GLY A CA 1 ATOM 4528 C C . GLY A 1 585 ? -2.646 -38.840 37.639 1.00 24.08 ? 620 GLY A C 1 ATOM 4529 O O . GLY A 1 585 ? -2.010 -37.943 38.222 1.00 23.00 ? 620 GLY A O 1 ATOM 4530 N N . TYR A 1 586 ? -2.766 -40.090 38.090 1.00 24.20 ? 621 TYR A N 1 ATOM 4531 C CA . TYR A 1 586 ? -2.271 -40.511 39.388 1.00 24.70 ? 621 TYR A CA 1 ATOM 4532 C C . TYR A 1 586 ? -0.842 -41.027 39.290 1.00 25.48 ? 621 TYR A C 1 ATOM 4533 O O . TYR A 1 586 ? -0.598 -42.048 38.641 1.00 28.23 ? 621 TYR A O 1 ATOM 4534 C CB . TYR A 1 586 ? -3.187 -41.594 39.973 1.00 25.69 ? 621 TYR A CB 1 ATOM 4535 C CG . TYR A 1 586 ? -2.734 -42.093 41.325 1.00 26.50 ? 621 TYR A CG 1 ATOM 4536 C CD1 . TYR A 1 586 ? -2.987 -41.351 42.482 1.00 25.56 ? 621 TYR A CD1 1 ATOM 4537 C CD2 . TYR A 1 586 ? -2.033 -43.282 41.455 1.00 27.28 ? 621 TYR A CD2 1 ATOM 4538 C CE1 . TYR A 1 586 ? -2.558 -41.794 43.728 1.00 25.95 ? 621 TYR A CE1 1 ATOM 4539 C CE2 . TYR A 1 586 ? -1.615 -43.736 42.696 1.00 28.26 ? 621 TYR A CE2 1 ATOM 4540 C CZ . TYR A 1 586 ? -1.856 -42.977 43.826 1.00 27.45 ? 621 TYR A CZ 1 ATOM 4541 O OH . TYR A 1 586 ? -1.436 -43.420 45.056 1.00 28.64 ? 621 TYR A OH 1 ATOM 4542 N N . SER A 1 587 ? 0.093 -40.345 39.942 1.00 25.22 ? 622 SER A N 1 ATOM 4543 C CA . SER A 1 587 ? 1.472 -40.807 39.992 1.00 25.90 ? 622 SER A CA 1 ATOM 4544 C C . SER A 1 587 ? 1.661 -41.988 40.949 1.00 28.13 ? 622 SER A C 1 ATOM 4545 O O . SER A 1 587 ? 1.442 -41.878 42.154 1.00 28.16 ? 622 SER A O 1 ATOM 4546 C CB . SER A 1 587 ? 2.415 -39.685 40.392 1.00 24.35 ? 622 SER A CB 1 ATOM 4547 O OG . SER A 1 587 ? 3.744 -40.150 40.493 1.00 24.14 ? 622 SER A OG 1 ATOM 4548 N N . GLU A 1 588 ? 2.114 -43.112 40.408 1.00 30.96 ? 623 GLU A N 1 ATOM 4549 C CA . GLU A 1 588 ? 2.481 -44.252 41.252 1.00 33.54 ? 623 GLU A CA 1 ATOM 4550 C C . GLU A 1 588 ? 3.817 -44.023 41.983 1.00 34.29 ? 623 GLU A C 1 ATOM 4551 O O . GLU A 1 588 ? 4.135 -44.761 42.903 1.00 37.15 ? 623 GLU A O 1 ATOM 4552 C CB . GLU A 1 588 ? 2.487 -45.546 40.440 1.00 35.82 ? 623 GLU A CB 1 ATOM 4553 C CG . GLU A 1 588 ? 1.076 -45.972 40.046 1.00 36.46 ? 623 GLU A CG 1 ATOM 4554 C CD . GLU A 1 588 ? 0.975 -47.392 39.528 1.00 38.59 ? 623 GLU A CD 1 ATOM 4555 O OE1 . GLU A 1 588 ? 2.009 -47.998 39.167 1.00 37.70 ? 623 GLU A OE1 1 ATOM 4556 O OE2 . GLU A 1 588 ? -0.167 -47.887 39.463 1.00 39.23 ? 623 GLU A OE2 1 ATOM 4557 N N . ILE A 1 589 ? 4.565 -42.990 41.592 1.00 31.62 ? 624 ILE A N 1 ATOM 4558 C CA . ILE A 1 589 ? 5.831 -42.634 42.240 1.00 32.23 ? 624 ILE A CA 1 ATOM 4559 C C . ILE A 1 589 ? 5.593 -41.705 43.436 1.00 31.60 ? 624 ILE A C 1 ATOM 4560 O O . ILE A 1 589 ? 6.084 -41.963 44.523 1.00 32.24 ? 624 ILE A O 1 ATOM 4561 C CB . ILE A 1 589 ? 6.825 -42.001 41.233 1.00 32.45 ? 624 ILE A CB 1 ATOM 4562 C CG1 . ILE A 1 589 ? 7.023 -42.906 40.004 1.00 33.99 ? 624 ILE A CG1 1 ATOM 4563 C CG2 . ILE A 1 589 ? 8.161 -41.677 41.900 1.00 33.72 ? 624 ILE A CG2 1 ATOM 4564 C CD1 . ILE A 1 589 ? 7.473 -44.327 40.302 1.00 37.22 ? 624 ILE A CD1 1 ATOM 4565 N N . PHE A 1 590 ? 4.832 -40.628 43.242 1.00 31.17 ? 625 PHE A N 1 ATOM 4566 C CA . PHE A 1 590 ? 4.535 -39.711 44.330 1.00 30.58 ? 625 PHE A CA 1 ATOM 4567 C C . PHE A 1 590 ? 3.318 -40.126 45.151 1.00 28.61 ? 625 PHE A C 1 ATOM 4568 O O . PHE A 1 590 ? 3.020 -39.476 46.142 1.00 27.55 ? 625 PHE A O 1 ATOM 4569 C CB . PHE A 1 590 ? 4.324 -38.279 43.806 1.00 32.35 ? 625 PHE A CB 1 ATOM 4570 C CG . PHE A 1 590 ? 5.548 -37.638 43.187 1.00 36.37 ? 625 PHE A CG 1 ATOM 4571 C CD1 . PHE A 1 590 ? 6.846 -38.069 43.461 1.00 41.77 ? 625 PHE A CD1 1 ATOM 4572 C CD2 . PHE A 1 590 ? 5.383 -36.541 42.348 1.00 43.02 ? 625 PHE A CD2 1 ATOM 4573 C CE1 . PHE A 1 590 ? 7.947 -37.447 42.889 1.00 42.88 ? 625 PHE A CE1 1 ATOM 4574 C CE2 . PHE A 1 590 ? 6.480 -35.906 41.779 1.00 45.10 ? 625 PHE A CE2 1 ATOM 4575 C CZ . PHE A 1 590 ? 7.765 -36.362 42.057 1.00 46.22 ? 625 PHE A CZ 1 ATOM 4576 N N . LEU A 1 591 ? 2.614 -41.185 44.739 1.00 29.63 ? 626 LEU A N 1 ATOM 4577 C CA . LEU A 1 591 ? 1.418 -41.685 45.447 1.00 29.55 ? 626 LEU A CA 1 ATOM 4578 C C . LEU A 1 591 ? 0.276 -40.653 45.519 1.00 28.44 ? 626 LEU A C 1 ATOM 4579 O O . LEU A 1 591 ? -0.483 -40.627 46.482 1.00 28.72 ? 626 LEU A O 1 ATOM 4580 C CB . LEU A 1 591 ? 1.787 -42.172 46.846 1.00 31.42 ? 626 LEU A CB 1 ATOM 4581 C CG . LEU A 1 591 ? 3.043 -43.028 46.972 1.00 32.93 ? 626 LEU A CG 1 ATOM 4582 C CD1 . LEU A 1 591 ? 3.295 -43.381 48.426 1.00 34.41 ? 626 LEU A CD1 1 ATOM 4583 C CD2 . LEU A 1 591 ? 2.907 -44.273 46.124 1.00 34.20 ? 626 LEU A CD2 1 ATOM 4584 N N . MET A 1 592 ? 0.155 -39.808 44.499 1.00 25.23 ? 627 MET A N 1 ATOM 4585 C CA . MET A 1 592 ? -0.917 -38.816 44.451 1.00 24.04 ? 627 MET A CA 1 ATOM 4586 C C . MET A 1 592 ? -1.073 -38.328 43.021 1.00 23.01 ? 627 MET A C 1 ATOM 4587 O O . MET A 1 592 ? -0.181 -38.589 42.181 1.00 23.82 ? 627 MET A O 1 ATOM 4588 C CB . MET A 1 592 ? -0.597 -37.637 45.384 1.00 23.44 ? 627 MET A CB 1 ATOM 4589 C CG . MET A 1 592 ? 0.617 -36.810 44.988 1.00 22.67 ? 627 MET A CG 1 ATOM 4590 S SD . MET A 1 592 ? 1.017 -35.518 46.193 1.00 22.37 ? 627 MET A SD 1 ATOM 4591 C CE . MET A 1 592 ? 1.661 -36.499 47.546 1.00 25.38 ? 627 MET A CE 1 ATOM 4592 N N . PRO A 1 593 ? -2.181 -37.631 42.724 1.00 21.84 ? 628 PRO A N 1 ATOM 4593 C CA . PRO A 1 593 ? -2.283 -37.101 41.370 1.00 21.42 ? 628 PRO A CA 1 ATOM 4594 C C . PRO A 1 593 ? -1.220 -36.064 41.027 1.00 21.16 ? 628 PRO A C 1 ATOM 4595 O O . PRO A 1 593 ? -0.809 -35.270 41.880 1.00 19.73 ? 628 PRO A O 1 ATOM 4596 C CB . PRO A 1 593 ? -3.686 -36.481 41.332 1.00 21.36 ? 628 PRO A CB 1 ATOM 4597 C CG . PRO A 1 593 ? -4.451 -37.230 42.382 1.00 21.01 ? 628 PRO A CG 1 ATOM 4598 C CD . PRO A 1 593 ? -3.438 -37.444 43.471 1.00 21.84 ? 628 PRO A CD 1 ATOM 4599 N N . LEU A 1 594 ? -0.779 -36.087 39.783 1.00 21.39 ? 629 LEU A N 1 ATOM 4600 C CA . LEU A 1 594 ? -0.023 -34.972 39.224 1.00 21.29 ? 629 LEU A CA 1 ATOM 4601 C C . LEU A 1 594 ? -0.988 -33.870 38.796 1.00 19.62 ? 629 LEU A C 1 ATOM 4602 O O . LEU A 1 594 ? -0.623 -32.696 38.772 1.00 17.38 ? 629 LEU A O 1 ATOM 4603 C CB . LEU A 1 594 ? 0.773 -35.432 38.008 1.00 22.27 ? 629 LEU A CB 1 ATOM 4604 C CG . LEU A 1 594 ? 1.711 -36.626 38.239 1.00 24.42 ? 629 LEU A CG 1 ATOM 4605 C CD1 . LEU A 1 594 ? 2.425 -37.007 36.952 1.00 25.31 ? 629 LEU A CD1 1 ATOM 4606 C CD2 . LEU A 1 594 ? 2.714 -36.290 39.339 1.00 24.96 ? 629 LEU A CD2 1 ATOM 4607 N N . TRP A 1 595 ? -2.183 -34.274 38.377 1.00 19.47 ? 630 TRP A N 1 ATOM 4608 C CA . TRP A 1 595 ? -3.231 -33.356 37.979 1.00 19.16 ? 630 TRP A CA 1 ATOM 4609 C C . TRP A 1 595 ? -4.571 -34.011 38.183 1.00 19.01 ? 630 TRP A C 1 ATOM 4610 O O . TRP A 1 595 ? -4.695 -35.227 38.062 1.00 19.01 ? 630 TRP A O 1 ATOM 4611 C CB . TRP A 1 595 ? -3.068 -32.915 36.492 1.00 19.19 ? 630 TRP A CB 1 ATOM 4612 C CG . TRP A 1 595 ? -3.037 -34.044 35.502 1.00 19.80 ? 630 TRP A CG 1 ATOM 4613 C CD1 . TRP A 1 595 ? -1.920 -34.636 34.968 1.00 20.78 ? 630 TRP A CD1 1 ATOM 4614 C CD2 . TRP A 1 595 ? -4.166 -34.703 34.896 1.00 20.79 ? 630 TRP A CD2 1 ATOM 4615 N NE1 . TRP A 1 595 ? -2.283 -35.629 34.091 1.00 21.80 ? 630 TRP A NE1 1 ATOM 4616 C CE2 . TRP A 1 595 ? -3.652 -35.690 34.023 1.00 20.84 ? 630 TRP A CE2 1 ATOM 4617 C CE3 . TRP A 1 595 ? -5.557 -34.552 35.005 1.00 19.58 ? 630 TRP A CE3 1 ATOM 4618 C CZ2 . TRP A 1 595 ? -4.485 -36.521 33.264 1.00 21.90 ? 630 TRP A CZ2 1 ATOM 4619 C CZ3 . TRP A 1 595 ? -6.391 -35.391 34.250 1.00 20.50 ? 630 TRP A CZ3 1 ATOM 4620 C CH2 . TRP A 1 595 ? -5.851 -36.367 33.405 1.00 21.23 ? 630 TRP A CH2 1 ATOM 4621 N N . THR A 1 596 ? -5.553 -33.177 38.499 1.00 19.40 ? 631 THR A N 1 ATOM 4622 C CA . THR A 1 596 ? -6.940 -33.577 38.671 1.00 19.87 ? 631 THR A CA 1 ATOM 4623 C C . THR A 1 596 ? -7.779 -32.548 37.929 1.00 18.90 ? 631 THR A C 1 ATOM 4624 O O . THR A 1 596 ? -7.647 -31.360 38.186 1.00 19.53 ? 631 THR A O 1 ATOM 4625 C CB . THR A 1 596 ? -7.322 -33.564 40.172 1.00 21.22 ? 631 THR A CB 1 ATOM 4626 O OG1 . THR A 1 596 ? -6.529 -34.522 40.896 1.00 22.54 ? 631 THR A OG1 1 ATOM 4627 C CG2 . THR A 1 596 ? -8.799 -33.870 40.374 1.00 22.46 ? 631 THR A CG2 1 ATOM 4628 N N . SER A 1 597 ? -8.667 -33.005 37.047 1.00 19.14 ? 632 SER A N 1 ATOM 4629 C CA . SER A 1 597 ? -9.372 -32.128 36.144 1.00 19.67 ? 632 SER A CA 1 ATOM 4630 C C . SER A 1 597 ? -10.881 -32.314 36.262 1.00 20.39 ? 632 SER A C 1 ATOM 4631 O O . SER A 1 597 ? -11.371 -33.456 36.298 1.00 20.65 ? 632 SER A O 1 ATOM 4632 C CB . SER A 1 597 ? -8.912 -32.420 34.706 1.00 19.82 ? 632 SER A CB 1 ATOM 4633 O OG . SER A 1 597 ? -9.545 -31.549 33.797 1.00 21.51 ? 632 SER A OG 1 ATOM 4634 N N . TYR A 1 598 ? -11.608 -31.199 36.317 1.00 19.53 ? 633 TYR A N 1 ATOM 4635 C CA . TYR A 1 598 ? -13.053 -31.234 36.470 1.00 19.93 ? 633 TYR A CA 1 ATOM 4636 C C . TYR A 1 598 ? -13.710 -29.939 36.051 1.00 20.39 ? 633 TYR A C 1 ATOM 4637 O O . TYR A 1 598 ? -13.121 -28.872 36.137 1.00 19.70 ? 633 TYR A O 1 ATOM 4638 C CB . TYR A 1 598 ? -13.420 -31.588 37.923 1.00 19.32 ? 633 TYR A CB 1 ATOM 4639 C CG . TYR A 1 598 ? -12.968 -30.587 38.986 1.00 18.73 ? 633 TYR A CG 1 ATOM 4640 C CD1 . TYR A 1 598 ? -11.674 -30.624 39.538 1.00 18.58 ? 633 TYR A CD1 1 ATOM 4641 C CD2 . TYR A 1 598 ? -13.850 -29.634 39.473 1.00 19.56 ? 633 TYR A CD2 1 ATOM 4642 C CE1 . TYR A 1 598 ? -11.287 -29.718 40.530 1.00 18.50 ? 633 TYR A CE1 1 ATOM 4643 C CE2 . TYR A 1 598 ? -13.483 -28.742 40.454 1.00 18.66 ? 633 TYR A CE2 1 ATOM 4644 C CZ . TYR A 1 598 ? -12.217 -28.783 40.990 1.00 18.78 ? 633 TYR A CZ 1 ATOM 4645 O OH . TYR A 1 598 ? -11.921 -27.883 41.977 1.00 17.40 ? 633 TYR A OH 1 ATOM 4646 N N . THR A 1 599 ? -14.952 -30.051 35.604 1.00 21.78 ? 634 THR A N 1 ATOM 4647 C CA . THR A 1 599 ? -15.720 -28.938 35.088 1.00 22.23 ? 634 THR A CA 1 ATOM 4648 C C . THR A 1 599 ? -16.898 -28.735 36.004 1.00 22.80 ? 634 THR A C 1 ATOM 4649 O O . THR A 1 599 ? -17.539 -29.700 36.428 1.00 23.70 ? 634 THR A O 1 ATOM 4650 C CB . THR A 1 599 ? -16.207 -29.191 33.654 1.00 23.48 ? 634 THR A CB 1 ATOM 4651 O OG1 . THR A 1 599 ? -15.068 -29.378 32.810 1.00 23.00 ? 634 THR A OG1 1 ATOM 4652 C CG2 . THR A 1 599 ? -17.044 -28.012 33.144 1.00 24.16 ? 634 THR A CG2 1 ATOM 4653 N N . ILE A 1 600 ? -17.169 -27.472 36.299 1.00 22.31 ? 635 ILE A N 1 ATOM 4654 C CA . ILE A 1 600 ? -18.224 -27.047 37.206 1.00 22.63 ? 635 ILE A CA 1 ATOM 4655 C C . ILE A 1 600 ? -19.081 -26.059 36.414 1.00 23.39 ? 635 ILE A C 1 ATOM 4656 O O . ILE A 1 600 ? -18.575 -25.041 35.967 1.00 22.07 ? 635 ILE A O 1 ATOM 4657 C CB . ILE A 1 600 ? -17.657 -26.341 38.463 1.00 22.48 ? 635 ILE A CB 1 ATOM 4658 C CG1 . ILE A 1 600 ? -16.744 -27.266 39.285 1.00 22.06 ? 635 ILE A CG1 1 ATOM 4659 C CG2 . ILE A 1 600 ? -18.796 -25.844 39.350 1.00 23.05 ? 635 ILE A CG2 1 ATOM 4660 C CD1 . ILE A 1 600 ? -17.402 -28.538 39.805 1.00 23.27 ? 635 ILE A CD1 1 ATOM 4661 N N . SER A 1 601 ? -20.362 -26.372 36.218 1.00 24.41 ? 636 SER A N 1 ATOM 4662 C CA . SER A 1 601 ? -21.261 -25.502 35.441 1.00 25.07 ? 636 SER A CA 1 ATOM 4663 C C . SER A 1 601 ? -21.670 -24.293 36.278 1.00 24.42 ? 636 SER A C 1 ATOM 4664 O O . SER A 1 601 ? -21.606 -24.335 37.499 1.00 23.87 ? 636 SER A O 1 ATOM 4665 C CB . SER A 1 601 ? -22.503 -26.276 34.956 1.00 26.78 ? 636 SER A CB 1 ATOM 4666 O OG . SER A 1 601 ? -23.473 -26.328 35.989 1.00 28.92 ? 636 SER A OG 1 ATOM 4667 N N . LYS A 1 602 ? -22.116 -23.229 35.615 1.00 25.90 ? 637 LYS A N 1 ATOM 4668 C CA . LYS A 1 602 ? -22.650 -22.028 36.290 1.00 26.84 ? 637 LYS A CA 1 ATOM 4669 C C . LYS A 1 602 ? -23.698 -22.338 37.375 1.00 28.12 ? 637 LYS A C 1 ATOM 4670 O O . LYS A 1 602 ? -23.751 -21.678 38.396 1.00 28.73 ? 637 LYS A O 1 ATOM 4671 C CB . LYS A 1 602 ? -23.283 -21.104 35.249 1.00 29.37 ? 637 LYS A CB 1 ATOM 4672 C CG . LYS A 1 602 ? -23.736 -19.744 35.747 1.00 31.11 ? 637 LYS A CG 1 ATOM 4673 C CD . LYS A 1 602 ? -24.611 -19.039 34.721 1.00 32.85 ? 637 LYS A CD 1 ATOM 4674 C CE . LYS A 1 602 ? -25.259 -17.825 35.353 1.00 35.66 ? 637 LYS A CE 1 ATOM 4675 N NZ . LYS A 1 602 ? -26.119 -17.049 34.407 1.00 39.02 ? 637 LYS A NZ 1 ATOM 4676 N N . GLN A 1 603 ? -24.518 -23.346 37.124 1.00 29.27 ? 638 GLN A N 1 ATOM 4677 C CA . GLN A 1 603 ? -25.665 -23.686 37.961 1.00 33.95 ? 638 GLN A CA 1 ATOM 4678 C C . GLN A 1 603 ? -25.371 -24.794 38.975 1.00 34.50 ? 638 GLN A C 1 ATOM 4679 O O . GLN A 1 603 ? -26.291 -25.268 39.652 1.00 33.88 ? 638 GLN A O 1 ATOM 4680 C CB . GLN A 1 603 ? -26.813 -24.142 37.052 1.00 36.06 ? 638 GLN A CB 1 ATOM 4681 C CG . GLN A 1 603 ? -27.219 -23.132 35.977 1.00 40.62 ? 638 GLN A CG 1 ATOM 4682 C CD . GLN A 1 603 ? -26.480 -23.276 34.639 1.00 45.09 ? 638 GLN A CD 1 ATOM 4683 O OE1 . GLN A 1 603 ? -25.613 -24.151 34.459 1.00 45.86 ? 638 GLN A OE1 1 ATOM 4684 N NE2 . GLN A 1 603 ? -26.827 -22.404 33.684 1.00 48.25 ? 638 GLN A NE2 1 ATOM 4685 N N . ALA A 1 604 ? -24.109 -25.209 39.085 1.00 32.97 ? 639 ALA A N 1 ATOM 4686 C CA . ALA A 1 604 ? -23.716 -26.294 39.989 1.00 33.03 ? 639 ALA A CA 1 ATOM 4687 C C . ALA A 1 604 ? -24.020 -25.966 41.441 1.00 33.23 ? 639 ALA A C 1 ATOM 4688 O O . ALA A 1 604 ? -23.915 -24.816 41.864 1.00 32.04 ? 639 ALA A O 1 ATOM 4689 C CB . ALA A 1 604 ? -22.232 -26.581 39.847 1.00 35.73 ? 639 ALA A CB 1 ATOM 4690 N N . GLU A 1 605 ? -24.355 -27.010 42.194 1.00 34.55 ? 640 GLU A N 1 ATOM 4691 C CA . GLU A 1 605 ? -24.728 -26.915 43.601 1.00 37.77 ? 640 GLU A CA 1 ATOM 4692 C C . GLU A 1 605 ? -23.569 -27.313 44.499 1.00 34.81 ? 640 GLU A C 1 ATOM 4693 O O . GLU A 1 605 ? -22.842 -28.270 44.198 1.00 33.84 ? 640 GLU A O 1 ATOM 4694 C CB . GLU A 1 605 ? -25.916 -27.850 43.888 1.00 41.52 ? 640 GLU A CB 1 ATOM 4695 C CG . GLU A 1 605 ? -27.112 -27.680 42.968 1.00 47.80 ? 640 GLU A CG 1 ATOM 4696 C CD . GLU A 1 605 ? -27.713 -26.290 43.042 1.00 52.93 ? 640 GLU A CD 1 ATOM 4697 O OE1 . GLU A 1 605 ? -27.056 -25.323 42.585 1.00 57.23 ? 640 GLU A OE1 1 ATOM 4698 O OE2 . GLU A 1 605 ? -28.847 -26.168 43.548 1.00 54.89 ? 640 GLU A OE2 1 ATOM 4699 N N . VAL A 1 606 ? -23.385 -26.557 45.582 1.00 33.57 ? 641 VAL A N 1 ATOM 4700 C CA . VAL A 1 606 ? -22.430 -26.904 46.622 1.00 33.33 ? 641 VAL A CA 1 ATOM 4701 C C . VAL A 1 606 ? -23.207 -27.680 47.682 1.00 33.25 ? 641 VAL A C 1 ATOM 4702 O O . VAL A 1 606 ? -24.313 -27.284 48.051 1.00 33.40 ? 641 VAL A O 1 ATOM 4703 C CB . VAL A 1 606 ? -21.749 -25.656 47.241 1.00 36.01 ? 641 VAL A CB 1 ATOM 4704 C CG1 . VAL A 1 606 ? -20.663 -26.062 48.239 1.00 35.46 ? 641 VAL A CG1 1 ATOM 4705 C CG2 . VAL A 1 606 ? -21.130 -24.772 46.149 1.00 36.22 ? 641 VAL A CG2 1 ATOM 4706 N N . SER A 1 607 ? -22.653 -28.800 48.132 1.00 33.52 ? 642 SER A N 1 ATOM 4707 C CA . SER A 1 607 ? -23.262 -29.596 49.216 1.00 35.35 ? 642 SER A CA 1 ATOM 4708 C C . SER A 1 607 ? -22.223 -29.856 50.296 1.00 37.95 ? 642 SER A C 1 ATOM 4709 O O . SER A 1 607 ? -21.033 -29.717 50.057 1.00 40.97 ? 642 SER A O 1 ATOM 4710 C CB . SER A 1 607 ? -23.837 -30.906 48.680 1.00 36.79 ? 642 SER A CB 1 ATOM 4711 O OG . SER A 1 607 ? -22.850 -31.654 47.994 1.00 37.62 ? 642 SER A OG 1 ATOM 4712 N N . SER A 1 608 ? -22.674 -30.167 51.505 1.00 39.53 ? 643 SER A N 1 ATOM 4713 C CA . SER A 1 608 ? -21.757 -30.353 52.629 1.00 42.19 ? 643 SER A CA 1 ATOM 4714 C C . SER A 1 608 ? -21.263 -31.787 52.627 1.00 44.24 ? 643 SER A C 1 ATOM 4715 O O . SER A 1 608 ? -21.823 -32.631 51.932 1.00 47.79 ? 643 SER A O 1 ATOM 4716 C CB . SER A 1 608 ? -22.459 -30.028 53.941 1.00 44.08 ? 643 SER A CB 1 ATOM 4717 O OG . SER A 1 608 ? -23.754 -30.591 53.945 1.00 47.39 ? 643 SER A OG 1 ATOM 4718 N N . ILE A 1 609 ? -20.209 -32.054 53.392 1.00 44.40 ? 644 ILE A N 1 ATOM 4719 C CA . ILE A 1 609 ? -19.735 -33.426 53.621 1.00 44.78 ? 644 ILE A CA 1 ATOM 4720 C C . ILE A 1 609 ? -20.578 -34.009 54.764 1.00 46.26 ? 644 ILE A C 1 ATOM 4721 O O . ILE A 1 609 ? -20.606 -33.429 55.842 1.00 46.00 ? 644 ILE A O 1 ATOM 4722 C CB . ILE A 1 609 ? -18.225 -33.455 53.978 1.00 43.03 ? 644 ILE A CB 1 ATOM 4723 C CG1 . ILE A 1 609 ? -17.398 -32.941 52.788 1.00 43.22 ? 644 ILE A CG1 1 ATOM 4724 C CG2 . ILE A 1 609 ? -17.783 -34.865 54.362 1.00 43.59 ? 644 ILE A CG2 1 ATOM 4725 C CD1 . ILE A 1 609 ? -15.945 -32.655 53.118 1.00 44.01 ? 644 ILE A CD1 1 ATOM 4726 N N . PRO A 1 610 ? -21.280 -35.144 54.537 1.00 47.92 ? 645 PRO A N 1 ATOM 4727 C CA . PRO A 1 610 ? -22.072 -35.690 55.649 1.00 48.69 ? 645 PRO A CA 1 ATOM 4728 C C . PRO A 1 610 ? -21.224 -36.104 56.854 1.00 50.65 ? 645 PRO A C 1 ATOM 4729 O O . PRO A 1 610 ? -20.035 -36.404 56.705 1.00 50.95 ? 645 PRO A O 1 ATOM 4730 C CB . PRO A 1 610 ? -22.766 -36.911 55.036 1.00 49.71 ? 645 PRO A CB 1 ATOM 4731 C CG . PRO A 1 610 ? -22.780 -36.648 53.574 1.00 49.64 ? 645 PRO A CG 1 ATOM 4732 C CD . PRO A 1 610 ? -21.522 -35.886 53.284 1.00 47.94 ? 645 PRO A CD 1 ATOM 4733 N N . GLU A 1 611 ? -21.853 -36.097 58.029 1.00 53.46 ? 646 GLU A N 1 ATOM 4734 C CA . GLU A 1 611 ? -21.218 -36.430 59.314 1.00 55.46 ? 646 GLU A CA 1 ATOM 4735 C C . GLU A 1 611 ? -20.414 -37.729 59.228 1.00 55.26 ? 646 GLU A C 1 ATOM 4736 O O . GLU A 1 611 ? -19.262 -37.785 59.650 1.00 54.29 ? 646 GLU A O 1 ATOM 4737 C CB . GLU A 1 611 ? -22.299 -36.554 60.406 1.00 60.92 ? 646 GLU A CB 1 ATOM 4738 C CG . GLU A 1 611 ? -21.794 -36.558 61.843 1.00 65.86 ? 646 GLU A CG 1 ATOM 4739 C CD . GLU A 1 611 ? -22.927 -36.570 62.867 1.00 71.35 ? 646 GLU A CD 1 ATOM 4740 O OE1 . GLU A 1 611 ? -23.768 -37.495 62.823 1.00 73.94 ? 646 GLU A OE1 1 ATOM 4741 O OE2 . GLU A 1 611 ? -22.977 -35.661 63.728 1.00 73.06 ? 646 GLU A OE2 1 ATOM 4742 N N . HIS A 1 612 ? -21.037 -38.753 58.652 1.00 56.24 ? 647 HIS A N 1 ATOM 4743 C CA . HIS A 1 612 ? -20.431 -40.084 58.505 1.00 57.24 ? 647 HIS A CA 1 ATOM 4744 C C . HIS A 1 612 ? -19.232 -40.167 57.548 1.00 52.50 ? 647 HIS A C 1 ATOM 4745 O O . HIS A 1 612 ? -18.425 -41.097 57.658 1.00 51.16 ? 647 HIS A O 1 ATOM 4746 C CB . HIS A 1 612 ? -21.498 -41.138 58.128 1.00 63.36 ? 647 HIS A CB 1 ATOM 4747 C CG . HIS A 1 612 ? -22.261 -40.837 56.867 1.00 69.09 ? 647 HIS A CG 1 ATOM 4748 N ND1 . HIS A 1 612 ? -23.428 -40.101 56.856 1.00 72.72 ? 647 HIS A ND1 1 ATOM 4749 C CD2 . HIS A 1 612 ? -22.041 -41.204 55.582 1.00 72.16 ? 647 HIS A CD2 1 ATOM 4750 C CE1 . HIS A 1 612 ? -23.882 -40.013 55.617 1.00 73.30 ? 647 HIS A CE1 1 ATOM 4751 N NE2 . HIS A 1 612 ? -23.058 -40.674 54.825 1.00 71.94 ? 647 HIS A NE2 1 ATOM 4752 N N . LEU A 1 613 ? -19.112 -39.214 56.623 1.00 48.83 ? 648 LEU A N 1 ATOM 4753 C CA . LEU A 1 613 ? -17.991 -39.179 55.674 1.00 46.71 ? 648 LEU A CA 1 ATOM 4754 C C . LEU A 1 613 ? -16.869 -38.199 56.027 1.00 44.94 ? 648 LEU A C 1 ATOM 4755 O O . LEU A 1 613 ? -15.876 -38.149 55.317 1.00 41.39 ? 648 LEU A O 1 ATOM 4756 C CB . LEU A 1 613 ? -18.503 -38.862 54.262 1.00 46.01 ? 648 LEU A CB 1 ATOM 4757 C CG . LEU A 1 613 ? -19.484 -39.836 53.608 1.00 48.70 ? 648 LEU A CG 1 ATOM 4758 C CD1 . LEU A 1 613 ? -19.636 -39.499 52.131 1.00 47.89 ? 648 LEU A CD1 1 ATOM 4759 C CD2 . LEU A 1 613 ? -19.043 -41.291 53.760 1.00 50.76 ? 648 LEU A CD2 1 ATOM 4760 N N . THR A 1 614 ? -17.007 -37.447 57.118 1.00 46.74 ? 649 THR A N 1 ATOM 4761 C CA . THR A 1 614 ? -16.024 -36.421 57.506 1.00 46.61 ? 649 THR A CA 1 ATOM 4762 C C . THR A 1 614 ? -14.573 -36.912 57.451 1.00 45.05 ? 649 THR A C 1 ATOM 4763 O O . THR A 1 614 ? -13.723 -36.272 56.822 1.00 46.39 ? 649 THR A O 1 ATOM 4764 C CB . THR A 1 614 ? -16.315 -35.893 58.925 1.00 49.35 ? 649 THR A CB 1 ATOM 4765 O OG1 . THR A 1 614 ? -17.724 -35.701 59.077 1.00 52.74 ? 649 THR A OG1 1 ATOM 4766 C CG2 . THR A 1 614 ? -15.598 -34.579 59.183 1.00 49.93 ? 649 THR A CG2 1 ATOM 4767 N N . ASN A 1 615 ? -14.312 -38.055 58.077 1.00 42.52 ? 650 ASN A N 1 ATOM 4768 C CA . ASN A 1 615 ? -12.972 -38.640 58.128 1.00 42.62 ? 650 ASN A CA 1 ATOM 4769 C C . ASN A 1 615 ? -12.840 -39.901 57.258 1.00 41.65 ? 650 ASN A C 1 ATOM 4770 O O . ASN A 1 615 ? -11.971 -40.745 57.488 1.00 39.96 ? 650 ASN A O 1 ATOM 4771 C CB . ASN A 1 615 ? -12.596 -38.925 59.589 1.00 46.46 ? 650 ASN A CB 1 ATOM 4772 C CG . ASN A 1 615 ? -12.427 -37.652 60.402 1.00 47.94 ? 650 ASN A CG 1 ATOM 4773 O OD1 . ASN A 1 615 ? -11.896 -36.651 59.918 1.00 54.59 ? 650 ASN A OD1 1 ATOM 4774 N ND2 . ASN A 1 615 ? -12.882 -37.681 61.643 1.00 51.93 ? 650 ASN A ND2 1 ATOM 4775 N N . CYS A 1 616 ? -13.670 -39.986 56.221 1.00 39.72 ? 651 CYS A N 1 ATOM 4776 C CA . CYS A 1 616 ? -13.737 -41.163 55.371 1.00 41.18 ? 651 CYS A CA 1 ATOM 4777 C C . CYS A 1 616 ? -12.622 -41.147 54.333 1.00 36.52 ? 651 CYS A C 1 ATOM 4778 O O . CYS A 1 616 ? -12.451 -40.158 53.627 1.00 34.36 ? 651 CYS A O 1 ATOM 4779 C CB . CYS A 1 616 ? -15.094 -41.252 54.663 1.00 46.38 ? 651 CYS A CB 1 ATOM 4780 S SG . CYS A 1 616 ? -15.161 -42.493 53.347 1.00 51.07 ? 651 CYS A SG 1 ATOM 4781 N N . VAL A 1 617 ? -11.858 -42.237 54.264 1.00 33.76 ? 652 VAL A N 1 ATOM 4782 C CA . VAL A 1 617 ? -10.907 -42.435 53.165 1.00 33.44 ? 652 VAL A CA 1 ATOM 4783 C C . VAL A 1 617 ? -11.105 -43.854 52.666 1.00 34.35 ? 652 VAL A C 1 ATOM 4784 O O . VAL A 1 617 ? -11.137 -44.797 53.473 1.00 32.74 ? 652 VAL A O 1 ATOM 4785 C CB . VAL A 1 617 ? -9.441 -42.213 53.583 1.00 34.28 ? 652 VAL A CB 1 ATOM 4786 C CG1 . VAL A 1 617 ? -8.502 -42.516 52.415 1.00 33.86 ? 652 VAL A CG1 1 ATOM 4787 C CG2 . VAL A 1 617 ? -9.229 -40.783 54.088 1.00 32.73 ? 652 VAL A CG2 1 ATOM 4788 N N . ARG A 1 618 ? -11.237 -44.000 51.346 1.00 32.67 ? 653 ARG A N 1 ATOM 4789 C CA . ARG A 1 618 ? -11.586 -45.283 50.741 1.00 35.37 ? 653 ARG A CA 1 ATOM 4790 C C . ARG A 1 618 ? -10.462 -45.840 49.855 1.00 34.78 ? 653 ARG A C 1 ATOM 4791 O O . ARG A 1 618 ? -9.896 -45.095 49.064 1.00 32.62 ? 653 ARG A O 1 ATOM 4792 C CB . ARG A 1 618 ? -12.876 -45.127 49.922 1.00 36.41 ? 653 ARG A CB 1 ATOM 4793 C CG . ARG A 1 618 ? -14.047 -44.608 50.745 1.00 37.56 ? 653 ARG A CG 1 ATOM 4794 C CD . ARG A 1 618 ? -15.306 -44.359 49.930 1.00 38.75 ? 653 ARG A CD 1 ATOM 4795 N NE . ARG A 1 618 ? -15.684 -45.517 49.114 1.00 39.86 ? 653 ARG A NE 1 ATOM 4796 C CZ . ARG A 1 618 ? -15.709 -45.572 47.774 1.00 40.69 ? 653 ARG A CZ 1 ATOM 4797 N NH1 . ARG A 1 618 ? -15.389 -44.529 47.007 1.00 40.63 ? 653 ARG A NH1 1 ATOM 4798 N NH2 . ARG A 1 618 ? -16.084 -46.702 47.181 1.00 42.98 ? 653 ARG A NH2 1 ATOM 4799 N N . PRO A 1 619 ? -10.155 -47.158 49.956 1.00 36.37 ? 654 PRO A N 1 ATOM 4800 C CA . PRO A 1 619 ? -9.187 -47.754 49.016 1.00 37.06 ? 654 PRO A CA 1 ATOM 4801 C C . PRO A 1 619 ? -9.689 -47.689 47.575 1.00 36.43 ? 654 PRO A C 1 ATOM 4802 O O . PRO A 1 619 ? -10.895 -47.748 47.354 1.00 35.34 ? 654 PRO A O 1 ATOM 4803 C CB . PRO A 1 619 ? -9.075 -49.212 49.480 1.00 39.60 ? 654 PRO A CB 1 ATOM 4804 C CG . PRO A 1 619 ? -9.553 -49.197 50.881 1.00 41.42 ? 654 PRO A CG 1 ATOM 4805 C CD . PRO A 1 619 ? -10.621 -48.148 50.940 1.00 39.58 ? 654 PRO A CD 1 ATOM 4806 N N . ASP A 1 620 ? -8.768 -47.516 46.623 1.00 36.67 ? 655 ASP A N 1 ATOM 4807 C CA . ASP A 1 620 ? -9.092 -47.449 45.191 1.00 35.44 ? 655 ASP A CA 1 ATOM 4808 C C . ASP A 1 620 ? -8.721 -48.790 44.569 1.00 36.56 ? 655 ASP A C 1 ATOM 4809 O O . ASP A 1 620 ? -7.540 -49.094 44.371 1.00 36.06 ? 655 ASP A O 1 ATOM 4810 C CB . ASP A 1 620 ? -8.342 -46.296 44.501 1.00 33.65 ? 655 ASP A CB 1 ATOM 4811 C CG . ASP A 1 620 ? -8.827 -46.046 43.080 1.00 32.55 ? 655 ASP A CG 1 ATOM 4812 O OD1 . ASP A 1 620 ? -9.255 -47.002 42.390 1.00 32.34 ? 655 ASP A OD1 1 ATOM 4813 O OD2 . ASP A 1 620 ? -8.787 -44.879 42.636 1.00 31.23 ? 655 ASP A OD2 1 ATOM 4814 N N . VAL A 1 621 ? -9.745 -49.588 44.276 1.00 37.69 ? 656 VAL A N 1 ATOM 4815 C CA . VAL A 1 621 ? -9.544 -50.929 43.708 1.00 40.31 ? 656 VAL A CA 1 ATOM 4816 C C . VAL A 1 621 ? -8.892 -50.971 42.312 1.00 39.89 ? 656 VAL A C 1 ATOM 4817 O O . VAL A 1 621 ? -8.620 -52.054 41.814 1.00 41.24 ? 656 VAL A O 1 ATOM 4818 C CB . VAL A 1 621 ? -10.858 -51.756 43.694 1.00 41.81 ? 656 VAL A CB 1 ATOM 4819 C CG1 . VAL A 1 621 ? -11.381 -51.949 45.107 1.00 42.33 ? 656 VAL A CG1 1 ATOM 4820 C CG2 . VAL A 1 621 ? -11.933 -51.124 42.814 1.00 42.67 ? 656 VAL A CG2 1 ATOM 4821 N N . ARG A 1 622 ? -8.676 -49.821 41.670 1.00 36.59 ? 657 ARG A N 1 ATOM 4822 C CA . ARG A 1 622 ? -7.865 -49.759 40.455 1.00 36.23 ? 657 ARG A CA 1 ATOM 4823 C C . ARG A 1 622 ? -6.353 -49.675 40.693 1.00 37.53 ? 657 ARG A C 1 ATOM 4824 O O . ARG A 1 622 ? -5.580 -49.849 39.752 1.00 36.49 ? 657 ARG A O 1 ATOM 4825 C CB . ARG A 1 622 ? -8.259 -48.562 39.617 1.00 35.02 ? 657 ARG A CB 1 ATOM 4826 C CG . ARG A 1 622 ? -9.670 -48.576 39.095 1.00 34.47 ? 657 ARG A CG 1 ATOM 4827 C CD . ARG A 1 622 ? -10.050 -47.196 38.606 1.00 33.59 ? 657 ARG A CD 1 ATOM 4828 N NE . ARG A 1 622 ? -10.137 -46.259 39.727 1.00 31.67 ? 657 ARG A NE 1 ATOM 4829 C CZ . ARG A 1 622 ? -10.592 -45.018 39.642 1.00 29.54 ? 657 ARG A CZ 1 ATOM 4830 N NH1 . ARG A 1 622 ? -11.011 -44.511 38.484 1.00 28.42 ? 657 ARG A NH1 1 ATOM 4831 N NH2 . ARG A 1 622 ? -10.633 -44.282 40.743 1.00 27.66 ? 657 ARG A NH2 1 ATOM 4832 N N . VAL A 1 623 ? -5.935 -49.369 41.922 1.00 38.12 ? 658 VAL A N 1 ATOM 4833 C CA . VAL A 1 623 ? -4.539 -49.049 42.226 1.00 38.59 ? 658 VAL A CA 1 ATOM 4834 C C . VAL A 1 623 ? -4.092 -49.951 43.356 1.00 42.14 ? 658 VAL A C 1 ATOM 4835 O O . VAL A 1 623 ? -4.816 -50.089 44.348 1.00 41.83 ? 658 VAL A O 1 ATOM 4836 C CB . VAL A 1 623 ? -4.405 -47.557 42.644 1.00 37.99 ? 658 VAL A CB 1 ATOM 4837 C CG1 . VAL A 1 623 ? -2.985 -47.221 43.081 1.00 38.04 ? 658 VAL A CG1 1 ATOM 4838 C CG2 . VAL A 1 623 ? -4.847 -46.657 41.494 1.00 36.55 ? 658 VAL A CG2 1 ATOM 4839 N N . SER A 1 624 ? -2.901 -50.541 43.230 1.00 44.26 ? 659 SER A N 1 ATOM 4840 C CA . SER A 1 624 ? -2.454 -51.535 44.206 1.00 46.64 ? 659 SER A CA 1 ATOM 4841 C C . SER A 1 624 ? -2.253 -50.852 45.547 1.00 46.30 ? 659 SER A C 1 ATOM 4842 O O . SER A 1 624 ? -1.997 -49.639 45.582 1.00 44.93 ? 659 SER A O 1 ATOM 4843 C CB . SER A 1 624 ? -1.140 -52.206 43.797 1.00 49.35 ? 659 SER A CB 1 ATOM 4844 O OG . SER A 1 624 ? -0.029 -51.417 44.192 1.00 51.68 ? 659 SER A OG 1 ATOM 4845 N N . PRO A 1 625 ? -2.370 -51.620 46.647 1.00 43.59 ? 660 PRO A N 1 ATOM 4846 C CA . PRO A 1 625 ? -2.022 -51.145 47.984 1.00 43.64 ? 660 PRO A CA 1 ATOM 4847 C C . PRO A 1 625 ? -0.634 -50.527 48.076 1.00 42.08 ? 660 PRO A C 1 ATOM 4848 O O . PRO A 1 625 ? -0.475 -49.483 48.695 1.00 43.32 ? 660 PRO A O 1 ATOM 4849 C CB . PRO A 1 625 ? -2.080 -52.421 48.835 1.00 44.13 ? 660 PRO A CB 1 ATOM 4850 C CG . PRO A 1 625 ? -3.064 -53.277 48.146 1.00 45.62 ? 660 PRO A CG 1 ATOM 4851 C CD . PRO A 1 625 ? -2.963 -52.972 46.686 1.00 45.92 ? 660 PRO A CD 1 ATOM 4852 N N . GLY A 1 626 ? 0.349 -51.171 47.457 1.00 43.90 ? 661 GLY A N 1 ATOM 4853 C CA . GLY A 1 626 ? 1.730 -50.695 47.453 1.00 43.11 ? 661 GLY A CA 1 ATOM 4854 C C . GLY A 1 626 ? 1.980 -49.368 46.745 1.00 42.18 ? 661 GLY A C 1 ATOM 4855 O O . GLY A 1 626 ? 2.983 -48.715 47.027 1.00 41.79 ? 661 GLY A O 1 ATOM 4856 N N . PHE A 1 627 ? 1.093 -48.979 45.825 1.00 41.71 ? 662 PHE A N 1 ATOM 4857 C CA . PHE A 1 627 ? 1.178 -47.667 45.153 1.00 40.58 ? 662 PHE A CA 1 ATOM 4858 C C . PHE A 1 627 ? 0.123 -46.668 45.659 1.00 39.09 ? 662 PHE A C 1 ATOM 4859 O O . PHE A 1 627 ? -0.179 -45.690 44.974 1.00 36.27 ? 662 PHE A O 1 ATOM 4860 C CB . PHE A 1 627 ? 1.062 -47.831 43.626 1.00 43.10 ? 662 PHE A CB 1 ATOM 4861 C CG . PHE A 1 627 ? 2.235 -48.536 42.992 1.00 45.91 ? 662 PHE A CG 1 ATOM 4862 C CD1 . PHE A 1 627 ? 3.536 -48.073 43.190 1.00 46.58 ? 662 PHE A CD1 1 ATOM 4863 C CD2 . PHE A 1 627 ? 2.040 -49.644 42.169 1.00 50.14 ? 662 PHE A CD2 1 ATOM 4864 C CE1 . PHE A 1 627 ? 4.616 -48.716 42.601 1.00 49.20 ? 662 PHE A CE1 1 ATOM 4865 C CE2 . PHE A 1 627 ? 3.121 -50.290 41.574 1.00 50.68 ? 662 PHE A CE2 1 ATOM 4866 C CZ . PHE A 1 627 ? 4.409 -49.825 41.792 1.00 50.05 ? 662 PHE A CZ 1 ATOM 4867 N N . SER A 1 628 ? -0.398 -46.901 46.866 1.00 37.21 ? 663 SER A N 1 ATOM 4868 C CA . SER A 1 628 ? -1.406 -46.055 47.489 1.00 35.69 ? 663 SER A CA 1 ATOM 4869 C C . SER A 1 628 ? -0.821 -45.414 48.744 1.00 35.11 ? 663 SER A C 1 ATOM 4870 O O . SER A 1 628 ? 0.126 -45.949 49.326 1.00 37.75 ? 663 SER A O 1 ATOM 4871 C CB . SER A 1 628 ? -2.633 -46.911 47.842 1.00 37.40 ? 663 SER A CB 1 ATOM 4872 O OG . SER A 1 628 ? -3.224 -47.506 46.680 1.00 37.40 ? 663 SER A OG 1 ATOM 4873 N N . GLN A 1 629 ? -1.372 -44.273 49.167 1.00 32.48 ? 664 GLN A N 1 ATOM 4874 C CA . GLN A 1 629 ? -1.034 -43.673 50.473 1.00 32.60 ? 664 GLN A CA 1 ATOM 4875 C C . GLN A 1 629 ? -1.689 -44.485 51.574 1.00 35.43 ? 664 GLN A C 1 ATOM 4876 O O . GLN A 1 629 ? -2.595 -45.277 51.321 1.00 35.10 ? 664 GLN A O 1 ATOM 4877 C CB . GLN A 1 629 ? -1.549 -42.245 50.596 1.00 31.26 ? 664 GLN A CB 1 ATOM 4878 C CG . GLN A 1 629 ? -0.922 -41.273 49.607 1.00 30.19 ? 664 GLN A CG 1 ATOM 4879 C CD . GLN A 1 629 ? -1.509 -39.885 49.705 1.00 29.68 ? 664 GLN A CD 1 ATOM 4880 O OE1 . GLN A 1 629 ? -1.770 -39.396 50.789 1.00 30.93 ? 664 GLN A OE1 1 ATOM 4881 N NE2 . GLN A 1 629 ? -1.730 -39.253 48.568 1.00 27.99 ? 664 GLN A NE2 1 ATOM 4882 N N . ASN A 1 630 ? -1.258 -44.240 52.802 1.00 39.13 ? 665 ASN A N 1 ATOM 4883 C CA . ASN A 1 630 ? -1.870 -44.882 53.960 1.00 43.01 ? 665 ASN A CA 1 ATOM 4884 C C . ASN A 1 630 ? -2.271 -43.862 55.018 1.00 41.99 ? 665 ASN A C 1 ATOM 4885 O O . ASN A 1 630 ? -1.569 -42.875 55.259 1.00 40.80 ? 665 ASN A O 1 ATOM 4886 C CB . ASN A 1 630 ? -0.958 -45.981 54.502 1.00 44.73 ? 665 ASN A CB 1 ATOM 4887 C CG . ASN A 1 630 ? 0.164 -45.451 55.353 1.00 47.62 ? 665 ASN A CG 1 ATOM 4888 O OD1 . ASN A 1 630 ? 0.003 -45.268 56.564 1.00 49.80 ? 665 ASN A OD1 1 ATOM 4889 N ND2 . ASN A 1 630 ? 1.321 -45.242 54.744 1.00 48.20 ? 665 ASN A ND2 1 ATOM 4890 N N . CYS A 1 631 ? -3.421 -44.107 55.634 1.00 42.02 ? 666 CYS A N 1 ATOM 4891 C CA . CYS A 1 631 ? -3.985 -43.185 56.596 1.00 42.75 ? 666 CYS A CA 1 ATOM 4892 C C . CYS A 1 631 ? -3.235 -43.173 57.926 1.00 42.38 ? 666 CYS A C 1 ATOM 4893 O O . CYS A 1 631 ? -3.303 -42.182 58.662 1.00 40.61 ? 666 CYS A O 1 ATOM 4894 C CB . CYS A 1 631 ? -5.473 -43.473 56.780 1.00 45.95 ? 666 CYS A CB 1 ATOM 4895 S SG . CYS A 1 631 ? -6.368 -43.220 55.226 1.00 52.50 ? 666 CYS A SG 1 ATOM 4896 N N . LEU A 1 632 ? -2.504 -44.251 58.220 1.00 41.96 ? 667 LEU A N 1 ATOM 4897 C CA . LEU A 1 632 ? -1.722 -44.339 59.459 1.00 41.65 ? 667 LEU A CA 1 ATOM 4898 C C . LEU A 1 632 ? -0.556 -43.335 59.480 1.00 39.26 ? 667 LEU A C 1 ATOM 4899 O O . LEU A 1 632 ? -0.226 -42.797 60.533 1.00 38.91 ? 667 LEU A O 1 ATOM 4900 C CB . LEU A 1 632 ? -1.246 -45.782 59.686 1.00 43.58 ? 667 LEU A CB 1 ATOM 4901 C CG . LEU A 1 632 ? -0.434 -46.117 60.941 1.00 44.95 ? 667 LEU A CG 1 ATOM 4902 C CD1 . LEU A 1 632 ? -1.146 -45.682 62.219 1.00 45.16 ? 667 LEU A CD1 1 ATOM 4903 C CD2 . LEU A 1 632 ? -0.133 -47.608 60.975 1.00 46.48 ? 667 LEU A CD2 1 ATOM 4904 N N . ALA A 1 633 ? 0.040 -43.059 58.319 1.00 36.92 ? 668 ALA A N 1 ATOM 4905 C CA . ALA A 1 633 ? 1.085 -42.035 58.212 1.00 36.46 ? 668 ALA A CA 1 ATOM 4906 C C . ALA A 1 633 ? 0.557 -40.691 58.693 1.00 34.15 ? 668 ALA A C 1 ATOM 4907 O O . ALA A 1 633 ? 1.213 -40.004 59.464 1.00 36.29 ? 668 ALA A O 1 ATOM 4908 C CB . ALA A 1 633 ? 1.591 -41.910 56.777 1.00 36.60 ? 668 ALA A CB 1 ATOM 4909 N N . TYR A 1 634 ? -0.646 -40.341 58.262 1.00 32.23 ? 669 TYR A N 1 ATOM 4910 C CA . TYR A 1 634 ? -1.268 -39.097 58.685 1.00 32.02 ? 669 TYR A CA 1 ATOM 4911 C C . TYR A 1 634 ? -1.595 -39.097 60.180 1.00 34.02 ? 669 TYR A C 1 ATOM 4912 O O . TYR A 1 634 ? -1.420 -38.081 60.845 1.00 33.97 ? 669 TYR A O 1 ATOM 4913 C CB . TYR A 1 634 ? -2.516 -38.813 57.853 1.00 31.09 ? 669 TYR A CB 1 ATOM 4914 C CG . TYR A 1 634 ? -2.186 -38.476 56.426 1.00 29.25 ? 669 TYR A CG 1 ATOM 4915 C CD1 . TYR A 1 634 ? -1.640 -37.243 56.103 1.00 27.96 ? 669 TYR A CD1 1 ATOM 4916 C CD2 . TYR A 1 634 ? -2.405 -39.398 55.398 1.00 29.14 ? 669 TYR A CD2 1 ATOM 4917 C CE1 . TYR A 1 634 ? -1.327 -36.916 54.792 1.00 28.66 ? 669 TYR A CE1 1 ATOM 4918 C CE2 . TYR A 1 634 ? -2.105 -39.086 54.081 1.00 29.74 ? 669 TYR A CE2 1 ATOM 4919 C CZ . TYR A 1 634 ? -1.558 -37.837 53.778 1.00 29.92 ? 669 TYR A CZ 1 ATOM 4920 O OH . TYR A 1 634 ? -1.246 -37.512 52.473 1.00 27.99 ? 669 TYR A OH 1 ATOM 4921 N N . LYS A 1 635 ? -2.082 -40.212 60.710 1.00 38.44 ? 670 LYS A N 1 ATOM 4922 C CA . LYS A 1 635 ? -2.282 -40.324 62.170 1.00 39.75 ? 670 LYS A CA 1 ATOM 4923 C C . LYS A 1 635 ? -0.999 -40.061 62.959 1.00 39.40 ? 670 LYS A C 1 ATOM 4924 O O . LYS A 1 635 ? -1.015 -39.356 63.970 1.00 41.04 ? 670 LYS A O 1 ATOM 4925 C CB . LYS A 1 635 ? -2.826 -41.710 62.560 1.00 45.49 ? 670 LYS A CB 1 ATOM 4926 C CG . LYS A 1 635 ? -4.332 -41.787 62.747 1.00 50.51 ? 670 LYS A CG 1 ATOM 4927 C CD . LYS A 1 635 ? -5.093 -41.980 61.442 1.00 53.83 ? 670 LYS A CD 1 ATOM 4928 C CE . LYS A 1 635 ? -6.461 -42.621 61.680 1.00 58.25 ? 670 LYS A CE 1 ATOM 4929 N NZ . LYS A 1 635 ? -7.053 -43.191 60.436 1.00 61.81 ? 670 LYS A NZ 1 ATOM 4930 N N . ASN A 1 636 ? 0.102 -40.643 62.508 1.00 39.25 ? 671 ASN A N 1 ATOM 4931 C CA . ASN A 1 636 ? 1.381 -40.546 63.226 1.00 40.83 ? 671 ASN A CA 1 ATOM 4932 C C . ASN A 1 636 ? 2.096 -39.219 63.018 1.00 40.37 ? 671 ASN A C 1 ATOM 4933 O O . ASN A 1 636 ? 2.886 -38.806 63.862 1.00 40.36 ? 671 ASN A O 1 ATOM 4934 C CB . ASN A 1 636 ? 2.309 -41.689 62.810 1.00 42.68 ? 671 ASN A CB 1 ATOM 4935 C CG . ASN A 1 636 ? 1.724 -43.061 63.123 1.00 43.81 ? 671 ASN A CG 1 ATOM 4936 O OD1 . ASN A 1 636 ? 0.862 -43.202 63.994 1.00 43.82 ? 671 ASN A OD1 1 ATOM 4937 N ND2 . ASN A 1 636 ? 2.171 -44.073 62.391 1.00 44.92 ? 671 ASN A ND2 1 ATOM 4938 N N . ASP A 1 637 ? 1.852 -38.569 61.881 1.00 37.36 ? 672 ASP A N 1 ATOM 4939 C CA . ASP A 1 637 ? 2.386 -37.230 61.639 1.00 35.79 ? 672 ASP A CA 1 ATOM 4940 C C . ASP A 1 637 ? 1.499 -36.218 62.341 1.00 35.13 ? 672 ASP A C 1 ATOM 4941 O O . ASP A 1 637 ? 0.403 -35.904 61.850 1.00 34.92 ? 672 ASP A O 1 ATOM 4942 C CB . ASP A 1 637 ? 2.461 -36.910 60.142 1.00 34.42 ? 672 ASP A CB 1 ATOM 4943 C CG . ASP A 1 637 ? 3.360 -35.724 59.849 1.00 33.68 ? 672 ASP A CG 1 ATOM 4944 O OD1 . ASP A 1 637 ? 3.315 -34.733 60.616 1.00 32.89 ? 672 ASP A OD1 1 ATOM 4945 O OD2 . ASP A 1 637 ? 4.110 -35.775 58.849 1.00 32.67 ? 672 ASP A OD2 1 ATOM 4946 N N . LYS A 1 638 ? 1.982 -35.695 63.468 1.00 36.17 ? 673 LYS A N 1 ATOM 4947 C CA . LYS A 1 638 ? 1.217 -34.768 64.305 1.00 36.48 ? 673 LYS A CA 1 ATOM 4948 C C . LYS A 1 638 ? 1.096 -33.368 63.717 1.00 34.89 ? 673 LYS A C 1 ATOM 4949 O O . LYS A 1 638 ? 0.249 -32.596 64.159 1.00 34.41 ? 673 LYS A O 1 ATOM 4950 C CB . LYS A 1 638 ? 1.835 -34.672 65.717 1.00 38.72 ? 673 LYS A CB 1 ATOM 4951 C CG . LYS A 1 638 ? 1.941 -35.992 66.489 1.00 41.41 ? 673 LYS A CG 1 ATOM 4952 C CD . LYS A 1 638 ? 0.655 -36.802 66.430 1.00 43.34 ? 673 LYS A CD 1 ATOM 4953 C CE . LYS A 1 638 ? 0.736 -38.075 67.266 1.00 47.82 ? 673 LYS A CE 1 ATOM 4954 N NZ . LYS A 1 638 ? -0.228 -39.104 66.771 1.00 49.29 ? 673 LYS A NZ 1 ATOM 4955 N N . GLN A 1 639 ? 1.931 -33.041 62.727 1.00 33.34 ? 674 GLN A N 1 ATOM 4956 C CA . GLN A 1 639 ? 1.880 -31.745 62.054 1.00 32.15 ? 674 GLN A CA 1 ATOM 4957 C C . GLN A 1 639 ? 1.101 -31.780 60.745 1.00 28.91 ? 674 GLN A C 1 ATOM 4958 O O . GLN A 1 639 ? 0.769 -30.722 60.235 1.00 27.83 ? 674 GLN A O 1 ATOM 4959 C CB . GLN A 1 639 ? 3.298 -31.221 61.782 1.00 34.55 ? 674 GLN A CB 1 ATOM 4960 C CG . GLN A 1 639 ? 4.026 -30.702 63.017 1.00 40.11 ? 674 GLN A CG 1 ATOM 4961 C CD . GLN A 1 639 ? 4.295 -31.792 64.038 1.00 47.86 ? 674 GLN A CD 1 ATOM 4962 O OE1 . GLN A 1 639 ? 4.829 -32.852 63.697 1.00 57.56 ? 674 GLN A OE1 1 ATOM 4963 N NE2 . GLN A 1 639 ? 3.918 -31.550 65.297 1.00 50.18 ? 674 GLN A NE2 1 ATOM 4964 N N . MET A 1 640 ? 0.818 -32.964 60.197 1.00 27.46 ? 675 MET A N 1 ATOM 4965 C CA . MET A 1 640 ? 0.274 -33.078 58.830 1.00 26.07 ? 675 MET A CA 1 ATOM 4966 C C . MET A 1 640 ? -1.132 -33.663 58.795 1.00 25.87 ? 675 MET A C 1 ATOM 4967 O O . MET A 1 640 ? -1.412 -34.656 59.477 1.00 26.61 ? 675 MET A O 1 ATOM 4968 C CB . MET A 1 640 ? 1.228 -33.928 57.976 1.00 26.49 ? 675 MET A CB 1 ATOM 4969 C CG . MET A 1 640 ? 0.931 -33.925 56.484 1.00 26.64 ? 675 MET A CG 1 ATOM 4970 S SD . MET A 1 640 ? 1.002 -32.300 55.708 1.00 26.30 ? 675 MET A SD 1 ATOM 4971 C CE . MET A 1 640 ? 2.737 -31.953 55.862 1.00 26.73 ? 675 MET A CE 1 ATOM 4972 N N . SER A 1 641 ? -2.029 -33.045 58.031 1.00 24.00 ? 676 SER A N 1 ATOM 4973 C CA . SER A 1 641 ? -3.345 -33.603 57.759 1.00 24.14 ? 676 SER A CA 1 ATOM 4974 C C . SER A 1 641 ? -3.428 -33.902 56.265 1.00 24.13 ? 676 SER A C 1 ATOM 4975 O O . SER A 1 641 ? -2.396 -34.088 55.630 1.00 23.40 ? 676 SER A O 1 ATOM 4976 C CB . SER A 1 641 ? -4.432 -32.640 58.244 1.00 24.60 ? 676 SER A CB 1 ATOM 4977 O OG . SER A 1 641 ? -5.705 -33.232 58.121 1.00 25.27 ? 676 SER A OG 1 ATOM 4978 N N . TYR A 1 642 ? -4.636 -33.995 55.713 1.00 24.92 ? 677 TYR A N 1 ATOM 4979 C CA . TYR A 1 642 ? -4.814 -34.250 54.295 1.00 24.31 ? 677 TYR A CA 1 ATOM 4980 C C . TYR A 1 642 ? -6.017 -33.505 53.753 1.00 24.08 ? 677 TYR A C 1 ATOM 4981 O O . TYR A 1 642 ? -6.947 -33.175 54.505 1.00 24.17 ? 677 TYR A O 1 ATOM 4982 C CB . TYR A 1 642 ? -4.948 -35.759 54.017 1.00 26.32 ? 677 TYR A CB 1 ATOM 4983 C CG . TYR A 1 642 ? -6.197 -36.380 54.611 1.00 26.94 ? 677 TYR A CG 1 ATOM 4984 C CD1 . TYR A 1 642 ? -6.198 -36.867 55.917 1.00 28.71 ? 677 TYR A CD1 1 ATOM 4985 C CD2 . TYR A 1 642 ? -7.388 -36.452 53.873 1.00 27.06 ? 677 TYR A CD2 1 ATOM 4986 C CE1 . TYR A 1 642 ? -7.345 -37.432 56.467 1.00 30.51 ? 677 TYR A CE1 1 ATOM 4987 C CE2 . TYR A 1 642 ? -8.542 -37.005 54.423 1.00 29.02 ? 677 TYR A CE2 1 ATOM 4988 C CZ . TYR A 1 642 ? -8.506 -37.497 55.716 1.00 30.36 ? 677 TYR A CZ 1 ATOM 4989 O OH . TYR A 1 642 ? -9.640 -38.040 56.267 1.00 31.86 ? 677 TYR A OH 1 ATOM 4990 N N . GLY A 1 643 ? -5.972 -33.231 52.445 1.00 22.33 ? 678 GLY A N 1 ATOM 4991 C CA . GLY A 1 643 ? -7.075 -32.642 51.712 1.00 20.91 ? 678 GLY A CA 1 ATOM 4992 C C . GLY A 1 643 ? -7.353 -33.484 50.495 1.00 20.65 ? 678 GLY A C 1 ATOM 4993 O O . GLY A 1 643 ? -6.720 -34.526 50.307 1.00 20.57 ? 678 GLY A O 1 ATOM 4994 N N . PHE A 1 644 ? -8.297 -33.022 49.677 1.00 20.51 ? 679 PHE A N 1 ATOM 4995 C CA . PHE A 1 644 ? -8.678 -33.675 48.421 1.00 21.40 ? 679 PHE A CA 1 ATOM 4996 C C . PHE A 1 644 ? -8.496 -32.724 47.241 1.00 20.67 ? 679 PHE A C 1 ATOM 4997 O O . PHE A 1 644 ? -8.741 -31.520 47.377 1.00 19.26 ? 679 PHE A O 1 ATOM 4998 C CB . PHE A 1 644 ? -10.131 -34.140 48.498 1.00 22.73 ? 679 PHE A CB 1 ATOM 4999 C CG . PHE A 1 644 ? -10.349 -35.227 49.521 1.00 24.10 ? 679 PHE A CG 1 ATOM 5000 C CD1 . PHE A 1 644 ? -9.848 -36.505 49.316 1.00 25.46 ? 679 PHE A CD1 1 ATOM 5001 C CD2 . PHE A 1 644 ? -11.012 -34.962 50.695 1.00 26.34 ? 679 PHE A CD2 1 ATOM 5002 C CE1 . PHE A 1 644 ? -10.040 -37.509 50.252 1.00 28.77 ? 679 PHE A CE1 1 ATOM 5003 C CE2 . PHE A 1 644 ? -11.191 -35.942 51.643 1.00 28.44 ? 679 PHE A CE2 1 ATOM 5004 C CZ . PHE A 1 644 ? -10.712 -37.229 51.422 1.00 29.80 ? 679 PHE A CZ 1 ATOM 5005 N N . LEU A 1 645 ? -8.099 -33.264 46.085 1.00 20.00 ? 680 LEU A N 1 ATOM 5006 C CA . LEU A 1 645 ? -7.923 -32.432 44.888 1.00 20.18 ? 680 LEU A CA 1 ATOM 5007 C C . LEU A 1 645 ? -9.245 -32.158 44.176 1.00 21.78 ? 680 LEU A C 1 ATOM 5008 O O . LEU A 1 645 ? -9.564 -30.999 43.905 1.00 20.49 ? 680 LEU A O 1 ATOM 5009 C CB . LEU A 1 645 ? -6.880 -33.001 43.932 1.00 19.95 ? 680 LEU A CB 1 ATOM 5010 C CG . LEU A 1 645 ? -5.442 -32.924 44.426 1.00 20.37 ? 680 LEU A CG 1 ATOM 5011 C CD1 . LEU A 1 645 ? -4.547 -33.715 43.496 1.00 21.20 ? 680 LEU A CD1 1 ATOM 5012 C CD2 . LEU A 1 645 ? -4.952 -31.482 44.480 1.00 20.50 ? 680 LEU A CD2 1 ATOM 5013 N N . PHE A 1 646 ? -10.041 -33.184 43.897 1.00 21.69 ? 681 PHE A N 1 ATOM 5014 C CA . PHE A 1 646 ? -11.438 -32.916 43.573 1.00 22.43 ? 681 PHE A CA 1 ATOM 5015 C C . PHE A 1 646 ? -12.217 -32.706 44.876 1.00 23.88 ? 681 PHE A C 1 ATOM 5016 O O . PHE A 1 646 ? -12.216 -33.607 45.735 1.00 24.56 ? 681 PHE A O 1 ATOM 5017 C CB . PHE A 1 646 ? -12.119 -34.028 42.776 1.00 22.45 ? 681 PHE A CB 1 ATOM 5018 C CG . PHE A 1 646 ? -13.562 -33.725 42.520 1.00 22.97 ? 681 PHE A CG 1 ATOM 5019 C CD1 . PHE A 1 646 ? -13.925 -32.806 41.539 1.00 21.89 ? 681 PHE A CD1 1 ATOM 5020 C CD2 . PHE A 1 646 ? -14.552 -34.284 43.307 1.00 24.49 ? 681 PHE A CD2 1 ATOM 5021 C CE1 . PHE A 1 646 ? -15.245 -32.447 41.349 1.00 21.73 ? 681 PHE A CE1 1 ATOM 5022 C CE2 . PHE A 1 646 ? -15.885 -33.950 43.109 1.00 24.05 ? 681 PHE A CE2 1 ATOM 5023 C CZ . PHE A 1 646 ? -16.227 -33.021 42.140 1.00 23.38 ? 681 PHE A CZ 1 ATOM 5024 N N . PRO A 1 647 ? -12.920 -31.559 44.999 1.00 24.34 ? 682 PRO A N 1 ATOM 5025 C CA . PRO A 1 647 ? -13.631 -31.284 46.240 1.00 26.74 ? 682 PRO A CA 1 ATOM 5026 C C . PRO A 1 647 ? -14.933 -32.082 46.427 1.00 27.35 ? 682 PRO A C 1 ATOM 5027 O O . PRO A 1 647 ? -15.814 -31.966 45.577 1.00 26.61 ? 682 PRO A O 1 ATOM 5028 C CB . PRO A 1 647 ? -13.995 -29.814 46.109 1.00 25.28 ? 682 PRO A CB 1 ATOM 5029 C CG . PRO A 1 647 ? -14.016 -29.505 44.678 1.00 27.14 ? 682 PRO A CG 1 ATOM 5030 C CD . PRO A 1 647 ? -13.103 -30.487 43.998 1.00 26.20 ? 682 PRO A CD 1 ATOM 5031 N N . PRO A 1 648 ? -15.076 -32.831 47.545 1.00 30.28 ? 683 PRO A N 1 ATOM 5032 C CA . PRO A 1 648 ? -16.351 -33.506 47.813 1.00 31.35 ? 683 PRO A CA 1 ATOM 5033 C C . PRO A 1 648 ? -17.562 -32.558 47.824 1.00 30.19 ? 683 PRO A C 1 ATOM 5034 O O . PRO A 1 648 ? -18.659 -33.000 47.541 1.00 29.66 ? 683 PRO A O 1 ATOM 5035 C CB . PRO A 1 648 ? -16.140 -34.126 49.202 1.00 34.27 ? 683 PRO A CB 1 ATOM 5036 C CG . PRO A 1 648 ? -14.661 -34.252 49.353 1.00 33.17 ? 683 PRO A CG 1 ATOM 5037 C CD . PRO A 1 648 ? -14.081 -33.110 48.600 1.00 32.04 ? 683 PRO A CD 1 ATOM 5038 N N . TYR A 1 649 ? -17.338 -31.278 48.138 1.00 27.98 ? 684 TYR A N 1 ATOM 5039 C CA . TYR A 1 649 ? -18.388 -30.251 48.151 1.00 28.92 ? 684 TYR A CA 1 ATOM 5040 C C . TYR A 1 649 ? -19.068 -30.027 46.815 1.00 27.61 ? 684 TYR A C 1 ATOM 5041 O O . TYR A 1 649 ? -20.193 -29.533 46.797 1.00 27.64 ? 684 TYR A O 1 ATOM 5042 C CB . TYR A 1 649 ? -17.859 -28.870 48.610 1.00 30.54 ? 684 TYR A CB 1 ATOM 5043 C CG . TYR A 1 649 ? -17.032 -28.883 49.869 1.00 34.11 ? 684 TYR A CG 1 ATOM 5044 C CD1 . TYR A 1 649 ? -17.631 -29.032 51.112 1.00 37.84 ? 684 TYR A CD1 1 ATOM 5045 C CD2 . TYR A 1 649 ? -15.637 -28.721 49.823 1.00 36.47 ? 684 TYR A CD2 1 ATOM 5046 C CE1 . TYR A 1 649 ? -16.874 -29.036 52.278 1.00 40.19 ? 684 TYR A CE1 1 ATOM 5047 C CE2 . TYR A 1 649 ? -14.869 -28.741 50.981 1.00 39.66 ? 684 TYR A CE2 1 ATOM 5048 C CZ . TYR A 1 649 ? -15.491 -28.890 52.202 1.00 40.72 ? 684 TYR A CZ 1 ATOM 5049 O OH . TYR A 1 649 ? -14.746 -28.896 53.356 1.00 43.23 ? 684 TYR A OH 1 ATOM 5050 N N . LEU A 1 650 ? -18.377 -30.319 45.709 1.00 26.07 ? 685 LEU A N 1 ATOM 5051 C CA . LEU A 1 650 ? -18.934 -30.109 44.383 1.00 27.12 ? 685 LEU A CA 1 ATOM 5052 C C . LEU A 1 650 ? -19.367 -31.389 43.673 1.00 26.87 ? 685 LEU A C 1 ATOM 5053 O O . LEU A 1 650 ? -19.584 -31.360 42.467 1.00 27.98 ? 685 LEU A O 1 ATOM 5054 C CB . LEU A 1 650 ? -17.954 -29.314 43.506 1.00 27.74 ? 685 LEU A CB 1 ATOM 5055 C CG . LEU A 1 650 ? -17.545 -27.954 44.091 1.00 28.31 ? 685 LEU A CG 1 ATOM 5056 C CD1 . LEU A 1 650 ? -16.507 -27.246 43.233 1.00 28.06 ? 685 LEU A CD1 1 ATOM 5057 C CD2 . LEU A 1 650 ? -18.755 -27.068 44.252 1.00 29.20 ? 685 LEU A CD2 1 ATOM 5058 N N . SER A 1 651 ? -19.526 -32.484 44.414 1.00 25.71 ? 686 SER A N 1 ATOM 5059 C CA . SER A 1 651 ? -20.065 -33.741 43.855 1.00 27.16 ? 686 SER A CA 1 ATOM 5060 C C . SER A 1 651 ? -21.426 -33.525 43.194 1.00 27.98 ? 686 SER A C 1 ATOM 5061 O O . SER A 1 651 ? -22.217 -32.705 43.654 1.00 28.86 ? 686 SER A O 1 ATOM 5062 C CB . SER A 1 651 ? -20.222 -34.790 44.946 1.00 28.68 ? 686 SER A CB 1 ATOM 5063 O OG . SER A 1 651 ? -21.104 -34.284 45.944 1.00 29.17 ? 686 SER A OG 1 ATOM 5064 N N . SER A 1 652 ? -21.689 -34.282 42.131 1.00 28.38 ? 687 SER A N 1 ATOM 5065 C CA . SER A 1 652 ? -22.919 -34.169 41.344 1.00 29.31 ? 687 SER A CA 1 ATOM 5066 C C . SER A 1 652 ? -24.086 -34.933 41.973 1.00 30.50 ? 687 SER A C 1 ATOM 5067 O O . SER A 1 652 ? -25.233 -34.671 41.634 1.00 30.79 ? 687 SER A O 1 ATOM 5068 C CB . SER A 1 652 ? -22.701 -34.677 39.917 1.00 30.23 ? 687 SER A CB 1 ATOM 5069 O OG . SER A 1 652 ? -22.197 -36.002 39.911 1.00 31.31 ? 687 SER A OG 1 ATOM 5070 N N . SER A 1 653 ? -23.785 -35.875 42.864 1.00 30.49 ? 688 SER A N 1 ATOM 5071 C CA . SER A 1 653 ? -24.806 -36.647 43.565 1.00 32.71 ? 688 SER A CA 1 ATOM 5072 C C . SER A 1 653 ? -24.220 -37.256 44.832 1.00 32.98 ? 688 SER A C 1 ATOM 5073 O O . SER A 1 653 ? -23.004 -37.368 44.950 1.00 30.68 ? 688 SER A O 1 ATOM 5074 C CB . SER A 1 653 ? -25.321 -37.772 42.675 1.00 33.57 ? 688 SER A CB 1 ATOM 5075 O OG . SER A 1 653 ? -24.303 -38.733 42.442 1.00 32.90 ? 688 SER A OG 1 ATOM 5076 N N . PRO A 1 654 ? -25.080 -37.675 45.780 1.00 35.85 ? 689 PRO A N 1 ATOM 5077 C CA . PRO A 1 654 ? -24.564 -38.410 46.951 1.00 36.70 ? 689 PRO A CA 1 ATOM 5078 C C . PRO A 1 654 ? -23.782 -39.669 46.560 1.00 37.76 ? 689 PRO A C 1 ATOM 5079 O O . PRO A 1 654 ? -22.768 -39.986 47.188 1.00 39.05 ? 689 PRO A O 1 ATOM 5080 C CB . PRO A 1 654 ? -25.833 -38.765 47.726 1.00 38.40 ? 689 PRO A CB 1 ATOM 5081 C CG . PRO A 1 654 ? -26.831 -37.745 47.304 1.00 38.00 ? 689 PRO A CG 1 ATOM 5082 C CD . PRO A 1 654 ? -26.541 -37.479 45.865 1.00 37.11 ? 689 PRO A CD 1 ATOM 5083 N N . GLU A 1 655 ? -24.236 -40.340 45.503 1.00 37.49 ? 690 GLU A N 1 ATOM 5084 C CA . GLU A 1 655 ? -23.537 -41.497 44.927 1.00 38.62 ? 690 GLU A CA 1 ATOM 5085 C C . GLU A 1 655 ? -22.125 -41.123 44.487 1.00 35.97 ? 690 GLU A C 1 ATOM 5086 O O . GLU A 1 655 ? -21.141 -41.728 44.916 1.00 34.65 ? 690 GLU A O 1 ATOM 5087 C CB . GLU A 1 655 ? -24.306 -42.058 43.717 1.00 41.03 ? 690 GLU A CB 1 ATOM 5088 C CG . GLU A 1 655 ? -25.624 -42.752 44.051 1.00 45.38 ? 690 GLU A CG 1 ATOM 5089 C CD . GLU A 1 655 ? -26.820 -41.812 44.208 1.00 48.04 ? 690 GLU A CD 1 ATOM 5090 O OE1 . GLU A 1 655 ? -26.688 -40.589 43.975 1.00 46.48 ? 690 GLU A OE1 1 ATOM 5091 O OE2 . GLU A 1 655 ? -27.914 -42.303 44.567 1.00 50.64 ? 690 GLU A OE2 1 ATOM 5092 N N . ALA A 1 656 ? -22.040 -40.105 43.637 1.00 33.94 ? 691 ALA A N 1 ATOM 5093 C CA . ALA A 1 656 ? -20.762 -39.654 43.109 1.00 32.63 ? 691 ALA A CA 1 ATOM 5094 C C . ALA A 1 656 ? -19.836 -39.088 44.208 1.00 31.98 ? 691 ALA A C 1 ATOM 5095 O O . ALA A 1 656 ? -18.625 -39.186 44.079 1.00 31.03 ? 691 ALA A O 1 ATOM 5096 C CB . ALA A 1 656 ? -20.971 -38.635 41.989 1.00 31.65 ? 691 ALA A CB 1 ATOM 5097 N N . LYS A 1 657 ? -20.392 -38.534 45.289 1.00 31.32 ? 692 LYS A N 1 ATOM 5098 C CA . LYS A 1 657 ? -19.555 -37.966 46.364 1.00 32.05 ? 692 LYS A CA 1 ATOM 5099 C C . LYS A 1 657 ? -18.570 -38.979 46.973 1.00 31.69 ? 692 LYS A C 1 ATOM 5100 O O . LYS A 1 657 ? -17.468 -38.596 47.380 1.00 28.93 ? 692 LYS A O 1 ATOM 5101 C CB . LYS A 1 657 ? -20.409 -37.313 47.461 1.00 33.22 ? 692 LYS A CB 1 ATOM 5102 C CG . LYS A 1 657 ? -19.655 -36.315 48.336 1.00 33.63 ? 692 LYS A CG 1 ATOM 5103 C CD . LYS A 1 657 ? -20.454 -35.889 49.564 1.00 36.09 ? 692 LYS A CD 1 ATOM 5104 C CE . LYS A 1 657 ? -21.551 -34.883 49.244 1.00 37.16 ? 692 LYS A CE 1 ATOM 5105 N NZ . LYS A 1 657 ? -21.017 -33.495 49.168 1.00 39.43 ? 692 LYS A NZ 1 ATOM 5106 N N . TYR A 1 658 ? -18.947 -40.259 46.993 1.00 32.58 ? 693 TYR A N 1 ATOM 5107 C CA . TYR A 1 658 ? -18.062 -41.331 47.472 1.00 33.86 ? 693 TYR A CA 1 ATOM 5108 C C . TYR A 1 658 ? -16.713 -41.407 46.756 1.00 32.14 ? 693 TYR A C 1 ATOM 5109 O O . TYR A 1 658 ? -15.721 -41.767 47.375 1.00 31.26 ? 693 TYR A O 1 ATOM 5110 C CB . TYR A 1 658 ? -18.774 -42.701 47.439 1.00 37.48 ? 693 TYR A CB 1 ATOM 5111 C CG . TYR A 1 658 ? -19.666 -42.907 48.653 1.00 40.12 ? 693 TYR A CG 1 ATOM 5112 C CD1 . TYR A 1 658 ? -20.977 -42.424 48.671 1.00 41.05 ? 693 TYR A CD1 1 ATOM 5113 C CD2 . TYR A 1 658 ? -19.180 -43.534 49.802 1.00 42.20 ? 693 TYR A CD2 1 ATOM 5114 C CE1 . TYR A 1 658 ? -21.786 -42.579 49.788 1.00 44.23 ? 693 TYR A CE1 1 ATOM 5115 C CE2 . TYR A 1 658 ? -19.980 -43.697 50.929 1.00 44.30 ? 693 TYR A CE2 1 ATOM 5116 C CZ . TYR A 1 658 ? -21.283 -43.218 50.921 1.00 45.40 ? 693 TYR A CZ 1 ATOM 5117 O OH . TYR A 1 658 ? -22.081 -43.371 52.033 1.00 46.08 ? 693 TYR A OH 1 ATOM 5118 N N . ASP A 1 659 ? -16.691 -41.076 45.461 1.00 32.25 ? 694 ASP A N 1 ATOM 5119 C CA . ASP A 1 659 ? -15.453 -41.056 44.657 1.00 31.97 ? 694 ASP A CA 1 ATOM 5120 C C . ASP A 1 659 ? -14.438 -40.040 45.174 1.00 29.16 ? 694 ASP A C 1 ATOM 5121 O O . ASP A 1 659 ? -13.222 -40.233 45.058 1.00 29.01 ? 694 ASP A O 1 ATOM 5122 C CB . ASP A 1 659 ? -15.743 -40.684 43.192 1.00 32.93 ? 694 ASP A CB 1 ATOM 5123 C CG . ASP A 1 659 ? -16.471 -41.772 42.417 1.00 37.36 ? 694 ASP A CG 1 ATOM 5124 O OD1 . ASP A 1 659 ? -16.446 -42.954 42.823 1.00 39.71 ? 694 ASP A OD1 1 ATOM 5125 O OD2 . ASP A 1 659 ? -17.062 -41.429 41.363 1.00 37.69 ? 694 ASP A OD2 1 ATOM 5126 N N . ALA A 1 660 ? -14.938 -38.933 45.700 1.00 28.04 ? 695 ALA A N 1 ATOM 5127 C CA . ALA A 1 660 ? -14.075 -37.886 46.180 1.00 26.14 ? 695 ALA A CA 1 ATOM 5128 C C . ALA A 1 660 ? -13.293 -38.280 47.445 1.00 26.50 ? 695 ALA A C 1 ATOM 5129 O O . ALA A 1 660 ? -12.277 -37.666 47.739 1.00 25.43 ? 695 ALA A O 1 ATOM 5130 C CB . ALA A 1 660 ? -14.869 -36.607 46.391 1.00 26.17 ? 695 ALA A CB 1 ATOM 5131 N N . PHE A 1 661 ? -13.749 -39.305 48.174 1.00 27.37 ? 696 PHE A N 1 ATOM 5132 C CA . PHE A 1 661 ? -13.025 -39.828 49.342 1.00 28.34 ? 696 PHE A CA 1 ATOM 5133 C C . PHE A 1 661 ? -12.063 -40.983 49.036 1.00 28.64 ? 696 PHE A C 1 ATOM 5134 O O . PHE A 1 661 ? -11.507 -41.600 49.956 1.00 28.76 ? 696 PHE A O 1 ATOM 5135 C CB . PHE A 1 661 ? -14.035 -40.205 50.437 1.00 30.37 ? 696 PHE A CB 1 ATOM 5136 C CG . PHE A 1 661 ? -14.871 -39.044 50.881 1.00 31.95 ? 696 PHE A CG 1 ATOM 5137 C CD1 . PHE A 1 661 ? -14.359 -38.105 51.760 1.00 32.87 ? 696 PHE A CD1 1 ATOM 5138 C CD2 . PHE A 1 661 ? -16.163 -38.869 50.393 1.00 34.91 ? 696 PHE A CD2 1 ATOM 5139 C CE1 . PHE A 1 661 ? -15.129 -37.020 52.165 1.00 34.33 ? 696 PHE A CE1 1 ATOM 5140 C CE2 . PHE A 1 661 ? -16.935 -37.784 50.788 1.00 35.21 ? 696 PHE A CE2 1 ATOM 5141 C CZ . PHE A 1 661 ? -16.417 -36.859 51.671 1.00 34.66 ? 696 PHE A CZ 1 ATOM 5142 N N . LEU A 1 662 ? -11.827 -41.264 47.749 1.00 27.78 ? 697 LEU A N 1 ATOM 5143 C CA . LEU A 1 662 ? -10.817 -42.254 47.384 1.00 28.17 ? 697 LEU A CA 1 ATOM 5144 C C . LEU A 1 662 ? -9.412 -41.785 47.783 1.00 27.00 ? 697 LEU A C 1 ATOM 5145 O O . LEU A 1 662 ? -9.079 -40.586 47.679 1.00 25.10 ? 697 LEU A O 1 ATOM 5146 C CB . LEU A 1 662 ? -10.851 -42.550 45.881 1.00 28.81 ? 697 LEU A CB 1 ATOM 5147 C CG . LEU A 1 662 ? -12.093 -43.263 45.339 1.00 30.09 ? 697 LEU A CG 1 ATOM 5148 C CD1 . LEU A 1 662 ? -12.206 -43.079 43.827 1.00 30.25 ? 697 LEU A CD1 1 ATOM 5149 C CD2 . LEU A 1 662 ? -12.030 -44.732 45.687 1.00 32.32 ? 697 LEU A CD2 1 ATOM 5150 N N . VAL A 1 663 ? -8.608 -42.741 48.243 1.00 28.02 ? 698 VAL A N 1 ATOM 5151 C CA . VAL A 1 663 ? -7.209 -42.517 48.654 1.00 28.02 ? 698 VAL A CA 1 ATOM 5152 C C . VAL A 1 663 ? -6.346 -41.967 47.522 1.00 26.58 ? 698 VAL A C 1 ATOM 5153 O O . VAL A 1 663 ? -5.312 -41.337 47.754 1.00 26.22 ? 698 VAL A O 1 ATOM 5154 C CB . VAL A 1 663 ? -6.602 -43.839 49.215 1.00 29.47 ? 698 VAL A CB 1 ATOM 5155 C CG1 . VAL A 1 663 ? -6.384 -44.871 48.111 1.00 30.76 ? 698 VAL A CG1 1 ATOM 5156 C CG2 . VAL A 1 663 ? -5.306 -43.604 49.969 1.00 29.36 ? 698 VAL A CG2 1 ATOM 5157 N N . THR A 1 664 ? -6.787 -42.196 46.293 1.00 26.06 ? 699 THR A N 1 ATOM 5158 C CA . THR A 1 664 ? -6.129 -41.687 45.111 1.00 25.52 ? 699 THR A CA 1 ATOM 5159 C C . THR A 1 664 ? -6.468 -40.224 44.792 1.00 24.08 ? 699 THR A C 1 ATOM 5160 O O . THR A 1 664 ? -5.914 -39.691 43.840 1.00 23.59 ? 699 THR A O 1 ATOM 5161 C CB . THR A 1 664 ? -6.458 -42.563 43.888 1.00 26.74 ? 699 THR A CB 1 ATOM 5162 O OG1 . THR A 1 664 ? -7.877 -42.804 43.824 1.00 26.96 ? 699 THR A OG1 1 ATOM 5163 C CG2 . THR A 1 664 ? -5.725 -43.870 43.992 1.00 28.32 ? 699 THR A CG2 1 ATOM 5164 N N . ASN A 1 665 ? -7.377 -39.609 45.564 1.00 23.08 ? 700 ASN A N 1 ATOM 5165 C CA . ASN A 1 665 ? -7.740 -38.179 45.442 1.00 22.17 ? 700 ASN A CA 1 ATOM 5166 C C . ASN A 1 665 ? -7.168 -37.370 46.617 1.00 22.88 ? 700 ASN A C 1 ATOM 5167 O O . ASN A 1 665 ? -7.373 -36.157 46.691 1.00 22.12 ? 700 ASN A O 1 ATOM 5168 C CB . ASN A 1 665 ? -9.280 -38.064 45.383 1.00 22.64 ? 700 ASN A CB 1 ATOM 5169 C CG . ASN A 1 665 ? -9.800 -36.645 45.088 1.00 21.33 ? 700 ASN A CG 1 ATOM 5170 O OD1 . ASN A 1 665 ? -9.274 -35.909 44.243 1.00 20.98 ? 700 ASN A OD1 1 ATOM 5171 N ND2 . ASN A 1 665 ? -10.866 -36.270 45.773 1.00 21.02 ? 700 ASN A ND2 1 ATOM 5172 N N . MET A 1 666 ? -6.458 -38.024 47.536 1.00 24.06 ? 701 MET A N 1 ATOM 5173 C CA . MET A 1 666 ? -6.023 -37.357 48.769 1.00 24.22 ? 701 MET A CA 1 ATOM 5174 C C . MET A 1 666 ? -4.612 -36.793 48.621 1.00 23.21 ? 701 MET A C 1 ATOM 5175 O O . MET A 1 666 ? -3.761 -37.346 47.908 1.00 24.63 ? 701 MET A O 1 ATOM 5176 C CB . MET A 1 666 ? -6.170 -38.290 49.996 1.00 27.97 ? 701 MET A CB 1 ATOM 5177 C CG . MET A 1 666 ? -4.929 -39.086 50.375 1.00 30.44 ? 701 MET A CG 1 ATOM 5178 S SD . MET A 1 666 ? -5.216 -40.326 51.655 1.00 36.56 ? 701 MET A SD 1 ATOM 5179 C CE . MET A 1 666 ? -5.748 -39.240 52.939 1.00 29.64 ? 701 MET A CE 1 ATOM 5180 N N . VAL A 1 667 ? -4.354 -35.671 49.267 1.00 21.26 ? 702 VAL A N 1 ATOM 5181 C CA . VAL A 1 667 ? -3.028 -35.062 49.203 1.00 20.78 ? 702 VAL A CA 1 ATOM 5182 C C . VAL A 1 667 ? -2.668 -34.516 50.584 1.00 21.14 ? 702 VAL A C 1 ATOM 5183 O O . VAL A 1 667 ? -3.560 -34.093 51.308 1.00 21.41 ? 702 VAL A O 1 ATOM 5184 C CB . VAL A 1 667 ? -2.965 -33.935 48.146 1.00 20.27 ? 702 VAL A CB 1 ATOM 5185 C CG1 . VAL A 1 667 ? -2.912 -34.507 46.740 1.00 21.25 ? 702 VAL A CG1 1 ATOM 5186 C CG2 . VAL A 1 667 ? -4.145 -32.968 48.275 1.00 19.53 ? 702 VAL A CG2 1 ATOM 5187 N N . PRO A 1 668 ? -1.374 -34.528 50.952 1.00 20.89 ? 703 PRO A N 1 ATOM 5188 C CA . PRO A 1 668 ? -0.985 -34.061 52.276 1.00 20.60 ? 703 PRO A CA 1 ATOM 5189 C C . PRO A 1 668 ? -1.099 -32.543 52.414 1.00 19.73 ? 703 PRO A C 1 ATOM 5190 O O . PRO A 1 668 ? -0.628 -31.811 51.536 1.00 19.16 ? 703 PRO A O 1 ATOM 5191 C CB . PRO A 1 668 ? 0.464 -34.528 52.412 1.00 21.40 ? 703 PRO A CB 1 ATOM 5192 C CG . PRO A 1 668 ? 0.953 -34.669 51.035 1.00 22.12 ? 703 PRO A CG 1 ATOM 5193 C CD . PRO A 1 668 ? -0.228 -35.047 50.193 1.00 21.57 ? 703 PRO A CD 1 ATOM 5194 N N . MET A 1 669 ? -1.744 -32.097 53.497 1.00 19.49 ? 704 MET A N 1 ATOM 5195 C CA . MET A 1 669 ? -1.985 -30.681 53.729 1.00 18.97 ? 704 MET A CA 1 ATOM 5196 C C . MET A 1 669 ? -1.844 -30.349 55.200 1.00 19.60 ? 704 MET A C 1 ATOM 5197 O O . MET A 1 669 ? -2.507 -30.955 56.049 1.00 18.91 ? 704 MET A O 1 ATOM 5198 C CB . MET A 1 669 ? -3.373 -30.261 53.224 1.00 19.01 ? 704 MET A CB 1 ATOM 5199 C CG . MET A 1 669 ? -3.497 -30.308 51.709 1.00 19.90 ? 704 MET A CG 1 ATOM 5200 S SD . MET A 1 669 ? -4.964 -29.479 51.070 1.00 19.78 ? 704 MET A SD 1 ATOM 5201 C CE . MET A 1 669 ? -4.463 -29.451 49.345 1.00 19.08 ? 704 MET A CE 1 ATOM 5202 N N . TYR A 1 670 ? -0.966 -29.409 55.523 1.00 19.05 ? 705 TYR A N 1 ATOM 5203 C CA . TYR A 1 670 ? -0.960 -28.779 56.834 1.00 19.89 ? 705 TYR A CA 1 ATOM 5204 C C . TYR A 1 670 ? -2.352 -28.248 57.170 1.00 19.46 ? 705 TYR A C 1 ATOM 5205 O O . TYR A 1 670 ? -3.034 -27.716 56.310 1.00 17.89 ? 705 TYR A O 1 ATOM 5206 C CB . TYR A 1 670 ? 0.025 -27.625 56.875 1.00 19.87 ? 705 TYR A CB 1 ATOM 5207 C CG . TYR A 1 670 ? 1.474 -28.028 56.735 1.00 21.81 ? 705 TYR A CG 1 ATOM 5208 C CD1 . TYR A 1 670 ? 2.102 -28.805 57.707 1.00 24.20 ? 705 TYR A CD1 1 ATOM 5209 C CD2 . TYR A 1 670 ? 2.228 -27.622 55.617 1.00 21.38 ? 705 TYR A CD2 1 ATOM 5210 C CE1 . TYR A 1 670 ? 3.437 -29.175 57.571 1.00 25.45 ? 705 TYR A CE1 1 ATOM 5211 C CE2 . TYR A 1 670 ? 3.565 -27.981 55.497 1.00 23.24 ? 705 TYR A CE2 1 ATOM 5212 C CZ . TYR A 1 670 ? 4.150 -28.754 56.487 1.00 24.93 ? 705 TYR A CZ 1 ATOM 5213 O OH . TYR A 1 670 ? 5.469 -29.104 56.370 1.00 29.20 ? 705 TYR A OH 1 ATOM 5214 N N . PRO A 1 671 ? -2.782 -28.399 58.437 1.00 20.46 ? 706 PRO A N 1 ATOM 5215 C CA . PRO A 1 671 ? -4.051 -27.814 58.874 1.00 21.03 ? 706 PRO A CA 1 ATOM 5216 C C . PRO A 1 671 ? -4.199 -26.316 58.548 1.00 20.20 ? 706 PRO A C 1 ATOM 5217 O O . PRO A 1 671 ? -5.270 -25.887 58.152 1.00 20.51 ? 706 PRO A O 1 ATOM 5218 C CB . PRO A 1 671 ? -4.028 -28.020 60.380 1.00 21.55 ? 706 PRO A CB 1 ATOM 5219 C CG . PRO A 1 671 ? -3.102 -29.180 60.622 1.00 22.41 ? 706 PRO A CG 1 ATOM 5220 C CD . PRO A 1 671 ? -2.121 -29.197 59.493 1.00 21.38 ? 706 PRO A CD 1 ATOM 5221 N N . ALA A 1 672 ? -3.119 -25.550 58.673 1.00 19.32 ? 707 ALA A N 1 ATOM 5222 C CA . ALA A 1 672 ? -3.141 -24.121 58.322 1.00 19.35 ? 707 ALA A CA 1 ATOM 5223 C C . ALA A 1 672 ? -3.493 -23.924 56.861 1.00 18.57 ? 707 ALA A C 1 ATOM 5224 O O . ALA A 1 672 ? -4.314 -23.054 56.522 1.00 17.60 ? 707 ALA A O 1 ATOM 5225 C CB . ALA A 1 672 ? -1.810 -23.449 58.639 1.00 20.08 ? 707 ALA A CB 1 ATOM 5226 N N . PHE A 1 673 ? -2.886 -24.746 56.003 1.00 18.79 ? 708 PHE A N 1 ATOM 5227 C CA . PHE A 1 673 ? -3.159 -24.674 54.582 1.00 18.07 ? 708 PHE A CA 1 ATOM 5228 C C . PHE A 1 673 ? -4.566 -25.119 54.230 1.00 18.54 ? 708 PHE A C 1 ATOM 5229 O O . PHE A 1 673 ? -5.170 -24.594 53.300 1.00 17.04 ? 708 PHE A O 1 ATOM 5230 C CB . PHE A 1 673 ? -2.125 -25.449 53.743 1.00 17.98 ? 708 PHE A CB 1 ATOM 5231 C CG . PHE A 1 673 ? -2.323 -25.247 52.277 1.00 17.03 ? 708 PHE A CG 1 ATOM 5232 C CD1 . PHE A 1 673 ? -1.958 -24.041 51.682 1.00 16.61 ? 708 PHE A CD1 1 ATOM 5233 C CD2 . PHE A 1 673 ? -2.989 -26.199 51.521 1.00 17.31 ? 708 PHE A CD2 1 ATOM 5234 C CE1 . PHE A 1 673 ? -2.208 -23.813 50.333 1.00 16.58 ? 708 PHE A CE1 1 ATOM 5235 C CE2 . PHE A 1 673 ? -3.233 -25.972 50.177 1.00 17.94 ? 708 PHE A CE2 1 ATOM 5236 C CZ . PHE A 1 673 ? -2.848 -24.770 49.585 1.00 16.90 ? 708 PHE A CZ 1 ATOM 5237 N N . LYS A 1 674 ? -5.080 -26.114 54.940 1.00 19.56 ? 709 LYS A N 1 ATOM 5238 C CA . LYS A 1 674 ? -6.452 -26.582 54.726 1.00 19.31 ? 709 LYS A CA 1 ATOM 5239 C C . LYS A 1 674 ? -7.485 -25.473 54.890 1.00 18.39 ? 709 LYS A C 1 ATOM 5240 O O . LYS A 1 674 ? -8.543 -25.512 54.231 1.00 16.98 ? 709 LYS A O 1 ATOM 5241 C CB . LYS A 1 674 ? -6.790 -27.741 55.669 1.00 20.92 ? 709 LYS A CB 1 ATOM 5242 C CG . LYS A 1 674 ? -6.120 -29.032 55.258 1.00 22.88 ? 709 LYS A CG 1 ATOM 5243 C CD . LYS A 1 674 ? -6.314 -30.181 56.234 1.00 25.74 ? 709 LYS A CD 1 ATOM 5244 C CE . LYS A 1 674 ? -7.760 -30.630 56.265 1.00 27.07 ? 709 LYS A CE 1 ATOM 5245 N NZ . LYS A 1 674 ? -7.906 -31.763 57.212 1.00 30.63 ? 709 LYS A NZ 1 ATOM 5246 N N . ARG A 1 675 ? -7.195 -24.482 55.741 1.00 18.05 ? 710 ARG A N 1 ATOM 5247 C CA . ARG A 1 675 ? -8.089 -23.326 55.859 1.00 18.90 ? 710 ARG A CA 1 ATOM 5248 C C . ARG A 1 675 ? -8.240 -22.613 54.517 1.00 17.88 ? 710 ARG A C 1 ATOM 5249 O O . ARG A 1 675 ? -9.345 -22.220 54.137 1.00 18.01 ? 710 ARG A O 1 ATOM 5250 C CB . ARG A 1 675 ? -7.609 -22.345 56.929 1.00 20.50 ? 710 ARG A CB 1 ATOM 5251 C CG . ARG A 1 675 ? -7.710 -22.920 58.344 1.00 20.93 ? 710 ARG A CG 1 ATOM 5252 C CD . ARG A 1 675 ? -7.242 -21.916 59.359 1.00 22.07 ? 710 ARG A CD 1 ATOM 5253 N NE . ARG A 1 675 ? -8.182 -20.796 59.435 1.00 22.85 ? 710 ARG A NE 1 ATOM 5254 C CZ . ARG A 1 675 ? -7.895 -19.576 59.873 1.00 22.67 ? 710 ARG A CZ 1 ATOM 5255 N NH1 . ARG A 1 675 ? -6.668 -19.256 60.288 1.00 23.78 ? 710 ARG A NH1 1 ATOM 5256 N NH2 . ARG A 1 675 ? -8.846 -18.657 59.878 1.00 24.20 ? 710 ARG A NH2 1 ATOM 5257 N N . VAL A 1 676 ? -7.121 -22.512 53.803 1.00 16.70 ? 711 VAL A N 1 ATOM 5258 C CA . VAL A 1 676 ? -7.060 -21.849 52.483 1.00 16.92 ? 711 VAL A CA 1 ATOM 5259 C C . VAL A 1 676 ? -7.748 -22.717 51.459 1.00 16.31 ? 711 VAL A C 1 ATOM 5260 O O . VAL A 1 676 ? -8.670 -22.265 50.761 1.00 16.46 ? 711 VAL A O 1 ATOM 5261 C CB . VAL A 1 676 ? -5.592 -21.584 52.073 1.00 15.33 ? 711 VAL A CB 1 ATOM 5262 C CG1 . VAL A 1 676 ? -5.492 -21.042 50.641 1.00 15.44 ? 711 VAL A CG1 1 ATOM 5263 C CG2 . VAL A 1 676 ? -4.937 -20.621 53.074 1.00 16.80 ? 711 VAL A CG2 1 ATOM 5264 N N . TRP A 1 677 ? -7.302 -23.972 51.398 1.00 16.00 ? 712 TRP A N 1 ATOM 5265 C CA . TRP A 1 677 ? -7.762 -24.928 50.395 1.00 15.96 ? 712 TRP A CA 1 ATOM 5266 C C . TRP A 1 677 ? -9.258 -25.169 50.486 1.00 17.93 ? 712 TRP A C 1 ATOM 5267 O O . TRP A 1 677 ? -9.945 -25.132 49.467 1.00 19.51 ? 712 TRP A O 1 ATOM 5268 C CB . TRP A 1 677 ? -6.972 -26.233 50.487 1.00 16.87 ? 712 TRP A CB 1 ATOM 5269 C CG . TRP A 1 677 ? -7.136 -27.130 49.304 1.00 17.26 ? 712 TRP A CG 1 ATOM 5270 C CD1 . TRP A 1 677 ? -7.762 -28.347 49.280 1.00 18.57 ? 712 TRP A CD1 1 ATOM 5271 C CD2 . TRP A 1 677 ? -6.684 -26.885 47.967 1.00 18.03 ? 712 TRP A CD2 1 ATOM 5272 N NE1 . TRP A 1 677 ? -7.734 -28.868 48.015 1.00 19.74 ? 712 TRP A NE1 1 ATOM 5273 C CE2 . TRP A 1 677 ? -7.084 -27.993 47.185 1.00 18.84 ? 712 TRP A CE2 1 ATOM 5274 C CE3 . TRP A 1 677 ? -5.999 -25.832 47.348 1.00 18.45 ? 712 TRP A CE3 1 ATOM 5275 C CZ2 . TRP A 1 677 ? -6.791 -28.093 45.820 1.00 19.75 ? 712 TRP A CZ2 1 ATOM 5276 C CZ3 . TRP A 1 677 ? -5.708 -25.923 45.976 1.00 19.91 ? 712 TRP A CZ3 1 ATOM 5277 C CH2 . TRP A 1 677 ? -6.110 -27.053 45.230 1.00 20.26 ? 712 TRP A CH2 1 ATOM 5278 N N . ALA A 1 678 ? -9.774 -25.357 51.700 1.00 18.10 ? 713 ALA A N 1 ATOM 5279 C CA . ALA A 1 678 ? -11.177 -25.613 51.870 1.00 19.44 ? 713 ALA A CA 1 ATOM 5280 C C . ALA A 1 678 ? -12.066 -24.457 51.425 1.00 19.35 ? 713 ALA A C 1 ATOM 5281 O O . ALA A 1 678 ? -13.139 -24.685 50.836 1.00 19.82 ? 713 ALA A O 1 ATOM 5282 C CB . ALA A 1 678 ? -11.466 -25.985 53.310 1.00 19.49 ? 713 ALA A CB 1 ATOM 5283 N N . TYR A 1 679 ? -11.617 -23.229 51.674 1.00 19.10 ? 714 TYR A N 1 ATOM 5284 C CA . TYR A 1 679 ? -12.329 -22.037 51.234 1.00 19.26 ? 714 TYR A CA 1 ATOM 5285 C C . TYR A 1 679 ? -12.326 -21.938 49.716 1.00 18.21 ? 714 TYR A C 1 ATOM 5286 O O . TYR A 1 679 ? -13.357 -21.679 49.105 1.00 19.17 ? 714 TYR A O 1 ATOM 5287 C CB . TYR A 1 679 ? -11.761 -20.774 51.888 1.00 20.59 ? 714 TYR A CB 1 ATOM 5288 C CG . TYR A 1 679 ? -12.599 -19.530 51.616 1.00 23.06 ? 714 TYR A CG 1 ATOM 5289 C CD1 . TYR A 1 679 ? -13.797 -19.278 52.321 1.00 24.99 ? 714 TYR A CD1 1 ATOM 5290 C CD2 . TYR A 1 679 ? -12.208 -18.620 50.650 1.00 23.23 ? 714 TYR A CD2 1 ATOM 5291 C CE1 . TYR A 1 679 ? -14.561 -18.138 52.036 1.00 27.03 ? 714 TYR A CE1 1 ATOM 5292 C CE2 . TYR A 1 679 ? -12.949 -17.494 50.376 1.00 24.83 ? 714 TYR A CE2 1 ATOM 5293 C CZ . TYR A 1 679 ? -14.120 -17.259 51.050 1.00 26.99 ? 714 TYR A CZ 1 ATOM 5294 O OH . TYR A 1 679 ? -14.813 -16.108 50.717 1.00 31.32 ? 714 TYR A OH 1 ATOM 5295 N N . PHE A 1 680 ? -11.176 -22.167 49.112 1.00 17.28 ? 715 PHE A N 1 ATOM 5296 C CA . PHE A 1 680 ? -11.066 -22.217 47.672 1.00 17.31 ? 715 PHE A CA 1 ATOM 5297 C C . PHE A 1 680 ? -12.068 -23.223 47.087 1.00 18.81 ? 715 PHE A C 1 ATOM 5298 O O . PHE A 1 680 ? -12.864 -22.882 46.188 1.00 17.72 ? 715 PHE A O 1 ATOM 5299 C CB . PHE A 1 680 ? -9.627 -22.562 47.272 1.00 16.80 ? 715 PHE A CB 1 ATOM 5300 C CG . PHE A 1 680 ? -9.494 -22.959 45.843 1.00 16.80 ? 715 PHE A CG 1 ATOM 5301 C CD1 . PHE A 1 680 ? -9.823 -22.059 44.847 1.00 17.77 ? 715 PHE A CD1 1 ATOM 5302 C CD2 . PHE A 1 680 ? -9.085 -24.244 45.494 1.00 18.36 ? 715 PHE A CD2 1 ATOM 5303 C CE1 . PHE A 1 680 ? -9.715 -22.408 43.519 1.00 18.21 ? 715 PHE A CE1 1 ATOM 5304 C CE2 . PHE A 1 680 ? -8.985 -24.602 44.168 1.00 19.06 ? 715 PHE A CE2 1 ATOM 5305 C CZ . PHE A 1 680 ? -9.307 -23.685 43.185 1.00 18.64 ? 715 PHE A CZ 1 ATOM 5306 N N . GLN A 1 681 ? -12.053 -24.429 47.656 1.00 18.27 ? 716 GLN A N 1 ATOM 5307 C CA A GLN A 1 681 ? -12.851 -25.524 47.110 0.50 19.33 ? 716 GLN A CA 1 ATOM 5308 C CA B GLN A 1 681 ? -12.851 -25.572 47.167 0.50 20.10 ? 716 GLN A CA 1 ATOM 5309 C C . GLN A 1 681 ? -14.345 -25.394 47.388 1.00 20.63 ? 716 GLN A C 1 ATOM 5310 O O . GLN A 1 681 ? -15.155 -25.697 46.520 1.00 22.16 ? 716 GLN A O 1 ATOM 5311 C CB A GLN A 1 681 ? -12.319 -26.852 47.630 0.50 19.14 ? 716 GLN A CB 1 ATOM 5312 C CB B GLN A 1 681 ? -12.441 -26.864 47.896 0.50 20.90 ? 716 GLN A CB 1 ATOM 5313 C CG A GLN A 1 681 ? -10.983 -27.230 47.008 0.50 18.29 ? 716 GLN A CG 1 ATOM 5314 C CG B GLN A 1 681 ? -11.005 -27.331 47.688 0.50 21.17 ? 716 GLN A CG 1 ATOM 5315 C CD A GLN A 1 681 ? -10.672 -28.682 47.221 0.50 18.73 ? 716 GLN A CD 1 ATOM 5316 C CD B GLN A 1 681 ? -10.776 -27.982 46.363 0.50 22.35 ? 716 GLN A CD 1 ATOM 5317 O OE1 A GLN A 1 681 ? -10.889 -29.210 48.301 0.50 19.50 ? 716 GLN A OE1 1 ATOM 5318 O OE1 B GLN A 1 681 ? -10.863 -27.334 45.318 0.50 23.09 ? 716 GLN A OE1 1 ATOM 5319 N NE2 A GLN A 1 681 ? -10.198 -29.348 46.183 0.50 19.61 ? 716 GLN A NE2 1 ATOM 5320 N NE2 B GLN A 1 681 ? -10.476 -29.273 46.387 0.50 23.25 ? 716 GLN A NE2 1 ATOM 5321 N N . ARG A 1 682 ? -14.708 -24.968 48.588 1.00 20.63 ? 717 ARG A N 1 ATOM 5322 C CA . ARG A 1 682 ? -16.105 -24.907 48.990 1.00 23.55 ? 717 ARG A CA 1 ATOM 5323 C C . ARG A 1 682 ? -16.799 -23.628 48.527 1.00 22.82 ? 717 ARG A C 1 ATOM 5324 O O . ARG A 1 682 ? -17.996 -23.664 48.234 1.00 24.02 ? 717 ARG A O 1 ATOM 5325 C CB . ARG A 1 682 ? -16.235 -25.077 50.520 1.00 25.86 ? 717 ARG A CB 1 ATOM 5326 C CG . ARG A 1 682 ? -17.673 -24.994 51.059 1.00 31.53 ? 717 ARG A CG 1 ATOM 5327 C CD . ARG A 1 682 ? -17.719 -25.205 52.567 1.00 34.43 ? 717 ARG A CD 1 ATOM 5328 N NE . ARG A 1 682 ? -17.009 -24.120 53.253 1.00 38.60 ? 717 ARG A NE 1 ATOM 5329 C CZ . ARG A 1 682 ? -17.521 -22.926 53.572 1.00 41.31 ? 717 ARG A CZ 1 ATOM 5330 N NH1 . ARG A 1 682 ? -18.787 -22.603 53.293 1.00 42.28 ? 717 ARG A NH1 1 ATOM 5331 N NH2 . ARG A 1 682 ? -16.746 -22.039 54.193 1.00 42.73 ? 717 ARG A NH2 1 ATOM 5332 N N . VAL A 1 683 ? -16.063 -22.517 48.465 1.00 21.04 ? 718 VAL A N 1 ATOM 5333 C CA . VAL A 1 683 ? -16.643 -21.207 48.167 1.00 20.83 ? 718 VAL A CA 1 ATOM 5334 C C . VAL A 1 683 ? -16.213 -20.636 46.806 1.00 19.87 ? 718 VAL A C 1 ATOM 5335 O O . VAL A 1 683 ? -17.061 -20.250 46.007 1.00 21.30 ? 718 VAL A O 1 ATOM 5336 C CB . VAL A 1 683 ? -16.315 -20.202 49.287 1.00 21.07 ? 718 VAL A CB 1 ATOM 5337 C CG1 . VAL A 1 683 ? -16.922 -18.825 49.009 1.00 22.19 ? 718 VAL A CG1 1 ATOM 5338 C CG2 . VAL A 1 683 ? -16.834 -20.719 50.630 1.00 21.90 ? 718 VAL A CG2 1 ATOM 5339 N N . LEU A 1 684 ? -14.911 -20.566 46.546 1.00 18.30 ? 719 LEU A N 1 ATOM 5340 C CA . LEU A 1 684 ? -14.417 -19.804 45.408 1.00 18.18 ? 719 LEU A CA 1 ATOM 5341 C C . LEU A 1 684 ? -14.628 -20.483 44.073 1.00 17.73 ? 719 LEU A C 1 ATOM 5342 O O . LEU A 1 684 ? -14.929 -19.804 43.096 1.00 18.94 ? 719 LEU A O 1 ATOM 5343 C CB . LEU A 1 684 ? -12.951 -19.421 45.598 1.00 18.09 ? 719 LEU A CB 1 ATOM 5344 C CG . LEU A 1 684 ? -12.682 -18.529 46.792 1.00 19.40 ? 719 LEU A CG 1 ATOM 5345 C CD1 . LEU A 1 684 ? -11.188 -18.290 46.905 1.00 19.36 ? 719 LEU A CD1 1 ATOM 5346 C CD2 . LEU A 1 684 ? -13.419 -17.198 46.691 1.00 21.35 ? 719 LEU A CD2 1 ATOM 5347 N N . VAL A 1 685 ? -14.495 -21.819 44.000 1.00 17.52 ? 720 VAL A N 1 ATOM 5348 C CA . VAL A 1 685 ? -14.697 -22.483 42.727 1.00 17.82 ? 720 VAL A CA 1 ATOM 5349 C C . VAL A 1 685 ? -16.136 -22.224 42.243 1.00 19.04 ? 720 VAL A C 1 ATOM 5350 O O . VAL A 1 685 ? -16.352 -21.896 41.080 1.00 17.86 ? 720 VAL A O 1 ATOM 5351 C CB . VAL A 1 685 ? -14.419 -24.005 42.796 1.00 19.28 ? 720 VAL A CB 1 ATOM 5352 C CG1 . VAL A 1 685 ? -14.911 -24.689 41.525 1.00 19.55 ? 720 VAL A CG1 1 ATOM 5353 C CG2 . VAL A 1 685 ? -12.922 -24.274 42.968 1.00 18.62 ? 720 VAL A CG2 1 ATOM 5354 N N . LYS A 1 686 ? -17.111 -22.384 43.132 1.00 18.63 ? 721 LYS A N 1 ATOM 5355 C CA . LYS A 1 686 ? -18.519 -22.078 42.797 1.00 21.42 ? 721 LYS A CA 1 ATOM 5356 C C . LYS A 1 686 ? -18.667 -20.612 42.375 1.00 20.79 ? 721 LYS A C 1 ATOM 5357 O O . LYS A 1 686 ? -19.316 -20.325 41.380 1.00 20.21 ? 721 LYS A O 1 ATOM 5358 C CB . LYS A 1 686 ? -19.449 -22.389 43.971 1.00 23.22 ? 721 LYS A CB 1 ATOM 5359 C CG . LYS A 1 686 ? -20.880 -21.851 43.860 1.00 26.66 ? 721 LYS A CG 1 ATOM 5360 C CD . LYS A 1 686 ? -21.615 -22.306 42.599 1.00 27.56 ? 721 LYS A CD 1 ATOM 5361 C CE . LYS A 1 686 ? -23.073 -21.847 42.605 1.00 31.13 ? 721 LYS A CE 1 ATOM 5362 N NZ . LYS A 1 686 ? -23.750 -22.163 41.314 1.00 31.71 ? 721 LYS A NZ 1 ATOM 5363 N N . LYS A 1 687 ? -18.045 -19.693 43.116 1.00 20.26 ? 722 LYS A N 1 ATOM 5364 C CA . LYS A 1 687 ? -18.075 -18.284 42.737 1.00 20.87 ? 722 LYS A CA 1 ATOM 5365 C C . LYS A 1 687 ? -17.586 -18.081 41.305 1.00 20.90 ? 722 LYS A C 1 ATOM 5366 O O . LYS A 1 687 ? -18.267 -17.433 40.510 1.00 20.32 ? 722 LYS A O 1 ATOM 5367 C CB . LYS A 1 687 ? -17.246 -17.444 43.702 1.00 22.42 ? 722 LYS A CB 1 ATOM 5368 C CG . LYS A 1 687 ? -17.296 -15.947 43.428 1.00 24.62 ? 722 LYS A CG 1 ATOM 5369 C CD . LYS A 1 687 ? -16.306 -15.253 44.349 1.00 28.58 ? 722 LYS A CD 1 ATOM 5370 C CE . LYS A 1 687 ? -16.133 -13.792 44.016 1.00 33.01 ? 722 LYS A CE 1 ATOM 5371 N NZ . LYS A 1 687 ? -14.872 -13.322 44.654 1.00 37.51 ? 722 LYS A NZ 1 ATOM 5372 N N . TYR A 1 688 ? -16.429 -18.662 40.984 1.00 19.61 ? 723 TYR A N 1 ATOM 5373 C CA . TYR A 1 688 ? -15.846 -18.521 39.642 1.00 18.96 ? 723 TYR A CA 1 ATOM 5374 C C . TYR A 1 688 ? -16.770 -19.096 38.577 1.00 18.76 ? 723 TYR A C 1 ATOM 5375 O O . TYR A 1 688 ? -17.014 -18.445 37.550 1.00 18.35 ? 723 TYR A O 1 ATOM 5376 C CB . TYR A 1 688 ? -14.435 -19.144 39.536 1.00 18.68 ? 723 TYR A CB 1 ATOM 5377 C CG . TYR A 1 688 ? -13.427 -18.595 40.550 1.00 19.30 ? 723 TYR A CG 1 ATOM 5378 C CD1 . TYR A 1 688 ? -13.537 -17.306 41.044 1.00 21.07 ? 723 TYR A CD1 1 ATOM 5379 C CD2 . TYR A 1 688 ? -12.384 -19.394 41.027 1.00 21.93 ? 723 TYR A CD2 1 ATOM 5380 C CE1 . TYR A 1 688 ? -12.645 -16.822 41.993 1.00 22.91 ? 723 TYR A CE1 1 ATOM 5381 C CE2 . TYR A 1 688 ? -11.474 -18.904 41.964 1.00 21.18 ? 723 TYR A CE2 1 ATOM 5382 C CZ . TYR A 1 688 ? -11.611 -17.629 42.425 1.00 23.12 ? 723 TYR A CZ 1 ATOM 5383 O OH . TYR A 1 688 ? -10.738 -17.138 43.358 1.00 28.54 ? 723 TYR A OH 1 ATOM 5384 N N . ALA A 1 689 ? -17.283 -20.307 38.811 1.00 17.85 ? 724 ALA A N 1 ATOM 5385 C CA . ALA A 1 689 ? -18.252 -20.913 37.895 1.00 19.19 ? 724 ALA A CA 1 ATOM 5386 C C . ALA A 1 689 ? -19.455 -19.972 37.692 1.00 19.39 ? 724 ALA A C 1 ATOM 5387 O O . ALA A 1 689 ? -19.898 -19.777 36.569 1.00 20.94 ? 724 ALA A O 1 ATOM 5388 C CB . ALA A 1 689 ? -18.725 -22.267 38.408 1.00 18.99 ? 724 ALA A CB 1 ATOM 5389 N N . SER A 1 690 ? -19.943 -19.369 38.764 1.00 20.04 ? 725 SER A N 1 ATOM 5390 C CA . SER A 1 690 ? -21.068 -18.432 38.676 1.00 22.22 ? 725 SER A CA 1 ATOM 5391 C C . SER A 1 690 ? -20.758 -17.109 37.931 1.00 23.15 ? 725 SER A C 1 ATOM 5392 O O . SER A 1 690 ? -21.667 -16.493 37.362 1.00 25.80 ? 725 SER A O 1 ATOM 5393 C CB . SER A 1 690 ? -21.633 -18.147 40.073 1.00 24.47 ? 725 SER A CB 1 ATOM 5394 O OG . SER A 1 690 ? -21.940 -19.373 40.733 1.00 25.73 ? 725 SER A OG 1 ATOM 5395 N N . GLU A 1 691 ? -19.497 -16.687 37.930 1.00 21.07 ? 726 GLU A N 1 ATOM 5396 C CA . GLU A 1 691 ? -19.087 -15.447 37.285 1.00 21.87 ? 726 GLU A CA 1 ATOM 5397 C C . GLU A 1 691 ? -18.707 -15.629 35.821 1.00 22.03 ? 726 GLU A C 1 ATOM 5398 O O . GLU A 1 691 ? -18.822 -14.688 35.045 1.00 23.97 ? 726 GLU A O 1 ATOM 5399 C CB . GLU A 1 691 ? -17.892 -14.828 38.020 1.00 22.08 ? 726 GLU A CB 1 ATOM 5400 C CG . GLU A 1 691 ? -18.216 -14.344 39.427 1.00 22.72 ? 726 GLU A CG 1 ATOM 5401 C CD . GLU A 1 691 ? -17.002 -13.794 40.169 1.00 23.93 ? 726 GLU A CD 1 ATOM 5402 O OE1 . GLU A 1 691 ? -15.890 -14.337 40.016 1.00 24.59 ? 726 GLU A OE1 1 ATOM 5403 O OE2 . GLU A 1 691 ? -17.193 -12.841 40.951 1.00 28.61 ? 726 GLU A OE2 1 ATOM 5404 N N . ARG A 1 692 ? -18.262 -16.827 35.454 1.00 20.90 ? 727 ARG A N 1 ATOM 5405 C CA . ARG A 1 692 ? -17.596 -17.053 34.168 1.00 20.22 ? 727 ARG A CA 1 ATOM 5406 C C . ARG A 1 692 ? -18.387 -17.957 33.226 1.00 20.42 ? 727 ARG A C 1 ATOM 5407 O O . ARG A 1 692 ? -17.872 -18.356 32.163 1.00 20.15 ? 727 ARG A O 1 ATOM 5408 C CB . ARG A 1 692 ? -16.185 -17.627 34.434 1.00 20.75 ? 727 ARG A CB 1 ATOM 5409 C CG . ARG A 1 692 ? -15.273 -16.610 35.101 1.00 21.38 ? 727 ARG A CG 1 ATOM 5410 C CD . ARG A 1 692 ? -13.954 -17.178 35.609 1.00 21.35 ? 727 ARG A CD 1 ATOM 5411 N NE . ARG A 1 692 ? -13.122 -17.756 34.556 1.00 23.12 ? 727 ARG A NE 1 ATOM 5412 C CZ . ARG A 1 692 ? -11.861 -18.160 34.717 1.00 22.47 ? 727 ARG A CZ 1 ATOM 5413 N NH1 . ARG A 1 692 ? -11.235 -18.036 35.905 1.00 20.70 ? 727 ARG A NH1 1 ATOM 5414 N NH2 . ARG A 1 692 ? -11.224 -18.701 33.678 1.00 20.42 ? 727 ARG A NH2 1 ATOM 5415 N N . ASN A 1 693 ? -19.655 -18.238 33.560 1.00 20.60 ? 728 ASN A N 1 ATOM 5416 C CA . ASN A 1 693 ? -20.467 -19.214 32.835 1.00 20.88 ? 728 ASN A CA 1 ATOM 5417 C C . ASN A 1 693 ? -19.834 -20.612 32.806 1.00 20.47 ? 728 ASN A C 1 ATOM 5418 O O . ASN A 1 693 ? -19.642 -21.234 31.744 1.00 21.56 ? 728 ASN A O 1 ATOM 5419 C CB . ASN A 1 693 ? -20.779 -18.725 31.426 1.00 21.88 ? 728 ASN A CB 1 ATOM 5420 C CG . ASN A 1 693 ? -22.055 -19.313 30.882 1.00 23.83 ? 728 ASN A CG 1 ATOM 5421 O OD1 . ASN A 1 693 ? -22.690 -20.177 31.513 1.00 24.18 ? 728 ASN A OD1 1 ATOM 5422 N ND2 . ASN A 1 693 ? -22.447 -18.855 29.699 1.00 23.86 ? 728 ASN A ND2 1 ATOM 5423 N N . GLY A 1 694 ? -19.476 -21.080 33.990 1.00 19.78 ? 729 GLY A N 1 ATOM 5424 C CA . GLY A 1 694 ? -18.829 -22.358 34.179 1.00 19.55 ? 729 GLY A CA 1 ATOM 5425 C C . GLY A 1 694 ? -17.324 -22.183 34.112 1.00 20.11 ? 729 GLY A C 1 ATOM 5426 O O . GLY A 1 694 ? -16.829 -21.229 33.502 1.00 18.88 ? 729 GLY A O 1 ATOM 5427 N N . VAL A 1 695 ? -16.617 -23.101 34.761 1.00 19.24 ? 730 VAL A N 1 ATOM 5428 C CA . VAL A 1 695 ? -15.151 -23.168 34.714 1.00 19.44 ? 730 VAL A CA 1 ATOM 5429 C C . VAL A 1 695 ? -14.704 -24.620 34.649 1.00 19.10 ? 730 VAL A C 1 ATOM 5430 O O . VAL A 1 695 ? -15.374 -25.512 35.170 1.00 20.78 ? 730 VAL A O 1 ATOM 5431 C CB . VAL A 1 695 ? -14.459 -22.511 35.932 1.00 17.79 ? 730 VAL A CB 1 ATOM 5432 C CG1 . VAL A 1 695 ? -14.692 -21.023 35.924 1.00 19.92 ? 730 VAL A CG1 1 ATOM 5433 C CG2 . VAL A 1 695 ? -14.900 -23.137 37.260 1.00 18.96 ? 730 VAL A CG2 1 ATOM 5434 N N . ASN A 1 696 ? -13.573 -24.829 33.998 1.00 18.00 ? 731 ASN A N 1 ATOM 5435 C CA . ASN A 1 696 ? -12.840 -26.071 34.082 1.00 18.73 ? 731 ASN A CA 1 ATOM 5436 C C . ASN A 1 696 ? -11.632 -25.822 34.968 1.00 19.12 ? 731 ASN A C 1 ATOM 5437 O O . ASN A 1 696 ? -10.904 -24.836 34.774 1.00 18.83 ? 731 ASN A O 1 ATOM 5438 C CB . ASN A 1 696 ? -12.378 -26.523 32.702 1.00 19.03 ? 731 ASN A CB 1 ATOM 5439 C CG . ASN A 1 696 ? -11.491 -27.743 32.772 1.00 19.66 ? 731 ASN A CG 1 ATOM 5440 O OD1 . ASN A 1 696 ? -10.264 -27.633 32.751 1.00 18.82 ? 731 ASN A OD1 1 ATOM 5441 N ND2 . ASN A 1 696 ? -12.096 -28.897 32.888 1.00 20.21 ? 731 ASN A ND2 1 ATOM 5442 N N . VAL A 1 697 ? -11.423 -26.722 35.925 1.00 17.53 ? 732 VAL A N 1 ATOM 5443 C CA . VAL A 1 697 ? -10.369 -26.604 36.925 1.00 17.02 ? 732 VAL A CA 1 ATOM 5444 C C . VAL A 1 697 ? -9.427 -27.799 36.780 1.00 18.06 ? 732 VAL A C 1 ATOM 5445 O O . VAL A 1 697 ? -9.879 -28.948 36.696 1.00 20.13 ? 732 VAL A O 1 ATOM 5446 C CB . VAL A 1 697 ? -10.974 -26.617 38.346 1.00 16.61 ? 732 VAL A CB 1 ATOM 5447 C CG1 . VAL A 1 697 ? -9.885 -26.457 39.412 1.00 16.90 ? 732 VAL A CG1 1 ATOM 5448 C CG2 . VAL A 1 697 ? -12.040 -25.527 38.467 1.00 17.20 ? 732 VAL A CG2 1 ATOM 5449 N N . ILE A 1 698 ? -8.124 -27.524 36.746 1.00 16.28 ? 733 ILE A N 1 ATOM 5450 C CA . ILE A 1 698 ? -7.109 -28.538 36.910 1.00 16.89 ? 733 ILE A CA 1 ATOM 5451 C C . ILE A 1 698 ? -6.246 -28.156 38.109 1.00 17.06 ? 733 ILE A C 1 ATOM 5452 O O . ILE A 1 698 ? -5.681 -27.075 38.126 1.00 16.29 ? 733 ILE A O 1 ATOM 5453 C CB . ILE A 1 698 ? -6.194 -28.695 35.671 1.00 18.10 ? 733 ILE A CB 1 ATOM 5454 C CG1 . ILE A 1 698 ? -7.029 -28.915 34.409 1.00 19.97 ? 733 ILE A CG1 1 ATOM 5455 C CG2 . ILE A 1 698 ? -5.236 -29.855 35.905 1.00 19.00 ? 733 ILE A CG2 1 ATOM 5456 C CD1 . ILE A 1 698 ? -6.187 -29.071 33.146 1.00 22.58 ? 733 ILE A CD1 1 ATOM 5457 N N . SER A 1 699 ? -6.164 -29.049 39.099 1.00 16.54 ? 734 SER A N 1 ATOM 5458 C CA . SER A 1 699 ? -5.407 -28.817 40.321 1.00 15.62 ? 734 SER A CA 1 ATOM 5459 C C . SER A 1 699 ? -4.372 -29.893 40.573 1.00 15.79 ? 734 SER A C 1 ATOM 5460 O O . SER A 1 699 ? -4.528 -31.024 40.139 1.00 16.50 ? 734 SER A O 1 ATOM 5461 C CB . SER A 1 699 ? -6.354 -28.776 41.518 1.00 15.97 ? 734 SER A CB 1 ATOM 5462 O OG . SER A 1 699 ? -7.293 -27.735 41.381 1.00 17.67 ? 734 SER A OG 1 ATOM 5463 N N . GLY A 1 700 ? -3.316 -29.559 41.306 1.00 15.39 ? 735 GLY A N 1 ATOM 5464 C CA . GLY A 1 700 ? -2.338 -30.570 41.636 1.00 15.93 ? 735 GLY A CA 1 ATOM 5465 C C . GLY A 1 700 ? -1.218 -30.054 42.514 1.00 15.95 ? 735 GLY A C 1 ATOM 5466 O O . GLY A 1 700 ? -1.212 -28.874 42.848 1.00 17.50 ? 735 GLY A O 1 ATOM 5467 N N . PRO A 1 701 ? -0.284 -30.937 42.889 1.00 16.57 ? 736 PRO A N 1 ATOM 5468 C CA . PRO A 1 701 ? 0.869 -30.618 43.726 1.00 16.70 ? 736 PRO A CA 1 ATOM 5469 C C . PRO A 1 701 ? 2.029 -30.076 42.909 1.00 17.25 ? 736 PRO A C 1 ATOM 5470 O O . PRO A 1 701 ? 2.155 -30.387 41.716 1.00 18.47 ? 736 PRO A O 1 ATOM 5471 C CB . PRO A 1 701 ? 1.253 -31.987 44.297 1.00 18.05 ? 736 PRO A CB 1 ATOM 5472 C CG . PRO A 1 701 ? 0.932 -32.923 43.183 1.00 18.07 ? 736 PRO A CG 1 ATOM 5473 C CD . PRO A 1 701 ? -0.338 -32.384 42.593 1.00 17.01 ? 736 PRO A CD 1 ATOM 5474 N N . ILE A 1 702 ? 2.915 -29.353 43.588 1.00 16.48 ? 737 ILE A N 1 ATOM 5475 C CA . ILE A 1 702 ? 4.189 -28.915 43.024 1.00 15.80 ? 737 ILE A CA 1 ATOM 5476 C C . ILE A 1 702 ? 5.246 -29.173 44.069 1.00 16.83 ? 737 ILE A C 1 ATOM 5477 O O . ILE A 1 702 ? 5.012 -28.908 45.236 1.00 17.64 ? 737 ILE A O 1 ATOM 5478 C CB . ILE A 1 702 ? 4.127 -27.418 42.668 1.00 14.62 ? 737 ILE A CB 1 ATOM 5479 C CG1 . ILE A 1 702 ? 3.480 -27.248 41.279 1.00 14.36 ? 737 ILE A CG1 1 ATOM 5480 C CG2 . ILE A 1 702 ? 5.502 -26.773 42.688 1.00 14.62 ? 737 ILE A CG2 1 ATOM 5481 C CD1 . ILE A 1 702 ? 3.010 -25.860 40.958 1.00 15.46 ? 737 ILE A CD1 1 ATOM 5482 N N . PHE A 1 703 ? 6.414 -29.653 43.635 1.00 15.42 ? 738 PHE A N 1 ATOM 5483 C CA . PHE A 1 703 ? 7.552 -29.891 44.488 1.00 16.49 ? 738 PHE A CA 1 ATOM 5484 C C . PHE A 1 703 ? 8.711 -29.060 43.958 1.00 17.48 ? 738 PHE A C 1 ATOM 5485 O O . PHE A 1 703 ? 9.256 -29.380 42.897 1.00 16.87 ? 738 PHE A O 1 ATOM 5486 C CB . PHE A 1 703 ? 7.926 -31.389 44.524 1.00 18.03 ? 738 PHE A CB 1 ATOM 5487 C CG . PHE A 1 703 ? 6.783 -32.292 44.898 1.00 18.58 ? 738 PHE A CG 1 ATOM 5488 C CD1 . PHE A 1 703 ? 5.908 -32.755 43.924 1.00 18.25 ? 738 PHE A CD1 1 ATOM 5489 C CD2 . PHE A 1 703 ? 6.577 -32.679 46.216 1.00 19.67 ? 738 PHE A CD2 1 ATOM 5490 C CE1 . PHE A 1 703 ? 4.842 -33.563 44.250 1.00 19.32 ? 738 PHE A CE1 1 ATOM 5491 C CE2 . PHE A 1 703 ? 5.510 -33.491 46.557 1.00 19.01 ? 738 PHE A CE2 1 ATOM 5492 C CZ . PHE A 1 703 ? 4.636 -33.941 45.571 1.00 19.12 ? 738 PHE A CZ 1 ATOM 5493 N N . ASP A 1 704 ? 9.067 -27.990 44.687 1.00 17.45 ? 739 ASP A N 1 ATOM 5494 C CA . ASP A 1 704 ? 10.233 -27.160 44.341 1.00 17.36 ? 739 ASP A CA 1 ATOM 5495 C C . ASP A 1 704 ? 11.079 -26.798 45.554 1.00 18.11 ? 739 ASP A C 1 ATOM 5496 O O . ASP A 1 704 ? 11.248 -25.609 45.897 1.00 17.39 ? 739 ASP A O 1 ATOM 5497 C CB . ASP A 1 704 ? 9.812 -25.907 43.569 1.00 16.29 ? 739 ASP A CB 1 ATOM 5498 C CG . ASP A 1 704 ? 11.003 -25.195 42.917 1.00 16.05 ? 739 ASP A CG 1 ATOM 5499 O OD1 . ASP A 1 704 ? 12.053 -25.839 42.703 1.00 16.00 ? 739 ASP A OD1 1 ATOM 5500 O OD2 . ASP A 1 704 ? 10.870 -23.976 42.629 1.00 14.72 ? 739 ASP A OD2 1 ATOM 5501 N N . TYR A 1 705 ? 11.629 -27.832 46.188 1.00 18.82 ? 740 TYR A N 1 ATOM 5502 C CA . TYR A 1 705 ? 12.445 -27.652 47.417 1.00 19.64 ? 740 TYR A CA 1 ATOM 5503 C C . TYR A 1 705 ? 13.722 -26.829 47.199 1.00 20.39 ? 740 TYR A C 1 ATOM 5504 O O . TYR A 1 705 ? 14.192 -26.151 48.112 1.00 19.43 ? 740 TYR A O 1 ATOM 5505 C CB . TYR A 1 705 ? 12.763 -29.007 48.073 1.00 20.87 ? 740 TYR A CB 1 ATOM 5506 C CG . TYR A 1 705 ? 11.580 -29.543 48.839 1.00 21.54 ? 740 TYR A CG 1 ATOM 5507 C CD1 . TYR A 1 705 ? 10.580 -30.275 48.211 1.00 21.22 ? 740 TYR A CD1 1 ATOM 5508 C CD2 . TYR A 1 705 ? 11.440 -29.270 50.200 1.00 23.28 ? 740 TYR A CD2 1 ATOM 5509 C CE1 . TYR A 1 705 ? 9.480 -30.731 48.925 1.00 22.02 ? 740 TYR A CE1 1 ATOM 5510 C CE2 . TYR A 1 705 ? 10.354 -29.724 50.911 1.00 22.75 ? 740 TYR A CE2 1 ATOM 5511 C CZ . TYR A 1 705 ? 9.379 -30.449 50.264 1.00 23.07 ? 740 TYR A CZ 1 ATOM 5512 O OH . TYR A 1 705 ? 8.296 -30.880 50.979 1.00 24.05 ? 740 TYR A OH 1 ATOM 5513 N N . ASN A 1 706 ? 14.271 -26.859 45.989 1.00 21.26 ? 741 ASN A N 1 ATOM 5514 C CA . ASN A 1 706 ? 15.497 -26.076 45.693 1.00 21.13 ? 741 ASN A CA 1 ATOM 5515 C C . ASN A 1 706 ? 15.185 -24.739 44.998 1.00 20.06 ? 741 ASN A C 1 ATOM 5516 O O . ASN A 1 706 ? 16.096 -24.079 44.477 1.00 19.50 ? 741 ASN A O 1 ATOM 5517 C CB . ASN A 1 706 ? 16.491 -26.913 44.887 1.00 21.43 ? 741 ASN A CB 1 ATOM 5518 C CG . ASN A 1 706 ? 15.975 -27.279 43.509 1.00 22.78 ? 741 ASN A CG 1 ATOM 5519 O OD1 . ASN A 1 706 ? 14.790 -27.117 43.194 1.00 20.07 ? 741 ASN A OD1 1 ATOM 5520 N ND2 . ASN A 1 706 ? 16.862 -27.775 42.680 1.00 24.68 ? 741 ASN A ND2 1 ATOM 5521 N N . TYR A 1 707 ? 13.907 -24.335 45.017 1.00 18.26 ? 742 TYR A N 1 ATOM 5522 C CA . TYR A 1 707 ? 13.453 -23.024 44.534 1.00 17.70 ? 742 TYR A CA 1 ATOM 5523 C C . TYR A 1 707 ? 14.061 -22.572 43.209 1.00 17.86 ? 742 TYR A C 1 ATOM 5524 O O . TYR A 1 707 ? 14.457 -21.427 43.070 1.00 16.96 ? 742 TYR A O 1 ATOM 5525 C CB . TYR A 1 707 ? 13.573 -21.949 45.635 1.00 18.02 ? 742 TYR A CB 1 ATOM 5526 C CG . TYR A 1 707 ? 14.917 -21.809 46.301 1.00 19.36 ? 742 TYR A CG 1 ATOM 5527 C CD1 . TYR A 1 707 ? 15.875 -20.937 45.806 1.00 21.31 ? 742 TYR A CD1 1 ATOM 5528 C CD2 . TYR A 1 707 ? 15.233 -22.549 47.450 1.00 22.44 ? 742 TYR A CD2 1 ATOM 5529 C CE1 . TYR A 1 707 ? 17.117 -20.803 46.411 1.00 23.09 ? 742 TYR A CE1 1 ATOM 5530 C CE2 . TYR A 1 707 ? 16.474 -22.420 48.070 1.00 24.40 ? 742 TYR A CE2 1 ATOM 5531 C CZ . TYR A 1 707 ? 17.409 -21.544 47.548 1.00 25.18 ? 742 TYR A CZ 1 ATOM 5532 O OH . TYR A 1 707 ? 18.640 -21.414 48.141 1.00 26.87 ? 742 TYR A OH 1 ATOM 5533 N N . ASP A 1 708 ? 14.155 -23.490 42.251 1.00 17.80 ? 743 ASP A N 1 ATOM 5534 C CA . ASP A 1 708 ? 14.696 -23.159 40.912 1.00 17.41 ? 743 ASP A CA 1 ATOM 5535 C C . ASP A 1 708 ? 13.583 -22.949 39.871 1.00 16.83 ? 743 ASP A C 1 ATOM 5536 O O . ASP A 1 708 ? 13.859 -22.699 38.695 1.00 16.18 ? 743 ASP A O 1 ATOM 5537 C CB . ASP A 1 708 ? 15.770 -24.179 40.445 1.00 18.05 ? 743 ASP A CB 1 ATOM 5538 C CG . ASP A 1 708 ? 15.208 -25.561 40.157 1.00 18.24 ? 743 ASP A CG 1 ATOM 5539 O OD1 . ASP A 1 708 ? 14.004 -25.809 40.410 1.00 17.54 ? 743 ASP A OD1 1 ATOM 5540 O OD2 . ASP A 1 708 ? 15.979 -26.409 39.658 1.00 20.13 ? 743 ASP A OD2 1 ATOM 5541 N N . GLY A 1 709 ? 12.321 -22.981 40.297 1.00 15.52 ? 744 GLY A N 1 ATOM 5542 C CA . GLY A 1 709 ? 11.192 -22.858 39.379 1.00 15.76 ? 744 GLY A CA 1 ATOM 5543 C C . GLY A 1 709 ? 10.878 -24.062 38.530 1.00 15.98 ? 744 GLY A C 1 ATOM 5544 O O . GLY A 1 709 ? 10.020 -23.963 37.638 1.00 16.23 ? 744 GLY A O 1 ATOM 5545 N N . LEU A 1 710 ? 11.566 -25.176 38.793 1.00 15.23 ? 745 LEU A N 1 ATOM 5546 C CA . LEU A 1 710 ? 11.487 -26.406 38.012 1.00 16.59 ? 745 LEU A CA 1 ATOM 5547 C C . LEU A 1 710 ? 11.054 -27.577 38.866 1.00 16.85 ? 745 LEU A C 1 ATOM 5548 O O . LEU A 1 710 ? 11.455 -27.693 40.009 1.00 17.16 ? 745 LEU A O 1 ATOM 5549 C CB . LEU A 1 710 ? 12.844 -26.744 37.389 1.00 18.31 ? 745 LEU A CB 1 ATOM 5550 C CG . LEU A 1 710 ? 13.515 -25.612 36.579 1.00 18.52 ? 745 LEU A CG 1 ATOM 5551 C CD1 . LEU A 1 710 ? 14.876 -26.015 36.048 1.00 20.04 ? 745 LEU A CD1 1 ATOM 5552 C CD2 . LEU A 1 710 ? 12.646 -25.160 35.427 1.00 17.60 ? 745 LEU A CD2 1 ATOM 5553 N N . ARG A 1 711 ? 10.293 -28.488 38.272 1.00 16.77 ? 746 ARG A N 1 ATOM 5554 C CA . ARG A 1 711 ? 9.894 -29.733 38.918 1.00 19.04 ? 746 ARG A CA 1 ATOM 5555 C C . ARG A 1 711 ? 11.066 -30.477 39.569 1.00 18.14 ? 746 ARG A C 1 ATOM 5556 O O . ARG A 1 711 ? 12.045 -30.784 38.926 1.00 17.17 ? 746 ARG A O 1 ATOM 5557 C CB . ARG A 1 711 ? 9.249 -30.631 37.859 1.00 21.88 ? 746 ARG A CB 1 ATOM 5558 C CG . ARG A 1 711 ? 9.074 -32.084 38.263 1.00 26.96 ? 746 ARG A CG 1 ATOM 5559 C CD . ARG A 1 711 ? 8.847 -33.000 37.073 1.00 28.90 ? 746 ARG A CD 1 ATOM 5560 N NE . ARG A 1 711 ? 10.009 -33.097 36.207 1.00 28.46 ? 746 ARG A NE 1 ATOM 5561 C CZ . ARG A 1 711 ? 11.018 -33.966 36.316 1.00 29.97 ? 746 ARG A CZ 1 ATOM 5562 N NH1 . ARG A 1 711 ? 11.087 -34.900 37.274 1.00 30.96 ? 746 ARG A NH1 1 ATOM 5563 N NH2 . ARG A 1 711 ? 11.984 -33.903 35.416 1.00 30.22 ? 746 ARG A NH2 1 ATOM 5564 N N . ASP A 1 712 ? 10.924 -30.819 40.843 1.00 19.03 ? 747 ASP A N 1 ATOM 5565 C CA . ASP A 1 712 ? 11.946 -31.562 41.563 1.00 19.72 ? 747 ASP A CA 1 ATOM 5566 C C . ASP A 1 712 ? 11.955 -33.006 41.107 1.00 21.68 ? 747 ASP A C 1 ATOM 5567 O O . ASP A 1 712 ? 10.904 -33.579 40.812 1.00 21.90 ? 747 ASP A O 1 ATOM 5568 C CB . ASP A 1 712 ? 11.657 -31.582 43.065 1.00 20.25 ? 747 ASP A CB 1 ATOM 5569 C CG . ASP A 1 712 ? 11.987 -30.291 43.748 1.00 20.37 ? 747 ASP A CG 1 ATOM 5570 O OD1 . ASP A 1 712 ? 12.511 -29.335 43.115 1.00 19.78 ? 747 ASP A OD1 1 ATOM 5571 O OD2 . ASP A 1 712 ? 11.706 -30.236 44.969 1.00 20.77 ? 747 ASP A OD2 1 ATOM 5572 N N . THR A 1 713 ? 13.148 -33.578 41.067 1.00 24.15 ? 748 THR A N 1 ATOM 5573 C CA . THR A 1 713 ? 13.302 -35.026 40.994 1.00 25.34 ? 748 THR A CA 1 ATOM 5574 C C . THR A 1 713 ? 13.046 -35.625 42.378 1.00 26.76 ? 748 THR A C 1 ATOM 5575 O O . THR A 1 713 ? 12.967 -34.924 43.385 1.00 24.31 ? 748 THR A O 1 ATOM 5576 C CB . THR A 1 713 ? 14.723 -35.401 40.569 1.00 27.20 ? 748 THR A CB 1 ATOM 5577 O OG1 . THR A 1 713 ? 15.655 -34.868 41.528 1.00 28.13 ? 748 THR A OG1 1 ATOM 5578 C CG2 . THR A 1 713 ? 15.018 -34.853 39.186 1.00 27.22 ? 748 THR A CG2 1 ATOM 5579 N N . GLU A 1 714 ? 12.967 -36.943 42.431 1.00 28.91 ? 749 GLU A N 1 ATOM 5580 C CA . GLU A 1 714 ? 12.660 -37.615 43.687 1.00 31.45 ? 749 GLU A CA 1 ATOM 5581 C C . GLU A 1 714 ? 13.726 -37.309 44.741 1.00 31.49 ? 749 GLU A C 1 ATOM 5582 O O . GLU A 1 714 ? 13.389 -37.050 45.911 1.00 29.49 ? 749 GLU A O 1 ATOM 5583 C CB . GLU A 1 714 ? 12.506 -39.124 43.469 1.00 36.75 ? 749 GLU A CB 1 ATOM 5584 C CG . GLU A 1 714 ? 11.338 -39.711 44.230 1.00 39.45 ? 749 GLU A CG 1 ATOM 5585 C CD . GLU A 1 714 ? 11.352 -41.219 44.215 1.00 43.08 ? 749 GLU A CD 1 ATOM 5586 O OE1 . GLU A 1 714 ? 11.425 -41.798 43.111 1.00 45.81 ? 749 GLU A OE1 1 ATOM 5587 O OE2 . GLU A 1 714 ? 11.306 -41.818 45.307 1.00 48.44 ? 749 GLU A OE2 1 ATOM 5588 N N . ASP A 1 715 ? 14.995 -37.285 44.322 1.00 33.44 ? 750 ASP A N 1 ATOM 5589 C CA . ASP A 1 715 ? 16.105 -37.006 45.240 1.00 36.60 ? 750 ASP A CA 1 ATOM 5590 C C . ASP A 1 715 ? 16.116 -35.574 45.769 1.00 35.02 ? 750 ASP A C 1 ATOM 5591 O O . ASP A 1 715 ? 16.672 -35.327 46.840 1.00 34.99 ? 750 ASP A O 1 ATOM 5592 C CB . ASP A 1 715 ? 17.464 -37.368 44.618 1.00 42.19 ? 750 ASP A CB 1 ATOM 5593 C CG . ASP A 1 715 ? 17.853 -38.849 44.840 1.00 48.03 ? 750 ASP A CG 1 ATOM 5594 O OD1 . ASP A 1 715 ? 16.966 -39.733 44.921 1.00 51.96 ? 750 ASP A OD1 1 ATOM 5595 O OD2 . ASP A 1 715 ? 19.065 -39.138 44.938 1.00 57.29 ? 750 ASP A OD2 1 ATOM 5596 N N . GLU A 1 716 ? 15.503 -34.639 45.042 1.00 31.18 ? 751 GLU A N 1 ATOM 5597 C CA . GLU A 1 716 ? 15.409 -33.249 45.503 1.00 30.42 ? 751 GLU A CA 1 ATOM 5598 C C . GLU A 1 716 ? 14.298 -32.985 46.531 1.00 29.33 ? 751 GLU A C 1 ATOM 5599 O O . GLU A 1 716 ? 14.290 -31.941 47.163 1.00 28.13 ? 751 GLU A O 1 ATOM 5600 C CB . GLU A 1 716 ? 15.287 -32.312 44.304 1.00 30.17 ? 751 GLU A CB 1 ATOM 5601 C CG . GLU A 1 716 ? 16.603 -32.231 43.548 1.00 32.52 ? 751 GLU A CG 1 ATOM 5602 C CD . GLU A 1 716 ? 16.484 -31.624 42.166 1.00 32.02 ? 751 GLU A CD 1 ATOM 5603 O OE1 . GLU A 1 716 ? 15.386 -31.629 41.574 1.00 28.55 ? 751 GLU A OE1 1 ATOM 5604 O OE2 . GLU A 1 716 ? 17.524 -31.169 41.666 1.00 35.35 ? 751 GLU A OE2 1 ATOM 5605 N N . ILE A 1 717 ? 13.376 -33.931 46.713 1.00 29.26 ? 752 ILE A N 1 ATOM 5606 C CA . ILE A 1 717 ? 12.270 -33.751 47.663 1.00 29.19 ? 752 ILE A CA 1 ATOM 5607 C C . ILE A 1 717 ? 12.777 -33.976 49.094 1.00 31.14 ? 752 ILE A C 1 ATOM 5608 O O . ILE A 1 717 ? 13.344 -35.004 49.393 1.00 31.65 ? 752 ILE A O 1 ATOM 5609 C CB . ILE A 1 717 ? 11.068 -34.636 47.268 1.00 30.88 ? 752 ILE A CB 1 ATOM 5610 C CG1 . ILE A 1 717 ? 10.444 -34.058 45.981 1.00 31.06 ? 752 ILE A CG1 1 ATOM 5611 C CG2 . ILE A 1 717 ? 10.059 -34.732 48.412 1.00 31.53 ? 752 ILE A CG2 1 ATOM 5612 C CD1 . ILE A 1 717 ? 9.436 -34.955 45.289 1.00 32.95 ? 752 ILE A CD1 1 ATOM 5613 N N . LYS A 1 718 ? 12.576 -32.995 49.973 1.00 32.59 ? 753 LYS A N 1 ATOM 5614 C CA . LYS A 1 718 ? 13.231 -33.005 51.294 1.00 33.33 ? 753 LYS A CA 1 ATOM 5615 C C . LYS A 1 718 ? 12.310 -33.236 52.476 1.00 33.17 ? 753 LYS A C 1 ATOM 5616 O O . LYS A 1 718 ? 12.770 -33.198 53.607 1.00 34.28 ? 753 LYS A O 1 ATOM 5617 C CB . LYS A 1 718 ? 14.010 -31.707 51.506 1.00 33.95 ? 753 LYS A CB 1 ATOM 5618 C CG . LYS A 1 718 ? 15.114 -31.464 50.485 1.00 33.94 ? 753 LYS A CG 1 ATOM 5619 C CD . LYS A 1 718 ? 16.145 -32.589 50.481 1.00 36.16 ? 753 LYS A CD 1 ATOM 5620 C CE . LYS A 1 718 ? 17.313 -32.241 49.583 1.00 37.15 ? 753 LYS A CE 1 ATOM 5621 N NZ . LYS A 1 718 ? 18.176 -33.425 49.351 1.00 38.74 ? 753 LYS A NZ 1 ATOM 5622 N N . GLN A 1 719 ? 11.026 -33.475 52.241 1.00 31.16 ? 754 GLN A N 1 ATOM 5623 C CA . GLN A 1 719 ? 10.120 -33.734 53.349 1.00 32.11 ? 754 GLN A CA 1 ATOM 5624 C C . GLN A 1 719 ? 9.014 -34.686 52.928 1.00 30.23 ? 754 GLN A C 1 ATOM 5625 O O . GLN A 1 719 ? 8.461 -34.566 51.836 1.00 25.48 ? 754 GLN A O 1 ATOM 5626 C CB . GLN A 1 719 ? 9.546 -32.425 53.854 1.00 32.61 ? 754 GLN A CB 1 ATOM 5627 C CG . GLN A 1 719 ? 8.713 -32.571 55.107 1.00 37.03 ? 754 GLN A CG 1 ATOM 5628 C CD . GLN A 1 719 ? 8.048 -31.273 55.471 1.00 39.74 ? 754 GLN A CD 1 ATOM 5629 O OE1 . GLN A 1 719 ? 8.521 -30.196 55.082 1.00 43.75 ? 754 GLN A OE1 1 ATOM 5630 N NE2 . GLN A 1 719 ? 6.946 -31.355 56.208 1.00 40.17 ? 754 GLN A NE2 1 ATOM 5631 N N . TYR A 1 720 ? 8.718 -35.637 53.818 1.00 28.98 ? 755 TYR A N 1 ATOM 5632 C CA . TYR A 1 720 ? 7.695 -36.629 53.598 1.00 30.29 ? 755 TYR A CA 1 ATOM 5633 C C . TYR A 1 720 ? 6.787 -36.655 54.815 1.00 29.91 ? 755 TYR A C 1 ATOM 5634 O O . TYR A 1 720 ? 7.158 -36.172 55.880 1.00 29.50 ? 755 TYR A O 1 ATOM 5635 C CB . TYR A 1 720 ? 8.327 -38.015 53.392 1.00 32.51 ? 755 TYR A CB 1 ATOM 5636 C CG . TYR A 1 720 ? 9.128 -38.105 52.109 1.00 32.05 ? 755 TYR A CG 1 ATOM 5637 C CD1 . TYR A 1 720 ? 10.434 -37.628 52.047 1.00 33.55 ? 755 TYR A CD1 1 ATOM 5638 C CD2 . TYR A 1 720 ? 8.577 -38.653 50.969 1.00 33.00 ? 755 TYR A CD2 1 ATOM 5639 C CE1 . TYR A 1 720 ? 11.162 -37.685 50.870 1.00 34.20 ? 755 TYR A CE1 1 ATOM 5640 C CE2 . TYR A 1 720 ? 9.294 -38.726 49.783 1.00 35.79 ? 755 TYR A CE2 1 ATOM 5641 C CZ . TYR A 1 720 ? 10.589 -38.235 49.737 1.00 36.03 ? 755 TYR A CZ 1 ATOM 5642 O OH . TYR A 1 720 ? 11.306 -38.311 48.562 1.00 35.36 ? 755 TYR A OH 1 ATOM 5643 N N . VAL A 1 721 ? 5.594 -37.197 54.638 1.00 29.48 ? 756 VAL A N 1 ATOM 5644 C CA . VAL A 1 721 ? 4.700 -37.469 55.768 1.00 30.77 ? 756 VAL A CA 1 ATOM 5645 C C . VAL A 1 721 ? 5.417 -38.490 56.669 1.00 33.39 ? 756 VAL A C 1 ATOM 5646 O O . VAL A 1 721 ? 5.915 -39.487 56.162 1.00 33.51 ? 756 VAL A O 1 ATOM 5647 C CB . VAL A 1 721 ? 3.329 -37.997 55.292 1.00 30.45 ? 756 VAL A CB 1 ATOM 5648 C CG1 . VAL A 1 721 ? 2.408 -38.295 56.470 1.00 31.63 ? 756 VAL A CG1 1 ATOM 5649 C CG2 . VAL A 1 721 ? 2.659 -36.972 54.363 1.00 30.09 ? 756 VAL A CG2 1 ATOM 5650 N N . GLU A 1 722 ? 5.517 -38.190 57.969 1.00 35.90 ? 757 GLU A N 1 ATOM 5651 C CA . GLU A 1 722 ? 6.164 -39.067 58.977 1.00 41.59 ? 757 GLU A CA 1 ATOM 5652 C C . GLU A 1 722 ? 6.157 -40.562 58.657 1.00 38.85 ? 757 GLU A C 1 ATOM 5653 O O . GLU A 1 722 ? 5.101 -41.143 58.488 1.00 39.68 ? 757 GLU A O 1 ATOM 5654 C CB . GLU A 1 722 ? 5.493 -38.891 60.346 1.00 46.64 ? 757 GLU A CB 1 ATOM 5655 C CG . GLU A 1 722 ? 6.176 -37.887 61.254 1.00 51.36 ? 757 GLU A CG 1 ATOM 5656 C CD . GLU A 1 722 ? 7.329 -38.504 62.016 1.00 56.20 ? 757 GLU A CD 1 ATOM 5657 O OE1 . GLU A 1 722 ? 8.479 -38.060 61.816 1.00 60.72 ? 757 GLU A OE1 1 ATOM 5658 O OE2 . GLU A 1 722 ? 7.083 -39.440 62.807 1.00 61.53 ? 757 GLU A OE2 1 ATOM 5659 N N . GLY A 1 723 ? 7.336 -41.163 58.549 1.00 39.86 ? 758 GLY A N 1 ATOM 5660 C CA . GLY A 1 723 ? 7.467 -42.619 58.405 1.00 40.70 ? 758 GLY A CA 1 ATOM 5661 C C . GLY A 1 723 ? 7.051 -43.213 57.066 1.00 39.96 ? 758 GLY A C 1 ATOM 5662 O O . GLY A 1 723 ? 7.020 -44.434 56.931 1.00 40.47 ? 758 GLY A O 1 ATOM 5663 N N . SER A 1 724 ? 6.747 -42.366 56.076 1.00 36.53 ? 759 SER A N 1 ATOM 5664 C CA . SER A 1 724 ? 6.181 -42.804 54.799 1.00 36.06 ? 759 SER A CA 1 ATOM 5665 C C . SER A 1 724 ? 7.037 -42.313 53.650 1.00 34.49 ? 759 SER A C 1 ATOM 5666 O O . SER A 1 724 ? 7.961 -41.541 53.844 1.00 35.45 ? 759 SER A O 1 ATOM 5667 C CB . SER A 1 724 ? 4.778 -42.221 54.617 1.00 35.63 ? 759 SER A CB 1 ATOM 5668 O OG . SER A 1 724 ? 4.850 -40.830 54.319 1.00 32.72 ? 759 SER A OG 1 ATOM 5669 N N . SER A 1 725 ? 6.699 -42.751 52.450 1.00 35.90 ? 760 SER A N 1 ATOM 5670 C CA . SER A 1 725 ? 7.278 -42.190 51.232 1.00 36.65 ? 760 SER A CA 1 ATOM 5671 C C . SER A 1 725 ? 6.287 -41.256 50.533 1.00 34.07 ? 760 SER A C 1 ATOM 5672 O O . SER A 1 725 ? 6.381 -41.055 49.327 1.00 33.54 ? 760 SER A O 1 ATOM 5673 C CB . SER A 1 725 ? 7.727 -43.315 50.290 1.00 41.33 ? 760 SER A CB 1 ATOM 5674 O OG . SER A 1 725 ? 6.615 -44.033 49.768 1.00 45.43 ? 760 SER A OG 1 ATOM 5675 N N . ILE A 1 726 ? 5.360 -40.657 51.284 1.00 32.12 ? 761 ILE A N 1 ATOM 5676 C CA . ILE A 1 726 ? 4.403 -39.717 50.701 1.00 29.39 ? 761 ILE A CA 1 ATOM 5677 C C . ILE A 1 726 ? 5.116 -38.352 50.732 1.00 27.41 ? 761 ILE A C 1 ATOM 5678 O O . ILE A 1 726 ? 5.324 -37.799 51.799 1.00 27.04 ? 761 ILE A O 1 ATOM 5679 C CB . ILE A 1 726 ? 3.073 -39.647 51.492 1.00 30.48 ? 761 ILE A CB 1 ATOM 5680 C CG1 . ILE A 1 726 ? 2.464 -41.040 51.746 1.00 32.21 ? 761 ILE A CG1 1 ATOM 5681 C CG2 . ILE A 1 726 ? 2.069 -38.752 50.765 1.00 30.26 ? 761 ILE A CG2 1 ATOM 5682 C CD1 . ILE A 1 726 ? 1.334 -41.029 52.763 1.00 31.77 ? 761 ILE A CD1 1 ATOM 5683 N N . PRO A 1 727 ? 5.525 -37.821 49.569 1.00 26.22 ? 762 PRO A N 1 ATOM 5684 C CA . PRO A 1 727 ? 6.249 -36.541 49.577 1.00 24.46 ? 762 PRO A CA 1 ATOM 5685 C C . PRO A 1 727 ? 5.313 -35.369 49.882 1.00 22.83 ? 762 PRO A C 1 ATOM 5686 O O . PRO A 1 727 ? 4.133 -35.411 49.531 1.00 23.08 ? 762 PRO A O 1 ATOM 5687 C CB . PRO A 1 727 ? 6.758 -36.441 48.145 1.00 24.69 ? 762 PRO A CB 1 ATOM 5688 C CG . PRO A 1 727 ? 5.644 -37.061 47.347 1.00 24.76 ? 762 PRO A CG 1 ATOM 5689 C CD . PRO A 1 727 ? 5.147 -38.207 48.198 1.00 26.50 ? 762 PRO A CD 1 ATOM 5690 N N . VAL A 1 728 ? 5.845 -34.329 50.508 1.00 21.58 ? 763 VAL A N 1 ATOM 5691 C CA . VAL A 1 728 ? 5.061 -33.141 50.858 1.00 20.93 ? 763 VAL A CA 1 ATOM 5692 C C . VAL A 1 728 ? 5.241 -32.064 49.781 1.00 20.18 ? 763 VAL A C 1 ATOM 5693 O O . VAL A 1 728 ? 6.379 -31.612 49.565 1.00 20.45 ? 763 VAL A O 1 ATOM 5694 C CB . VAL A 1 728 ? 5.500 -32.570 52.223 1.00 21.53 ? 763 VAL A CB 1 ATOM 5695 C CG1 . VAL A 1 728 ? 4.639 -31.363 52.579 1.00 22.06 ? 763 VAL A CG1 1 ATOM 5696 C CG2 . VAL A 1 728 ? 5.391 -33.649 53.295 1.00 22.97 ? 763 VAL A CG2 1 ATOM 5697 N N . PRO A 1 729 ? 4.143 -31.643 49.115 1.00 18.91 ? 764 PRO A N 1 ATOM 5698 C CA . PRO A 1 729 ? 4.294 -30.544 48.155 1.00 18.01 ? 764 PRO A CA 1 ATOM 5699 C C . PRO A 1 729 ? 4.758 -29.233 48.802 1.00 17.34 ? 764 PRO A C 1 ATOM 5700 O O . PRO A 1 729 ? 4.398 -28.923 49.935 1.00 16.22 ? 764 PRO A O 1 ATOM 5701 C CB . PRO A 1 729 ? 2.890 -30.400 47.573 1.00 16.95 ? 764 PRO A CB 1 ATOM 5702 C CG . PRO A 1 729 ? 2.319 -31.783 47.705 1.00 17.73 ? 764 PRO A CG 1 ATOM 5703 C CD . PRO A 1 729 ? 2.771 -32.170 49.067 1.00 18.51 ? 764 PRO A CD 1 ATOM 5704 N N . THR A 1 730 ? 5.556 -28.478 48.066 1.00 16.61 ? 765 THR A N 1 ATOM 5705 C CA . THR A 1 730 ? 5.885 -27.117 48.445 1.00 15.69 ? 765 THR A CA 1 ATOM 5706 C C . THR A 1 730 ? 4.737 -26.152 48.111 1.00 15.06 ? 765 THR A C 1 ATOM 5707 O O . THR A 1 730 ? 4.602 -25.109 48.752 1.00 14.80 ? 765 THR A O 1 ATOM 5708 C CB . THR A 1 730 ? 7.217 -26.640 47.826 1.00 15.54 ? 765 THR A CB 1 ATOM 5709 O OG1 . THR A 1 730 ? 7.130 -26.723 46.398 1.00 15.10 ? 765 THR A OG1 1 ATOM 5710 C CG2 . THR A 1 730 ? 8.402 -27.459 48.339 1.00 17.27 ? 765 THR A CG2 1 ATOM 5711 N N . HIS A 1 731 ? 3.922 -26.485 47.097 1.00 14.45 ? 766 HIS A N 1 ATOM 5712 C CA . HIS A 1 731 ? 2.840 -25.635 46.616 1.00 14.00 ? 766 HIS A CA 1 ATOM 5713 C C . HIS A 1 731 ? 1.735 -26.490 46.057 1.00 14.33 ? 766 HIS A C 1 ATOM 5714 O O . HIS A 1 731 ? 1.960 -27.652 45.747 1.00 14.98 ? 766 HIS A O 1 ATOM 5715 C CB . HIS A 1 731 ? 3.325 -24.736 45.444 1.00 13.38 ? 766 HIS A CB 1 ATOM 5716 C CG . HIS A 1 731 ? 4.449 -23.811 45.807 1.00 14.32 ? 766 HIS A CG 1 ATOM 5717 N ND1 . HIS A 1 731 ? 5.752 -24.245 45.940 1.00 13.89 ? 766 HIS A ND1 1 ATOM 5718 C CD2 . HIS A 1 731 ? 4.461 -22.489 46.101 1.00 14.13 ? 766 HIS A CD2 1 ATOM 5719 C CE1 . HIS A 1 731 ? 6.519 -23.230 46.280 1.00 14.21 ? 766 HIS A CE1 1 ATOM 5720 N NE2 . HIS A 1 731 ? 5.764 -22.150 46.372 1.00 14.11 ? 766 HIS A NE2 1 ATOM 5721 N N . TYR A 1 732 ? 0.554 -25.889 45.900 1.00 13.44 ? 767 TYR A N 1 ATOM 5722 C CA . TYR A 1 732 ? -0.583 -26.499 45.215 1.00 14.92 ? 767 TYR A CA 1 ATOM 5723 C C . TYR A 1 732 ? -1.043 -25.540 44.113 1.00 14.74 ? 767 TYR A C 1 ATOM 5724 O O . TYR A 1 732 ? -1.212 -24.323 44.351 1.00 15.24 ? 767 TYR A O 1 ATOM 5725 C CB . TYR A 1 732 ? -1.724 -26.833 46.189 1.00 15.68 ? 767 TYR A CB 1 ATOM 5726 C CG . TYR A 1 732 ? -1.466 -28.123 46.967 1.00 15.50 ? 767 TYR A CG 1 ATOM 5727 C CD1 . TYR A 1 732 ? -1.713 -29.363 46.386 1.00 17.35 ? 767 TYR A CD1 1 ATOM 5728 C CD2 . TYR A 1 732 ? -0.917 -28.103 48.264 1.00 16.65 ? 767 TYR A CD2 1 ATOM 5729 C CE1 . TYR A 1 732 ? -1.448 -30.548 47.068 1.00 17.79 ? 767 TYR A CE1 1 ATOM 5730 C CE2 . TYR A 1 732 ? -0.677 -29.277 48.974 1.00 17.54 ? 767 TYR A CE2 1 ATOM 5731 C CZ . TYR A 1 732 ? -0.930 -30.503 48.355 1.00 17.60 ? 767 TYR A CZ 1 ATOM 5732 O OH . TYR A 1 732 ? -0.689 -31.672 49.025 1.00 18.29 ? 767 TYR A OH 1 ATOM 5733 N N . TYR A 1 733 ? -1.244 -26.050 42.902 1.00 15.24 ? 768 TYR A N 1 ATOM 5734 C CA . TYR A 1 733 ? -1.682 -25.184 41.813 1.00 14.78 ? 768 TYR A CA 1 ATOM 5735 C C . TYR A 1 733 ? -3.137 -25.431 41.450 1.00 15.51 ? 768 TYR A C 1 ATOM 5736 O O . TYR A 1 733 ? -3.694 -26.492 41.748 1.00 15.08 ? 768 TYR A O 1 ATOM 5737 C CB . TYR A 1 733 ? -0.795 -25.375 40.554 1.00 14.10 ? 768 TYR A CB 1 ATOM 5738 C CG . TYR A 1 733 ? -0.996 -26.674 39.817 1.00 15.06 ? 768 TYR A CG 1 ATOM 5739 C CD1 . TYR A 1 733 ? -1.998 -26.801 38.851 1.00 15.56 ? 768 TYR A CD1 1 ATOM 5740 C CD2 . TYR A 1 733 ? -0.176 -27.790 40.064 1.00 15.56 ? 768 TYR A CD2 1 ATOM 5741 C CE1 . TYR A 1 733 ? -2.205 -27.996 38.198 1.00 15.29 ? 768 TYR A CE1 1 ATOM 5742 C CE2 . TYR A 1 733 ? -0.377 -28.982 39.392 1.00 16.86 ? 768 TYR A CE2 1 ATOM 5743 C CZ . TYR A 1 733 ? -1.404 -29.074 38.467 1.00 15.67 ? 768 TYR A CZ 1 ATOM 5744 O OH . TYR A 1 733 ? -1.627 -30.229 37.774 1.00 17.63 ? 768 TYR A OH 1 ATOM 5745 N N . SER A 1 734 ? -3.729 -24.452 40.782 1.00 15.35 ? 769 SER A N 1 ATOM 5746 C CA . SER A 1 734 ? -4.955 -24.666 40.022 1.00 16.66 ? 769 SER A CA 1 ATOM 5747 C C . SER A 1 734 ? -4.953 -23.778 38.794 1.00 16.47 ? 769 SER A C 1 ATOM 5748 O O . SER A 1 734 ? -4.469 -22.637 38.867 1.00 15.98 ? 769 SER A O 1 ATOM 5749 C CB . SER A 1 734 ? -6.183 -24.360 40.841 1.00 18.06 ? 769 SER A CB 1 ATOM 5750 O OG . SER A 1 734 ? -6.299 -25.279 41.887 1.00 22.82 ? 769 SER A OG 1 ATOM 5751 N N . ILE A 1 735 ? -5.484 -24.313 37.695 1.00 14.72 ? 770 ILE A N 1 ATOM 5752 C CA . ILE A 1 735 ? -5.658 -23.592 36.437 1.00 14.41 ? 770 ILE A CA 1 ATOM 5753 C C . ILE A 1 735 ? -7.142 -23.599 36.142 1.00 15.55 ? 770 ILE A C 1 ATOM 5754 O O . ILE A 1 735 ? -7.747 -24.684 36.018 1.00 16.85 ? 770 ILE A O 1 ATOM 5755 C CB . ILE A 1 735 ? -4.932 -24.306 35.309 1.00 14.97 ? 770 ILE A CB 1 ATOM 5756 C CG1 . ILE A 1 735 ? -3.430 -24.385 35.594 1.00 15.31 ? 770 ILE A CG1 1 ATOM 5757 C CG2 . ILE A 1 735 ? -5.225 -23.632 33.957 1.00 15.19 ? 770 ILE A CG2 1 ATOM 5758 C CD1 . ILE A 1 735 ? -2.693 -25.386 34.729 1.00 16.78 ? 770 ILE A CD1 1 ATOM 5759 N N . ILE A 1 736 ? -7.725 -22.411 36.055 1.00 15.22 ? 771 ILE A N 1 ATOM 5760 C CA . ILE A 1 736 ? -9.163 -22.240 35.958 1.00 17.22 ? 771 ILE A CA 1 ATOM 5761 C C . ILE A 1 736 ? -9.480 -21.614 34.609 1.00 17.21 ? 771 ILE A C 1 ATOM 5762 O O . ILE A 1 736 ? -9.181 -20.444 34.380 1.00 16.99 ? 771 ILE A O 1 ATOM 5763 C CB . ILE A 1 736 ? -9.695 -21.408 37.121 1.00 18.08 ? 771 ILE A CB 1 ATOM 5764 C CG1 . ILE A 1 736 ? -9.209 -22.037 38.454 1.00 19.27 ? 771 ILE A CG1 1 ATOM 5765 C CG2 . ILE A 1 736 ? -11.216 -21.323 37.073 1.00 18.26 ? 771 ILE A CG2 1 ATOM 5766 C CD1 . ILE A 1 736 ? -9.642 -21.339 39.698 1.00 21.23 ? 771 ILE A CD1 1 ATOM 5767 N N . THR A 1 737 ? -10.094 -22.405 33.719 1.00 16.27 ? 772 THR A N 1 ATOM 5768 C CA . THR A 1 737 ? -10.294 -22.002 32.334 1.00 17.62 ? 772 THR A CA 1 ATOM 5769 C C . THR A 1 737 ? -11.798 -21.889 32.042 1.00 18.36 ? 772 THR A C 1 ATOM 5770 O O . THR A 1 737 ? -12.597 -22.616 32.614 1.00 17.20 ? 772 THR A O 1 ATOM 5771 C CB . THR A 1 737 ? -9.665 -23.014 31.354 1.00 18.60 ? 772 THR A CB 1 ATOM 5772 O OG1 . THR A 1 737 ? -8.338 -23.373 31.769 1.00 18.15 ? 772 THR A OG1 1 ATOM 5773 C CG2 . THR A 1 737 ? -9.642 -22.451 29.919 1.00 19.68 ? 772 THR A CG2 1 ATOM 5774 N N . SER A 1 738 ? -12.173 -20.922 31.211 1.00 16.87 ? 773 SER A N 1 ATOM 5775 C CA . SER A 1 738 ? -13.534 -20.753 30.750 1.00 18.21 ? 773 SER A CA 1 ATOM 5776 C C . SER A 1 738 ? -13.497 -20.128 29.341 1.00 19.31 ? 773 SER A C 1 ATOM 5777 O O . SER A 1 738 ? -12.418 -19.958 28.739 1.00 17.74 ? 773 SER A O 1 ATOM 5778 C CB . SER A 1 738 ? -14.313 -19.887 31.742 1.00 18.83 ? 773 SER A CB 1 ATOM 5779 O OG . SER A 1 738 ? -13.729 -18.595 31.838 1.00 19.50 ? 773 SER A OG 1 ATOM 5780 N N . CYS A 1 739 ? -14.660 -19.800 28.809 1.00 18.80 ? 774 CYS A N 1 ATOM 5781 C CA . CYS A 1 739 ? -14.730 -19.195 27.476 1.00 19.21 ? 774 CYS A CA 1 ATOM 5782 C C . CYS A 1 739 ? -14.533 -17.698 27.579 1.00 19.14 ? 774 CYS A C 1 ATOM 5783 O O . CYS A 1 739 ? -15.236 -17.036 28.342 1.00 20.09 ? 774 CYS A O 1 ATOM 5784 C CB . CYS A 1 739 ? -16.100 -19.487 26.858 1.00 21.27 ? 774 CYS A CB 1 ATOM 5785 S SG . CYS A 1 739 ? -16.138 -19.337 25.067 1.00 22.66 ? 774 CYS A SG 1 ATOM 5786 N N . LEU A 1 740 ? -13.653 -17.131 26.742 1.00 19.02 ? 775 LEU A N 1 ATOM 5787 C CA . LEU A 1 740 ? -13.493 -15.674 26.744 1.00 19.92 ? 775 LEU A CA 1 ATOM 5788 C C . LEU A 1 740 ? -14.831 -14.992 26.403 1.00 20.42 ? 775 LEU A C 1 ATOM 5789 O O . LEU A 1 740 ? -15.196 -14.000 27.024 1.00 21.91 ? 775 LEU A O 1 ATOM 5790 C CB . LEU A 1 740 ? -12.361 -15.244 25.806 1.00 21.40 ? 775 LEU A CB 1 ATOM 5791 C CG . LEU A 1 740 ? -11.990 -13.762 25.844 1.00 23.06 ? 775 LEU A CG 1 ATOM 5792 C CD1 . LEU A 1 740 ? -11.403 -13.362 27.187 1.00 23.98 ? 775 LEU A CD1 1 ATOM 5793 C CD2 . LEU A 1 740 ? -11.017 -13.479 24.713 1.00 25.90 ? 775 LEU A CD2 1 ATOM 5794 N N . ASP A 1 741 ? -15.563 -15.545 25.439 1.00 20.33 ? 776 ASP A N 1 ATOM 5795 C CA . ASP A 1 741 ? -16.947 -15.159 25.185 1.00 21.31 ? 776 ASP A CA 1 ATOM 5796 C C . ASP A 1 741 ? -17.805 -15.811 26.273 1.00 20.83 ? 776 ASP A C 1 ATOM 5797 O O . ASP A 1 741 ? -18.230 -16.959 26.155 1.00 20.16 ? 776 ASP A O 1 ATOM 5798 C CB . ASP A 1 741 ? -17.382 -15.608 23.779 1.00 22.68 ? 776 ASP A CB 1 ATOM 5799 C CG . ASP A 1 741 ? -18.836 -15.311 23.479 1.00 23.70 ? 776 ASP A CG 1 ATOM 5800 O OD1 . ASP A 1 741 ? -19.545 -14.661 24.301 1.00 23.36 ? 776 ASP A OD1 1 ATOM 5801 O OD2 . ASP A 1 741 ? -19.279 -15.737 22.386 1.00 23.67 ? 776 ASP A OD2 1 ATOM 5802 N N . PHE A 1 742 ? -18.053 -15.046 27.326 1.00 21.21 ? 777 PHE A N 1 ATOM 5803 C CA . PHE A 1 742 ? -18.860 -15.490 28.467 1.00 21.55 ? 777 PHE A CA 1 ATOM 5804 C C . PHE A 1 742 ? -20.326 -15.821 28.153 1.00 22.89 ? 777 PHE A C 1 ATOM 5805 O O . PHE A 1 742 ? -21.034 -16.343 29.024 1.00 23.67 ? 777 PHE A O 1 ATOM 5806 C CB . PHE A 1 742 ? -18.798 -14.453 29.603 1.00 22.03 ? 777 PHE A CB 1 ATOM 5807 C CG . PHE A 1 742 ? -19.238 -13.077 29.195 1.00 23.04 ? 777 PHE A CG 1 ATOM 5808 C CD1 . PHE A 1 742 ? -20.584 -12.745 29.150 1.00 24.67 ? 777 PHE A CD1 1 ATOM 5809 C CD2 . PHE A 1 742 ? -18.296 -12.101 28.856 1.00 23.50 ? 777 PHE A CD2 1 ATOM 5810 C CE1 . PHE A 1 742 ? -20.989 -11.490 28.760 1.00 25.71 ? 777 PHE A CE1 1 ATOM 5811 C CE2 . PHE A 1 742 ? -18.703 -10.841 28.462 1.00 24.29 ? 777 PHE A CE2 1 ATOM 5812 C CZ . PHE A 1 742 ? -20.047 -10.535 28.423 1.00 27.04 ? 777 PHE A CZ 1 ATOM 5813 N N . THR A 1 743 ? -20.808 -15.478 26.955 1.00 22.63 ? 778 THR A N 1 ATOM 5814 C CA . THR A 1 743 ? -22.157 -15.904 26.531 1.00 24.05 ? 778 THR A CA 1 ATOM 5815 C C . THR A 1 743 ? -22.210 -17.398 26.203 1.00 24.69 ? 778 THR A C 1 ATOM 5816 O O . THR A 1 743 ? -23.291 -17.933 26.013 1.00 26.37 ? 778 THR A O 1 ATOM 5817 C CB . THR A 1 743 ? -22.711 -15.096 25.348 1.00 24.49 ? 778 THR A CB 1 ATOM 5818 O OG1 . THR A 1 743 ? -21.996 -15.417 24.152 1.00 23.84 ? 778 THR A OG1 1 ATOM 5819 C CG2 . THR A 1 743 ? -22.638 -13.608 25.606 1.00 24.23 ? 778 THR A CG2 1 ATOM 5820 N N . GLN A 1 744 ? -21.045 -18.048 26.101 1.00 24.10 ? 779 GLN A N 1 ATOM 5821 C CA . GLN A 1 744 ? -20.948 -19.482 25.910 1.00 24.27 ? 779 GLN A CA 1 ATOM 5822 C C . GLN A 1 744 ? -20.459 -20.156 27.188 1.00 23.72 ? 779 GLN A C 1 ATOM 5823 O O . GLN A 1 744 ? -19.517 -19.663 27.856 1.00 23.37 ? 779 GLN A O 1 ATOM 5824 C CB . GLN A 1 744 ? -20.001 -19.803 24.737 1.00 24.90 ? 779 GLN A CB 1 ATOM 5825 C CG . GLN A 1 744 ? -20.499 -19.279 23.405 1.00 27.30 ? 779 GLN A CG 1 ATOM 5826 C CD . GLN A 1 744 ? -19.712 -19.816 22.212 1.00 29.15 ? 779 GLN A CD 1 ATOM 5827 O OE1 . GLN A 1 744 ? -18.540 -20.137 22.323 1.00 27.62 ? 779 GLN A OE1 1 ATOM 5828 N NE2 . GLN A 1 744 ? -20.374 -19.918 21.062 1.00 30.85 ? 779 GLN A NE2 1 ATOM 5829 N N . PRO A 1 745 ? -21.073 -21.295 27.552 1.00 23.63 ? 780 PRO A N 1 ATOM 5830 C CA . PRO A 1 745 ? -20.598 -21.996 28.733 1.00 23.79 ? 780 PRO A CA 1 ATOM 5831 C C . PRO A 1 745 ? -19.220 -22.604 28.501 1.00 23.22 ? 780 PRO A C 1 ATOM 5832 O O . PRO A 1 745 ? -18.850 -22.833 27.358 1.00 23.00 ? 780 PRO A O 1 ATOM 5833 C CB . PRO A 1 745 ? -21.660 -23.073 28.963 1.00 24.81 ? 780 PRO A CB 1 ATOM 5834 C CG . PRO A 1 745 ? -22.241 -23.295 27.636 1.00 26.74 ? 780 PRO A CG 1 ATOM 5835 C CD . PRO A 1 745 ? -22.218 -21.981 26.929 1.00 26.24 ? 780 PRO A CD 1 ATOM 5836 N N . ALA A 1 746 ? -18.467 -22.852 29.572 1.00 23.23 ? 781 ALA A N 1 ATOM 5837 C CA . ALA A 1 746 ? -17.080 -23.339 29.437 1.00 22.19 ? 781 ALA A CA 1 ATOM 5838 C C . ALA A 1 746 ? -16.979 -24.643 28.625 1.00 24.70 ? 781 ALA A C 1 ATOM 5839 O O . ALA A 1 746 ? -16.014 -24.848 27.876 1.00 23.01 ? 781 ALA A O 1 ATOM 5840 C CB . ALA A 1 746 ? -16.431 -23.510 30.792 1.00 22.47 ? 781 ALA A CB 1 ATOM 5841 N N . ASP A 1 747 ? -17.996 -25.496 28.719 1.00 26.43 ? 782 ASP A N 1 ATOM 5842 C CA . ASP A 1 747 ? -17.974 -26.779 28.033 1.00 29.60 ? 782 ASP A CA 1 ATOM 5843 C C . ASP A 1 747 ? -18.450 -26.725 26.563 1.00 31.54 ? 782 ASP A C 1 ATOM 5844 O O . ASP A 1 747 ? -18.452 -27.752 25.903 1.00 35.30 ? 782 ASP A O 1 ATOM 5845 C CB . ASP A 1 747 ? -18.769 -27.816 28.830 1.00 33.56 ? 782 ASP A CB 1 ATOM 5846 C CG . ASP A 1 747 ? -20.276 -27.616 28.744 1.00 35.95 ? 782 ASP A CG 1 ATOM 5847 O OD1 . ASP A 1 747 ? -20.756 -26.491 28.472 1.00 36.94 ? 782 ASP A OD1 1 ATOM 5848 O OD2 . ASP A 1 747 ? -20.990 -28.606 28.972 1.00 43.90 ? 782 ASP A OD2 1 ATOM 5849 N N . LYS A 1 748 ? -18.859 -25.556 26.061 1.00 31.86 ? 783 LYS A N 1 ATOM 5850 C CA . LYS A 1 748 ? -19.313 -25.405 24.672 1.00 34.22 ? 783 LYS A CA 1 ATOM 5851 C C . LYS A 1 748 ? -18.775 -24.102 24.082 1.00 32.34 ? 783 LYS A C 1 ATOM 5852 O O . LYS A 1 748 ? -19.521 -23.309 23.506 1.00 34.26 ? 783 LYS A O 1 ATOM 5853 C CB . LYS A 1 748 ? -20.848 -25.435 24.614 1.00 38.28 ? 783 LYS A CB 1 ATOM 5854 C CG . LYS A 1 748 ? -21.466 -26.755 25.034 1.00 42.30 ? 783 LYS A CG 1 ATOM 5855 C CD . LYS A 1 748 ? -22.980 -26.716 24.896 1.00 47.82 ? 783 LYS A CD 1 ATOM 5856 C CE . LYS A 1 748 ? -23.599 -28.100 25.023 1.00 52.20 ? 783 LYS A CE 1 ATOM 5857 N NZ . LYS A 1 748 ? -23.483 -28.683 26.391 1.00 54.18 ? 783 LYS A NZ 1 ATOM 5858 N N . CYS A 1 749 ? -17.471 -23.893 24.242 1.00 29.50 ? 784 CYS A N 1 ATOM 5859 C CA . CYS A 1 749 ? -16.808 -22.666 23.852 1.00 27.35 ? 784 CYS A CA 1 ATOM 5860 C C . CYS A 1 749 ? -16.239 -22.870 22.458 1.00 29.42 ? 784 CYS A C 1 ATOM 5861 O O . CYS A 1 749 ? -15.449 -23.790 22.260 1.00 29.92 ? 784 CYS A O 1 ATOM 5862 C CB . CYS A 1 749 ? -15.671 -22.337 24.833 1.00 25.35 ? 784 CYS A CB 1 ATOM 5863 S SG . CYS A 1 749 ? -14.787 -20.792 24.472 1.00 27.06 ? 784 CYS A SG 1 ATOM 5864 N N . ASP A 1 750 ? -16.622 -22.004 21.518 1.00 29.76 ? 785 ASP A N 1 ATOM 5865 C CA . ASP A 1 750 ? -16.162 -22.070 20.120 1.00 31.91 ? 785 ASP A CA 1 ATOM 5866 C C . ASP A 1 750 ? -14.816 -21.429 19.875 1.00 30.38 ? 785 ASP A C 1 ATOM 5867 O O . ASP A 1 750 ? -14.152 -21.751 18.878 1.00 32.25 ? 785 ASP A O 1 ATOM 5868 C CB . ASP A 1 750 ? -17.141 -21.331 19.183 1.00 33.95 ? 785 ASP A CB 1 ATOM 5869 C CG . ASP A 1 750 ? -18.442 -22.052 18.990 1.00 37.53 ? 785 ASP A CG 1 ATOM 5870 O OD1 . ASP A 1 750 ? -18.494 -23.284 19.169 1.00 38.75 ? 785 ASP A OD1 1 ATOM 5871 O OD2 . ASP A 1 750 ? -19.430 -21.374 18.628 1.00 41.19 ? 785 ASP A OD2 1 ATOM 5872 N N . GLY A 1 751 ? -14.446 -20.464 20.711 1.00 25.90 ? 786 GLY A N 1 ATOM 5873 C CA . GLY A 1 751 ? -13.403 -19.530 20.366 1.00 25.67 ? 786 GLY A CA 1 ATOM 5874 C C . GLY A 1 751 ? -12.310 -19.432 21.399 1.00 22.61 ? 786 GLY A C 1 ATOM 5875 O O . GLY A 1 751 ? -12.010 -20.401 22.073 1.00 20.65 ? 786 GLY A O 1 ATOM 5876 N N . PRO A 1 752 ? -11.694 -18.246 21.525 1.00 23.79 ? 787 PRO A N 1 ATOM 5877 C CA . PRO A 1 752 ? -10.638 -18.049 22.508 1.00 20.99 ? 787 PRO A CA 1 ATOM 5878 C C . PRO A 1 752 ? -11.051 -18.378 23.953 1.00 20.52 ? 787 PRO A C 1 ATOM 5879 O O . PRO A 1 752 ? -12.219 -18.269 24.312 1.00 18.81 ? 787 PRO A O 1 ATOM 5880 C CB . PRO A 1 752 ? -10.317 -16.565 22.379 1.00 22.75 ? 787 PRO A CB 1 ATOM 5881 C CG . PRO A 1 752 ? -10.664 -16.226 20.974 1.00 24.18 ? 787 PRO A CG 1 ATOM 5882 C CD . PRO A 1 752 ? -11.875 -17.059 20.663 1.00 23.65 ? 787 PRO A CD 1 ATOM 5883 N N . LEU A 1 753 ? -10.065 -18.801 24.730 1.00 18.90 ? 788 LEU A N 1 ATOM 5884 C CA . LEU A 1 753 ? -10.202 -19.200 26.118 1.00 19.16 ? 788 LEU A CA 1 ATOM 5885 C C . LEU A 1 753 ? -9.809 -18.074 27.050 1.00 18.97 ? 788 LEU A C 1 ATOM 5886 O O . LEU A 1 753 ? -9.131 -17.139 26.659 1.00 19.47 ? 788 LEU A O 1 ATOM 5887 C CB . LEU A 1 753 ? -9.329 -20.434 26.384 1.00 20.04 ? 788 LEU A CB 1 ATOM 5888 C CG . LEU A 1 753 ? -9.658 -21.653 25.524 1.00 20.30 ? 788 LEU A CG 1 ATOM 5889 C CD1 . LEU A 1 753 ? -8.681 -22.790 25.778 1.00 20.86 ? 788 LEU A CD1 1 ATOM 5890 C CD2 . LEU A 1 753 ? -11.084 -22.089 25.763 1.00 20.92 ? 788 LEU A CD2 1 ATOM 5891 N N . SER A 1 754 ? -10.292 -18.149 28.290 1.00 18.92 ? 789 SER A N 1 ATOM 5892 C CA . SER A 1 754 ? -9.930 -17.219 29.343 1.00 18.42 ? 789 SER A CA 1 ATOM 5893 C C . SER A 1 754 ? -9.377 -18.066 30.472 1.00 17.32 ? 789 SER A C 1 ATOM 5894 O O . SER A 1 754 ? -9.979 -19.069 30.824 1.00 16.95 ? 789 SER A O 1 ATOM 5895 C CB . SER A 1 754 ? -11.171 -16.447 29.795 1.00 20.18 ? 789 SER A CB 1 ATOM 5896 O OG . SER A 1 754 ? -10.894 -15.672 30.937 1.00 20.17 ? 789 SER A OG 1 ATOM 5897 N N . VAL A 1 755 ? -8.244 -17.669 31.042 1.00 15.69 ? 790 VAL A N 1 ATOM 5898 C CA . VAL A 1 755 ? -7.601 -18.484 32.077 1.00 16.27 ? 790 VAL A CA 1 ATOM 5899 C C . VAL A 1 755 ? -7.136 -17.609 33.228 1.00 16.08 ? 790 VAL A C 1 ATOM 5900 O O . VAL A 1 755 ? -6.755 -16.471 33.030 1.00 17.14 ? 790 VAL A O 1 ATOM 5901 C CB . VAL A 1 755 ? -6.417 -19.352 31.541 1.00 16.90 ? 790 VAL A CB 1 ATOM 5902 C CG1 . VAL A 1 755 ? -5.239 -18.483 31.091 1.00 18.20 ? 790 VAL A CG1 1 ATOM 5903 C CG2 . VAL A 1 755 ? -5.935 -20.398 32.560 1.00 16.05 ? 790 VAL A CG2 1 ATOM 5904 N N . SER A 1 756 ? -7.258 -18.141 34.433 1.00 16.28 ? 791 SER A N 1 ATOM 5905 C CA . SER A 1 756 ? -6.552 -17.620 35.594 1.00 17.68 ? 791 SER A CA 1 ATOM 5906 C C . SER A 1 756 ? -5.999 -18.816 36.370 1.00 17.72 ? 791 SER A C 1 ATOM 5907 O O . SER A 1 756 ? -6.643 -19.878 36.442 1.00 17.60 ? 791 SER A O 1 ATOM 5908 C CB . SER A 1 756 ? -7.467 -16.785 36.459 1.00 19.15 ? 791 SER A CB 1 ATOM 5909 O OG . SER A 1 756 ? -8.549 -17.535 36.913 1.00 23.09 ? 791 SER A OG 1 ATOM 5910 N N . SER A 1 757 ? -4.812 -18.641 36.942 1.00 15.21 ? 792 SER A N 1 ATOM 5911 C CA . SER A 1 757 ? -4.141 -19.722 37.640 1.00 15.46 ? 792 SER A CA 1 ATOM 5912 C C . SER A 1 757 ? -3.449 -19.195 38.882 1.00 14.25 ? 792 SER A C 1 ATOM 5913 O O . SER A 1 757 ? -3.197 -18.000 39.003 1.00 13.22 ? 792 SER A O 1 ATOM 5914 C CB . SER A 1 757 ? -3.061 -20.361 36.743 1.00 17.34 ? 792 SER A CB 1 ATOM 5915 O OG . SER A 1 757 ? -3.579 -20.671 35.473 1.00 19.03 ? 792 SER A OG 1 ATOM 5916 N N . PHE A 1 758 ? -3.141 -20.126 39.774 1.00 13.96 ? 793 PHE A N 1 ATOM 5917 C CA A PHE A 1 758 ? -2.557 -19.875 41.079 0.50 13.84 ? 793 PHE A CA 1 ATOM 5918 C CA B PHE A 1 758 ? -2.395 -19.806 40.976 0.50 14.25 ? 793 PHE A CA 1 ATOM 5919 C C . PHE A 1 758 ? -1.469 -20.930 41.393 1.00 13.68 ? 793 PHE A C 1 ATOM 5920 O O . PHE A 1 758 ? -1.616 -22.086 40.992 1.00 13.50 ? 793 PHE A O 1 ATOM 5921 C CB A PHE A 1 758 ? -3.675 -19.979 42.140 0.50 14.50 ? 793 PHE A CB 1 ATOM 5922 C CB B PHE A 1 758 ? -3.309 -19.380 42.132 0.50 15.57 ? 793 PHE A CB 1 ATOM 5923 C CG A PHE A 1 758 ? -4.860 -19.062 41.896 0.50 14.94 ? 793 PHE A CG 1 ATOM 5924 C CG B PHE A 1 758 ? -4.228 -20.460 42.636 0.50 16.13 ? 793 PHE A CG 1 ATOM 5925 C CD1 A PHE A 1 758 ? -4.811 -17.733 42.284 0.50 14.16 ? 793 PHE A CD1 1 ATOM 5926 C CD1 B PHE A 1 758 ? -3.739 -21.562 43.312 0.50 16.69 ? 793 PHE A CD1 1 ATOM 5927 C CD2 A PHE A 1 758 ? -6.020 -19.529 41.294 0.50 15.40 ? 793 PHE A CD2 1 ATOM 5928 C CD2 B PHE A 1 758 ? -5.579 -20.353 42.460 0.50 17.31 ? 793 PHE A CD2 1 ATOM 5929 C CE1 A PHE A 1 758 ? -5.869 -16.881 42.074 0.50 14.19 ? 793 PHE A CE1 1 ATOM 5930 C CE1 B PHE A 1 758 ? -4.583 -22.543 43.793 0.50 17.06 ? 793 PHE A CE1 1 ATOM 5931 C CE2 A PHE A 1 758 ? -7.101 -18.684 41.074 0.50 16.24 ? 793 PHE A CE2 1 ATOM 5932 C CE2 B PHE A 1 758 ? -6.433 -21.330 42.944 0.50 16.57 ? 793 PHE A CE2 1 ATOM 5933 C CZ A PHE A 1 758 ? -7.036 -17.361 41.468 0.50 15.82 ? 793 PHE A CZ 1 ATOM 5934 C CZ B PHE A 1 758 ? -5.939 -22.418 43.616 0.50 16.67 ? 793 PHE A CZ 1 ATOM 5935 N N . ILE A 1 759 ? -0.453 -20.553 42.176 1.00 13.40 ? 794 ILE A N 1 ATOM 5936 C CA . ILE A 1 759 ? 0.495 -21.496 42.736 1.00 13.24 ? 794 ILE A CA 1 ATOM 5937 C C . ILE A 1 759 ? 0.537 -21.121 44.207 1.00 14.71 ? 794 ILE A C 1 ATOM 5938 O O . ILE A 1 759 ? 1.246 -20.192 44.585 1.00 13.93 ? 794 ILE A O 1 ATOM 5939 C CB . ILE A 1 759 ? 1.908 -21.416 42.096 1.00 13.81 ? 794 ILE A CB 1 ATOM 5940 C CG1 . ILE A 1 759 ? 1.837 -21.737 40.592 1.00 13.46 ? 794 ILE A CG1 1 ATOM 5941 C CG2 . ILE A 1 759 ? 2.863 -22.362 42.820 1.00 14.16 ? 794 ILE A CG2 1 ATOM 5942 C CD1 . ILE A 1 759 ? 3.052 -21.279 39.801 1.00 12.37 ? 794 ILE A CD1 1 ATOM 5943 N N . LEU A 1 760 ? -0.231 -21.825 45.035 1.00 15.48 ? 795 LEU A N 1 ATOM 5944 C CA . LEU A 1 760 ? -0.316 -21.460 46.446 1.00 17.16 ? 795 LEU A CA 1 ATOM 5945 C C . LEU A 1 760 ? 0.786 -22.099 47.263 1.00 16.53 ? 795 LEU A C 1 ATOM 5946 O O . LEU A 1 760 ? 0.983 -23.302 47.164 1.00 15.70 ? 795 LEU A O 1 ATOM 5947 C CB . LEU A 1 760 ? -1.644 -21.904 47.040 1.00 20.19 ? 795 LEU A CB 1 ATOM 5948 C CG . LEU A 1 760 ? -2.893 -21.390 46.340 1.00 26.39 ? 795 LEU A CG 1 ATOM 5949 C CD1 . LEU A 1 760 ? -4.182 -21.723 47.082 1.00 28.18 ? 795 LEU A CD1 1 ATOM 5950 C CD2 . LEU A 1 760 ? -2.833 -19.901 46.009 1.00 28.86 ? 795 LEU A CD2 1 ATOM 5951 N N . PRO A 1 761 ? 1.481 -21.312 48.121 1.00 16.63 ? 796 PRO A N 1 ATOM 5952 C CA . PRO A 1 761 ? 2.475 -21.895 48.997 1.00 16.75 ? 796 PRO A CA 1 ATOM 5953 C C . PRO A 1 761 ? 1.825 -22.818 50.024 1.00 16.54 ? 796 PRO A C 1 ATOM 5954 O O . PRO A 1 761 ? 0.854 -22.438 50.696 1.00 17.19 ? 796 PRO A O 1 ATOM 5955 C CB . PRO A 1 761 ? 3.104 -20.685 49.687 1.00 19.00 ? 796 PRO A CB 1 ATOM 5956 C CG . PRO A 1 761 ? 2.844 -19.549 48.782 1.00 21.10 ? 796 PRO A CG 1 ATOM 5957 C CD . PRO A 1 761 ? 1.471 -19.838 48.232 1.00 18.97 ? 796 PRO A CD 1 ATOM 5958 N N . HIS A 1 762 ? 2.343 -24.026 50.097 1.00 15.98 ? 797 HIS A N 1 ATOM 5959 C CA . HIS A 1 762 ? 1.862 -25.014 51.064 1.00 16.53 ? 797 HIS A CA 1 ATOM 5960 C C . HIS A 1 762 ? 2.633 -24.808 52.364 1.00 16.92 ? 797 HIS A C 1 ATOM 5961 O O . HIS A 1 762 ? 3.655 -25.470 52.632 1.00 17.74 ? 797 HIS A O 1 ATOM 5962 C CB . HIS A 1 762 ? 2.047 -26.406 50.526 1.00 16.35 ? 797 HIS A CB 1 ATOM 5963 C CG . HIS A 1 762 ? 1.562 -27.464 51.459 1.00 17.09 ? 797 HIS A CG 1 ATOM 5964 N ND1 . HIS A 1 762 ? 2.147 -28.706 51.556 1.00 17.72 ? 797 HIS A ND1 1 ATOM 5965 C CD2 . HIS A 1 762 ? 0.580 -27.434 52.382 1.00 16.89 ? 797 HIS A CD2 1 ATOM 5966 C CE1 . HIS A 1 762 ? 1.532 -29.407 52.491 1.00 18.22 ? 797 HIS A CE1 1 ATOM 5967 N NE2 . HIS A 1 762 ? 0.569 -28.661 52.989 1.00 18.52 ? 797 HIS A NE2 1 ATOM 5968 N N . ARG A 1 763 ? 2.115 -23.909 53.182 1.00 18.17 ? 798 ARG A N 1 ATOM 5969 C CA . ARG A 1 763 ? 2.813 -23.515 54.396 1.00 18.48 ? 798 ARG A CA 1 ATOM 5970 C C . ARG A 1 763 ? 2.089 -24.016 55.650 1.00 18.93 ? 798 ARG A C 1 ATOM 5971 O O . ARG A 1 763 ? 0.864 -24.070 55.660 1.00 18.49 ? 798 ARG A O 1 ATOM 5972 C CB . ARG A 1 763 ? 3.013 -22.008 54.429 1.00 20.14 ? 798 ARG A CB 1 ATOM 5973 C CG . ARG A 1 763 ? 4.049 -21.576 53.381 1.00 20.57 ? 798 ARG A CG 1 ATOM 5974 C CD . ARG A 1 763 ? 4.319 -20.104 53.356 1.00 24.64 ? 798 ARG A CD 1 ATOM 5975 N NE . ARG A 1 763 ? 4.771 -19.555 54.635 1.00 26.62 ? 798 ARG A NE 1 ATOM 5976 C CZ . ARG A 1 763 ? 5.082 -18.274 54.831 1.00 27.54 ? 798 ARG A CZ 1 ATOM 5977 N NH1 . ARG A 1 763 ? 5.026 -17.391 53.833 1.00 27.78 ? 798 ARG A NH1 1 ATOM 5978 N NH2 . ARG A 1 763 ? 5.458 -17.869 56.044 1.00 29.96 ? 798 ARG A NH2 1 ATOM 5979 N N . PRO A 1 764 ? 2.864 -24.363 56.695 1.00 19.16 ? 799 PRO A N 1 ATOM 5980 C CA . PRO A 1 764 ? 2.303 -24.893 57.943 1.00 19.96 ? 799 PRO A CA 1 ATOM 5981 C C . PRO A 1 764 ? 1.695 -23.819 58.842 1.00 20.59 ? 799 PRO A C 1 ATOM 5982 O O . PRO A 1 764 ? 1.200 -24.121 59.928 1.00 20.66 ? 799 PRO A O 1 ATOM 5983 C CB . PRO A 1 764 ? 3.526 -25.511 58.614 1.00 20.85 ? 799 PRO A CB 1 ATOM 5984 C CG . PRO A 1 764 ? 4.644 -24.633 58.201 1.00 20.25 ? 799 PRO A CG 1 ATOM 5985 C CD . PRO A 1 764 ? 4.346 -24.385 56.739 1.00 19.57 ? 799 PRO A CD 1 ATOM 5986 N N . ASP A 1 765 ? 1.760 -22.567 58.424 1.00 18.99 ? 800 ASP A N 1 ATOM 5987 C CA . ASP A 1 765 ? 1.114 -21.463 59.130 1.00 20.61 ? 800 ASP A CA 1 ATOM 5988 C C . ASP A 1 765 ? 0.597 -20.476 58.098 1.00 18.55 ? 800 ASP A C 1 ATOM 5989 O O . ASP A 1 765 ? 0.955 -20.576 56.904 1.00 17.86 ? 800 ASP A O 1 ATOM 5990 C CB . ASP A 1 765 ? 2.131 -20.778 60.047 1.00 22.27 ? 800 ASP A CB 1 ATOM 5991 C CG . ASP A 1 765 ? 3.326 -20.242 59.276 1.00 24.39 ? 800 ASP A CG 1 ATOM 5992 O OD1 . ASP A 1 765 ? 3.166 -19.279 58.502 1.00 23.45 ? 800 ASP A OD1 1 ATOM 5993 O OD2 . ASP A 1 765 ? 4.424 -20.803 59.412 1.00 29.50 ? 800 ASP A OD2 1 ATOM 5994 N N . ASN A 1 766 ? -0.234 -19.542 58.557 1.00 17.72 ? 801 ASN A N 1 ATOM 5995 C CA . ASN A 1 766 ? -0.704 -18.431 57.723 1.00 17.12 ? 801 ASN A CA 1 ATOM 5996 C C . ASN A 1 766 ? -0.120 -17.096 58.155 1.00 16.52 ? 801 ASN A C 1 ATOM 5997 O O . ASN A 1 766 ? -0.802 -16.046 58.125 1.00 16.32 ? 801 ASN A O 1 ATOM 5998 C CB . ASN A 1 766 ? -2.223 -18.412 57.725 1.00 17.27 ? 801 ASN A CB 1 ATOM 5999 C CG . ASN A 1 766 ? -2.808 -19.529 56.898 1.00 16.86 ? 801 ASN A CG 1 ATOM 6000 O OD1 . ASN A 1 766 ? -2.604 -19.579 55.695 1.00 16.38 ? 801 ASN A OD1 1 ATOM 6001 N ND2 . ASN A 1 766 ? -3.513 -20.453 57.551 1.00 17.43 ? 801 ASN A ND2 1 ATOM 6002 N N . ASP A 1 767 ? 1.163 -17.115 58.521 1.00 17.70 ? 802 ASP A N 1 ATOM 6003 C CA . ASP A 1 767 ? 1.858 -15.898 58.954 1.00 17.87 ? 802 ASP A CA 1 ATOM 6004 C C . ASP A 1 767 ? 1.898 -14.857 57.828 1.00 17.29 ? 802 ASP A C 1 ATOM 6005 O O . ASP A 1 767 ? 1.904 -13.665 58.101 1.00 17.17 ? 802 ASP A O 1 ATOM 6006 C CB . ASP A 1 767 ? 3.279 -16.191 59.444 1.00 18.56 ? 802 ASP A CB 1 ATOM 6007 C CG . ASP A 1 767 ? 3.314 -17.057 60.711 1.00 20.78 ? 802 ASP A CG 1 ATOM 6008 O OD1 . ASP A 1 767 ? 2.256 -17.323 61.320 1.00 20.28 ? 802 ASP A OD1 1 ATOM 6009 O OD2 . ASP A 1 767 ? 4.426 -17.479 61.084 1.00 24.20 ? 802 ASP A OD2 1 ATOM 6010 N N . GLU A 1 768 ? 1.886 -15.307 56.578 1.00 17.46 ? 803 GLU A N 1 ATOM 6011 C CA . GLU A 1 768 ? 1.813 -14.392 55.431 1.00 17.98 ? 803 GLU A CA 1 ATOM 6012 C C . GLU A 1 768 ? 0.579 -13.496 55.450 1.00 18.82 ? 803 GLU A C 1 ATOM 6013 O O . GLU A 1 768 ? 0.637 -12.340 55.027 1.00 18.71 ? 803 GLU A O 1 ATOM 6014 C CB . GLU A 1 768 ? 1.857 -15.157 54.117 1.00 18.49 ? 803 GLU A CB 1 ATOM 6015 C CG . GLU A 1 768 ? 2.000 -14.273 52.896 1.00 18.73 ? 803 GLU A CG 1 ATOM 6016 C CD . GLU A 1 768 ? 2.097 -15.051 51.601 1.00 18.65 ? 803 GLU A CD 1 ATOM 6017 O OE1 . GLU A 1 768 ? 2.187 -16.316 51.619 1.00 16.84 ? 803 GLU A OE1 1 ATOM 6018 O OE2 . GLU A 1 768 ? 2.094 -14.350 50.566 1.00 17.69 ? 803 GLU A OE2 1 ATOM 6019 N N . SER A 1 769 ? -0.515 -14.029 55.998 1.00 17.59 ? 804 SER A N 1 ATOM 6020 C CA . SER A 1 769 ? -1.809 -13.371 56.003 1.00 17.49 ? 804 SER A CA 1 ATOM 6021 C C . SER A 1 769 ? -2.066 -12.764 57.375 1.00 18.51 ? 804 SER A C 1 ATOM 6022 O O . SER A 1 769 ? -2.462 -13.472 58.310 1.00 17.76 ? 804 SER A O 1 ATOM 6023 C CB . SER A 1 769 ? -2.887 -14.400 55.654 1.00 17.10 ? 804 SER A CB 1 ATOM 6024 O OG . SER A 1 769 ? -2.682 -14.862 54.309 1.00 15.99 ? 804 SER A OG 1 ATOM 6025 N N . CYS A 1 770 ? -1.862 -11.454 57.501 1.00 17.72 ? 805 CYS A N 1 ATOM 6026 C CA . CYS A 1 770 ? -1.961 -10.806 58.809 1.00 20.14 ? 805 CYS A CA 1 ATOM 6027 C C . CYS A 1 770 ? -3.383 -10.850 59.343 1.00 19.45 ? 805 CYS A C 1 ATOM 6028 O O . CYS A 1 770 ? -3.587 -10.791 60.562 1.00 19.40 ? 805 CYS A O 1 ATOM 6029 C CB . CYS A 1 770 ? -1.452 -9.358 58.755 1.00 21.76 ? 805 CYS A CB 1 ATOM 6030 S SG . CYS A 1 770 ? 0.320 -9.184 58.372 1.00 25.13 ? 805 CYS A SG 1 ATOM 6031 N N . ALA A 1 771 ? -4.364 -11.009 58.461 1.00 19.37 ? 806 ALA A N 1 ATOM 6032 C CA . ALA A 1 771 ? -5.776 -11.078 58.897 1.00 19.56 ? 806 ALA A CA 1 ATOM 6033 C C . ALA A 1 771 ? -6.326 -12.498 59.079 1.00 19.89 ? 806 ALA A C 1 ATOM 6034 O O . ALA A 1 771 ? -7.543 -12.662 59.219 1.00 21.85 ? 806 ALA A O 1 ATOM 6035 C CB . ALA A 1 771 ? -6.650 -10.287 57.933 1.00 20.07 ? 806 ALA A CB 1 ATOM 6036 N N . SER A 1 772 ? -5.454 -13.503 59.161 1.00 19.51 ? 807 SER A N 1 ATOM 6037 C CA . SER A 1 772 ? -5.875 -14.904 59.138 1.00 19.69 ? 807 SER A CA 1 ATOM 6038 C C . SER A 1 772 ? -6.665 -15.366 60.366 1.00 21.88 ? 807 SER A C 1 ATOM 6039 O O . SER A 1 772 ? -7.324 -16.416 60.291 1.00 23.23 ? 807 SER A O 1 ATOM 6040 C CB . SER A 1 772 ? -4.698 -15.856 58.910 1.00 18.52 ? 807 SER A CB 1 ATOM 6041 O OG . SER A 1 772 ? -3.816 -15.903 60.010 1.00 18.40 ? 807 SER A OG 1 ATOM 6042 N N . SER A 1 773 ? -6.619 -14.626 61.473 1.00 23.92 ? 808 SER A N 1 ATOM 6043 C CA . SER A 1 773 ? -7.525 -14.960 62.579 1.00 27.48 ? 808 SER A CA 1 ATOM 6044 C C . SER A 1 773 ? -9.005 -14.667 62.245 1.00 28.82 ? 808 SER A C 1 ATOM 6045 O O . SER A 1 773 ? -9.897 -15.163 62.920 1.00 31.03 ? 808 SER A O 1 ATOM 6046 C CB . SER A 1 773 ? -7.112 -14.270 63.867 1.00 29.81 ? 808 SER A CB 1 ATOM 6047 O OG . SER A 1 773 ? -5.876 -14.780 64.352 1.00 30.59 ? 808 SER A OG 1 ATOM 6048 N N . GLU A 1 774 ? -9.261 -13.878 61.209 1.00 28.03 ? 809 GLU A N 1 ATOM 6049 C CA . GLU A 1 774 ? -10.614 -13.536 60.792 1.00 28.33 ? 809 GLU A CA 1 ATOM 6050 C C . GLU A 1 774 ? -11.210 -14.650 59.916 1.00 27.87 ? 809 GLU A C 1 ATOM 6051 O O . GLU A 1 774 ? -10.525 -15.625 59.590 1.00 26.22 ? 809 GLU A O 1 ATOM 6052 C CB . GLU A 1 774 ? -10.615 -12.196 60.056 1.00 31.45 ? 809 GLU A CB 1 ATOM 6053 C CG . GLU A 1 774 ? -10.028 -11.053 60.882 1.00 38.58 ? 809 GLU A CG 1 ATOM 6054 C CD . GLU A 1 774 ? -9.968 -9.740 60.128 1.00 45.16 ? 809 GLU A CD 1 ATOM 6055 O OE1 . GLU A 1 774 ? -10.828 -9.498 59.254 1.00 53.32 ? 809 GLU A OE1 1 ATOM 6056 O OE2 . GLU A 1 774 ? -9.060 -8.931 60.417 1.00 59.92 ? 809 GLU A OE2 1 ATOM 6057 N N . ASP A 1 775 ? -12.491 -14.511 59.577 1.00 26.31 ? 810 ASP A N 1 ATOM 6058 C CA . ASP A 1 775 ? -13.168 -15.441 58.676 1.00 27.21 ? 810 ASP A CA 1 ATOM 6059 C C . ASP A 1 775 ? -12.432 -15.433 57.342 1.00 24.59 ? 810 ASP A C 1 ATOM 6060 O O . ASP A 1 775 ? -11.967 -14.388 56.896 1.00 23.86 ? 810 ASP A O 1 ATOM 6061 C CB . ASP A 1 775 ? -14.618 -15.004 58.441 1.00 29.88 ? 810 ASP A CB 1 ATOM 6062 C CG . ASP A 1 775 ? -15.401 -15.997 57.628 1.00 33.09 ? 810 ASP A CG 1 ATOM 6063 O OD1 . ASP A 1 775 ? -15.830 -17.005 58.212 1.00 38.04 ? 810 ASP A OD1 1 ATOM 6064 O OD2 . ASP A 1 775 ? -15.577 -15.785 56.405 1.00 35.94 ? 810 ASP A OD2 1 ATOM 6065 N N . GLU A 1 776 ? -12.353 -16.605 56.724 1.00 24.88 ? 811 GLU A N 1 ATOM 6066 C CA . GLU A 1 776 ? -11.620 -16.798 55.468 1.00 23.67 ? 811 GLU A CA 1 ATOM 6067 C C . GLU A 1 776 ? -12.064 -15.870 54.333 1.00 23.11 ? 811 GLU A C 1 ATOM 6068 O O . GLU A 1 776 ? -11.258 -15.504 53.450 1.00 19.79 ? 811 GLU A O 1 ATOM 6069 C CB . GLU A 1 776 ? -11.709 -18.265 55.029 1.00 23.78 ? 811 GLU A CB 1 ATOM 6070 C CG . GLU A 1 776 ? -10.823 -19.198 55.842 1.00 25.75 ? 811 GLU A CG 1 ATOM 6071 C CD . GLU A 1 776 ? -11.498 -19.826 57.066 1.00 28.95 ? 811 GLU A CD 1 ATOM 6072 O OE1 . GLU A 1 776 ? -12.654 -19.480 57.376 1.00 28.76 ? 811 GLU A OE1 1 ATOM 6073 O OE2 . GLU A 1 776 ? -10.845 -20.662 57.726 1.00 33.62 ? 811 GLU A OE2 1 ATOM 6074 N N . SER A 1 777 ? -13.334 -15.465 54.356 1.00 23.17 ? 812 SER A N 1 ATOM 6075 C CA . SER A 1 777 ? -13.842 -14.443 53.428 1.00 24.59 ? 812 SER A CA 1 ATOM 6076 C C . SER A 1 777 ? -13.126 -13.100 53.507 1.00 25.55 ? 812 SER A C 1 ATOM 6077 O O . SER A 1 777 ? -13.291 -12.292 52.609 1.00 27.35 ? 812 SER A O 1 ATOM 6078 C CB . SER A 1 777 ? -15.352 -14.223 53.653 1.00 26.22 ? 812 SER A CB 1 ATOM 6079 O OG . SER A 1 777 ? -15.595 -13.714 54.956 1.00 26.83 ? 812 SER A OG 1 ATOM 6080 N N . LYS A 1 778 ? -12.361 -12.847 54.574 1.00 25.20 ? 813 LYS A N 1 ATOM 6081 C CA . LYS A 1 778 ? -11.614 -11.596 54.744 1.00 25.97 ? 813 LYS A CA 1 ATOM 6082 C C . LYS A 1 778 ? -10.130 -11.655 54.366 1.00 24.11 ? 813 LYS A C 1 ATOM 6083 O O . LYS A 1 778 ? -9.444 -10.633 54.427 1.00 22.84 ? 813 LYS A O 1 ATOM 6084 C CB . LYS A 1 778 ? -11.705 -11.147 56.211 1.00 29.14 ? 813 LYS A CB 1 ATOM 6085 C CG . LYS A 1 778 ? -13.126 -11.043 56.762 1.00 33.91 ? 813 LYS A CG 1 ATOM 6086 C CD . LYS A 1 778 ? -13.937 -10.037 55.966 1.00 38.48 ? 813 LYS A CD 1 ATOM 6087 C CE . LYS A 1 778 ? -15.188 -9.604 56.712 1.00 44.45 ? 813 LYS A CE 1 ATOM 6088 N NZ . LYS A 1 778 ? -16.015 -8.715 55.852 1.00 48.13 ? 813 LYS A NZ 1 ATOM 6089 N N . TRP A 1 779 ? -9.619 -12.830 54.007 1.00 21.31 ? 814 TRP A N 1 ATOM 6090 C CA . TRP A 1 779 ? -8.184 -12.980 53.754 1.00 19.62 ? 814 TRP A CA 1 ATOM 6091 C C . TRP A 1 779 ? -7.740 -13.998 52.726 1.00 19.51 ? 814 TRP A C 1 ATOM 6092 O O . TRP A 1 779 ? -6.650 -13.825 52.161 1.00 19.41 ? 814 TRP A O 1 ATOM 6093 C CB . TRP A 1 779 ? -7.417 -13.218 55.070 1.00 20.15 ? 814 TRP A CB 1 ATOM 6094 C CG . TRP A 1 779 ? -7.722 -14.494 55.773 1.00 19.94 ? 814 TRP A CG 1 ATOM 6095 C CD1 . TRP A 1 779 ? -8.720 -14.703 56.691 1.00 19.77 ? 814 TRP A CD1 1 ATOM 6096 C CD2 . TRP A 1 779 ? -7.009 -15.722 55.672 1.00 18.60 ? 814 TRP A CD2 1 ATOM 6097 N NE1 . TRP A 1 779 ? -8.675 -15.991 57.144 1.00 19.99 ? 814 TRP A NE1 1 ATOM 6098 C CE2 . TRP A 1 779 ? -7.643 -16.644 56.525 1.00 19.57 ? 814 TRP A CE2 1 ATOM 6099 C CE3 . TRP A 1 779 ? -5.887 -16.144 54.930 1.00 18.15 ? 814 TRP A CE3 1 ATOM 6100 C CZ2 . TRP A 1 779 ? -7.193 -17.963 56.675 1.00 19.91 ? 814 TRP A CZ2 1 ATOM 6101 C CZ3 . TRP A 1 779 ? -5.442 -17.450 55.086 1.00 19.10 ? 814 TRP A CZ3 1 ATOM 6102 C CH2 . TRP A 1 779 ? -6.102 -18.352 55.955 1.00 19.01 ? 814 TRP A CH2 1 ATOM 6103 N N . VAL A 1 780 ? -8.514 -15.055 52.471 1.00 18.89 ? 815 VAL A N 1 ATOM 6104 C CA . VAL A 1 780 ? -8.012 -16.126 51.607 1.00 18.42 ? 815 VAL A CA 1 ATOM 6105 C C . VAL A 1 780 ? -7.858 -15.658 50.150 1.00 19.66 ? 815 VAL A C 1 ATOM 6106 O O . VAL A 1 780 ? -6.827 -15.943 49.501 1.00 16.64 ? 815 VAL A O 1 ATOM 6107 C CB . VAL A 1 780 ? -8.875 -17.409 51.701 1.00 18.78 ? 815 VAL A CB 1 ATOM 6108 C CG1 . VAL A 1 780 ? -8.490 -18.396 50.601 1.00 18.33 ? 815 VAL A CG1 1 ATOM 6109 C CG2 . VAL A 1 780 ? -8.700 -18.073 53.058 1.00 17.31 ? 815 VAL A CG2 1 ATOM 6110 N N . GLU A 1 781 ? -8.875 -14.981 49.627 1.00 20.82 ? 816 GLU A N 1 ATOM 6111 C CA . GLU A 1 781 ? -8.776 -14.470 48.238 1.00 23.52 ? 816 GLU A CA 1 ATOM 6112 C C . GLU A 1 781 ? -7.603 -13.539 47.994 1.00 21.50 ? 816 GLU A C 1 ATOM 6113 O O . GLU A 1 781 ? -6.952 -13.624 46.945 1.00 19.97 ? 816 GLU A O 1 ATOM 6114 C CB . GLU A 1 781 ? -10.071 -13.796 47.775 1.00 27.62 ? 816 GLU A CB 1 ATOM 6115 C CG . GLU A 1 781 ? -10.801 -14.658 46.777 1.00 31.35 ? 816 GLU A CG 1 ATOM 6116 C CD . GLU A 1 781 ? -11.919 -13.932 46.072 1.00 34.83 ? 816 GLU A CD 1 ATOM 6117 O OE1 . GLU A 1 781 ? -12.764 -13.377 46.789 1.00 33.99 ? 816 GLU A OE1 1 ATOM 6118 O OE2 . GLU A 1 781 ? -11.959 -13.954 44.813 1.00 35.81 ? 816 GLU A OE2 1 ATOM 6119 N N . GLU A 1 782 ? -7.344 -12.644 48.941 1.00 20.93 ? 817 GLU A N 1 ATOM 6120 C CA . GLU A 1 782 ? -6.186 -11.728 48.868 1.00 21.20 ? 817 GLU A CA 1 ATOM 6121 C C . GLU A 1 782 ? -4.875 -12.541 48.746 1.00 19.12 ? 817 GLU A C 1 ATOM 6122 O O . GLU A 1 782 ? -3.982 -12.204 47.930 1.00 16.50 ? 817 GLU A O 1 ATOM 6123 C CB . GLU A 1 782 ? -6.193 -10.788 50.089 1.00 23.99 ? 817 GLU A CB 1 ATOM 6124 C CG . GLU A 1 782 ? -4.944 -9.942 50.317 1.00 28.81 ? 817 GLU A CG 1 ATOM 6125 C CD . GLU A 1 782 ? -4.996 -9.085 51.594 1.00 31.94 ? 817 GLU A CD 1 ATOM 6126 O OE1 . GLU A 1 782 ? -6.086 -8.861 52.166 1.00 37.97 ? 817 GLU A OE1 1 ATOM 6127 O OE2 . GLU A 1 782 ? -3.938 -8.606 52.033 1.00 35.79 ? 817 GLU A OE2 1 ATOM 6128 N N . LEU A 1 783 ? -4.778 -13.634 49.503 1.00 16.27 ? 818 LEU A N 1 ATOM 6129 C CA . LEU A 1 783 ? -3.595 -14.496 49.449 1.00 16.17 ? 818 LEU A CA 1 ATOM 6130 C C . LEU A 1 783 ? -3.478 -15.102 48.067 1.00 15.20 ? 818 LEU A C 1 ATOM 6131 O O . LEU A 1 783 ? -2.402 -15.117 47.425 1.00 16.81 ? 818 LEU A O 1 ATOM 6132 C CB . LEU A 1 783 ? -3.688 -15.597 50.518 1.00 15.54 ? 818 LEU A CB 1 ATOM 6133 C CG . LEU A 1 783 ? -2.577 -16.640 50.489 1.00 15.47 ? 818 LEU A CG 1 ATOM 6134 C CD1 . LEU A 1 783 ? -1.243 -16.047 50.892 1.00 15.77 ? 818 LEU A CD1 1 ATOM 6135 C CD2 . LEU A 1 783 ? -2.905 -17.813 51.402 1.00 16.33 ? 818 LEU A CD2 1 ATOM 6136 N N . MET A 1 784 ? -4.593 -15.611 47.576 1.00 16.21 ? 819 MET A N 1 ATOM 6137 C CA . MET A 1 784 ? -4.583 -16.252 46.281 1.00 16.82 ? 819 MET A CA 1 ATOM 6138 C C . MET A 1 784 ? -4.223 -15.302 45.151 1.00 15.21 ? 819 MET A C 1 ATOM 6139 O O . MET A 1 784 ? -3.453 -15.677 44.265 1.00 14.97 ? 819 MET A O 1 ATOM 6140 C CB . MET A 1 784 ? -5.911 -16.923 46.012 1.00 19.22 ? 819 MET A CB 1 ATOM 6141 C CG . MET A 1 784 ? -6.093 -18.115 46.927 1.00 22.75 ? 819 MET A CG 1 ATOM 6142 S SD . MET A 1 784 ? -7.717 -18.780 46.734 1.00 27.93 ? 819 MET A SD 1 ATOM 6143 C CE . MET A 1 784 ? -7.775 -19.020 44.955 1.00 29.91 ? 819 MET A CE 1 ATOM 6144 N N . LYS A 1 785 ? -4.732 -14.086 45.187 1.00 14.91 ? 820 LYS A N 1 ATOM 6145 C CA . LYS A 1 785 ? -4.398 -13.081 44.150 1.00 15.64 ? 820 LYS A CA 1 ATOM 6146 C C . LYS A 1 785 ? -2.902 -12.746 44.119 1.00 15.01 ? 820 LYS A C 1 ATOM 6147 O O . LYS A 1 785 ? -2.319 -12.558 43.048 1.00 12.92 ? 820 LYS A O 1 ATOM 6148 C CB . LYS A 1 785 ? -5.247 -11.816 44.325 1.00 17.61 ? 820 LYS A CB 1 ATOM 6149 C CG . LYS A 1 785 ? -6.717 -12.064 44.034 1.00 19.15 ? 820 LYS A CG 1 ATOM 6150 C CD . LYS A 1 785 ? -7.588 -10.884 44.399 1.00 23.23 ? 820 LYS A CD 1 ATOM 6151 C CE . LYS A 1 785 ? -9.057 -11.208 44.132 1.00 26.73 ? 820 LYS A CE 1 ATOM 6152 N NZ . LYS A 1 785 ? -9.843 -9.995 44.474 1.00 31.40 ? 820 LYS A NZ 1 ATOM 6153 N N . MET A 1 786 ? -2.270 -12.717 45.286 1.00 14.55 ? 821 MET A N 1 ATOM 6154 C CA A MET A 1 786 ? -0.848 -12.450 45.366 0.50 14.58 ? 821 MET A CA 1 ATOM 6155 C CA B MET A 1 786 ? -0.835 -12.456 45.383 0.50 14.26 ? 821 MET A CA 1 ATOM 6156 C C . MET A 1 786 ? -0.020 -13.555 44.691 1.00 13.93 ? 821 MET A C 1 ATOM 6157 O O . MET A 1 786 ? 1.088 -13.298 44.196 1.00 13.86 ? 821 MET A O 1 ATOM 6158 C CB A MET A 1 786 ? -0.445 -12.299 46.837 0.50 16.15 ? 821 MET A CB 1 ATOM 6159 C CB B MET A 1 786 ? -0.435 -12.336 46.869 0.50 15.34 ? 821 MET A CB 1 ATOM 6160 C CG A MET A 1 786 ? 0.873 -11.600 47.038 0.50 18.12 ? 821 MET A CG 1 ATOM 6161 C CG B MET A 1 786 ? 1.044 -12.141 47.169 0.50 16.52 ? 821 MET A CG 1 ATOM 6162 S SD A MET A 1 786 ? 0.973 -9.968 46.276 0.50 18.28 ? 821 MET A SD 1 ATOM 6163 S SD B MET A 1 786 ? 1.777 -10.631 46.482 0.50 16.37 ? 821 MET A SD 1 ATOM 6164 C CE A MET A 1 786 ? 2.621 -9.559 46.852 0.50 18.45 ? 821 MET A CE 1 ATOM 6165 C CE B MET A 1 786 ? 0.488 -9.404 46.745 0.50 17.62 ? 821 MET A CE 1 ATOM 6166 N N . HIS A 1 787 ? -0.574 -14.774 44.681 1.00 12.79 ? 822 HIS A N 1 ATOM 6167 C CA . HIS A 1 787 ? 0.067 -15.987 44.172 1.00 13.02 ? 822 HIS A CA 1 ATOM 6168 C C . HIS A 1 787 ? -0.516 -16.443 42.831 1.00 13.88 ? 822 HIS A C 1 ATOM 6169 O O . HIS A 1 787 ? -0.296 -17.593 42.420 1.00 14.20 ? 822 HIS A O 1 ATOM 6170 C CB . HIS A 1 787 ? 0.025 -17.057 45.263 1.00 13.07 ? 822 HIS A CB 1 ATOM 6171 C CG . HIS A 1 787 ? 0.897 -16.709 46.425 1.00 13.06 ? 822 HIS A CG 1 ATOM 6172 N ND1 . HIS A 1 787 ? 2.253 -16.932 46.414 1.00 13.14 ? 822 HIS A ND1 1 ATOM 6173 C CD2 . HIS A 1 787 ? 0.627 -16.099 47.602 1.00 14.30 ? 822 HIS A CD2 1 ATOM 6174 C CE1 . HIS A 1 787 ? 2.784 -16.483 47.534 1.00 13.15 ? 822 HIS A CE1 1 ATOM 6175 N NE2 . HIS A 1 787 ? 1.822 -15.959 48.265 1.00 14.45 ? 822 HIS A NE2 1 ATOM 6176 N N . THR A 1 788 ? -1.150 -15.493 42.130 1.00 13.68 ? 823 THR A N 1 ATOM 6177 C CA . THR A 1 788 ? -1.506 -15.668 40.733 1.00 13.29 ? 823 THR A CA 1 ATOM 6178 C C . THR A 1 788 ? -0.285 -16.118 39.929 1.00 12.27 ? 823 THR A C 1 ATOM 6179 O O . THR A 1 788 ? 0.859 -15.845 40.298 1.00 12.74 ? 823 THR A O 1 ATOM 6180 C CB . THR A 1 788 ? -2.136 -14.390 40.115 1.00 13.88 ? 823 THR A CB 1 ATOM 6181 O OG1 . THR A 1 788 ? -2.737 -14.680 38.845 1.00 13.77 ? 823 THR A OG1 1 ATOM 6182 C CG2 . THR A 1 788 ? -1.124 -13.223 39.987 1.00 13.57 ? 823 THR A CG2 1 ATOM 6183 N N . ALA A 1 789 ? -0.546 -16.840 38.856 1.00 12.96 ? 824 ALA A N 1 ATOM 6184 C CA . ALA A 1 789 ? 0.533 -17.459 38.059 1.00 12.71 ? 824 ALA A CA 1 ATOM 6185 C C . ALA A 1 789 ? 0.136 -17.611 36.621 1.00 12.16 ? 824 ALA A C 1 ATOM 6186 O O . ALA A 1 789 ? -1.031 -17.618 36.294 1.00 12.25 ? 824 ALA A O 1 ATOM 6187 C CB . ALA A 1 789 ? 0.901 -18.819 38.602 1.00 13.40 ? 824 ALA A CB 1 ATOM 6188 N N . ARG A 1 790 ? 1.144 -17.728 35.760 1.00 12.77 ? 825 ARG A N 1 ATOM 6189 C CA . ARG A 1 790 ? 0.938 -18.146 34.371 1.00 12.50 ? 825 ARG A CA 1 ATOM 6190 C C . ARG A 1 790 ? 0.845 -19.671 34.272 1.00 13.26 ? 825 ARG A C 1 ATOM 6191 O O . ARG A 1 790 ? 1.499 -20.398 35.022 1.00 13.84 ? 825 ARG A O 1 ATOM 6192 C CB . ARG A 1 790 ? 2.140 -17.718 33.515 1.00 12.45 ? 825 ARG A CB 1 ATOM 6193 C CG . ARG A 1 790 ? 2.503 -16.238 33.578 1.00 13.08 ? 825 ARG A CG 1 ATOM 6194 C CD . ARG A 1 790 ? 3.725 -15.925 32.715 1.00 13.34 ? 825 ARG A CD 1 ATOM 6195 N NE . ARG A 1 790 ? 4.805 -16.850 33.042 1.00 13.52 ? 825 ARG A NE 1 ATOM 6196 C CZ . ARG A 1 790 ? 5.723 -17.311 32.204 1.00 12.97 ? 825 ARG A CZ 1 ATOM 6197 N NH1 . ARG A 1 790 ? 5.775 -16.901 30.917 1.00 14.01 ? 825 ARG A NH1 1 ATOM 6198 N NH2 . ARG A 1 790 ? 6.580 -18.224 32.643 1.00 13.90 ? 825 ARG A NH2 1 ATOM 6199 N N . VAL A 1 791 ? 0.077 -20.173 33.313 1.00 13.84 ? 826 VAL A N 1 ATOM 6200 C CA . VAL A 1 791 ? 0.106 -21.611 33.065 1.00 13.92 ? 826 VAL A CA 1 ATOM 6201 C C . VAL A 1 791 ? 1.548 -22.092 32.790 1.00 14.61 ? 826 VAL A C 1 ATOM 6202 O O . VAL A 1 791 ? 1.960 -23.143 33.280 1.00 13.16 ? 826 VAL A O 1 ATOM 6203 C CB . VAL A 1 791 ? -0.865 -22.021 31.941 1.00 13.83 ? 826 VAL A CB 1 ATOM 6204 C CG1 . VAL A 1 791 ? -0.666 -23.480 31.556 1.00 13.74 ? 826 VAL A CG1 1 ATOM 6205 C CG2 . VAL A 1 791 ? -2.304 -21.784 32.384 1.00 14.66 ? 826 VAL A CG2 1 ATOM 6206 N N . ARG A 1 792 ? 2.332 -21.292 32.065 1.00 13.84 ? 827 ARG A N 1 ATOM 6207 C CA A ARG A 1 792 ? 3.754 -21.624 31.804 0.50 14.92 ? 827 ARG A CA 1 ATOM 6208 C CA B ARG A 1 792 ? 3.732 -21.628 31.796 0.50 14.62 ? 827 ARG A CA 1 ATOM 6209 C C . ARG A 1 792 ? 4.583 -21.844 33.086 1.00 13.86 ? 827 ARG A C 1 ATOM 6210 O O . ARG A 1 792 ? 5.496 -22.686 33.114 1.00 15.55 ? 827 ARG A O 1 ATOM 6211 C CB A ARG A 1 792 ? 4.454 -20.544 30.956 0.50 16.22 ? 827 ARG A CB 1 ATOM 6212 C CB B ARG A 1 792 ? 4.346 -20.534 30.914 0.50 15.53 ? 827 ARG A CB 1 ATOM 6213 C CG A ARG A 1 792 ? 4.145 -20.575 29.472 0.50 18.11 ? 827 ARG A CG 1 ATOM 6214 C CG B ARG A 1 792 ? 5.616 -20.919 30.197 0.50 16.57 ? 827 ARG A CG 1 ATOM 6215 C CD A ARG A 1 792 ? 4.682 -21.829 28.796 0.50 19.02 ? 827 ARG A CD 1 ATOM 6216 C CD B ARG A 1 792 ? 5.342 -21.871 29.036 0.50 18.83 ? 827 ARG A CD 1 ATOM 6217 N NE A ARG A 1 792 ? 6.148 -21.840 28.687 0.50 20.49 ? 827 ARG A NE 1 ATOM 6218 N NE B ARG A 1 792 ? 6.585 -22.324 28.416 0.50 20.18 ? 827 ARG A NE 1 ATOM 6219 C CZ A ARG A 1 792 ? 6.903 -22.936 28.727 0.50 22.14 ? 827 ARG A CZ 1 ATOM 6220 C CZ B ARG A 1 792 ? 7.187 -23.471 28.720 0.50 22.99 ? 827 ARG A CZ 1 ATOM 6221 N NH1 A ARG A 1 792 ? 6.350 -24.135 28.885 0.50 23.15 ? 827 ARG A NH1 1 ATOM 6222 N NH1 B ARG A 1 792 ? 6.645 -24.290 29.610 0.50 22.68 ? 827 ARG A NH1 1 ATOM 6223 N NH2 A ARG A 1 792 ? 8.223 -22.839 28.630 0.50 20.89 ? 827 ARG A NH2 1 ATOM 6224 N NH2 B ARG A 1 792 ? 8.322 -23.805 28.135 0.50 24.51 ? 827 ARG A NH2 1 ATOM 6225 N N . ASP A 1 793 ? 4.266 -21.101 34.145 1.00 14.10 ? 828 ASP A N 1 ATOM 6226 C CA . ASP A 1 793 ? 4.962 -21.221 35.436 1.00 14.42 ? 828 ASP A CA 1 ATOM 6227 C C . ASP A 1 793 ? 4.704 -22.601 36.031 1.00 14.25 ? 828 ASP A C 1 ATOM 6228 O O . ASP A 1 793 ? 5.613 -23.255 36.537 1.00 14.97 ? 828 ASP A O 1 ATOM 6229 C CB . ASP A 1 793 ? 4.478 -20.157 36.424 1.00 13.92 ? 828 ASP A CB 1 ATOM 6230 C CG . ASP A 1 793 ? 4.839 -18.724 36.006 1.00 15.38 ? 828 ASP A CG 1 ATOM 6231 O OD1 . ASP A 1 793 ? 5.946 -18.567 35.417 1.00 14.74 ? 828 ASP A OD1 1 ATOM 6232 O OD2 . ASP A 1 793 ? 4.037 -17.781 36.297 1.00 14.71 ? 828 ASP A OD2 1 ATOM 6233 N N . ILE A 1 794 ? 3.442 -23.019 35.963 1.00 13.74 ? 829 ILE A N 1 ATOM 6234 C CA . ILE A 1 794 ? 3.031 -24.337 36.442 1.00 13.92 ? 829 ILE A CA 1 ATOM 6235 C C . ILE A 1 794 ? 3.652 -25.449 35.592 1.00 14.53 ? 829 ILE A C 1 ATOM 6236 O O . ILE A 1 794 ? 4.072 -26.468 36.116 1.00 14.21 ? 829 ILE A O 1 ATOM 6237 C CB . ILE A 1 794 ? 1.488 -24.462 36.495 1.00 14.71 ? 829 ILE A CB 1 ATOM 6238 C CG1 . ILE A 1 794 ? 0.919 -23.459 37.511 1.00 14.92 ? 829 ILE A CG1 1 ATOM 6239 C CG2 . ILE A 1 794 ? 1.049 -25.892 36.822 1.00 13.97 ? 829 ILE A CG2 1 ATOM 6240 C CD1 . ILE A 1 794 ? -0.575 -23.211 37.389 1.00 16.13 ? 829 ILE A CD1 1 ATOM 6241 N N . GLU A 1 795 ? 3.712 -25.249 34.279 1.00 14.84 ? 830 GLU A N 1 ATOM 6242 C CA . GLU A 1 795 ? 4.344 -26.222 33.409 1.00 15.16 ? 830 GLU A CA 1 ATOM 6243 C C . GLU A 1 795 ? 5.812 -26.470 33.807 1.00 14.97 ? 830 GLU A C 1 ATOM 6244 O O . GLU A 1 795 ? 6.243 -27.630 33.882 1.00 16.03 ? 830 GLU A O 1 ATOM 6245 C CB . GLU A 1 795 ? 4.229 -25.787 31.942 1.00 15.29 ? 830 GLU A CB 1 ATOM 6246 C CG . GLU A 1 795 ? 2.803 -25.830 31.418 1.00 16.60 ? 830 GLU A CG 1 ATOM 6247 C CD . GLU A 1 795 ? 2.697 -25.617 29.910 1.00 18.73 ? 830 GLU A CD 1 ATOM 6248 O OE1 . GLU A 1 795 ? 3.598 -24.967 29.324 1.00 20.51 ? 830 GLU A OE1 1 ATOM 6249 O OE2 . GLU A 1 795 ? 1.725 -26.132 29.294 1.00 18.56 ? 830 GLU A OE2 1 ATOM 6250 N N . HIS A 1 796 ? 6.572 -25.410 34.068 1.00 14.50 ? 831 HIS A N 1 ATOM 6251 C CA . HIS A 1 796 ? 7.961 -25.562 34.487 1.00 16.34 ? 831 HIS A CA 1 ATOM 6252 C C . HIS A 1 796 ? 8.051 -26.333 35.800 1.00 14.96 ? 831 HIS A C 1 ATOM 6253 O O . HIS A 1 796 ? 8.948 -27.156 36.002 1.00 15.85 ? 831 HIS A O 1 ATOM 6254 C CB . HIS A 1 796 ? 8.625 -24.225 34.795 1.00 18.65 ? 831 HIS A CB 1 ATOM 6255 C CG . HIS A 1 796 ? 8.774 -23.295 33.637 1.00 20.46 ? 831 HIS A CG 1 ATOM 6256 N ND1 . HIS A 1 796 ? 9.212 -23.703 32.396 1.00 24.00 ? 831 HIS A ND1 1 ATOM 6257 C CD2 . HIS A 1 796 ? 8.681 -21.945 33.582 1.00 21.48 ? 831 HIS A CD2 1 ATOM 6258 C CE1 . HIS A 1 796 ? 9.303 -22.648 31.601 1.00 25.58 ? 831 HIS A CE1 1 ATOM 6259 N NE2 . HIS A 1 796 ? 8.984 -21.570 32.295 1.00 23.11 ? 831 HIS A NE2 1 ATOM 6260 N N . LEU A 1 797 ? 7.134 -26.011 36.713 1.00 14.80 ? 832 LEU A N 1 ATOM 6261 C CA . LEU A 1 797 ? 7.164 -26.586 38.027 1.00 15.14 ? 832 LEU A CA 1 ATOM 6262 C C . LEU A 1 797 ? 6.664 -28.003 38.112 1.00 15.59 ? 832 LEU A C 1 ATOM 6263 O O . LEU A 1 797 ? 6.879 -28.641 39.136 1.00 16.30 ? 832 LEU A O 1 ATOM 6264 C CB . LEU A 1 797 ? 6.360 -25.718 38.979 1.00 14.79 ? 832 LEU A CB 1 ATOM 6265 C CG . LEU A 1 797 ? 7.111 -24.465 39.424 1.00 15.07 ? 832 LEU A CG 1 ATOM 6266 C CD1 . LEU A 1 797 ? 6.128 -23.451 39.975 1.00 15.89 ? 832 LEU A CD1 1 ATOM 6267 C CD2 . LEU A 1 797 ? 8.161 -24.807 40.480 1.00 16.39 ? 832 LEU A CD2 1 ATOM 6268 N N . THR A 1 798 ? 5.950 -28.469 37.085 1.00 15.05 ? 833 THR A N 1 ATOM 6269 C CA . THR A 1 798 ? 5.319 -29.792 37.094 1.00 16.45 ? 833 THR A CA 1 ATOM 6270 C C . THR A 1 798 ? 5.815 -30.746 36.018 1.00 17.15 ? 833 THR A C 1 ATOM 6271 O O . THR A 1 798 ? 5.596 -31.946 36.135 1.00 17.97 ? 833 THR A O 1 ATOM 6272 C CB . THR A 1 798 ? 3.789 -29.707 36.909 1.00 16.55 ? 833 THR A CB 1 ATOM 6273 O OG1 . THR A 1 798 ? 3.462 -29.104 35.647 1.00 16.92 ? 833 THR A OG1 1 ATOM 6274 C CG2 . THR A 1 798 ? 3.132 -28.936 38.055 1.00 17.29 ? 833 THR A CG2 1 ATOM 6275 N N . GLY A 1 799 ? 6.460 -30.235 34.967 1.00 16.69 ? 834 GLY A N 1 ATOM 6276 C CA . GLY A 1 799 ? 6.773 -31.068 33.799 1.00 17.77 ? 834 GLY A CA 1 ATOM 6277 C C . GLY A 1 799 ? 5.528 -31.521 33.029 1.00 17.34 ? 834 GLY A C 1 ATOM 6278 O O . GLY A 1 799 ? 5.582 -32.526 32.315 1.00 18.06 ? 834 GLY A O 1 ATOM 6279 N N . LEU A 1 800 ? 4.415 -30.799 33.167 1.00 16.63 ? 835 LEU A N 1 ATOM 6280 C CA . LEU A 1 800 ? 3.193 -31.065 32.410 1.00 17.27 ? 835 LEU A CA 1 ATOM 6281 C C . LEU A 1 800 ? 3.044 -30.059 31.268 1.00 18.64 ? 835 LEU A C 1 ATOM 6282 O O . LEU A 1 800 ? 3.555 -28.927 31.350 1.00 18.54 ? 835 LEU A O 1 ATOM 6283 C CB . LEU A 1 800 ? 1.957 -31.015 33.325 1.00 17.25 ? 835 LEU A CB 1 ATOM 6284 C CG . LEU A 1 800 ? 1.961 -31.986 34.490 1.00 17.88 ? 835 LEU A CG 1 ATOM 6285 C CD1 . LEU A 1 800 ? 0.806 -31.641 35.414 1.00 18.09 ? 835 LEU A CD1 1 ATOM 6286 C CD2 . LEU A 1 800 ? 1.888 -33.429 34.028 1.00 19.92 ? 835 LEU A CD2 1 ATOM 6287 N N . ASP A 1 801 ? 2.308 -30.460 30.230 1.00 19.07 ? 836 ASP A N 1 ATOM 6288 C CA . ASP A 1 801 ? 2.030 -29.612 29.080 1.00 19.01 ? 836 ASP A CA 1 ATOM 6289 C C . ASP A 1 801 ? 0.505 -29.618 28.855 1.00 18.44 ? 836 ASP A C 1 ATOM 6290 O O . ASP A 1 801 ? -0.076 -30.663 28.575 1.00 20.33 ? 836 ASP A O 1 ATOM 6291 C CB . ASP A 1 801 ? 2.773 -30.128 27.860 1.00 19.35 ? 836 ASP A CB 1 ATOM 6292 C CG . ASP A 1 801 ? 2.756 -29.151 26.690 1.00 21.41 ? 836 ASP A CG 1 ATOM 6293 O OD1 . ASP A 1 801 ? 3.380 -28.083 26.812 1.00 21.92 ? 836 ASP A OD1 1 ATOM 6294 O OD2 . ASP A 1 801 ? 2.156 -29.458 25.623 1.00 24.49 ? 836 ASP A OD2 1 ATOM 6295 N N . PHE A 1 802 ? -0.106 -28.448 28.975 1.00 16.97 ? 837 PHE A N 1 ATOM 6296 C CA . PHE A 1 802 ? -1.559 -28.292 28.990 1.00 17.42 ? 837 PHE A CA 1 ATOM 6297 C C . PHE A 1 802 ? -2.064 -27.844 27.614 1.00 17.92 ? 837 PHE A C 1 ATOM 6298 O O . PHE A 1 802 ? -1.261 -27.503 26.696 1.00 18.58 ? 837 PHE A O 1 ATOM 6299 C CB . PHE A 1 802 ? -1.980 -27.304 30.077 1.00 16.79 ? 837 PHE A CB 1 ATOM 6300 C CG . PHE A 1 802 ? -1.590 -27.719 31.470 1.00 16.50 ? 837 PHE A CG 1 ATOM 6301 C CD1 . PHE A 1 802 ? -2.361 -28.636 32.175 1.00 17.31 ? 837 PHE A CD1 1 ATOM 6302 C CD2 . PHE A 1 802 ? -0.440 -27.217 32.069 1.00 16.61 ? 837 PHE A CD2 1 ATOM 6303 C CE1 . PHE A 1 802 ? -2.006 -29.027 33.450 1.00 17.01 ? 837 PHE A CE1 1 ATOM 6304 C CE2 . PHE A 1 802 ? -0.060 -27.629 33.327 1.00 16.58 ? 837 PHE A CE2 1 ATOM 6305 C CZ . PHE A 1 802 ? -0.844 -28.538 34.024 1.00 16.71 ? 837 PHE A CZ 1 ATOM 6306 N N . TYR A 1 803 ? -3.392 -27.862 27.462 1.00 18.08 ? 838 TYR A N 1 ATOM 6307 C CA . TYR A 1 803 ? -4.073 -27.357 26.268 1.00 18.39 ? 838 TYR A CA 1 ATOM 6308 C C . TYR A 1 803 ? -3.591 -28.029 24.985 1.00 20.29 ? 838 TYR A C 1 ATOM 6309 O O . TYR A 1 803 ? -3.328 -27.379 23.986 1.00 19.29 ? 838 TYR A O 1 ATOM 6310 C CB . TYR A 1 803 ? -3.943 -25.835 26.152 1.00 17.65 ? 838 TYR A CB 1 ATOM 6311 C CG . TYR A 1 803 ? -4.476 -25.075 27.351 1.00 18.26 ? 838 TYR A CG 1 ATOM 6312 C CD1 . TYR A 1 803 ? -5.843 -25.095 27.661 1.00 20.20 ? 838 TYR A CD1 1 ATOM 6313 C CD2 . TYR A 1 803 ? -3.628 -24.352 28.177 1.00 19.08 ? 838 TYR A CD2 1 ATOM 6314 C CE1 . TYR A 1 803 ? -6.338 -24.420 28.766 1.00 19.22 ? 838 TYR A CE1 1 ATOM 6315 C CE2 . TYR A 1 803 ? -4.114 -23.668 29.263 1.00 19.13 ? 838 TYR A CE2 1 ATOM 6316 C CZ . TYR A 1 803 ? -5.479 -23.705 29.562 1.00 19.02 ? 838 TYR A CZ 1 ATOM 6317 O OH . TYR A 1 803 ? -5.961 -23.012 30.657 1.00 19.20 ? 838 TYR A OH 1 ATOM 6318 N N . ARG A 1 804 ? -3.488 -29.346 25.024 1.00 21.16 ? 839 ARG A N 1 ATOM 6319 C CA . ARG A 1 804 ? -2.961 -30.088 23.886 1.00 22.90 ? 839 ARG A CA 1 ATOM 6320 C C . ARG A 1 804 ? -4.017 -30.401 22.840 1.00 25.02 ? 839 ARG A C 1 ATOM 6321 O O . ARG A 1 804 ? -3.655 -30.696 21.711 1.00 25.30 ? 839 ARG A O 1 ATOM 6322 C CB . ARG A 1 804 ? -2.287 -31.340 24.392 1.00 24.42 ? 839 ARG A CB 1 ATOM 6323 C CG . ARG A 1 804 ? -0.998 -30.961 25.106 1.00 23.89 ? 839 ARG A CG 1 ATOM 6324 C CD . ARG A 1 804 ? -0.315 -32.175 25.619 1.00 26.17 ? 839 ARG A CD 1 ATOM 6325 N NE . ARG A 1 804 ? 0.272 -32.972 24.546 1.00 26.66 ? 839 ARG A NE 1 ATOM 6326 C CZ . ARG A 1 804 ? 1.502 -32.847 24.048 1.00 26.07 ? 839 ARG A CZ 1 ATOM 6327 N NH1 . ARG A 1 804 ? 2.342 -31.921 24.474 1.00 26.32 ? 839 ARG A NH1 1 ATOM 6328 N NH2 . ARG A 1 804 ? 1.906 -33.698 23.101 1.00 28.16 ? 839 ARG A NH2 1 ATOM 6329 N N . LYS A 1 805 ? -5.297 -30.303 23.197 1.00 24.15 ? 840 LYS A N 1 ATOM 6330 C CA . LYS A 1 805 ? -6.386 -30.610 22.259 1.00 28.37 ? 840 LYS A CA 1 ATOM 6331 C C . LYS A 1 805 ? -7.435 -29.523 22.288 1.00 26.65 ? 840 LYS A C 1 ATOM 6332 O O . LYS A 1 805 ? -8.398 -29.604 23.029 1.00 26.59 ? 840 LYS A O 1 ATOM 6333 C CB . LYS A 1 805 ? -7.006 -31.966 22.594 1.00 30.93 ? 840 LYS A CB 1 ATOM 6334 C CG . LYS A 1 805 ? -6.082 -33.155 22.406 1.00 36.45 ? 840 LYS A CG 1 ATOM 6335 C CD . LYS A 1 805 ? -5.883 -33.521 20.940 1.00 42.84 ? 840 LYS A CD 1 ATOM 6336 C CE . LYS A 1 805 ? -4.665 -34.413 20.736 1.00 46.94 ? 840 LYS A CE 1 ATOM 6337 N NZ . LYS A 1 805 ? -4.717 -35.653 21.561 1.00 48.93 ? 840 LYS A NZ 1 ATOM 6338 N N . THR A 1 806 ? -7.222 -28.474 21.506 1.00 26.93 ? 841 THR A N 1 ATOM 6339 C CA . THR A 1 806 ? -8.171 -27.365 21.428 1.00 26.64 ? 841 THR A CA 1 ATOM 6340 C C . THR A 1 806 ? -8.463 -27.060 19.961 1.00 27.75 ? 841 THR A C 1 ATOM 6341 O O . THR A 1 806 ? -7.901 -27.682 19.073 1.00 28.76 ? 841 THR A O 1 ATOM 6342 C CB . THR A 1 806 ? -7.605 -26.099 22.101 1.00 25.37 ? 841 THR A CB 1 ATOM 6343 O OG1 . THR A 1 806 ? -6.622 -25.515 21.246 1.00 23.55 ? 841 THR A OG1 1 ATOM 6344 C CG2 . THR A 1 806 ? -6.992 -26.418 23.501 1.00 24.77 ? 841 THR A CG2 1 ATOM 6345 N N . SER A 1 807 ? -9.329 -26.080 19.734 1.00 27.19 ? 842 SER A N 1 ATOM 6346 C CA . SER A 1 807 ? -9.642 -25.589 18.393 1.00 28.88 ? 842 SER A CA 1 ATOM 6347 C C . SER A 1 807 ? -8.795 -24.366 18.045 1.00 26.92 ? 842 SER A C 1 ATOM 6348 O O . SER A 1 807 ? -9.055 -23.713 17.041 1.00 28.98 ? 842 SER A O 1 ATOM 6349 C CB . SER A 1 807 ? -11.128 -25.217 18.333 1.00 30.14 ? 842 SER A CB 1 ATOM 6350 O OG . SER A 1 807 ? -11.383 -24.152 19.239 1.00 31.42 ? 842 SER A OG 1 ATOM 6351 N N . ARG A 1 808 ? -7.776 -24.073 18.852 1.00 23.69 ? 843 ARG A N 1 ATOM 6352 C CA . ARG A 1 808 ? -6.954 -22.871 18.709 1.00 24.20 ? 843 ARG A CA 1 ATOM 6353 C C . ARG A 1 808 ? -5.623 -23.258 18.072 1.00 22.63 ? 843 ARG A C 1 ATOM 6354 O O . ARG A 1 808 ? -5.187 -24.410 18.177 1.00 21.59 ? 843 ARG A O 1 ATOM 6355 C CB . ARG A 1 808 ? -6.719 -22.229 20.092 1.00 25.28 ? 843 ARG A CB 1 ATOM 6356 C CG . ARG A 1 808 ? -7.969 -22.010 20.948 1.00 26.99 ? 843 ARG A CG 1 ATOM 6357 C CD . ARG A 1 808 ? -9.171 -21.446 20.202 1.00 30.14 ? 843 ARG A CD 1 ATOM 6358 N NE . ARG A 1 808 ? -8.935 -20.117 19.628 1.00 32.65 ? 843 ARG A NE 1 ATOM 6359 C CZ . ARG A 1 808 ? -9.679 -19.551 18.675 1.00 35.10 ? 843 ARG A CZ 1 ATOM 6360 N NH1 . ARG A 1 808 ? -10.727 -20.177 18.135 1.00 41.25 ? 843 ARG A NH1 1 ATOM 6361 N NH2 . ARG A 1 808 ? -9.366 -18.344 18.239 1.00 37.54 ? 843 ARG A NH2 1 ATOM 6362 N N . SER A 1 809 ? -4.999 -22.311 17.384 1.00 23.05 ? 844 SER A N 1 ATOM 6363 C CA . SER A 1 809 ? -3.647 -22.510 16.857 1.00 23.47 ? 844 SER A CA 1 ATOM 6364 C C . SER A 1 809 ? -2.640 -22.641 18.002 1.00 22.06 ? 844 SER A C 1 ATOM 6365 O O . SER A 1 809 ? -2.889 -22.164 19.126 1.00 21.74 ? 844 SER A O 1 ATOM 6366 C CB . SER A 1 809 ? -3.231 -21.352 15.940 1.00 26.00 ? 844 SER A CB 1 ATOM 6367 O OG . SER A 1 809 ? -2.805 -20.245 16.723 1.00 26.86 ? 844 SER A OG 1 ATOM 6368 N N . TYR A 1 810 ? -1.519 -23.310 17.749 1.00 20.29 ? 845 TYR A N 1 ATOM 6369 C CA . TYR A 1 810 ? -0.532 -23.489 18.815 1.00 20.52 ? 845 TYR A CA 1 ATOM 6370 C C . TYR A 1 810 ? 0.061 -22.159 19.283 1.00 20.64 ? 845 TYR A C 1 ATOM 6371 O O . TYR A 1 810 ? 0.271 -21.979 20.476 1.00 19.84 ? 845 TYR A O 1 ATOM 6372 C CB . TYR A 1 810 ? 0.539 -24.516 18.454 1.00 21.23 ? 845 TYR A CB 1 ATOM 6373 C CG . TYR A 1 810 ? 1.498 -24.861 19.571 1.00 20.87 ? 845 TYR A CG 1 ATOM 6374 C CD1 . TYR A 1 810 ? 1.037 -25.318 20.800 1.00 22.30 ? 845 TYR A CD1 1 ATOM 6375 C CD2 . TYR A 1 810 ? 2.867 -24.759 19.395 1.00 21.01 ? 845 TYR A CD2 1 ATOM 6376 C CE1 . TYR A 1 810 ? 1.910 -25.645 21.825 1.00 21.24 ? 845 TYR A CE1 1 ATOM 6377 C CE2 . TYR A 1 810 ? 3.744 -25.086 20.412 1.00 21.78 ? 845 TYR A CE2 1 ATOM 6378 C CZ . TYR A 1 810 ? 3.252 -25.534 21.628 1.00 21.96 ? 845 TYR A CZ 1 ATOM 6379 O OH . TYR A 1 810 ? 4.122 -25.862 22.640 1.00 24.43 ? 845 TYR A OH 1 ATOM 6380 N N . SER A 1 811 ? 0.245 -21.198 18.390 1.00 21.24 ? 846 SER A N 1 ATOM 6381 C CA A SER A 1 811 ? 0.742 -19.882 18.798 0.50 21.06 ? 846 SER A CA 1 ATOM 6382 C CA B SER A 1 811 ? 0.747 -19.886 18.797 0.50 21.18 ? 846 SER A CA 1 ATOM 6383 C C . SER A 1 811 ? -0.255 -19.158 19.716 1.00 20.85 ? 846 SER A C 1 ATOM 6384 O O . SER A 1 811 ? 0.160 -18.516 20.663 1.00 17.98 ? 846 SER A O 1 ATOM 6385 C CB A SER A 1 811 ? 1.078 -19.006 17.590 0.50 22.05 ? 846 SER A CB 1 ATOM 6386 C CB B SER A 1 811 ? 1.121 -19.026 17.583 0.50 22.35 ? 846 SER A CB 1 ATOM 6387 O OG A SER A 1 811 ? -0.061 -18.767 16.797 0.50 22.27 ? 846 SER A OG 1 ATOM 6388 O OG B SER A 1 811 ? 2.332 -19.494 16.993 0.50 22.58 ? 846 SER A OG 1 ATOM 6389 N N . GLU A 1 812 ? -1.567 -19.280 19.441 1.00 20.55 ? 847 GLU A N 1 ATOM 6390 C CA . GLU A 1 812 ? -2.605 -18.718 20.319 1.00 21.07 ? 847 GLU A CA 1 ATOM 6391 C C . GLU A 1 812 ? -2.572 -19.363 21.724 1.00 19.20 ? 847 GLU A C 1 ATOM 6392 O O . GLU A 1 812 ? -2.649 -18.679 22.729 1.00 18.29 ? 847 GLU A O 1 ATOM 6393 C CB . GLU A 1 812 ? -4.012 -18.913 19.737 1.00 25.33 ? 847 GLU A CB 1 ATOM 6394 C CG . GLU A 1 812 ? -4.275 -18.023 18.529 1.00 28.29 ? 847 GLU A CG 1 ATOM 6395 C CD . GLU A 1 812 ? -5.517 -18.387 17.713 1.00 34.51 ? 847 GLU A CD 1 ATOM 6396 O OE1 . GLU A 1 812 ? -6.070 -19.528 17.796 1.00 32.53 ? 847 GLU A OE1 1 ATOM 6397 O OE2 . GLU A 1 812 ? -5.931 -17.486 16.956 1.00 37.78 ? 847 GLU A OE2 1 ATOM 6398 N N . ILE A 1 813 ? -2.422 -20.680 21.763 1.00 18.05 ? 848 ILE A N 1 ATOM 6399 C CA . ILE A 1 813 ? -2.229 -21.401 23.035 1.00 16.76 ? 848 ILE A CA 1 ATOM 6400 C C . ILE A 1 813 ? -0.961 -20.955 23.753 1.00 15.37 ? 848 ILE A C 1 ATOM 6401 O O . ILE A 1 813 ? -0.954 -20.815 24.970 1.00 15.34 ? 848 ILE A O 1 ATOM 6402 C CB . ILE A 1 813 ? -2.223 -22.936 22.800 1.00 17.88 ? 848 ILE A CB 1 ATOM 6403 C CG1 . ILE A 1 813 ? -3.628 -23.418 22.395 1.00 18.14 ? 848 ILE A CG1 1 ATOM 6404 C CG2 . ILE A 1 813 ? -1.677 -23.721 23.986 1.00 18.40 ? 848 ILE A CG2 1 ATOM 6405 C CD1 . ILE A 1 813 ? -4.771 -23.016 23.299 1.00 18.88 ? 848 ILE A CD1 1 ATOM 6406 N N . LEU A 1 814 ? 0.126 -20.715 23.036 1.00 15.21 ? 849 LEU A N 1 ATOM 6407 C CA . LEU A 1 814 ? 1.322 -20.198 23.727 1.00 15.99 ? 849 LEU A CA 1 ATOM 6408 C C . LEU A 1 814 ? 1.092 -18.832 24.379 1.00 15.33 ? 849 LEU A C 1 ATOM 6409 O O . LEU A 1 814 ? 1.542 -18.601 25.510 1.00 17.00 ? 849 LEU A O 1 ATOM 6410 C CB . LEU A 1 814 ? 2.525 -20.170 22.780 1.00 16.37 ? 849 LEU A CB 1 ATOM 6411 C CG . LEU A 1 814 ? 3.047 -21.560 22.382 1.00 16.77 ? 849 LEU A CG 1 ATOM 6412 C CD1 . LEU A 1 814 ? 4.235 -21.404 21.466 1.00 17.64 ? 849 LEU A CD1 1 ATOM 6413 C CD2 . LEU A 1 814 ? 3.409 -22.426 23.573 1.00 16.83 ? 849 LEU A CD2 1 ATOM 6414 N N . THR A 1 815 ? 0.357 -17.949 23.696 1.00 17.09 ? 850 THR A N 1 ATOM 6415 C CA . THR A 1 815 ? -0.056 -16.664 24.241 1.00 16.11 ? 850 THR A CA 1 ATOM 6416 C C . THR A 1 815 ? -0.913 -16.899 25.503 1.00 16.15 ? 850 THR A C 1 ATOM 6417 O O . THR A 1 815 ? -0.647 -16.315 26.546 1.00 16.81 ? 850 THR A O 1 ATOM 6418 C CB . THR A 1 815 ? -0.834 -15.833 23.190 1.00 18.99 ? 850 THR A CB 1 ATOM 6419 O OG1 . THR A 1 815 ? -0.029 -15.686 21.992 1.00 18.09 ? 850 THR A OG1 1 ATOM 6420 C CG2 . THR A 1 815 ? -1.200 -14.480 23.730 1.00 21.11 ? 850 THR A CG2 1 ATOM 6421 N N . LEU A 1 816 ? -1.913 -17.774 25.409 1.00 14.52 ? 851 LEU A N 1 ATOM 6422 C CA . LEU A 1 816 ? -2.735 -18.135 26.577 1.00 15.10 ? 851 LEU A CA 1 ATOM 6423 C C . LEU A 1 816 ? -1.896 -18.601 27.766 1.00 14.99 ? 851 LEU A C 1 ATOM 6424 O O . LEU A 1 816 ? -2.136 -18.185 28.906 1.00 15.65 ? 851 LEU A O 1 ATOM 6425 C CB . LEU A 1 816 ? -3.738 -19.221 26.225 1.00 15.89 ? 851 LEU A CB 1 ATOM 6426 C CG . LEU A 1 816 ? -4.773 -19.658 27.261 1.00 16.21 ? 851 LEU A CG 1 ATOM 6427 C CD1 . LEU A 1 816 ? -5.821 -18.600 27.535 1.00 16.74 ? 851 LEU A CD1 1 ATOM 6428 C CD2 . LEU A 1 816 ? -5.429 -20.938 26.803 1.00 17.51 ? 851 LEU A CD2 1 ATOM 6429 N N . LYS A 1 817 ? -0.906 -19.456 27.521 1.00 15.13 ? 852 LYS A N 1 ATOM 6430 C CA . LYS A 1 817 ? -0.092 -20.035 28.596 1.00 15.16 ? 852 LYS A CA 1 ATOM 6431 C C . LYS A 1 817 ? 0.808 -19.022 29.269 1.00 14.40 ? 852 LYS A C 1 ATOM 6432 O O . LYS A 1 817 ? 1.206 -19.218 30.407 1.00 14.83 ? 852 LYS A O 1 ATOM 6433 C CB . LYS A 1 817 ? 0.744 -21.222 28.081 1.00 16.16 ? 852 LYS A CB 1 ATOM 6434 C CG . LYS A 1 817 ? -0.084 -22.422 27.670 1.00 17.42 ? 852 LYS A CG 1 ATOM 6435 C CD . LYS A 1 817 ? 0.858 -23.546 27.247 1.00 19.46 ? 852 LYS A CD 1 ATOM 6436 C CE . LYS A 1 817 ? 0.123 -24.862 27.157 1.00 22.40 ? 852 LYS A CE 1 ATOM 6437 N NZ . LYS A 1 817 ? 1.080 -25.934 26.735 1.00 24.35 ? 852 LYS A NZ 1 ATOM 6438 N N . THR A 1 818 ? 1.144 -17.937 28.565 1.00 14.80 ? 853 THR A N 1 ATOM 6439 C CA . THR A 1 818 ? 1.939 -16.869 29.179 1.00 15.21 ? 853 THR A CA 1 ATOM 6440 C C . THR A 1 818 ? 1.118 -15.761 29.854 1.00 14.79 ? 853 THR A C 1 ATOM 6441 O O . THR A 1 818 ? 1.696 -14.857 30.487 1.00 14.20 ? 853 THR A O 1 ATOM 6442 C CB . THR A 1 818 ? 2.901 -16.207 28.159 1.00 15.50 ? 853 THR A CB 1 ATOM 6443 O OG1 . THR A 1 818 ? 2.156 -15.581 27.124 1.00 16.59 ? 853 THR A OG1 1 ATOM 6444 C CG2 . THR A 1 818 ? 3.868 -17.190 27.571 1.00 15.72 ? 853 THR A CG2 1 ATOM 6445 N N . TYR A 1 819 ? -0.210 -15.803 29.710 1.00 14.17 ? 854 TYR A N 1 ATOM 6446 C CA . TYR A 1 819 ? -1.118 -14.840 30.345 1.00 14.46 ? 854 TYR A CA 1 ATOM 6447 C C . TYR A 1 819 ? -0.966 -14.877 31.870 1.00 13.06 ? 854 TYR A C 1 ATOM 6448 O O . TYR A 1 819 ? -0.793 -15.932 32.476 1.00 13.67 ? 854 TYR A O 1 ATOM 6449 C CB . TYR A 1 819 ? -2.571 -15.159 29.961 1.00 15.50 ? 854 TYR A CB 1 ATOM 6450 C CG . TYR A 1 819 ? -3.557 -14.225 30.584 1.00 15.98 ? 854 TYR A CG 1 ATOM 6451 C CD1 . TYR A 1 819 ? -3.705 -12.911 30.112 1.00 18.72 ? 854 TYR A CD1 1 ATOM 6452 C CD2 . TYR A 1 819 ? -4.299 -14.610 31.702 1.00 16.55 ? 854 TYR A CD2 1 ATOM 6453 C CE1 . TYR A 1 819 ? -4.593 -12.020 30.710 1.00 18.99 ? 854 TYR A CE1 1 ATOM 6454 C CE2 . TYR A 1 819 ? -5.204 -13.743 32.281 1.00 16.39 ? 854 TYR A CE2 1 ATOM 6455 C CZ . TYR A 1 819 ? -5.339 -12.457 31.799 1.00 20.03 ? 854 TYR A CZ 1 ATOM 6456 O OH . TYR A 1 819 ? -6.225 -11.592 32.400 1.00 21.71 ? 854 TYR A OH 1 ATOM 6457 N N . LEU A 1 820 ? -0.988 -13.706 32.495 1.00 12.60 ? 855 LEU A N 1 ATOM 6458 C CA . LEU A 1 820 ? -1.072 -13.623 33.947 1.00 12.87 ? 855 LEU A CA 1 ATOM 6459 C C . LEU A 1 820 ? -2.295 -12.806 34.288 1.00 13.50 ? 855 LEU A C 1 ATOM 6460 O O . LEU A 1 820 ? -2.420 -11.672 33.834 1.00 15.56 ? 855 LEU A O 1 ATOM 6461 C CB . LEU A 1 820 ? 0.166 -12.919 34.507 1.00 12.70 ? 855 LEU A CB 1 ATOM 6462 C CG . LEU A 1 820 ? 0.271 -12.840 36.031 1.00 13.19 ? 855 LEU A CG 1 ATOM 6463 C CD1 . LEU A 1 820 ? 0.585 -14.226 36.581 1.00 13.06 ? 855 LEU A CD1 1 ATOM 6464 C CD2 . LEU A 1 820 ? 1.365 -11.853 36.401 1.00 14.02 ? 855 LEU A CD2 1 ATOM 6465 N N . HIS A 1 821 ? -3.191 -13.351 35.108 1.00 15.16 ? 856 HIS A N 1 ATOM 6466 C CA . HIS A 1 821 ? -4.301 -12.553 35.654 1.00 17.47 ? 856 HIS A CA 1 ATOM 6467 C C . HIS A 1 821 ? -3.782 -11.734 36.820 1.00 17.50 ? 856 HIS A C 1 ATOM 6468 O O . HIS A 1 821 ? -3.478 -12.309 37.857 1.00 17.91 ? 856 HIS A O 1 ATOM 6469 C CB . HIS A 1 821 ? -5.449 -13.456 36.117 1.00 18.84 ? 856 HIS A CB 1 ATOM 6470 C CG . HIS A 1 821 ? -6.735 -12.721 36.262 1.00 22.90 ? 856 HIS A CG 1 ATOM 6471 N ND1 . HIS A 1 821 ? -7.804 -12.920 35.420 1.00 31.88 ? 856 HIS A ND1 1 ATOM 6472 C CD2 . HIS A 1 821 ? -7.102 -11.728 37.100 1.00 30.54 ? 856 HIS A CD2 1 ATOM 6473 C CE1 . HIS A 1 821 ? -8.795 -12.114 35.766 1.00 31.08 ? 856 HIS A CE1 1 ATOM 6474 N NE2 . HIS A 1 821 ? -8.395 -11.383 36.785 1.00 27.91 ? 856 HIS A NE2 1 ATOM 6475 N N . THR A 1 822 ? -3.692 -10.401 36.678 1.00 17.32 ? 857 THR A N 1 ATOM 6476 C CA . THR A 1 822 ? -2.959 -9.592 37.680 1.00 19.63 ? 857 THR A CA 1 ATOM 6477 C C . THR A 1 822 ? -3.825 -9.087 38.832 1.00 22.93 ? 857 THR A C 1 ATOM 6478 O O . THR A 1 822 ? -3.278 -8.771 39.915 1.00 23.80 ? 857 THR A O 1 ATOM 6479 C CB . THR A 1 822 ? -2.271 -8.377 37.052 1.00 21.23 ? 857 THR A CB 1 ATOM 6480 O OG1 . THR A 1 822 ? -3.247 -7.540 36.442 1.00 23.83 ? 857 THR A OG1 1 ATOM 6481 C CG2 . THR A 1 822 ? -1.289 -8.821 36.010 1.00 22.53 ? 857 THR A CG2 1 ATOM 6482 N N . TYR A 1 823 ? -5.142 -8.979 38.600 1.00 23.17 ? 858 TYR A N 1 ATOM 6483 C CA . TYR A 1 823 ? -6.093 -8.445 39.620 1.00 24.86 ? 858 TYR A CA 1 ATOM 6484 C C . TYR A 1 823 ? -5.843 -6.976 39.921 1.00 29.27 ? 858 TYR A C 1 ATOM 6485 O O . TYR A 1 823 ? -6.146 -6.494 41.011 1.00 31.84 ? 858 TYR A O 1 ATOM 6486 C CB . TYR A 1 823 ? -6.104 -9.276 40.922 1.00 23.05 ? 858 TYR A CB 1 ATOM 6487 C CG . TYR A 1 823 ? -6.440 -10.701 40.664 1.00 23.37 ? 858 TYR A CG 1 ATOM 6488 C CD1 . TYR A 1 823 ? -7.765 -11.094 40.488 1.00 24.05 ? 858 TYR A CD1 1 ATOM 6489 C CD2 . TYR A 1 823 ? -5.441 -11.662 40.532 1.00 22.95 ? 858 TYR A CD2 1 ATOM 6490 C CE1 . TYR A 1 823 ? -8.090 -12.413 40.222 1.00 25.68 ? 858 TYR A CE1 1 ATOM 6491 C CE2 . TYR A 1 823 ? -5.752 -12.979 40.268 1.00 22.25 ? 858 TYR A CE2 1 ATOM 6492 C CZ . TYR A 1 823 ? -7.076 -13.355 40.098 1.00 24.88 ? 858 TYR A CZ 1 ATOM 6493 O OH . TYR A 1 823 ? -7.386 -14.673 39.816 1.00 26.22 ? 858 TYR A OH 1 ATOM 6494 N N . GLU A 1 824 ? -5.331 -6.265 38.923 1.00 30.43 ? 859 GLU A N 1 ATOM 6495 C CA . GLU A 1 824 ? -5.085 -4.837 39.009 1.00 35.42 ? 859 GLU A CA 1 ATOM 6496 C C . GLU A 1 824 ? -6.076 -4.071 38.138 1.00 42.56 ? 859 GLU A C 1 ATOM 6497 O O . GLU A 1 824 ? -6.519 -4.572 37.102 1.00 49.19 ? 859 GLU A O 1 ATOM 6498 C CB . GLU A 1 824 ? -3.672 -4.573 38.539 1.00 32.95 ? 859 GLU A CB 1 ATOM 6499 C CG . GLU A 1 824 ? -2.622 -5.075 39.501 1.00 32.31 ? 859 GLU A CG 1 ATOM 6500 C CD . GLU A 1 824 ? -2.335 -4.092 40.630 1.00 33.80 ? 859 GLU A CD 1 ATOM 6501 O OE1 . GLU A 1 824 ? -2.132 -2.868 40.382 1.00 31.80 ? 859 GLU A OE1 1 ATOM 6502 O OE2 . GLU A 1 824 ? -2.292 -4.545 41.789 1.00 37.68 ? 859 GLU A OE2 1 ATOM 6503 N N . SER A 1 825 ? -6.413 -2.854 38.553 1.00 40.47 ? 860 SER A N 1 HETATM 6504 C C1 . NAG B 2 . ? 15.230 -19.731 32.554 1.00 15.51 ? 901 NAG A C1 1 HETATM 6505 C C2 . NAG B 2 . ? 14.869 -21.014 33.244 1.00 16.17 ? 901 NAG A C2 1 HETATM 6506 C C3 . NAG B 2 . ? 16.128 -21.698 33.743 1.00 16.12 ? 901 NAG A C3 1 HETATM 6507 C C4 . NAG B 2 . ? 17.126 -21.906 32.596 1.00 17.97 ? 901 NAG A C4 1 HETATM 6508 C C5 . NAG B 2 . ? 17.314 -20.624 31.782 1.00 17.58 ? 901 NAG A C5 1 HETATM 6509 C C6 . NAG B 2 . ? 18.162 -20.883 30.538 1.00 19.54 ? 901 NAG A C6 1 HETATM 6510 C C7 . NAG B 2 . ? 12.741 -21.273 34.417 1.00 17.35 ? 901 NAG A C7 1 HETATM 6511 C C8 . NAG B 2 . ? 12.010 -20.983 35.687 1.00 17.62 ? 901 NAG A C8 1 HETATM 6512 N N2 . NAG B 2 . ? 13.983 -20.776 34.364 1.00 15.44 ? 901 NAG A N2 1 HETATM 6513 O O3 . NAG B 2 . ? 15.802 -22.967 34.307 1.00 16.60 ? 901 NAG A O3 1 HETATM 6514 O O4 . NAG B 2 . ? 18.379 -22.165 33.198 1.00 20.46 ? 901 NAG A O4 1 HETATM 6515 O O5 . NAG B 2 . ? 16.048 -20.097 31.414 1.00 15.85 ? 901 NAG A O5 1 HETATM 6516 O O6 . NAG B 2 . ? 17.604 -21.933 29.737 1.00 21.20 ? 901 NAG A O6 1 HETATM 6517 O O7 . NAG B 2 . ? 12.222 -21.931 33.522 1.00 19.56 ? 901 NAG A O7 1 HETATM 6518 C C1 . NAG C 2 . ? 18.995 -23.345 32.709 1.00 27.27 ? 902 NAG A C1 1 HETATM 6519 C C2 . NAG C 2 . ? 20.494 -23.266 33.010 1.00 32.05 ? 902 NAG A C2 1 HETATM 6520 C C3 . NAG C 2 . ? 21.142 -24.601 32.638 1.00 34.87 ? 902 NAG A C3 1 HETATM 6521 C C4 . NAG C 2 . ? 20.429 -25.866 33.132 1.00 35.66 ? 902 NAG A C4 1 HETATM 6522 C C5 . NAG C 2 . ? 18.924 -25.729 32.842 1.00 34.48 ? 902 NAG A C5 1 HETATM 6523 C C6 . NAG C 2 . ? 18.057 -26.809 33.478 1.00 35.92 ? 902 NAG A C6 1 HETATM 6524 C C7 . NAG C 2 . ? 21.265 -20.933 32.469 1.00 39.15 ? 902 NAG A C7 1 HETATM 6525 C C8 . NAG C 2 . ? 21.923 -20.097 31.396 1.00 41.90 ? 902 NAG A C8 1 HETATM 6526 N N2 . NAG C 2 . ? 21.104 -22.227 32.183 1.00 37.20 ? 902 NAG A N2 1 HETATM 6527 O O3 . NAG C 2 . ? 22.517 -24.539 33.057 1.00 40.70 ? 902 NAG A O3 1 HETATM 6528 O O4 . NAG C 2 . ? 20.996 -26.961 32.375 1.00 44.21 ? 902 NAG A O4 1 HETATM 6529 O O5 . NAG C 2 . ? 18.403 -24.479 33.326 1.00 28.03 ? 902 NAG A O5 1 HETATM 6530 O O6 . NAG C 2 . ? 18.310 -26.804 34.889 1.00 37.56 ? 902 NAG A O6 1 HETATM 6531 O O7 . NAG C 2 . ? 20.909 -20.433 33.506 1.00 43.35 ? 902 NAG A O7 1 HETATM 6532 C C1 . BMA D 3 . ? 21.011 -28.300 32.930 1.00 58.45 ? 903 BMA A C1 1 HETATM 6533 C C2 . BMA D 3 . ? 20.535 -29.258 31.843 1.00 62.92 ? 903 BMA A C2 1 HETATM 6534 C C3 . BMA D 3 . ? 20.511 -30.723 32.305 1.00 72.16 ? 903 BMA A C3 1 HETATM 6535 C C4 . BMA D 3 . ? 21.763 -31.143 33.078 1.00 73.08 ? 903 BMA A C4 1 HETATM 6536 C C5 . BMA D 3 . ? 22.330 -30.038 33.974 1.00 70.30 ? 903 BMA A C5 1 HETATM 6537 C C6 . BMA D 3 . ? 23.766 -30.382 34.365 1.00 72.41 ? 903 BMA A C6 1 HETATM 6538 O O2 . BMA D 3 . ? 21.418 -29.112 30.727 1.00 56.42 ? 903 BMA A O2 1 HETATM 6539 O O3 . BMA D 3 . ? 20.383 -31.612 31.182 1.00 76.32 ? 903 BMA A O3 1 HETATM 6540 O O4 . BMA D 3 . ? 21.431 -32.285 33.881 1.00 68.79 ? 903 BMA A O4 1 HETATM 6541 O O5 . BMA D 3 . ? 22.310 -28.756 33.320 1.00 67.22 ? 903 BMA A O5 1 HETATM 6542 O O6 . BMA D 3 . ? 24.017 -30.012 35.724 1.00 74.99 ? 903 BMA A O6 1 HETATM 6543 ZN ZN . ZN E 4 . ? 14.716 5.350 38.405 1.00 18.39 ? 904 ZN A ZN 1 HETATM 6544 ZN ZN . ZN F 4 . ? 15.073 2.539 34.871 1.00 21.03 ? 905 ZN A ZN 1 HETATM 6545 C C18 . 5JK G 5 . ? 29.606 -4.231 31.253 1.00 24.56 ? 906 5JK A C18 1 HETATM 6546 C C13 . 5JK G 5 . ? 28.628 -4.114 30.063 1.00 24.75 ? 906 5JK A C13 1 HETATM 6547 C C12 . 5JK G 5 . ? 27.399 -5.010 30.229 1.00 22.55 ? 906 5JK A C12 1 HETATM 6548 C C11 . 5JK G 5 . ? 27.757 -6.491 30.175 1.00 22.21 ? 906 5JK A C11 1 HETATM 6549 C C9 . 5JK G 5 . ? 28.587 -6.915 28.929 1.00 23.08 ? 906 5JK A C9 1 HETATM 6550 C C10 . 5JK G 5 . ? 29.051 -8.369 29.014 1.00 22.28 ? 906 5JK A C10 1 HETATM 6551 C C19 . 5JK G 5 . ? 30.035 -8.649 30.172 1.00 22.16 ? 906 5JK A C19 1 HETATM 6552 C C1 . 5JK G 5 . ? 27.783 -9.236 29.104 1.00 21.16 ? 906 5JK A C1 1 HETATM 6553 C C2 . 5JK G 5 . ? 28.011 -10.696 28.795 1.00 22.70 ? 906 5JK A C2 1 HETATM 6554 C C3 . 5JK G 5 . ? 28.467 -10.780 27.361 1.00 24.35 ? 906 5JK A C3 1 HETATM 6555 O O1 . 5JK G 5 . ? 28.589 -12.134 26.969 1.00 24.83 ? 906 5JK A O1 1 HETATM 6556 C C4 . 5JK G 5 . ? 29.773 -10.060 27.138 1.00 24.55 ? 906 5JK A C4 1 HETATM 6557 C C5 . 5JK G 5 . ? 29.850 -8.704 27.772 1.00 23.69 ? 906 5JK A C5 1 HETATM 6558 C C6 . 5JK G 5 . ? 30.643 -7.791 27.160 1.00 24.25 ? 906 5JK A C6 1 HETATM 6559 C C7 . 5JK G 5 . ? 30.350 -6.321 27.286 1.00 24.34 ? 906 5JK A C7 1 HETATM 6560 O O2 . 5JK G 5 . ? 29.400 -6.113 26.230 1.00 21.59 ? 906 5JK A O2 1 HETATM 6561 C C8 . 5JK G 5 . ? 29.749 -5.955 28.642 1.00 23.49 ? 906 5JK A C8 1 HETATM 6562 C C14 . 5JK G 5 . ? 29.260 -4.509 28.719 1.00 24.91 ? 906 5JK A C14 1 HETATM 6563 C C15 . 5JK G 5 . ? 30.259 -3.403 28.448 1.00 27.07 ? 906 5JK A C15 1 HETATM 6564 C C16 . 5JK G 5 . ? 29.569 -2.164 29.008 1.00 27.30 ? 906 5JK A C16 1 HETATM 6565 C C17 . 5JK G 5 . ? 28.315 -2.634 29.752 1.00 26.89 ? 906 5JK A C17 1 HETATM 6566 C C20 . 5JK G 5 . ? 27.912 -1.663 30.885 1.00 29.98 ? 906 5JK A C20 1 HETATM 6567 C C21 . 5JK G 5 . ? 26.767 -2.214 31.739 1.00 30.40 ? 906 5JK A C21 1 HETATM 6568 C C22 . 5JK G 5 . ? 27.485 -0.299 30.331 1.00 30.80 ? 906 5JK A C22 1 HETATM 6569 C C23 . 5JK G 5 . ? 27.460 0.813 31.386 1.00 32.59 ? 906 5JK A C23 1 HETATM 6570 C C24 . 5JK G 5 . ? 27.409 2.181 30.708 1.00 33.54 ? 906 5JK A C24 1 HETATM 6571 C C25 . 5JK G 5 . ? 26.942 3.303 31.630 1.00 38.02 ? 906 5JK A C25 1 HETATM 6572 C C27 . 5JK G 5 . ? 26.584 4.532 30.799 1.00 38.22 ? 906 5JK A C27 1 HETATM 6573 C C26 . 5JK G 5 . ? 27.972 3.623 32.719 1.00 40.30 ? 906 5JK A C26 1 HETATM 6574 CA CA . CA H 6 . ? 13.105 -27.635 41.690 1.00 16.92 ? 907 CA A CA 1 HETATM 6575 I I . IOD I 7 . ? 18.066 -3.018 43.957 0.95 22.37 ? 908 IOD A I 1 HETATM 6576 I I . IOD J 7 . ? 24.529 -4.536 48.108 0.45 37.63 ? 909 IOD A I 1 HETATM 6577 I I . IOD K 7 . ? 16.762 -6.252 3.278 0.35 37.03 ? 910 IOD A I 1 HETATM 6578 I I . IOD L 7 . ? 36.121 -10.174 35.901 0.35 36.60 ? 911 IOD A I 1 HETATM 6579 I I . IOD M 7 . ? 0.700 1.296 65.661 0.35 38.89 ? 912 IOD A I 1 HETATM 6580 I I . IOD N 7 . ? -7.870 -49.742 54.000 0.55 54.60 ? 913 IOD A I 1 HETATM 6581 I I . IOD O 7 . ? -22.854 -46.210 41.531 0.40 46.43 ? 914 IOD A I 1 HETATM 6582 I I . IOD P 7 . ? -6.744 -18.951 23.241 0.60 28.57 ? 915 IOD A I 1 HETATM 6583 I I . IOD Q 7 . ? -19.947 -25.512 31.842 0.45 31.10 ? 916 IOD A I 1 HETATM 6584 I I . IOD R 7 . ? 0.981 -21.892 15.070 0.35 42.18 ? 917 IOD A I 1 HETATM 6585 S S . SCN S 8 . ? -9.811 -33.950 55.682 1.00 66.14 ? 918 SCN A S 1 HETATM 6586 C C . SCN S 8 . ? -11.093 -33.449 54.704 1.00 56.08 ? 918 SCN A C 1 HETATM 6587 N N . SCN S 8 . ? -11.991 -33.126 54.048 1.00 56.94 ? 918 SCN A N 1 HETATM 6588 S S . SCN T 8 . ? 28.911 -3.272 24.741 1.00 55.84 ? 919 SCN A S 1 HETATM 6589 C C . SCN T 8 . ? 27.687 -3.612 23.629 1.00 46.67 ? 919 SCN A C 1 HETATM 6590 N N . SCN T 8 . ? 26.840 -3.853 22.880 1.00 41.12 ? 919 SCN A N 1 HETATM 6591 S S . SCN U 8 . ? 30.275 10.343 31.272 1.00 41.79 ? 920 SCN A S 1 HETATM 6592 C C . SCN U 8 . ? 30.947 9.395 32.489 1.00 31.87 ? 920 SCN A C 1 HETATM 6593 N N . SCN U 8 . ? 31.411 8.738 33.314 1.00 38.57 ? 920 SCN A N 1 HETATM 6594 S S . SCN V 8 . ? 15.484 11.345 24.654 1.00 33.23 ? 921 SCN A S 1 HETATM 6595 C C . SCN V 8 . ? 15.091 12.591 25.721 1.00 42.59 ? 921 SCN A C 1 HETATM 6596 N N . SCN V 8 . ? 14.862 13.433 26.479 1.00 40.21 ? 921 SCN A N 1 HETATM 6597 S S . SCN W 8 . ? -0.213 -6.769 9.049 1.00 31.22 ? 922 SCN A S 1 HETATM 6598 C C . SCN W 8 . ? -0.013 -8.422 8.802 1.00 30.29 ? 922 SCN A C 1 HETATM 6599 N N . SCN W 8 . ? 0.129 -9.563 8.651 1.00 37.88 ? 922 SCN A N 1 HETATM 6600 S S . SCN X 8 . ? 25.659 -14.672 36.201 1.00 48.72 ? 923 SCN A S 1 HETATM 6601 C C . SCN X 8 . ? 27.160 -14.485 36.924 1.00 33.85 ? 923 SCN A C 1 HETATM 6602 N N . SCN X 8 . ? 28.183 -14.360 37.421 1.00 26.49 ? 923 SCN A N 1 HETATM 6603 S S . SCN Y 8 . ? 9.509 -44.939 34.538 1.00 56.06 ? 924 SCN A S 1 HETATM 6604 C C . SCN Y 8 . ? 9.460 -44.529 36.176 1.00 44.67 ? 924 SCN A C 1 HETATM 6605 N N . SCN Y 8 . ? 9.432 -44.223 37.295 1.00 45.62 ? 924 SCN A N 1 HETATM 6606 S S . SCN Z 8 . ? -5.606 -5.971 24.548 1.00 46.49 ? 925 SCN A S 1 HETATM 6607 C C . SCN Z 8 . ? -5.619 -6.448 22.920 1.00 34.90 ? 925 SCN A C 1 HETATM 6608 N N . SCN Z 8 . ? -5.628 -6.784 21.803 1.00 32.76 ? 925 SCN A N 1 HETATM 6609 S S . SCN AA 8 . ? 37.942 10.334 30.021 1.00 46.45 ? 926 SCN A S 1 HETATM 6610 C C . SCN AA 8 . ? 37.586 11.700 29.102 1.00 39.23 ? 926 SCN A C 1 HETATM 6611 N N . SCN AA 8 . ? 37.334 12.627 28.458 1.00 44.69 ? 926 SCN A N 1 HETATM 6612 S S . SCN BA 8 . ? 11.090 -38.312 39.117 1.00 47.13 ? 927 SCN A S 1 HETATM 6613 C C . SCN BA 8 . ? 12.758 -38.539 39.249 1.00 51.09 ? 927 SCN A C 1 HETATM 6614 N N . SCN BA 8 . ? 13.902 -38.702 39.344 1.00 55.23 ? 927 SCN A N 1 HETATM 6615 NA NA . NA CA 9 . ? -1.845 -35.794 61.331 1.00 31.11 ? 928 NA A NA 1 HETATM 6616 NA NA . NA DA 9 . ? -1.643 -14.846 60.077 1.00 18.54 ? 929 NA A NA 1 HETATM 6617 C C1 . GOL EA 10 . ? 1.417 -27.121 15.653 1.00 48.64 ? 930 GOL A C1 1 HETATM 6618 O O1 . GOL EA 10 . ? 2.585 -26.308 15.466 1.00 48.24 ? 930 GOL A O1 1 HETATM 6619 C C2 . GOL EA 10 . ? 1.477 -27.868 16.989 1.00 44.99 ? 930 GOL A C2 1 HETATM 6620 O O2 . GOL EA 10 . ? 2.659 -28.679 17.047 1.00 39.61 ? 930 GOL A O2 1 HETATM 6621 C C3 . GOL EA 10 . ? 0.240 -28.750 17.168 1.00 47.65 ? 930 GOL A C3 1 HETATM 6622 O O3 . GOL EA 10 . ? -0.866 -28.015 17.713 1.00 52.95 ? 930 GOL A O3 1 HETATM 6623 C C1 . GOL FA 10 . ? -5.868 -35.268 60.605 1.00 54.33 ? 931 GOL A C1 1 HETATM 6624 O O1 . GOL FA 10 . ? -6.986 -34.706 59.911 1.00 57.84 ? 931 GOL A O1 1 HETATM 6625 C C2 . GOL FA 10 . ? -5.158 -36.271 59.707 1.00 50.11 ? 931 GOL A C2 1 HETATM 6626 O O2 . GOL FA 10 . ? -3.792 -36.373 60.124 1.00 52.20 ? 931 GOL A O2 1 HETATM 6627 C C3 . GOL FA 10 . ? -5.823 -37.642 59.778 1.00 55.00 ? 931 GOL A C3 1 HETATM 6628 O O3 . GOL FA 10 . ? -5.357 -38.429 60.887 1.00 58.17 ? 931 GOL A O3 1 HETATM 6629 C C1 . GOL GA 10 . ? 19.713 -25.097 28.241 1.00 50.41 ? 932 GOL A C1 1 HETATM 6630 O O1 . GOL GA 10 . ? 18.617 -24.560 29.005 1.00 46.70 ? 932 GOL A O1 1 HETATM 6631 C C2 . GOL GA 10 . ? 21.062 -24.532 28.691 1.00 49.15 ? 932 GOL A C2 1 HETATM 6632 O O2 . GOL GA 10 . ? 22.018 -24.654 27.634 1.00 60.49 ? 932 GOL A O2 1 HETATM 6633 C C3 . GOL GA 10 . ? 20.926 -23.064 29.061 1.00 44.04 ? 932 GOL A C3 1 HETATM 6634 O O3 . GOL GA 10 . ? 22.159 -22.437 29.424 1.00 48.36 ? 932 GOL A O3 1 HETATM 6635 C C1 . GOL HA 10 . ? 23.722 11.515 8.798 1.00 49.49 ? 933 GOL A C1 1 HETATM 6636 O O1 . GOL HA 10 . ? 24.198 11.982 7.530 1.00 48.34 ? 933 GOL A O1 1 HETATM 6637 C C2 . GOL HA 10 . ? 22.311 12.041 8.986 1.00 44.53 ? 933 GOL A C2 1 HETATM 6638 O O2 . GOL HA 10 . ? 22.095 12.275 10.371 1.00 38.31 ? 933 GOL A O2 1 HETATM 6639 C C3 . GOL HA 10 . ? 21.319 11.046 8.389 1.00 46.65 ? 933 GOL A C3 1 HETATM 6640 O O3 . GOL HA 10 . ? 20.026 11.629 8.309 1.00 41.96 ? 933 GOL A O3 1 HETATM 6641 C C1 . GOL IA 10 . ? -4.955 -3.329 28.872 1.00 50.65 ? 934 GOL A C1 1 HETATM 6642 O O1 . GOL IA 10 . ? -5.470 -4.635 28.599 1.00 50.90 ? 934 GOL A O1 1 HETATM 6643 C C2 . GOL IA 10 . ? -5.607 -2.722 30.109 1.00 47.41 ? 934 GOL A C2 1 HETATM 6644 O O2 . GOL IA 10 . ? -4.860 -3.070 31.274 1.00 53.18 ? 934 GOL A O2 1 HETATM 6645 C C3 . GOL IA 10 . ? -5.638 -1.207 30.014 1.00 49.89 ? 934 GOL A C3 1 HETATM 6646 O O3 . GOL IA 10 . ? -4.312 -0.701 29.824 1.00 51.65 ? 934 GOL A O3 1 HETATM 6647 C C1 . GOL JA 10 . ? -23.632 -14.769 34.335 1.00 35.58 ? 935 GOL A C1 1 HETATM 6648 O O1 . GOL JA 10 . ? -24.393 -15.267 33.227 1.00 42.96 ? 935 GOL A O1 1 HETATM 6649 C C2 . GOL JA 10 . ? -22.176 -15.274 34.330 1.00 36.35 ? 935 GOL A C2 1 HETATM 6650 O O2 . GOL JA 10 . ? -22.088 -16.650 34.728 1.00 38.05 ? 935 GOL A O2 1 HETATM 6651 C C3 . GOL JA 10 . ? -21.518 -15.148 32.958 1.00 36.01 ? 935 GOL A C3 1 HETATM 6652 O O3 . GOL JA 10 . ? -21.326 -13.779 32.596 1.00 32.72 ? 935 GOL A O3 1 HETATM 6653 C C1 . GOL KA 10 . ? 16.612 5.190 51.770 1.00 35.43 ? 936 GOL A C1 1 HETATM 6654 O O1 . GOL KA 10 . ? 17.462 4.352 52.573 1.00 30.22 ? 936 GOL A O1 1 HETATM 6655 C C2 . GOL KA 10 . ? 15.645 4.350 50.931 1.00 29.56 ? 936 GOL A C2 1 HETATM 6656 O O2 . GOL KA 10 . ? 14.414 4.341 51.576 1.00 22.42 ? 936 GOL A O2 1 HETATM 6657 C C3 . GOL KA 10 . ? 15.320 4.915 49.552 1.00 36.92 ? 936 GOL A C3 1 HETATM 6658 O O3 . GOL KA 10 . ? 16.162 4.380 48.524 1.00 45.38 ? 936 GOL A O3 1 HETATM 6659 S S . SCN LA 8 . ? 1.233 -2.857 46.620 1.00 47.07 ? 937 SCN A S 1 HETATM 6660 C C . SCN LA 8 . ? 2.704 -3.530 46.136 1.00 41.67 ? 937 SCN A C 1 HETATM 6661 N N . SCN LA 8 . ? 3.720 -3.966 45.807 1.00 43.35 ? 937 SCN A N 1 HETATM 6662 O O . HOH MA 11 . ? 15.499 -22.112 28.442 1.00 26.46 ? 1001 HOH A O 1 HETATM 6663 O O . HOH MA 11 . ? 27.566 -14.389 27.097 1.00 24.45 ? 1002 HOH A O 1 HETATM 6664 O O . HOH MA 11 . ? 14.716 2.887 42.295 1.00 31.32 ? 1003 HOH A O 1 HETATM 6665 O O . HOH MA 11 . ? -10.748 -30.621 50.367 1.00 20.54 ? 1004 HOH A O 1 HETATM 6666 O O . HOH MA 11 . ? 32.198 1.246 23.174 1.00 33.86 ? 1005 HOH A O 1 HETATM 6667 O O . HOH MA 11 . ? 14.960 -17.008 15.238 1.00 31.06 ? 1006 HOH A O 1 HETATM 6668 O O . HOH MA 11 . ? 15.199 4.126 46.178 1.00 41.35 ? 1007 HOH A O 1 HETATM 6669 O O . HOH MA 11 . ? 3.316 -26.027 25.053 1.00 23.62 ? 1008 HOH A O 1 HETATM 6670 O O . HOH MA 11 . ? -4.462 -17.575 61.842 1.00 24.70 ? 1009 HOH A O 1 HETATM 6671 O O . HOH MA 11 . ? -0.720 -16.307 17.131 1.00 37.61 ? 1010 HOH A O 1 HETATM 6672 O O . HOH MA 11 . ? 5.543 -18.380 63.224 1.00 33.71 ? 1011 HOH A O 1 HETATM 6673 O O . HOH MA 11 . ? 8.025 4.918 7.665 1.00 25.35 ? 1012 HOH A O 1 HETATM 6674 O O . HOH MA 11 . ? -17.381 -42.461 39.017 1.00 34.04 ? 1013 HOH A O 1 HETATM 6675 O O . HOH MA 11 . ? 23.418 0.782 42.768 1.00 34.32 ? 1014 HOH A O 1 HETATM 6676 O O . HOH MA 11 . ? -22.771 -30.810 45.548 1.00 29.39 ? 1015 HOH A O 1 HETATM 6677 O O . HOH MA 11 . ? -23.973 -37.849 39.535 1.00 38.81 ? 1016 HOH A O 1 HETATM 6678 O O . HOH MA 11 . ? 6.544 -24.945 22.643 1.00 31.56 ? 1017 HOH A O 1 HETATM 6679 O O . HOH MA 11 . ? 29.393 -16.399 38.466 1.00 29.65 ? 1018 HOH A O 1 HETATM 6680 O O . HOH MA 11 . ? 12.207 7.489 51.727 1.00 30.46 ? 1019 HOH A O 1 HETATM 6681 O O . HOH MA 11 . ? 4.667 -33.845 37.788 1.00 35.24 ? 1020 HOH A O 1 HETATM 6682 O O . HOH MA 11 . ? 13.553 17.198 34.870 1.00 34.25 ? 1021 HOH A O 1 HETATM 6683 O O . HOH MA 11 . ? 13.891 13.165 3.867 1.00 38.89 ? 1022 HOH A O 1 HETATM 6684 O O . HOH MA 11 . ? -7.833 -36.520 41.957 1.00 22.54 ? 1023 HOH A O 1 HETATM 6685 O O . HOH MA 11 . ? 32.825 13.284 1.546 1.00 39.49 ? 1024 HOH A O 1 HETATM 6686 O O . HOH MA 11 . ? 15.089 16.447 22.798 1.00 36.16 ? 1025 HOH A O 1 HETATM 6687 O O . HOH MA 11 . ? 14.474 1.418 45.970 1.00 30.48 ? 1026 HOH A O 1 HETATM 6688 O O . HOH MA 11 . ? 4.335 -4.244 8.232 1.00 26.76 ? 1027 HOH A O 1 HETATM 6689 O O . HOH MA 11 . ? 34.175 -3.977 30.657 1.00 40.74 ? 1028 HOH A O 1 HETATM 6690 O O . HOH MA 11 . ? 14.021 4.226 65.038 1.00 38.06 ? 1029 HOH A O 1 HETATM 6691 O O . HOH MA 11 . ? -15.922 -16.985 30.871 1.00 19.63 ? 1030 HOH A O 1 HETATM 6692 O O . HOH MA 11 . ? -10.830 -45.308 35.780 1.00 27.99 ? 1031 HOH A O 1 HETATM 6693 O O . HOH MA 11 . ? -9.890 -15.340 39.404 1.00 38.26 ? 1032 HOH A O 1 HETATM 6694 O O . HOH MA 11 . ? 14.684 -13.192 38.912 1.00 15.62 ? 1033 HOH A O 1 HETATM 6695 O O . HOH MA 11 . ? 7.730 -17.470 28.951 1.00 15.27 ? 1034 HOH A O 1 HETATM 6696 O O . HOH MA 11 . ? 19.224 -13.007 54.493 1.00 30.83 ? 1035 HOH A O 1 HETATM 6697 O O . HOH MA 11 . ? -14.344 -23.114 54.113 1.00 28.50 ? 1036 HOH A O 1 HETATM 6698 O O . HOH MA 11 . ? 6.509 -16.470 59.829 1.00 30.84 ? 1037 HOH A O 1 HETATM 6699 O O . HOH MA 11 . ? 13.743 -21.099 20.131 1.00 29.27 ? 1038 HOH A O 1 HETATM 6700 O O . HOH MA 11 . ? 15.632 28.161 8.789 1.00 42.68 ? 1039 HOH A O 1 HETATM 6701 O O . HOH MA 11 . ? 22.104 -17.482 12.586 1.00 29.59 ? 1040 HOH A O 1 HETATM 6702 O O . HOH MA 11 . ? 34.910 -16.542 48.041 1.00 34.43 ? 1041 HOH A O 1 HETATM 6703 O O . HOH MA 11 . ? -5.221 -16.027 39.133 1.00 25.61 ? 1042 HOH A O 1 HETATM 6704 O O . HOH MA 11 . ? 5.321 -38.837 38.824 1.00 34.99 ? 1043 HOH A O 1 HETATM 6705 O O . HOH MA 11 . ? 2.606 12.565 40.708 1.00 32.88 ? 1044 HOH A O 1 HETATM 6706 O O . HOH MA 11 . ? -25.941 -53.958 36.699 1.00 42.96 ? 1045 HOH A O 1 HETATM 6707 O O . HOH MA 11 . ? -2.752 -8.768 44.616 1.00 30.78 ? 1046 HOH A O 1 HETATM 6708 O O . HOH MA 11 . ? 1.877 -12.241 30.119 1.00 23.52 ? 1047 HOH A O 1 HETATM 6709 O O . HOH MA 11 . ? -0.959 -0.134 16.750 1.00 24.42 ? 1048 HOH A O 1 HETATM 6710 O O . HOH MA 11 . ? 19.223 -20.350 35.848 1.00 33.56 ? 1049 HOH A O 1 HETATM 6711 O O . HOH MA 11 . ? -13.603 -23.486 27.887 1.00 26.01 ? 1050 HOH A O 1 HETATM 6712 O O . HOH MA 11 . ? 6.930 -28.126 54.385 1.00 41.08 ? 1051 HOH A O 1 HETATM 6713 O O . HOH MA 11 . ? -7.578 -39.293 41.691 1.00 23.16 ? 1052 HOH A O 1 HETATM 6714 O O . HOH MA 11 . ? 25.289 -5.690 9.073 1.00 28.15 ? 1053 HOH A O 1 HETATM 6715 O O . HOH MA 11 . ? 15.229 -19.098 36.386 1.00 18.98 ? 1054 HOH A O 1 HETATM 6716 O O . HOH MA 11 . ? -1.457 -37.011 31.722 1.00 24.64 ? 1055 HOH A O 1 HETATM 6717 O O . HOH MA 11 . ? 6.355 -14.140 58.414 1.00 24.91 ? 1056 HOH A O 1 HETATM 6718 O O . HOH MA 11 . ? -0.005 1.375 49.152 1.00 25.55 ? 1057 HOH A O 1 HETATM 6719 O O . HOH MA 11 . ? 7.901 16.176 18.597 1.00 26.23 ? 1058 HOH A O 1 HETATM 6720 O O . HOH MA 11 . ? 1.243 -6.589 34.787 1.00 21.18 ? 1059 HOH A O 1 HETATM 6721 O O . HOH MA 11 . ? 17.491 18.117 13.482 1.00 30.18 ? 1060 HOH A O 1 HETATM 6722 O O . HOH MA 11 . ? -13.540 -13.993 49.267 1.00 31.52 ? 1061 HOH A O 1 HETATM 6723 O O . HOH MA 11 . ? 8.209 -25.912 31.043 1.00 33.54 ? 1062 HOH A O 1 HETATM 6724 O O . HOH MA 11 . ? 12.192 -12.430 66.741 1.00 32.87 ? 1063 HOH A O 1 HETATM 6725 O O . HOH MA 11 . ? -0.249 -20.527 52.203 1.00 22.90 ? 1064 HOH A O 1 HETATM 6726 O O . HOH MA 11 . ? 5.385 -27.481 28.477 1.00 25.50 ? 1065 HOH A O 1 HETATM 6727 O O . HOH MA 11 . ? -9.337 -13.540 30.501 1.00 33.22 ? 1066 HOH A O 1 HETATM 6728 O O . HOH MA 11 . ? 7.389 -0.401 67.091 1.00 32.86 ? 1067 HOH A O 1 HETATM 6729 O O . HOH MA 11 . ? 12.733 -14.215 24.766 1.00 13.93 ? 1068 HOH A O 1 HETATM 6730 O O . HOH MA 11 . ? 11.012 -23.981 48.013 1.00 24.44 ? 1069 HOH A O 1 HETATM 6731 O O . HOH MA 11 . ? 10.203 -31.697 33.929 1.00 41.04 ? 1070 HOH A O 1 HETATM 6732 O O . HOH MA 11 . ? 25.870 -9.093 61.901 1.00 40.72 ? 1071 HOH A O 1 HETATM 6733 O O . HOH MA 11 . ? -20.141 -22.499 49.347 1.00 36.92 ? 1072 HOH A O 1 HETATM 6734 O O . HOH MA 11 . ? 10.566 -16.582 61.528 1.00 37.70 ? 1073 HOH A O 1 HETATM 6735 O O . HOH MA 11 . ? -21.521 -15.382 20.953 1.00 36.98 ? 1074 HOH A O 1 HETATM 6736 O O . HOH MA 11 . ? 30.463 15.590 30.755 1.00 41.13 ? 1075 HOH A O 1 HETATM 6737 O O . HOH MA 11 . ? 9.327 -35.515 39.212 1.00 43.28 ? 1076 HOH A O 1 HETATM 6738 O O . HOH MA 11 . ? 0.768 -10.089 23.166 1.00 20.78 ? 1077 HOH A O 1 HETATM 6739 O O . HOH MA 11 . ? 7.235 -14.953 33.973 1.00 17.45 ? 1078 HOH A O 1 HETATM 6740 O O . HOH MA 11 . ? 4.925 7.639 7.019 1.00 35.80 ? 1079 HOH A O 1 HETATM 6741 O O . HOH MA 11 . ? 8.897 8.491 34.919 1.00 20.72 ? 1080 HOH A O 1 HETATM 6742 O O . HOH MA 11 . ? 10.029 -20.853 28.820 1.00 27.62 ? 1081 HOH A O 1 HETATM 6743 O O . HOH MA 11 . ? -15.738 -51.096 36.075 1.00 46.32 ? 1082 HOH A O 1 HETATM 6744 O O . HOH MA 11 . ? 15.203 -24.931 32.563 1.00 24.24 ? 1083 HOH A O 1 HETATM 6745 O O . HOH MA 11 . ? 28.148 15.104 13.515 1.00 41.10 ? 1084 HOH A O 1 HETATM 6746 O O . HOH MA 11 . ? 17.193 -8.466 9.983 1.00 22.60 ? 1085 HOH A O 1 HETATM 6747 O O . HOH MA 11 . ? 6.934 18.373 7.258 1.00 34.74 ? 1086 HOH A O 1 HETATM 6748 O O . HOH MA 11 . ? 32.077 -3.587 14.168 1.00 45.29 ? 1087 HOH A O 1 HETATM 6749 O O . HOH MA 11 . ? -7.593 -26.779 59.192 1.00 28.42 ? 1088 HOH A O 1 HETATM 6750 O O . HOH MA 11 . ? -8.409 -25.584 33.313 1.00 18.11 ? 1089 HOH A O 1 HETATM 6751 O O . HOH MA 11 . ? 9.222 -4.691 46.856 1.00 15.10 ? 1090 HOH A O 1 HETATM 6752 O O . HOH MA 11 . ? 9.735 -22.027 46.459 1.00 21.45 ? 1091 HOH A O 1 HETATM 6753 O O . HOH MA 11 . ? 2.624 -10.948 64.289 1.00 30.63 ? 1092 HOH A O 1 HETATM 6754 O O . HOH MA 11 . ? -9.482 -40.860 42.850 1.00 22.80 ? 1093 HOH A O 1 HETATM 6755 O O . HOH MA 11 . ? 3.174 -45.342 56.709 1.00 41.66 ? 1094 HOH A O 1 HETATM 6756 O O . HOH MA 11 . ? -5.231 -12.163 62.216 1.00 27.42 ? 1095 HOH A O 1 HETATM 6757 O O . HOH MA 11 . ? 9.239 -6.091 66.137 1.00 24.00 ? 1096 HOH A O 1 HETATM 6758 O O . HOH MA 11 . ? 4.315 14.466 46.173 1.00 55.99 ? 1097 HOH A O 1 HETATM 6759 O O . HOH MA 11 . ? 17.234 -42.344 31.910 1.00 44.14 ? 1098 HOH A O 1 HETATM 6760 O O . HOH MA 11 . ? 0.407 5.748 40.312 1.00 34.92 ? 1099 HOH A O 1 HETATM 6761 O O . HOH MA 11 . ? -2.057 -18.115 15.087 1.00 35.96 ? 1100 HOH A O 1 HETATM 6762 O O . HOH MA 11 . ? 30.174 -12.669 31.248 1.00 24.39 ? 1101 HOH A O 1 HETATM 6763 O O . HOH MA 11 . ? -25.214 -21.102 31.185 1.00 38.34 ? 1102 HOH A O 1 HETATM 6764 O O . HOH MA 11 . ? -1.648 -18.391 31.726 1.00 12.24 ? 1103 HOH A O 1 HETATM 6765 O O . HOH MA 11 . ? 0.790 -28.287 61.423 1.00 30.37 ? 1104 HOH A O 1 HETATM 6766 O O . HOH MA 11 . ? 16.763 -25.983 30.379 1.00 39.36 ? 1105 HOH A O 1 HETATM 6767 O O . HOH MA 11 . ? -12.894 -15.283 32.726 1.00 40.72 ? 1106 HOH A O 1 HETATM 6768 O O . HOH MA 11 . ? -9.252 -29.954 31.623 1.00 22.33 ? 1107 HOH A O 1 HETATM 6769 O O . HOH MA 11 . ? 12.493 -11.684 38.547 1.00 17.14 ? 1108 HOH A O 1 HETATM 6770 O O . HOH MA 11 . ? -3.088 -43.019 47.171 1.00 28.67 ? 1109 HOH A O 1 HETATM 6771 O O . HOH MA 11 . ? 4.456 12.102 44.534 1.00 32.88 ? 1110 HOH A O 1 HETATM 6772 O O . HOH MA 11 . ? 27.846 22.267 0.424 1.00 43.11 ? 1111 HOH A O 1 HETATM 6773 O O . HOH MA 11 . ? -5.909 -47.638 46.301 1.00 37.53 ? 1112 HOH A O 1 HETATM 6774 O O . HOH MA 11 . ? 14.697 16.273 12.511 1.00 24.97 ? 1113 HOH A O 1 HETATM 6775 O O . HOH MA 11 . ? 30.746 -6.038 23.872 1.00 40.57 ? 1114 HOH A O 1 HETATM 6776 O O . HOH MA 11 . ? 14.167 -37.477 48.620 1.00 48.07 ? 1115 HOH A O 1 HETATM 6777 O O . HOH MA 11 . ? 11.967 -19.563 39.096 1.00 17.52 ? 1116 HOH A O 1 HETATM 6778 O O . HOH MA 11 . ? -19.420 -32.275 39.911 1.00 24.87 ? 1117 HOH A O 1 HETATM 6779 O O . HOH MA 11 . ? 10.807 -19.410 43.386 1.00 18.84 ? 1118 HOH A O 1 HETATM 6780 O O . HOH MA 11 . ? 5.361 -12.735 56.251 1.00 20.21 ? 1119 HOH A O 1 HETATM 6781 O O . HOH MA 11 . ? 17.542 -22.989 36.399 1.00 24.69 ? 1120 HOH A O 1 HETATM 6782 O O . HOH MA 11 . ? 38.321 3.675 20.811 1.00 39.64 ? 1121 HOH A O 1 HETATM 6783 O O . HOH MA 11 . ? 29.342 22.571 8.780 1.00 35.62 ? 1122 HOH A O 1 HETATM 6784 O O . HOH MA 11 . ? 3.793 2.145 8.229 1.00 36.41 ? 1123 HOH A O 1 HETATM 6785 O O . HOH MA 11 . ? -11.699 -22.701 55.417 1.00 22.86 ? 1124 HOH A O 1 HETATM 6786 O O . HOH MA 11 . ? 36.762 -10.484 44.336 1.00 29.59 ? 1125 HOH A O 1 HETATM 6787 O O . HOH MA 11 . ? 13.278 14.280 28.527 1.00 36.16 ? 1126 HOH A O 1 HETATM 6788 O O . HOH MA 11 . ? -14.386 -17.048 23.201 1.00 20.81 ? 1127 HOH A O 1 HETATM 6789 O O . HOH MA 11 . ? 20.408 -15.017 26.758 1.00 12.57 ? 1128 HOH A O 1 HETATM 6790 O O . HOH MA 11 . ? -8.526 -46.287 34.491 1.00 30.95 ? 1129 HOH A O 1 HETATM 6791 O O . HOH MA 11 . ? -3.634 -9.652 47.036 1.00 22.30 ? 1130 HOH A O 1 HETATM 6792 O O . HOH MA 11 . ? 6.208 -12.930 64.718 1.00 27.82 ? 1131 HOH A O 1 HETATM 6793 O O . HOH MA 11 . ? -4.352 -27.018 21.407 1.00 25.25 ? 1132 HOH A O 1 HETATM 6794 O O . HOH MA 11 . ? 32.553 -1.886 11.723 1.00 30.64 ? 1133 HOH A O 1 HETATM 6795 O O . HOH MA 11 . ? 3.878 -5.529 50.228 1.00 27.46 ? 1134 HOH A O 1 HETATM 6796 O O . HOH MA 11 . ? 16.856 2.984 40.732 1.00 32.74 ? 1135 HOH A O 1 HETATM 6797 O O . HOH MA 11 . ? 8.313 -32.833 41.240 1.00 21.27 ? 1136 HOH A O 1 HETATM 6798 O O . HOH MA 11 . ? 5.550 17.985 21.497 1.00 32.46 ? 1137 HOH A O 1 HETATM 6799 O O . HOH MA 11 . ? 25.384 22.329 13.997 1.00 31.93 ? 1138 HOH A O 1 HETATM 6800 O O . HOH MA 11 . ? 4.872 -12.756 36.015 1.00 19.95 ? 1139 HOH A O 1 HETATM 6801 O O . HOH MA 11 . ? -4.532 -12.357 53.067 1.00 28.46 ? 1140 HOH A O 1 HETATM 6802 O O . HOH MA 11 . ? 9.181 -15.025 23.122 1.00 15.13 ? 1141 HOH A O 1 HETATM 6803 O O . HOH MA 11 . ? 13.723 -30.410 36.802 1.00 31.87 ? 1142 HOH A O 1 HETATM 6804 O O . HOH MA 11 . ? 10.093 -28.519 33.922 1.00 28.89 ? 1143 HOH A O 1 HETATM 6805 O O . HOH MA 11 . ? 10.395 -8.170 7.006 1.00 23.96 ? 1144 HOH A O 1 HETATM 6806 O O . HOH MA 11 . ? 2.482 -9.735 50.133 1.00 28.16 ? 1145 HOH A O 1 HETATM 6807 O O . HOH MA 11 . ? 3.857 12.988 50.854 1.00 47.83 ? 1146 HOH A O 1 HETATM 6808 O O . HOH MA 11 . ? -4.989 -28.944 29.408 1.00 28.38 ? 1147 HOH A O 1 HETATM 6809 O O . HOH MA 11 . ? 18.779 -23.556 44.269 1.00 38.37 ? 1148 HOH A O 1 HETATM 6810 O O . HOH MA 11 . ? 8.243 -22.844 21.784 1.00 31.20 ? 1149 HOH A O 1 HETATM 6811 O O . HOH MA 11 . ? 7.528 5.248 59.663 1.00 42.62 ? 1150 HOH A O 1 HETATM 6812 O O . HOH MA 11 . ? -7.712 -30.155 29.410 1.00 23.28 ? 1151 HOH A O 1 HETATM 6813 O O . HOH MA 11 . ? 23.119 21.528 0.668 1.00 39.73 ? 1152 HOH A O 1 HETATM 6814 O O . HOH MA 11 . ? 6.435 -30.694 40.903 1.00 17.69 ? 1153 HOH A O 1 HETATM 6815 O O . HOH MA 11 . ? -19.473 -19.061 46.559 1.00 23.93 ? 1154 HOH A O 1 HETATM 6816 O O . HOH MA 11 . ? 23.519 6.304 29.343 1.00 31.91 ? 1155 HOH A O 1 HETATM 6817 O O . HOH MA 11 . ? 3.067 -44.339 33.023 1.00 34.96 ? 1156 HOH A O 1 HETATM 6818 O O . HOH MA 11 . ? 0.155 0.579 51.973 1.00 31.42 ? 1157 HOH A O 1 HETATM 6819 O O . HOH MA 11 . ? -7.473 -20.159 15.517 1.00 48.21 ? 1158 HOH A O 1 HETATM 6820 O O . HOH MA 11 . ? 20.367 -19.371 47.172 1.00 32.55 ? 1159 HOH A O 1 HETATM 6821 O O . HOH MA 11 . ? -12.006 -37.692 54.909 1.00 29.84 ? 1160 HOH A O 1 HETATM 6822 O O . HOH MA 11 . ? 39.102 -11.217 32.525 1.00 41.18 ? 1161 HOH A O 1 HETATM 6823 O O . HOH MA 11 . ? 22.751 -2.384 8.125 1.00 22.23 ? 1162 HOH A O 1 HETATM 6824 O O . HOH MA 11 . ? 0.949 11.592 15.435 1.00 33.90 ? 1163 HOH A O 1 HETATM 6825 O O . HOH MA 11 . ? -0.782 -4.941 36.054 1.00 29.16 ? 1164 HOH A O 1 HETATM 6826 O O . HOH MA 11 . ? -3.272 -16.017 36.287 1.00 17.79 ? 1165 HOH A O 1 HETATM 6827 O O . HOH MA 11 . ? 13.105 2.802 3.367 1.00 23.37 ? 1166 HOH A O 1 HETATM 6828 O O . HOH MA 11 . ? -15.598 -26.010 25.412 1.00 31.07 ? 1167 HOH A O 1 HETATM 6829 O O . HOH MA 11 . ? 20.834 -16.364 49.639 1.00 33.60 ? 1168 HOH A O 1 HETATM 6830 O O . HOH MA 11 . ? -3.804 -39.596 46.239 1.00 30.62 ? 1169 HOH A O 1 HETATM 6831 O O . HOH MA 11 . ? 23.610 -16.373 49.260 1.00 28.92 ? 1170 HOH A O 1 HETATM 6832 O O . HOH MA 11 . ? -12.613 -23.071 22.403 1.00 30.42 ? 1171 HOH A O 1 HETATM 6833 O O . HOH MA 11 . ? 10.490 0.835 8.545 1.00 23.19 ? 1172 HOH A O 1 HETATM 6834 O O . HOH MA 11 . ? 13.136 -8.946 9.890 1.00 31.18 ? 1173 HOH A O 1 HETATM 6835 O O . HOH MA 11 . ? 18.131 13.636 32.725 1.00 40.67 ? 1174 HOH A O 1 HETATM 6836 O O . HOH MA 11 . ? -1.360 -17.265 54.608 1.00 16.23 ? 1175 HOH A O 1 HETATM 6837 O O . HOH MA 11 . ? 29.789 6.726 8.397 1.00 32.54 ? 1176 HOH A O 1 HETATM 6838 O O . HOH MA 11 . ? 3.242 -18.325 44.199 1.00 13.23 ? 1177 HOH A O 1 HETATM 6839 O O . HOH MA 11 . ? 21.377 -4.871 7.801 1.00 27.39 ? 1178 HOH A O 1 HETATM 6840 O O . HOH MA 11 . ? 29.313 -7.129 16.424 1.00 30.90 ? 1179 HOH A O 1 HETATM 6841 O O . HOH MA 11 . ? 5.591 -14.344 29.693 1.00 14.90 ? 1180 HOH A O 1 HETATM 6842 O O . HOH MA 11 . ? 3.707 -13.821 25.667 1.00 17.01 ? 1181 HOH A O 1 HETATM 6843 O O . HOH MA 11 . ? -9.383 -28.366 43.091 1.00 18.80 ? 1182 HOH A O 1 HETATM 6844 O O . HOH MA 11 . ? 4.470 -11.142 38.418 1.00 18.04 ? 1183 HOH A O 1 HETATM 6845 O O . HOH MA 11 . ? 16.617 -19.254 51.403 1.00 43.56 ? 1184 HOH A O 1 HETATM 6846 O O . HOH MA 11 . ? -2.125 -15.057 20.306 1.00 27.36 ? 1185 HOH A O 1 HETATM 6847 O O . HOH MA 11 . ? -1.961 -10.400 52.746 1.00 26.58 ? 1186 HOH A O 1 HETATM 6848 O O . HOH MA 11 . ? -0.643 -26.164 60.183 1.00 19.65 ? 1187 HOH A O 1 HETATM 6849 O O . HOH MA 11 . ? 9.038 13.485 12.255 1.00 21.75 ? 1188 HOH A O 1 HETATM 6850 O O . HOH MA 11 . ? 3.162 -1.746 7.872 1.00 25.03 ? 1189 HOH A O 1 HETATM 6851 O O . HOH MA 11 . ? 6.256 -28.601 30.851 1.00 24.03 ? 1190 HOH A O 1 HETATM 6852 O O . HOH MA 11 . ? -8.654 -14.347 33.208 1.00 31.99 ? 1191 HOH A O 1 HETATM 6853 O O . HOH MA 11 . ? 15.770 -40.136 34.693 1.00 36.00 ? 1192 HOH A O 1 HETATM 6854 O O . HOH MA 11 . ? 8.185 17.403 20.905 1.00 28.58 ? 1193 HOH A O 1 HETATM 6855 O O . HOH MA 11 . ? 22.229 25.530 13.093 1.00 35.17 ? 1194 HOH A O 1 HETATM 6856 O O . HOH MA 11 . ? 13.084 -19.333 41.886 1.00 18.62 ? 1195 HOH A O 1 HETATM 6857 O O . HOH MA 11 . ? -17.131 -24.062 45.338 1.00 21.08 ? 1196 HOH A O 1 HETATM 6858 O O . HOH MA 11 . ? 22.723 -8.660 46.883 1.00 20.62 ? 1197 HOH A O 1 HETATM 6859 O O . HOH MA 11 . ? -4.268 2.723 13.985 1.00 42.88 ? 1198 HOH A O 1 HETATM 6860 O O . HOH MA 11 . ? -14.537 -13.121 29.572 1.00 26.04 ? 1199 HOH A O 1 HETATM 6861 O O . HOH MA 11 . ? 29.848 -0.875 40.145 1.00 25.18 ? 1200 HOH A O 1 HETATM 6862 O O . HOH MA 11 . ? -20.749 -23.928 51.845 1.00 51.16 ? 1201 HOH A O 1 HETATM 6863 O O . HOH MA 11 . ? 2.543 -18.913 63.577 1.00 23.42 ? 1202 HOH A O 1 HETATM 6864 O O . HOH MA 11 . ? -3.132 -18.344 34.027 1.00 16.53 ? 1203 HOH A O 1 HETATM 6865 O O . HOH MA 11 . ? 12.099 -20.966 30.921 1.00 18.71 ? 1204 HOH A O 1 HETATM 6866 O O . HOH MA 11 . ? 23.829 1.366 19.195 1.00 19.70 ? 1205 HOH A O 1 HETATM 6867 O O . HOH MA 11 . ? 4.539 -17.682 51.055 1.00 19.03 ? 1206 HOH A O 1 HETATM 6868 O O . HOH MA 11 . ? 9.361 -33.989 24.853 1.00 33.05 ? 1207 HOH A O 1 HETATM 6869 O O . HOH MA 11 . ? 13.798 -10.395 26.454 1.00 14.22 ? 1208 HOH A O 1 HETATM 6870 O O . HOH MA 11 . ? 1.487 -15.717 19.024 1.00 24.89 ? 1209 HOH A O 1 HETATM 6871 O O . HOH MA 11 . ? 16.188 -21.341 38.010 1.00 18.82 ? 1210 HOH A O 1 HETATM 6872 O O . HOH MA 11 . ? 12.580 -24.242 32.015 1.00 36.01 ? 1211 HOH A O 1 HETATM 6873 O O . HOH MA 11 . ? 20.717 -19.389 50.796 1.00 35.91 ? 1212 HOH A O 1 HETATM 6874 O O . HOH MA 11 . ? 3.069 -11.392 56.998 1.00 19.32 ? 1213 HOH A O 1 HETATM 6875 O O . HOH MA 11 . ? 26.092 -6.208 1.208 1.00 34.27 ? 1214 HOH A O 1 HETATM 6876 O O . HOH MA 11 . ? 12.180 16.237 16.144 1.00 28.31 ? 1215 HOH A O 1 HETATM 6877 O O . HOH MA 11 . ? -3.793 0.611 23.401 1.00 40.87 ? 1216 HOH A O 1 HETATM 6878 O O . HOH MA 11 . ? -17.832 -16.641 20.184 1.00 39.89 ? 1217 HOH A O 1 HETATM 6879 O O . HOH MA 11 . ? -1.247 -9.661 55.211 1.00 21.45 ? 1218 HOH A O 1 HETATM 6880 O O . HOH MA 11 . ? 4.232 4.899 7.469 1.00 30.38 ? 1219 HOH A O 1 HETATM 6881 O O . HOH MA 11 . ? 12.566 -19.306 24.688 1.00 21.56 ? 1220 HOH A O 1 HETATM 6882 O O . HOH MA 11 . ? 21.036 -17.603 27.589 1.00 16.76 ? 1221 HOH A O 1 HETATM 6883 O O . HOH MA 11 . ? 2.852 0.272 25.374 1.00 24.46 ? 1222 HOH A O 1 HETATM 6884 O O . HOH MA 11 . ? -26.454 -21.509 41.115 1.00 36.77 ? 1223 HOH A O 1 HETATM 6885 O O . HOH MA 11 . ? 8.175 -21.907 37.243 1.00 17.08 ? 1224 HOH A O 1 HETATM 6886 O O . HOH MA 11 . ? 9.380 -18.751 31.713 1.00 16.31 ? 1225 HOH A O 1 HETATM 6887 O O . HOH MA 11 . ? 9.611 -19.168 40.972 1.00 23.12 ? 1226 HOH A O 1 HETATM 6888 O O . HOH MA 11 . ? 0.230 -5.963 60.025 1.00 31.38 ? 1227 HOH A O 1 HETATM 6889 O O . HOH MA 11 . ? 36.466 -7.474 44.102 1.00 41.69 ? 1228 HOH A O 1 HETATM 6890 O O . HOH MA 11 . ? -14.044 -12.425 60.592 1.00 42.46 ? 1229 HOH A O 1 HETATM 6891 O O . HOH MA 11 . ? 24.112 -11.083 48.926 1.00 24.35 ? 1230 HOH A O 1 HETATM 6892 O O . HOH MA 11 . ? 10.065 -17.755 45.562 1.00 13.78 ? 1231 HOH A O 1 HETATM 6893 O O . HOH MA 11 . ? 23.208 2.013 -0.424 1.00 34.55 ? 1232 HOH A O 1 HETATM 6894 O O . HOH MA 11 . ? -16.254 -18.574 21.700 1.00 26.87 ? 1233 HOH A O 1 HETATM 6895 O O . HOH MA 11 . ? 37.515 13.932 13.222 1.00 48.57 ? 1234 HOH A O 1 HETATM 6896 O O . HOH MA 11 . ? -2.136 -10.160 28.604 1.00 28.42 ? 1235 HOH A O 1 HETATM 6897 O O . HOH MA 11 . ? 16.707 5.339 39.072 1.00 32.75 ? 1236 HOH A O 1 HETATM 6898 O O . HOH MA 11 . ? -10.462 -31.473 23.306 1.00 37.07 ? 1237 HOH A O 1 HETATM 6899 O O . HOH MA 11 . ? 5.708 -21.045 56.811 1.00 35.25 ? 1238 HOH A O 1 HETATM 6900 O O . HOH MA 11 . ? 6.038 -46.236 44.331 1.00 40.83 ? 1239 HOH A O 1 HETATM 6901 O O . HOH MA 11 . ? -2.084 -12.898 52.404 1.00 25.25 ? 1240 HOH A O 1 HETATM 6902 O O . HOH MA 11 . ? 6.169 4.841 5.484 1.00 26.62 ? 1241 HOH A O 1 HETATM 6903 O O . HOH MA 11 . ? -11.230 -14.222 50.940 1.00 20.28 ? 1242 HOH A O 1 HETATM 6904 O O . HOH MA 11 . ? 1.282 2.148 26.924 1.00 31.27 ? 1243 HOH A O 1 HETATM 6905 O O . HOH MA 11 . ? -7.343 -15.869 24.913 1.00 28.66 ? 1244 HOH A O 1 HETATM 6906 O O . HOH MA 11 . ? 20.393 0.727 53.899 1.00 33.06 ? 1245 HOH A O 1 HETATM 6907 O O . HOH MA 11 . ? -6.101 -26.908 17.065 1.00 39.06 ? 1246 HOH A O 1 HETATM 6908 O O . HOH MA 11 . ? 5.587 -27.436 52.107 1.00 36.11 ? 1247 HOH A O 1 HETATM 6909 O O . HOH MA 11 . ? -17.231 -36.975 43.058 1.00 32.01 ? 1248 HOH A O 1 HETATM 6910 O O . HOH MA 11 . ? -1.464 -24.767 15.347 1.00 27.43 ? 1249 HOH A O 1 HETATM 6911 O O . HOH MA 11 . ? -17.213 -31.822 38.342 1.00 22.00 ? 1250 HOH A O 1 HETATM 6912 O O . HOH MA 11 . ? 2.045 -32.101 39.490 1.00 24.24 ? 1251 HOH A O 1 HETATM 6913 O O . HOH MA 11 . ? -0.445 -13.556 27.053 1.00 31.07 ? 1252 HOH A O 1 HETATM 6914 O O . HOH MA 11 . ? 16.153 -10.719 49.426 1.00 16.96 ? 1253 HOH A O 1 HETATM 6915 O O . HOH MA 11 . ? 19.203 -28.855 43.805 1.00 41.30 ? 1254 HOH A O 1 HETATM 6916 O O . HOH MA 11 . ? 15.412 15.896 6.967 1.00 35.58 ? 1255 HOH A O 1 HETATM 6917 O O . HOH MA 11 . ? -14.682 -32.120 25.283 1.00 44.59 ? 1256 HOH A O 1 HETATM 6918 O O . HOH MA 11 . ? 45.191 11.617 24.598 1.00 42.73 ? 1257 HOH A O 1 HETATM 6919 O O . HOH MA 11 . ? 31.631 3.700 19.641 1.00 28.86 ? 1258 HOH A O 1 HETATM 6920 O O . HOH MA 11 . ? 9.764 -40.543 55.763 1.00 43.55 ? 1259 HOH A O 1 HETATM 6921 O O . HOH MA 11 . ? 5.486 -15.385 35.998 1.00 18.05 ? 1260 HOH A O 1 HETATM 6922 O O . HOH MA 11 . ? -16.500 -45.946 27.975 1.00 35.47 ? 1261 HOH A O 1 HETATM 6923 O O . HOH MA 11 . ? 2.964 -16.764 41.928 1.00 15.47 ? 1262 HOH A O 1 HETATM 6924 O O . HOH MA 11 . ? 8.443 -14.912 18.205 1.00 26.42 ? 1263 HOH A O 1 HETATM 6925 O O . HOH MA 11 . ? 7.820 -15.492 20.736 1.00 16.18 ? 1264 HOH A O 1 HETATM 6926 O O . HOH MA 11 . ? -17.178 -38.679 40.745 1.00 25.17 ? 1265 HOH A O 1 HETATM 6927 O O . HOH MA 11 . ? 0.722 -18.205 53.118 1.00 16.57 ? 1266 HOH A O 1 HETATM 6928 O O . HOH MA 11 . ? 8.618 -9.612 32.607 1.00 16.88 ? 1267 HOH A O 1 HETATM 6929 O O . HOH MA 11 . ? 7.678 -12.151 36.468 1.00 20.52 ? 1268 HOH A O 1 HETATM 6930 O O . HOH MA 11 . ? -20.081 -30.722 35.746 1.00 43.30 ? 1269 HOH A O 1 HETATM 6931 O O . HOH MA 11 . ? 2.748 -5.769 67.717 1.00 35.26 ? 1270 HOH A O 1 HETATM 6932 O O . HOH MA 11 . ? -0.148 -12.638 50.411 1.00 23.50 ? 1271 HOH A O 1 HETATM 6933 O O . HOH MA 11 . ? -13.830 -25.135 20.254 1.00 36.46 ? 1272 HOH A O 1 HETATM 6934 O O . HOH MA 11 . ? 16.708 17.894 20.689 1.00 45.17 ? 1273 HOH A O 1 HETATM 6935 O O . HOH MA 11 . ? -1.582 -34.942 23.720 1.00 46.94 ? 1274 HOH A O 1 HETATM 6936 O O . HOH MA 11 . ? 20.403 16.542 14.020 1.00 28.77 ? 1275 HOH A O 1 HETATM 6937 O O . HOH MA 11 . ? 6.574 -4.701 46.023 1.00 16.06 ? 1276 HOH A O 1 HETATM 6938 O O . HOH MA 11 . ? -22.008 -29.744 41.928 1.00 39.90 ? 1277 HOH A O 1 HETATM 6939 O O . HOH MA 11 . ? 24.435 -17.560 19.721 1.00 23.70 ? 1278 HOH A O 1 HETATM 6940 O O . HOH MA 11 . ? -2.182 -9.934 16.016 1.00 36.79 ? 1279 HOH A O 1 HETATM 6941 O O . HOH MA 11 . ? 24.809 -17.759 32.555 1.00 35.68 ? 1280 HOH A O 1 HETATM 6942 O O . HOH MA 11 . ? -17.411 -19.823 29.751 1.00 22.72 ? 1281 HOH A O 1 HETATM 6943 O O . HOH MA 11 . ? 16.196 -29.842 47.027 1.00 25.07 ? 1282 HOH A O 1 HETATM 6944 O O . HOH MA 11 . ? 2.702 -7.151 56.132 1.00 17.35 ? 1283 HOH A O 1 HETATM 6945 O O . HOH MA 11 . ? 2.602 -6.651 45.975 1.00 34.27 ? 1284 HOH A O 1 HETATM 6946 O O . HOH MA 11 . ? 9.872 -15.930 43.346 1.00 15.66 ? 1285 HOH A O 1 HETATM 6947 O O . HOH MA 11 . ? 10.647 -12.909 11.549 1.00 38.00 ? 1286 HOH A O 1 HETATM 6948 O O . HOH MA 11 . ? 22.532 16.698 -0.378 1.00 38.31 ? 1287 HOH A O 1 HETATM 6949 O O . HOH MA 11 . ? 19.886 -23.892 39.583 1.00 31.61 ? 1288 HOH A O 1 HETATM 6950 O O . HOH MA 11 . ? 27.130 -8.977 54.191 1.00 45.35 ? 1289 HOH A O 1 HETATM 6951 O O A HOH MA 11 . ? 12.246 -3.754 28.914 0.50 18.95 ? 1290 HOH A O 1 HETATM 6952 O O B HOH MA 11 . ? 11.073 -3.718 30.691 0.50 14.30 ? 1290 HOH A O 1 HETATM 6953 O O . HOH MA 11 . ? 30.182 -0.732 0.976 1.00 47.54 ? 1291 HOH A O 1 HETATM 6954 O O . HOH MA 11 . ? 16.848 -0.137 66.613 1.00 51.96 ? 1292 HOH A O 1 HETATM 6955 O O . HOH MA 11 . ? 6.259 -23.328 50.235 1.00 26.54 ? 1293 HOH A O 1 HETATM 6956 O O . HOH MA 11 . ? 0.371 -27.424 24.359 1.00 27.02 ? 1294 HOH A O 1 HETATM 6957 O O . HOH MA 11 . ? 22.187 -19.421 19.841 1.00 23.24 ? 1295 HOH A O 1 HETATM 6958 O O . HOH MA 11 . ? 0.421 -9.107 65.581 1.00 28.55 ? 1296 HOH A O 1 HETATM 6959 O O . HOH MA 11 . ? 4.412 -24.123 26.716 1.00 28.44 ? 1297 HOH A O 1 HETATM 6960 O O . HOH MA 11 . ? 18.359 2.626 54.672 1.00 26.51 ? 1298 HOH A O 1 HETATM 6961 O O . HOH MA 11 . ? 6.665 -19.533 47.196 1.00 17.53 ? 1299 HOH A O 1 HETATM 6962 O O . HOH MA 11 . ? -19.212 -29.934 55.042 1.00 39.58 ? 1300 HOH A O 1 HETATM 6963 O O . HOH MA 11 . ? 1.405 10.344 52.268 1.00 39.54 ? 1301 HOH A O 1 HETATM 6964 O O . HOH MA 11 . ? 23.886 -18.020 41.984 1.00 25.12 ? 1302 HOH A O 1 HETATM 6965 O O . HOH MA 11 . ? 13.876 -6.677 67.687 1.00 41.01 ? 1303 HOH A O 1 HETATM 6966 O O . HOH MA 11 . ? 4.088 -12.584 28.128 1.00 15.03 ? 1304 HOH A O 1 HETATM 6967 O O . HOH MA 11 . ? -3.439 -9.003 18.271 1.00 46.70 ? 1305 HOH A O 1 HETATM 6968 O O . HOH MA 11 . ? 9.809 -10.996 37.597 1.00 19.33 ? 1306 HOH A O 1 HETATM 6969 O O . HOH MA 11 . ? 28.043 -4.569 20.370 1.00 40.86 ? 1307 HOH A O 1 HETATM 6970 O O . HOH MA 11 . ? 26.386 -8.097 9.803 1.00 30.94 ? 1308 HOH A O 1 HETATM 6971 O O . HOH MA 11 . ? 20.972 -19.026 38.830 1.00 25.86 ? 1309 HOH A O 1 HETATM 6972 O O . HOH MA 11 . ? 15.140 -6.170 11.952 1.00 16.04 ? 1310 HOH A O 1 HETATM 6973 O O . HOH MA 11 . ? 17.619 -2.686 -2.787 1.00 33.27 ? 1311 HOH A O 1 HETATM 6974 O O . HOH MA 11 . ? 29.769 5.387 37.527 1.00 42.78 ? 1312 HOH A O 1 HETATM 6975 O O . HOH MA 11 . ? 3.474 0.115 10.070 1.00 24.08 ? 1313 HOH A O 1 HETATM 6976 O O . HOH MA 11 . ? -1.317 1.743 3.726 1.00 34.24 ? 1314 HOH A O 1 HETATM 6977 O O . HOH MA 11 . ? -3.772 -30.952 27.405 1.00 26.68 ? 1315 HOH A O 1 HETATM 6978 O O . HOH MA 11 . ? 9.204 -15.798 14.161 1.00 38.17 ? 1316 HOH A O 1 HETATM 6979 O O . HOH MA 11 . ? -28.948 -39.134 42.915 1.00 49.74 ? 1317 HOH A O 1 HETATM 6980 O O . HOH MA 11 . ? 14.565 -29.049 40.563 1.00 21.46 ? 1318 HOH A O 1 HETATM 6981 O O . HOH MA 11 . ? 21.159 -13.232 10.062 1.00 39.81 ? 1319 HOH A O 1 HETATM 6982 O O . HOH MA 11 . ? 4.040 -8.930 57.863 1.00 18.12 ? 1320 HOH A O 1 HETATM 6983 O O . HOH MA 11 . ? 10.711 -21.349 23.976 1.00 22.20 ? 1321 HOH A O 1 HETATM 6984 O O . HOH MA 11 . ? 26.286 -19.442 21.788 1.00 36.65 ? 1322 HOH A O 1 HETATM 6985 O O . HOH MA 11 . ? 4.894 -1.905 11.460 1.00 20.74 ? 1323 HOH A O 1 HETATM 6986 O O . HOH MA 11 . ? -25.949 -16.812 25.722 1.00 23.33 ? 1324 HOH A O 1 HETATM 6987 O O . HOH MA 11 . ? -24.968 -19.379 28.364 1.00 34.87 ? 1325 HOH A O 1 HETATM 6988 O O . HOH MA 11 . ? -20.355 -34.342 36.760 1.00 32.52 ? 1326 HOH A O 1 HETATM 6989 O O . HOH MA 11 . ? 7.148 8.643 5.605 1.00 29.48 ? 1327 HOH A O 1 HETATM 6990 O O . HOH MA 11 . ? 30.856 -17.719 16.857 1.00 42.31 ? 1328 HOH A O 1 HETATM 6991 O O . HOH MA 11 . ? 8.344 -24.991 19.719 1.00 38.90 ? 1329 HOH A O 1 HETATM 6992 O O . HOH MA 11 . ? 21.231 3.441 32.944 1.00 35.72 ? 1330 HOH A O 1 HETATM 6993 O O . HOH MA 11 . ? -4.341 -11.075 55.555 1.00 18.71 ? 1331 HOH A O 1 HETATM 6994 O O . HOH MA 11 . ? 10.598 -35.931 56.019 1.00 34.23 ? 1332 HOH A O 1 HETATM 6995 O O . HOH MA 11 . ? 35.357 -7.163 32.175 1.00 33.46 ? 1333 HOH A O 1 HETATM 6996 O O . HOH MA 11 . ? 18.466 0.774 47.044 1.00 35.93 ? 1334 HOH A O 1 HETATM 6997 O O . HOH MA 11 . ? 2.181 -4.705 53.701 1.00 34.00 ? 1335 HOH A O 1 HETATM 6998 O O . HOH MA 11 . ? 28.694 -19.089 39.226 1.00 29.09 ? 1336 HOH A O 1 HETATM 6999 O O . HOH MA 11 . ? -18.949 -11.835 24.704 1.00 37.81 ? 1337 HOH A O 1 HETATM 7000 O O . HOH MA 11 . ? -11.595 -27.092 23.925 1.00 34.25 ? 1338 HOH A O 1 HETATM 7001 O O . HOH MA 11 . ? 17.247 -21.696 19.718 1.00 59.34 ? 1339 HOH A O 1 HETATM 7002 O O . HOH MA 11 . ? -6.998 -15.292 29.893 1.00 21.06 ? 1340 HOH A O 1 HETATM 7003 O O . HOH MA 11 . ? 5.284 17.645 40.925 1.00 39.42 ? 1341 HOH A O 1 HETATM 7004 O O . HOH MA 11 . ? 12.818 -37.652 32.394 1.00 37.57 ? 1342 HOH A O 1 HETATM 7005 O O . HOH MA 11 . ? 23.223 -4.955 5.647 1.00 27.23 ? 1343 HOH A O 1 HETATM 7006 O O . HOH MA 11 . ? 20.623 -20.471 44.416 1.00 43.05 ? 1344 HOH A O 1 HETATM 7007 O O . HOH MA 11 . ? 20.235 14.742 16.424 1.00 29.86 ? 1345 HOH A O 1 HETATM 7008 O O . HOH MA 11 . ? 8.346 2.587 60.523 1.00 34.07 ? 1346 HOH A O 1 HETATM 7009 O O . HOH MA 11 . ? 33.892 17.194 0.897 1.00 45.78 ? 1347 HOH A O 1 HETATM 7010 O O . HOH MA 11 . ? 3.278 -36.641 21.767 1.00 43.61 ? 1348 HOH A O 1 HETATM 7011 O O . HOH MA 11 . ? -9.472 -11.947 50.833 1.00 23.66 ? 1349 HOH A O 1 HETATM 7012 O O . HOH MA 11 . ? 31.376 -1.432 44.189 1.00 38.61 ? 1350 HOH A O 1 HETATM 7013 O O . HOH MA 11 . ? 4.956 -22.844 61.451 1.00 35.32 ? 1351 HOH A O 1 HETATM 7014 O O . HOH MA 11 . ? 8.755 -16.465 54.974 1.00 24.32 ? 1352 HOH A O 1 HETATM 7015 O O . HOH MA 11 . ? 3.240 14.532 3.906 1.00 47.84 ? 1353 HOH A O 1 HETATM 7016 O O . HOH MA 11 . ? 14.880 -20.781 24.804 1.00 20.10 ? 1354 HOH A O 1 HETATM 7017 O O . HOH MA 11 . ? 21.871 -13.256 7.124 1.00 47.17 ? 1355 HOH A O 1 HETATM 7018 O O . HOH MA 11 . ? 20.804 17.417 25.141 1.00 40.65 ? 1356 HOH A O 1 HETATM 7019 O O . HOH MA 11 . ? -2.364 -36.782 63.482 1.00 35.81 ? 1357 HOH A O 1 HETATM 7020 O O . HOH MA 11 . ? -3.826 -4.173 9.588 1.00 47.06 ? 1358 HOH A O 1 HETATM 7021 O O . HOH MA 11 . ? 32.301 8.159 25.869 1.00 26.29 ? 1359 HOH A O 1 HETATM 7022 O O . HOH MA 11 . ? -0.752 -11.170 30.998 1.00 26.65 ? 1360 HOH A O 1 HETATM 7023 O O . HOH MA 11 . ? 0.111 -13.416 60.436 1.00 20.02 ? 1361 HOH A O 1 HETATM 7024 O O . HOH MA 11 . ? -4.848 -9.325 34.180 1.00 28.53 ? 1362 HOH A O 1 HETATM 7025 O O . HOH MA 11 . ? 1.658 0.355 0.999 1.00 41.74 ? 1363 HOH A O 1 HETATM 7026 O O . HOH MA 11 . ? 4.751 -36.088 64.436 1.00 50.54 ? 1364 HOH A O 1 HETATM 7027 O O . HOH MA 11 . ? 28.573 7.133 31.897 1.00 32.96 ? 1365 HOH A O 1 HETATM 7028 O O . HOH MA 11 . ? 28.500 11.492 15.978 1.00 36.45 ? 1366 HOH A O 1 HETATM 7029 O O . HOH MA 11 . ? 33.627 0.751 11.576 1.00 44.07 ? 1367 HOH A O 1 HETATM 7030 O O . HOH MA 11 . ? 23.121 -15.339 10.895 1.00 42.66 ? 1368 HOH A O 1 HETATM 7031 O O . HOH MA 11 . ? 1.398 -13.413 12.771 1.00 33.47 ? 1369 HOH A O 1 HETATM 7032 O O . HOH MA 11 . ? 2.102 -18.113 55.647 1.00 15.61 ? 1370 HOH A O 1 HETATM 7033 O O . HOH MA 11 . ? 32.010 -2.708 2.358 1.00 43.57 ? 1371 HOH A O 1 HETATM 7034 O O . HOH MA 11 . ? -1.372 -19.793 61.288 1.00 24.67 ? 1372 HOH A O 1 HETATM 7035 O O . HOH MA 11 . ? 31.256 13.001 16.685 1.00 45.58 ? 1373 HOH A O 1 HETATM 7036 O O . HOH MA 11 . ? -12.667 -48.411 45.063 1.00 38.65 ? 1374 HOH A O 1 HETATM 7037 O O . HOH MA 11 . ? 33.231 -4.514 46.267 1.00 32.06 ? 1375 HOH A O 1 HETATM 7038 O O . HOH MA 11 . ? -5.057 -8.411 54.921 1.00 43.73 ? 1376 HOH A O 1 HETATM 7039 O O . HOH MA 11 . ? -1.664 2.841 35.884 1.00 42.79 ? 1377 HOH A O 1 HETATM 7040 O O . HOH MA 11 . ? -1.107 -21.938 54.665 1.00 21.51 ? 1378 HOH A O 1 HETATM 7041 O O . HOH MA 11 . ? -24.194 -40.888 52.080 1.00 34.26 ? 1379 HOH A O 1 HETATM 7042 O O . HOH MA 11 . ? -5.555 -4.672 16.265 1.00 29.28 ? 1380 HOH A O 1 HETATM 7043 O O . HOH MA 11 . ? -18.994 -30.735 31.624 1.00 45.97 ? 1381 HOH A O 1 HETATM 7044 O O . HOH MA 11 . ? 14.080 -21.382 55.694 1.00 47.16 ? 1382 HOH A O 1 HETATM 7045 O O . HOH MA 11 . ? 27.317 -16.791 30.097 1.00 31.41 ? 1383 HOH A O 1 HETATM 7046 O O . HOH MA 11 . ? 27.238 -20.565 43.575 1.00 43.48 ? 1384 HOH A O 1 HETATM 7047 O O . HOH MA 11 . ? -21.569 -28.918 37.207 1.00 40.44 ? 1385 HOH A O 1 HETATM 7048 O O . HOH MA 11 . ? 5.201 -14.413 54.055 1.00 30.70 ? 1386 HOH A O 1 HETATM 7049 O O . HOH MA 11 . ? -23.331 -50.497 34.728 1.00 40.12 ? 1387 HOH A O 1 HETATM 7050 O O . HOH MA 11 . ? 13.588 13.665 6.637 1.00 46.80 ? 1388 HOH A O 1 HETATM 7051 O O . HOH MA 11 . ? 24.547 15.939 1.727 1.00 36.75 ? 1389 HOH A O 1 HETATM 7052 O O . HOH MA 11 . ? 19.664 1.976 -3.538 1.00 23.31 ? 1390 HOH A O 1 HETATM 7053 O O . HOH MA 11 . ? -24.116 -34.274 45.881 1.00 31.53 ? 1391 HOH A O 1 HETATM 7054 O O . HOH MA 11 . ? 23.520 3.544 27.806 1.00 31.83 ? 1392 HOH A O 1 HETATM 7055 O O . HOH MA 11 . ? -10.706 -25.123 22.242 1.00 35.09 ? 1393 HOH A O 1 HETATM 7056 O O . HOH MA 11 . ? -22.061 -23.115 32.599 1.00 28.75 ? 1394 HOH A O 1 HETATM 7057 O O . HOH MA 11 . ? -2.807 -25.843 19.359 1.00 30.16 ? 1395 HOH A O 1 HETATM 7058 O O . HOH MA 11 . ? -4.241 -16.191 22.099 1.00 43.26 ? 1396 HOH A O 1 HETATM 7059 O O . HOH MA 11 . ? 5.625 6.644 3.463 1.00 38.03 ? 1397 HOH A O 1 HETATM 7060 O O . HOH MA 11 . ? -0.053 -5.498 64.263 1.00 51.02 ? 1398 HOH A O 1 HETATM 7061 O O . HOH MA 11 . ? 22.789 -17.527 37.360 1.00 34.95 ? 1399 HOH A O 1 HETATM 7062 O O . HOH MA 11 . ? -0.687 -16.603 61.310 1.00 24.63 ? 1400 HOH A O 1 HETATM 7063 O O . HOH MA 11 . ? -4.055 -20.839 60.507 1.00 22.76 ? 1401 HOH A O 1 HETATM 7064 O O . HOH MA 11 . ? 8.493 -12.074 33.833 1.00 21.11 ? 1402 HOH A O 1 HETATM 7065 O O . HOH MA 11 . ? 19.452 4.713 50.311 1.00 47.22 ? 1403 HOH A O 1 HETATM 7066 O O . HOH MA 11 . ? 3.447 1.681 59.970 1.00 36.10 ? 1404 HOH A O 1 HETATM 7067 O O . HOH MA 11 . ? -6.859 -8.231 36.202 1.00 38.44 ? 1405 HOH A O 1 HETATM 7068 O O . HOH MA 11 . ? 18.826 1.761 42.629 1.00 33.97 ? 1406 HOH A O 1 HETATM 7069 O O . HOH MA 11 . ? 33.018 3.089 13.093 1.00 42.33 ? 1407 HOH A O 1 HETATM 7070 O O . HOH MA 11 . ? 21.317 -14.295 52.763 1.00 29.99 ? 1408 HOH A O 1 HETATM 7071 O O . HOH MA 11 . ? -4.935 -28.973 19.519 1.00 29.39 ? 1409 HOH A O 1 HETATM 7072 O O . HOH MA 11 . ? 10.817 -26.308 32.037 1.00 36.02 ? 1410 HOH A O 1 HETATM 7073 O O . HOH MA 11 . ? -6.410 -40.633 58.843 1.00 51.00 ? 1411 HOH A O 1 HETATM 7074 O O . HOH MA 11 . ? 22.524 -1.060 55.535 1.00 35.03 ? 1412 HOH A O 1 HETATM 7075 O O . HOH MA 11 . ? -25.756 -29.672 51.781 1.00 47.98 ? 1413 HOH A O 1 HETATM 7076 O O . HOH MA 11 . ? -2.383 -33.097 61.966 1.00 39.62 ? 1414 HOH A O 1 HETATM 7077 O O . HOH MA 11 . ? 3.473 -10.607 68.463 1.00 42.45 ? 1415 HOH A O 1 HETATM 7078 O O . HOH MA 11 . ? -13.112 -51.771 35.059 1.00 46.80 ? 1416 HOH A O 1 HETATM 7079 O O . HOH MA 11 . ? 6.849 -24.503 25.491 1.00 38.88 ? 1417 HOH A O 1 HETATM 7080 O O . HOH MA 11 . ? 16.003 -20.679 22.117 1.00 38.66 ? 1418 HOH A O 1 HETATM 7081 O O . HOH MA 11 . ? 23.917 -13.145 55.994 1.00 43.41 ? 1419 HOH A O 1 HETATM 7082 O O . HOH MA 11 . ? -22.961 -38.811 50.070 1.00 41.49 ? 1420 HOH A O 1 HETATM 7083 O O . HOH MA 11 . ? 1.780 18.044 18.668 1.00 46.22 ? 1421 HOH A O 1 HETATM 7084 O O . HOH MA 11 . ? -24.742 -23.755 45.843 1.00 43.75 ? 1422 HOH A O 1 HETATM 7085 O O . HOH MA 11 . ? -2.854 -50.164 31.605 1.00 54.69 ? 1423 HOH A O 1 HETATM 7086 O O . HOH MA 11 . ? 5.189 -47.136 33.262 1.00 53.42 ? 1424 HOH A O 1 HETATM 7087 O O . HOH MA 11 . ? 25.838 -5.937 6.123 1.00 37.79 ? 1425 HOH A O 1 HETATM 7088 O O . HOH MA 11 . ? 30.123 4.632 34.753 1.00 43.72 ? 1426 HOH A O 1 HETATM 7089 O O . HOH MA 11 . ? 2.914 8.747 56.118 1.00 46.82 ? 1427 HOH A O 1 HETATM 7090 O O . HOH MA 11 . ? 19.323 5.351 39.328 1.00 27.07 ? 1428 HOH A O 1 HETATM 7091 O O . HOH MA 11 . ? 10.981 -23.150 13.130 1.00 38.38 ? 1429 HOH A O 1 HETATM 7092 O O . HOH MA 11 . ? 17.598 15.293 24.642 1.00 43.62 ? 1430 HOH A O 1 HETATM 7093 O O . HOH MA 11 . ? 1.027 2.590 33.880 1.00 32.77 ? 1431 HOH A O 1 HETATM 7094 O O . HOH MA 11 . ? 14.282 -17.557 58.706 1.00 41.29 ? 1432 HOH A O 1 HETATM 7095 O O . HOH MA 11 . ? 38.162 -11.896 50.015 1.00 40.48 ? 1433 HOH A O 1 HETATM 7096 O O . HOH MA 11 . ? -21.080 -26.891 51.666 1.00 40.06 ? 1434 HOH A O 1 HETATM 7097 O O . HOH MA 11 . ? 6.674 -24.252 52.954 1.00 45.15 ? 1435 HOH A O 1 HETATM 7098 O O . HOH MA 11 . ? 30.337 20.111 0.968 1.00 42.86 ? 1436 HOH A O 1 HETATM 7099 O O . HOH MA 11 . ? 0.290 9.266 34.305 1.00 38.74 ? 1437 HOH A O 1 HETATM 7100 O O . HOH MA 11 . ? -2.424 -13.748 62.072 1.00 24.41 ? 1438 HOH A O 1 HETATM 7101 O O . HOH MA 11 . ? -27.518 -51.011 51.699 1.00 32.92 ? 1439 HOH A O 1 HETATM 7102 O O . HOH MA 11 . ? 25.109 3.370 42.986 1.00 37.67 ? 1440 HOH A O 1 HETATM 7103 O O . HOH MA 11 . ? -28.225 -19.985 35.512 1.00 43.53 ? 1441 HOH A O 1 HETATM 7104 O O . HOH MA 11 . ? -15.465 -28.791 24.810 1.00 49.58 ? 1442 HOH A O 1 HETATM 7105 O O . HOH MA 11 . ? 0.552 -5.657 57.124 1.00 30.69 ? 1443 HOH A O 1 HETATM 7106 O O . HOH MA 11 . ? 10.051 7.102 62.818 1.00 42.20 ? 1444 HOH A O 1 HETATM 7107 O O . HOH MA 11 . ? -5.955 -26.283 31.586 1.00 32.01 ? 1445 HOH A O 1 HETATM 7108 O O . HOH MA 11 . ? 16.477 -28.403 49.325 1.00 39.21 ? 1446 HOH A O 1 HETATM 7109 O O . HOH MA 11 . ? 12.428 -11.780 9.807 1.00 42.12 ? 1447 HOH A O 1 HETATM 7110 O O . HOH MA 11 . ? 25.544 -15.594 40.383 1.00 20.04 ? 1448 HOH A O 1 HETATM 7111 O O . HOH MA 11 . ? -7.122 -29.818 59.957 1.00 35.34 ? 1449 HOH A O 1 HETATM 7112 O O . HOH MA 11 . ? 3.873 -44.787 52.245 1.00 34.21 ? 1450 HOH A O 1 HETATM 7113 O O . HOH MA 11 . ? 12.217 19.037 29.855 1.00 50.77 ? 1451 HOH A O 1 HETATM 7114 O O . HOH MA 11 . ? 38.154 -14.488 31.926 1.00 28.95 ? 1452 HOH A O 1 HETATM 7115 O O . HOH MA 11 . ? 20.834 23.149 -0.344 1.00 36.30 ? 1453 HOH A O 1 HETATM 7116 O O . HOH MA 11 . ? 8.068 -15.645 61.966 1.00 38.65 ? 1454 HOH A O 1 HETATM 7117 O O . HOH MA 11 . ? 8.287 -20.742 39.738 1.00 29.27 ? 1455 HOH A O 1 HETATM 7118 O O . HOH MA 11 . ? 4.528 -32.672 40.383 1.00 27.63 ? 1456 HOH A O 1 HETATM 7119 O O . HOH MA 11 . ? -9.776 -26.441 57.433 1.00 37.59 ? 1457 HOH A O 1 HETATM 7120 O O . HOH MA 11 . ? 9.556 -11.114 67.285 1.00 31.78 ? 1458 HOH A O 1 HETATM 7121 O O . HOH MA 11 . ? 7.655 -27.091 26.854 1.00 36.71 ? 1459 HOH A O 1 HETATM 7122 O O . HOH MA 11 . ? 0.577 -6.829 53.069 1.00 36.27 ? 1460 HOH A O 1 HETATM 7123 O O . HOH MA 11 . ? -4.644 -23.719 61.408 1.00 30.39 ? 1461 HOH A O 1 HETATM 7124 O O . HOH MA 11 . ? 14.060 16.805 29.573 1.00 43.52 ? 1462 HOH A O 1 HETATM 7125 O O . HOH MA 11 . ? -13.087 -24.822 24.841 1.00 31.28 ? 1463 HOH A O 1 HETATM 7126 O O . HOH MA 11 . ? 28.304 17.659 24.273 1.00 35.02 ? 1464 HOH A O 1 HETATM 7127 O O . HOH MA 11 . ? -3.912 0.041 16.476 1.00 44.42 ? 1465 HOH A O 1 HETATM 7128 O O . HOH MA 11 . ? 0.784 -15.794 14.596 1.00 37.37 ? 1466 HOH A O 1 HETATM 7129 O O . HOH MA 11 . ? -2.260 -24.967 62.212 1.00 33.78 ? 1467 HOH A O 1 HETATM 7130 O O . HOH MA 11 . ? 6.649 16.035 48.933 1.00 33.06 ? 1468 HOH A O 1 HETATM 7131 O O . HOH MA 11 . ? 1.469 -12.407 24.569 1.00 22.00 ? 1469 HOH A O 1 HETATM 7132 O O . HOH MA 11 . ? -15.006 -12.346 23.539 1.00 37.13 ? 1470 HOH A O 1 HETATM 7133 O O . HOH MA 11 . ? -14.059 -14.465 22.160 1.00 24.81 ? 1471 HOH A O 1 HETATM 7134 O O . HOH MA 11 . ? 31.934 5.678 12.371 1.00 40.21 ? 1472 HOH A O 1 HETATM 7135 O O . HOH MA 11 . ? -3.206 -14.927 17.549 1.00 46.19 ? 1473 HOH A O 1 HETATM 7136 O O . HOH MA 11 . ? -25.252 -34.564 48.330 1.00 48.00 ? 1474 HOH A O 1 HETATM 7137 O O . HOH MA 11 . ? -11.626 -24.374 57.508 1.00 36.33 ? 1475 HOH A O 1 HETATM 7138 O O . HOH MA 11 . ? 15.283 -15.087 8.781 1.00 41.40 ? 1476 HOH A O 1 HETATM 7139 O O . HOH MA 11 . ? 16.532 -11.056 8.805 1.00 31.47 ? 1477 HOH A O 1 HETATM 7140 O O . HOH MA 11 . ? 8.791 -29.159 31.481 1.00 37.39 ? 1478 HOH A O 1 HETATM 7141 O O . HOH MA 11 . ? -6.381 -14.534 27.261 1.00 36.17 ? 1479 HOH A O 1 HETATM 7142 O O . HOH MA 11 . ? -1.426 2.657 24.598 1.00 30.12 ? 1480 HOH A O 1 HETATM 7143 O O . HOH MA 11 . ? 30.077 -9.720 13.025 1.00 28.10 ? 1481 HOH A O 1 HETATM 7144 O O . HOH MA 11 . ? -14.344 -13.425 36.543 1.00 33.63 ? 1482 HOH A O 1 HETATM 7145 O O . HOH MA 11 . ? 23.592 -20.798 15.478 1.00 40.98 ? 1483 HOH A O 1 HETATM 7146 O O . HOH MA 11 . ? 13.812 -23.090 30.028 1.00 38.25 ? 1484 HOH A O 1 HETATM 7147 O O . HOH MA 11 . ? 11.766 6.752 -0.022 1.00 56.42 ? 1485 HOH A O 1 HETATM 7148 O O . HOH MA 11 . ? -9.117 -29.246 52.920 1.00 21.34 ? 1486 HOH A O 1 HETATM 7149 O O . HOH MA 11 . ? 10.745 -42.989 28.168 1.00 48.73 ? 1487 HOH A O 1 HETATM 7150 O O . HOH MA 11 . ? 9.705 17.295 16.921 1.00 29.43 ? 1488 HOH A O 1 HETATM 7151 O O . HOH MA 11 . ? -0.841 -28.744 63.732 1.00 44.39 ? 1489 HOH A O 1 HETATM 7152 O O . HOH MA 11 . ? -2.790 -51.086 34.368 1.00 39.00 ? 1490 HOH A O 1 HETATM 7153 O O . HOH MA 11 . ? -1.870 -6.877 61.923 1.00 44.15 ? 1491 HOH A O 1 HETATM 7154 O O . HOH MA 11 . ? -6.721 -15.601 20.473 1.00 40.90 ? 1492 HOH A O 1 HETATM 7155 O O . HOH MA 11 . ? 23.519 -18.777 27.585 1.00 37.07 ? 1493 HOH A O 1 HETATM 7156 O O . HOH MA 11 . ? -3.564 5.992 34.884 1.00 46.12 ? 1494 HOH A O 1 HETATM 7157 O O . HOH MA 11 . ? 9.086 -23.965 49.955 1.00 35.03 ? 1495 HOH A O 1 HETATM 7158 O O . HOH MA 11 . ? 9.697 -17.901 57.329 1.00 26.88 ? 1496 HOH A O 1 HETATM 7159 O O . HOH MA 11 . ? -0.265 -9.847 50.530 1.00 33.06 ? 1497 HOH A O 1 HETATM 7160 O O . HOH MA 11 . ? -1.293 -0.653 33.036 1.00 38.70 ? 1498 HOH A O 1 HETATM 7161 O O . HOH MA 11 . ? 14.989 -19.696 15.539 1.00 33.16 ? 1499 HOH A O 1 HETATM 7162 O O . HOH MA 11 . ? 22.437 -21.442 21.821 1.00 37.21 ? 1500 HOH A O 1 HETATM 7163 O O . HOH MA 11 . ? 15.659 -8.255 65.878 1.00 52.71 ? 1501 HOH A O 1 HETATM 7164 O O . HOH MA 11 . ? 33.989 -7.007 29.272 1.00 29.38 ? 1502 HOH A O 1 HETATM 7165 O O . HOH MA 11 . ? 15.296 -21.480 17.629 1.00 40.73 ? 1503 HOH A O 1 HETATM 7166 O O . HOH MA 11 . ? 9.429 19.948 21.072 1.00 39.01 ? 1504 HOH A O 1 HETATM 7167 O O . HOH MA 11 . ? 18.651 -30.606 46.094 1.00 43.49 ? 1505 HOH A O 1 HETATM 7168 O O . HOH MA 11 . ? 45.182 14.450 27.895 1.00 46.11 ? 1506 HOH A O 1 HETATM 7169 O O . HOH MA 11 . ? 11.738 -22.871 21.534 1.00 45.87 ? 1507 HOH A O 1 HETATM 7170 O O . HOH MA 11 . ? 22.801 -0.864 49.169 1.00 45.78 ? 1508 HOH A O 1 HETATM 7171 O O . HOH MA 11 . ? -1.752 -6.936 55.966 1.00 34.90 ? 1509 HOH A O 1 HETATM 7172 O O . HOH MA 11 . ? 27.547 -18.322 47.930 1.00 30.44 ? 1510 HOH A O 1 HETATM 7173 O O . HOH MA 11 . ? 11.622 -17.846 59.271 1.00 40.13 ? 1511 HOH A O 1 HETATM 7174 O O . HOH MA 11 . ? -22.441 -12.424 20.821 1.00 34.21 ? 1512 HOH A O 1 HETATM 7175 O O . HOH MA 11 . ? -3.587 -12.936 26.098 1.00 33.65 ? 1513 HOH A O 1 HETATM 7176 O O . HOH MA 11 . ? 20.435 -1.460 26.182 1.00 51.92 ? 1514 HOH A O 1 HETATM 7177 O O . HOH MA 11 . ? 3.483 -27.492 61.914 1.00 40.16 ? 1515 HOH A O 1 HETATM 7178 O O A HOH MA 11 . ? -6.243 -8.275 47.422 0.50 29.15 ? 1516 HOH A O 1 HETATM 7179 O O B HOH MA 11 . ? -8.334 -9.454 47.566 0.50 28.35 ? 1516 HOH A O 1 HETATM 7180 O O . HOH MA 11 . ? 26.470 -19.339 18.973 1.00 35.98 ? 1517 HOH A O 1 HETATM 7181 O O . HOH MA 11 . ? -21.615 -20.707 47.666 1.00 34.88 ? 1518 HOH A O 1 HETATM 7182 O O . HOH MA 11 . ? 12.787 -29.351 34.361 1.00 30.22 ? 1519 HOH A O 1 HETATM 7183 O O . HOH MA 11 . ? 25.337 -18.403 49.541 1.00 42.25 ? 1520 HOH A O 1 HETATM 7184 O O . HOH MA 11 . ? -5.712 -1.885 9.179 1.00 46.60 ? 1521 HOH A O 1 HETATM 7185 O O . HOH MA 11 . ? 27.251 -20.436 46.286 1.00 41.24 ? 1522 HOH A O 1 HETATM 7186 O O . HOH MA 11 . ? 10.564 -29.788 29.443 1.00 44.95 ? 1523 HOH A O 1 HETATM 7187 O O . HOH MA 11 . ? -7.759 -13.550 23.276 1.00 41.60 ? 1524 HOH A O 1 HETATM 7188 O O . HOH MA 11 . ? 32.914 -9.532 24.632 1.00 39.11 ? 1525 HOH A O 1 HETATM 7189 O O . HOH MA 11 . ? -4.741 -13.080 23.487 1.00 40.08 ? 1526 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 . GLY A 21 ? 0.5252 0.7219 0.6102 -0.1348 0.0755 -0.0066 56 GLY A N 2 C CA . GLY A 21 ? 0.5283 0.7175 0.6061 -0.1454 0.0724 -0.0093 56 GLY A CA 3 C C . GLY A 21 ? 0.5411 0.7027 0.6016 -0.1479 0.0748 -0.0115 56 GLY A C 4 O O . GLY A 21 ? 0.5666 0.7204 0.6203 -0.1562 0.0729 -0.0140 56 GLY A O 5 N N . SER A 22 ? 0.5249 0.6717 0.5780 -0.1405 0.0789 -0.0105 57 SER A N 6 C CA . SER A 22 ? 0.5129 0.6346 0.5505 -0.1423 0.0823 -0.0115 57 SER A CA 7 C C . SER A 22 ? 0.4830 0.5913 0.5137 -0.1303 0.0819 -0.0104 57 SER A C 8 O O . SER A 22 ? 0.4668 0.5833 0.5033 -0.1218 0.0818 -0.0088 57 SER A O 9 C CB . SER A 22 ? 0.5269 0.6450 0.5619 -0.1485 0.0896 -0.0105 57 SER A CB 10 O OG . SER A 22 ? 0.5368 0.6306 0.5569 -0.1501 0.0932 -0.0108 57 SER A OG 11 N N . CYS A 23 ? 0.4627 0.5502 0.4807 -0.1299 0.0819 -0.0113 58 CYS A N 12 C CA . CYS A 23 ? 0.4823 0.5570 0.4933 -0.1195 0.0813 -0.0101 58 CYS A CA 13 C C . CYS A 23 ? 0.5128 0.5747 0.5154 -0.1175 0.0872 -0.0080 58 CYS A C 14 O O . CYS A 23 ? 0.4972 0.5486 0.4933 -0.1096 0.0867 -0.0068 58 CYS A O 15 C CB . CYS A 23 ? 0.4549 0.5162 0.4581 -0.1183 0.0774 -0.0116 58 CYS A CB 16 S SG . CYS A 23 ? 0.4247 0.5004 0.4366 -0.1165 0.0697 -0.0133 58 CYS A SG 17 N N . LYS A 24 ? 0.5671 0.6307 0.5699 -0.1247 0.0925 -0.0074 59 LYS A N 18 C CA . LYS A 24 ? 0.5949 0.6469 0.5895 -0.1231 0.0983 -0.0050 59 LYS A CA 19 C C . LYS A 24 ? 0.5667 0.6234 0.5631 -0.1129 0.0981 -0.0034 59 LYS A C 20 O O . LYS A 24 ? 0.5339 0.6076 0.5409 -0.1108 0.0976 -0.0036 59 LYS A O 21 C CB . LYS A 24 ? 0.6914 0.7483 0.6881 -0.1324 0.1042 -0.0045 59 LYS A CB 22 C CG . LYS A 24 ? 0.7587 0.7994 0.7439 -0.1331 0.1105 -0.0020 59 LYS A CG 23 C CD . LYS A 24 ? 0.8224 0.8702 0.8109 -0.1413 0.1168 -0.0012 59 LYS A CD 24 C CE . LYS A 24 ? 0.8674 0.9177 0.8585 -0.1538 0.1175 -0.0034 59 LYS A CE 25 N NZ . LYS A 24 ? 0.8922 0.9205 0.8707 -0.1578 0.1182 -0.0041 59 LYS A NZ 26 N N . GLY A 25 ? 0.5688 0.6105 0.5549 -0.1066 0.0983 -0.0019 60 GLY A N 27 C CA . GLY A 25 ? 0.5451 0.5888 0.5307 -0.0975 0.0978 -0.0007 60 GLY A CA 28 C C . GLY A 25 ? 0.5354 0.5868 0.5272 -0.0905 0.0918 -0.0022 60 GLY A C 29 O O . GLY A 25 ? 0.5757 0.6309 0.5686 -0.0836 0.0917 -0.0018 60 GLY A O 30 N N . ARG A 26 ? 0.5102 0.5632 0.5053 -0.0924 0.0872 -0.0039 61 ARG A N 31 C CA . ARG A 26 ? 0.4663 0.5273 0.4678 -0.0867 0.0816 -0.0050 61 ARG A CA 32 C C . ARG A 26 ? 0.4315 0.4817 0.4275 -0.0847 0.0770 -0.0058 61 ARG A C 33 O O . ARG A 26 ? 0.3872 0.4428 0.3876 -0.0803 0.0723 -0.0067 61 ARG A O 34 C CB . ARG A 26 ? 0.4787 0.5579 0.4928 -0.0907 0.0800 -0.0062 61 ARG A CB 35 C CG . ARG A 26 ? 0.4716 0.5654 0.4943 -0.0910 0.0840 -0.0053 61 ARG A CG 36 C CD . ARG A 26 ? 0.4557 0.5685 0.4914 -0.0956 0.0820 -0.0059 61 ARG A CD 37 N NE . ARG A 26 ? 0.4278 0.5472 0.4691 -0.0907 0.0758 -0.0065 61 ARG A NE 38 C CZ . ARG A 26 ? 0.4096 0.5412 0.4587 -0.0950 0.0717 -0.0071 61 ARG A CZ 39 N NH1 . ARG A 26 ? 0.4133 0.5530 0.4665 -0.1048 0.0729 -0.0075 61 ARG A NH1 40 N NH2 . ARG A 26 ? 0.3659 0.5017 0.4186 -0.0897 0.0663 -0.0072 61 ARG A NH2 41 N N . CYS A 27 ? 0.4567 0.4912 0.4428 -0.0874 0.0786 -0.0052 62 CYS A N 42 C CA . CYS A 27 ? 0.4461 0.4709 0.4276 -0.0860 0.0750 -0.0060 62 CYS A CA 43 C C . CYS A 27 ? 0.4118 0.4347 0.3921 -0.0769 0.0712 -0.0054 62 CYS A C 44 O O . CYS A 27 ? 0.4029 0.4214 0.3788 -0.0721 0.0726 -0.0036 62 CYS A O 45 C CB . CYS A 27 ? 0.4967 0.5039 0.4676 -0.0894 0.0784 -0.0050 62 CYS A CB 46 S SG . CYS A 27 ? 0.5860 0.5931 0.5573 -0.1016 0.0821 -0.0067 62 CYS A SG 47 N N . PHE A 28 ? 0.3854 0.4122 0.3695 -0.0751 0.0664 -0.0069 63 PHE A N 48 C CA . PHE A 28 ? 0.3966 0.4231 0.3808 -0.0672 0.0625 -0.0066 63 PHE A CA 49 C C . PHE A 28 ? 0.4022 0.4364 0.3900 -0.0618 0.0629 -0.0060 63 PHE A C 50 O O . PHE A 28 ? 0.3814 0.4115 0.3659 -0.0558 0.0612 -0.0053 63 PHE A O 51 C CB . PHE A 28 ? 0.4071 0.4182 0.3819 -0.0642 0.0624 -0.0052 63 PHE A CB 52 C CG . PHE A 28 ? 0.4047 0.4069 0.3755 -0.0689 0.0628 -0.0061 63 PHE A CG 53 C CD1 . PHE A 28 ? 0.4250 0.4290 0.3982 -0.0691 0.0590 -0.0080 63 PHE A CD1 54 C CD2 . PHE A 28 ? 0.4465 0.4382 0.4109 -0.0735 0.0674 -0.0051 63 PHE A CD2 55 C CE1 . PHE A 28 ? 0.4265 0.4217 0.3952 -0.0739 0.0599 -0.0093 63 PHE A CE1 56 C CE2 . PHE A 28 ? 0.4364 0.4186 0.3964 -0.0781 0.0685 -0.0063 63 PHE A CE2 57 C CZ . PHE A 28 ? 0.4525 0.4364 0.4145 -0.0784 0.0648 -0.0085 63 PHE A CZ 58 N N . GLU A 29 ? 0.4028 0.4487 0.3977 -0.0643 0.0652 -0.0063 64 GLU A N 59 C CA . GLU A 29 ? 0.4027 0.4565 0.4016 -0.0593 0.0664 -0.0060 64 GLU A CA 60 C C . GLU A 29 ? 0.3832 0.4411 0.3861 -0.0532 0.0618 -0.0068 64 GLU A C 61 O O . GLU A 29 ? 0.3639 0.4253 0.3708 -0.0542 0.0580 -0.0075 64 GLU A O 62 C CB . GLU A 29 ? 0.4205 0.4881 0.4283 -0.0629 0.0696 -0.0061 64 GLU A CB 63 C CG . GLU A 29 ? 0.4510 0.5324 0.4696 -0.0645 0.0661 -0.0070 64 GLU A CG 64 C CD . GLU A 29 ? 0.5031 0.5990 0.5309 -0.0698 0.0690 -0.0067 64 GLU A CD 65 O OE1 . GLU A 29 ? 0.5055 0.6019 0.5324 -0.0718 0.0742 -0.0060 64 GLU A OE1 66 O OE2 . GLU A 29 ? 0.4961 0.6038 0.5322 -0.0723 0.0657 -0.0070 64 GLU A OE2 67 N N . LEU A 30 ? 0.4158 0.4728 0.4170 -0.0472 0.0625 -0.0066 65 LEU A N 68 C CA . LEU A 30 ? 0.4603 0.5202 0.4648 -0.0413 0.0590 -0.0073 65 LEU A CA 69 C C . LEU A 30 ? 0.5204 0.5946 0.5358 -0.0394 0.0596 -0.0075 65 LEU A C 70 O O . LEU A 30 ? 0.5593 0.6374 0.5792 -0.0354 0.0564 -0.0078 65 LEU A O 71 C CB . LEU A 30 ? 0.4366 0.4879 0.4333 -0.0364 0.0596 -0.0073 65 LEU A CB 72 C CG . LEU A 30 ? 0.4304 0.4691 0.4175 -0.0367 0.0577 -0.0064 65 LEU A CG 73 C CD1 . LEU A 30 ? 0.4539 0.4860 0.4327 -0.0340 0.0595 -0.0059 65 LEU A CD1 74 C CD2 . LEU A 30 ? 0.4208 0.4572 0.4087 -0.0346 0.0526 -0.0068 65 LEU A CD2 75 N N . GLN A 31 ? 0.5993 0.6814 0.6193 -0.0423 0.0639 -0.0071 66 GLN A N 76 C CA . GLN A 31 ? 0.6924 0.7901 0.7243 -0.0409 0.0650 -0.0067 66 GLN A CA 77 C C . GLN A 31 ? 0.6993 0.8059 0.7391 -0.0419 0.0599 -0.0064 66 GLN A C 78 O O . GLN A 31 ? 0.6418 0.7461 0.6796 -0.0474 0.0572 -0.0067 66 GLN A O 79 C CB . GLN A 31 ? 0.7765 0.8819 0.8123 -0.0461 0.0700 -0.0061 66 GLN A CB 80 C CG . GLN A 31 ? 0.8659 0.9882 0.9143 -0.0440 0.0725 -0.0052 66 GLN A CG 81 C CD . GLN A 31 ? 0.9534 1.0745 1.0012 -0.0365 0.0763 -0.0054 66 GLN A CD 82 O OE1 . GLN A 31 ? 1.0015 1.1161 1.0425 -0.0365 0.0811 -0.0058 66 GLN A OE1 83 N NE2 . GLN A 31 ? 0.9863 1.1130 1.0406 -0.0301 0.0744 -0.0050 66 GLN A NE2 84 N N . GLU A 32 ? 0.7680 0.8844 0.8162 -0.0366 0.0589 -0.0056 67 GLU A N 85 C CA . GLU A 32 ? 0.8205 0.9459 0.8760 -0.0364 0.0538 -0.0048 67 GLU A CA 86 C C . GLU A 32 ? 0.7505 0.8937 0.8175 -0.0407 0.0544 -0.0034 67 GLU A C 87 O O . GLU A 32 ? 0.7485 0.9033 0.8245 -0.0369 0.0573 -0.0019 67 GLU A O 88 C CB . GLU A 32 ? 0.8593 0.9851 0.9175 -0.0279 0.0521 -0.0042 67 GLU A CB 89 C CG . GLU A 32 ? 0.9311 1.0603 0.9931 -0.0214 0.0571 -0.0037 67 GLU A CG 90 C CD . GLU A 32 ? 0.9814 1.0954 1.0323 -0.0186 0.0601 -0.0055 67 GLU A CD 91 O OE1 . GLU A 32 ? 0.9703 1.0785 1.0147 -0.0226 0.0631 -0.0064 67 GLU A OE1 92 O OE2 . GLU A 32 ? 1.0225 1.1304 1.0708 -0.0126 0.0596 -0.0060 67 GLU A OE2 93 N N . VAL A 33 ? 0.6623 0.8077 0.7289 -0.0488 0.0521 -0.0039 68 VAL A N 94 C CA . VAL A 33 ? 0.6015 0.7642 0.6784 -0.0546 0.0522 -0.0027 68 VAL A CA 95 C C . VAL A 33 ? 0.6094 0.7833 0.6931 -0.0548 0.0460 -0.0015 68 VAL A C 96 O O . VAL A 33 ? 0.5711 0.7375 0.6484 -0.0577 0.0418 -0.0027 68 VAL A O 97 C CB . VAL A 33 ? 0.5989 0.7570 0.6705 -0.0647 0.0540 -0.0042 68 VAL A CB 98 C CG1 . VAL A 33 ? 0.5985 0.7753 0.6809 -0.0717 0.0540 -0.0031 68 VAL A CG1 99 C CG2 . VAL A 33 ? 0.6157 0.7625 0.6799 -0.0642 0.0601 -0.0048 68 VAL A CG2 100 N N . GLY A 34 ? 0.5858 0.7776 0.6823 -0.0512 0.0458 0.0011 69 GLY A N 101 C CA . GLY A 34 ? 0.5704 0.7751 0.6744 -0.0505 0.0399 0.0032 69 GLY A CA 102 C C . GLY A 34 ? 0.5513 0.7709 0.6613 -0.0604 0.0374 0.0036 69 GLY A C 103 O O . GLY A 34 ? 0.5043 0.7270 0.6153 -0.0669 0.0410 0.0027 69 GLY A O 104 N N . PRO A 35 ? 0.5808 0.8102 0.6947 -0.0619 0.0311 0.0050 70 PRO A N 105 C CA . PRO A 35 ? 0.6072 0.8521 0.7266 -0.0720 0.0279 0.0054 70 PRO A CA 106 C C . PRO A 35 ? 0.6139 0.8824 0.7491 -0.0717 0.0298 0.0088 70 PRO A C 107 O O . PRO A 35 ? 0.5662 0.8412 0.7096 -0.0618 0.0319 0.0118 70 PRO A O 108 C CB . PRO A 35 ? 0.6245 0.8732 0.7432 -0.0716 0.0206 0.0065 70 PRO A CB 109 C CG . PRO A 35 ? 0.5980 0.8428 0.7184 -0.0591 0.0206 0.0088 70 PRO A CG 110 C CD . PRO A 35 ? 0.5849 0.8115 0.6977 -0.0546 0.0266 0.0065 70 PRO A CD 111 N N . PRO A 36 ? 0.6102 0.8913 0.7499 -0.0824 0.0294 0.0085 71 PRO A N 112 C CA . PRO A 36 ? 0.6165 0.8902 0.7465 -0.0945 0.0268 0.0050 71 PRO A CA 113 C C . PRO A 36 ? 0.6170 0.8718 0.7358 -0.1001 0.0325 0.0011 71 PRO A C 114 O O . PRO A 36 ? 0.7040 0.9528 0.8154 -0.1109 0.0317 -0.0017 71 PRO A O 115 C CB . PRO A 36 ? 0.6007 0.8998 0.7430 -0.1031 0.0242 0.0070 71 PRO A CB 116 C CG . PRO A 36 ? 0.5983 0.9118 0.7540 -0.0975 0.0294 0.0102 71 PRO A CG 117 C CD . PRO A 36 ? 0.5755 0.8761 0.7287 -0.0840 0.0331 0.0109 71 PRO A CD 118 N N . ASP A 37 ? 0.5675 0.8123 0.6843 -0.0930 0.0383 0.0011 72 ASP A N 119 C CA . ASP A 37 ? 0.5256 0.7570 0.6343 -0.0982 0.0444 -0.0012 72 ASP A CA 120 C C . ASP A 37 ? 0.4728 0.6805 0.5654 -0.1014 0.0437 -0.0046 72 ASP A C 121 O O . ASP A 37 ? 0.4703 0.6679 0.5571 -0.0953 0.0406 -0.0050 72 ASP A O 122 C CB . ASP A 37 ? 0.5598 0.7876 0.6702 -0.0895 0.0505 0.0000 72 ASP A CB 123 C CG . ASP A 37 ? 0.5844 0.8351 0.7110 -0.0863 0.0525 0.0032 72 ASP A CG 124 O OD1 . ASP A 37 ? 0.6446 0.9059 0.7769 -0.0934 0.0558 0.0036 72 ASP A OD1 125 O OD2 . ASP A 37 ? 0.5732 0.8310 0.7068 -0.0765 0.0511 0.0057 72 ASP A OD2 126 N N . CYS A 38 ? 0.4317 0.6306 0.5172 -0.1108 0.0470 -0.0069 73 CYS A N 127 C CA . CYS A 38 ? 0.3991 0.5756 0.4696 -0.1144 0.0470 -0.0099 73 CYS A CA 128 C C . CYS A 38 ? 0.3868 0.5450 0.4488 -0.1059 0.0506 -0.0099 73 CYS A C 129 O O . CYS A 38 ? 0.3438 0.5028 0.4082 -0.1020 0.0552 -0.0086 73 CYS A O 130 C CB . CYS A 38 ? 0.4247 0.5964 0.4898 -0.1271 0.0498 -0.0122 73 CYS A CB 131 S SG . CYS A 38 ? 0.4886 0.6561 0.5528 -0.1301 0.0583 -0.0116 73 CYS A SG 132 N N . ARG A 39 ? 0.3783 0.5204 0.4302 -0.1033 0.0483 -0.0113 74 ARG A N 133 C CA . ARG A 39 ? 0.3755 0.5025 0.4203 -0.0946 0.0500 -0.0110 74 ARG A CA 134 C C . ARG A 39 ? 0.3633 0.4700 0.3953 -0.0980 0.0537 -0.0124 74 ARG A C 135 O O . ARG A 39 ? 0.3416 0.4429 0.3687 -0.1069 0.0545 -0.0141 74 ARG A O 136 C CB . ARG A 39 ? 0.3941 0.5193 0.4381 -0.0881 0.0448 -0.0109 74 ARG A CB 137 C CG . ARG A 39 ? 0.4045 0.5473 0.4605 -0.0818 0.0421 -0.0086 74 ARG A CG 138 C CD . ARG A 39 ? 0.4085 0.5521 0.4645 -0.0781 0.0363 -0.0084 74 ARG A CD 139 N NE . ARG A 39 ? 0.4123 0.5377 0.4580 -0.0733 0.0360 -0.0095 74 ARG A NE 140 C CZ . ARG A 39 ? 0.4447 0.5671 0.4884 -0.0693 0.0318 -0.0094 74 ARG A CZ 141 N NH1 . ARG A 39 ? 0.4688 0.6045 0.5195 -0.0690 0.0273 -0.0082 74 ARG A NH1 142 N NH2 . ARG A 39 ? 0.4392 0.5457 0.4740 -0.0655 0.0321 -0.0103 74 ARG A NH2 143 N N . CYS A 40 ? 0.3486 0.4442 0.3752 -0.0910 0.0561 -0.0114 75 CYS A N 144 C CA . CYS A 40 ? 0.3589 0.4355 0.3738 -0.0922 0.0597 -0.0117 75 CYS A CA 145 C C . CYS A 40 ? 0.3515 0.4159 0.3598 -0.0838 0.0580 -0.0111 75 CYS A C 146 O O . CYS A 40 ? 0.3532 0.4032 0.3526 -0.0825 0.0608 -0.0104 75 CYS A O 147 C CB . CYS A 40 ? 0.3746 0.4509 0.3891 -0.0938 0.0655 -0.0104 75 CYS A CB 148 S SG . CYS A 40 ? 0.3953 0.4871 0.4183 -0.1043 0.0680 -0.0108 75 CYS A SG 149 N N . ASP A 41 ? 0.3253 0.3956 0.3378 -0.0784 0.0534 -0.0112 76 ASP A N 150 C CA . ASP A 41 ? 0.3406 0.4020 0.3485 -0.0704 0.0517 -0.0106 76 ASP A CA 151 C C . ASP A 41 ? 0.3230 0.3734 0.3242 -0.0714 0.0492 -0.0117 76 ASP A C 152 O O . ASP A 41 ? 0.2999 0.3497 0.2999 -0.0780 0.0487 -0.0132 76 ASP A O 153 C CB . ASP A 41 ? 0.3488 0.4214 0.3645 -0.0638 0.0486 -0.0100 76 ASP A CB 154 C CG . ASP A 41 ? 0.3622 0.4455 0.3844 -0.0657 0.0441 -0.0106 76 ASP A CG 155 O OD1 . ASP A 41 ? 0.3765 0.4729 0.4062 -0.0702 0.0443 -0.0104 76 ASP A OD1 156 O OD2 . ASP A 41 ? 0.4029 0.4820 0.4226 -0.0631 0.0405 -0.0110 76 ASP A OD2 157 N N . ASN A 42 ? 0.3075 0.3494 0.3042 -0.0648 0.0479 -0.0110 77 ASN A N 158 C CA . ASN A 42 ? 0.3300 0.3622 0.3212 -0.0636 0.0455 -0.0116 77 ASN A CA 159 C C . ASN A 42 ? 0.3247 0.3615 0.3180 -0.0672 0.0421 -0.0134 77 ASN A C 160 O O . ASN A 42 ? 0.3523 0.3794 0.3396 -0.0696 0.0421 -0.0145 77 ASN A O 161 C CB . ASN A 42 ? 0.3506 0.3813 0.3416 -0.0555 0.0430 -0.0106 77 ASN A CB 162 C CG . ASN A 42 ? 0.3563 0.3776 0.3414 -0.0518 0.0455 -0.0089 77 ASN A CG 163 O OD1 . ASN A 42 ? 0.4222 0.4412 0.4050 -0.0540 0.0492 -0.0081 77 ASN A OD1 164 N ND2 . ASN A 42 ? 0.3233 0.3395 0.3056 -0.0465 0.0433 -0.0082 77 ASN A ND2 165 N N . LEU A 43 ? 0.3244 0.3756 0.3261 -0.0668 0.0392 -0.0134 78 LEU A N 166 C CA . LEU A 43 ? 0.3371 0.3941 0.3409 -0.0695 0.0352 -0.0145 78 LEU A CA 167 C C . LEU A 43 ? 0.3350 0.4030 0.3433 -0.0776 0.0348 -0.0155 78 LEU A C 168 O O . LEU A 43 ? 0.3256 0.4008 0.3361 -0.0803 0.0310 -0.0162 78 LEU A O 169 C CB . LEU A 43 ? 0.3665 0.4314 0.3758 -0.0627 0.0312 -0.0133 78 LEU A CB 170 C CG . LEU A 43 ? 0.3858 0.4400 0.3900 -0.0561 0.0304 -0.0128 78 LEU A CG 171 C CD1 . LEU A 43 ? 0.4143 0.4763 0.4242 -0.0500 0.0271 -0.0116 78 LEU A CD1 172 C CD2 . LEU A 43 ? 0.3786 0.4221 0.3754 -0.0585 0.0298 -0.0142 78 LEU A CD2 173 N N . CYS A 44 ? 0.3218 0.3917 0.3313 -0.0822 0.0386 -0.0155 79 CYS A N 174 C CA . CYS A 44 ? 0.3146 0.3975 0.3298 -0.0903 0.0380 -0.0162 79 CYS A CA 175 C C . CYS A 44 ? 0.3266 0.4058 0.3362 -0.0985 0.0362 -0.0188 79 CYS A C 176 O O . CYS A 44 ? 0.3358 0.4286 0.3508 -0.1035 0.0328 -0.0192 79 CYS A O 177 C CB . CYS A 44 ? 0.3259 0.4104 0.3426 -0.0943 0.0430 -0.0158 79 CYS A CB 178 S SG . CYS A 44 ? 0.3177 0.3825 0.3224 -0.1007 0.0486 -0.0173 79 CYS A SG 179 N N . LYS A 45 ? 0.3278 0.3887 0.3266 -0.0997 0.0385 -0.0204 80 LYS A N 180 C CA . LYS A 45 ? 0.3736 0.4273 0.3650 -0.1070 0.0378 -0.0234 80 LYS A CA 181 C C . LYS A 45 ? 0.3688 0.4286 0.3614 -0.1048 0.0322 -0.0237 80 LYS A C 182 O O . LYS A 45 ? 0.4128 0.4769 0.4037 -0.1121 0.0298 -0.0258 80 LYS A O 183 C CB . LYS A 45 ? 0.3886 0.4203 0.3683 -0.1067 0.0422 -0.0245 80 LYS A CB 184 C CG . LYS A 45 ? 0.4458 0.4679 0.4217 -0.1095 0.0481 -0.0241 80 LYS A CG 185 C CD . LYS A 45 ? 0.5061 0.5275 0.4790 -0.1214 0.0504 -0.0268 80 LYS A CD 186 C CE . LYS A 45 ? 0.5591 0.5620 0.5200 -0.1260 0.0532 -0.0297 80 LYS A CE 187 N NZ . LYS A 45 ? 0.6021 0.6070 0.5603 -0.1387 0.0539 -0.0330 80 LYS A NZ 188 N N . SER A 46 ? 0.3604 0.4205 0.3555 -0.0951 0.0302 -0.0217 81 SER A N 189 C CA . SER A 46 ? 0.3781 0.4428 0.3742 -0.0919 0.0252 -0.0214 81 SER A CA 190 C C . SER A 46 ? 0.4088 0.4940 0.4145 -0.0938 0.0206 -0.0201 81 SER A C 191 O O . SER A 46 ? 0.4216 0.5114 0.4263 -0.0955 0.0164 -0.0205 81 SER A O 192 C CB . SER A 46 ? 0.3488 0.4085 0.3455 -0.0814 0.0248 -0.0194 81 SER A CB 193 O OG . SER A 46 ? 0.3626 0.4050 0.3509 -0.0795 0.0285 -0.0201 81 SER A OG 194 N N . TYR A 47 ? 0.4272 0.5246 0.4419 -0.0931 0.0214 -0.0183 82 TYR A N 195 C CA . TYR A 47 ? 0.4435 0.5620 0.4688 -0.0951 0.0176 -0.0165 82 TYR A CA 196 C C . TYR A 47 ? 0.4640 0.5902 0.4904 -0.1066 0.0182 -0.0181 82 TYR A C 197 O O . TYR A 47 ? 0.5236 0.6690 0.5600 -0.1087 0.0156 -0.0162 82 TYR A O 198 C CB . TYR A 47 ? 0.4162 0.5449 0.4518 -0.0873 0.0185 -0.0132 82 TYR A CB 199 C CG . TYR A 47 ? 0.4345 0.5587 0.4707 -0.0764 0.0176 -0.0114 82 TYR A CG 200 C CD1 . TYR A 47 ? 0.4416 0.5507 0.4719 -0.0714 0.0212 -0.0119 82 TYR A CD1 201 C CD2 . TYR A 47 ? 0.4369 0.5722 0.4796 -0.0713 0.0133 -0.0089 82 TYR A CD2 202 C CE1 . TYR A 47 ? 0.4486 0.5535 0.4790 -0.0624 0.0204 -0.0106 82 TYR A CE1 203 C CE2 . TYR A 47 ? 0.4099 0.5400 0.4526 -0.0619 0.0129 -0.0074 82 TYR A CE2 204 C CZ . TYR A 47 ? 0.4252 0.5401 0.4616 -0.0579 0.0165 -0.0085 82 TYR A CZ 205 O OH . TYR A 47 ? 0.4441 0.5538 0.4801 -0.0496 0.0161 -0.0073 82 TYR A OH 206 N N . SER A 48 ? 0.4512 0.5630 0.4675 -0.1139 0.0216 -0.0214 83 SER A N 207 C CA . SER A 48 ? 0.4524 0.5687 0.4682 -0.1258 0.0230 -0.0234 83 SER A CA 208 C C . SER A 48 ? 0.4366 0.5689 0.4639 -0.1265 0.0244 -0.0211 83 SER A C 209 O O . SER A 48 ? 0.4338 0.5827 0.4677 -0.1340 0.0221 -0.0209 83 SER A O 210 C CB . SER A 48 ? 0.4731 0.5982 0.4873 -0.1339 0.0178 -0.0251 83 SER A CB 211 O OG . SER A 48 ? 0.5307 0.6387 0.5322 -0.1355 0.0180 -0.0281 83 SER A OG 212 N N . SER A 49 ? 0.4253 0.5528 0.4548 -0.1191 0.0284 -0.0194 84 SER A N 213 C CA . SER A 49 ? 0.4065 0.5491 0.4475 -0.1171 0.0301 -0.0167 84 SER A CA 214 C C . SER A 49 ? 0.3712 0.5038 0.4089 -0.1182 0.0368 -0.0170 84 SER A C 215 O O . SER A 49 ? 0.3236 0.4658 0.3694 -0.1147 0.0391 -0.0149 84 SER A O 216 C CB . SER A 49 ? 0.4105 0.5604 0.4590 -0.1051 0.0281 -0.0136 84 SER A CB 217 O OG . SER A 49 ? 0.4618 0.5939 0.5024 -0.0975 0.0301 -0.0139 84 SER A OG 218 N N . CYS A 50 ? 0.3694 0.4826 0.3951 -0.1226 0.0402 -0.0195 85 CYS A N 219 C CA . CYS A 50 ? 0.3639 0.4664 0.3857 -0.1229 0.0466 -0.0192 85 CYS A CA 220 C C . CYS A 50 ? 0.3756 0.4885 0.4023 -0.1325 0.0493 -0.0194 85 CYS A C 221 O O . CYS A 50 ? 0.3637 0.4857 0.3925 -0.1416 0.0468 -0.0210 85 CYS A O 222 C CB . CYS A 50 ? 0.3821 0.4608 0.3899 -0.1243 0.0499 -0.0210 85 CYS A CB 223 S SG . CYS A 50 ? 0.3731 0.4387 0.3743 -0.1147 0.0470 -0.0210 85 CYS A SG 224 N N . CYS A 51 ? 0.4011 0.5129 0.4294 -0.1310 0.0545 -0.0179 86 CYS A N 225 C CA . CYS A 51 ? 0.4292 0.5475 0.4604 -0.1408 0.0583 -0.0182 86 CYS A CA 226 C C . CYS A 51 ? 0.4802 0.5821 0.4996 -0.1510 0.0607 -0.0212 86 CYS A C 227 O O . CYS A 51 ? 0.4379 0.5203 0.4462 -0.1485 0.0613 -0.0225 86 CYS A O 228 C CB . CYS A 51 ? 0.4391 0.5562 0.4720 -0.1372 0.0641 -0.0160 86 CYS A CB 229 S SG . CYS A 51 ? 0.4492 0.5830 0.4945 -0.1250 0.0629 -0.0128 86 CYS A SG 230 N N . HIS A 52 ? 0.5194 0.6296 0.5418 -0.1625 0.0625 -0.0223 87 HIS A N 231 C CA . HIS A 52 ? 0.5536 0.6502 0.5656 -0.1745 0.0651 -0.0256 87 HIS A CA 232 C C . HIS A 52 ? 0.5396 0.6097 0.5381 -0.1730 0.0714 -0.0259 87 HIS A C 233 O O . HIS A 52 ? 0.5821 0.6348 0.5692 -0.1783 0.0729 -0.0286 87 HIS A O 234 C CB . HIS A 52 ? 0.6150 0.7265 0.6339 -0.1868 0.0669 -0.0261 87 HIS A CB 235 C CG . HIS A 52 ? 0.6450 0.7559 0.6662 -0.1865 0.0735 -0.0238 87 HIS A CG 236 N ND1 . HIS A 52 ? 0.6705 0.7977 0.7034 -0.1788 0.0738 -0.0204 87 HIS A ND1 237 C CD2 . HIS A 52 ? 0.6897 0.7850 0.7022 -0.1929 0.0803 -0.0244 87 HIS A CD2 238 C CE1 . HIS A 52 ? 0.6939 0.8160 0.7252 -0.1808 0.0804 -0.0191 87 HIS A CE1 239 N NE2 . HIS A 52 ? 0.7165 0.8195 0.7356 -0.1893 0.0843 -0.0213 87 HIS A NE2 240 N N . ASP A 53 ? 0.5286 0.5957 0.5282 -0.1657 0.0752 -0.0228 88 ASP A N 241 C CA . ASP A 53 ? 0.5313 0.5752 0.5190 -0.1635 0.0811 -0.0219 88 ASP A CA 242 C C . ASP A 53 ? 0.5408 0.5734 0.5238 -0.1506 0.0797 -0.0202 88 ASP A C 243 O O . ASP A 53 ? 0.5246 0.5423 0.5003 -0.1462 0.0840 -0.0181 88 ASP A O 244 C CB . ASP A 53 ? 0.5265 0.5731 0.5166 -0.1657 0.0869 -0.0196 88 ASP A CB 245 C CG . ASP A 53 ? 0.5419 0.6059 0.5432 -0.1572 0.0857 -0.0168 88 ASP A CG 246 O OD1 . ASP A 53 ? 0.5140 0.5876 0.5214 -0.1491 0.0804 -0.0164 88 ASP A OD1 247 O OD2 . ASP A 53 ? 0.5609 0.6283 0.5645 -0.1585 0.0905 -0.0149 88 ASP A OD2 248 N N . PHE A 54 ? 0.5134 0.5534 0.5005 -0.1449 0.0736 -0.0208 89 PHE A N 249 C CA . PHE A 54 ? 0.5102 0.5415 0.4939 -0.1332 0.0719 -0.0192 89 PHE A CA 250 C C . PHE A 54 ? 0.5614 0.5691 0.5319 -0.1333 0.0748 -0.0199 89 PHE A C 251 O O . PHE A 54 ? 0.5473 0.5423 0.5119 -0.1271 0.0779 -0.0174 89 PHE A O 252 C CB . PHE A 54 ? 0.4628 0.5059 0.4529 -0.1283 0.0651 -0.0199 89 PHE A CB 253 C CG . PHE A 54 ? 0.4397 0.4732 0.4257 -0.1176 0.0632 -0.0186 89 PHE A CG 254 C CD1 . PHE A 54 ? 0.4353 0.4721 0.4247 -0.1085 0.0633 -0.0160 89 PHE A CD1 255 C CD2 . PHE A 54 ? 0.4438 0.4647 0.4222 -0.1171 0.0619 -0.0202 89 PHE A CD2 256 C CE1 . PHE A 54 ? 0.4128 0.4414 0.3985 -0.0995 0.0615 -0.0149 89 PHE A CE1 257 C CE2 . PHE A 54 ? 0.4409 0.4540 0.4162 -0.1076 0.0603 -0.0189 89 PHE A CE2 258 C CZ . PHE A 54 ? 0.4282 0.4455 0.4073 -0.0991 0.0599 -0.0162 89 PHE A CZ 259 N N . ASP A 55 ? 0.6033 0.6058 0.5692 -0.1406 0.0740 -0.0232 90 ASP A N 260 C CA . ASP A 55 ? 0.6983 0.6787 0.6520 -0.1405 0.0767 -0.0243 90 ASP A CA 261 C C . ASP A 55 ? 0.7234 0.6860 0.6683 -0.1431 0.0841 -0.0229 90 ASP A C 262 O O . ASP A 55 ? 0.7871 0.7314 0.7231 -0.1385 0.0868 -0.0219 90 ASP A O 263 C CB . ASP A 55 ? 0.6828 0.6615 0.6327 -0.1489 0.0748 -0.0287 90 ASP A CB 264 C CG . ASP A 55 ? 0.7038 0.7016 0.6627 -0.1472 0.0673 -0.0296 90 ASP A CG 265 O OD1 . ASP A 55 ? 0.7357 0.7535 0.7049 -0.1503 0.0645 -0.0292 90 ASP A OD1 266 O OD2 . ASP A 55 ? 0.6691 0.6622 0.6248 -0.1426 0.0643 -0.0305 90 ASP A OD2 267 N N . GLU A 56 ? 0.7747 0.7428 0.7222 -0.1497 0.0874 -0.0223 91 GLU A N 268 C CA . GLU A 56 ? 0.7974 0.7490 0.7366 -0.1518 0.0946 -0.0203 91 GLU A CA 269 C C . GLU A 56 ? 0.8146 0.7668 0.7553 -0.1427 0.0962 -0.0156 91 GLU A C 270 O O . GLU A 56 ? 0.8998 0.8348 0.8318 -0.1384 0.1002 -0.0129 91 GLU A O 271 C CB . GLU A 56 ? 0.8689 0.8229 0.8081 -0.1652 0.0985 -0.0223 91 GLU A CB 272 C CG . GLU A 56 ? 0.8859 0.8619 0.8368 -0.1681 0.0975 -0.0212 91 GLU A CG 273 C CD . GLU A 56 ? 0.9737 0.9491 0.9232 -0.1812 0.1026 -0.0225 91 GLU A CD 274 O OE1 . GLU A 56 ? 1.0068 0.9690 0.9478 -0.1904 0.1051 -0.0256 91 GLU A OE1 275 O OE2 . GLU A 56 ? 0.9712 0.9593 0.9279 -0.1826 0.1044 -0.0205 91 GLU A OE2 276 N N . LEU A 57 ? 0.7599 0.7317 0.7112 -0.1398 0.0932 -0.0146 92 LEU A N 277 C CA . LEU A 57 ? 0.7174 0.6906 0.6696 -0.1319 0.0948 -0.0107 92 LEU A CA 278 C C . LEU A 57 ? 0.7067 0.6755 0.6570 -0.1200 0.0913 -0.0087 92 LEU A C 279 O O . LEU A 57 ? 0.6962 0.6555 0.6408 -0.1142 0.0938 -0.0053 92 LEU A O 280 C CB . LEU A 57 ? 0.7221 0.7171 0.6860 -0.1326 0.0936 -0.0104 92 LEU A CB 281 C CG . LEU A 57 ? 0.7283 0.7307 0.6957 -0.1434 0.0976 -0.0112 92 LEU A CG 282 C CD1 . LEU A 57 ? 0.7105 0.7350 0.6902 -0.1412 0.0964 -0.0103 92 LEU A CD1 283 C CD2 . LEU A 57 ? 0.7649 0.7505 0.7223 -0.1468 0.1048 -0.0090 92 LEU A CD2 284 N N . CYS A 58 ? 0.6891 0.6655 0.6442 -0.1168 0.0856 -0.0107 93 CYS A N 285 C CA . CYS A 58 ? 0.6773 0.6531 0.6327 -0.1061 0.0817 -0.0092 93 CYS A CA 286 C C . CYS A 58 ? 0.6785 0.6379 0.6257 -0.1030 0.0816 -0.0091 93 CYS A C 287 O O . CYS A 58 ? 0.7151 0.6689 0.6594 -0.0946 0.0807 -0.0065 93 CYS A O 288 C CB . CYS A 58 ? 0.6149 0.6088 0.5806 -0.1035 0.0758 -0.0109 93 CYS A CB 289 S SG . CYS A 58 ? 0.5481 0.5627 0.5250 -0.1060 0.0762 -0.0106 93 CYS A SG 290 N N . LEU A 59 ? 0.6884 0.6405 0.6317 -0.1098 0.0827 -0.0120 94 LEU A N 291 C CA . LEU A 59 ? 0.6791 0.6146 0.6143 -0.1071 0.0837 -0.0121 94 LEU A CA 292 C C . LEU A 59 ? 0.6838 0.6000 0.6089 -0.1107 0.0907 -0.0107 94 LEU A C 293 O O . LEU A 59 ? 0.7498 0.6535 0.6684 -0.1158 0.0935 -0.0131 94 LEU A O 294 C CB . LEU A 59 ? 0.6495 0.5878 0.5856 -0.1116 0.0805 -0.0164 94 LEU A CB 295 C CG . LEU A 59 ? 0.6421 0.5994 0.5880 -0.1088 0.0737 -0.0176 94 LEU A CG 296 C CD1 . LEU A 59 ? 0.5986 0.5573 0.5437 -0.1141 0.0709 -0.0215 94 LEU A CD1 297 C CD2 . LEU A 59 ? 0.6405 0.5988 0.5883 -0.0974 0.0707 -0.0149 94 LEU A CD2 298 N N . LYS A 60 ? 0.7106 0.6234 0.6337 -0.1077 0.0939 -0.0067 95 LYS A N 299 C CA . LYS A 60 ? 0.6955 0.5895 0.6088 -0.1100 0.1007 -0.0044 95 LYS A CA 300 C C . LYS A 60 ? 0.7227 0.6006 0.6291 -0.1027 0.1019 -0.0023 95 LYS A C 301 O O . LYS A 60 ? 0.6585 0.5404 0.5673 -0.0933 0.0982 0.0001 95 LYS A O 302 C CB . LYS A 60 ? 0.7032 0.5986 0.6159 -0.1076 0.1033 -0.0001 95 LYS A CB 303 C CG . LYS A 60 ? 0.6868 0.5980 0.6065 -0.1139 0.1032 -0.0015 95 LYS A CG 304 C CD . LYS A 60 ? 0.7169 0.6277 0.6345 -0.1115 0.1065 0.0027 95 LYS A CD 305 C CE . LYS A 60 ? 0.7309 0.6492 0.6511 -0.1010 0.1025 0.0055 95 LYS A CE 306 N NZ . LYS A 60 ? 0.7687 0.6847 0.6847 -0.0992 0.1061 0.0098 95 LYS A NZ 307 N N . THR A 61 ? 0.6655 0.5254 0.5634 -0.1071 0.1071 -0.0033 96 THR A N 308 C CA . THR A 61 ? 0.6404 0.4834 0.5314 -0.1001 0.1096 -0.0009 96 THR A CA 309 C C . THR A 61 ? 0.6095 0.4325 0.4909 -0.0994 0.1171 0.0033 96 THR A C 310 O O . THR A 61 ? 0.5850 0.3944 0.4613 -0.0923 0.1196 0.0065 96 THR A O 311 C CB . THR A 61 ? 0.6695 0.5060 0.5579 -0.1036 0.1096 -0.0058 96 THR A CB 312 O OG1 . THR A 61 ? 0.7208 0.5489 0.6038 -0.1153 0.1142 -0.0098 96 THR A OG1 313 C CG2 . THR A 61 ? 0.6820 0.5372 0.5793 -0.1029 0.1020 -0.0092 96 THR A CG2 314 N N . ALA A 62 ? 0.5870 0.4088 0.4664 -0.1061 0.1209 0.0040 97 ALA A N 315 C CA . ALA A 62 ? 0.6139 0.4150 0.4831 -0.1074 0.1289 0.0077 97 ALA A CA 316 C C . ALA A 62 ? 0.6229 0.4172 0.4890 -0.0958 0.1298 0.0152 97 ALA A C 317 O O . ALA A 62 ? 0.5650 0.3728 0.4361 -0.0903 0.1255 0.0183 97 ALA A O 318 C CB . ALA A 62 ? 0.6327 0.4361 0.5012 -0.1171 0.1323 0.0070 97 ALA A CB 319 N N . ARG A 63 ? 0.6128 0.3861 0.4704 -0.0924 0.1355 0.0180 98 ARG A N 320 C CA . ARG A 63 ? 0.6111 0.3754 0.4650 -0.0813 0.1371 0.0258 98 ARG A CA 321 C C . ARG A 63 ? 0.5883 0.3631 0.4484 -0.0706 0.1307 0.0276 98 ARG A C 322 O O . ARG A 63 ? 0.5933 0.3656 0.4522 -0.0611 0.1304 0.0343 98 ARG A O 323 C CB . ARG A 63 ? 0.6410 0.4063 0.4923 -0.0807 0.1389 0.0315 98 ARG A CB 324 C CG . ARG A 63 ? 0.6595 0.4141 0.5045 -0.0915 0.1457 0.0299 98 ARG A CG 325 C CD . ARG A 63 ? 0.6948 0.4452 0.5348 -0.0900 0.1491 0.0367 98 ARG A CD 326 N NE . ARG A 63 ? 0.7373 0.4686 0.5690 -0.0819 0.1540 0.0440 98 ARG A NE 327 C CZ . ARG A 63 ? 0.7763 0.5014 0.6021 -0.0781 0.1570 0.0514 98 ARG A CZ 328 N NH1 . ARG A 63 ? 0.7828 0.5188 0.6097 -0.0819 0.1560 0.0525 98 ARG A NH1 329 N NH2 . ARG A 63 ? 0.8064 0.5144 0.6254 -0.0701 0.1613 0.0583 98 ARG A NH2 330 N N . GLY A 64 ? 0.5611 0.3472 0.4277 -0.0723 0.1256 0.0218 99 GLY A N 331 C CA . GLY A 64 ? 0.5506 0.3454 0.4228 -0.0634 0.1201 0.0228 99 GLY A CA 332 C C . GLY A 64 ? 0.5287 0.3407 0.4071 -0.0575 0.1138 0.0263 99 GLY A C 333 O O . GLY A 64 ? 0.5263 0.3471 0.4062 -0.0614 0.1127 0.0261 99 GLY A O 334 N N . TRP A 65 ? 0.4973 0.3135 0.3789 -0.0482 0.1101 0.0294 100 TRP A N 335 C CA . TRP A 65 ? 0.4748 0.3086 0.3627 -0.0433 0.1031 0.0311 100 TRP A CA 336 C C . TRP A 65 ? 0.4797 0.3118 0.3650 -0.0348 0.1028 0.0391 100 TRP A C 337 O O . TRP A 65 ? 0.4658 0.3113 0.3555 -0.0303 0.0970 0.0407 100 TRP A O 338 C CB . TRP A 65 ? 0.4720 0.3163 0.3669 -0.0406 0.0975 0.0275 100 TRP A CB 339 C CG . TRP A 65 ? 0.4877 0.3325 0.3842 -0.0483 0.0978 0.0205 100 TRP A CG 340 C CD1 . TRP A 65 ? 0.5006 0.3345 0.3943 -0.0497 0.1009 0.0177 100 TRP A CD1 341 C CD2 . TRP A 65 ? 0.4896 0.3468 0.3906 -0.0556 0.0949 0.0153 100 TRP A CD2 342 N NE1 . TRP A 65 ? 0.5172 0.3561 0.4128 -0.0580 0.0997 0.0112 100 TRP A NE1 343 C CE2 . TRP A 65 ? 0.4985 0.3521 0.3992 -0.0616 0.0959 0.0098 100 TRP A CE2 344 C CE3 . TRP A 65 ? 0.4955 0.3665 0.4009 -0.0576 0.0917 0.0150 100 TRP A CE3 345 C CZ2 . TRP A 65 ? 0.5076 0.3723 0.4127 -0.0694 0.0933 0.0045 100 TRP A CZ2 346 C CZ3 . TRP A 65 ? 0.4930 0.3745 0.4032 -0.0648 0.0898 0.0096 100 TRP A CZ3 347 C CH2 . TRP A 65 ? 0.5072 0.3862 0.4176 -0.0706 0.0903 0.0047 100 TRP A CH2 348 N N . GLU A 66 ? 0.4931 0.3089 0.3710 -0.0328 0.1090 0.0442 101 GLU A N 349 C CA . GLU A 66 ? 0.5086 0.3222 0.3837 -0.0244 0.1090 0.0527 101 GLU A CA 350 C C . GLU A 66 ? 0.5359 0.3396 0.4031 -0.0268 0.1142 0.0571 101 GLU A C 351 O O . GLU A 66 ? 0.5485 0.3362 0.4098 -0.0313 0.1211 0.0564 101 GLU A O 352 C CB . GLU A 66 ? 0.5461 0.3490 0.4204 -0.0168 0.1116 0.0564 101 GLU A CB 353 C CG . GLU A 66 ? 0.5544 0.3689 0.4366 -0.0125 0.1059 0.0540 101 GLU A CG 354 C CD . GLU A 66 ? 0.5855 0.3893 0.4675 -0.0058 0.1094 0.0567 101 GLU A CD 355 O OE1 . GLU A 66 ? 0.6497 0.4360 0.5253 -0.0039 0.1166 0.0605 101 GLU A OE1 356 O OE2 . GLU A 66 ? 0.6272 0.4400 0.5156 -0.0023 0.1053 0.0550 101 GLU A OE2 357 N N . CYS A 67 ? 0.5299 0.3423 0.3962 -0.0239 0.1111 0.0618 102 CYS A N 358 C CA . CYS A 67 ? 0.5707 0.3735 0.4287 -0.0242 0.1158 0.0677 102 CYS A CA 359 C C . CYS A 67 ? 0.5807 0.3665 0.4335 -0.0172 0.1209 0.0749 102 CYS A C 360 O O . CYS A 67 ? 0.5595 0.3467 0.4158 -0.0093 0.1186 0.0777 102 CYS A O 361 C CB . CYS A 67 ? 0.5818 0.3977 0.4391 -0.0219 0.1110 0.0717 102 CYS A CB 362 S SG . CYS A 67 ? 0.5921 0.4241 0.4533 -0.0305 0.1078 0.0643 102 CYS A SG 363 N N . THR A 68 ? 0.6064 0.3757 0.4509 -0.0202 0.1282 0.0778 103 THR A N 364 C CA . THR A 68 ? 0.6352 0.3876 0.4735 -0.0131 0.1338 0.0859 103 THR A CA 365 C C . THR A 68 ? 0.6520 0.4025 0.4831 -0.0126 0.1353 0.0931 103 THR A C 366 O O . THR A 68 ? 0.6494 0.4072 0.4795 -0.0197 0.1343 0.0900 103 THR A O 367 C CB . THR A 68 ? 0.6501 0.3812 0.4835 -0.0176 0.1424 0.0828 103 THR A CB 368 O OG1 . THR A 68 ? 0.6610 0.3879 0.4903 -0.0289 0.1461 0.0780 103 THR A OG1 369 C CG2 . THR A 68 ? 0.6599 0.3936 0.4996 -0.0182 0.1407 0.0756 103 THR A CG2 370 N N . LYS A 69 ? 0.6860 0.4269 0.5123 -0.0039 0.1379 0.1028 104 LYS A N 371 C CA . LYS A 69 ? 0.7169 0.4571 0.5361 -0.0018 0.1384 0.1110 104 LYS A CA 372 C C . LYS A 69 ? 0.7071 0.4369 0.5185 -0.0114 0.1447 0.1092 104 LYS A C 373 O O . LYS A 69 ? 0.6839 0.4215 0.4919 -0.0141 0.1428 0.1111 104 LYS A O 374 C CB . LYS A 69 ? 0.7636 0.4929 0.5788 0.0092 0.1412 0.1222 104 LYS A CB 375 C CG . LYS A 69 ? 0.8407 0.5720 0.6490 0.0132 0.1401 0.1321 104 LYS A CG 376 C CD . LYS A 69 ? 0.8884 0.6436 0.7010 0.0154 0.1300 0.1329 104 LYS A CD 377 C CE . LYS A 69 ? 0.9321 0.6895 0.7359 0.0156 0.1294 0.1403 104 LYS A CE 378 N NZ . LYS A 69 ? 0.9239 0.7031 0.7303 0.0133 0.1207 0.1374 104 LYS A NZ 379 N N . ASP A 70 ? 0.7097 0.4220 0.5180 -0.0170 0.1522 0.1052 105 ASP A N 380 C CA . ASP A 70 ? 0.7274 0.4290 0.5287 -0.0273 0.1588 0.1028 105 ASP A CA 381 C C . ASP A 70 ? 0.6964 0.4147 0.5022 -0.0371 0.1550 0.0949 105 ASP A C 382 O O . ASP A 70 ? 0.6902 0.4047 0.4907 -0.0444 0.1591 0.0948 105 ASP A O 383 C CB . ASP A 70 ? 0.7603 0.4402 0.5577 -0.0321 0.1673 0.0991 105 ASP A CB 384 C CG . ASP A 70 ? 0.7743 0.4605 0.5795 -0.0366 0.1646 0.0890 105 ASP A CG 385 O OD1 . ASP A 70 ? 0.7756 0.4672 0.5866 -0.0288 0.1606 0.0893 105 ASP A OD1 386 O OD2 . ASP A 70 ? 0.8106 0.4971 0.6162 -0.0479 0.1664 0.0812 105 ASP A OD2 387 N N . ARG A 71 ? 0.6630 0.3992 0.4786 -0.0372 0.1477 0.0885 106 ARG A N 388 C CA . ARG A 71 ? 0.6402 0.3938 0.4613 -0.0451 0.1437 0.0813 106 ARG A CA 389 C C . ARG A 71 ? 0.6275 0.3971 0.4488 -0.0422 0.1384 0.0846 106 ARG A C 390 O O . ARG A 71 ? 0.6048 0.3868 0.4292 -0.0486 0.1366 0.0796 106 ARG A O 391 C CB . ARG A 71 ? 0.6047 0.3699 0.4359 -0.0464 0.1385 0.0730 106 ARG A CB 392 C CG . ARG A 71 ? 0.6241 0.3765 0.4552 -0.0525 0.1435 0.0674 106 ARG A CG 393 C CD . ARG A 71 ? 0.5955 0.3613 0.4362 -0.0550 0.1380 0.0591 106 ARG A CD 394 N NE . ARG A 71 ? 0.5641 0.3481 0.4106 -0.0613 0.1339 0.0540 106 ARG A NE 395 C CZ . ARG A 71 ? 0.5488 0.3471 0.4042 -0.0641 0.1288 0.0471 106 ARG A CZ 396 N NH1 . ARG A 71 ? 0.5397 0.3362 0.3984 -0.0618 0.1269 0.0440 106 ARG A NH1 397 N NH2 . ARG A 71 ? 0.5283 0.3425 0.3889 -0.0689 0.1258 0.0434 106 ARG A NH2 398 N N . CYS A 72 ? 0.6236 0.3934 0.4415 -0.0329 0.1358 0.0928 107 CYS A N 399 C CA . CYS A 72 ? 0.6182 0.4036 0.4357 -0.0303 0.1300 0.0955 107 CYS A CA 400 C C . CYS A 72 ? 0.6328 0.4172 0.4435 -0.0368 0.1340 0.0964 107 CYS A C 401 O O . CYS A 72 ? 0.6491 0.4179 0.4515 -0.0385 0.1408 0.1012 107 CYS A O 402 C CB . CYS A 72 ? 0.6312 0.4166 0.4457 -0.0196 0.1267 0.1047 107 CYS A CB 403 S SG . CYS A 72 ? 0.6582 0.4487 0.4822 -0.0116 0.1214 0.1037 107 CYS A SG 404 N N . GLY A 73 ? 0.6125 0.4130 0.4268 -0.0409 0.1303 0.0914 108 GLY A N 405 C CA . GLY A 73 ? 0.6273 0.4290 0.4362 -0.0475 0.1341 0.0913 108 GLY A CA 406 C C . GLY A 73 ? 0.6266 0.4208 0.4363 -0.0574 0.1410 0.0863 108 GLY A C 407 O O . GLY A 73 ? 0.6457 0.4381 0.4502 -0.0630 0.1457 0.0872 108 GLY A O 408 N N . GLU A 74 ? 0.6091 0.3993 0.4251 -0.0600 0.1417 0.0809 109 GLU A N 409 C CA . GLU A 74 ? 0.6219 0.4073 0.4397 -0.0703 0.1472 0.0751 109 GLU A CA 410 C C . GLU A 74 ? 0.6409 0.4423 0.4636 -0.0772 0.1464 0.0699 109 GLU A C 411 O O . GLU A 74 ? 0.6041 0.4219 0.4316 -0.0740 0.1406 0.0681 109 GLU A O 412 C CB . GLU A 74 ? 0.6281 0.4122 0.4533 -0.0719 0.1457 0.0687 109 GLU A CB 413 C CG . GLU A 74 ? 0.5924 0.3964 0.4286 -0.0700 0.1377 0.0628 109 GLU A CG 414 C CD . GLU A 74 ? 0.5778 0.3807 0.4203 -0.0706 0.1358 0.0572 109 GLU A CD 415 O OE1 . GLU A 74 ? 0.5801 0.3661 0.4182 -0.0718 0.1406 0.0580 109 GLU A OE1 416 O OE2 . GLU A 74 ? 0.5520 0.3706 0.4035 -0.0701 0.1297 0.0521 109 GLU A OE2 417 N N . VAL A 75 ? 0.6828 0.4793 0.5044 -0.0868 0.1527 0.0675 110 VAL A N 418 C CA . VAL A 75 ? 0.7012 0.5136 0.5303 -0.0943 0.1524 0.0613 110 VAL A CA 419 C C . VAL A 75 ? 0.6873 0.5089 0.5273 -0.0957 0.1477 0.0539 110 VAL A C 420 O O . VAL A 75 ? 0.6693 0.4800 0.5091 -0.0968 0.1488 0.0525 110 VAL A O 421 C CB . VAL A 75 ? 0.7694 0.5743 0.5946 -0.1048 0.1606 0.0611 110 VAL A CB 422 C CG1 . VAL A 75 ? 0.7762 0.5994 0.6113 -0.1127 0.1603 0.0544 110 VAL A CG1 423 C CG2 . VAL A 75 ? 0.7905 0.5864 0.6042 -0.1030 0.1652 0.0688 110 VAL A CG2 424 N N . ARG A 76 ? 0.6722 0.5132 0.5211 -0.0951 0.1426 0.0496 111 ARG A N 425 C CA . ARG A 76 ? 0.6521 0.5040 0.5119 -0.0962 0.1377 0.0429 111 ARG A CA 426 C C . ARG A 76 ? 0.6509 0.4988 0.5135 -0.1064 0.1417 0.0384 111 ARG A C 427 O O . ARG A 76 ? 0.6620 0.5120 0.5245 -0.1144 0.1465 0.0376 111 ARG A O 428 C CB . ARG A 76 ? 0.6097 0.4826 0.4780 -0.0952 0.1333 0.0394 111 ARG A CB 429 C CG . ARG A 76 ? 0.5866 0.4729 0.4668 -0.0977 0.1290 0.0326 111 ARG A CG 430 C CD . ARG A 76 ? 0.5662 0.4712 0.4538 -0.0952 0.1253 0.0301 111 ARG A CD 431 N NE . ARG A 76 ? 0.5365 0.4427 0.4214 -0.0857 0.1204 0.0326 111 ARG A NE 432 C CZ . ARG A 76 ? 0.5429 0.4535 0.4325 -0.0804 0.1143 0.0306 111 ARG A CZ 433 N NH1 . ARG A 76 ? 0.5467 0.4614 0.4441 -0.0831 0.1120 0.0260 111 ARG A NH1 434 N NH2 . ARG A 76 ? 0.5372 0.4486 0.4236 -0.0727 0.1102 0.0332 111 ARG A NH2 435 N N . ASN A 77 ? 0.6300 0.4719 0.4944 -0.1065 0.1399 0.0356 112 ASN A N 436 C CA . ASN A 77 ? 0.6454 0.4871 0.5138 -0.1162 0.1418 0.0299 112 ASN A CA 437 C C . ASN A 77 ? 0.6492 0.5076 0.5286 -0.1149 0.1347 0.0244 112 ASN A C 438 O O . ASN A 77 ? 0.5971 0.4535 0.4772 -0.1081 0.1304 0.0242 112 ASN A O 439 C CB . ASN A 77 ? 0.6613 0.4808 0.5213 -0.1181 0.1462 0.0308 112 ASN A CB 440 C CG . ASN A 77 ? 0.6955 0.5127 0.5573 -0.1300 0.1491 0.0249 112 ASN A CG 441 O OD1 . ASN A 77 ? 0.6858 0.5177 0.5566 -0.1337 0.1447 0.0193 112 ASN A OD1 442 N ND2 . ASN A 77 ? 0.7659 0.5643 0.6185 -0.1364 0.1566 0.0263 112 ASN A ND2 443 N N . GLU A 78 ? 0.6311 0.5061 0.5193 -0.1215 0.1337 0.0201 113 GLU A N 444 C CA . GLU A 78 ? 0.6447 0.5375 0.5440 -0.1198 0.1269 0.0156 113 GLU A CA 445 C C . GLU A 78 ? 0.6129 0.5014 0.5136 -0.1218 0.1242 0.0116 113 GLU A C 446 O O . GLU A 78 ? 0.6194 0.5187 0.5269 -0.1175 0.1182 0.0092 113 GLU A O 447 C CB . GLU A 78 ? 0.6709 0.5828 0.5799 -0.1263 0.1270 0.0126 113 GLU A CB 448 C CG . GLU A 78 ? 0.6970 0.6163 0.6060 -0.1235 0.1290 0.0157 113 GLU A CG 449 C CD . GLU A 78 ? 0.7368 0.6661 0.6492 -0.1133 0.1236 0.0165 113 GLU A CD 450 O OE1 . GLU A 78 ? 0.7395 0.6671 0.6524 -0.1069 0.1185 0.0159 113 GLU A OE1 451 O OE2 . GLU A 78 ? 0.7542 0.6931 0.6686 -0.1119 0.1249 0.0175 113 GLU A OE2 452 N N . GLU A 79 ? 0.6263 0.4983 0.5199 -0.1280 0.1290 0.0110 114 GLU A N 453 C CA . GLU A 79 ? 0.6304 0.4959 0.5233 -0.1299 0.1272 0.0071 114 GLU A CA 454 C C . GLU A 79 ? 0.5616 0.4176 0.4507 -0.1193 0.1246 0.0094 114 GLU A C 455 O O . GLU A 79 ? 0.5597 0.4135 0.4496 -0.1194 0.1222 0.0060 114 GLU A O 456 C CB . GLU A 79 ? 0.7004 0.5490 0.5853 -0.1401 0.1338 0.0055 114 GLU A CB 457 C CG . GLU A 79 ? 0.7637 0.6230 0.6534 -0.1525 0.1357 0.0021 114 GLU A CG 458 C CD . GLU A 79 ? 0.8310 0.6719 0.7114 -0.1631 0.1431 0.0010 114 GLU A CD 459 O OE1 . GLU A 79 ? 0.9016 0.7213 0.7722 -0.1612 0.1463 0.0016 114 GLU A OE1 460 O OE2 . GLU A 79 ? 0.9317 0.7791 0.8145 -0.1734 0.1460 -0.0005 114 GLU A OE2 461 N N . ASN A 80 ? 0.5156 0.3664 0.4005 -0.1105 0.1252 0.0151 115 ASN A N 462 C CA . ASN A 80 ? 0.5120 0.3545 0.3937 -0.1004 0.1230 0.0181 115 ASN A CA 463 C C . ASN A 80 ? 0.4795 0.3384 0.3701 -0.0943 0.1152 0.0160 115 ASN A C 464 O O . ASN A 80 ? 0.4522 0.3280 0.3498 -0.0944 0.1116 0.0147 115 ASN A O 465 C CB . ASN A 80 ? 0.5224 0.3558 0.3970 -0.0934 0.1257 0.0254 115 ASN A CB 466 C CG . ASN A 80 ? 0.5560 0.3684 0.4203 -0.0974 0.1338 0.0284 115 ASN A CG 467 O OD1 . ASN A 80 ? 0.5687 0.3680 0.4293 -0.1019 0.1374 0.0258 115 ASN A OD1 468 N ND2 . ASN A 80 ? 0.5667 0.3748 0.4255 -0.0956 0.1371 0.0340 115 ASN A ND2 469 N N . ALA A 81 ? 0.4775 0.3304 0.3672 -0.0891 0.1131 0.0156 116 ALA A N 470 C CA . ALA A 81 ? 0.4713 0.3375 0.3686 -0.0836 0.1060 0.0136 116 ALA A CA 471 C C . ALA A 81 ? 0.4577 0.3332 0.3572 -0.0754 0.1022 0.0175 116 ALA A C 472 O O . ALA A 81 ? 0.4395 0.3306 0.3464 -0.0738 0.0970 0.0153 116 ALA A O 473 C CB . ALA A 81 ? 0.4698 0.3256 0.3645 -0.0797 0.1057 0.0131 116 ALA A CB 474 N N . CYS A 82 ? 0.4550 0.3204 0.3477 -0.0703 0.1049 0.0234 117 CYS A N 475 C CA . CYS A 82 ? 0.4551 0.3280 0.3478 -0.0638 0.1020 0.0275 117 CYS A CA 476 C C . CYS A 82 ? 0.4565 0.3185 0.3405 -0.0639 0.1073 0.0332 117 CYS A C 477 O O . CYS A 82 ? 0.4586 0.3065 0.3371 -0.0683 0.1133 0.0340 117 CYS A O 478 C CB . CYS A 82 ? 0.4641 0.3392 0.3585 -0.0547 0.0970 0.0297 117 CYS A CB 479 S SG . CYS A 82 ? 0.4838 0.3408 0.3726 -0.0498 0.1002 0.0334 117 CYS A SG 480 N N . HIS A 83 ? 0.4331 0.3011 0.3154 -0.0594 0.1054 0.0371 118 HIS A N 481 C CA . HIS A 83 ? 0.4664 0.3276 0.3409 -0.0605 0.1101 0.0419 118 HIS A CA 482 C C . HIS A 83 ? 0.4672 0.3232 0.3352 -0.0523 0.1091 0.0494 118 HIS A C 483 O O . HIS A 83 ? 0.4580 0.3212 0.3287 -0.0457 0.1035 0.0504 118 HIS A O 484 C CB . HIS A 83 ? 0.4525 0.3265 0.3299 -0.0653 0.1101 0.0393 118 HIS A CB 485 C CG . HIS A 83 ? 0.4617 0.3421 0.3462 -0.0733 0.1111 0.0328 118 HIS A CG 486 N ND1 . HIS A 83 ? 0.4786 0.3507 0.3606 -0.0814 0.1170 0.0318 118 HIS A ND1 487 C CD2 . HIS A 83 ? 0.4704 0.3642 0.3643 -0.0744 0.1066 0.0274 118 HIS A CD2 488 C CE1 . HIS A 83 ? 0.4816 0.3633 0.3715 -0.0876 0.1158 0.0259 118 HIS A CE1 489 N NE2 . HIS A 83 ? 0.4749 0.3699 0.3722 -0.0831 0.1096 0.0233 118 HIS A NE2 490 N N . CYS A 84 ? 0.4759 0.3194 0.3352 -0.0530 0.1146 0.0547 119 CYS A N 491 C CA . CYS A 84 ? 0.4894 0.3274 0.3417 -0.0458 0.1144 0.0628 119 CYS A CA 492 C C . CYS A 84 ? 0.4853 0.3234 0.3306 -0.0486 0.1175 0.0662 119 CYS A C 493 O O . CYS A 84 ? 0.4883 0.3180 0.3253 -0.0448 0.1195 0.0736 119 CYS A O 494 C CB . CYS A 84 ? 0.5334 0.3532 0.3809 -0.0426 0.1188 0.0673 119 CYS A CB 495 S SG . CYS A 84 ? 0.5772 0.3946 0.4320 -0.0417 0.1173 0.0618 119 CYS A SG 496 N N . SER A 85 ? 0.4768 0.3254 0.3258 -0.0549 0.1177 0.0609 120 SER A N 497 C CA . SER A 85 ? 0.4965 0.3463 0.3397 -0.0588 0.1214 0.0628 120 SER A CA 498 C C . SER A 85 ? 0.4988 0.3610 0.3406 -0.0544 0.1165 0.0643 120 SER A C 499 O O . SER A 85 ? 0.4651 0.3378 0.3127 -0.0505 0.1102 0.0615 120 SER A O 500 C CB . SER A 85 ? 0.5083 0.3640 0.3572 -0.0681 0.1246 0.0563 120 SER A CB 501 O OG . SER A 85 ? 0.5092 0.3789 0.3688 -0.0684 0.1195 0.0496 120 SER A OG 502 N N . GLU A 86 ? 0.4995 0.3602 0.3330 -0.0556 0.1195 0.0683 121 GLU A N 503 C CA . GLU A 86 ? 0.5233 0.3944 0.3534 -0.0522 0.1154 0.0696 121 GLU A CA 504 C C . GLU A 86 ? 0.5097 0.3963 0.3477 -0.0548 0.1128 0.0620 121 GLU A C 505 O O . GLU A 86 ? 0.5241 0.4194 0.3604 -0.0516 0.1086 0.0617 121 GLU A O 506 C CB . GLU A 86 ? 0.5791 0.4450 0.3976 -0.0536 0.1198 0.0753 121 GLU A CB 507 C CG . GLU A 86 ? 0.6340 0.4866 0.4430 -0.0488 0.1210 0.0845 121 GLU A CG 508 C CD . GLU A 86 ? 0.6478 0.5050 0.4549 -0.0406 0.1138 0.0888 121 GLU A CD 509 O OE1 . GLU A 86 ? 0.6598 0.5302 0.4708 -0.0390 0.1080 0.0850 121 GLU A OE1 510 O OE2 . GLU A 86 ? 0.7133 0.5607 0.5149 -0.0357 0.1143 0.0965 121 GLU A OE2 511 N N . ASP A 87 ? 0.4882 0.3782 0.3346 -0.0605 0.1154 0.0561 122 ASP A N 512 C CA . ASP A 87 ? 0.4703 0.3750 0.3253 -0.0622 0.1131 0.0493 122 ASP A CA 513 C C . ASP A 87 ? 0.4680 0.3792 0.3327 -0.0592 0.1071 0.0449 122 ASP A C 514 O O . ASP A 87 ? 0.4640 0.3871 0.3364 -0.0600 0.1051 0.0396 122 ASP A O 515 C CB . ASP A 87 ? 0.4872 0.3952 0.3468 -0.0700 0.1188 0.0457 122 ASP A CB 516 C CG . ASP A 87 ? 0.5045 0.4066 0.3695 -0.0747 0.1209 0.0437 122 ASP A CG 517 O OD1 . ASP A 87 ? 0.5090 0.4055 0.3758 -0.0717 0.1177 0.0437 122 ASP A OD1 518 O OD2 . ASP A 87 ? 0.5387 0.4418 0.4060 -0.0818 0.1260 0.0418 122 ASP A OD2 519 N N . CYS A 88 ? 0.4712 0.3748 0.3356 -0.0555 0.1046 0.0473 123 CYS A N 520 C CA . CYS A 88 ? 0.4560 0.3640 0.3296 -0.0542 0.1004 0.0429 123 CYS A CA 521 C C . CYS A 88 ? 0.4742 0.3937 0.3517 -0.0495 0.0940 0.0405 123 CYS A C 522 O O . CYS A 88 ? 0.4765 0.4043 0.3628 -0.0502 0.0913 0.0352 123 CYS A O 523 C CB . CYS A 88 ? 0.4511 0.3468 0.3233 -0.0518 0.1006 0.0458 123 CYS A CB 524 S SG . CYS A 88 ? 0.4456 0.3355 0.3111 -0.0429 0.0971 0.0532 123 CYS A SG 525 N N . LEU A 89 ? 0.5072 0.4273 0.3778 -0.0451 0.0915 0.0444 124 LEU A N 526 C CA . LEU A 89 ? 0.5350 0.4658 0.4082 -0.0419 0.0860 0.0416 124 LEU A CA 527 C C . LEU A 89 ? 0.5385 0.4789 0.4159 -0.0454 0.0877 0.0360 124 LEU A C 528 O O . LEU A 89 ? 0.5538 0.5023 0.4386 -0.0445 0.0844 0.0314 124 LEU A O 529 C CB . LEU A 89 ? 0.5134 0.4436 0.3774 -0.0377 0.0831 0.0466 124 LEU A CB 530 C CG . LEU A 89 ? 0.5148 0.4383 0.3762 -0.0328 0.0804 0.0525 124 LEU A CG 531 C CD1 . LEU A 89 ? 0.5170 0.4394 0.3680 -0.0298 0.0788 0.0590 124 LEU A CD1 532 C CD2 . LEU A 89 ? 0.5257 0.4544 0.3949 -0.0293 0.0747 0.0500 124 LEU A CD2 533 N N . SER A 90 ? 0.5667 0.5062 0.4400 -0.0494 0.0932 0.0367 125 SER A N 534 C CA . SER A 90 ? 0.5726 0.5216 0.4506 -0.0525 0.0957 0.0318 125 SER A CA 535 C C . SER A 90 ? 0.5842 0.5396 0.4747 -0.0551 0.0956 0.0268 125 SER A C 536 O O . SER A 90 ? 0.5804 0.5457 0.4776 -0.0545 0.0943 0.0224 125 SER A O 537 C CB . SER A 90 ? 0.5755 0.5221 0.4477 -0.0568 0.1024 0.0337 125 SER A CB 538 O OG . SER A 90 ? 0.5895 0.5314 0.4647 -0.0618 0.1068 0.0341 125 SER A OG 539 N N . ARG A 91 ? 0.6016 0.5508 0.4945 -0.0581 0.0972 0.0275 126 ARG A N 540 C CA . ARG A 91 ? 0.5766 0.5313 0.4803 -0.0615 0.0970 0.0232 126 ARG A CA 541 C C . ARG A 91 ? 0.5393 0.4961 0.4485 -0.0577 0.0909 0.0211 126 ARG A C 542 O O . ARG A 91 ? 0.5361 0.4986 0.4540 -0.0599 0.0898 0.0174 126 ARG A O 543 C CB . ARG A 91 ? 0.6162 0.5623 0.5186 -0.0673 0.1015 0.0246 126 ARG A CB 544 C CG . ARG A 91 ? 0.6489 0.5939 0.5475 -0.0726 0.1081 0.0261 126 ARG A CG 545 C CD . ARG A 91 ? 0.7035 0.6613 0.6119 -0.0777 0.1104 0.0217 126 ARG A CD 546 N NE . ARG A 91 ? 0.7536 0.7144 0.6707 -0.0816 0.1088 0.0184 126 ARG A NE 547 C CZ . ARG A 91 ? 0.7878 0.7435 0.7052 -0.0887 0.1124 0.0182 126 ARG A CZ 548 N NH1 . ARG A 91 ? 0.8004 0.7469 0.7103 -0.0930 0.1183 0.0213 126 ARG A NH1 549 N NH2 . ARG A 91 ? 0.7751 0.7346 0.6999 -0.0922 0.1101 0.0147 126 ARG A NH2 550 N N . GLY A 92 ? 0.5382 0.4908 0.4424 -0.0522 0.0871 0.0237 127 GLY A N 551 C CA . GLY A 92 ? 0.4775 0.4321 0.3865 -0.0483 0.0815 0.0221 127 GLY A CA 552 C C . GLY A 92 ? 0.5037 0.4510 0.4149 -0.0496 0.0815 0.0222 127 GLY A C 553 O O . GLY A 92 ? 0.4805 0.4318 0.3984 -0.0490 0.0782 0.0191 127 GLY A O 554 N N . ASP A 93 ? 0.4474 0.3833 0.3524 -0.0513 0.0854 0.0259 128 ASP A N 555 C CA . ASP A 93 ? 0.4229 0.3503 0.3290 -0.0536 0.0869 0.0255 128 ASP A CA 556 C C . ASP A 93 ? 0.4092 0.3218 0.3071 -0.0513 0.0896 0.0310 128 ASP A C 557 O O . ASP A 93 ? 0.3998 0.3025 0.2962 -0.0548 0.0933 0.0309 128 ASP A O 558 C CB . ASP A 93 ? 0.4436 0.3729 0.3535 -0.0614 0.0908 0.0220 128 ASP A CB 559 C CG . ASP A 93 ? 0.4691 0.3954 0.3738 -0.0655 0.0964 0.0244 128 ASP A CG 560 O OD1 . ASP A 93 ? 0.4934 0.4135 0.3900 -0.0624 0.0978 0.0291 128 ASP A OD1 561 O OD2 . ASP A 93 ? 0.4916 0.4219 0.4001 -0.0723 0.0996 0.0216 128 ASP A OD2 562 N N . CYS A 94 ? 0.3920 0.3028 0.2846 -0.0454 0.0876 0.0358 129 CYS A N 563 C CA . CYS A 94 ? 0.4140 0.3118 0.3000 -0.0418 0.0896 0.0417 129 CYS A CA 564 C C . CYS A 94 ? 0.4104 0.3042 0.3003 -0.0390 0.0877 0.0407 129 CYS A C 565 O O . CYS A 94 ? 0.3878 0.2906 0.2843 -0.0374 0.0830 0.0370 129 CYS A O 566 C CB . CYS A 94 ? 0.4187 0.3182 0.2993 -0.0356 0.0866 0.0474 129 CYS A CB 567 S SG . CYS A 94 ? 0.4433 0.3482 0.3174 -0.0374 0.0877 0.0491 129 CYS A SG 568 N N . CYS A 95 ? 0.4390 0.3188 0.3246 -0.0381 0.0918 0.0440 130 CYS A N 569 C CA . CYS A 95 ? 0.4425 0.3175 0.3306 -0.0339 0.0905 0.0442 130 CYS A CA 570 C C . CYS A 95 ? 0.4241 0.3066 0.3134 -0.0261 0.0849 0.0480 130 CYS A C 571 O O . CYS A 95 ? 0.4206 0.3054 0.3053 -0.0235 0.0839 0.0527 130 CYS A O 572 C CB . CYS A 95 ? 0.4608 0.3179 0.3430 -0.0334 0.0967 0.0478 130 CYS A CB 573 S SG . CYS A 95 ? 0.4917 0.3375 0.3706 -0.0436 0.1040 0.0436 130 CYS A SG 574 N N . THR A 96 ? 0.4024 0.2890 0.2973 -0.0227 0.0811 0.0462 131 THR A N 575 C CA . THR A 96 ? 0.3905 0.2866 0.2876 -0.0165 0.0753 0.0489 131 THR A CA 576 C C . THR A 96 ? 0.3960 0.2866 0.2882 -0.0101 0.0758 0.0573 131 THR A C 577 O O . THR A 96 ? 0.4092 0.3085 0.3014 -0.0062 0.0711 0.0605 131 THR A O 578 C CB . THR A 96 ? 0.3684 0.2701 0.2729 -0.0144 0.0714 0.0454 131 THR A CB 579 O OG1 . THR A 96 ? 0.4019 0.2925 0.3062 -0.0124 0.0751 0.0466 131 THR A OG1 580 C CG2 . THR A 96 ? 0.3679 0.2773 0.2776 -0.0200 0.0697 0.0379 131 THR A CG2 581 N N . ASN A 97 ? 0.4183 0.2946 0.3062 -0.0090 0.0816 0.0610 132 ASN A N 582 C CA . ASN A 97 ? 0.4382 0.3085 0.3213 -0.0024 0.0828 0.0699 132 ASN A CA 583 C C . ASN A 97 ? 0.4591 0.3244 0.3338 -0.0042 0.0860 0.0744 132 ASN A C 584 O O . ASN A 97 ? 0.4931 0.3511 0.3628 0.0007 0.0881 0.0822 132 ASN A O 585 C CB . ASN A 97 ? 0.4566 0.3128 0.3394 0.0010 0.0880 0.0723 132 ASN A CB 586 C CG . ASN A 97 ? 0.4716 0.3122 0.3491 -0.0048 0.0956 0.0700 132 ASN A CG 587 O OD1 . ASN A 97 ? 0.4730 0.3157 0.3503 -0.0126 0.0964 0.0642 132 ASN A OD1 588 N ND2 . ASN A 97 ? 0.5033 0.3282 0.3769 -0.0012 0.1015 0.0744 132 ASN A ND2 589 N N . TYR A 98 ? 0.4626 0.3317 0.3358 -0.0111 0.0866 0.0697 133 TYR A N 590 C CA . TYR A 98 ? 0.4744 0.3386 0.3394 -0.0139 0.0902 0.0733 133 TYR A CA 591 C C . TYR A 98 ? 0.5056 0.3725 0.3648 -0.0080 0.0876 0.0817 133 TYR A C 592 O O . TYR A 98 ? 0.5268 0.3829 0.3791 -0.0057 0.0918 0.0886 133 TYR A O 593 C CB . TYR A 98 ? 0.4503 0.3225 0.3163 -0.0213 0.0901 0.0668 133 TYR A CB 594 C CG . TYR A 98 ? 0.4592 0.3301 0.3171 -0.0238 0.0928 0.0702 133 TYR A CG 595 C CD1 . TYR A 98 ? 0.4703 0.3271 0.3213 -0.0261 0.0997 0.0740 133 TYR A CD1 596 C CD2 . TYR A 98 ? 0.4484 0.3312 0.3049 -0.0242 0.0889 0.0694 133 TYR A CD2 597 C CE1 . TYR A 98 ? 0.4790 0.3345 0.3221 -0.0286 0.1024 0.0773 133 TYR A CE1 598 C CE2 . TYR A 98 ? 0.4635 0.3449 0.3117 -0.0266 0.0917 0.0725 133 TYR A CE2 599 C CZ . TYR A 98 ? 0.4822 0.3503 0.3241 -0.0287 0.0984 0.0765 133 TYR A CZ 600 O OH . TYR A 98 ? 0.4958 0.3625 0.3292 -0.0313 0.1014 0.0796 133 TYR A OH 601 N N . GLN A 99 ? 0.5124 0.3934 0.3740 -0.0058 0.0808 0.0813 134 GLN A N 602 C CA . GLN A 99 ? 0.5250 0.4105 0.3808 -0.0011 0.0774 0.0889 134 GLN A CA 603 C C . GLN A 99 ? 0.5212 0.4019 0.3775 0.0068 0.0772 0.0970 134 GLN A C 604 O O . GLN A 99 ? 0.5380 0.4158 0.3876 0.0105 0.0776 0.1053 134 GLN A O 605 C CB . GLN A 99 ? 0.5192 0.4207 0.3768 -0.0016 0.0702 0.0861 134 GLN A CB 606 C CG . GLN A 99 ? 0.5239 0.4295 0.3771 -0.0079 0.0711 0.0815 134 GLN A CG 607 C CD . GLN A 99 ? 0.5480 0.4675 0.4017 -0.0084 0.0646 0.0785 134 GLN A CD 608 O OE1 . GLN A 99 ? 0.5366 0.4635 0.3951 -0.0049 0.0591 0.0788 134 GLN A OE1 609 N NE2 . GLN A 99 ? 0.5503 0.4730 0.3986 -0.0129 0.0656 0.0757 134 GLN A NE2 610 N N . VAL A 100 ? 0.5184 0.3981 0.3825 0.0097 0.0768 0.0950 135 VAL A N 611 C CA . VAL A 100 ? 0.5403 0.4150 0.4061 0.0179 0.0775 0.1025 135 VAL A CA 612 C C . VAL A 100 ? 0.5717 0.4282 0.4306 0.0193 0.0855 0.1081 135 VAL A C 613 O O . VAL A 100 ? 0.6207 0.4737 0.4758 0.0258 0.0862 0.1176 135 VAL A O 614 C CB . VAL A 100 ? 0.5465 0.4225 0.4217 0.0200 0.0767 0.0981 135 VAL A CB 615 C CG1 . VAL A 100 ? 0.5600 0.4285 0.4369 0.0285 0.0794 0.1057 135 VAL A CG1 616 C CG2 . VAL A 100 ? 0.5491 0.4427 0.4309 0.0198 0.0687 0.0942 135 VAL A CG2 617 N N . VAL A 101 ? 0.5518 0.3969 0.4091 0.0132 0.0916 0.1025 136 VAL A N 618 C CA . VAL A 101 ? 0.5590 0.3850 0.4095 0.0134 0.0999 0.1067 136 VAL A CA 619 C C . VAL A 101 ? 0.5664 0.3893 0.4073 0.0110 0.1019 0.1115 136 VAL A C 620 O O . VAL A 101 ? 0.5807 0.3924 0.4151 0.0154 0.1060 0.1199 136 VAL A O 621 C CB . VAL A 101 ? 0.5573 0.3722 0.4090 0.0064 0.1056 0.0985 136 VAL A CB 622 C CG1 . VAL A 101 ? 0.5665 0.3606 0.4100 0.0050 0.1147 0.1021 136 VAL A CG1 623 C CG2 . VAL A 101 ? 0.5510 0.3670 0.4107 0.0092 0.1044 0.0945 136 VAL A CG2 624 N N . CYS A 102 ? 0.5502 0.3826 0.3900 0.0043 0.0994 0.1063 137 CYS A N 625 C CA . CYS A 102 ? 0.5752 0.4038 0.4056 0.0003 0.1025 0.1092 137 CYS A CA 626 C C . CYS A 102 ? 0.5822 0.4222 0.4078 0.0033 0.0970 0.1149 137 CYS A C 627 O O . CYS A 102 ? 0.5816 0.4163 0.3978 0.0020 0.1000 0.1199 137 CYS A O 628 C CB . CYS A 102 ? 0.5823 0.4128 0.4138 -0.0095 0.1048 0.1001 137 CYS A CB 629 S SG . CYS A 102 ? 0.6057 0.4224 0.4410 -0.0148 0.1115 0.0936 137 CYS A SG 630 N N . LYS A 103 ? 0.5745 0.4296 0.4054 0.0068 0.0892 0.1142 138 LYS A N 631 C CA . LYS A 103 ? 0.5756 0.4429 0.4015 0.0083 0.0833 0.1184 138 LYS A CA 632 C C . LYS A 103 ? 0.5744 0.4500 0.4031 0.0166 0.0772 0.1255 138 LYS A C 633 O O . LYS A 103 ? 0.6025 0.4910 0.4288 0.0171 0.0708 0.1273 138 LYS A O 634 C CB . LYS A 103 ? 0.5554 0.4357 0.3834 0.0021 0.0793 0.1095 138 LYS A CB 635 C CG . LYS A 103 ? 0.5735 0.4490 0.4001 -0.0059 0.0847 0.1025 138 LYS A CG 636 C CD . LYS A 103 ? 0.6114 0.4794 0.4267 -0.0085 0.0896 0.1075 138 LYS A CD 637 C CE . LYS A 103 ? 0.6245 0.4891 0.4398 -0.0167 0.0952 0.1004 138 LYS A CE 638 N NZ . LYS A 103 ? 0.6716 0.5301 0.4760 -0.0199 0.1001 0.1047 138 LYS A NZ 639 N N . GLY A 104 ? 0.5993 0.4677 0.4328 0.0229 0.0793 0.1297 139 GLY A N 640 C CA . GLY A 104 ? 0.6048 0.4809 0.4416 0.0315 0.0743 0.1378 139 GLY A CA 641 C C . GLY A 104 ? 0.6068 0.4999 0.4526 0.0323 0.0664 0.1336 139 GLY A C 642 O O . GLY A 104 ? 0.6021 0.5046 0.4510 0.0386 0.0614 0.1403 139 GLY A O 643 N N . GLU A 105 ? 0.5873 0.4844 0.4378 0.0261 0.0654 0.1230 140 GLU A N 644 C CA . GLU A 105 ? 0.5944 0.5066 0.4526 0.0259 0.0584 0.1183 140 GLU A CA 645 C C . GLU A 105 ? 0.5652 0.4763 0.4334 0.0313 0.0587 0.1186 140 GLU A C 646 O O . GLU A 105 ? 0.5632 0.4606 0.4324 0.0335 0.0652 0.1196 140 GLU A O 647 C CB . GLU A 105 ? 0.6293 0.5455 0.4887 0.0179 0.0576 0.1073 140 GLU A CB 648 C CG . GLU A 105 ? 0.6703 0.5979 0.5240 0.0141 0.0525 0.1060 140 GLU A CG 649 C CD . GLU A 105 ? 0.7180 0.6606 0.5772 0.0154 0.0446 0.1044 140 GLU A CD 650 O OE1 . GLU A 105 ? 0.6666 0.6138 0.5302 0.0215 0.0415 0.1106 140 GLU A OE1 651 O OE2 . GLU A 105 ? 0.7595 0.7090 0.6190 0.0103 0.0419 0.0970 140 GLU A OE2 652 N N . SER A 106 ? 0.5190 0.4443 0.3940 0.0332 0.0521 0.1177 141 SER A N 653 C CA . SER A 106 ? 0.4925 0.4191 0.3773 0.0382 0.0519 0.1179 141 SER A CA 654 C C . SER A 106 ? 0.4512 0.3784 0.3421 0.0330 0.0521 0.1070 141 SER A C 655 O O . SER A 106 ? 0.4385 0.3711 0.3277 0.0266 0.0495 0.1002 141 SER A O 656 C CB . SER A 106 ? 0.4857 0.4286 0.3750 0.0429 0.0444 0.1237 141 SER A CB 657 O OG . SER A 106 ? 0.4639 0.4199 0.3525 0.0372 0.0379 0.1182 141 SER A OG 658 N N . HIS A 107 ? 0.4357 0.3567 0.3331 0.0360 0.0555 0.1056 142 HIS A N 659 C CA . HIS A 107 ? 0.4095 0.3331 0.3135 0.0322 0.0546 0.0964 142 HIS A CA 660 C C . HIS A 107 ? 0.3787 0.3196 0.2880 0.0321 0.0467 0.0951 142 HIS A C 661 O O . HIS A 107 ? 0.3760 0.3257 0.2875 0.0373 0.0428 0.1020 142 HIS A O 662 C CB . HIS A 107 ? 0.4268 0.3415 0.3362 0.0363 0.0594 0.0963 142 HIS A CB 663 C CG . HIS A 107 ? 0.4537 0.3501 0.3581 0.0346 0.0677 0.0951 142 HIS A CG 664 N ND1 . HIS A 107 ? 0.4596 0.3501 0.3620 0.0269 0.0703 0.0868 142 HIS A ND1 665 C CD2 . HIS A 107 ? 0.4746 0.3571 0.3757 0.0394 0.0741 0.1012 142 HIS A CD2 666 C CE1 . HIS A 107 ? 0.4952 0.3692 0.3929 0.0263 0.0778 0.0875 142 HIS A CE1 667 N NE2 . HIS A 107 ? 0.4887 0.3566 0.3852 0.0339 0.0804 0.0961 142 HIS A NE2 668 N N . TRP A 108 ? 0.3791 0.3246 0.2906 0.0263 0.0444 0.0864 143 TRP A N 669 C CA . TRP A 108 ? 0.3540 0.3139 0.2702 0.0252 0.0375 0.0838 143 TRP A CA 670 C C . TRP A 108 ? 0.3485 0.3147 0.2730 0.0311 0.0355 0.0876 143 TRP A C 671 O O . TRP A 108 ? 0.3358 0.3145 0.2625 0.0327 0.0297 0.0910 143 TRP A O 672 C CB . TRP A 108 ? 0.3485 0.3094 0.2667 0.0190 0.0371 0.0739 143 TRP A CB 673 C CG . TRP A 108 ? 0.3229 0.2966 0.2457 0.0177 0.0307 0.0707 143 TRP A CG 674 C CD1 . TRP A 108 ? 0.3202 0.3029 0.2396 0.0146 0.0259 0.0696 143 TRP A CD1 675 C CD2 . TRP A 108 ? 0.3197 0.2976 0.2507 0.0191 0.0291 0.0682 143 TRP A CD2 676 N NE1 . TRP A 108 ? 0.3325 0.3245 0.2575 0.0137 0.0212 0.0665 143 TRP A NE1 677 C CE2 . TRP A 108 ? 0.3145 0.3041 0.2469 0.0166 0.0231 0.0658 143 TRP A CE2 678 C CE3 . TRP A 108 ? 0.3194 0.2919 0.2562 0.0220 0.0326 0.0677 143 TRP A CE3 679 C CZ2 . TRP A 108 ? 0.3110 0.3070 0.2506 0.0168 0.0203 0.0631 143 TRP A CZ2 680 C CZ3 . TRP A 108 ? 0.3132 0.2925 0.2571 0.0224 0.0298 0.0651 143 TRP A CZ3 681 C CH2 . TRP A 108 ? 0.3099 0.3011 0.2554 0.0199 0.0237 0.0630 143 TRP A CH2 682 N N . VAL A 109 ? 0.3529 0.3103 0.2816 0.0341 0.0404 0.0872 144 VAL A N 683 C CA . VAL A 109 ? 0.3667 0.3293 0.3037 0.0398 0.0395 0.0904 144 VAL A CA 684 C C . VAL A 109 ? 0.3932 0.3615 0.3313 0.0471 0.0381 0.1010 144 VAL A C 685 O O . VAL A 109 ? 0.3860 0.3655 0.3315 0.0510 0.0346 0.1044 144 VAL A O 686 C CB . VAL A 109 ? 0.3632 0.3135 0.3031 0.0413 0.0462 0.0873 144 VAL A CB 687 C CG1 . VAL A 109 ? 0.3870 0.3224 0.3222 0.0456 0.0532 0.0928 144 VAL A CG1 688 C CG2 . VAL A 109 ? 0.3657 0.3232 0.3147 0.0453 0.0447 0.0877 144 VAL A CG2 689 N N . ASP A 110 ? 0.4043 0.3656 0.3353 0.0487 0.0406 0.1066 145 ASP A N 690 C CA . ASP A 110 ? 0.4579 0.4243 0.3892 0.0559 0.0392 0.1176 145 ASP A CA 691 C C . ASP A 110 ? 0.4622 0.4450 0.3915 0.0539 0.0309 0.1207 145 ASP A C 692 O O . ASP A 110 ? 0.5038 0.4948 0.4346 0.0594 0.0282 0.1298 145 ASP A O 693 C CB . ASP A 110 ? 0.4834 0.4343 0.4074 0.0589 0.0459 0.1230 145 ASP A CB 694 C CG . ASP A 110 ? 0.5019 0.4360 0.4275 0.0613 0.0544 0.1208 145 ASP A CG 695 O OD1 . ASP A 110 ? 0.5284 0.4644 0.4619 0.0658 0.0555 0.1212 145 ASP A OD1 696 O OD2 . ASP A 110 ? 0.5363 0.4551 0.4548 0.0583 0.0602 0.1185 145 ASP A OD2 697 N N . ASP A 111 ? 0.4426 0.4305 0.3686 0.0461 0.0270 0.1131 146 ASP A N 698 C CA . ASP A 111 ? 0.4544 0.4566 0.3772 0.0431 0.0194 0.1147 146 ASP A CA 699 C C . ASP A 111 ? 0.4456 0.4632 0.3772 0.0435 0.0135 0.1143 146 ASP A C 700 O O . ASP A 111 ? 0.4069 0.4236 0.3454 0.0429 0.0147 0.1087 146 ASP A O 701 C CB . ASP A 111 ? 0.4571 0.4569 0.3721 0.0347 0.0186 0.1065 146 ASP A CB 702 C CG . ASP A 111 ? 0.4776 0.4639 0.3835 0.0334 0.0242 0.1072 146 ASP A CG 703 O OD1 . ASP A 111 ? 0.4726 0.4535 0.3761 0.0387 0.0270 0.1154 146 ASP A OD1 704 O OD2 . ASP A 111 ? 0.4660 0.4473 0.3675 0.0273 0.0260 0.0997 146 ASP A OD2 705 N N . ASP A 112 ? 0.4460 0.4778 0.3769 0.0441 0.0069 0.1202 147 ASP A N 706 C CA . ASP A 112 ? 0.4671 0.5152 0.4056 0.0431 0.0005 0.1198 147 ASP A CA 707 C C . ASP A 112 ? 0.4549 0.5039 0.3923 0.0350 -0.0015 0.1089 147 ASP A C 708 O O . ASP A 112 ? 0.4579 0.5007 0.3867 0.0294 -0.0009 0.1034 147 ASP A O 709 C CB . ASP A 112 ? 0.5018 0.5656 0.4375 0.0429 -0.0068 0.1272 147 ASP A CB 710 C CG . ASP A 112 ? 0.5435 0.6128 0.4843 0.0520 -0.0067 0.1394 147 ASP A CG 711 O OD1 . ASP A 112 ? 0.5908 0.6535 0.5391 0.0589 -0.0012 0.1420 147 ASP A OD1 712 O OD2 . ASP A 112 ? 0.5669 0.6475 0.5039 0.0523 -0.0122 0.1465 147 ASP A OD2 713 N N . CYS A 113 ? 0.4557 0.5124 0.4021 0.0348 -0.0037 0.1064 148 CYS A N 714 C CA . CYS A 113 ? 0.4870 0.5484 0.4334 0.0277 -0.0073 0.0980 148 CYS A CA 715 C C . CYS A 113 ? 0.4612 0.5324 0.3998 0.0220 -0.0138 0.0981 148 CYS A C 716 O O . CYS A 113 ? 0.4556 0.5398 0.3957 0.0235 -0.0189 0.1052 148 CYS A O 717 C CB . CYS A 113 ? 0.5784 0.6494 0.5364 0.0297 -0.0092 0.0985 148 CYS A CB 718 S SG . CYS A 113 ? 0.6830 0.7539 0.6438 0.0231 -0.0103 0.0876 148 CYS A SG 719 N N . GLU A 114 ? 0.4313 0.4966 0.3614 0.0155 -0.0136 0.0907 149 GLU A N 720 C CA . GLU A 114 ? 0.4303 0.5031 0.3515 0.0094 -0.0191 0.0896 149 GLU A CA 721 C C . GLU A 114 ? 0.3895 0.4604 0.3090 0.0024 -0.0199 0.0794 149 GLU A C 722 O O . GLU A 114 ? 0.3707 0.4302 0.2883 0.0010 -0.0151 0.0730 149 GLU A O 723 C CB . GLU A 114 ? 0.4712 0.5373 0.3809 0.0088 -0.0172 0.0919 149 GLU A CB 724 C CG . GLU A 114 ? 0.5354 0.6087 0.4342 0.0026 -0.0226 0.0914 149 GLU A CG 725 C CD . GLU A 114 ? 0.6147 0.6799 0.5011 0.0013 -0.0198 0.0924 149 GLU A CD 726 O OE1 . GLU A 114 ? 0.6158 0.6699 0.5021 0.0053 -0.0138 0.0940 149 GLU A OE1 727 O OE2 . GLU A 114 ? 0.6280 0.6978 0.5040 -0.0039 -0.0236 0.0915 149 GLU A OE2 728 N N . GLU A 115 ? 0.3588 0.4408 0.2782 -0.0020 -0.0258 0.0781 150 GLU A N 729 C CA . GLU A 115 ? 0.3755 0.4556 0.2929 -0.0086 -0.0266 0.0689 150 GLU A CA 730 C C . GLU A 115 ? 0.3706 0.4399 0.2770 -0.0127 -0.0234 0.0626 150 GLU A C 731 O O . GLU A 115 ? 0.3566 0.4251 0.2537 -0.0135 -0.0237 0.0654 150 GLU A O 732 C CB . GLU A 115 ? 0.3926 0.4862 0.3091 -0.0138 -0.0338 0.0694 150 GLU A CB 733 C CG . GLU A 115 ? 0.4267 0.5178 0.3414 -0.0205 -0.0344 0.0602 150 GLU A CG 734 C CD . GLU A 115 ? 0.4511 0.5556 0.3680 -0.0254 -0.0410 0.0607 150 GLU A CD 735 O OE1 . GLU A 115 ? 0.4844 0.6019 0.4034 -0.0244 -0.0458 0.0681 150 GLU A OE1 736 O OE2 . GLU A 115 ? 0.4642 0.5660 0.3806 -0.0305 -0.0412 0.0537 150 GLU A OE2 737 N N . ILE A 116 ? 0.3442 0.4056 0.2520 -0.0149 -0.0202 0.0546 151 ILE A N 738 C CA . ILE A 116 ? 0.3632 0.4150 0.2621 -0.0186 -0.0167 0.0480 151 ILE A CA 739 C C . ILE A 116 ? 0.3807 0.4340 0.2754 -0.0250 -0.0193 0.0412 151 ILE A C 740 O O . ILE A 116 ? 0.3873 0.4369 0.2870 -0.0258 -0.0177 0.0358 151 ILE A O 741 C CB . ILE A 116 ? 0.3596 0.4006 0.2630 -0.0159 -0.0103 0.0442 151 ILE A CB 742 C CG1 . ILE A 116 ? 0.3806 0.4186 0.2887 -0.0098 -0.0072 0.0503 151 ILE A CG1 743 C CG2 . ILE A 116 ? 0.3774 0.4103 0.2720 -0.0191 -0.0066 0.0388 151 ILE A CG2 744 C CD1 . ILE A 116 ? 0.3781 0.4087 0.2939 -0.0074 -0.0025 0.0470 151 ILE A CD1 745 N N . LYS A 117 ? 0.3997 0.4576 0.2844 -0.0298 -0.0231 0.0416 152 LYS A N 746 C CA . LYS A 117 ? 0.4387 0.4978 0.3182 -0.0367 -0.0257 0.0353 152 LYS A CA 747 C C . LYS A 117 ? 0.4411 0.4884 0.3142 -0.0394 -0.0207 0.0269 152 LYS A C 748 O O . LYS A 117 ? 0.4421 0.4869 0.3154 -0.0429 -0.0208 0.0209 152 LYS A O 749 C CB . LYS A 117 ? 0.4802 0.5479 0.3500 -0.0417 -0.0314 0.0381 152 LYS A CB 750 C CG . LYS A 117 ? 0.5263 0.6080 0.4027 -0.0395 -0.0372 0.0465 152 LYS A CG 751 C CD . LYS A 117 ? 0.5830 0.6734 0.4485 -0.0443 -0.0427 0.0500 152 LYS A CD 752 C CE . LYS A 117 ? 0.6580 0.7638 0.5309 -0.0411 -0.0483 0.0599 152 LYS A CE 753 N NZ . LYS A 117 ? 0.6861 0.8016 0.5691 -0.0429 -0.0523 0.0595 152 LYS A NZ 754 N N . VAL A 118 ? 0.4286 0.4688 0.2963 -0.0377 -0.0162 0.0267 153 VAL A N 755 C CA . VAL A 118 ? 0.4277 0.4575 0.2906 -0.0393 -0.0106 0.0195 153 VAL A CA 756 C C . VAL A 118 ? 0.3851 0.4092 0.2516 -0.0344 -0.0051 0.0212 153 VAL A C 757 O O . VAL A 118 ? 0.4059 0.4326 0.2735 -0.0313 -0.0056 0.0277 153 VAL A O 758 C CB . VAL A 118 ? 0.4747 0.5020 0.3224 -0.0449 -0.0106 0.0163 153 VAL A CB 759 C CG1 . VAL A 118 ? 0.5012 0.5330 0.3441 -0.0510 -0.0156 0.0136 153 VAL A CG1 760 C CG2 . VAL A 118 ? 0.4902 0.5206 0.3301 -0.0444 -0.0115 0.0224 153 VAL A CG2 761 N N . PRO A 119 ? 0.3678 0.3841 0.2363 -0.0338 0.0001 0.0156 154 PRO A N 762 C CA . PRO A 119 ? 0.3459 0.3579 0.2180 -0.0300 0.0050 0.0172 154 PRO A CA 763 C C . PRO A 119 ? 0.3674 0.3782 0.2295 -0.0308 0.0065 0.0204 154 PRO A C 764 O O . PRO A 119 ? 0.3787 0.3887 0.2300 -0.0348 0.0062 0.0180 154 PRO A O 765 C CB . PRO A 119 ? 0.3673 0.3729 0.2415 -0.0303 0.0098 0.0104 154 PRO A CB 766 C CG . PRO A 119 ? 0.3774 0.3841 0.2536 -0.0324 0.0070 0.0064 154 PRO A CG 767 C CD . PRO A 119 ? 0.3710 0.3826 0.2390 -0.0362 0.0019 0.0082 154 PRO A CD 768 N N . GLU A 120 ? 0.3565 0.3667 0.2217 -0.0273 0.0081 0.0260 155 GLU A N 769 C CA . GLU A 120 ? 0.3762 0.3843 0.2324 -0.0276 0.0102 0.0297 155 GLU A CA 770 C C . GLU A 120 ? 0.3846 0.3859 0.2440 -0.0260 0.0169 0.0279 155 GLU A C 771 O O . GLU A 120 ? 0.4138 0.4133 0.2786 -0.0229 0.0187 0.0320 155 GLU A O 772 C CB . GLU A 120 ? 0.3751 0.3880 0.2314 -0.0249 0.0066 0.0383 155 GLU A CB 773 C CG . GLU A 120 ? 0.4013 0.4230 0.2543 -0.0270 -0.0003 0.0403 155 GLU A CG 774 C CD . GLU A 120 ? 0.4095 0.4378 0.2642 -0.0236 -0.0042 0.0496 155 GLU A CD 775 O OE1 . GLU A 120 ? 0.4149 0.4394 0.2705 -0.0197 -0.0011 0.0548 155 GLU A OE1 776 O OE2 . GLU A 120 ? 0.4429 0.4804 0.2986 -0.0246 -0.0102 0.0520 155 GLU A OE2 777 N N . CYS A 121 ? 0.4015 0.3991 0.2579 -0.0284 0.0207 0.0217 156 CYS A N 778 C CA . CYS A 121 ? 0.4034 0.3964 0.2644 -0.0274 0.0268 0.0192 156 CYS A CA 779 C C . CYS A 121 ? 0.4127 0.4025 0.2640 -0.0293 0.0313 0.0197 156 CYS A C 780 O O . CYS A 121 ? 0.4161 0.4061 0.2564 -0.0321 0.0304 0.0188 156 CYS A O 781 C CB . CYS A 121 ? 0.4270 0.4192 0.2936 -0.0279 0.0285 0.0123 156 CYS A CB 782 S SG . CYS A 121 ? 0.4528 0.4480 0.3319 -0.0255 0.0245 0.0117 156 CYS A SG 783 N N . PRO A 122 ? 0.4049 0.3914 0.2595 -0.0283 0.0362 0.0211 157 PRO A N 784 C CA . PRO A 122 ? 0.4021 0.3855 0.2477 -0.0303 0.0411 0.0216 157 PRO A CA 785 C C . PRO A 122 ? 0.3817 0.3639 0.2238 -0.0325 0.0451 0.0150 157 PRO A C 786 O O . PRO A 122 ? 0.3539 0.3372 0.2016 -0.0321 0.0447 0.0100 157 PRO A O 787 C CB . PRO A 122 ? 0.4329 0.4132 0.2850 -0.0290 0.0456 0.0239 157 PRO A CB 788 C CG . PRO A 122 ? 0.4219 0.4031 0.2845 -0.0263 0.0426 0.0255 157 PRO A CG 789 C CD . PRO A 122 ? 0.4020 0.3873 0.2678 -0.0258 0.0377 0.0224 157 PRO A CD 790 N N . ALA A 123 ? 0.3630 0.3427 0.1959 -0.0345 0.0496 0.0152 158 ALA A N 791 C CA . ALA A 123 ? 0.3678 0.3461 0.1976 -0.0362 0.0550 0.0093 158 ALA A CA 792 C C . ALA A 123 ? 0.3538 0.3332 0.1965 -0.0344 0.0584 0.0051 158 ALA A C 793 O O . ALA A 123 ? 0.3534 0.3337 0.2054 -0.0330 0.0593 0.0073 158 ALA A O 794 C CB . ALA A 123 ? 0.3799 0.3554 0.2007 -0.0380 0.0605 0.0113 158 ALA A CB 795 N N . GLY A 124 ? 0.3646 0.3438 0.2077 -0.0344 0.0602 -0.0006 159 GLY A N 796 C CA . GLY A 124 ? 0.3635 0.3446 0.2185 -0.0324 0.0638 -0.0043 159 GLY A CA 797 C C . GLY A 124 ? 0.3615 0.3448 0.2272 -0.0302 0.0593 -0.0053 159 GLY A C 798 O O . GLY A 124 ? 0.3533 0.3384 0.2278 -0.0284 0.0616 -0.0086 159 GLY A O 799 N N . PHE A 125 ? 0.3680 0.3517 0.2333 -0.0301 0.0531 -0.0022 160 PHE A N 800 C CA . PHE A 125 ? 0.3667 0.3524 0.2408 -0.0282 0.0486 -0.0032 160 PHE A CA 801 C C . PHE A 125 ? 0.4131 0.3971 0.2825 -0.0290 0.0471 -0.0076 160 PHE A C 802 O O . PHE A 125 ? 0.4517 0.4340 0.3102 -0.0314 0.0450 -0.0076 160 PHE A O 803 C CB . PHE A 125 ? 0.3544 0.3414 0.2300 -0.0277 0.0432 0.0019 160 PHE A CB 804 C CG . PHE A 125 ? 0.3402 0.3275 0.2232 -0.0265 0.0449 0.0052 160 PHE A CG 805 C CD1 . PHE A 125 ? 0.3508 0.3362 0.2295 -0.0276 0.0487 0.0080 160 PHE A CD1 806 C CD2 . PHE A 125 ? 0.3247 0.3136 0.2184 -0.0246 0.0430 0.0052 160 PHE A CD2 807 C CE1 . PHE A 125 ? 0.3424 0.3270 0.2272 -0.0272 0.0507 0.0106 160 PHE A CE1 808 C CE2 . PHE A 125 ? 0.3230 0.3112 0.2223 -0.0243 0.0449 0.0076 160 PHE A CE2 809 C CZ . PHE A 125 ? 0.3345 0.3203 0.2295 -0.0256 0.0487 0.0102 160 PHE A CZ 810 N N . VAL A 126 ? 0.4251 0.4094 0.3025 -0.0271 0.0481 -0.0113 161 VAL A N 811 C CA . VAL A 126 ? 0.4222 0.4033 0.2957 -0.0276 0.0477 -0.0160 161 VAL A CA 812 C C . VAL A 126 ? 0.4205 0.4025 0.2983 -0.0274 0.0418 -0.0158 161 VAL A C 813 O O . VAL A 126 ? 0.4072 0.3861 0.2804 -0.0287 0.0406 -0.0191 161 VAL A O 814 C CB . VAL A 126 ? 0.4660 0.4457 0.3443 -0.0253 0.0536 -0.0202 161 VAL A CB 815 C CG1 . VAL A 126 ? 0.5018 0.4815 0.3770 -0.0256 0.0600 -0.0204 161 VAL A CG1 816 C CG2 . VAL A 126 ? 0.4665 0.4500 0.3591 -0.0221 0.0528 -0.0198 161 VAL A CG2 817 N N . ARG A 127 ? 0.3510 0.3369 0.2373 -0.0259 0.0385 -0.0121 162 ARG A N 818 C CA . ARG A 127 ? 0.3349 0.3224 0.2257 -0.0255 0.0332 -0.0113 162 ARG A CA 819 C C . ARG A 127 ? 0.3124 0.3035 0.2087 -0.0243 0.0304 -0.0061 162 ARG A C 820 O O . ARG A 127 ? 0.2931 0.2847 0.1926 -0.0233 0.0334 -0.0043 162 ARG A O 821 C CB . ARG A 127 ? 0.3534 0.3402 0.2525 -0.0234 0.0341 -0.0146 162 ARG A CB 822 C CG . ARG A 127 ? 0.3494 0.3390 0.2594 -0.0206 0.0365 -0.0137 162 ARG A CG 823 C CD . ARG A 127 ? 0.3592 0.3486 0.2766 -0.0183 0.0371 -0.0165 162 ARG A CD 824 N NE . ARG A 127 ? 0.3667 0.3529 0.2812 -0.0175 0.0419 -0.0203 162 ARG A NE 825 C CZ . ARG A 127 ? 0.3881 0.3759 0.3055 -0.0160 0.0471 -0.0210 162 ARG A CZ 826 N NH1 . ARG A 127 ? 0.3656 0.3583 0.2887 -0.0158 0.0481 -0.0184 162 ARG A NH1 827 N NH2 . ARG A 127 ? 0.4283 0.4127 0.3429 -0.0148 0.0516 -0.0245 162 ARG A NH2 828 N N . PRO A 128 ? 0.2977 0.2912 0.1956 -0.0244 0.0252 -0.0038 163 PRO A N 829 C CA . PRO A 128 ? 0.2916 0.2874 0.1954 -0.0225 0.0236 0.0009 163 PRO A CA 830 C C . PRO A 128 ? 0.2810 0.2769 0.1950 -0.0203 0.0255 0.0000 163 PRO A C 831 O O . PRO A 128 ? 0.2820 0.2782 0.2007 -0.0197 0.0247 -0.0028 163 PRO A O 832 C CB . PRO A 128 ? 0.2976 0.2967 0.2019 -0.0227 0.0180 0.0031 163 PRO A CB 833 C CG . PRO A 128 ? 0.3224 0.3206 0.2224 -0.0252 0.0166 -0.0011 163 PRO A CG 834 C CD . PRO A 128 ? 0.3112 0.3053 0.2045 -0.0266 0.0210 -0.0049 163 PRO A CD 835 N N . PRO A 129 ? 0.2733 0.2686 0.1902 -0.0195 0.0281 0.0022 164 PRO A N 836 C CA . PRO A 129 ? 0.2455 0.2415 0.1716 -0.0182 0.0293 0.0012 164 PRO A CA 837 C C . PRO A 129 ? 0.2399 0.2371 0.1713 -0.0168 0.0256 0.0026 164 PRO A C 838 O O . PRO A 129 ? 0.2298 0.2277 0.1584 -0.0166 0.0224 0.0055 164 PRO A O 839 C CB . PRO A 129 ? 0.2483 0.2428 0.1748 -0.0186 0.0326 0.0037 164 PRO A CB 840 C CG . PRO A 129 ? 0.2589 0.2520 0.1765 -0.0200 0.0347 0.0045 164 PRO A CG 841 C CD . PRO A 129 ? 0.2707 0.2645 0.1823 -0.0202 0.0306 0.0053 164 PRO A CD 842 N N . LEU A 130 ? 0.2367 0.2346 0.1754 -0.0160 0.0259 0.0008 165 LEU A N 843 C CA . LEU A 130 ? 0.2233 0.2219 0.1672 -0.0148 0.0232 0.0021 165 LEU A CA 844 C C . LEU A 130 ? 0.2183 0.2157 0.1666 -0.0146 0.0255 0.0030 165 LEU A C 845 O O . LEU A 130 ? 0.2166 0.2147 0.1677 -0.0156 0.0281 0.0008 165 LEU A O 846 C CB . LEU A 130 ? 0.2264 0.2264 0.1741 -0.0144 0.0215 -0.0009 165 LEU A CB 847 C CG . LEU A 130 ? 0.2236 0.2244 0.1769 -0.0133 0.0193 -0.0002 165 LEU A CG 848 C CD1 . LEU A 130 ? 0.2395 0.2412 0.1913 -0.0127 0.0164 0.0029 165 LEU A CD1 849 C CD2 . LEU A 130 ? 0.2251 0.2268 0.1818 -0.0130 0.0183 -0.0032 165 LEU A CD2 850 N N . ILE A 131 ? 0.2180 0.2136 0.1668 -0.0136 0.0247 0.0061 166 ILE A N 851 C CA . ILE A 131 ? 0.2217 0.2149 0.1741 -0.0138 0.0267 0.0066 166 ILE A CA 852 C C . ILE A 131 ? 0.2112 0.2046 0.1677 -0.0123 0.0246 0.0069 166 ILE A C 853 O O . ILE A 131 ? 0.2071 0.2008 0.1628 -0.0105 0.0226 0.0095 166 ILE A O 854 C CB . ILE A 131 ? 0.2413 0.2300 0.1900 -0.0137 0.0293 0.0102 166 ILE A CB 855 C CG1 . ILE A 131 ? 0.2695 0.2578 0.2134 -0.0154 0.0317 0.0102 166 ILE A CG1 856 C CG2 . ILE A 131 ? 0.2487 0.2335 0.2001 -0.0147 0.0319 0.0099 166 ILE A CG2 857 C CD1 . ILE A 131 ? 0.3004 0.2840 0.2394 -0.0151 0.0338 0.0145 166 ILE A CD1 858 N N . ILE A 132 ? 0.2028 0.1968 0.1636 -0.0132 0.0250 0.0043 167 ILE A N 859 C CA . ILE A 132 ? 0.2203 0.2141 0.1847 -0.0123 0.0235 0.0041 167 ILE A CA 860 C C . ILE A 132 ? 0.2427 0.2317 0.2070 -0.0129 0.0263 0.0051 167 ILE A C 861 O O . ILE A 132 ? 0.2655 0.2535 0.2301 -0.0154 0.0284 0.0034 167 ILE A O 862 C CB . ILE A 132 ? 0.2241 0.2212 0.1923 -0.0130 0.0222 0.0009 167 ILE A CB 863 C CG1 . ILE A 132 ? 0.2407 0.2408 0.2083 -0.0123 0.0202 -0.0002 167 ILE A CG1 864 C CG2 . ILE A 132 ? 0.2246 0.2213 0.1956 -0.0123 0.0209 0.0009 167 ILE A CG2 865 C CD1 . ILE A 132 ? 0.2598 0.2625 0.2298 -0.0129 0.0208 -0.0030 167 ILE A CD1 866 N N . PHE A 133 ? 0.2411 0.2270 0.2048 -0.0107 0.0265 0.0079 168 PHE A N 867 C CA . PHE A 133 ? 0.2250 0.2043 0.1875 -0.0109 0.0298 0.0090 168 PHE A CA 868 C C . PHE A 133 ? 0.2267 0.2057 0.1921 -0.0103 0.0292 0.0077 168 PHE A C 869 O O . PHE A 133 ? 0.2226 0.2025 0.1893 -0.0074 0.0280 0.0099 168 PHE A O 870 C CB . PHE A 133 ? 0.2441 0.2200 0.2037 -0.0080 0.0311 0.0136 168 PHE A CB 871 C CG . PHE A 133 ? 0.2483 0.2154 0.2054 -0.0080 0.0356 0.0151 168 PHE A CG 872 C CD1 . PHE A 133 ? 0.2410 0.2037 0.1993 -0.0070 0.0373 0.0148 168 PHE A CD1 873 C CD2 . PHE A 133 ? 0.2736 0.2359 0.2266 -0.0090 0.0385 0.0168 168 PHE A CD2 874 C CE1 . PHE A 133 ? 0.2661 0.2191 0.2212 -0.0071 0.0420 0.0159 168 PHE A CE1 875 C CE2 . PHE A 133 ? 0.2816 0.2343 0.2316 -0.0092 0.0431 0.0182 168 PHE A CE2 876 C CZ . PHE A 133 ? 0.2825 0.2301 0.2334 -0.0082 0.0450 0.0176 168 PHE A CZ 877 N N . SER A 134 ? 0.2438 0.2224 0.2102 -0.0133 0.0298 0.0044 169 SER A N 878 C CA . SER A 134 ? 0.2603 0.2390 0.2287 -0.0134 0.0291 0.0028 169 SER A CA 879 C C . SER A 134 ? 0.2490 0.2195 0.2146 -0.0142 0.0329 0.0027 169 SER A C 880 O O . SER A 134 ? 0.2460 0.2121 0.2089 -0.0173 0.0357 0.0017 169 SER A O 881 C CB . SER A 134 ? 0.3073 0.2909 0.2779 -0.0163 0.0272 -0.0005 169 SER A CB 882 O OG . SER A 134 ? 0.4024 0.3919 0.3755 -0.0148 0.0239 -0.0007 169 SER A OG 883 N N . VAL A 135 ? 0.2358 0.2042 0.2019 -0.0117 0.0334 0.0038 170 VAL A N 884 C CA . VAL A 135 ? 0.2537 0.2132 0.2167 -0.0119 0.0377 0.0037 170 VAL A CA 885 C C . VAL A 135 ? 0.2674 0.2278 0.2311 -0.0132 0.0370 0.0010 170 VAL A C 886 O O . VAL A 135 ? 0.3092 0.2749 0.2760 -0.0112 0.0342 0.0015 170 VAL A O 887 C CB . VAL A 135 ? 0.2579 0.2132 0.2206 -0.0069 0.0402 0.0080 170 VAL A CB 888 C CG1 . VAL A 135 ? 0.2662 0.2171 0.2260 -0.0067 0.0425 0.0104 170 VAL A CG1 889 C CG2 . VAL A 135 ? 0.2653 0.2285 0.2325 -0.0030 0.0366 0.0108 170 VAL A CG2 890 N N . ASP A 136 ? 0.2636 0.2188 0.2236 -0.0173 0.0392 -0.0019 171 ASP A N 891 C CA . ASP A 136 ? 0.2459 0.2021 0.2054 -0.0194 0.0383 -0.0047 171 ASP A CA 892 C C . ASP A 136 ? 0.2686 0.2181 0.2261 -0.0165 0.0418 -0.0038 171 ASP A C 893 O O . ASP A 136 ? 0.2687 0.2089 0.2226 -0.0158 0.0466 -0.0031 171 ASP A O 894 C CB . ASP A 136 ? 0.2666 0.2204 0.2223 -0.0256 0.0393 -0.0083 171 ASP A CB 895 C CG . ASP A 136 ? 0.2873 0.2458 0.2430 -0.0285 0.0365 -0.0109 171 ASP A CG 896 O OD1 . ASP A 136 ? 0.2521 0.2094 0.2074 -0.0265 0.0368 -0.0108 171 ASP A OD1 897 O OD2 . ASP A 136 ? 0.3301 0.2938 0.2864 -0.0327 0.0342 -0.0128 171 ASP A OD2 898 N N . GLY A 137 ? 0.2328 0.1866 0.1926 -0.0150 0.0399 -0.0038 172 GLY A N 899 C CA . GLY A 137 ? 0.2404 0.1889 0.1988 -0.0124 0.0434 -0.0032 172 GLY A CA 900 C C . GLY A 137 ? 0.2538 0.2000 0.2146 -0.0065 0.0462 0.0009 172 GLY A C 901 O O . GLY A 137 ? 0.2616 0.2004 0.2201 -0.0044 0.0510 0.0014 172 GLY A O 902 N N . PHE A 138 ? 0.2582 0.2107 0.2233 -0.0039 0.0433 0.0041 173 PHE A N 903 C CA . PHE A 138 ? 0.2617 0.2144 0.2297 0.0015 0.0448 0.0089 173 PHE A CA 904 C C . PHE A 138 ? 0.2643 0.2245 0.2376 0.0045 0.0429 0.0107 173 PHE A C 905 O O . PHE A 138 ? 0.2480 0.2171 0.2250 0.0042 0.0381 0.0113 173 PHE A O 906 C CB . PHE A 138 ? 0.2687 0.2254 0.2380 0.0021 0.0422 0.0112 173 PHE A CB 907 C CG . PHE A 138 ? 0.2659 0.2211 0.2366 0.0072 0.0444 0.0165 173 PHE A CG 908 C CD1 . PHE A 138 ? 0.2670 0.2291 0.2430 0.0119 0.0431 0.0205 173 PHE A CD1 909 C CD2 . PHE A 138 ? 0.2845 0.2323 0.2513 0.0074 0.0475 0.0180 173 PHE A CD2 910 C CE1 . PHE A 138 ? 0.2708 0.2329 0.2485 0.0169 0.0446 0.0261 173 PHE A CE1 911 C CE2 . PHE A 138 ? 0.2943 0.2409 0.2621 0.0126 0.0493 0.0235 173 PHE A CE2 912 C CZ . PHE A 138 ? 0.2784 0.2326 0.2519 0.0175 0.0477 0.0277 173 PHE A CZ 913 N N . ARG A 139 ? 0.2808 0.2365 0.2539 0.0071 0.0472 0.0114 174 ARG A N 914 C CA . ARG A 139 ? 0.3033 0.2655 0.2814 0.0099 0.0465 0.0132 174 ARG A CA 915 C C . ARG A 139 ? 0.3004 0.2705 0.2847 0.0145 0.0446 0.0186 174 ARG A C 916 O O . ARG A 139 ? 0.3008 0.2677 0.2848 0.0176 0.0468 0.0219 174 ARG A O 917 C CB . ARG A 139 ? 0.3473 0.3011 0.3228 0.0118 0.0529 0.0126 174 ARG A CB 918 C CG . ARG A 139 ? 0.4122 0.3717 0.3921 0.0141 0.0532 0.0138 174 ARG A CG 919 C CD . ARG A 139 ? 0.4091 0.3588 0.3852 0.0158 0.0604 0.0127 174 ARG A CD 920 N NE . ARG A 139 ? 0.4218 0.3778 0.4041 0.0200 0.0619 0.0158 174 ARG A NE 921 C CZ . ARG A 139 ? 0.3847 0.3372 0.3651 0.0202 0.0662 0.0141 174 ARG A CZ 922 N NH1 . ARG A 139 ? 0.3753 0.3176 0.3469 0.0162 0.0691 0.0092 174 ARG A NH1 923 N NH2 . ARG A 139 ? 0.4256 0.3855 0.4129 0.0243 0.0674 0.0175 174 ARG A NH2 924 N N . ALA A 140 ? 0.2710 0.2514 0.2605 0.0146 0.0405 0.0198 175 ALA A N 925 C CA . ALA A 140 ? 0.2884 0.2782 0.2839 0.0178 0.0377 0.0246 175 ALA A CA 926 C C . ALA A 140 ? 0.2853 0.2740 0.2839 0.0238 0.0421 0.0296 175 ALA A C 927 O O . ALA A 140 ? 0.2999 0.2921 0.3005 0.0266 0.0409 0.0339 175 ALA A O 928 C CB . ALA A 140 ? 0.2781 0.2782 0.2786 0.0165 0.0338 0.0248 175 ALA A CB 929 N N . SER A 141 ? 0.2742 0.2580 0.2730 0.0261 0.0474 0.0294 176 SER A N 930 C CA . SER A 141 ? 0.2995 0.2824 0.3021 0.0328 0.0523 0.0345 176 SER A CA 931 C C . SER A 141 ? 0.3150 0.2874 0.3130 0.0354 0.0563 0.0362 176 SER A C 932 O O . SER A 141 ? 0.3234 0.2963 0.3252 0.0416 0.0594 0.0418 176 SER A O 933 C CB . SER A 141 ? 0.3217 0.3005 0.3248 0.0348 0.0580 0.0334 176 SER A CB 934 O OG . SER A 141 ? 0.3570 0.3229 0.3515 0.0312 0.0616 0.0278 176 SER A OG 935 N N . TYR A 142 ? 0.3020 0.2654 0.2925 0.0307 0.0563 0.0319 177 TYR A N 936 C CA . TYR A 142 ? 0.3197 0.2731 0.3056 0.0324 0.0599 0.0336 177 TYR A CA 937 C C . TYR A 142 ? 0.3380 0.2990 0.3278 0.0360 0.0567 0.0397 177 TYR A C 938 O O . TYR A 142 ? 0.3616 0.3158 0.3498 0.0401 0.0607 0.0436 177 TYR A O 939 C CB . TYR A 142 ? 0.3061 0.2513 0.2842 0.0259 0.0595 0.0281 177 TYR A CB 940 C CG . TYR A 142 ? 0.3124 0.2482 0.2846 0.0216 0.0629 0.0221 177 TYR A CG 941 C CD1 . TYR A 142 ? 0.3353 0.2652 0.3068 0.0241 0.0684 0.0215 177 TYR A CD1 942 C CD2 . TYR A 142 ? 0.3029 0.2357 0.2698 0.0149 0.0608 0.0170 177 TYR A CD2 943 C CE1 . TYR A 142 ? 0.3501 0.2714 0.3149 0.0194 0.0713 0.0158 177 TYR A CE1 944 C CE2 . TYR A 142 ? 0.3091 0.2343 0.2702 0.0103 0.0634 0.0117 177 TYR A CE2 945 C CZ . TYR A 142 ? 0.3439 0.2632 0.3034 0.0123 0.0685 0.0109 177 TYR A CZ 946 O OH . TYR A 142 ? 0.3283 0.2400 0.2809 0.0071 0.0708 0.0055 177 TYR A OH 947 N N . MET A 143 ? 0.3284 0.3028 0.3227 0.0344 0.0499 0.0407 178 MET A N 948 C CA . MET A 143 ? 0.3590 0.3424 0.3570 0.0375 0.0463 0.0467 178 MET A CA 949 C C . MET A 143 ? 0.3884 0.3760 0.3928 0.0452 0.0492 0.0539 178 MET A C 950 O O . MET A 143 ? 0.3993 0.3909 0.4052 0.0488 0.0480 0.0598 178 MET A O 951 C CB . MET A 143 ? 0.3451 0.3419 0.3463 0.0337 0.0388 0.0458 178 MET A CB 952 C CG . MET A 143 ? 0.3564 0.3511 0.3521 0.0272 0.0353 0.0404 178 MET A CG 953 S SD . MET A 143 ? 0.3981 0.3857 0.3873 0.0268 0.0361 0.0417 178 MET A SD 954 C CE . MET A 143 ? 0.4324 0.4241 0.4185 0.0199 0.0305 0.0363 178 MET A CE 955 N N . LYS A 144 ? 0.4259 0.4134 0.4342 0.0479 0.0530 0.0538 179 LYS A N 956 C CA . LYS A 144 ? 0.4803 0.4713 0.4954 0.0559 0.0569 0.0607 179 LYS A CA 957 C C . LYS A 144 ? 0.4911 0.4694 0.5025 0.0615 0.0635 0.0644 179 LYS A C 958 O O . LYS A 144 ? 0.5118 0.4946 0.5289 0.0689 0.0655 0.0718 179 LYS A O 959 C CB . LYS A 144 ? 0.5088 0.5006 0.5279 0.0574 0.0608 0.0590 179 LYS A CB 960 C CG . LYS A 144 ? 0.5506 0.5562 0.5750 0.0533 0.0550 0.0571 179 LYS A CG 961 C CD . LYS A 144 ? 0.6037 0.6273 0.6375 0.0559 0.0498 0.0637 179 LYS A CD 962 C CE . LYS A 144 ? 0.6452 0.6749 0.6881 0.0637 0.0545 0.0699 179 LYS A CE 963 N NZ . LYS A 144 ? 0.6542 0.7002 0.7054 0.0673 0.0498 0.0778 179 LYS A NZ 964 N N . LYS A 145 ? 0.4948 0.4576 0.4969 0.0580 0.0669 0.0597 180 LYS A N 965 C CA . LYS A 145 ? 0.5268 0.4750 0.5238 0.0622 0.0737 0.0625 180 LYS A CA 966 C C . LYS A 145 ? 0.5516 0.5047 0.5496 0.0655 0.0707 0.0694 180 LYS A C 967 O O . LYS A 145 ? 0.5768 0.5231 0.5747 0.0721 0.0758 0.0752 180 LYS A O 968 C CB . LYS A 145 ? 0.5296 0.4613 0.5162 0.0561 0.0773 0.0552 180 LYS A CB 969 C CG . LYS A 145 ? 0.5593 0.4831 0.5439 0.0549 0.0826 0.0500 180 LYS A CG 970 C CD . LYS A 145 ? 0.5888 0.5014 0.5640 0.0466 0.0835 0.0418 180 LYS A CD 971 C CE . LYS A 145 ? 0.6080 0.5170 0.5814 0.0441 0.0864 0.0363 180 LYS A CE 972 N NZ . LYS A 145 ? 0.6367 0.5336 0.6083 0.0497 0.0958 0.0376 180 LYS A NZ 973 N N . GLY A 146 ? 0.5576 0.5222 0.5564 0.0609 0.0626 0.0688 181 GLY A N 974 C CA . GLY A 146 ? 0.5544 0.5298 0.5565 0.0642 0.0581 0.0761 181 GLY A CA 975 C C . GLY A 146 ? 0.5638 0.5290 0.5585 0.0646 0.0600 0.0784 181 GLY A C 976 O O . GLY A 146 ? 0.5146 0.4651 0.5014 0.0609 0.0640 0.0735 181 GLY A O 977 N N . SER A 147 ? 0.5543 0.5281 0.5517 0.0691 0.0571 0.0864 182 SER A N 978 C CA . SER A 147 ? 0.5905 0.5584 0.5813 0.0691 0.0571 0.0897 182 SER A CA 979 C C . SER A 147 ? 0.6102 0.5584 0.5948 0.0725 0.0660 0.0909 182 SER A C 980 O O . SER A 147 ? 0.5965 0.5356 0.5733 0.0696 0.0669 0.0903 182 SER A O 981 C CB . SER A 147 ? 0.6188 0.6015 0.6145 0.0742 0.0521 0.0990 182 SER A CB 982 O OG . SER A 147 ? 0.7287 0.7081 0.7172 0.0726 0.0505 0.1014 182 SER A OG 983 N N . LYS A 148 ? 0.5901 0.5311 0.5779 0.0785 0.0728 0.0927 183 LYS A N 984 C CA . LYS A 148 ? 0.6210 0.5417 0.6025 0.0821 0.0821 0.0940 183 LYS A CA 985 C C . LYS A 148 ? 0.5485 0.4534 0.5207 0.0739 0.0857 0.0844 183 LYS A C 986 O O . LYS A 148 ? 0.5557 0.4442 0.5201 0.0734 0.0914 0.0845 183 LYS A O 987 C CB . LYS A 148 ? 0.7069 0.6243 0.6943 0.0913 0.0890 0.0986 183 LYS A CB 988 C CG . LYS A 148 ? 0.7895 0.6868 0.7713 0.0974 0.0989 0.1027 183 LYS A CG 989 C CD . LYS A 148 ? 0.8444 0.7445 0.8265 0.1036 0.0977 0.1130 183 LYS A CD 990 C CE . LYS A 148 ? 0.9012 0.7790 0.8725 0.1036 0.1051 0.1136 183 LYS A CE 991 N NZ . LYS A 148 ? 0.9004 0.7730 0.8627 0.0927 0.1020 0.1061 183 LYS A NZ 992 N N . VAL A 149 ? 0.4896 0.3998 0.4627 0.0672 0.0822 0.0766 184 VAL A N 993 C CA . VAL A 149 ? 0.4572 0.3556 0.4224 0.0588 0.0843 0.0675 184 VAL A CA 994 C C . VAL A 149 ? 0.4088 0.3137 0.3710 0.0509 0.0776 0.0637 184 VAL A C 995 O O . VAL A 149 ? 0.3838 0.2780 0.3386 0.0453 0.0798 0.0596 184 VAL A O 996 C CB . VAL A 149 ? 0.4774 0.3763 0.4449 0.0566 0.0855 0.0614 184 VAL A CB 997 C CG1 . VAL A 149 ? 0.4706 0.3594 0.4303 0.0477 0.0869 0.0523 184 VAL A CG1 998 C CG2 . VAL A 149 ? 0.4981 0.3891 0.4678 0.0645 0.0933 0.0649 184 VAL A CG2 999 N N . MET A 150 ? 0.3642 0.2864 0.3321 0.0505 0.0697 0.0651 185 MET A N 1000 C CA . MET A 150 ? 0.3542 0.2837 0.3199 0.0434 0.0634 0.0610 185 MET A CA 1001 C C . MET A 150 ? 0.3354 0.2776 0.3035 0.0456 0.0574 0.0670 185 MET A C 1002 O O . MET A 150 ? 0.2930 0.2491 0.2655 0.0439 0.0510 0.0662 185 MET A O 1003 C CB . MET A 150 ? 0.3405 0.2777 0.3096 0.0387 0.0595 0.0545 185 MET A CB 1004 C CG . MET A 150 ? 0.3564 0.2825 0.3224 0.0356 0.0645 0.0482 185 MET A CG 1005 S SD . MET A 150 ? 0.3833 0.3188 0.3526 0.0300 0.0595 0.0411 185 MET A SD 1006 C CE . MET A 150 ? 0.3770 0.3275 0.3558 0.0359 0.0558 0.0464 185 MET A CE 1007 N N . PRO A 151 ? 0.3372 0.2742 0.3017 0.0490 0.0596 0.0731 186 PRO A N 1008 C CA . PRO A 151 ? 0.3368 0.2864 0.3029 0.0512 0.0538 0.0794 186 PRO A CA 1009 C C . PRO A 151 ? 0.3207 0.2788 0.2841 0.0442 0.0473 0.0751 186 PRO A C 1010 O O . PRO A 151 ? 0.3137 0.2859 0.2805 0.0442 0.0410 0.0772 186 PRO A O 1011 C CB . PRO A 151 ? 0.3549 0.2942 0.3159 0.0556 0.0585 0.0860 186 PRO A CB 1012 C CG . PRO A 151 ? 0.3558 0.2764 0.3104 0.0527 0.0659 0.0812 186 PRO A CG 1013 C CD . PRO A 151 ? 0.3615 0.2811 0.3200 0.0513 0.0675 0.0751 186 PRO A CD 1014 N N . ASN A 152 ? 0.3178 0.2673 0.2751 0.0381 0.0491 0.0692 187 ASN A N 1015 C CA . ASN A 152 ? 0.3039 0.2605 0.2587 0.0318 0.0439 0.0649 187 ASN A CA 1016 C C . ASN A 152 ? 0.2972 0.2646 0.2573 0.0291 0.0389 0.0601 187 ASN A C 1017 O O . ASN A 152 ? 0.2912 0.2697 0.2521 0.0275 0.0332 0.0604 187 ASN A O 1018 C CB . ASN A 152 ? 0.3106 0.2567 0.2591 0.0261 0.0473 0.0595 187 ASN A CB 1019 C CG . ASN A 152 ? 0.3290 0.2660 0.2710 0.0273 0.0512 0.0641 187 ASN A CG 1020 O OD1 . ASN A 152 ? 0.3398 0.2814 0.2783 0.0263 0.0484 0.0665 187 ASN A OD1 1021 N ND2 . ASN A 152 ? 0.3454 0.2686 0.2850 0.0291 0.0579 0.0651 187 ASN A ND2 1022 N N . ILE A 153 ? 0.2849 0.2485 0.2480 0.0284 0.0413 0.0558 188 ILE A N 1023 C CA . ILE A 153 ? 0.2920 0.2644 0.2598 0.0259 0.0372 0.0514 188 ILE A CA 1024 C C . ILE A 153 ? 0.2888 0.2735 0.2628 0.0299 0.0333 0.0563 188 ILE A C 1025 O O . ILE A 153 ? 0.2657 0.2607 0.2417 0.0271 0.0278 0.0546 188 ILE A O 1026 C CB . ILE A 153 ? 0.2894 0.2547 0.2584 0.0246 0.0410 0.0463 188 ILE A CB 1027 C CG1 . ILE A 153 ? 0.2968 0.2533 0.2602 0.0190 0.0433 0.0408 188 ILE A CG1 1028 C CG2 . ILE A 153 ? 0.2886 0.2629 0.2630 0.0233 0.0372 0.0433 188 ILE A CG2 1029 C CD1 . ILE A 153 ? 0.3021 0.2491 0.2645 0.0175 0.0480 0.0366 188 ILE A CD1 1030 N N . GLU A 154 ? 0.3194 0.3033 0.2966 0.0363 0.0361 0.0626 189 GLU A N 1031 C CA . GLU A 154 ? 0.3483 0.3455 0.3322 0.0403 0.0323 0.0681 189 GLU A CA 1032 C C . GLU A 154 ? 0.3156 0.3234 0.2977 0.0386 0.0261 0.0713 189 GLU A C 1033 O O . GLU A 154 ? 0.2817 0.3025 0.2682 0.0377 0.0208 0.0723 189 GLU A O 1034 C CB . GLU A 154 ? 0.4172 0.4118 0.4052 0.0484 0.0371 0.0752 189 GLU A CB 1035 C CG . GLU A 154 ? 0.4935 0.4978 0.4907 0.0519 0.0364 0.0772 189 GLU A CG 1036 C CD . GLU A 154 ? 0.5418 0.5430 0.5403 0.0480 0.0377 0.0696 189 GLU A CD 1037 O OE1 . GLU A 154 ? 0.5454 0.5578 0.5482 0.0452 0.0329 0.0678 189 GLU A OE1 1038 O OE2 . GLU A 154 ? 0.7037 0.6915 0.6983 0.0473 0.0433 0.0655 189 GLU A OE2 1039 N N . LYS A 155 ? 0.3071 0.3090 0.2821 0.0379 0.0270 0.0728 190 LYS A N 1040 C CA . LYS A 155 ? 0.3102 0.3209 0.2816 0.0355 0.0214 0.0751 190 LYS A CA 1041 C C . LYS A 155 ? 0.2868 0.3022 0.2563 0.0284 0.0171 0.0679 190 LYS A C 1042 O O . LYS A 155 ? 0.2752 0.3021 0.2458 0.0264 0.0114 0.0687 190 LYS A O 1043 C CB . LYS A 155 ? 0.3266 0.3291 0.2901 0.0360 0.0239 0.0781 190 LYS A CB 1044 C CG . LYS A 155 ? 0.3482 0.3601 0.3072 0.0341 0.0182 0.0814 190 LYS A CG 1045 C CD . LYS A 155 ? 0.3668 0.3706 0.3175 0.0345 0.0208 0.0847 190 LYS A CD 1046 C CE . LYS A 155 ? 0.3724 0.3849 0.3171 0.0308 0.0152 0.0858 190 LYS A CE 1047 N NZ . LYS A 155 ? 0.3993 0.4039 0.3351 0.0304 0.0179 0.0884 190 LYS A NZ 1048 N N . LEU A 156 ? 0.2704 0.2769 0.2371 0.0245 0.0198 0.0610 191 LEU A N 1049 C CA . LEU A 156 ? 0.2698 0.2801 0.2356 0.0186 0.0163 0.0542 191 LEU A CA 1050 C C . LEU A 156 ? 0.2724 0.2926 0.2448 0.0184 0.0126 0.0535 191 LEU A C 1051 O O . LEU A 156 ? 0.2654 0.2935 0.2370 0.0149 0.0078 0.0519 191 LEU A O 1052 C CB . LEU A 156 ? 0.2855 0.2862 0.2496 0.0155 0.0200 0.0476 191 LEU A CB 1053 C CG . LEU A 156 ? 0.3050 0.2968 0.2625 0.0135 0.0234 0.0463 191 LEU A CG 1054 C CD1 . LEU A 156 ? 0.3230 0.3078 0.2810 0.0105 0.0265 0.0400 191 LEU A CD1 1055 C CD2 . LEU A 156 ? 0.3018 0.2979 0.2541 0.0101 0.0202 0.0453 191 LEU A CD2 1056 N N . ARG A 157 ? 0.2806 0.2994 0.2589 0.0218 0.0153 0.0544 192 ARG A N 1057 C CA . ARG A 157 ? 0.3048 0.3321 0.2898 0.0217 0.0128 0.0538 192 ARG A CA 1058 C C . ARG A 157 ? 0.3009 0.3417 0.2892 0.0229 0.0078 0.0594 192 ARG A C 1059 O O . ARG A 157 ? 0.2808 0.3299 0.2705 0.0190 0.0033 0.0572 192 ARG A O 1060 C CB . ARG A 157 ? 0.3261 0.3486 0.3162 0.0257 0.0176 0.0544 192 ARG A CB 1061 C CG . ARG A 157 ? 0.3683 0.3985 0.3651 0.0252 0.0158 0.0531 192 ARG A CG 1062 C CD . ARG A 157 ? 0.4164 0.4425 0.4179 0.0299 0.0210 0.0546 192 ARG A CD 1063 N NE . ARG A 157 ? 0.4596 0.4903 0.4657 0.0364 0.0224 0.0624 192 ARG A NE 1064 C CZ . ARG A 157 ? 0.5249 0.5694 0.5381 0.0387 0.0191 0.0674 192 ARG A CZ 1065 N NH1 . ARG A 157 ? 0.5265 0.5812 0.5426 0.0342 0.0141 0.0652 192 ARG A NH1 1066 N NH2 . ARG A 157 ? 0.5697 0.6178 0.5872 0.0454 0.0210 0.0751 192 ARG A NH2 1067 N N . SER A 158 ? 0.2928 0.3357 0.2821 0.0281 0.0086 0.0667 193 SER A N 1068 C CA . SER A 158 ? 0.3235 0.3811 0.3170 0.0296 0.0037 0.0730 193 SER A CA 1069 C C . SER A 158 ? 0.3240 0.3874 0.3108 0.0245 -0.0018 0.0726 193 SER A C 1070 O O . SER A 158 ? 0.3125 0.3886 0.3016 0.0220 -0.0073 0.0740 193 SER A O 1071 C CB . SER A 158 ? 0.3466 0.4055 0.3441 0.0376 0.0064 0.0818 193 SER A CB 1072 O OG . SER A 158 ? 0.4109 0.4598 0.4014 0.0394 0.0094 0.0840 193 SER A OG 1073 N N . CYS A 159 ? 0.3307 0.3849 0.3090 0.0226 -0.0002 0.0703 194 CYS A N 1074 C CA . CYS A 159 ? 0.3503 0.4087 0.3210 0.0180 -0.0046 0.0699 194 CYS A CA 1075 C C . CYS A 159 ? 0.2965 0.3544 0.2639 0.0111 -0.0069 0.0618 194 CYS A C 1076 O O . CYS A 159 ? 0.2916 0.3565 0.2547 0.0067 -0.0116 0.0612 194 CYS A O 1077 C CB . CYS A 159 ? 0.4198 0.4690 0.3826 0.0191 -0.0016 0.0715 194 CYS A CB 1078 S SG . CYS A 159 ? 0.5786 0.6316 0.5439 0.0268 -0.0009 0.0828 194 CYS A SG 1079 N N . GLY A 160 ? 0.2442 0.2939 0.2131 0.0100 -0.0035 0.0558 195 GLY A N 1080 C CA . GLY A 160 ? 0.2424 0.2904 0.2083 0.0043 -0.0049 0.0484 195 GLY A CA 1081 C C . GLY A 160 ? 0.2352 0.2898 0.2073 0.0026 -0.0074 0.0465 195 GLY A C 1082 O O . GLY A 160 ? 0.2431 0.3079 0.2203 0.0038 -0.0104 0.0511 195 GLY A O 1083 N N . THR A 161 ? 0.2329 0.2818 0.2047 -0.0002 -0.0061 0.0400 196 THR A N 1084 C CA . THR A 161 ? 0.2339 0.2862 0.2107 -0.0021 -0.0074 0.0373 196 THR A CA 1085 C C . THR A 161 ? 0.2292 0.2754 0.2111 0.0009 -0.0031 0.0361 196 THR A C 1086 O O . THR A 161 ? 0.2507 0.2878 0.2300 0.0016 0.0004 0.0335 196 THR A O 1087 C CB . THR A 161 ? 0.2421 0.2919 0.2138 -0.0078 -0.0091 0.0310 196 THR A CB 1088 O OG1 . THR A 161 ? 0.2596 0.3150 0.2258 -0.0112 -0.0130 0.0320 196 THR A OG1 1089 C CG2 . THR A 161 ? 0.2463 0.2978 0.2224 -0.0100 -0.0100 0.0281 196 THR A CG2 1090 N N . HIS A 162 ? 0.2119 0.2632 0.2009 0.0026 -0.0032 0.0379 197 HIS A N 1091 C CA . HIS A 162 ? 0.2153 0.2604 0.2079 0.0052 0.0010 0.0365 197 HIS A CA 1092 C C . HIS A 162 ? 0.2124 0.2627 0.2106 0.0040 0.0000 0.0355 197 HIS A C 1093 O O . HIS A 162 ? 0.1984 0.2585 0.1995 0.0024 -0.0036 0.0377 197 HIS A O 1094 C CB . HIS A 162 ? 0.2273 0.2702 0.2225 0.0111 0.0047 0.0415 197 HIS A CB 1095 C CG . HIS A 162 ? 0.2448 0.2972 0.2474 0.0146 0.0040 0.0471 197 HIS A CG 1096 N ND1 . HIS A 162 ? 0.2520 0.3153 0.2563 0.0150 0.0000 0.0522 197 HIS A ND1 1097 C CD2 . HIS A 162 ? 0.2498 0.3034 0.2588 0.0178 0.0068 0.0485 197 HIS A CD2 1098 C CE1 . HIS A 162 ? 0.2693 0.3409 0.2816 0.0186 0.0003 0.0568 197 HIS A CE1 1099 N NE2 . HIS A 162 ? 0.2684 0.3338 0.2837 0.0204 0.0047 0.0546 197 HIS A NE2 1100 N N . ALA A 163 ? 0.2098 0.2536 0.2090 0.0042 0.0030 0.0322 198 ALA A N 1101 C CA . ALA A 163 ? 0.2328 0.2799 0.2372 0.0039 0.0032 0.0316 198 ALA A CA 1102 C C . ALA A 163 ? 0.2295 0.2746 0.2382 0.0090 0.0078 0.0345 198 ALA A C 1103 O O . ALA A 163 ? 0.2246 0.2621 0.2306 0.0116 0.0112 0.0348 198 ALA A O 1104 C CB . ALA A 163 ? 0.2384 0.2795 0.2399 0.0003 0.0034 0.0259 198 ALA A CB 1105 N N . PRO A 164 ? 0.2374 0.2889 0.2524 0.0101 0.0082 0.0366 199 PRO A N 1106 C CA . PRO A 164 ? 0.2513 0.2995 0.2697 0.0148 0.0134 0.0384 199 PRO A CA 1107 C C . PRO A 164 ? 0.2407 0.2768 0.2543 0.0141 0.0172 0.0336 199 PRO A C 1108 O O . PRO A 164 ? 0.2403 0.2693 0.2529 0.0177 0.0220 0.0344 199 PRO A O 1109 C CB . PRO A 164 ? 0.2548 0.3121 0.2801 0.0144 0.0127 0.0398 199 PRO A CB 1110 C CG . PRO A 164 ? 0.2735 0.3415 0.3005 0.0109 0.0070 0.0413 199 PRO A CG 1111 C CD . PRO A 164 ? 0.2484 0.3106 0.2676 0.0071 0.0043 0.0375 199 PRO A CD 1112 N N . TYR A 165 ? 0.2224 0.2560 0.2327 0.0095 0.0151 0.0288 200 TYR A N 1113 C CA . TYR A 165 ? 0.2138 0.2377 0.2194 0.0082 0.0176 0.0244 200 TYR A CA 1114 C C . TYR A 165 ? 0.2014 0.2246 0.2037 0.0036 0.0141 0.0203 200 TYR A C 1115 O O . TYR A 165 ? 0.1982 0.2274 0.2018 0.0013 0.0105 0.0205 200 TYR A O 1116 C CB . TYR A 165 ? 0.2380 0.2592 0.2452 0.0095 0.0214 0.0238 200 TYR A CB 1117 C CG . TYR A 165 ? 0.2814 0.3081 0.2918 0.0072 0.0197 0.0230 200 TYR A CG 1118 C CD1 . TYR A 165 ? 0.3002 0.3236 0.3071 0.0034 0.0181 0.0190 200 TYR A CD1 1119 C CD2 . TYR A 165 ? 0.3505 0.3857 0.3674 0.0089 0.0199 0.0267 200 TYR A CD2 1120 C CE1 . TYR A 165 ? 0.3380 0.3651 0.3468 0.0011 0.0168 0.0184 200 TYR A CE1 1121 C CE2 . TYR A 165 ? 0.3741 0.4138 0.3935 0.0061 0.0185 0.0258 200 TYR A CE2 1122 C CZ . TYR A 165 ? 0.3826 0.4174 0.3974 0.0022 0.0171 0.0216 200 TYR A CZ 1123 O OH . TYR A 165 ? 0.4719 0.5096 0.4881 -0.0007 0.0160 0.0207 200 TYR A OH 1124 N N . MET A 166 ? 0.1961 0.2120 0.1940 0.0022 0.0154 0.0168 201 MET A N 1125 C CA . MET A 166 ? 0.1840 0.1985 0.1792 -0.0011 0.0131 0.0131 201 MET A CA 1126 C C . MET A 166 ? 0.1899 0.2003 0.1841 -0.0020 0.0148 0.0107 201 MET A C 1127 O O . MET A 166 ? 0.1881 0.1936 0.1806 -0.0009 0.0181 0.0102 201 MET A O 1128 C CB . MET A 166 ? 0.1909 0.2020 0.1822 -0.0020 0.0127 0.0115 201 MET A CB 1129 C CG . MET A 166 ? 0.1847 0.1949 0.1739 -0.0048 0.0105 0.0082 201 MET A CG 1130 S SD . MET A 166 ? 0.2063 0.2139 0.1918 -0.0058 0.0104 0.0064 201 MET A SD 1131 C CE . MET A 166 ? 0.2144 0.2166 0.1987 -0.0054 0.0139 0.0053 201 MET A CE 1132 N N . ARG A 167 ? 0.1775 0.1895 0.1720 -0.0042 0.0128 0.0092 202 ARG A N 1133 C CA . ARG A 167 ? 0.1740 0.1828 0.1670 -0.0052 0.0140 0.0074 202 ARG A CA 1134 C C . ARG A 167 ? 0.1679 0.1729 0.1573 -0.0067 0.0133 0.0045 202 ARG A C 1135 O O . ARG A 167 ? 0.1754 0.1813 0.1643 -0.0078 0.0109 0.0035 202 ARG A O 1136 C CB . ARG A 167 ? 0.1850 0.1968 0.1798 -0.0067 0.0122 0.0075 202 ARG A CB 1137 C CG . ARG A 167 ? 0.1962 0.2052 0.1893 -0.0076 0.0136 0.0063 202 ARG A CG 1138 C CD . ARG A 167 ? 0.2139 0.2254 0.2086 -0.0092 0.0123 0.0069 202 ARG A CD 1139 N NE . ARG A 167 ? 0.2190 0.2361 0.2182 -0.0086 0.0127 0.0095 202 ARG A NE 1140 C CZ . ARG A 167 ? 0.2073 0.2292 0.2090 -0.0101 0.0102 0.0105 202 ARG A CZ 1141 N NH1 . ARG A 167 ? 0.2306 0.2509 0.2300 -0.0127 0.0075 0.0088 202 ARG A NH1 1142 N NH2 . ARG A 167 ? 0.1960 0.2244 0.2024 -0.0093 0.0105 0.0133 202 ARG A NH2 1143 N N . PRO A 168 ? 0.1765 0.1774 0.1634 -0.0069 0.0155 0.0032 203 PRO A N 1144 C CA . PRO A 168 ? 0.1691 0.1680 0.1533 -0.0087 0.0147 0.0009 203 PRO A CA 1145 C C . PRO A 168 ? 0.1762 0.1761 0.1599 -0.0099 0.0129 0.0001 203 PRO A C 1146 O O . PRO A 168 ? 0.1783 0.1795 0.1634 -0.0097 0.0126 0.0012 203 PRO A O 1147 C CB . PRO A 168 ? 0.1900 0.1845 0.1713 -0.0091 0.0179 0.0000 203 PRO A CB 1148 C CG . PRO A 168 ? 0.1832 0.1767 0.1651 -0.0077 0.0203 0.0013 203 PRO A CG 1149 C CD . PRO A 168 ? 0.1720 0.1701 0.1583 -0.0058 0.0191 0.0038 203 PRO A CD 1150 N N . VAL A 169 ? 0.1745 0.1743 0.1568 -0.0111 0.0117 -0.0012 204 VAL A N 1151 C CA . VAL A 169 ? 0.1782 0.1787 0.1597 -0.0118 0.0101 -0.0014 204 VAL A CA 1152 C C . VAL A 169 ? 0.1911 0.1898 0.1694 -0.0133 0.0114 -0.0021 204 VAL A C 1153 O O . VAL A 169 ? 0.1982 0.1948 0.1745 -0.0142 0.0133 -0.0032 204 VAL A O 1154 C CB . VAL A 169 ? 0.1918 0.1941 0.1740 -0.0118 0.0079 -0.0019 204 VAL A CB 1155 C CG1 . VAL A 169 ? 0.2013 0.2039 0.1853 -0.0107 0.0068 -0.0015 204 VAL A CG1 1156 C CG2 . VAL A 169 ? 0.1811 0.1844 0.1629 -0.0127 0.0083 -0.0031 204 VAL A CG2 1157 N N . TYR A 170 ? 0.1863 0.1852 0.1632 -0.0138 0.0105 -0.0016 205 TYR A N 1158 C CA . TYR A 170 ? 0.1919 0.1896 0.1646 -0.0157 0.0112 -0.0023 205 TYR A CA 1159 C C . TYR A 170 ? 0.1853 0.1858 0.1571 -0.0171 0.0087 -0.0029 205 TYR A C 1160 O O . TYR A 170 ? 0.1899 0.1930 0.1643 -0.0158 0.0064 -0.0019 205 TYR A O 1161 C CB . TYR A 170 ? 0.1807 0.1777 0.1521 -0.0157 0.0112 -0.0010 205 TYR A CB 1162 C CG . TYR A 170 ? 0.1889 0.1841 0.1548 -0.0179 0.0124 -0.0018 205 TYR A CG 1163 C CD1 . TYR A 170 ? 0.1996 0.1911 0.1627 -0.0186 0.0161 -0.0030 205 TYR A CD1 1164 C CD2 . TYR A 170 ? 0.1972 0.1942 0.1604 -0.0191 0.0099 -0.0012 205 TYR A CD2 1165 C CE1 . TYR A 170 ? 0.2015 0.1903 0.1582 -0.0210 0.0176 -0.0042 205 TYR A CE1 1166 C CE2 . TYR A 170 ? 0.2054 0.2010 0.1625 -0.0217 0.0107 -0.0020 205 TYR A CE2 1167 C CZ . TYR A 170 ? 0.2190 0.2102 0.1725 -0.0229 0.0146 -0.0038 205 TYR A CZ 1168 O OH . TYR A 170 ? 0.2185 0.2075 0.1648 -0.0259 0.0157 -0.0050 205 TYR A OH 1169 N N . PRO A 171 ? 0.1896 0.1897 0.1576 -0.0198 0.0092 -0.0043 206 PRO A N 1170 C CA . PRO A 171 ? 0.1970 0.1923 0.1612 -0.0214 0.0127 -0.0060 206 PRO A CA 1171 C C . PRO A 171 ? 0.1968 0.1901 0.1629 -0.0206 0.0147 -0.0067 206 PRO A C 1172 O O . PRO A 171 ? 0.1940 0.1902 0.1632 -0.0203 0.0132 -0.0067 206 PRO A O 1173 C CB . PRO A 171 ? 0.2096 0.2057 0.1690 -0.0253 0.0119 -0.0077 206 PRO A CB 1174 C CG . PRO A 171 ? 0.2197 0.2222 0.1824 -0.0254 0.0082 -0.0069 206 PRO A CG 1175 C CD . PRO A 171 ? 0.2009 0.2056 0.1684 -0.0216 0.0065 -0.0046 206 PRO A CD 1176 N N . THR A 172 ? 0.1919 0.1801 0.1563 -0.0200 0.0184 -0.0071 207 THR A N 1177 C CA . THR A 172 ? 0.1938 0.1793 0.1598 -0.0185 0.0208 -0.0069 207 THR A CA 1178 C C . THR A 172 ? 0.2095 0.1915 0.1718 -0.0215 0.0224 -0.0091 207 THR A C 1179 O O . THR A 172 ? 0.2202 0.1956 0.1792 -0.0219 0.0266 -0.0101 207 THR A O 1180 C CB . THR A 172 ? 0.1955 0.1779 0.1625 -0.0155 0.0243 -0.0055 207 THR A CB 1181 O OG1 . THR A 172 ? 0.1918 0.1695 0.1539 -0.0168 0.0275 -0.0067 207 THR A OG1 1182 C CG2 . THR A 172 ? 0.1992 0.1863 0.1709 -0.0132 0.0221 -0.0032 207 THR A CG2 1183 N N . LYS A 173 ? 0.2216 0.2083 0.1850 -0.0235 0.0194 -0.0098 208 LYS A N 1184 C CA . LYS A 173 ? 0.2333 0.2190 0.1940 -0.0274 0.0199 -0.0118 208 LYS A CA 1185 C C . LYS A 173 ? 0.2191 0.2085 0.1844 -0.0263 0.0187 -0.0110 208 LYS A C 1186 O O . LYS A 173 ? 0.1943 0.1878 0.1642 -0.0232 0.0166 -0.0093 208 LYS A O 1187 C CB . LYS A 173 ? 0.2467 0.2371 0.2053 -0.0311 0.0170 -0.0129 208 LYS A CB 1188 C CG . LYS A 173 ? 0.2813 0.2684 0.2342 -0.0326 0.0180 -0.0138 208 LYS A CG 1189 C CD . LYS A 173 ? 0.3109 0.2904 0.2567 -0.0367 0.0218 -0.0167 208 LYS A CD 1190 C CE . LYS A 173 ? 0.3511 0.3285 0.2900 -0.0397 0.0222 -0.0181 208 LYS A CE 1191 N NZ . LYS A 173 ? 0.4178 0.3883 0.3488 -0.0451 0.0253 -0.0216 208 LYS A NZ 1192 N N . TPO A 174 ? 0.2135 0.2012 0.1770 -0.0295 0.0201 -0.0125 209 TPO A N 1193 C CA . TPO A 174 ? 0.2231 0.2132 0.1901 -0.0289 0.0200 -0.0119 209 TPO A CA 1194 C CB . TPO A 174 ? 0.2651 0.2512 0.2284 -0.0335 0.0226 -0.0139 209 TPO A CB 1195 C CG2 . TPO A 174 ? 0.2610 0.2486 0.2271 -0.0332 0.0232 -0.0132 209 TPO A CG2 1196 O OG1 . TPO A 174 ? 0.2980 0.2743 0.2565 -0.0333 0.0268 -0.0144 209 TPO A OG1 1197 P P . TPO A 174 ? 0.5702 0.5406 0.5215 -0.0386 0.0290 -0.0175 209 TPO A P 1198 O O1P . TPO A 174 ? 0.3757 0.3349 0.3233 -0.0363 0.0344 -0.0172 209 TPO A O1P 1199 O O2P . TPO A 174 ? 0.2943 0.2690 0.2450 -0.0387 0.0262 -0.0178 209 TPO A O2P 1200 O O3P . TPO A 174 ? 0.4014 0.3736 0.3512 -0.0447 0.0288 -0.0196 209 TPO A O3P 1201 C C . TPO A 174 ? 0.2061 0.2050 0.1781 -0.0281 0.0163 -0.0111 209 TPO A C 1202 O O . TPO A 174 ? 0.1901 0.1907 0.1655 -0.0248 0.0157 -0.0097 209 TPO A O 1203 N N . PHE A 175 ? 0.2031 0.2078 0.1755 -0.0310 0.0140 -0.0119 210 PHE A N 1204 C CA . PHE A 175 ? 0.2033 0.2166 0.1812 -0.0297 0.0112 -0.0108 210 PHE A CA 1205 C C . PHE A 175 ? 0.1903 0.2053 0.1711 -0.0250 0.0093 -0.0089 210 PHE A C 1206 O O . PHE A 175 ? 0.1851 0.2022 0.1695 -0.0223 0.0090 -0.0080 210 PHE A O 1207 C CB . PHE A 175 ? 0.2468 0.2676 0.2255 -0.0336 0.0088 -0.0113 210 PHE A CB 1208 C CG . PHE A 175 ? 0.2989 0.3221 0.2783 -0.0377 0.0101 -0.0127 210 PHE A CG 1209 C CD1 . PHE A 175 ? 0.3510 0.3661 0.3261 -0.0403 0.0137 -0.0143 210 PHE A CD1 1210 C CD2 . PHE A 175 ? 0.3646 0.3983 0.3492 -0.0390 0.0078 -0.0120 210 PHE A CD2 1211 C CE1 . PHE A 175 ? 0.3884 0.4051 0.3637 -0.0447 0.0151 -0.0155 210 PHE A CE1 1212 C CE2 . PHE A 175 ? 0.3803 0.4170 0.3659 -0.0433 0.0091 -0.0131 210 PHE A CE2 1213 C CZ . PHE A 175 ? 0.3719 0.3998 0.3526 -0.0464 0.0127 -0.0150 210 PHE A CZ 1214 N N . PRO A 176 ? 0.1682 0.1809 0.1467 -0.0243 0.0085 -0.0085 211 PRO A N 1215 C CA . PRO A 176 ? 0.1738 0.1872 0.1549 -0.0204 0.0072 -0.0067 211 PRO A CA 1216 C C . PRO A 176 ? 0.1669 0.1767 0.1490 -0.0178 0.0087 -0.0063 211 PRO A C 1217 O O . PRO A 176 ? 0.1683 0.1795 0.1530 -0.0153 0.0077 -0.0055 211 PRO A O 1218 C CB . PRO A 176 ? 0.1612 0.1721 0.1389 -0.0207 0.0068 -0.0064 211 PRO A CB 1219 C CG . PRO A 176 ? 0.1735 0.1857 0.1478 -0.0249 0.0065 -0.0077 211 PRO A CG 1220 C CD . PRO A 176 ? 0.1814 0.1922 0.1551 -0.0273 0.0086 -0.0094 211 PRO A CD 1221 N N . ASN A 177 ? 0.1826 0.1875 0.1623 -0.0184 0.0111 -0.0068 212 ASN A N 1222 C CA . ASN A 177 ? 0.1745 0.1770 0.1551 -0.0160 0.0122 -0.0059 212 ASN A CA 1223 C C . ASN A 177 ? 0.1826 0.1865 0.1646 -0.0157 0.0126 -0.0060 212 ASN A C 1224 O O . ASN A 177 ? 0.1768 0.1813 0.1601 -0.0137 0.0120 -0.0052 212 ASN A O 1225 C CB . ASN A 177 ? 0.1835 0.1809 0.1618 -0.0158 0.0147 -0.0055 212 ASN A CB 1226 C CG . ASN A 177 ? 0.1707 0.1675 0.1489 -0.0145 0.0144 -0.0046 212 ASN A CG 1227 O OD1 . ASN A 177 ? 0.1550 0.1530 0.1353 -0.0125 0.0135 -0.0032 212 ASN A OD1 1228 N ND2 . ASN A 177 ? 0.1701 0.1655 0.1457 -0.0162 0.0149 -0.0055 212 ASN A ND2 1229 N N . LEU A 178 ? 0.1971 0.2015 0.1785 -0.0182 0.0138 -0.0070 213 LEU A N 1230 C CA . LEU A 178 ? 0.2197 0.2258 0.2024 -0.0182 0.0145 -0.0071 213 LEU A CA 1231 C C . LEU A 178 ? 0.1899 0.2013 0.1761 -0.0165 0.0126 -0.0069 213 LEU A C 1232 O O . LEU A 178 ? 0.1920 0.2034 0.1787 -0.0148 0.0130 -0.0066 213 LEU A O 1233 C CB . LEU A 178 ? 0.2373 0.2429 0.2187 -0.0217 0.0164 -0.0082 213 LEU A CB 1234 C CG . LEU A 178 ? 0.2954 0.2934 0.2728 -0.0226 0.0194 -0.0081 213 LEU A CG 1235 C CD1 . LEU A 178 ? 0.3375 0.3347 0.3133 -0.0269 0.0214 -0.0095 213 LEU A CD1 1236 C CD2 . LEU A 178 ? 0.3234 0.3183 0.3003 -0.0196 0.0206 -0.0062 213 LEU A CD2 1237 N N . TYR A 179 ? 0.1753 0.1906 0.1632 -0.0167 0.0107 -0.0070 214 TYR A N 1238 C CA . TYR A 179 ? 0.1635 0.1832 0.1549 -0.0143 0.0095 -0.0065 214 TYR A CA 1239 C C . TYR A 179 ? 0.1655 0.1819 0.1563 -0.0115 0.0088 -0.0058 214 TYR A C 1240 O O . TYR A 179 ? 0.1656 0.1825 0.1576 -0.0095 0.0091 -0.0059 214 TYR A O 1241 C CB . TYR A 179 ? 0.1651 0.1911 0.1593 -0.0150 0.0077 -0.0060 214 TYR A CB 1242 C CG . TYR A 179 ? 0.1561 0.1877 0.1549 -0.0127 0.0076 -0.0053 214 TYR A CG 1243 C CD1 . TYR A 179 ? 0.1548 0.1884 0.1554 -0.0129 0.0096 -0.0059 214 TYR A CD1 1244 C CD2 . TYR A 179 ? 0.1592 0.1940 0.1607 -0.0099 0.0059 -0.0037 214 TYR A CD2 1245 C CE1 . TYR A 179 ? 0.1574 0.1963 0.1625 -0.0103 0.0102 -0.0053 214 TYR A CE1 1246 C CE2 . TYR A 179 ? 0.1595 0.1991 0.1655 -0.0070 0.0064 -0.0028 214 TYR A CE2 1247 C CZ . TYR A 179 ? 0.1567 0.1984 0.1647 -0.0071 0.0088 -0.0037 214 TYR A CZ 1248 O OH . TYR A 179 ? 0.1696 0.2163 0.1824 -0.0038 0.0099 -0.0028 214 TYR A OH 1249 N N . THR A 180 ? 0.1641 0.1771 0.1527 -0.0116 0.0083 -0.0054 215 THR A N 1250 C CA . THR A 180 ? 0.1668 0.1768 0.1547 -0.0099 0.0078 -0.0049 215 THR A CA 1251 C C . THR A 180 ? 0.1739 0.1820 0.1606 -0.0096 0.0088 -0.0052 215 THR A C 1252 O O . THR A 180 ? 0.1773 0.1845 0.1637 -0.0084 0.0086 -0.0055 215 THR A O 1253 C CB . THR A 180 ? 0.1705 0.1780 0.1568 -0.0103 0.0073 -0.0042 215 THR A CB 1254 O OG1 . THR A 180 ? 0.1593 0.1682 0.1460 -0.0103 0.0060 -0.0037 215 THR A OG1 1255 C CG2 . THR A 180 ? 0.1767 0.1820 0.1625 -0.0095 0.0070 -0.0037 215 THR A CG2 1256 N N . LEU A 181 ? 0.1697 0.1770 0.1552 -0.0106 0.0101 -0.0051 216 LEU A N 1257 C CA A LEU A 181 ? 0.1791 0.1851 0.1630 -0.0103 0.0110 -0.0048 216 LEU A CA 1258 C CA B LEU A 181 ? 0.1784 0.1844 0.1623 -0.0103 0.0109 -0.0048 216 LEU A CA 1259 C C . LEU A 181 ? 0.1791 0.1866 0.1634 -0.0098 0.0115 -0.0058 216 LEU A C 1260 O O . LEU A 181 ? 0.1913 0.1977 0.1738 -0.0093 0.0114 -0.0061 216 LEU A O 1261 C CB A LEU A 181 ? 0.1964 0.2008 0.1790 -0.0113 0.0128 -0.0042 216 LEU A CB 1262 C CB B LEU A 181 ? 0.1945 0.1988 0.1770 -0.0112 0.0127 -0.0041 216 LEU A CB 1263 C CG A LEU A 181 ? 0.2080 0.2113 0.1885 -0.0110 0.0138 -0.0033 216 LEU A CG 1264 C CG B LEU A 181 ? 0.1985 0.2005 0.1803 -0.0107 0.0129 -0.0026 216 LEU A CG 1265 C CD1 A LEU A 181 ? 0.2118 0.2150 0.1915 -0.0099 0.0123 -0.0019 216 LEU A CD1 1266 C CD1 B LEU A 181 ? 0.2190 0.2180 0.1995 -0.0115 0.0154 -0.0023 216 LEU A CD1 1267 C CD2 A LEU A 181 ? 0.2170 0.2175 0.1960 -0.0117 0.0161 -0.0024 216 LEU A CD2 1268 C CD2 B LEU A 181 ? 0.2082 0.2106 0.1895 -0.0095 0.0121 -0.0010 216 LEU A CD2 1269 N N . ALA A 182 ? 0.1639 0.1744 0.1504 -0.0102 0.0122 -0.0064 217 ALA A N 1270 C CA . ALA A 182 ? 0.1730 0.1858 0.1607 -0.0095 0.0134 -0.0072 217 ALA A CA 1271 C C . ALA A 182 ? 0.1758 0.1884 0.1645 -0.0072 0.0130 -0.0077 217 ALA A C 1272 O O . ALA A 182 ? 0.1789 0.1916 0.1673 -0.0062 0.0146 -0.0085 217 ALA A O 1273 C CB . ALA A 182 ? 0.1837 0.2011 0.1745 -0.0108 0.0141 -0.0074 217 ALA A CB 1274 N N . THR A 183 ? 0.1567 0.1684 0.1460 -0.0064 0.0113 -0.0071 218 THR A N 1275 C CA . THR A 183 ? 0.1595 0.1701 0.1498 -0.0040 0.0112 -0.0072 218 THR A CA 1276 C C . THR A 183 ? 0.1623 0.1677 0.1496 -0.0039 0.0104 -0.0073 218 THR A C 1277 O O . THR A 183 ? 0.1656 0.1680 0.1524 -0.0022 0.0111 -0.0077 218 THR A O 1278 C CB . THR A 183 ? 0.1645 0.1791 0.1585 -0.0029 0.0100 -0.0058 218 THR A CB 1279 O OG1 . THR A 183 ? 0.1648 0.1787 0.1578 -0.0046 0.0082 -0.0051 218 THR A OG1 1280 C CG2 . THR A 183 ? 0.1568 0.1781 0.1546 -0.0033 0.0106 -0.0056 218 THR A CG2 1281 N N . GLY A 184 ? 0.1570 0.1611 0.1426 -0.0057 0.0091 -0.0069 219 GLY A N 1282 C CA . GLY A 184 ? 0.1616 0.1619 0.1450 -0.0063 0.0081 -0.0068 219 GLY A CA 1283 C C . GLY A 184 ? 0.1690 0.1685 0.1538 -0.0054 0.0072 -0.0058 219 GLY A C 1284 O O . GLY A 184 ? 0.1778 0.1738 0.1610 -0.0060 0.0067 -0.0057 219 GLY A O 1285 N N . LEU A 185 ? 0.1574 0.1604 0.1448 -0.0045 0.0068 -0.0048 220 LEU A N 1286 C CA . LEU A 185 ? 0.1713 0.1742 0.1597 -0.0034 0.0059 -0.0034 220 LEU A CA 1287 C C . LEU A 185 ? 0.1602 0.1648 0.1484 -0.0051 0.0047 -0.0025 220 LEU A C 1288 O O . LEU A 185 ? 0.1585 0.1655 0.1468 -0.0066 0.0049 -0.0029 220 LEU A O 1289 C CB . LEU A 185 ? 0.1718 0.1785 0.1633 -0.0010 0.0061 -0.0026 220 LEU A CB 1290 C CG . LEU A 185 ? 0.1769 0.1811 0.1688 0.0015 0.0080 -0.0031 220 LEU A CG 1291 C CD1 . LEU A 185 ? 0.1785 0.1891 0.1750 0.0038 0.0084 -0.0021 220 LEU A CD1 1292 C CD2 . LEU A 185 ? 0.1869 0.1848 0.1770 0.0031 0.0083 -0.0025 220 LEU A CD2 1293 N N . TYR A 186 ? 0.1600 0.1626 0.1472 -0.0050 0.0039 -0.0012 221 TYR A N 1294 C CA . TYR A 186 ? 0.1506 0.1548 0.1371 -0.0063 0.0031 -0.0003 221 TYR A CA 1295 C C . TYR A 186 ? 0.1551 0.1642 0.1430 -0.0061 0.0023 0.0001 221 TYR A C 1296 O O . TYR A 186 ? 0.1548 0.1663 0.1450 -0.0040 0.0019 0.0009 221 TYR A O 1297 C CB . TYR A 186 ? 0.1630 0.1642 0.1479 -0.0060 0.0026 0.0012 221 TYR A CB 1298 C CG . TYR A 186 ? 0.1527 0.1496 0.1363 -0.0070 0.0032 0.0009 221 TYR A CG 1299 C CD1 . TYR A 186 ? 0.1621 0.1597 0.1455 -0.0089 0.0037 0.0003 221 TYR A CD1 1300 C CD2 . TYR A 186 ? 0.1644 0.1568 0.1471 -0.0063 0.0035 0.0012 221 TYR A CD2 1301 C CE1 . TYR A 186 ? 0.1633 0.1591 0.1465 -0.0102 0.0039 0.0003 221 TYR A CE1 1302 C CE2 . TYR A 186 ? 0.1674 0.1566 0.1488 -0.0083 0.0039 0.0007 221 TYR A CE2 1303 C CZ . TYR A 186 ? 0.1653 0.1571 0.1473 -0.0103 0.0039 0.0003 221 TYR A CZ 1304 O OH . TYR A 186 ? 0.1776 0.1679 0.1591 -0.0125 0.0039 0.0001 221 TYR A OH 1305 N N . PRO A 187 ? 0.1591 0.1701 0.1455 -0.0083 0.0021 -0.0001 222 PRO A N 1306 C CA . PRO A 187 ? 0.1616 0.1780 0.1488 -0.0092 0.0008 0.0003 222 PRO A CA 1307 C C . PRO A 187 ? 0.1765 0.1959 0.1650 -0.0072 -0.0010 0.0027 222 PRO A C 1308 O O . PRO A 187 ? 0.1764 0.2020 0.1679 -0.0064 -0.0021 0.0036 222 PRO A O 1309 C CB . PRO A 187 ? 0.1691 0.1846 0.1528 -0.0124 0.0012 -0.0006 222 PRO A CB 1310 C CG . PRO A 187 ? 0.1645 0.1755 0.1474 -0.0126 0.0033 -0.0019 222 PRO A CG 1311 C CD . PRO A 187 ? 0.1719 0.1804 0.1562 -0.0103 0.0033 -0.0011 222 PRO A CD 1312 N N . GLU A 188 ? 0.1888 0.2044 0.1753 -0.0061 -0.0013 0.0042 223 GLU A N 1313 C CA . GLU A 188 ? 0.1858 0.2032 0.1729 -0.0038 -0.0029 0.0072 223 GLU A CA 1314 C C . GLU A 188 ? 0.1912 0.2099 0.1827 0.0000 -0.0024 0.0081 223 GLU A C 1315 O O . GLU A 188 ? 0.1953 0.2188 0.1892 0.0024 -0.0038 0.0108 223 GLU A O 1316 C CB . GLU A 188 ? 0.1960 0.2077 0.1798 -0.0035 -0.0027 0.0087 223 GLU A CB 1317 C CG . GLU A 188 ? 0.1885 0.1933 0.1722 -0.0024 -0.0009 0.0079 223 GLU A CG 1318 C CD . GLU A 188 ? 0.2001 0.1994 0.1808 -0.0025 -0.0005 0.0096 223 GLU A CD 1319 O OE1 . GLU A 188 ? 0.2016 0.2021 0.1798 -0.0033 -0.0016 0.0115 223 GLU A OE1 1320 O OE2 . GLU A 188 ? 0.1968 0.1906 0.1772 -0.0023 0.0008 0.0089 223 GLU A OE2 1321 N N . SER A 189 ? 0.1840 0.1989 0.1763 0.0006 -0.0004 0.0061 224 SER A N 1322 C CA . SER A 189 ? 0.1929 0.2077 0.1883 0.0040 0.0009 0.0063 224 SER A CA 1323 C C . SER A 189 ? 0.2122 0.2339 0.2115 0.0039 0.0012 0.0052 224 SER A C 1324 O O . SER A 189 ? 0.2321 0.2579 0.2354 0.0071 0.0016 0.0067 224 SER A O 1325 C CB . SER A 189 ? 0.1904 0.1969 0.1836 0.0044 0.0030 0.0044 224 SER A CB 1326 O OG . SER A 189 ? 0.2102 0.2104 0.2006 0.0050 0.0031 0.0058 224 SER A OG 1327 N N . HIS A 190 ? 0.1895 0.2123 0.1877 0.0004 0.0014 0.0029 225 HIS A N 1328 C CA . HIS A 190 ? 0.1764 0.2053 0.1779 -0.0002 0.0021 0.0020 225 HIS A CA 1329 C C . HIS A 190 ? 0.1838 0.2217 0.1878 -0.0019 0.0000 0.0034 225 HIS A C 1330 O O . HIS A 190 ? 0.1985 0.2434 0.2067 -0.0018 0.0001 0.0035 225 HIS A O 1331 C CB . HIS A 190 ? 0.1771 0.2030 0.1765 -0.0028 0.0037 -0.0006 225 HIS A CB 1332 C CG . HIS A 190 ? 0.1582 0.1819 0.1540 -0.0064 0.0032 -0.0015 225 HIS A CG 1333 N ND1 . HIS A 190 ? 0.1598 0.1874 0.1551 -0.0092 0.0021 -0.0015 225 HIS A ND1 1334 C CD2 . HIS A 190 ? 0.1593 0.1775 0.1520 -0.0076 0.0042 -0.0027 225 HIS A CD2 1335 C CE1 . HIS A 190 ? 0.1656 0.1889 0.1572 -0.0117 0.0029 -0.0028 225 HIS A CE1 1336 N NE2 . HIS A 190 ? 0.1641 0.1823 0.1546 -0.0104 0.0041 -0.0032 225 HIS A NE2 1337 N N . GLY A 191 ? 0.1641 0.2022 0.1653 -0.0035 -0.0021 0.0045 226 GLY A N 1338 C CA . GLY A 191 ? 0.1815 0.2282 0.1841 -0.0054 -0.0047 0.0060 226 GLY A CA 1339 C C . GLY A 191 ? 0.1696 0.2172 0.1687 -0.0110 -0.0051 0.0037 226 GLY A C 1340 O O . GLY A 191 ? 0.1723 0.2253 0.1701 -0.0137 -0.0075 0.0046 226 GLY A O 1341 N N . ILE A 192 ? 0.1687 0.2106 0.1655 -0.0130 -0.0027 0.0009 227 ILE A N 1342 C CA . ILE A 192 ? 0.1712 0.2121 0.1641 -0.0181 -0.0022 -0.0013 227 ILE A CA 1343 C C . ILE A 192 ? 0.1732 0.2066 0.1604 -0.0189 -0.0017 -0.0018 227 ILE A C 1344 O O . ILE A 192 ? 0.1701 0.1967 0.1553 -0.0186 0.0005 -0.0031 227 ILE A O 1345 C CB . ILE A 192 ? 0.1787 0.2174 0.1722 -0.0194 0.0003 -0.0034 227 ILE A CB 1346 C CG1 . ILE A 192 ? 0.1811 0.2271 0.1809 -0.0178 0.0004 -0.0026 227 ILE A CG1 1347 C CG2 . ILE A 192 ? 0.1882 0.2254 0.1777 -0.0248 0.0012 -0.0056 227 ILE A CG2 1348 C CD1 . ILE A 192 ? 0.1857 0.2427 0.1892 -0.0196 -0.0019 -0.0013 227 ILE A CD1 1349 N N . VAL A 193 ? 0.1836 0.2193 0.1685 -0.0197 -0.0039 -0.0004 228 VAL A N 1350 C CA . VAL A 193 ? 0.1816 0.2110 0.1611 -0.0202 -0.0033 -0.0005 228 VAL A CA 1351 C C . VAL A 193 ? 0.1848 0.2106 0.1585 -0.0249 -0.0018 -0.0030 228 VAL A C 1352 O O . VAL A 193 ? 0.2007 0.2209 0.1699 -0.0253 -0.0005 -0.0034 228 VAL A O 1353 C CB . VAL A 193 ? 0.1883 0.2205 0.1669 -0.0187 -0.0060 0.0024 228 VAL A CB 1354 C CG1 . VAL A 193 ? 0.1974 0.2311 0.1813 -0.0137 -0.0066 0.0050 228 VAL A CG1 1355 C CG2 . VAL A 193 ? 0.1955 0.2353 0.1725 -0.0221 -0.0089 0.0032 228 VAL A CG2 1356 N N . GLY A 194 ? 0.2001 0.2288 0.1736 -0.0284 -0.0017 -0.0048 229 GLY A N 1357 C CA . GLY A 194 ? 0.1989 0.2224 0.1664 -0.0331 0.0006 -0.0077 229 GLY A CA 1358 C C . GLY A 194 ? 0.2181 0.2439 0.1870 -0.0363 0.0014 -0.0096 229 GLY A C 1359 O O . GLY A 194 ? 0.1988 0.2322 0.1735 -0.0355 -0.0003 -0.0084 229 GLY A O 1360 N N . ASN A 195 ? 0.2142 0.2329 0.1776 -0.0400 0.0045 -0.0123 230 ASN A N 1361 C CA . ASN A 195 ? 0.2358 0.2557 0.1982 -0.0451 0.0054 -0.0145 230 ASN A CA 1362 C C . ASN A 195 ? 0.2408 0.2697 0.2023 -0.0501 0.0018 -0.0146 230 ASN A C 1363 O O . ASN A 195 ? 0.2430 0.2779 0.2071 -0.0535 0.0010 -0.0153 230 ASN A O 1364 C CB . ASN A 195 ? 0.2405 0.2491 0.1957 -0.0482 0.0100 -0.0175 230 ASN A CB 1365 C CG . ASN A 195 ? 0.2428 0.2441 0.1998 -0.0440 0.0137 -0.0171 230 ASN A CG 1366 O OD1 . ASN A 195 ? 0.2274 0.2321 0.1906 -0.0398 0.0128 -0.0151 230 ASN A OD1 1367 N ND2 . ASN A 195 ? 0.2496 0.2405 0.2009 -0.0450 0.0180 -0.0188 230 ASN A ND2 1368 N N . SER A 196 ? 0.2285 0.2586 0.1859 -0.0509 -0.0002 -0.0140 231 SER A N 1369 C CA . SER A 196 ? 0.2573 0.2976 0.2141 -0.0548 -0.0046 -0.0131 231 SER A CA 1370 C C . SER A 196 ? 0.2449 0.2913 0.2053 -0.0497 -0.0081 -0.0091 231 SER A C 1371 O O . SER A 196 ? 0.2589 0.2986 0.2173 -0.0459 -0.0068 -0.0083 231 SER A O 1372 C CB . SER A 196 ? 0.2829 0.3183 0.2291 -0.0615 -0.0039 -0.0162 231 SER A CB 1373 O OG . SER A 196 ? 0.3227 0.3544 0.2657 -0.0674 -0.0013 -0.0197 231 SER A OG 1374 N N . MET A 197 ? 0.2258 0.2848 0.1919 -0.0494 -0.0123 -0.0063 232 MET A N 1375 C CA . MET A 197 ? 0.2407 0.3057 0.2105 -0.0442 -0.0155 -0.0018 232 MET A CA 1376 C C . MET A 197 ? 0.2475 0.3266 0.2200 -0.0465 -0.0205 0.0008 232 MET A C 1377 O O . MET A 197 ? 0.2435 0.3307 0.2190 -0.0507 -0.0216 0.0000 232 MET A O 1378 C CB . MET A 197 ? 0.2580 0.3235 0.2364 -0.0370 -0.0145 0.0003 232 MET A CB 1379 C CG . MET A 197 ? 0.2729 0.3283 0.2517 -0.0348 -0.0102 -0.0019 232 MET A CG 1380 S SD . MET A 197 ? 0.2351 0.2931 0.2229 -0.0272 -0.0100 0.0009 232 MET A SD 1381 C CE . MET A 197 ? 0.2386 0.3044 0.2331 -0.0285 -0.0093 0.0001 232 MET A CE 1382 N N . TYR A 198 ? 0.2352 0.3180 0.2070 -0.0436 -0.0235 0.0046 233 TYR A N 1383 C CA . TYR A 198 ? 0.2372 0.3347 0.2131 -0.0438 -0.0287 0.0088 233 TYR A CA 1384 C C . TYR A 198 ? 0.2327 0.3333 0.2163 -0.0349 -0.0295 0.0140 233 TYR A C 1385 O O . TYR A 198 ? 0.2220 0.3136 0.2028 -0.0306 -0.0280 0.0152 233 TYR A O 1386 C CB . TYR A 198 ? 0.2478 0.3473 0.2144 -0.0488 -0.0319 0.0093 233 TYR A CB 1387 C CG . TYR A 198 ? 0.2506 0.3660 0.2215 -0.0480 -0.0377 0.0148 233 TYR A CG 1388 C CD1 . TYR A 198 ? 0.2683 0.3981 0.2443 -0.0523 -0.0409 0.0152 233 TYR A CD1 1389 C CD2 . TYR A 198 ? 0.2609 0.3776 0.2314 -0.0427 -0.0400 0.0199 233 TYR A CD2 1390 C CE1 . TYR A 198 ? 0.2769 0.4231 0.2581 -0.0511 -0.0464 0.0209 233 TYR A CE1 1391 C CE2 . TYR A 198 ? 0.2697 0.4014 0.2447 -0.0412 -0.0453 0.0257 233 TYR A CE2 1392 C CZ . TYR A 198 ? 0.2841 0.4311 0.2647 -0.0453 -0.0486 0.0263 233 TYR A CZ 1393 O OH . TYR A 198 ? 0.3138 0.4775 0.2997 -0.0436 -0.0542 0.0326 233 TYR A OH 1394 N N . ASP A 199 ? 0.2157 0.3286 0.2089 -0.0322 -0.0314 0.0171 234 ASP A N 1395 C CA . ASP A 199 ? 0.2093 0.3250 0.2099 -0.0236 -0.0318 0.0221 234 ASP A CA 1396 C C . ASP A 199 ? 0.2280 0.3579 0.2313 -0.0227 -0.0371 0.0278 234 ASP A C 1397 O O . ASP A 199 ? 0.2059 0.3501 0.2143 -0.0257 -0.0400 0.0290 234 ASP A O 1398 C CB . ASP A 199 ? 0.2053 0.3232 0.2152 -0.0198 -0.0289 0.0216 234 ASP A CB 1399 C CG . ASP A 199 ? 0.2047 0.3222 0.2211 -0.0107 -0.0279 0.0259 234 ASP A CG 1400 O OD1 . ASP A 199 ? 0.2212 0.3464 0.2402 -0.0072 -0.0310 0.0312 234 ASP A OD1 1401 O OD2 . ASP A 199 ? 0.2083 0.3174 0.2268 -0.0070 -0.0238 0.0241 234 ASP A OD2 1402 N N . PRO A 200 ? 0.2479 0.3745 0.2477 -0.0187 -0.0384 0.0318 235 PRO A N 1403 C CA . PRO A 200 ? 0.2717 0.4118 0.2731 -0.0178 -0.0438 0.0379 235 PRO A CA 1404 C C . PRO A 200 ? 0.2705 0.4232 0.2845 -0.0106 -0.0450 0.0436 235 PRO A C 1405 O O . PRO A 200 ? 0.2770 0.4450 0.2944 -0.0109 -0.0498 0.0485 235 PRO A O 1406 C CB . PRO A 200 ? 0.2859 0.4165 0.2793 -0.0154 -0.0439 0.0403 235 PRO A CB 1407 C CG . PRO A 200 ? 0.2953 0.4088 0.2858 -0.0131 -0.0385 0.0365 235 PRO A CG 1408 C CD . PRO A 200 ? 0.2622 0.3729 0.2557 -0.0159 -0.0353 0.0308 235 PRO A CD 1409 N N . VAL A 201 ? 0.2542 0.4009 0.2747 -0.0044 -0.0406 0.0431 236 VAL A N 1410 C CA . VAL A 201 ? 0.2496 0.4072 0.2823 0.0025 -0.0404 0.0478 236 VAL A CA 1411 C C . VAL A 201 ? 0.2539 0.4258 0.2934 -0.0023 -0.0416 0.0459 236 VAL A C 1412 O O . VAL A 201 ? 0.2436 0.4328 0.2918 -0.0005 -0.0448 0.0509 236 VAL A O 1413 C CB . VAL A 201 ? 0.2470 0.3918 0.2828 0.0101 -0.0347 0.0471 236 VAL A CB 1414 C CG1 . VAL A 201 ? 0.2487 0.4038 0.2970 0.0169 -0.0332 0.0506 236 VAL A CG1 1415 C CG2 . VAL A 201 ? 0.2663 0.3989 0.2965 0.0151 -0.0338 0.0499 236 VAL A CG2 1416 N N . PHE A 202 ? 0.2301 0.3954 0.2661 -0.0086 -0.0390 0.0392 237 PHE A N 1417 C CA . PHE A 202 ? 0.2483 0.4261 0.2895 -0.0145 -0.0400 0.0371 237 PHE A CA 1418 C C . PHE A 202 ? 0.2729 0.4617 0.3097 -0.0232 -0.0455 0.0373 237 PHE A C 1419 O O . PHE A 202 ? 0.2709 0.4757 0.3141 -0.0272 -0.0480 0.0382 237 PHE A O 1420 C CB . PHE A 202 ? 0.2396 0.4062 0.2773 -0.0191 -0.0354 0.0301 237 PHE A CB 1421 C CG . PHE A 202 ? 0.2143 0.3692 0.2545 -0.0124 -0.0300 0.0288 237 PHE A CG 1422 C CD1 . PHE A 202 ? 0.2192 0.3761 0.2669 -0.0031 -0.0286 0.0333 237 PHE A CD1 1423 C CD2 . PHE A 202 ? 0.2070 0.3487 0.2417 -0.0156 -0.0261 0.0230 237 PHE A CD2 1424 C CE1 . PHE A 202 ? 0.2115 0.3567 0.2602 0.0019 -0.0234 0.0313 237 PHE A CE1 1425 C CE2 . PHE A 202 ? 0.2116 0.3431 0.2478 -0.0103 -0.0215 0.0216 237 PHE A CE2 1426 C CZ . PHE A 202 ? 0.2111 0.3442 0.2539 -0.0019 -0.0202 0.0255 237 PHE A CZ 1427 N N . ASP A 203 ? 0.2776 0.4578 0.3030 -0.0264 -0.0471 0.0363 238 ASP A N 1428 C CA . ASP A 203 ? 0.2856 0.4716 0.3029 -0.0360 -0.0514 0.0347 238 ASP A CA 1429 C C . ASP A 203 ? 0.2777 0.4635 0.2936 -0.0447 -0.0496 0.0284 238 ASP A C 1430 O O . ASP A 203 ? 0.2818 0.4825 0.3008 -0.0511 -0.0531 0.0287 238 ASP A O 1431 C CB . ASP A 203 ? 0.3192 0.5254 0.3413 -0.0361 -0.0580 0.0413 238 ASP A CB 1432 C CG . ASP A 203 ? 0.3508 0.5620 0.3625 -0.0468 -0.0627 0.0394 238 ASP A CG 1433 O OD1 . ASP A 203 ? 0.3845 0.5809 0.3836 -0.0517 -0.0608 0.0344 238 ASP A OD1 1434 O OD2 . ASP A 203 ? 0.4000 0.6303 0.4161 -0.0506 -0.0681 0.0428 238 ASP A OD2 1435 N N . ALA A 204 ? 0.2453 0.4143 0.2567 -0.0448 -0.0442 0.0231 239 ALA A N 1436 C CA . ALA A 204 ? 0.2401 0.4046 0.2495 -0.0516 -0.0411 0.0172 239 ALA A CA 1437 C C . ALA A 204 ? 0.2554 0.3993 0.2551 -0.0522 -0.0364 0.0122 239 ALA A C 1438 O O . ALA A 204 ? 0.2266 0.3609 0.2243 -0.0459 -0.0348 0.0135 239 ALA A O 1439 C CB . ALA A 204 ? 0.2338 0.4042 0.2549 -0.0478 -0.0386 0.0179 239 ALA A CB 1440 N N . SER A 205 ? 0.2606 0.3984 0.2546 -0.0598 -0.0340 0.0067 240 SER A N 1441 C CA . SER A 205 ? 0.2766 0.3959 0.2616 -0.0609 -0.0292 0.0020 240 SER A CA 1442 C C . SER A 205 ? 0.2696 0.3831 0.2581 -0.0609 -0.0246 -0.0010 240 SER A C 1443 O O . SER A 205 ? 0.2786 0.4007 0.2717 -0.0651 -0.0250 -0.0017 240 SER A O 1444 C CB . SER A 205 ? 0.3041 0.4188 0.2770 -0.0701 -0.0298 -0.0018 240 SER A CB 1445 O OG . SER A 205 ? 0.3321 0.4501 0.3001 -0.0699 -0.0337 0.0009 240 SER A OG 1446 N N . PHE A 206 ? 0.2504 0.3497 0.2365 -0.0564 -0.0203 -0.0025 241 PHE A N 1447 C CA . PHE A 206 ? 0.2517 0.3432 0.2397 -0.0554 -0.0157 -0.0051 241 PHE A CA 1448 C C . PHE A 206 ? 0.2894 0.3669 0.2670 -0.0605 -0.0122 -0.0097 241 PHE A C 1449 O O . PHE A 206 ? 0.2625 0.3324 0.2331 -0.0601 -0.0119 -0.0102 241 PHE A O 1450 C CB . PHE A 206 ? 0.2472 0.3330 0.2391 -0.0464 -0.0139 -0.0030 241 PHE A CB 1451 C CG . PHE A 206 ? 0.2192 0.2963 0.2123 -0.0443 -0.0094 -0.0050 241 PHE A CG 1452 C CD1 . PHE A 206 ? 0.2254 0.2890 0.2114 -0.0455 -0.0059 -0.0079 241 PHE A CD1 1453 C CD2 . PHE A 206 ? 0.2127 0.2951 0.2140 -0.0402 -0.0085 -0.0034 241 PHE A CD2 1454 C CE1 . PHE A 206 ? 0.2315 0.2877 0.2185 -0.0430 -0.0022 -0.0090 241 PHE A CE1 1455 C CE2 . PHE A 206 ? 0.2079 0.2824 0.2094 -0.0383 -0.0046 -0.0050 241 PHE A CE2 1456 C CZ . PHE A 206 ? 0.2138 0.2754 0.2082 -0.0396 -0.0017 -0.0076 241 PHE A CZ 1457 N N . HIS A 207 ? 0.2995 0.3732 0.2761 -0.0649 -0.0090 -0.0127 242 HIS A N 1458 C CA . HIS A 207 ? 0.3410 0.4001 0.3081 -0.0691 -0.0048 -0.0169 242 HIS A CA 1459 C C . HIS A 207 ? 0.3520 0.4040 0.3211 -0.0679 -0.0002 -0.0182 242 HIS A C 1460 O O . HIS A 207 ? 0.3358 0.3954 0.3124 -0.0669 -0.0005 -0.0170 242 HIS A O 1461 C CB . HIS A 207 ? 0.3645 0.4249 0.3243 -0.0790 -0.0056 -0.0200 242 HIS A CB 1462 C CG . HIS A 207 ? 0.3904 0.4559 0.3456 -0.0812 -0.0098 -0.0192 242 HIS A CG 1463 N ND1 . HIS A 207 ? 0.4186 0.4749 0.3668 -0.0787 -0.0088 -0.0194 242 HIS A ND1 1464 C CD2 . HIS A 207 ? 0.3807 0.4604 0.3372 -0.0857 -0.0150 -0.0177 242 HIS A CD2 1465 C CE1 . HIS A 207 ? 0.3976 0.4614 0.3425 -0.0815 -0.0131 -0.0182 242 HIS A CE1 1466 N NE2 . HIS A 207 ? 0.3963 0.4745 0.3460 -0.0858 -0.0172 -0.0171 242 HIS A NE2 1467 N N . LEU A 208 ? 0.3936 0.4311 0.3559 -0.0678 0.0041 -0.0205 243 LEU A N 1468 C CA . LEU A 208 ? 0.4544 0.4838 0.4175 -0.0663 0.0086 -0.0213 243 LEU A CA 1469 C C . LEU A 208 ? 0.4799 0.5116 0.4425 -0.0737 0.0098 -0.0234 243 LEU A C 1470 O O . LEU A 208 ? 0.4717 0.5040 0.4387 -0.0725 0.0117 -0.0228 243 LEU A O 1471 C CB . LEU A 208 ? 0.4893 0.5032 0.4453 -0.0644 0.0130 -0.0228 243 LEU A CB 1472 C CG . LEU A 208 ? 0.5655 0.5719 0.5233 -0.0602 0.0169 -0.0221 243 LEU A CG 1473 C CD1 . LEU A 208 ? 0.5834 0.5820 0.5400 -0.0538 0.0186 -0.0208 243 LEU A CD1 1474 C CD2 . LEU A 208 ? 0.5860 0.5834 0.5383 -0.0656 0.0214 -0.0247 243 LEU A CD2 1475 N N . ARG A 209 ? 0.5016 0.5353 0.4589 -0.0816 0.0086 -0.0258 244 ARG A N 1476 C CA . ARG A 209 ? 0.5438 0.5821 0.5011 -0.0898 0.0089 -0.0277 244 ARG A CA 1477 C C . ARG A 209 ? 0.5216 0.5792 0.4865 -0.0920 0.0031 -0.0256 244 ARG A C 1478 O O . ARG A 209 ? 0.5112 0.5756 0.4764 -0.0904 -0.0010 -0.0239 244 ARG A O 1479 C CB . ARG A 209 ? 0.6411 0.6683 0.5866 -0.0984 0.0117 -0.0322 244 ARG A CB 1480 C CG . ARG A 209 ? 0.7206 0.7285 0.6590 -0.0966 0.0184 -0.0341 244 ARG A CG 1481 C CD . ARG A 209 ? 0.8023 0.7979 0.7283 -0.1051 0.0218 -0.0388 244 ARG A CD 1482 N NE . ARG A 209 ? 0.8997 0.8766 0.8187 -0.1015 0.0282 -0.0400 244 ARG A NE 1483 C CZ . ARG A 209 ? 0.9641 0.9291 0.8809 -0.1013 0.0339 -0.0407 244 ARG A CZ 1484 N NH1 . ARG A 209 ? 0.9822 0.9508 0.9026 -0.1051 0.0344 -0.0406 244 ARG A NH1 1485 N NH2 . ARG A 209 ? 0.9900 0.9391 0.9009 -0.0971 0.0393 -0.0411 244 ARG A NH2 1486 N N . GLY A 210 ? 0.4895 0.5562 0.4606 -0.0954 0.0030 -0.0252 245 GLY A N 1487 C CA . GLY A 210 ? 0.4689 0.5556 0.4490 -0.0972 -0.0020 -0.0227 245 GLY A CA 1488 C C . GLY A 210 ? 0.4502 0.5465 0.4422 -0.0894 -0.0023 -0.0188 245 GLY A C 1489 O O . GLY A 210 ? 0.4064 0.4937 0.3993 -0.0827 0.0010 -0.0182 245 GLY A O 1490 N N . ARG A 211 ? 0.4362 0.5511 0.4372 -0.0905 -0.0063 -0.0161 246 ARG A N 1491 C CA . ARG A 211 ? 0.4473 0.5736 0.4603 -0.0845 -0.0062 -0.0127 246 ARG A CA 1492 C C . ARG A 211 ? 0.3684 0.4989 0.3868 -0.0743 -0.0087 -0.0087 246 ARG A C 1493 O O . ARG A 211 ? 0.3365 0.4704 0.3626 -0.0674 -0.0072 -0.0063 246 ARG A O 1494 C CB . ARG A 211 ? 0.5269 0.6719 0.5476 -0.0912 -0.0087 -0.0117 246 ARG A CB 1495 C CG . ARG A 211 ? 0.6241 0.7863 0.6590 -0.0852 -0.0098 -0.0072 246 ARG A CG 1496 C CD . ARG A 211 ? 0.7112 0.8676 0.7500 -0.0798 -0.0044 -0.0071 246 ARG A CD 1497 N NE . ARG A 211 ? 0.8087 0.9642 0.8470 -0.0873 -0.0008 -0.0096 246 ARG A NE 1498 C CZ . ARG A 211 ? 0.8440 1.0157 0.8909 -0.0922 -0.0013 -0.0085 246 ARG A CZ 1499 N NH1 . ARG A 211 ? 0.8810 1.0728 0.9386 -0.0901 -0.0054 -0.0046 246 ARG A NH1 1500 N NH2 . ARG A 211 ? 0.8292 0.9971 0.8739 -0.0993 0.0025 -0.0111 246 ARG A NH2 1501 N N . GLU A 212 ? 0.3107 0.4402 0.3245 -0.0737 -0.0121 -0.0080 247 GLU A N 1502 C CA . GLU A 212 ? 0.2909 0.4256 0.3096 -0.0652 -0.0149 -0.0038 247 GLU A CA 1503 C C . GLU A 212 ? 0.2644 0.3878 0.2838 -0.0565 -0.0112 -0.0034 247 GLU A C 1504 O O . GLU A 212 ? 0.2533 0.3824 0.2803 -0.0492 -0.0116 0.0000 247 GLU A O 1505 C CB . GLU A 212 ? 0.2890 0.4220 0.3005 -0.0668 -0.0185 -0.0035 247 GLU A CB 1506 C CG . GLU A 212 ? 0.2892 0.4269 0.3050 -0.0584 -0.0214 0.0010 247 GLU A CG 1507 C CD . GLU A 212 ? 0.3017 0.4580 0.3297 -0.0550 -0.0242 0.0058 247 GLU A CD 1508 O OE1 . GLU A 212 ? 0.3213 0.4915 0.3525 -0.0614 -0.0271 0.0063 247 GLU A OE1 1509 O OE2 . GLU A 212 ? 0.2653 0.4226 0.2999 -0.0461 -0.0233 0.0091 247 GLU A OE2 1510 N N . LYS A 213 ? 0.2557 0.3630 0.2670 -0.0575 -0.0077 -0.0067 248 LYS A N 1511 C CA . LYS A 213 ? 0.2492 0.3454 0.2600 -0.0504 -0.0044 -0.0066 248 LYS A CA 1512 C C . LYS A 213 ? 0.2454 0.3455 0.2638 -0.0464 -0.0018 -0.0055 248 LYS A C 1513 O O . LYS A 213 ? 0.2318 0.3262 0.2512 -0.0397 -0.0002 -0.0045 248 LYS A O 1514 C CB . LYS A 213 ? 0.2611 0.3412 0.2626 -0.0529 -0.0010 -0.0100 248 LYS A CB 1515 C CG . LYS A 213 ? 0.2675 0.3443 0.2666 -0.0593 0.0021 -0.0128 248 LYS A CG 1516 C CD . LYS A 213 ? 0.2984 0.3586 0.2891 -0.0596 0.0060 -0.0152 248 LYS A CD 1517 C CE . LYS A 213 ? 0.3381 0.3930 0.3264 -0.0645 0.0099 -0.0173 248 LYS A CE 1518 N NZ . LYS A 213 ? 0.3501 0.4062 0.3339 -0.0736 0.0096 -0.0198 248 LYS A NZ 1519 N N . PHE A 214 ? 0.2527 0.3619 0.2758 -0.0508 -0.0012 -0.0058 249 PHE A N 1520 C CA . PHE A 214 ? 0.2793 0.3934 0.3097 -0.0473 0.0015 -0.0046 249 PHE A CA 1521 C C . PHE A 214 ? 0.2675 0.3939 0.3075 -0.0408 -0.0002 -0.0007 249 PHE A C 1522 O O . PHE A 214 ? 0.2747 0.4036 0.3203 -0.0364 0.0026 0.0001 249 PHE A O 1523 C CB . PHE A 214 ? 0.3188 0.4392 0.3515 -0.0545 0.0031 -0.0060 249 PHE A CB 1524 C CG . PHE A 214 ? 0.3571 0.4638 0.3807 -0.0602 0.0063 -0.0096 249 PHE A CG 1525 C CD1 . PHE A 214 ? 0.4194 0.5142 0.4396 -0.0570 0.0105 -0.0105 249 PHE A CD1 1526 C CD2 . PHE A 214 ? 0.4224 0.5277 0.4402 -0.0686 0.0052 -0.0119 249 PHE A CD2 1527 C CE1 . PHE A 214 ? 0.4174 0.4996 0.4295 -0.0615 0.0136 -0.0131 249 PHE A CE1 1528 C CE2 . PHE A 214 ? 0.4232 0.5145 0.4323 -0.0733 0.0088 -0.0151 249 PHE A CE2 1529 C CZ . PHE A 214 ? 0.4267 0.5065 0.4333 -0.0693 0.0130 -0.0154 249 PHE A CZ 1530 N N . ASN A 215 ? 0.2374 0.3716 0.2792 -0.0401 -0.0046 0.0015 250 ASN A N 1531 C CA . ASN A 215 ? 0.2239 0.3684 0.2745 -0.0328 -0.0060 0.0058 250 ASN A CA 1532 C C . ASN A 215 ? 0.2102 0.3428 0.2585 -0.0247 -0.0038 0.0063 250 ASN A C 1533 O O . ASN A 215 ? 0.2008 0.3220 0.2414 -0.0242 -0.0045 0.0051 250 ASN A O 1534 C CB . ASN A 215 ? 0.2338 0.3895 0.2860 -0.0344 -0.0115 0.0087 250 ASN A CB 1535 C CG . ASN A 215 ? 0.2822 0.4529 0.3385 -0.0425 -0.0139 0.0087 250 ASN A CG 1536 O OD1 . ASN A 215 ? 0.2948 0.4725 0.3572 -0.0444 -0.0114 0.0083 250 ASN A OD1 1537 N ND2 . ASN A 215 ? 0.3344 0.5102 0.3869 -0.0477 -0.0185 0.0091 250 ASN A ND2 1538 N N . HIS A 216 ? 0.2040 0.3391 0.2586 -0.0186 -0.0010 0.0078 251 HIS A N 1539 C CA . HIS A 216 ? 0.2043 0.3278 0.2563 -0.0117 0.0013 0.0078 251 HIS A CA 1540 C C . HIS A 216 ? 0.1901 0.3111 0.2406 -0.0071 -0.0013 0.0104 251 HIS A C 1541 O O . HIS A 216 ? 0.1802 0.2887 0.2255 -0.0038 0.0000 0.0095 251 HIS A O 1542 C CB . HIS A 216 ? 0.2166 0.3430 0.2750 -0.0063 0.0055 0.0087 251 HIS A CB 1543 C CG . HIS A 216 ? 0.2179 0.3597 0.2871 -0.0021 0.0047 0.0129 251 HIS A CG 1544 N ND1 . HIS A 216 ? 0.2255 0.3682 0.2976 0.0049 0.0037 0.0165 251 HIS A ND1 1545 C CD2 . HIS A 216 ? 0.2327 0.3899 0.3109 -0.0036 0.0051 0.0146 251 HIS A CD2 1546 C CE1 . HIS A 216 ? 0.2317 0.3898 0.3144 0.0081 0.0034 0.0204 251 HIS A CE1 1547 N NE2 . HIS A 216 ? 0.2316 0.3994 0.3186 0.0028 0.0042 0.0193 251 HIS A NE2 1548 N N . ARG A 217 ? 0.1737 0.3064 0.2284 -0.0075 -0.0053 0.0137 252 ARG A N 1549 C CA . ARG A 217 ? 0.1839 0.3152 0.2375 -0.0030 -0.0080 0.0170 252 ARG A CA 1550 C C . ARG A 217 ? 0.1811 0.2974 0.2244 -0.0044 -0.0084 0.0146 252 ARG A C 1551 O O . ARG A 217 ? 0.1946 0.3050 0.2360 0.0003 -0.0087 0.0165 252 ARG A O 1552 C CB . ARG A 217 ? 0.1815 0.3279 0.2394 -0.0048 -0.0129 0.0208 252 ARG A CB 1553 C CG . ARG A 217 ? 0.1811 0.3311 0.2341 -0.0143 -0.0161 0.0184 252 ARG A CG 1554 C CD . ARG A 217 ? 0.1919 0.3586 0.2497 -0.0156 -0.0214 0.0228 252 ARG A CD 1555 N NE . ARG A 217 ? 0.1949 0.3656 0.2472 -0.0253 -0.0247 0.0204 252 ARG A NE 1556 C CZ . ARG A 217 ? 0.2091 0.3937 0.2630 -0.0287 -0.0299 0.0234 252 ARG A CZ 1557 N NH1 . ARG A 217 ? 0.2104 0.4077 0.2723 -0.0227 -0.0328 0.0296 252 ARG A NH1 1558 N NH2 . ARG A 217 ? 0.2227 0.4086 0.2699 -0.0383 -0.0323 0.0204 252 ARG A NH2 1559 N N . TRP A 218 ? 0.1824 0.2928 0.2192 -0.0109 -0.0081 0.0108 253 TRP A N 1560 C CA . TRP A 218 ? 0.1730 0.2711 0.2006 -0.0128 -0.0085 0.0087 253 TRP A CA 1561 C C . TRP A 218 ? 0.1846 0.2694 0.2088 -0.0091 -0.0051 0.0070 253 TRP A C 1562 O O . TRP A 218 ? 0.1852 0.2612 0.2037 -0.0086 -0.0055 0.0066 253 TRP A O 1563 C CB . TRP A 218 ? 0.1805 0.2763 0.2024 -0.0206 -0.0087 0.0053 253 TRP A CB 1564 C CG . TRP A 218 ? 0.1820 0.2887 0.2044 -0.0258 -0.0124 0.0062 253 TRP A CG 1565 C CD1 . TRP A 218 ? 0.1967 0.3146 0.2239 -0.0302 -0.0131 0.0060 253 TRP A CD1 1566 C CD2 . TRP A 218 ? 0.1913 0.2993 0.2089 -0.0280 -0.0160 0.0073 253 TRP A CD2 1567 N NE1 . TRP A 218 ? 0.2006 0.3271 0.2263 -0.0352 -0.0172 0.0069 253 TRP A NE1 1568 C CE2 . TRP A 218 ? 0.1974 0.3179 0.2169 -0.0339 -0.0190 0.0078 253 TRP A CE2 1569 C CE3 . TRP A 218 ? 0.2016 0.3014 0.2131 -0.0260 -0.0168 0.0081 253 TRP A CE3 1570 C CZ2 . TRP A 218 ? 0.2045 0.3294 0.2193 -0.0379 -0.0231 0.0088 253 TRP A CZ2 1571 C CZ3 . TRP A 218 ? 0.2076 0.3115 0.2147 -0.0295 -0.0205 0.0092 253 TRP A CZ3 1572 C CH2 . TRP A 218 ? 0.2053 0.3214 0.2136 -0.0355 -0.0236 0.0094 253 TRP A CH2 1573 N N . TRP A 219 ? 0.1671 0.2512 0.1946 -0.0070 -0.0019 0.0060 254 TRP A N 1574 C CA . TRP A 219 ? 0.1725 0.2446 0.1955 -0.0058 0.0011 0.0035 254 TRP A CA 1575 C C . TRP A 219 ? 0.1787 0.2470 0.2036 0.0005 0.0029 0.0049 254 TRP A C 1576 O O . TRP A 219 ? 0.1862 0.2598 0.2167 0.0038 0.0047 0.0060 254 TRP A O 1577 C CB . TRP A 219 ? 0.1717 0.2442 0.1952 -0.0088 0.0037 0.0012 254 TRP A CB 1578 C CG . TRP A 219 ? 0.1720 0.2476 0.1935 -0.0154 0.0027 -0.0002 254 TRP A CG 1579 C CD1 . TRP A 219 ? 0.1802 0.2672 0.2060 -0.0188 0.0010 0.0005 254 TRP A CD1 1580 C CD2 . TRP A 219 ? 0.1690 0.2358 0.1836 -0.0195 0.0035 -0.0027 254 TRP A CD2 1581 N NE1 . TRP A 219 ? 0.1827 0.2675 0.2038 -0.0255 0.0008 -0.0017 254 TRP A NE1 1582 C CE2 . TRP A 219 ? 0.1650 0.2369 0.1792 -0.0256 0.0027 -0.0037 254 TRP A CE2 1583 C CE3 . TRP A 219 ? 0.1652 0.2206 0.1741 -0.0187 0.0050 -0.0041 254 TRP A CE3 1584 C CZ2 . TRP A 219 ? 0.1795 0.2437 0.1871 -0.0304 0.0039 -0.0062 254 TRP A CZ2 1585 C CZ3 . TRP A 219 ? 0.1759 0.2252 0.1793 -0.0229 0.0060 -0.0061 254 TRP A CZ3 1586 C CH2 . TRP A 219 ? 0.1755 0.2283 0.1780 -0.0285 0.0057 -0.0072 254 TRP A CH2 1587 N N . GLY A 220 ? 0.1684 0.2268 0.1882 0.0020 0.0029 0.0046 255 GLY A N 1588 C CA . GLY A 220 ? 0.1767 0.2292 0.1967 0.0073 0.0048 0.0054 255 GLY A CA 1589 C C . GLY A 220 ? 0.1730 0.2158 0.1884 0.0069 0.0076 0.0024 255 GLY A C 1590 O O . GLY A 220 ? 0.1904 0.2324 0.2038 0.0034 0.0082 0.0002 255 GLY A O 1591 N N . GLY A 221 ? 0.1782 0.2134 0.1917 0.0104 0.0093 0.0024 256 GLY A N 1592 C CA . GLY A 221 ? 0.1804 0.2071 0.1892 0.0097 0.0116 -0.0003 256 GLY A CA 1593 C C . GLY A 221 ? 0.1865 0.2159 0.1970 0.0098 0.0144 -0.0018 256 GLY A C 1594 O O . GLY A 221 ? 0.1971 0.2345 0.2136 0.0119 0.0154 -0.0005 256 GLY A O 1595 N N . GLN A 222 ? 0.1697 0.1932 0.1752 0.0076 0.0158 -0.0044 257 GLN A N 1596 C CA . GLN A 222 ? 0.1790 0.2037 0.1846 0.0074 0.0187 -0.0059 257 GLN A CA 1597 C C . GLN A 222 ? 0.1622 0.1844 0.1632 0.0032 0.0182 -0.0075 257 GLN A C 1598 O O . GLN A 222 ? 0.1887 0.2039 0.1843 0.0022 0.0181 -0.0087 257 GLN A O 1599 C CB . GLN A 222 ? 0.1984 0.2169 0.2018 0.0106 0.0222 -0.0071 257 GLN A CB 1600 C CG . GLN A 222 ? 0.2081 0.2288 0.2117 0.0106 0.0257 -0.0086 257 GLN A CG 1601 C CD . GLN A 222 ? 0.2320 0.2454 0.2320 0.0135 0.0296 -0.0103 257 GLN A CD 1602 O OE1 . GLN A 222 ? 0.2241 0.2305 0.2170 0.0112 0.0307 -0.0127 257 GLN A OE1 1603 N NE2 . GLN A 222 ? 0.2548 0.2696 0.2594 0.0184 0.0320 -0.0090 257 GLN A NE2 1604 N N . PRO A 223 ? 0.1563 0.1840 0.1593 0.0006 0.0178 -0.0072 258 PRO A N 1605 C CA . PRO A 223 ? 0.1544 0.1789 0.1531 -0.0028 0.0175 -0.0081 258 PRO A CA 1606 C C . PRO A 223 ? 0.1670 0.1885 0.1621 -0.0030 0.0203 -0.0095 258 PRO A C 1607 O O . PRO A 223 ? 0.1694 0.1925 0.1661 -0.0009 0.0230 -0.0100 258 PRO A O 1608 C CB . PRO A 223 ? 0.1638 0.1945 0.1656 -0.0056 0.0169 -0.0075 258 PRO A CB 1609 C CG . PRO A 223 ? 0.1589 0.1975 0.1670 -0.0038 0.0178 -0.0066 258 PRO A CG 1610 C CD . PRO A 223 ? 0.1592 0.1963 0.1685 0.0003 0.0175 -0.0059 258 PRO A CD 1611 N N . LEU A 224 ? 0.1643 0.1818 0.1546 -0.0052 0.0197 -0.0098 259 LEU A N 1612 C CA . LEU A 224 ? 0.1854 0.1992 0.1707 -0.0058 0.0216 -0.0107 259 LEU A CA 1613 C C . LEU A 224 ? 0.1928 0.2100 0.1793 -0.0058 0.0249 -0.0112 259 LEU A C 1614 O O . LEU A 224 ? 0.2016 0.2166 0.1852 -0.0048 0.0273 -0.0124 259 LEU A O 1615 C CB . LEU A 224 ? 0.1962 0.2072 0.1774 -0.0081 0.0203 -0.0099 259 LEU A CB 1616 C CG . LEU A 224 ? 0.2119 0.2195 0.1870 -0.0089 0.0214 -0.0103 259 LEU A CG 1617 C CD1 . LEU A 224 ? 0.2275 0.2313 0.1991 -0.0081 0.0207 -0.0117 259 LEU A CD1 1618 C CD2 . LEU A 224 ? 0.2160 0.2223 0.1886 -0.0104 0.0200 -0.0085 259 LEU A CD2 1619 N N . TRP A 225 ? 0.1912 0.2137 0.1818 -0.0074 0.0253 -0.0103 260 TRP A N 1620 C CA . TRP A 225 ? 0.2002 0.2267 0.1926 -0.0080 0.0286 -0.0106 260 TRP A CA 1621 C C . TRP A 225 ? 0.2067 0.2373 0.2035 -0.0047 0.0309 -0.0111 260 TRP A C 1622 O O . TRP A 225 ? 0.2066 0.2380 0.2028 -0.0042 0.0345 -0.0118 260 TRP A O 1623 C CB . TRP A 225 ? 0.2001 0.2314 0.1958 -0.0113 0.0285 -0.0097 260 TRP A CB 1624 C CG . TRP A 225 ? 0.1909 0.2279 0.1924 -0.0117 0.0260 -0.0090 260 TRP A CG 1625 C CD1 . TRP A 225 ? 0.2182 0.2641 0.2267 -0.0112 0.0264 -0.0085 260 TRP A CD1 1626 C CD2 . TRP A 225 ? 0.1990 0.2337 0.1994 -0.0129 0.0229 -0.0086 260 TRP A CD2 1627 N NE1 . TRP A 225 ? 0.2174 0.2668 0.2287 -0.0123 0.0232 -0.0077 260 TRP A NE1 1628 C CE2 . TRP A 225 ? 0.1983 0.2403 0.2043 -0.0134 0.0213 -0.0080 260 TRP A CE2 1629 C CE3 . TRP A 225 ? 0.2040 0.2317 0.1993 -0.0135 0.0215 -0.0086 260 TRP A CE3 1630 C CZ2 . TRP A 225 ? 0.2028 0.2443 0.2083 -0.0148 0.0184 -0.0077 260 TRP A CZ2 1631 C CZ3 . TRP A 225 ? 0.2081 0.2353 0.2037 -0.0145 0.0190 -0.0082 260 TRP A CZ3 1632 C CH2 . TRP A 225 ? 0.2017 0.2354 0.2019 -0.0153 0.0176 -0.0080 260 TRP A CH2 1633 N N . ILE A 226 ? 0.1837 0.2162 0.1846 -0.0021 0.0292 -0.0105 261 ILE A N 1634 C CA . ILE A 226 ? 0.1837 0.2191 0.1890 0.0020 0.0314 -0.0104 261 ILE A CA 1635 C C . ILE A 226 ? 0.1865 0.2131 0.1858 0.0043 0.0333 -0.0121 261 ILE A C 1636 O O . ILE A 226 ? 0.1942 0.2204 0.1936 0.0067 0.0374 -0.0130 261 ILE A O 1637 C CB . ILE A 226 ? 0.1897 0.2305 0.2015 0.0040 0.0288 -0.0084 261 ILE A CB 1638 C CG1 . ILE A 226 ? 0.2017 0.2523 0.2192 0.0009 0.0271 -0.0070 261 ILE A CG1 1639 C CG2 . ILE A 226 ? 0.1928 0.2352 0.2087 0.0094 0.0314 -0.0078 261 ILE A CG2 1640 C CD1 . ILE A 226 ? 0.2081 0.2669 0.2305 0.0002 0.0303 -0.0068 261 ILE A CD1 1641 N N . THR A 227 ? 0.1836 0.2031 0.1775 0.0033 0.0307 -0.0127 262 THR A N 1642 C CA . THR A 227 ? 0.1922 0.2029 0.1791 0.0040 0.0322 -0.0147 262 THR A CA 1643 C C . THR A 227 ? 0.1960 0.2047 0.1775 0.0025 0.0354 -0.0164 262 THR A C 1644 O O . THR A 227 ? 0.1990 0.2034 0.1771 0.0043 0.0390 -0.0182 262 THR A O 1645 C CB . THR A 227 ? 0.2010 0.2062 0.1830 0.0017 0.0285 -0.0149 262 THR A CB 1646 O OG1 . THR A 227 ? 0.1833 0.1904 0.1699 0.0030 0.0258 -0.0132 262 THR A OG1 1647 C CG2 . THR A 227 ? 0.2116 0.2083 0.1864 0.0016 0.0297 -0.0171 262 THR A CG2 1648 N N . ALA A 228 ? 0.1991 0.2104 0.1795 -0.0005 0.0345 -0.0156 263 ALA A N 1649 C CA . ALA A 228 ? 0.2109 0.2206 0.1858 -0.0022 0.0374 -0.0166 263 ALA A CA 1650 C C . ALA A 228 ? 0.2231 0.2369 0.2017 0.0000 0.0423 -0.0171 263 ALA A C 1651 O O . ALA A 228 ? 0.2382 0.2478 0.2119 0.0009 0.0461 -0.0191 263 ALA A O 1652 C CB . ALA A 228 ? 0.2039 0.2152 0.1773 -0.0056 0.0355 -0.0150 263 ALA A CB 1653 N N . THR A 229 ? 0.2203 0.2427 0.2077 0.0006 0.0425 -0.0155 264 THR A N 1654 C CA . THR A 229 ? 0.2467 0.2752 0.2393 0.0026 0.0472 -0.0155 264 THR A CA 1655 C C . THR A 229 ? 0.2527 0.2786 0.2462 0.0075 0.0506 -0.0166 264 THR A C 1656 O O . THR A 229 ? 0.2460 0.2713 0.2381 0.0091 0.0558 -0.0179 264 THR A O 1657 C CB . THR A 229 ? 0.2599 0.2996 0.2627 0.0021 0.0461 -0.0132 264 THR A CB 1658 O OG1 . THR A 229 ? 0.2994 0.3397 0.3006 -0.0026 0.0434 -0.0124 264 THR A OG1 1659 C CG2 . THR A 229 ? 0.2819 0.3292 0.2904 0.0034 0.0510 -0.0129 264 THR A CG2 1660 N N . LYS A 230 ? 0.2223 0.2457 0.2176 0.0100 0.0482 -0.0162 265 LYS A N 1661 C CA . LYS A 230 ? 0.2503 0.2693 0.2458 0.0150 0.0516 -0.0171 265 LYS A CA 1662 C C . LYS A 230 ? 0.2621 0.2697 0.2465 0.0143 0.0548 -0.0205 265 LYS A C 1663 O O . LYS A 230 ? 0.2759 0.2792 0.2592 0.0180 0.0598 -0.0219 265 LYS A O 1664 C CB . LYS A 230 ? 0.2579 0.2748 0.2559 0.0171 0.0481 -0.0157 265 LYS A CB 1665 C CG . LYS A 230 ? 0.2617 0.2899 0.2707 0.0189 0.0456 -0.0123 265 LYS A CG 1666 C CD . LYS A 230 ? 0.2849 0.3100 0.2947 0.0208 0.0422 -0.0109 265 LYS A CD 1667 C CE . LYS A 230 ? 0.2931 0.3295 0.3130 0.0227 0.0396 -0.0072 265 LYS A CE 1668 N NZ . LYS A 230 ? 0.2995 0.3426 0.3274 0.0285 0.0435 -0.0053 265 LYS A NZ 1669 N N . GLN A 231 ? 0.2486 0.2513 0.2246 0.0095 0.0521 -0.0217 266 GLN A N 1670 C CA . GLN A 231 ? 0.2547 0.2473 0.2192 0.0078 0.0542 -0.0249 266 GLN A CA 1671 C C . GLN A 231 ? 0.2733 0.2668 0.2325 0.0050 0.0569 -0.0257 266 GLN A C 1672 O O . GLN A 231 ? 0.2803 0.2666 0.2289 0.0023 0.0574 -0.0280 266 GLN A O 1673 C CB . GLN A 231 ? 0.2543 0.2409 0.2128 0.0045 0.0491 -0.0253 266 GLN A CB 1674 C CG . GLN A 231 ? 0.2722 0.2557 0.2341 0.0073 0.0478 -0.0250 266 GLN A CG 1675 C CD . GLN A 231 ? 0.2642 0.2425 0.2211 0.0040 0.0431 -0.0253 266 GLN A CD 1676 O OE1 . GLN A 231 ? 0.2759 0.2485 0.2237 0.0003 0.0424 -0.0274 266 GLN A OE1 1677 N NE2 . GLN A 231 ? 0.2496 0.2305 0.2126 0.0052 0.0397 -0.0232 266 GLN A NE2 1678 N N . GLY A 232 ? 0.2650 0.2675 0.2313 0.0054 0.0584 -0.0238 267 GLY A N 1679 C CA . GLY A 232 ? 0.2796 0.2833 0.2415 0.0032 0.0619 -0.0243 267 GLY A CA 1680 C C . GLY A 232 ? 0.2875 0.2906 0.2437 -0.0016 0.0582 -0.0232 267 GLY A C 1681 O O . GLY A 232 ? 0.3012 0.3019 0.2499 -0.0038 0.0606 -0.0239 267 GLY A O 1682 N N . VAL A 233 ? 0.2711 0.2762 0.2306 -0.0029 0.0527 -0.0212 268 VAL A N 1683 C CA . VAL A 233 ? 0.2578 0.2627 0.2134 -0.0067 0.0493 -0.0195 268 VAL A CA 1684 C C . VAL A 233 ? 0.2772 0.2896 0.2413 -0.0074 0.0485 -0.0170 268 VAL A C 1685 O O . VAL A 233 ? 0.2733 0.2894 0.2448 -0.0062 0.0460 -0.0161 268 VAL A O 1686 C CB . VAL A 233 ? 0.2617 0.2621 0.2134 -0.0078 0.0441 -0.0193 268 VAL A CB 1687 C CG1 . VAL A 233 ? 0.2723 0.2734 0.2218 -0.0107 0.0408 -0.0167 268 VAL A CG1 1688 C CG2 . VAL A 233 ? 0.2798 0.2728 0.2220 -0.0084 0.0449 -0.0219 268 VAL A CG2 1689 N N A ARG A 234 ? 0.2716 0.2858 0.2340 -0.0098 0.0506 -0.0159 269 ARG A N 1690 N N B ARG A 234 ? 0.2590 0.2733 0.2216 -0.0098 0.0507 -0.0159 269 ARG A N 1691 C CA A ARG A 234 ? 0.2811 0.3020 0.2509 -0.0114 0.0508 -0.0140 269 ARG A CA 1692 C CA B ARG A 234 ? 0.2572 0.2782 0.2272 -0.0113 0.0508 -0.0140 269 ARG A CA 1693 C C A ARG A 234 ? 0.2644 0.2840 0.2347 -0.0133 0.0461 -0.0122 269 ARG A C 1694 C C B ARG A 234 ? 0.2512 0.2709 0.2216 -0.0133 0.0461 -0.0123 269 ARG A C 1695 O O A ARG A 234 ? 0.2552 0.2694 0.2187 -0.0145 0.0441 -0.0114 269 ARG A O 1696 O O B ARG A 234 ? 0.2434 0.2575 0.2069 -0.0145 0.0441 -0.0114 269 ARG A O 1697 C CB A ARG A 234 ? 0.3126 0.3344 0.2793 -0.0137 0.0551 -0.0135 269 ARG A CB 1698 C CB B ARG A 234 ? 0.2675 0.2900 0.2352 -0.0137 0.0551 -0.0134 269 ARG A CB 1699 C CG A ARG A 234 ? 0.3556 0.3862 0.3311 -0.0137 0.0589 -0.0133 269 ARG A CG 1700 C CG B ARG A 234 ? 0.2776 0.3071 0.2529 -0.0161 0.0558 -0.0119 269 ARG A CG 1701 C CD A ARG A 234 ? 0.3869 0.4177 0.3588 -0.0137 0.0648 -0.0142 269 ARG A CD 1702 C CD B ARG A 234 ? 0.2958 0.3268 0.2689 -0.0185 0.0609 -0.0114 269 ARG A CD 1703 N NE A ARG A 234 ? 0.4129 0.4366 0.3736 -0.0163 0.0654 -0.0136 269 ARG A NE 1704 N NE B ARG A 234 ? 0.3222 0.3545 0.2944 -0.0160 0.0656 -0.0131 269 ARG A NE 1705 C CZ A ARG A 234 ? 0.4239 0.4418 0.3753 -0.0156 0.0675 -0.0151 269 ARG A CZ 1706 C CZ B ARG A 234 ? 0.3373 0.3777 0.3181 -0.0140 0.0690 -0.0137 269 ARG A CZ 1707 N NH1 A ARG A 234 ? 0.4572 0.4743 0.4088 -0.0124 0.0698 -0.0177 269 ARG A NH1 1708 N NH1 B ARG A 234 ? 0.3546 0.3944 0.3331 -0.0115 0.0740 -0.0153 269 ARG A NH1 1709 N NH2 A ARG A 234 ? 0.4292 0.4418 0.3707 -0.0182 0.0675 -0.0140 269 ARG A NH2 1710 N NH2 B ARG A 234 ? 0.3364 0.3856 0.3278 -0.0144 0.0675 -0.0126 269 ARG A NH2 1711 N N . ALA A 235 ? 0.2505 0.2755 0.2289 -0.0134 0.0445 -0.0116 270 ALA A N 1712 C CA . ALA A 235 ? 0.2692 0.2929 0.2483 -0.0152 0.0408 -0.0103 270 ALA A CA 1713 C C . ALA A 235 ? 0.2874 0.3142 0.2692 -0.0187 0.0423 -0.0092 270 ALA A C 1714 O O . ALA A 235 ? 0.3026 0.3364 0.2903 -0.0195 0.0446 -0.0095 270 ALA A O 1715 C CB . ALA A 235 ? 0.2723 0.2985 0.2570 -0.0133 0.0376 -0.0106 270 ALA A CB 1716 N N . GLY A 236 ? 0.2923 0.3140 0.2699 -0.0210 0.0413 -0.0078 271 GLY A N 1717 C CA . GLY A 236 ? 0.3247 0.3473 0.3041 -0.0248 0.0425 -0.0070 271 GLY A CA 1718 C C . GLY A 236 ? 0.3318 0.3587 0.3174 -0.0255 0.0398 -0.0076 271 GLY A C 1719 O O . GLY A 236 ? 0.3396 0.3674 0.3271 -0.0227 0.0369 -0.0081 271 GLY A O 1720 N N . THR A 237 ? 0.3210 0.3506 0.3094 -0.0296 0.0407 -0.0076 272 THR A N 1721 C CA . THR A 237 ? 0.3188 0.3522 0.3118 -0.0312 0.0380 -0.0082 272 THR A CA 1722 C C . THR A 237 ? 0.3197 0.3445 0.3076 -0.0311 0.0360 -0.0078 272 THR A C 1723 O O . THR A 237 ? 0.3331 0.3508 0.3160 -0.0331 0.0378 -0.0070 272 THR A O 1724 C CB . THR A 237 ? 0.3445 0.3833 0.3410 -0.0366 0.0398 -0.0086 272 THR A CB 1725 O OG1 . THR A 237 ? 0.3653 0.4130 0.3672 -0.0363 0.0421 -0.0086 272 THR A OG1 1726 C CG2 . THR A 237 ? 0.3731 0.4167 0.3737 -0.0389 0.0366 -0.0093 272 THR A CG2 1727 N N . PHE A 238 ? 0.3197 0.3453 0.3093 -0.0286 0.0326 -0.0082 273 PHE A N 1728 C CA . PHE A 238 ? 0.3274 0.3457 0.3129 -0.0276 0.0308 -0.0077 273 PHE A CA 1729 C C . PHE A 238 ? 0.3547 0.3701 0.3391 -0.0315 0.0309 -0.0082 273 PHE A C 1730 O O . PHE A 238 ? 0.3762 0.3840 0.3563 -0.0310 0.0310 -0.0075 273 PHE A O 1731 C CB . PHE A 238 ? 0.3194 0.3397 0.3070 -0.0240 0.0275 -0.0080 273 PHE A CB 1732 C CG . PHE A 238 ? 0.3028 0.3207 0.2880 -0.0202 0.0271 -0.0075 273 PHE A CG 1733 C CD1 . PHE A 238 ? 0.2940 0.3121 0.2775 -0.0197 0.0295 -0.0074 273 PHE A CD1 1734 C CD2 . PHE A 238 ? 0.2862 0.3014 0.2703 -0.0178 0.0245 -0.0073 273 PHE A CD2 1735 C CE1 . PHE A 238 ? 0.2768 0.2923 0.2570 -0.0171 0.0290 -0.0074 273 PHE A CE1 1736 C CE2 . PHE A 238 ? 0.2896 0.3027 0.2710 -0.0154 0.0240 -0.0071 273 PHE A CE2 1737 C CZ . PHE A 238 ? 0.2702 0.2834 0.2494 -0.0151 0.0261 -0.0074 273 PHE A CZ 1738 N N . PHE A 239 ? 0.3614 0.3829 0.3495 -0.0353 0.0310 -0.0093 274 PHE A N 1739 C CA . PHE A 239 ? 0.3571 0.3765 0.3437 -0.0397 0.0307 -0.0104 274 PHE A CA 1740 C C . PHE A 239 ? 0.3363 0.3532 0.3208 -0.0453 0.0341 -0.0110 274 PHE A C 1741 O O . PHE A 239 ? 0.3107 0.3320 0.2975 -0.0466 0.0360 -0.0106 274 PHE A O 1742 C CB . PHE A 239 ? 0.4163 0.4452 0.4083 -0.0406 0.0275 -0.0112 274 PHE A CB 1743 C CG . PHE A 239 ? 0.4356 0.4661 0.4294 -0.0352 0.0246 -0.0105 274 PHE A CG 1744 C CD1 . PHE A 239 ? 0.5134 0.5378 0.5037 -0.0338 0.0230 -0.0106 274 PHE A CD1 1745 C CD2 . PHE A 239 ? 0.4507 0.4877 0.4492 -0.0315 0.0239 -0.0098 274 PHE A CD2 1746 C CE1 . PHE A 239 ? 0.5616 0.5870 0.5533 -0.0293 0.0206 -0.0098 274 PHE A CE1 1747 C CE2 . PHE A 239 ? 0.4615 0.4985 0.4609 -0.0269 0.0217 -0.0092 274 PHE A CE2 1748 C CZ . PHE A 239 ? 0.4997 0.5309 0.4956 -0.0260 0.0199 -0.0092 274 PHE A CZ 1749 N N . TRP A 240 ? 0.2914 0.3003 0.2709 -0.0487 0.0351 -0.0119 275 TRP A N 1750 C CA . TRP A 240 ? 0.2971 0.2995 0.2725 -0.0542 0.0391 -0.0124 275 TRP A CA 1751 C C . TRP A 240 ? 0.2841 0.2860 0.2579 -0.0603 0.0386 -0.0149 275 TRP A C 1752 O O . TRP A 240 ? 0.2917 0.2886 0.2624 -0.0594 0.0375 -0.0157 275 TRP A O 1753 C CB . TRP A 240 ? 0.2967 0.2858 0.2653 -0.0516 0.0421 -0.0108 275 TRP A CB 1754 C CG . TRP A 240 ? 0.2798 0.2693 0.2489 -0.0458 0.0419 -0.0083 275 TRP A CG 1755 C CD1 . TRP A 240 ? 0.2849 0.2752 0.2548 -0.0400 0.0392 -0.0071 275 TRP A CD1 1756 C CD2 . TRP A 240 ? 0.2779 0.2672 0.2459 -0.0459 0.0445 -0.0068 275 TRP A CD2 1757 N NE1 . TRP A 240 ? 0.2729 0.2634 0.2419 -0.0368 0.0398 -0.0052 275 TRP A NE1 1758 C CE2 . TRP A 240 ? 0.2708 0.2606 0.2385 -0.0401 0.0431 -0.0049 275 TRP A CE2 1759 C CE3 . TRP A 240 ? 0.2735 0.2622 0.2406 -0.0507 0.0481 -0.0069 275 TRP A CE3 1760 C CZ2 . TRP A 240 ? 0.2791 0.2688 0.2450 -0.0389 0.0450 -0.0031 275 TRP A CZ2 1761 C CZ3 . TRP A 240 ? 0.2810 0.2694 0.2466 -0.0493 0.0503 -0.0049 275 TRP A CZ3 1762 C CH2 . TRP A 240 ? 0.2825 0.2715 0.2473 -0.0434 0.0487 -0.0031 275 TRP A CH2 1763 N N . SER A 241 ? 0.3032 0.3109 0.2790 -0.0669 0.0395 -0.0162 276 SER A N 1764 C CA . SER A 241 ? 0.3074 0.3131 0.2799 -0.0743 0.0397 -0.0189 276 SER A CA 1765 C C . SER A 241 ? 0.3330 0.3215 0.2962 -0.0751 0.0434 -0.0196 276 SER A C 1766 O O . SER A 241 ? 0.3220 0.3010 0.2816 -0.0727 0.0471 -0.0179 276 SER A O 1767 C CB . SER A 241 ? 0.3283 0.3412 0.3036 -0.0820 0.0411 -0.0199 276 SER A CB 1768 O OG . SER A 241 ? 0.3391 0.3691 0.3236 -0.0812 0.0373 -0.0192 276 SER A OG 1769 N N . VAL A 242 ? 0.3545 0.3389 0.3134 -0.0783 0.0427 -0.0219 277 VAL A N 1770 C CA . VAL A 242 ? 0.3893 0.3572 0.3396 -0.0776 0.0464 -0.0225 277 VAL A CA 1771 C C . VAL A 242 ? 0.3858 0.3414 0.3297 -0.0826 0.0523 -0.0232 277 VAL A C 1772 O O . VAL A 242 ? 0.4058 0.3472 0.3438 -0.0795 0.0563 -0.0221 277 VAL A O 1773 C CB . VAL A 242 ? 0.4187 0.3844 0.3650 -0.0803 0.0448 -0.0253 277 VAL A CB 1774 C CG1 . VAL A 242 ? 0.4353 0.4101 0.3868 -0.0741 0.0398 -0.0240 277 VAL A CG1 1775 C CG2 . VAL A 242 ? 0.4163 0.3872 0.3612 -0.0904 0.0439 -0.0287 277 VAL A CG2 1776 N N . SER A 243 ? 0.3915 0.3528 0.3370 -0.0901 0.0528 -0.0245 278 SER A N 1777 C CA . SER A 243 ? 0.4089 0.3593 0.3487 -0.0956 0.0586 -0.0250 278 SER A CA 1778 C C . SER A 243 ? 0.4076 0.3520 0.3472 -0.0898 0.0618 -0.0211 278 SER A C 1779 O O . SER A 243 ? 0.4438 0.3745 0.3767 -0.0923 0.0672 -0.0207 278 SER A O 1780 C CB . SER A 243 ? 0.4375 0.3988 0.3810 -0.1048 0.0578 -0.0268 278 SER A CB 1781 O OG . SER A 243 ? 0.5215 0.4864 0.4632 -0.1121 0.0556 -0.0305 278 SER A OG 1782 N N . ILE A 244 ? 0.3549 0.3088 0.3010 -0.0826 0.0587 -0.0183 279 ILE A N 1783 C CA . ILE A 244 ? 0.3382 0.2882 0.2838 -0.0778 0.0612 -0.0147 279 ILE A CA 1784 C C . ILE A 244 ? 0.3478 0.2834 0.2872 -0.0716 0.0636 -0.0124 279 ILE A C 1785 O O . ILE A 244 ? 0.3345 0.2717 0.2755 -0.0660 0.0607 -0.0119 279 ILE A O 1786 C CB . ILE A 244 ? 0.3375 0.3016 0.2909 -0.0724 0.0574 -0.0128 279 ILE A CB 1787 C CG1 . ILE A 244 ? 0.3381 0.3172 0.2985 -0.0776 0.0553 -0.0145 279 ILE A CG1 1788 C CG2 . ILE A 244 ? 0.3268 0.2863 0.2781 -0.0682 0.0601 -0.0092 279 ILE A CG2 1789 C CD1 . ILE A 244 ? 0.3441 0.3370 0.3124 -0.0720 0.0512 -0.0135 279 ILE A CD1 1790 N N . PRO A 245 ? 0.3730 0.2948 0.3058 -0.0726 0.0692 -0.0108 280 PRO A N 1791 C CA . PRO A 245 ? 0.3859 0.2945 0.3136 -0.0662 0.0718 -0.0079 280 PRO A CA 1792 C C . PRO A 245 ? 0.3687 0.2836 0.3003 -0.0573 0.0685 -0.0039 280 PRO A C 1793 O O . PRO A 245 ? 0.3407 0.2653 0.2763 -0.0566 0.0665 -0.0027 280 PRO A O 1794 C CB . PRO A 245 ? 0.4087 0.3030 0.3292 -0.0689 0.0783 -0.0061 280 PRO A CB 1795 C CG . PRO A 245 ? 0.4149 0.3134 0.3359 -0.0784 0.0794 -0.0091 280 PRO A CG 1796 C CD . PRO A 245 ? 0.3889 0.3068 0.3188 -0.0792 0.0734 -0.0108 280 PRO A CD 1797 N N . HIS A 246 ? 0.3602 0.2701 0.2907 -0.0510 0.0682 -0.0021 281 HIS A N 1798 C CA . HIS A 246 ? 0.3733 0.2891 0.3071 -0.0432 0.0650 0.0016 281 HIS A CA 1799 C C . HIS A 246 ? 0.3655 0.2800 0.2975 -0.0411 0.0666 0.0058 281 HIS A C 1800 O O . HIS A 246 ? 0.3563 0.2804 0.2917 -0.0381 0.0631 0.0072 281 HIS A O 1801 C CB . HIS A 246 ? 0.3903 0.3002 0.3231 -0.0371 0.0653 0.0035 281 HIS A CB 1802 C CG . HIS A 246 ? 0.4261 0.3389 0.3609 -0.0383 0.0631 0.0000 281 HIS A CG 1803 N ND1 . HIS A 246 ? 0.5269 0.4317 0.4594 -0.0353 0.0652 0.0001 281 HIS A ND1 1804 C CD2 . HIS A 246 ? 0.4460 0.3688 0.3846 -0.0423 0.0593 -0.0039 281 HIS A CD2 1805 C CE1 . HIS A 246 ? 0.5079 0.4175 0.4421 -0.0375 0.0626 -0.0034 281 HIS A CE1 1806 N NE2 . HIS A 246 ? 0.4580 0.3785 0.3959 -0.0417 0.0588 -0.0058 281 HIS A NE2 1807 N N . GLU A 247 ? 0.3865 0.2886 0.3124 -0.0429 0.0722 0.0075 282 GLU A N 1808 C CA . GLU A 247 ? 0.3856 0.2853 0.3086 -0.0412 0.0741 0.0119 282 GLU A CA 1809 C C . GLU A 247 ? 0.3663 0.2771 0.2924 -0.0453 0.0724 0.0102 282 GLU A C 1810 O O . GLU A 247 ? 0.3585 0.2737 0.2845 -0.0423 0.0713 0.0133 282 GLU A O 1811 C CB . GLU A 247 ? 0.4167 0.3000 0.3321 -0.0434 0.0810 0.0138 282 GLU A CB 1812 C CG . GLU A 247 ? 0.4401 0.3108 0.3519 -0.0381 0.0840 0.0164 282 GLU A CG 1813 C CD . GLU A 247 ? 0.4632 0.3270 0.3735 -0.0420 0.0861 0.0116 282 GLU A CD 1814 O OE1 . GLU A 247 ? 0.4174 0.2897 0.3311 -0.0472 0.0830 0.0064 282 GLU A OE1 1815 O OE2 . GLU A 247 ? 0.4863 0.3358 0.3916 -0.0395 0.0910 0.0132 282 GLU A OE2 1816 N N . ARG A 248 ? 0.3478 0.2633 0.2766 -0.0521 0.0723 0.0056 283 ARG A N 1817 C CA . ARG A 248 ? 0.3473 0.2744 0.2803 -0.0562 0.0711 0.0039 283 ARG A CA 1818 C C . ARG A 248 ? 0.3271 0.2682 0.2668 -0.0521 0.0654 0.0031 283 ARG A C 1819 O O . ARG A 248 ? 0.3422 0.2913 0.2842 -0.0518 0.0647 0.0036 283 ARG A O 1820 C CB . ARG A 248 ? 0.3601 0.2886 0.2944 -0.0650 0.0726 -0.0003 283 ARG A CB 1821 C CG . ARG A 248 ? 0.3616 0.3041 0.3021 -0.0695 0.0713 -0.0023 283 ARG A CG 1822 C CD . ARG A 248 ? 0.3889 0.3304 0.3271 -0.0703 0.0748 0.0003 283 ARG A CD 1823 N NE . ARG A 248 ? 0.4304 0.3582 0.3615 -0.0754 0.0807 0.0012 283 ARG A NE 1824 C CZ . ARG A 248 ? 0.4364 0.3582 0.3627 -0.0753 0.0847 0.0046 283 ARG A CZ 1825 N NH1 . ARG A 248 ? 0.4546 0.3830 0.3820 -0.0707 0.0834 0.0071 283 ARG A NH1 1826 N NH2 . ARG A 248 ? 0.4447 0.3527 0.3641 -0.0800 0.0903 0.0054 283 ARG A NH2 1827 N N . ARG A 249 ? 0.3076 0.2510 0.2499 -0.0490 0.0619 0.0019 284 ARG A N 1828 C CA . ARG A 249 ? 0.2929 0.2474 0.2406 -0.0447 0.0568 0.0015 284 ARG A CA 1829 C C . ARG A 249 ? 0.3014 0.2559 0.2470 -0.0391 0.0561 0.0052 284 ARG A C 1830 O O . ARG A 249 ? 0.2914 0.2544 0.2396 -0.0378 0.0539 0.0050 284 ARG A O 1831 C CB . ARG A 249 ? 0.2899 0.2453 0.2398 -0.0423 0.0536 0.0000 284 ARG A CB 1832 C CG . ARG A 249 ? 0.2969 0.2536 0.2485 -0.0480 0.0535 -0.0038 284 ARG A CG 1833 C CD . ARG A 249 ? 0.3069 0.2634 0.2594 -0.0457 0.0508 -0.0050 284 ARG A CD 1834 N NE . ARG A 249 ? 0.3189 0.2720 0.2696 -0.0518 0.0522 -0.0082 284 ARG A NE 1835 C CZ . ARG A 249 ? 0.3381 0.2919 0.2891 -0.0524 0.0502 -0.0104 284 ARG A CZ 1836 N NH1 . ARG A 249 ? 0.3430 0.3008 0.2968 -0.0470 0.0468 -0.0096 284 ARG A NH1 1837 N NH2 . ARG A 249 ? 0.3625 0.3126 0.3104 -0.0589 0.0518 -0.0135 284 ARG A NH2 1838 N N . ILE A 250 ? 0.3042 0.2488 0.2446 -0.0361 0.0581 0.0088 285 ILE A N 1839 C CA . ILE A 250 ? 0.3104 0.2549 0.2479 -0.0312 0.0572 0.0131 285 ILE A CA 1840 C C . ILE A 250 ? 0.3125 0.2578 0.2471 -0.0336 0.0597 0.0142 285 ILE A C 1841 O O . ILE A 250 ? 0.3016 0.2534 0.2363 -0.0316 0.0576 0.0149 285 ILE A O 1842 C CB . ILE A 250 ? 0.3152 0.2498 0.2486 -0.0268 0.0588 0.0175 285 ILE A CB 1843 C CG1 . ILE A 250 ? 0.3134 0.2486 0.2502 -0.0238 0.0564 0.0165 285 ILE A CG1 1844 C CG2 . ILE A 250 ? 0.3261 0.2619 0.2562 -0.0224 0.0577 0.0224 285 ILE A CG2 1845 C CD1 . ILE A 250 ? 0.3037 0.2496 0.2451 -0.0208 0.0509 0.0156 285 ILE A CD1 1846 N N . LEU A 251 ? 0.3210 0.2593 0.2525 -0.0381 0.0644 0.0143 286 LEU A N 1847 C CA . LEU A 251 ? 0.3380 0.2768 0.2666 -0.0411 0.0675 0.0154 286 LEU A CA 1848 C C . LEU A 251 ? 0.3270 0.2784 0.2611 -0.0434 0.0658 0.0119 286 LEU A C 1849 O O . LEU A 251 ? 0.3202 0.2750 0.2524 -0.0430 0.0667 0.0131 286 LEU A O 1850 C CB . LEU A 251 ? 0.3723 0.3012 0.2971 -0.0465 0.0731 0.0155 286 LEU A CB 1851 C CG . LEU A 251 ? 0.4086 0.3234 0.3262 -0.0436 0.0764 0.0204 286 LEU A CG 1852 C CD1 . LEU A 251 ? 0.4303 0.3335 0.3443 -0.0493 0.0819 0.0193 286 LEU A CD1 1853 C CD2 . LEU A 251 ? 0.4437 0.3574 0.3560 -0.0407 0.0774 0.0253 286 LEU A CD2 1854 N N . THR A 252 ? 0.2985 0.2568 0.2391 -0.0453 0.0635 0.0079 287 THR A N 1855 C CA . THR A 252 ? 0.3013 0.2720 0.2481 -0.0465 0.0619 0.0051 287 THR A CA 1856 C C . THR A 252 ? 0.2873 0.2638 0.2349 -0.0411 0.0584 0.0055 287 THR A C 1857 O O . THR A 252 ? 0.2868 0.2695 0.2354 -0.0410 0.0592 0.0049 287 THR A O 1858 C CB . THR A 252 ? 0.2885 0.2653 0.2420 -0.0496 0.0600 0.0014 287 THR A CB 1859 O OG1 . THR A 252 ? 0.3070 0.2789 0.2591 -0.0560 0.0636 0.0005 287 THR A OG1 1860 C CG2 . THR A 252 ? 0.2741 0.2642 0.2348 -0.0496 0.0583 -0.0007 287 THR A CG2 1861 N N . ILE A 253 ? 0.2846 0.2589 0.2316 -0.0368 0.0550 0.0063 288 ILE A N 1862 C CA . ILE A 253 ? 0.2851 0.2635 0.2316 -0.0323 0.0518 0.0069 288 ILE A CA 1863 C C . ILE A 253 ? 0.2962 0.2718 0.2359 -0.0314 0.0536 0.0099 288 ILE A C 1864 O O . ILE A 253 ? 0.2885 0.2692 0.2275 -0.0305 0.0532 0.0090 288 ILE A O 1865 C CB . ILE A 253 ? 0.3046 0.2809 0.2515 -0.0285 0.0480 0.0077 288 ILE A CB 1866 C CG1 . ILE A 253 ? 0.2877 0.2684 0.2411 -0.0295 0.0459 0.0044 288 ILE A CG1 1867 C CG2 . ILE A 253 ? 0.3207 0.3001 0.2655 -0.0247 0.0449 0.0089 288 ILE A CG2 1868 C CD1 . ILE A 253 ? 0.3004 0.2776 0.2542 -0.0269 0.0435 0.0050 288 ILE A CD1 1869 N N . LEU A 254 ? 0.3059 0.2731 0.2401 -0.0316 0.0561 0.0135 289 LEU A N 1870 C CA . LEU A 254 ? 0.3053 0.2694 0.2322 -0.0308 0.0579 0.0171 289 LEU A CA 1871 C C . LEU A 254 ? 0.3156 0.2827 0.2417 -0.0345 0.0616 0.0157 289 LEU A C 1872 O O . LEU A 254 ? 0.3102 0.2791 0.2316 -0.0336 0.0620 0.0168 289 LEU A O 1873 C CB . LEU A 254 ? 0.3193 0.2731 0.2408 -0.0298 0.0600 0.0218 289 LEU A CB 1874 C CG . LEU A 254 ? 0.3089 0.2602 0.2311 -0.0251 0.0567 0.0241 289 LEU A CG 1875 C CD1 . LEU A 254 ? 0.3145 0.2548 0.2328 -0.0241 0.0601 0.0283 289 LEU A CD1 1876 C CD2 . LEU A 254 ? 0.3278 0.2842 0.2476 -0.0212 0.0526 0.0263 289 LEU A CD2 1877 N N . GLN A 255 ? 0.3098 0.2780 0.2404 -0.0388 0.0644 0.0133 290 GLN A N 1878 C CA . GLN A 255 ? 0.3371 0.3100 0.2687 -0.0426 0.0681 0.0118 290 GLN A CA 1879 C C . GLN A 255 ? 0.2831 0.2661 0.2188 -0.0408 0.0664 0.0089 290 GLN A C 1880 O O . GLN A 255 ? 0.2759 0.2613 0.2086 -0.0410 0.0688 0.0090 290 GLN A O 1881 C CB . GLN A 255 ? 0.3846 0.3582 0.3212 -0.0481 0.0707 0.0098 290 GLN A CB 1882 C CG . GLN A 255 ? 0.4887 0.4667 0.4265 -0.0527 0.0753 0.0091 290 GLN A CG 1883 C CD . GLN A 255 ? 0.5599 0.5372 0.5014 -0.0591 0.0778 0.0076 290 GLN A CD 1884 O OE1 . GLN A 255 ? 0.6248 0.6119 0.5745 -0.0618 0.0770 0.0045 290 GLN A OE1 1885 N NE2 . GLN A 255 ? 0.5622 0.5276 0.4974 -0.0615 0.0806 0.0099 290 GLN A NE2 1886 N N . TRP A 256 ? 0.2626 0.2506 0.2046 -0.0388 0.0625 0.0063 291 TRP A N 1887 C CA . TRP A 256 ? 0.2530 0.2490 0.1987 -0.0365 0.0610 0.0036 291 TRP A CA 1888 C C . TRP A 256 ? 0.2611 0.2548 0.1995 -0.0332 0.0597 0.0048 291 TRP A C 1889 O O . TRP A 256 ? 0.2495 0.2471 0.1870 -0.0325 0.0612 0.0032 291 TRP A O 1890 C CB . TRP A 256 ? 0.2438 0.2442 0.1966 -0.0349 0.0570 0.0013 291 TRP A CB 1891 C CG . TRP A 256 ? 0.2458 0.2510 0.2062 -0.0384 0.0576 -0.0003 291 TRP A CG 1892 C CD1 . TRP A 256 ? 0.2571 0.2662 0.2206 -0.0428 0.0613 -0.0008 291 TRP A CD1 1893 C CD2 . TRP A 256 ? 0.2494 0.2569 0.2151 -0.0380 0.0540 -0.0018 291 TRP A CD2 1894 N NE1 . TRP A 256 ? 0.2597 0.2737 0.2300 -0.0456 0.0599 -0.0025 291 TRP A NE1 1895 C CE2 . TRP A 256 ? 0.2521 0.2649 0.2235 -0.0426 0.0555 -0.0031 291 TRP A CE2 1896 C CE3 . TRP A 256 ? 0.2628 0.2686 0.2288 -0.0346 0.0498 -0.0020 291 TRP A CE3 1897 C CZ2 . TRP A 256 ? 0.2558 0.2723 0.2326 -0.0438 0.0526 -0.0047 291 TRP A CZ2 1898 C CZ3 . TRP A 256 ? 0.2672 0.2761 0.2385 -0.0356 0.0474 -0.0036 291 TRP A CZ3 1899 C CH2 . TRP A 256 ? 0.2534 0.2674 0.2297 -0.0402 0.0487 -0.0048 291 TRP A CH2 1900 N N . LEU A 257 ? 0.2622 0.2498 0.1952 -0.0313 0.0571 0.0076 292 LEU A N 1901 C CA . LEU A 257 ? 0.2688 0.2547 0.1943 -0.0288 0.0553 0.0093 292 LEU A CA 1902 C C . LEU A 257 ? 0.2820 0.2656 0.1996 -0.0304 0.0592 0.0112 292 LEU A C 1903 O O . LEU A 257 ? 0.2804 0.2641 0.1914 -0.0293 0.0582 0.0116 292 LEU A O 1904 C CB . LEU A 257 ? 0.2884 0.2699 0.2111 -0.0263 0.0516 0.0126 292 LEU A CB 1905 C CG . LEU A 257 ? 0.2841 0.2686 0.2123 -0.0240 0.0470 0.0106 292 LEU A CG 1906 C CD1 . LEU A 257 ? 0.3049 0.2854 0.2328 -0.0219 0.0445 0.0140 292 LEU A CD1 1907 C CD2 . LEU A 257 ? 0.2891 0.2771 0.2146 -0.0227 0.0445 0.0087 292 LEU A CD2 1908 N N . SER A 258 ? 0.2738 0.2555 0.1920 -0.0336 0.0636 0.0122 293 SER A N 1909 C CA . SER A 258 ? 0.3067 0.2863 0.2179 -0.0357 0.0682 0.0140 293 SER A CA 1910 C C . SER A 258 ? 0.3082 0.2943 0.2226 -0.0375 0.0721 0.0105 293 SER A C 1911 O O . SER A 258 ? 0.3174 0.3025 0.2262 -0.0395 0.0764 0.0116 293 SER A O 1912 C CB . SER A 258 ? 0.3148 0.2876 0.2241 -0.0384 0.0714 0.0173 293 SER A CB 1913 O OG . SER A 258 ? 0.3397 0.3064 0.2467 -0.0359 0.0683 0.0207 293 SER A OG 1914 N N . LEU A 259 ? 0.3039 0.2969 0.2274 -0.0368 0.0709 0.0067 294 LEU A N 1915 C CA . LEU A 259 ? 0.3108 0.3111 0.2391 -0.0377 0.0748 0.0037 294 LEU A CA 1916 C C . LEU A 259 ? 0.3242 0.3246 0.2456 -0.0357 0.0761 0.0025 294 LEU A C 1917 O O . LEU A 259 ? 0.3114 0.3079 0.2261 -0.0336 0.0726 0.0030 294 LEU A O 1918 C CB . LEU A 259 ? 0.3029 0.3106 0.2424 -0.0364 0.0725 0.0006 294 LEU A CB 1919 C CG . LEU A 259 ? 0.2979 0.3079 0.2451 -0.0396 0.0725 0.0008 294 LEU A CG 1920 C CD1 . LEU A 259 ? 0.2815 0.2978 0.2378 -0.0376 0.0687 -0.0015 294 LEU A CD1 1921 C CD2 . LEU A 259 ? 0.3175 0.3323 0.2678 -0.0438 0.0780 0.0008 294 LEU A CD2 1922 N N . PRO A 260 ? 0.3210 0.3260 0.2439 -0.0368 0.0814 0.0008 295 PRO A N 1923 C CA . PRO A 260 ? 0.3358 0.3402 0.2520 -0.0348 0.0832 -0.0011 295 PRO A CA 1924 C C . PRO A 260 ? 0.3315 0.3368 0.2498 -0.0311 0.0794 -0.0041 295 PRO A C 1925 O O . PRO A 260 ? 0.3135 0.3224 0.2411 -0.0297 0.0763 -0.0051 295 PRO A O 1926 C CB . PRO A 260 ? 0.3417 0.3524 0.2624 -0.0360 0.0900 -0.0027 295 PRO A CB 1927 C CG . PRO A 260 ? 0.3547 0.3704 0.2850 -0.0390 0.0913 -0.0015 295 PRO A CG 1928 C CD . PRO A 260 ? 0.3271 0.3391 0.2591 -0.0395 0.0857 0.0001 295 PRO A CD 1929 N N . ASP A 261 ? 0.3565 0.3583 0.2655 -0.0300 0.0799 -0.0056 296 ASP A N 1930 C CA . ASP A 261 ? 0.3768 0.3770 0.2846 -0.0273 0.0761 -0.0083 296 ASP A CA 1931 C C . ASP A 261 ? 0.3672 0.3730 0.2866 -0.0244 0.0769 -0.0113 296 ASP A C 1932 O O . ASP A 261 ? 0.3894 0.3950 0.3127 -0.0225 0.0723 -0.0122 296 ASP A O 1933 C CB . ASP A 261 ? 0.4191 0.4144 0.3142 -0.0275 0.0780 -0.0101 296 ASP A CB 1934 C CG . ASP A 261 ? 0.4487 0.4392 0.3315 -0.0301 0.0766 -0.0066 296 ASP A CG 1935 O OD1 . ASP A 261 ? 0.4352 0.4245 0.3184 -0.0305 0.0721 -0.0029 296 ASP A OD1 1936 O OD2 . ASP A 261 ? 0.4983 0.4859 0.3705 -0.0315 0.0802 -0.0073 296 ASP A OD2 1937 N N . ASN A 262 ? 0.3897 0.4011 0.3153 -0.0241 0.0825 -0.0124 297 ASN A N 1938 C CA . ASN A 262 ? 0.3968 0.4143 0.3335 -0.0208 0.0834 -0.0146 297 ASN A CA 1939 C C . ASN A 262 ? 0.3845 0.4091 0.3338 -0.0212 0.0806 -0.0131 297 ASN A C 1940 O O . ASN A 262 ? 0.3821 0.4124 0.3408 -0.0183 0.0804 -0.0142 297 ASN A O 1941 C CB . ASN A 262 ? 0.4602 0.4813 0.3984 -0.0192 0.0909 -0.0166 297 ASN A CB 1942 C CG . ASN A 262 ? 0.5023 0.5297 0.4446 -0.0220 0.0959 -0.0148 297 ASN A CG 1943 O OD1 . ASN A 262 ? 0.5299 0.5591 0.4750 -0.0254 0.0939 -0.0122 297 ASN A OD1 1944 N ND2 . ASN A 262 ? 0.5994 0.6296 0.5418 -0.0208 0.1029 -0.0163 297 ASN A ND2 1945 N N . GLU A 263 ? 0.3371 0.3609 0.2859 -0.0248 0.0786 -0.0104 298 GLU A N 1946 C CA . GLU A 263 ? 0.3217 0.3504 0.2801 -0.0262 0.0756 -0.0091 298 GLU A CA 1947 C C . GLU A 263 ? 0.2959 0.3189 0.2516 -0.0262 0.0694 -0.0080 298 GLU A C 1948 O O . GLU A 263 ? 0.2728 0.2992 0.2359 -0.0266 0.0664 -0.0078 298 GLU A O 1949 C CB . GLU A 263 ? 0.3498 0.3811 0.3100 -0.0308 0.0787 -0.0071 298 GLU A CB 1950 C CG . GLU A 263 ? 0.4122 0.4525 0.3791 -0.0315 0.0845 -0.0078 298 GLU A CG 1951 C CD . GLU A 263 ? 0.4557 0.4976 0.4233 -0.0369 0.0876 -0.0058 298 GLU A CD 1952 O OE1 . GLU A 263 ? 0.5618 0.6044 0.5333 -0.0401 0.0850 -0.0048 298 GLU A OE1 1953 O OE2 . GLU A 263 ? 0.5427 0.5848 0.5064 -0.0383 0.0931 -0.0055 298 GLU A OE2 1954 N N . ARG A 264 ? 0.2862 0.3013 0.2315 -0.0260 0.0676 -0.0071 299 ARG A N 1955 C CA . ARG A 264 ? 0.2856 0.2958 0.2283 -0.0262 0.0624 -0.0052 299 ARG A CA 1956 C C . ARG A 264 ? 0.2783 0.2891 0.2246 -0.0232 0.0580 -0.0069 299 ARG A C 1957 O O . ARG A 264 ? 0.2771 0.2868 0.2204 -0.0211 0.0579 -0.0090 299 ARG A O 1958 C CB . ARG A 264 ? 0.2950 0.2983 0.2258 -0.0267 0.0620 -0.0032 299 ARG A CB 1959 C CG . ARG A 264 ? 0.2882 0.2869 0.2163 -0.0264 0.0572 -0.0004 299 ARG A CG 1960 C CD . ARG A 264 ? 0.3063 0.3000 0.2232 -0.0266 0.0565 0.0021 299 ARG A CD 1961 N NE . ARG A 264 ? 0.3248 0.3184 0.2359 -0.0257 0.0561 -0.0003 299 ARG A NE 1962 C CZ . ARG A 264 ? 0.3558 0.3482 0.2589 -0.0268 0.0596 -0.0010 299 ARG A CZ 1963 N NH1 . ARG A 264 ? 0.3628 0.3543 0.2625 -0.0288 0.0640 0.0009 299 ARG A NH1 1964 N NH2 . ARG A 264 ? 0.3743 0.3657 0.2719 -0.0263 0.0590 -0.0038 299 ARG A NH2 1965 N N . PRO A 265 ? 0.2614 0.2731 0.2134 -0.0234 0.0545 -0.0062 300 PRO A N 1966 C CA . PRO A 265 ? 0.2487 0.2601 0.2029 -0.0208 0.0502 -0.0073 300 PRO A CA 1967 C C . PRO A 265 ? 0.2490 0.2548 0.1955 -0.0199 0.0469 -0.0065 300 PRO A C 1968 O O . PRO A 265 ? 0.2478 0.2498 0.1877 -0.0212 0.0469 -0.0042 300 PRO A O 1969 C CB . PRO A 265 ? 0.2400 0.2534 0.2009 -0.0218 0.0479 -0.0065 300 PRO A CB 1970 C CG . PRO A 265 ? 0.2452 0.2622 0.2098 -0.0248 0.0514 -0.0060 300 PRO A CG 1971 C CD . PRO A 265 ? 0.2584 0.2721 0.2156 -0.0261 0.0550 -0.0049 300 PRO A CD 1972 N N . SER A 266 ? 0.2378 0.2433 0.1852 -0.0179 0.0441 -0.0082 301 SER A N 1973 C CA . SER A 266 ? 0.2488 0.2504 0.1903 -0.0176 0.0403 -0.0075 301 SER A CA 1974 C C . SER A 266 ? 0.2404 0.2422 0.1864 -0.0168 0.0362 -0.0062 301 SER A C 1975 O O . SER A 266 ? 0.2333 0.2330 0.1756 -0.0168 0.0331 -0.0048 301 SER A O 1976 C CB . SER A 266 ? 0.2623 0.2622 0.2000 -0.0165 0.0402 -0.0104 301 SER A CB 1977 O OG . SER A 266 ? 0.2795 0.2775 0.2098 -0.0175 0.0436 -0.0115 301 SER A OG 1978 N N . VAL A 267 ? 0.2254 0.2301 0.1792 -0.0165 0.0362 -0.0067 302 VAL A N 1979 C CA . VAL A 267 ? 0.2289 0.2335 0.1865 -0.0160 0.0328 -0.0058 302 VAL A CA 1980 C C . VAL A 267 ? 0.2221 0.2279 0.1841 -0.0175 0.0340 -0.0048 302 VAL A C 1981 O O . VAL A 267 ? 0.2148 0.2244 0.1808 -0.0186 0.0364 -0.0059 302 VAL A O 1982 C CB . VAL A 267 ? 0.2353 0.2412 0.1966 -0.0142 0.0305 -0.0077 302 VAL A CB 1983 C CG1 . VAL A 267 ? 0.2370 0.2472 0.2043 -0.0133 0.0325 -0.0095 302 VAL A CG1 1984 C CG2 . VAL A 267 ? 0.2261 0.2315 0.1901 -0.0139 0.0272 -0.0065 302 VAL A CG2 1985 N N . TYR A 268 ? 0.2130 0.2157 0.1741 -0.0178 0.0324 -0.0028 303 TYR A N 1986 C CA . TYR A 268 ? 0.2294 0.2309 0.1926 -0.0197 0.0338 -0.0019 303 TYR A CA 1987 C C . TYR A 268 ? 0.2239 0.2237 0.1892 -0.0190 0.0312 -0.0015 303 TYR A C 1988 O O . TYR A 268 ? 0.2314 0.2300 0.1954 -0.0169 0.0287 -0.0006 303 TYR A O 1989 C CB . TYR A 268 ? 0.2318 0.2284 0.1897 -0.0209 0.0361 0.0007 303 TYR A CB 1990 C CG . TYR A 268 ? 0.2374 0.2348 0.1917 -0.0218 0.0389 0.0007 303 TYR A CG 1991 C CD1 . TYR A 268 ? 0.2405 0.2376 0.1897 -0.0203 0.0380 0.0010 303 TYR A CD1 1992 C CD2 . TYR A 268 ? 0.2492 0.2476 0.2047 -0.0246 0.0426 0.0003 303 TYR A CD2 1993 C CE1 . TYR A 268 ? 0.2540 0.2513 0.1988 -0.0212 0.0410 0.0009 303 TYR A CE1 1994 C CE2 . TYR A 268 ? 0.2426 0.2418 0.1946 -0.0255 0.0457 0.0004 303 TYR A CE2 1995 C CZ . TYR A 268 ? 0.2515 0.2498 0.1979 -0.0236 0.0450 0.0007 303 TYR A CZ 1996 O OH . TYR A 268 ? 0.2603 0.2590 0.2024 -0.0246 0.0484 0.0006 303 TYR A OH 1997 N N . ALA A 269 ? 0.2226 0.2222 0.1908 -0.0211 0.0322 -0.0020 304 ALA A N 1998 C CA . ALA A 269 ? 0.2198 0.2160 0.1884 -0.0208 0.0309 -0.0015 304 ALA A CA 1999 C C . ALA A 269 ? 0.2338 0.2249 0.2006 -0.0236 0.0338 -0.0009 304 ALA A C 2000 O O . ALA A 269 ? 0.2325 0.2251 0.2005 -0.0270 0.0359 -0.0022 304 ALA A O 2001 C CB . ALA A 269 ? 0.2345 0.2350 0.2077 -0.0206 0.0285 -0.0035 304 ALA A CB 2002 N N . PHE A 270 ? 0.2425 0.2275 0.2068 -0.0222 0.0342 0.0009 305 PHE A N 2003 C CA . PHE A 270 ? 0.2450 0.2229 0.2069 -0.0243 0.0371 0.0012 305 PHE A CA 2004 C C . PHE A 270 ? 0.2417 0.2189 0.2055 -0.0239 0.0356 0.0000 305 PHE A C 2005 O O . PHE A 270 ? 0.2362 0.2155 0.2014 -0.0206 0.0330 0.0006 305 PHE A O 2006 C CB . PHE A 270 ? 0.2553 0.2258 0.2125 -0.0220 0.0394 0.0049 305 PHE A CB 2007 C CG . PHE A 270 ? 0.2627 0.2240 0.2172 -0.0231 0.0428 0.0055 305 PHE A CG 2008 C CD1 . PHE A 270 ? 0.2579 0.2158 0.2127 -0.0204 0.0424 0.0061 305 PHE A CD1 2009 C CD2 . PHE A 270 ? 0.2676 0.2230 0.2189 -0.0270 0.0468 0.0051 305 PHE A CD2 2010 C CE1 . PHE A 270 ? 0.2649 0.2133 0.2166 -0.0212 0.0463 0.0063 305 PHE A CE1 2011 C CE2 . PHE A 270 ? 0.2767 0.2219 0.2244 -0.0284 0.0506 0.0052 305 PHE A CE2 2012 C CZ . PHE A 270 ? 0.2747 0.2161 0.2225 -0.0253 0.0504 0.0057 305 PHE A CZ 2013 N N . TYR A 271 ? 0.2409 0.2152 0.2040 -0.0278 0.0374 -0.0020 306 TYR A N 2014 C CA . TYR A 271 ? 0.2560 0.2281 0.2192 -0.0279 0.0368 -0.0034 306 TYR A CA 2015 C C . TYR A 271 ? 0.2662 0.2277 0.2245 -0.0300 0.0410 -0.0034 306 TYR A C 2016 O O . TYR A 271 ? 0.2808 0.2389 0.2367 -0.0341 0.0439 -0.0042 306 TYR A O 2017 C CB . TYR A 271 ? 0.2716 0.2512 0.2383 -0.0309 0.0342 -0.0063 306 TYR A CB 2018 C CG . TYR A 271 ? 0.3003 0.2770 0.2657 -0.0325 0.0340 -0.0081 306 TYR A CG 2019 C CD1 . TYR A 271 ? 0.3180 0.2949 0.2841 -0.0290 0.0321 -0.0075 306 TYR A CD1 2020 C CD2 . TYR A 271 ? 0.3367 0.3105 0.2994 -0.0380 0.0359 -0.0104 306 TYR A CD2 2021 C CE1 . TYR A 271 ? 0.3116 0.2856 0.2757 -0.0307 0.0323 -0.0092 306 TYR A CE1 2022 C CE2 . TYR A 271 ? 0.3321 0.3027 0.2922 -0.0401 0.0360 -0.0123 306 TYR A CE2 2023 C CZ . TYR A 271 ? 0.3283 0.2990 0.2891 -0.0362 0.0343 -0.0117 306 TYR A CZ 2024 O OH . TYR A 271 ? 0.3537 0.3208 0.3110 -0.0387 0.0349 -0.0138 306 TYR A OH 2025 N N . SER A 272 ? 0.2563 0.2123 0.2131 -0.0273 0.0419 -0.0026 307 SER A N 2026 C CA . SER A 272 ? 0.2730 0.2176 0.2246 -0.0289 0.0465 -0.0031 307 SER A CA 2027 C C . SER A 272 ? 0.2806 0.2250 0.2318 -0.0304 0.0457 -0.0059 307 SER A C 2028 O O . SER A 272 ? 0.2664 0.2154 0.2206 -0.0268 0.0430 -0.0052 307 SER A O 2029 C CB . SER A 272 ? 0.3030 0.2399 0.2525 -0.0235 0.0494 0.0008 307 SER A CB 2030 O OG . SER A 272 ? 0.3312 0.2559 0.2756 -0.0245 0.0546 0.0002 307 SER A OG 2031 N N . GLU A 273 ? 0.2809 0.2189 0.2276 -0.0358 0.0486 -0.0089 308 GLU A N 2032 C CA A GLU A 273 ? 0.2964 0.2320 0.2404 -0.0383 0.0488 -0.0119 308 GLU A CA 2033 C CA B GLU A 273 ? 0.2987 0.2347 0.2430 -0.0381 0.0486 -0.0118 308 GLU A CA 2034 C C . GLU A 273 ? 0.3071 0.2329 0.2481 -0.0339 0.0526 -0.0105 308 GLU A C 2035 O O . GLU A 273 ? 0.3200 0.2436 0.2587 -0.0347 0.0530 -0.0125 308 GLU A O 2036 C CB A GLU A 273 ? 0.3064 0.2374 0.2454 -0.0465 0.0511 -0.0157 308 GLU A CB 2037 C CB B GLU A 273 ? 0.3118 0.2448 0.2515 -0.0464 0.0501 -0.0159 308 GLU A CB 2038 C CG A GLU A 273 ? 0.3047 0.2468 0.2475 -0.0516 0.0476 -0.0172 308 GLU A CG 2039 C CG B GLU A 273 ? 0.3346 0.2525 0.2666 -0.0494 0.0566 -0.0170 308 GLU A CG 2040 C CD A GLU A 273 ? 0.3014 0.2435 0.2453 -0.0522 0.0492 -0.0155 308 GLU A CD 2041 C CD B GLU A 273 ? 0.3407 0.2540 0.2725 -0.0478 0.0594 -0.0141 308 GLU A CD 2042 O OE1 A GLU A 273 ? 0.2996 0.2328 0.2409 -0.0488 0.0528 -0.0129 308 GLU A OE1 2043 O OE1 B GLU A 273 ? 0.3255 0.2486 0.2625 -0.0470 0.0562 -0.0125 308 GLU A OE1 2044 O OE2 A GLU A 273 ? 0.2909 0.2424 0.2385 -0.0559 0.0469 -0.0164 308 GLU A OE2 2045 O OE2 B GLU A 273 ? 0.3760 0.2756 0.3021 -0.0473 0.0652 -0.0132 308 GLU A OE2 2046 N N . GLN A 274 ? 0.2996 0.2194 0.2401 -0.0292 0.0557 -0.0068 309 GLN A N 2047 C CA . GLN A 274 ? 0.3007 0.2118 0.2394 -0.0238 0.0598 -0.0044 309 GLN A CA 2048 C C . GLN A 274 ? 0.2893 0.2094 0.2346 -0.0171 0.0562 -0.0005 309 GLN A C 2049 O O . GLN A 274 ? 0.2835 0.2126 0.2328 -0.0164 0.0521 0.0009 309 GLN A O 2050 C CB . GLN A 274 ? 0.3263 0.2242 0.2600 -0.0229 0.0660 -0.0024 309 GLN A CB 2051 C CG . GLN A 274 ? 0.3542 0.2400 0.2800 -0.0296 0.0709 -0.0066 309 GLN A CG 2052 C CD . GLN A 274 ? 0.3676 0.2434 0.2884 -0.0292 0.0753 -0.0088 309 GLN A CD 2053 O OE1 . GLN A 274 ? 0.3672 0.2488 0.2908 -0.0268 0.0730 -0.0092 309 GLN A OE1 2054 N NE2 . GLN A 274 ? 0.3934 0.2536 0.3063 -0.0318 0.0821 -0.0103 309 GLN A NE2 2055 N N . PRO A 275 ? 0.2669 0.1852 0.2133 -0.0124 0.0578 0.0010 310 PRO A N 2056 C CA . PRO A 275 ? 0.2964 0.2029 0.2377 -0.0120 0.0637 -0.0001 310 PRO A CA 2057 C C . PRO A 275 ? 0.2941 0.2009 0.2329 -0.0161 0.0631 -0.0047 310 PRO A C 2058 O O . PRO A 275 ? 0.3042 0.2026 0.2393 -0.0149 0.0678 -0.0057 310 PRO A O 2059 C CB . PRO A 275 ? 0.2901 0.1975 0.2357 -0.0039 0.0652 0.0048 310 PRO A CB 2060 C CG . PRO A 275 ? 0.2736 0.1955 0.2262 -0.0023 0.0585 0.0063 310 PRO A CG 2061 C CD . PRO A 275 ? 0.2714 0.1980 0.2241 -0.0062 0.0549 0.0053 310 PRO A CD 2062 N N . ASP A 276 ? 0.2885 0.2047 0.2291 -0.0206 0.0577 -0.0074 311 ASP A N 2063 C CA . ASP A 276 ? 0.2700 0.1881 0.2083 -0.0244 0.0563 -0.0112 311 ASP A CA 2064 C C . ASP A 276 ? 0.2909 0.1965 0.2201 -0.0294 0.0616 -0.0151 311 ASP A C 2065 O O . ASP A 276 ? 0.2923 0.1931 0.2178 -0.0294 0.0642 -0.0168 311 ASP A O 2066 C CB . ASP A 276 ? 0.2692 0.1990 0.2106 -0.0285 0.0500 -0.0129 311 ASP A CB 2067 C CG . ASP A 276 ? 0.2662 0.2005 0.2067 -0.0308 0.0473 -0.0153 311 ASP A CG 2068 O OD1 . ASP A 276 ? 0.2793 0.2159 0.2223 -0.0267 0.0468 -0.0137 311 ASP A OD1 2069 O OD2 . ASP A 276 ? 0.2852 0.2211 0.2225 -0.0369 0.0458 -0.0185 311 ASP A OD2 2070 N N . PHE A 277 ? 0.3232 0.2229 0.2485 -0.0341 0.0636 -0.0167 312 PHE A N 2071 C CA . PHE A 277 ? 0.3713 0.2592 0.2871 -0.0405 0.0683 -0.0211 312 PHE A CA 2072 C C . PHE A 277 ? 0.3680 0.2410 0.2783 -0.0368 0.0759 -0.0207 312 PHE A C 2073 O O . PHE A 277 ? 0.3633 0.2294 0.2671 -0.0395 0.0789 -0.0242 312 PHE A O 2074 C CB . PHE A 277 ? 0.4218 0.3061 0.3344 -0.0468 0.0693 -0.0228 312 PHE A CB 2075 C CG . PHE A 277 ? 0.5035 0.3753 0.4057 -0.0544 0.0740 -0.0277 312 PHE A CG 2076 C CD1 . PHE A 277 ? 0.5457 0.4207 0.4439 -0.0599 0.0718 -0.0319 312 PHE A CD1 2077 C CD2 . PHE A 277 ? 0.5639 0.4198 0.4593 -0.0557 0.0810 -0.0282 312 PHE A CD2 2078 C CE1 . PHE A 277 ? 0.6026 0.4658 0.4901 -0.0675 0.0761 -0.0369 312 PHE A CE1 2079 C CE2 . PHE A 277 ? 0.6032 0.4463 0.4880 -0.0633 0.0858 -0.0332 312 PHE A CE2 2080 C CZ . PHE A 277 ? 0.6072 0.4540 0.4878 -0.0694 0.0833 -0.0378 312 PHE A CZ 2081 N N . SER A 278 ? 0.3508 0.2191 0.2639 -0.0301 0.0792 -0.0162 313 SER A N 2082 C CA . SER A 278 ? 0.3663 0.2216 0.2759 -0.0248 0.0866 -0.0147 313 SER A CA 2083 C C . SER A 278 ? 0.3449 0.2049 0.2575 -0.0203 0.0862 -0.0142 313 SER A C 2084 O O . SER A 278 ? 0.3697 0.2189 0.2765 -0.0195 0.0923 -0.0160 313 SER A O 2085 C CB . SER A 278 ? 0.3870 0.2387 0.3001 -0.0178 0.0894 -0.0089 313 SER A CB 2086 O OG . SER A 278 ? 0.4211 0.2639 0.3289 -0.0224 0.0920 -0.0100 313 SER A OG 2087 N N . GLY A 279 ? 0.3168 0.1924 0.2379 -0.0176 0.0794 -0.0119 314 GLY A N 2088 C CA . GLY A 279 ? 0.3153 0.1964 0.2391 -0.0146 0.0786 -0.0116 314 GLY A CA 2089 C C . GLY A 279 ? 0.3159 0.1931 0.2320 -0.0210 0.0794 -0.0172 314 GLY A C 2090 O O . GLY A 279 ? 0.3290 0.2007 0.2421 -0.0190 0.0837 -0.0180 314 GLY A O 2091 N N . HIS A 280 ? 0.3135 0.1937 0.2261 -0.0288 0.0755 -0.0209 315 HIS A N 2092 C CA . HIS A 280 ? 0.3143 0.1916 0.2188 -0.0357 0.0756 -0.0262 315 HIS A CA 2093 C C . HIS A 280 ? 0.3488 0.2081 0.2424 -0.0383 0.0841 -0.0296 315 HIS A C 2094 O O . HIS A 280 ? 0.3479 0.2018 0.2349 -0.0401 0.0871 -0.0326 315 HIS A O 2095 C CB . HIS A 280 ? 0.3168 0.2014 0.2202 -0.0437 0.0699 -0.0290 315 HIS A CB 2096 C CG . HIS A 280 ? 0.3046 0.2059 0.2164 -0.0426 0.0619 -0.0269 315 HIS A CG 2097 N ND1 . HIS A 280 ? 0.3054 0.2132 0.2179 -0.0420 0.0590 -0.0271 315 HIS A ND1 2098 C CD2 . HIS A 280 ? 0.2897 0.2016 0.2089 -0.0419 0.0566 -0.0247 315 HIS A CD2 2099 C CE1 . HIS A 280 ? 0.2964 0.2177 0.2165 -0.0408 0.0523 -0.0250 315 HIS A CE1 2100 N NE2 . HIS A 280 ? 0.2824 0.2064 0.2068 -0.0406 0.0509 -0.0236 315 HIS A NE2 2101 N N . LYS A 281 ? 0.3579 0.2071 0.2491 -0.0384 0.0884 -0.0291 316 LYS A N 2102 C CA . LYS A 281 ? 0.4121 0.2424 0.2920 -0.0415 0.0969 -0.0327 316 LYS A CA 2103 C C . LYS A 281 ? 0.4237 0.2436 0.3027 -0.0334 0.1047 -0.0305 316 LYS A C 2104 O O . LYS A 281 ? 0.4501 0.2582 0.3197 -0.0357 0.1107 -0.0345 316 LYS A O 2105 C CB . LYS A 281 ? 0.4438 0.2658 0.3209 -0.0447 0.0994 -0.0328 316 LYS A CB 2106 C CG . LYS A 281 ? 0.5029 0.3042 0.3665 -0.0502 0.1080 -0.0376 316 LYS A CG 2107 C CD . LYS A 281 ? 0.5609 0.3549 0.4210 -0.0557 0.1096 -0.0384 316 LYS A CD 2108 C CE . LYS A 281 ? 0.6168 0.3911 0.4622 -0.0638 0.1171 -0.0445 316 LYS A CE 2109 N NZ . LYS A 281 ? 0.6673 0.4378 0.5093 -0.0718 0.1170 -0.0462 316 LYS A NZ 2110 N N . TYR A 282 ? 0.4216 0.2465 0.3102 -0.0241 0.1047 -0.0243 317 TYR A N 2111 C CA . TYR A 282 ? 0.4509 0.2671 0.3405 -0.0154 0.1123 -0.0211 317 TYR A CA 2112 C C . TYR A 282 ? 0.4344 0.2631 0.3329 -0.0086 0.1098 -0.0176 317 TYR A C 2113 O O . TYR A 282 ? 0.4367 0.2599 0.3365 -0.0016 0.1161 -0.0151 317 TYR A O 2114 C CB . TYR A 282 ? 0.4961 0.3066 0.3891 -0.0096 0.1156 -0.0160 317 TYR A CB 2115 C CG . TYR A 282 ? 0.5327 0.3283 0.4158 -0.0162 0.1196 -0.0194 317 TYR A CG 2116 C CD1 . TYR A 282 ? 0.6043 0.3809 0.4749 -0.0203 0.1280 -0.0245 317 TYR A CD1 2117 C CD2 . TYR A 282 ? 0.5524 0.3522 0.4378 -0.0192 0.1154 -0.0180 317 TYR A CD2 2118 C CE1 . TYR A 282 ? 0.6292 0.3913 0.4900 -0.0275 0.1319 -0.0281 317 TYR A CE1 2119 C CE2 . TYR A 282 ? 0.5807 0.3668 0.4570 -0.0260 0.1194 -0.0213 317 TYR A CE2 2120 C CZ . TYR A 282 ? 0.6233 0.3905 0.4873 -0.0304 0.1276 -0.0264 317 TYR A CZ 2121 O OH . TYR A 282 ? 0.7090 0.4617 0.5633 -0.0380 0.1318 -0.0300 317 TYR A OH 2122 N N . GLY A 283 ? 0.4038 0.2490 0.3084 -0.0108 0.1011 -0.0174 318 GLY A N 2123 C CA . GLY A 283 ? 0.3889 0.2471 0.3030 -0.0048 0.0980 -0.0136 318 GLY A CA 2124 C C . GLY A 283 ? 0.3930 0.2595 0.3178 0.0025 0.0957 -0.0069 318 GLY A C 2125 O O . GLY A 283 ? 0.4162 0.2752 0.3403 0.0050 0.0990 -0.0046 318 GLY A O 2126 N N . PRO A 284 ? 0.3654 0.2470 0.2995 0.0058 0.0902 -0.0037 319 PRO A N 2127 C CA . PRO A 284 ? 0.3727 0.2644 0.3168 0.0116 0.0867 0.0023 319 PRO A CA 2128 C C . PRO A 284 ? 0.4182 0.3056 0.3663 0.0202 0.0928 0.0078 319 PRO A C 2129 O O . PRO A 284 ? 0.4273 0.3199 0.3811 0.0241 0.0905 0.0127 319 PRO A O 2130 C CB . PRO A 284 ? 0.3453 0.2523 0.2967 0.0121 0.0805 0.0035 319 PRO A CB 2131 C CG . PRO A 284 ? 0.3428 0.2459 0.2896 0.0102 0.0839 0.0000 319 PRO A CG 2132 C CD . PRO A 284 ? 0.3474 0.2374 0.2828 0.0038 0.0869 -0.0055 319 PRO A CD 2133 N N . PHE A 285 ? 0.4461 0.3250 0.3916 0.0235 0.1003 0.0074 320 PHE A N 2134 C CA . PHE A 285 ? 0.5244 0.4002 0.4748 0.0327 0.1066 0.0132 320 PHE A CA 2135 C C . PHE A 285 ? 0.5290 0.3852 0.4709 0.0341 0.1155 0.0124 320 PHE A C 2136 O O . PHE A 285 ? 0.5707 0.4217 0.5155 0.0422 0.1222 0.0170 320 PHE A O 2137 C CB . PHE A 285 ? 0.5909 0.4712 0.5455 0.0368 0.1099 0.0142 320 PHE A CB 2138 C CG . PHE A 285 ? 0.6718 0.5701 0.6344 0.0355 0.1020 0.0151 320 PHE A CG 2139 C CD1 . PHE A 285 ? 0.6974 0.6103 0.6699 0.0382 0.0953 0.0203 320 PHE A CD1 2140 C CD2 . PHE A 285 ? 0.7500 0.6502 0.7096 0.0312 0.1013 0.0108 320 PHE A CD2 2141 C CE1 . PHE A 285 ? 0.7242 0.6524 0.7033 0.0364 0.0884 0.0209 320 PHE A CE1 2142 C CE2 . PHE A 285 ? 0.7715 0.6871 0.7380 0.0298 0.0944 0.0119 320 PHE A CE2 2143 C CZ . PHE A 285 ? 0.7615 0.6907 0.7377 0.0323 0.0882 0.0168 320 PHE A CZ 2144 N N . GLY A 286 ? 0.5120 0.3574 0.4438 0.0263 0.1158 0.0068 321 GLY A N 2145 C CA . GLY A 286 ? 0.5751 0.4005 0.4977 0.0264 0.1244 0.0055 321 GLY A CA 2146 C C . GLY A 286 ? 0.5483 0.3728 0.4756 0.0327 0.1252 0.0123 321 GLY A C 2147 O O . GLY A 286 ? 0.5220 0.3597 0.4559 0.0325 0.1175 0.0154 321 GLY A O 2148 N N . PRO A 287 ? 0.5549 0.3633 0.4783 0.0383 0.1349 0.0146 322 PRO A N 2149 C CA . PRO A 287 ? 0.5451 0.3502 0.4709 0.0434 0.1360 0.0209 322 PRO A CA 2150 C C . PRO A 287 ? 0.5249 0.3249 0.4439 0.0351 0.1328 0.0177 322 PRO A C 2151 O O . PRO A 287 ? 0.5112 0.3141 0.4333 0.0377 0.1305 0.0227 322 PRO A O 2152 C CB . PRO A 287 ? 0.5711 0.3565 0.4916 0.0498 0.1483 0.0225 322 PRO A CB 2153 C CG . PRO A 287 ? 0.5869 0.3597 0.4967 0.0432 0.1533 0.0141 322 PRO A CG 2154 C CD . PRO A 287 ? 0.5795 0.3703 0.4947 0.0396 0.1455 0.0114 322 PRO A CD 2155 N N . GLU A 288 ? 0.5258 0.3194 0.4357 0.0251 0.1324 0.0096 323 GLU A N 2156 C CA . GLU A 288 ? 0.5501 0.3421 0.4546 0.0160 0.1284 0.0060 323 GLU A CA 2157 C C . GLU A 288 ? 0.4831 0.2952 0.3962 0.0144 0.1177 0.0080 323 GLU A C 2158 O O . GLU A 288 ? 0.5003 0.3121 0.4106 0.0087 0.1148 0.0066 323 GLU A O 2159 C CB . GLU A 288 ? 0.5708 0.3558 0.4653 0.0053 0.1290 -0.0029 323 GLU A CB 2160 C CG . GLU A 288 ? 0.6340 0.3974 0.5172 0.0043 0.1396 -0.0067 323 GLU A CG 2161 C CD . GLU A 288 ? 0.6210 0.3852 0.5048 0.0079 0.1427 -0.0081 323 GLU A CD 2162 O OE1 . GLU A 288 ? 0.5611 0.3421 0.4554 0.0132 0.1376 -0.0045 323 GLU A OE1 2163 O OE2 . GLU A 288 ? 0.7177 0.4648 0.5908 0.0053 0.1509 -0.0128 323 GLU A OE2 2164 N N . MET A 289 ? 0.4341 0.2630 0.3569 0.0187 0.1120 0.0108 324 MET A N 2165 C CA . MET A 289 ? 0.4193 0.2662 0.3496 0.0174 0.1024 0.0128 324 MET A CA 2166 C C . MET A 289 ? 0.4193 0.2688 0.3537 0.0225 0.1012 0.0194 324 MET A C 2167 O O . MET A 289 ? 0.3954 0.2556 0.3329 0.0198 0.0945 0.0201 324 MET A O 2168 C CB . MET A 289 ? 0.4096 0.2725 0.3485 0.0203 0.0972 0.0140 324 MET A CB 2169 C CG . MET A 289 ? 0.4145 0.2784 0.3498 0.0144 0.0960 0.0076 324 MET A CG 2170 S SD . MET A 289 ? 0.4275 0.2922 0.3566 0.0030 0.0908 0.0010 324 MET A SD 2171 C CE . MET A 289 ? 0.3988 0.2810 0.3372 0.0043 0.0818 0.0049 324 MET A CE 2172 N N . THR A 290 ? 0.4276 0.2674 0.3616 0.0297 0.1080 0.0245 325 THR A N 2173 C CA . THR A 290 ? 0.4347 0.2776 0.3727 0.0355 0.1070 0.0319 325 THR A CA 2174 C C . THR A 290 ? 0.4282 0.2661 0.3605 0.0294 0.1056 0.0305 325 THR A C 2175 O O . THR A 290 ? 0.4000 0.2491 0.3363 0.0295 0.0995 0.0336 325 THR A O 2176 C CB . THR A 290 ? 0.4717 0.3029 0.4095 0.0446 0.1156 0.0376 325 THR A CB 2177 O OG1 . THR A 290 ? 0.5091 0.3474 0.4536 0.0504 0.1165 0.0393 325 THR A OG1 2178 C CG2 . THR A 290 ? 0.4788 0.3135 0.4203 0.0509 0.1144 0.0461 325 THR A CG2 2179 N N . ASN A 291 ? 0.4563 0.2777 0.3788 0.0237 0.1113 0.0256 326 ASN A N 2180 C CA . ASN A 291 ? 0.4966 0.3123 0.4135 0.0176 0.1110 0.0243 326 ASN A CA 2181 C C . ASN A 291 ? 0.4582 0.2889 0.3779 0.0104 0.1021 0.0207 326 ASN A C 2182 O O . ASN A 291 ? 0.4261 0.2619 0.3472 0.0098 0.0989 0.0235 326 ASN A O 2183 C CB . ASN A 291 ? 0.5757 0.3701 0.4814 0.0121 0.1193 0.0195 326 ASN A CB 2184 C CG . ASN A 291 ? 0.6562 0.4332 0.5581 0.0197 0.1288 0.0245 326 ASN A CG 2185 O OD1 . ASN A 291 ? 0.6959 0.4763 0.6030 0.0283 0.1288 0.0325 326 ASN A OD1 2186 N ND2 . ASN A 291 ? 0.7305 0.4887 0.6231 0.0166 0.1370 0.0199 326 ASN A ND2 2187 N N . PRO A 292 ? 0.4280 0.2661 0.3488 0.0054 0.0983 0.0150 327 PRO A N 2188 C CA . PRO A 292 ? 0.4025 0.2554 0.3270 0.0000 0.0901 0.0125 327 PRO A CA 2189 C C . PRO A 292 ? 0.3603 0.2287 0.2932 0.0052 0.0838 0.0177 327 PRO A C 2190 O O . PRO A 292 ? 0.3437 0.2197 0.2780 0.0024 0.0793 0.0179 327 PRO A O 2191 C CB . PRO A 292 ? 0.4242 0.2816 0.3485 -0.0044 0.0878 0.0066 327 PRO A CB 2192 C CG . PRO A 292 ? 0.4645 0.3087 0.3841 -0.0022 0.0951 0.0054 327 PRO A CG 2193 C CD . PRO A 292 ? 0.4501 0.2803 0.3664 0.0029 0.1023 0.0099 327 PRO A CD 2194 N N . LEU A 293 ? 0.3368 0.2096 0.2751 0.0128 0.0839 0.0221 328 LEU A N 2195 C CA . LEU A 293 ? 0.3334 0.2208 0.2792 0.0174 0.0780 0.0273 328 LEU A CA 2196 C C . LEU A 293 ? 0.3475 0.2322 0.2919 0.0203 0.0789 0.0328 328 LEU A C 2197 O O . LEU A 293 ? 0.3300 0.2252 0.2771 0.0197 0.0733 0.0346 328 LEU A O 2198 C CB . LEU A 293 ? 0.3331 0.2266 0.2852 0.0243 0.0780 0.0308 328 LEU A CB 2199 C CG . LEU A 293 ? 0.3307 0.2301 0.2850 0.0215 0.0757 0.0259 328 LEU A CG 2200 C CD1 . LEU A 293 ? 0.3530 0.2564 0.3132 0.0285 0.0775 0.0297 328 LEU A CD1 2201 C CD2 . LEU A 293 ? 0.3145 0.2276 0.2722 0.0169 0.0676 0.0233 328 LEU A CD2 2202 N N . ARG A 294 ? 0.3529 0.2229 0.2926 0.0234 0.0861 0.0356 329 ARG A N 2203 C CA . ARG A 294 ? 0.3709 0.2361 0.3077 0.0253 0.0877 0.0406 329 ARG A CA 2204 C C . ARG A 294 ? 0.3701 0.2353 0.3026 0.0173 0.0854 0.0368 329 ARG A C 2205 O O . ARG A 294 ? 0.3540 0.2246 0.2868 0.0178 0.0825 0.0404 329 ARG A O 2206 C CB . ARG A 294 ? 0.4017 0.2482 0.3328 0.0290 0.0969 0.0433 329 ARG A CB 2207 C CG . ARG A 294 ? 0.4353 0.2813 0.3711 0.0389 0.1003 0.0493 329 ARG A CG 2208 C CD . ARG A 294 ? 0.5024 0.3299 0.4323 0.0435 0.1092 0.0536 329 ARG A CD 2209 N NE . ARG A 294 ? 0.5496 0.3755 0.4842 0.0532 0.1136 0.0590 329 ARG A NE 2210 C CZ . ARG A 294 ? 0.6065 0.4446 0.5492 0.0617 0.1106 0.0673 329 ARG A CZ 2211 N NH1 . ARG A 294 ? 0.6131 0.4653 0.5591 0.0614 0.1031 0.0710 329 ARG A NH1 2212 N NH2 . ARG A 294 ? 0.6397 0.4762 0.5871 0.0706 0.1154 0.0720 329 ARG A NH2 2213 N N . GLU A 295 ? 0.3735 0.2332 0.3019 0.0098 0.0868 0.0298 330 GLU A N 2214 C CA . GLU A 295 ? 0.3893 0.2495 0.3142 0.0018 0.0852 0.0260 330 GLU A CA 2215 C C . GLU A 295 ? 0.3531 0.2309 0.2838 0.0002 0.0770 0.0253 330 GLU A C 2216 O O . GLU A 295 ? 0.3389 0.2201 0.2686 -0.0021 0.0752 0.0261 330 GLU A O 2217 C CB . GLU A 295 ? 0.4255 0.2776 0.3454 -0.0061 0.0881 0.0188 330 GLU A CB 2218 C CG . GLU A 295 ? 0.4926 0.3246 0.4043 -0.0069 0.0969 0.0184 330 GLU A CG 2219 C CD . GLU A 295 ? 0.5551 0.3775 0.4615 -0.0084 0.1007 0.0213 330 GLU A CD 2220 O OE1 . GLU A 295 ? 0.5653 0.3966 0.4736 -0.0109 0.0966 0.0222 330 GLU A OE1 2221 O OE2 . GLU A 295 ? 0.6818 0.4869 0.5818 -0.0070 0.1083 0.0228 330 GLU A OE2 2222 N N . ILE A 296 ? 0.3271 0.2155 0.2633 0.0016 0.0726 0.0237 331 ILE A N 2223 C CA . ILE A 296 ? 0.3110 0.2148 0.2524 0.0006 0.0654 0.0231 331 ILE A CA 2224 C C . ILE A 296 ? 0.3076 0.2170 0.2507 0.0057 0.0631 0.0294 331 ILE A C 2225 O O . ILE A 296 ? 0.3007 0.2170 0.2439 0.0034 0.0596 0.0294 331 ILE A O 2226 C CB . ILE A 296 ? 0.3144 0.2272 0.2610 0.0014 0.0615 0.0208 331 ILE A CB 2227 C CG1 . ILE A 296 ? 0.3314 0.2403 0.2755 -0.0044 0.0627 0.0145 331 ILE A CG1 2228 C CG2 . ILE A 296 ? 0.3148 0.2419 0.2660 0.0009 0.0546 0.0207 331 ILE A CG2 2229 C CD1 . ILE A 296 ? 0.3441 0.2566 0.2913 -0.0025 0.0615 0.0131 331 ILE A CD1 2230 N N . ASP A 297 ? 0.3051 0.2120 0.2496 0.0125 0.0652 0.0349 332 ASP A N 2231 C CA . ASP A 297 ? 0.3094 0.2227 0.2555 0.0173 0.0626 0.0414 332 ASP A CA 2232 C C . ASP A 297 ? 0.3143 0.2209 0.2544 0.0153 0.0649 0.0434 332 ASP A C 2233 O O . ASP A 297 ? 0.2940 0.2081 0.2339 0.0155 0.0612 0.0461 332 ASP A O 2234 C CB . ASP A 297 ? 0.3146 0.2262 0.2635 0.0253 0.0651 0.0478 332 ASP A CB 2235 C CG . ASP A 297 ? 0.3249 0.2476 0.2769 0.0298 0.0605 0.0543 332 ASP A CG 2236 O OD1 . ASP A 297 ? 0.3199 0.2558 0.2770 0.0295 0.0546 0.0535 332 ASP A OD1 2237 O OD2 . ASP A 297 ? 0.3352 0.2534 0.2841 0.0331 0.0626 0.0602 332 ASP A OD2 2238 N N . LYS A 298 ? 0.3368 0.2288 0.2714 0.0132 0.0713 0.0421 333 LYS A N 2239 C CA . LYS A 298 ? 0.3609 0.2455 0.2893 0.0103 0.0742 0.0434 333 LYS A CA 2240 C C . LYS A 298 ? 0.3452 0.2386 0.2737 0.0037 0.0699 0.0391 333 LYS A C 2241 O O . LYS A 298 ? 0.3303 0.2262 0.2564 0.0032 0.0688 0.0419 333 LYS A O 2242 C CB . LYS A 298 ? 0.4049 0.2717 0.3272 0.0077 0.0820 0.0416 333 LYS A CB 2243 C CG . LYS A 298 ? 0.4783 0.3350 0.3937 0.0050 0.0862 0.0436 333 LYS A CG 2244 C CD . LYS A 298 ? 0.5256 0.3632 0.4346 0.0026 0.0944 0.0417 333 LYS A CD 2245 C CE . LYS A 298 ? 0.5838 0.4114 0.4857 -0.0032 0.0986 0.0414 333 LYS A CE 2246 N NZ . LYS A 298 ? 0.6181 0.4360 0.5156 0.0023 0.1028 0.0493 333 LYS A NZ 2247 N N . THR A 299 ? 0.3419 0.2404 0.2732 -0.0009 0.0676 0.0327 334 THR A N 2248 C CA . THR A 299 ? 0.3300 0.2377 0.2625 -0.0064 0.0637 0.0287 334 THR A CA 2249 C C . THR A 299 ? 0.3101 0.2307 0.2459 -0.0035 0.0579 0.0311 334 THR A C 2250 O O . THR A 299 ? 0.2935 0.2185 0.2277 -0.0059 0.0564 0.0310 334 THR A O 2251 C CB . THR A 299 ? 0.3383 0.2492 0.2735 -0.0112 0.0623 0.0221 334 THR A CB 2252 O OG1 . THR A 299 ? 0.3621 0.2607 0.2931 -0.0147 0.0678 0.0197 334 THR A OG1 2253 C CG2 . THR A 299 ? 0.3223 0.2425 0.2593 -0.0165 0.0591 0.0183 334 THR A CG2 2254 N N . VAL A 300 ? 0.2908 0.2173 0.2308 0.0012 0.0548 0.0331 335 VAL A N 2255 C CA . VAL A 300 ? 0.2893 0.2274 0.2317 0.0037 0.0493 0.0357 335 VAL A CA 2256 C C . VAL A 300 ? 0.3090 0.2454 0.2469 0.0060 0.0500 0.0415 335 VAL A C 2257 O O . VAL A 300 ? 0.3079 0.2511 0.2443 0.0045 0.0469 0.0417 335 VAL A O 2258 C CB . VAL A 300 ? 0.2984 0.2431 0.2462 0.0082 0.0462 0.0374 335 VAL A CB 2259 C CG1 . VAL A 300 ? 0.2964 0.2525 0.2458 0.0099 0.0407 0.0402 335 VAL A CG1 2260 C CG2 . VAL A 300 ? 0.2903 0.2376 0.2419 0.0055 0.0449 0.0316 335 VAL A CG2 2261 N N . GLY A 301 ? 0.3093 0.2364 0.2448 0.0099 0.0544 0.0464 336 GLY A N 2262 C CA . GLY A 301 ? 0.3186 0.2422 0.2491 0.0123 0.0560 0.0527 336 GLY A CA 2263 C C . GLY A 301 ? 0.3289 0.2491 0.2538 0.0068 0.0577 0.0506 336 GLY A C 2264 O O . GLY A 301 ? 0.3281 0.2526 0.2497 0.0070 0.0557 0.0537 336 GLY A O 2265 N N . GLN A 302 ? 0.3305 0.2440 0.2545 0.0016 0.0612 0.0452 337 GLN A N 2266 C CA . GLN A 302 ? 0.3474 0.2591 0.2673 -0.0041 0.0631 0.0428 337 GLN A CA 2267 C C . GLN A 302 ? 0.3324 0.2569 0.2541 -0.0064 0.0579 0.0401 337 GLN A C 2268 O O . GLN A 302 ? 0.3359 0.2619 0.2535 -0.0079 0.0582 0.0417 337 GLN A O 2269 C CB . GLN A 302 ? 0.3642 0.2686 0.2838 -0.0100 0.0671 0.0373 337 GLN A CB 2270 C CG . GLN A 302 ? 0.3917 0.2803 0.3065 -0.0096 0.0738 0.0395 337 GLN A CG 2271 C CD . GLN A 302 ? 0.4271 0.3088 0.3415 -0.0159 0.0772 0.0335 337 GLN A CD 2272 O OE1 . GLN A 302 ? 0.4077 0.2976 0.3258 -0.0206 0.0744 0.0278 337 GLN A OE1 2273 N NE2 . GLN A 302 ? 0.4790 0.3456 0.3884 -0.0160 0.0834 0.0347 337 GLN A NE2 2274 N N . LEU A 303 ? 0.3037 0.2368 0.2312 -0.0065 0.0538 0.0363 338 LEU A N 2275 C CA . LEU A 303 ? 0.2923 0.2362 0.2213 -0.0081 0.0493 0.0336 338 LEU A CA 2276 C C . LEU A 303 ? 0.2932 0.2421 0.2192 -0.0049 0.0463 0.0384 338 LEU A C 2277 O O . LEU A 303 ? 0.2956 0.2481 0.2181 -0.0070 0.0455 0.0379 338 LEU A O 2278 C CB . LEU A 303 ? 0.2783 0.2293 0.2136 -0.0081 0.0455 0.0295 338 LEU A CB 2279 C CG . LEU A 303 ? 0.2713 0.2323 0.2081 -0.0094 0.0413 0.0265 338 LEU A CG 2280 C CD1 . LEU A 303 ? 0.2661 0.2277 0.2015 -0.0139 0.0434 0.0231 338 LEU A CD1 2281 C CD2 . LEU A 303 ? 0.2710 0.2378 0.2137 -0.0089 0.0377 0.0232 338 LEU A CD2 2282 N N . MET A 304 ? 0.2886 0.2383 0.2159 0.0001 0.0445 0.0430 339 MET A N 2283 C CA . MET A 304 ? 0.2897 0.2459 0.2144 0.0028 0.0408 0.0478 339 MET A CA 2284 C C . MET A 304 ? 0.2989 0.2501 0.2160 0.0030 0.0434 0.0528 339 MET A C 2285 O O . MET A 304 ? 0.3009 0.2575 0.2136 0.0020 0.0408 0.0539 339 MET A O 2286 C CB . MET A 304 ? 0.2954 0.2558 0.2244 0.0081 0.0380 0.0521 339 MET A CB 2287 C CG . MET A 304 ? 0.2823 0.2494 0.2181 0.0077 0.0346 0.0477 339 MET A CG 2288 S SD . MET A 304 ? 0.2861 0.2616 0.2222 0.0027 0.0305 0.0411 339 MET A SD 2289 C CE . MET A 304 ? 0.2975 0.2816 0.2295 0.0038 0.0255 0.0456 339 MET A CE 2290 N N . ASP A 305 ? 0.3177 0.2579 0.2327 0.0043 0.0487 0.0556 340 ASP A N 2291 C CA . ASP A 305 ? 0.3394 0.2727 0.2468 0.0040 0.0522 0.0602 340 ASP A CA 2292 C C . ASP A 305 ? 0.3386 0.2727 0.2426 -0.0021 0.0536 0.0555 340 ASP A C 2293 O O . ASP A 305 ? 0.3340 0.2693 0.2317 -0.0029 0.0534 0.0581 340 ASP A O 2294 C CB . ASP A 305 ? 0.3521 0.2713 0.2577 0.0053 0.0587 0.0628 340 ASP A CB 2295 C CG . ASP A 305 ? 0.3855 0.3019 0.2936 0.0125 0.0590 0.0689 340 ASP A CG 2296 O OD1 . ASP A 305 ? 0.4168 0.3431 0.3280 0.0166 0.0541 0.0722 340 ASP A OD1 2297 O OD2 . ASP A 305 ? 0.4256 0.3296 0.3327 0.0139 0.0648 0.0703 340 ASP A OD2 2298 N N . GLY A 306 ? 0.3301 0.2639 0.2381 -0.0063 0.0549 0.0487 341 GLY A N 2299 C CA . GLY A 306 ? 0.3302 0.2667 0.2367 -0.0118 0.0561 0.0441 341 GLY A CA 2300 C C . GLY A 306 ? 0.3245 0.2714 0.2299 -0.0122 0.0517 0.0426 341 GLY A C 2301 O O . GLY A 306 ? 0.3432 0.2911 0.2436 -0.0148 0.0531 0.0423 341 GLY A O 2302 N N . LEU A 307 ? 0.3042 0.2584 0.2139 -0.0100 0.0467 0.0414 342 LEU A N 2303 C CA . LEU A 307 ? 0.3115 0.2742 0.2191 -0.0105 0.0425 0.0400 342 LEU A CA 2304 C C . LEU A 307 ? 0.3340 0.2972 0.2337 -0.0089 0.0414 0.0459 342 LEU A C 2305 O O . LEU A 307 ? 0.3457 0.3120 0.2398 -0.0112 0.0409 0.0448 342 LEU A O 2306 C CB . LEU A 307 ? 0.3054 0.2749 0.2188 -0.0087 0.0376 0.0380 342 LEU A CB 2307 C CG . LEU A 307 ? 0.3009 0.2716 0.2214 -0.0105 0.0378 0.0318 342 LEU A CG 2308 C CD1 . LEU A 307 ? 0.3033 0.2792 0.2291 -0.0083 0.0334 0.0311 342 LEU A CD1 2309 C CD2 . LEU A 307 ? 0.3090 0.2831 0.2292 -0.0141 0.0386 0.0267 342 LEU A CD2 2310 N N . LYS A 308 ? 0.3352 0.2955 0.2342 -0.0047 0.0410 0.0523 343 LYS A N 2311 C CA . LYS A 308 ? 0.3458 0.3073 0.2376 -0.0027 0.0396 0.0590 343 LYS A CA 2312 C C . LYS A 308 ? 0.3735 0.3288 0.2572 -0.0054 0.0441 0.0603 343 LYS A C 2313 O O . LYS A 308 ? 0.3677 0.3265 0.2439 -0.0066 0.0425 0.0621 343 LYS A O 2314 C CB . LYS A 308 ? 0.3605 0.3198 0.2544 0.0030 0.0391 0.0662 343 LYS A CB 2315 C CG . LYS A 308 ? 0.3878 0.3513 0.2756 0.0058 0.0359 0.0738 343 LYS A CG 2316 C CD . LYS A 308 ? 0.4095 0.3716 0.3009 0.0124 0.0358 0.0813 343 LYS A CD 2317 C CE . LYS A 308 ? 0.4426 0.4072 0.3269 0.0154 0.0338 0.0902 343 LYS A CE 2318 N NZ . LYS A 308 ? 0.4593 0.4187 0.3463 0.0222 0.0362 0.0982 343 LYS A NZ 2319 N N . GLN A 309 ? 0.3706 0.3169 0.2553 -0.0070 0.0499 0.0592 344 GLN A N 2320 C CA . GLN A 309 ? 0.4132 0.3537 0.2912 -0.0105 0.0548 0.0595 344 GLN A CA 2321 C C . GLN A 309 ? 0.3931 0.3397 0.2687 -0.0149 0.0545 0.0542 344 GLN A C 2322 O O . GLN A 309 ? 0.4174 0.3625 0.2851 -0.0168 0.0567 0.0562 344 GLN A O 2323 C CB . GLN A 309 ? 0.4481 0.3794 0.3289 -0.0132 0.0608 0.0572 344 GLN A CB 2324 C CG . GLN A 309 ? 0.5172 0.4386 0.3983 -0.0097 0.0635 0.0621 344 GLN A CG 2325 C CD . GLN A 309 ? 0.5341 0.4443 0.4138 -0.0136 0.0705 0.0609 344 GLN A CD 2326 O OE1 . GLN A 309 ? 0.6014 0.5014 0.4758 -0.0119 0.0743 0.0666 344 GLN A OE1 2327 N NE2 . GLN A 309 ? 0.5165 0.4285 0.4009 -0.0189 0.0720 0.0539 344 GLN A NE2 2328 N N . LEU A 310 ? 0.3868 0.3397 0.2690 -0.0163 0.0522 0.0477 345 LEU A N 2329 C CA . LEU A 310 ? 0.3907 0.3494 0.2713 -0.0197 0.0521 0.0425 345 LEU A CA 2330 C C . LEU A 310 ? 0.3718 0.3373 0.2478 -0.0187 0.0469 0.0428 345 LEU A C 2331 O O . LEU A 310 ? 0.3741 0.3437 0.2488 -0.0210 0.0466 0.0380 345 LEU A O 2332 C CB . LEU A 310 ? 0.3973 0.3591 0.2869 -0.0215 0.0526 0.0357 345 LEU A CB 2333 C CG . LEU A 310 ? 0.4288 0.3856 0.3233 -0.0238 0.0572 0.0341 345 LEU A CG 2334 C CD1 . LEU A 310 ? 0.4321 0.3942 0.3356 -0.0250 0.0561 0.0279 345 LEU A CD1 2335 C CD2 . LEU A 310 ? 0.4594 0.4127 0.3489 -0.0274 0.0628 0.0347 345 LEU A CD2 2336 N N . ARG A 311 ? 0.3680 0.3347 0.2416 -0.0153 0.0430 0.0484 346 ARG A N 2337 C CA . ARG A 311 ? 0.3648 0.3389 0.2347 -0.0149 0.0372 0.0489 346 ARG A CA 2338 C C . ARG A 311 ? 0.3386 0.3184 0.2146 -0.0159 0.0340 0.0425 346 ARG A C 2339 O O . ARG A 311 ? 0.3102 0.2946 0.1816 -0.0179 0.0313 0.0398 346 ARG A O 2340 C CB . ARG A 311 ? 0.4056 0.3801 0.2638 -0.0175 0.0380 0.0503 346 ARG A CB 2341 C CG . ARG A 311 ? 0.4880 0.4570 0.3396 -0.0159 0.0404 0.0580 346 ARG A CG 2342 C CD . ARG A 311 ? 0.5710 0.5425 0.4235 -0.0112 0.0359 0.0654 346 ARG A CD 2343 N NE . ARG A 311 ? 0.6662 0.6294 0.5193 -0.0081 0.0398 0.0716 346 ARG A NE 2344 C CZ . ARG A 311 ? 0.6822 0.6411 0.5268 -0.0069 0.0417 0.0786 346 ARG A CZ 2345 N NH1 . ARG A 311 ? 0.8058 0.7687 0.6400 -0.0088 0.0396 0.0808 346 ARG A NH1 2346 N NH2 . ARG A 311 ? 0.7239 0.6737 0.5697 -0.0040 0.0459 0.0836 346 ARG A NH2 2347 N N . LEU A 312 ? 0.3165 0.2955 0.2022 -0.0146 0.0344 0.0403 347 LEU A N 2348 C CA . LEU A 312 ? 0.3127 0.2961 0.2048 -0.0152 0.0319 0.0345 347 LEU A CA 2349 C C . LEU A 312 ? 0.2980 0.2850 0.1963 -0.0122 0.0274 0.0365 347 LEU A C 2350 O O . LEU A 312 ? 0.2814 0.2720 0.1849 -0.0127 0.0250 0.0324 347 LEU A O 2351 C CB . LEU A 312 ? 0.3271 0.3077 0.2257 -0.0166 0.0359 0.0297 347 LEU A CB 2352 C CG . LEU A 312 ? 0.3465 0.3266 0.2421 -0.0198 0.0399 0.0258 347 LEU A CG 2353 C CD1 . LEU A 312 ? 0.3348 0.3131 0.2378 -0.0210 0.0437 0.0226 347 LEU A CD1 2354 C CD2 . LEU A 312 ? 0.3568 0.3412 0.2501 -0.0210 0.0379 0.0213 347 LEU A CD2 2355 N N . HIS A 313 ? 0.2930 0.2789 0.1907 -0.0090 0.0267 0.0431 348 HIS A N 2356 C CA . HIS A 313 ? 0.2894 0.2788 0.1935 -0.0055 0.0233 0.0459 348 HIS A CA 2357 C C . HIS A 313 ? 0.2897 0.2881 0.1935 -0.0060 0.0173 0.0459 348 HIS A C 2358 O O . HIS A 313 ? 0.2942 0.2968 0.2046 -0.0038 0.0145 0.0470 348 HIS A O 2359 C CB . HIS A 313 ? 0.2940 0.2796 0.1978 -0.0013 0.0248 0.0535 348 HIS A CB 2360 C CG . HIS A 313 ? 0.3137 0.3020 0.2096 -0.0004 0.0228 0.0598 348 HIS A CG 2361 N ND1 . HIS A 313 ? 0.3257 0.3116 0.2126 -0.0033 0.0247 0.0596 348 HIS A ND1 2362 C CD2 . HIS A 313 ? 0.3194 0.3132 0.2150 0.0031 0.0191 0.0668 348 HIS A CD2 2363 C CE1 . HIS A 313 ? 0.3487 0.3381 0.2292 -0.0019 0.0219 0.0660 348 HIS A CE1 2364 N NE2 . HIS A 313 ? 0.3426 0.3373 0.2287 0.0021 0.0184 0.0707 348 HIS A NE2 2365 N N . ARG A 314 ? 0.2927 0.2942 0.1886 -0.0092 0.0154 0.0446 349 ARG A N 2366 C CA . ARG A 314 ? 0.2963 0.3056 0.1908 -0.0113 0.0100 0.0432 349 ARG A CA 2367 C C . ARG A 314 ? 0.3126 0.3208 0.2039 -0.0156 0.0107 0.0355 349 ARG A C 2368 O O . ARG A 314 ? 0.3204 0.3327 0.2063 -0.0186 0.0074 0.0337 349 ARG A O 2369 C CB . ARG A 314 ? 0.3130 0.3275 0.1996 -0.0113 0.0064 0.0493 349 ARG A CB 2370 C CG . ARG A 314 ? 0.3201 0.3371 0.2110 -0.0062 0.0050 0.0577 349 ARG A CG 2371 C CD . ARG A 314 ? 0.3388 0.3608 0.2215 -0.0059 0.0019 0.0646 349 ARG A CD 2372 N NE . ARG A 314 ? 0.3457 0.3774 0.2245 -0.0097 -0.0042 0.0635 349 ARG A NE 2373 C CZ . ARG A 314 ? 0.3618 0.4031 0.2470 -0.0089 -0.0093 0.0654 349 ARG A CZ 2374 N NH1 . ARG A 314 ? 0.3727 0.4153 0.2686 -0.0038 -0.0089 0.0689 349 ARG A NH1 2375 N NH2 . ARG A 314 ? 0.3888 0.4383 0.2693 -0.0137 -0.0148 0.0638 349 ARG A NH2 2376 N N . CYS A 315 ? 0.3089 0.3116 0.2040 -0.0158 0.0153 0.0311 350 CYS A N 2377 C CA . CYS A 315 ? 0.3294 0.3303 0.2232 -0.0187 0.0173 0.0241 350 CYS A CA 2378 C C . CYS A 315 ? 0.3168 0.3171 0.2203 -0.0178 0.0180 0.0200 350 CYS A C 2379 O O . CYS A 315 ? 0.3578 0.3593 0.2620 -0.0193 0.0167 0.0155 350 CYS A O 2380 C CB . CYS A 315 ? 0.3705 0.3663 0.2596 -0.0197 0.0227 0.0234 350 CYS A CB 2381 S SG . CYS A 315 ? 0.4197 0.4132 0.3096 -0.0219 0.0270 0.0157 350 CYS A SG 2382 N N . VAL A 316 ? 0.2963 0.2942 0.2065 -0.0154 0.0201 0.0216 351 VAL A N 2383 C CA . VAL A 316 ? 0.2893 0.2865 0.2080 -0.0148 0.0209 0.0180 351 VAL A CA 2384 C C . VAL A 316 ? 0.2795 0.2805 0.2035 -0.0133 0.0168 0.0188 351 VAL A C 2385 O O . VAL A 316 ? 0.2932 0.2965 0.2174 -0.0114 0.0145 0.0236 351 VAL A O 2386 C CB . VAL A 316 ? 0.3050 0.2977 0.2275 -0.0137 0.0249 0.0192 351 VAL A CB 2387 C CG1 . VAL A 316 ? 0.3292 0.3217 0.2599 -0.0131 0.0252 0.0165 351 VAL A CG1 2388 C CG2 . VAL A 316 ? 0.3035 0.2936 0.2221 -0.0158 0.0292 0.0177 351 VAL A CG2 2389 N N . ASN A 317 ? 0.2547 0.2565 0.1830 -0.0140 0.0161 0.0145 352 ASN A N 2390 C CA . ASN A 317 ? 0.2367 0.2412 0.1714 -0.0126 0.0133 0.0150 352 ASN A CA 2391 C C . ASN A 317 ? 0.2348 0.2362 0.1758 -0.0108 0.0159 0.0151 352 ASN A C 2392 O O . ASN A 317 ? 0.2398 0.2386 0.1822 -0.0117 0.0188 0.0120 352 ASN A O 2393 C CB . ASN A 317 ? 0.2334 0.2396 0.1688 -0.0144 0.0113 0.0106 352 ASN A CB 2394 C CG . ASN A 317 ? 0.2489 0.2578 0.1776 -0.0169 0.0083 0.0104 352 ASN A CG 2395 O OD1 . ASN A 317 ? 0.2486 0.2620 0.1762 -0.0169 0.0049 0.0142 352 ASN A OD1 2396 N ND2 . ASN A 317 ? 0.2426 0.2490 0.1664 -0.0192 0.0097 0.0061 352 ASN A ND2 2397 N N . VAL A 318 ? 0.2319 0.2339 0.1764 -0.0084 0.0151 0.0186 353 VAL A N 2398 C CA . VAL A 318 ? 0.2427 0.2409 0.1920 -0.0069 0.0177 0.0186 353 VAL A CA 2399 C C . VAL A 318 ? 0.2401 0.2411 0.1951 -0.0059 0.0155 0.0178 353 VAL A C 2400 O O . VAL A 318 ? 0.2476 0.2531 0.2037 -0.0048 0.0126 0.0204 353 VAL A O 2401 C CB . VAL A 318 ? 0.2533 0.2477 0.2013 -0.0045 0.0200 0.0236 353 VAL A CB 2402 C CG1 . VAL A 318 ? 0.2622 0.2513 0.2141 -0.0037 0.0232 0.0229 353 VAL A CG1 2403 C CG2 . VAL A 318 ? 0.2664 0.2578 0.2083 -0.0058 0.0223 0.0246 353 VAL A CG2 2404 N N . ILE A 319 ? 0.2197 0.2186 0.1782 -0.0067 0.0169 0.0144 354 ILE A N 2405 C CA . ILE A 319 ? 0.2281 0.2286 0.1916 -0.0058 0.0156 0.0137 354 ILE A CA 2406 C C . ILE A 319 ? 0.2411 0.2367 0.2065 -0.0045 0.0188 0.0145 354 ILE A C 2407 O O . ILE A 319 ? 0.2455 0.2373 0.2101 -0.0061 0.0214 0.0125 354 ILE A O 2408 C CB . ILE A 319 ? 0.2341 0.2360 0.1993 -0.0076 0.0144 0.0093 354 ILE A CB 2409 C CG1 . ILE A 319 ? 0.2305 0.2359 0.1933 -0.0089 0.0115 0.0085 354 ILE A CG1 2410 C CG2 . ILE A 319 ? 0.2379 0.2400 0.2077 -0.0069 0.0140 0.0085 354 ILE A CG2 2411 C CD1 . ILE A 319 ? 0.2299 0.2352 0.1932 -0.0104 0.0111 0.0043 354 ILE A CD1 2412 N N . PHE A 320 ? 0.2263 0.2222 0.1941 -0.0019 0.0187 0.0175 355 PHE A N 2413 C CA . PHE A 320 ? 0.2272 0.2176 0.1964 -0.0005 0.0222 0.0180 355 PHE A CA 2414 C C . PHE A 320 ? 0.2112 0.2037 0.1843 -0.0005 0.0211 0.0160 355 PHE A C 2415 O O . PHE A 320 ? 0.2233 0.2207 0.1992 0.0010 0.0189 0.0179 355 PHE A O 2416 C CB . PHE A 320 ? 0.2285 0.2171 0.1975 0.0032 0.0239 0.0234 355 PHE A CB 2417 C CG . PHE A 320 ? 0.2439 0.2246 0.2129 0.0048 0.0285 0.0239 355 PHE A CG 2418 C CD1 . PHE A 320 ? 0.2491 0.2216 0.2141 0.0035 0.0324 0.0234 355 PHE A CD1 2419 C CD2 . PHE A 320 ? 0.2365 0.2175 0.2092 0.0074 0.0293 0.0249 355 PHE A CD2 2420 C CE1 . PHE A 320 ? 0.2609 0.2246 0.2249 0.0044 0.0371 0.0235 355 PHE A CE1 2421 C CE2 . PHE A 320 ? 0.2389 0.2114 0.2107 0.0088 0.0342 0.0250 355 PHE A CE2 2422 C CZ . PHE A 320 ? 0.2528 0.2163 0.2199 0.0072 0.0381 0.0241 355 PHE A CZ 2423 N N . VAL A 321 ? 0.2088 0.1979 0.1820 -0.0026 0.0226 0.0125 356 VAL A N 2424 C CA . VAL A 321 ? 0.2233 0.2145 0.1993 -0.0033 0.0212 0.0102 356 VAL A CA 2425 C C . VAL A 321 ? 0.2271 0.2130 0.2023 -0.0046 0.0241 0.0080 356 VAL A C 2426 O O . VAL A 321 ? 0.2264 0.2082 0.1990 -0.0067 0.0262 0.0065 356 VAL A O 2427 C CB . VAL A 321 ? 0.2531 0.2489 0.2295 -0.0054 0.0180 0.0076 356 VAL A CB 2428 C CG1 . VAL A 321 ? 0.2556 0.2497 0.2305 -0.0079 0.0191 0.0047 356 VAL A CG1 2429 C CG2 . VAL A 321 ? 0.3073 0.3058 0.2864 -0.0056 0.0161 0.0062 356 VAL A CG2 2430 N N . GLY A 322 ? 0.2162 0.2020 0.1931 -0.0038 0.0243 0.0077 357 GLY A N 2431 C CA . GLY A 322 ? 0.2248 0.2060 0.2002 -0.0057 0.0266 0.0052 357 GLY A CA 2432 C C . GLY A 322 ? 0.2270 0.2117 0.2035 -0.0078 0.0240 0.0024 357 GLY A C 2433 O O . GLY A 322 ? 0.2128 0.2029 0.1916 -0.0074 0.0209 0.0026 357 GLY A O 2434 N N . ASP A 323 ? 0.2334 0.2149 0.2077 -0.0104 0.0255 0.0000 358 ASP A N 2435 C CA . ASP A 323 ? 0.2148 0.2000 0.1899 -0.0124 0.0229 -0.0022 358 ASP A CA 2436 C C . ASP A 323 ? 0.2087 0.1931 0.1837 -0.0116 0.0233 -0.0021 358 ASP A C 2437 O O . ASP A 323 ? 0.1919 0.1803 0.1684 -0.0118 0.0207 -0.0025 358 ASP A O 2438 C CB . ASP A 323 ? 0.2302 0.2149 0.2032 -0.0162 0.0231 -0.0048 358 ASP A CB 2439 C CG . ASP A 323 ? 0.2354 0.2130 0.2040 -0.0185 0.0268 -0.0061 358 ASP A CG 2440 O OD1 . ASP A 323 ? 0.2119 0.1835 0.1788 -0.0165 0.0301 -0.0048 358 ASP A OD1 2441 O OD2 . ASP A 323 ? 0.2824 0.2604 0.2490 -0.0225 0.0265 -0.0085 358 ASP A OD2 2442 N N . HIS A 324 ? 0.2025 0.1815 0.1757 -0.0103 0.0270 -0.0013 359 HIS A N 2443 C CA . HIS A 324 ? 0.2071 0.1848 0.1800 -0.0093 0.0285 -0.0012 359 HIS A CA 2444 C C . HIS A 324 ? 0.2161 0.1869 0.1873 -0.0070 0.0336 0.0000 359 HIS A C 2445 O O . HIS A 324 ? 0.2081 0.1745 0.1776 -0.0067 0.0358 0.0006 359 HIS A O 2446 C CB . HIS A 324 ? 0.1976 0.1741 0.1669 -0.0130 0.0282 -0.0042 359 HIS A CB 2447 C CG . HIS A 324 ? 0.2068 0.1780 0.1714 -0.0165 0.0303 -0.0066 359 HIS A CG 2448 N ND1 . HIS A 324 ? 0.2132 0.1757 0.1735 -0.0167 0.0352 -0.0073 359 HIS A ND1 2449 C CD2 . HIS A 324 ? 0.2185 0.1919 0.1822 -0.0200 0.0283 -0.0084 359 HIS A CD2 2450 C CE1 . HIS A 324 ? 0.2225 0.1816 0.1788 -0.0209 0.0361 -0.0097 359 HIS A CE1 2451 N NE2 . HIS A 324 ? 0.2195 0.1860 0.1783 -0.0230 0.0318 -0.0103 359 HIS A NE2 2452 N N . GLY A 325 ? 0.2203 0.1895 0.1915 -0.0054 0.0360 0.0005 360 GLY A N 2453 C CA . GLY A 325 ? 0.2268 0.1891 0.1965 -0.0026 0.0416 0.0017 360 GLY A CA 2454 C C . GLY A 325 ? 0.2288 0.1817 0.1913 -0.0057 0.0457 -0.0017 360 GLY A C 2455 O O . GLY A 325 ? 0.2369 0.1881 0.1952 -0.0104 0.0444 -0.0049 360 GLY A O 2456 N N . MET A 326 ? 0.2423 0.1894 0.2033 -0.0030 0.0510 -0.0010 361 MET A N 2457 C CA . MET A 326 ? 0.2471 0.1834 0.2003 -0.0055 0.0562 -0.0044 361 MET A CA 2458 C C . MET A 326 ? 0.2560 0.1894 0.2090 -0.0022 0.0610 -0.0036 361 MET A C 2459 O O . MET A 326 ? 0.2503 0.1860 0.2090 0.0034 0.0630 0.0003 361 MET A O 2460 C CB . MET A 326 ? 0.2522 0.1789 0.2019 -0.0051 0.0605 -0.0042 361 MET A CB 2461 C CG . MET A 326 ? 0.2782 0.1920 0.2183 -0.0089 0.0661 -0.0084 361 MET A CG 2462 S SD . MET A 326 ? 0.2806 0.1950 0.2140 -0.0182 0.0623 -0.0139 361 MET A SD 2463 C CE . MET A 326 ? 0.2590 0.1772 0.1955 -0.0199 0.0586 -0.0129 361 MET A CE 2464 N N . GLU A 327 ? 0.2748 0.2035 0.2211 -0.0059 0.0630 -0.0073 362 GLU A N 2465 C CA . GLU A 327 ? 0.2916 0.2169 0.2366 -0.0034 0.0680 -0.0072 362 GLU A CA 2466 C C . GLU A 327 ? 0.3148 0.2255 0.2497 -0.0054 0.0752 -0.0108 362 GLU A C 2467 O O . GLU A 327 ? 0.3089 0.2136 0.2372 -0.0107 0.0748 -0.0142 362 GLU A O 2468 C CB . GLU A 327 ? 0.2811 0.2135 0.2259 -0.0062 0.0642 -0.0083 362 GLU A CB 2469 C CG . GLU A 327 ? 0.2872 0.2177 0.2304 -0.0044 0.0688 -0.0084 362 GLU A CG 2470 C CD . GLU A 327 ? 0.2977 0.2329 0.2499 0.0025 0.0715 -0.0036 362 GLU A CD 2471 O OE1 . GLU A 327 ? 0.3216 0.2500 0.2740 0.0066 0.0774 -0.0023 362 GLU A OE1 2472 O OE2 . GLU A 327 ? 0.3143 0.2600 0.2735 0.0037 0.0678 -0.0010 362 GLU A OE2 2473 N N . ASP A 328 ? 0.3233 0.2283 0.2572 -0.0015 0.0819 -0.0101 363 ASP A N 2474 C CA . ASP A 328 ? 0.3555 0.2456 0.2784 -0.0039 0.0895 -0.0142 363 ASP A CA 2475 C C . ASP A 328 ? 0.3429 0.2328 0.2577 -0.0107 0.0875 -0.0189 363 ASP A C 2476 O O . ASP A 328 ? 0.3079 0.2040 0.2248 -0.0097 0.0866 -0.0181 363 ASP A O 2477 C CB . ASP A 328 ? 0.4050 0.2903 0.3300 0.0030 0.0975 -0.0118 363 ASP A CB 2478 C CG . ASP A 328 ? 0.4526 0.3350 0.3834 0.0097 0.1011 -0.0074 363 ASP A CG 2479 O OD1 . ASP A 328 ? 0.5458 0.4164 0.4703 0.0082 0.1044 -0.0092 363 ASP A OD1 2480 O OD2 . ASP A 328 ? 0.5394 0.4311 0.4806 0.0163 0.1006 -0.0021 363 ASP A OD2 2481 N N . VAL A 329 ? 0.3429 0.2260 0.2484 -0.0178 0.0869 -0.0234 364 VAL A N 2482 C CA . VAL A 329 ? 0.3638 0.2468 0.2604 -0.0251 0.0846 -0.0278 364 VAL A CA 2483 C C . VAL A 329 ? 0.4022 0.2702 0.2861 -0.0310 0.0899 -0.0331 364 VAL A C 2484 O O . VAL A 329 ? 0.4051 0.2692 0.2881 -0.0332 0.0895 -0.0339 364 VAL A O 2485 C CB . VAL A 329 ? 0.3493 0.2451 0.2497 -0.0292 0.0749 -0.0275 364 VAL A CB 2486 C CG1 . VAL A 329 ? 0.3789 0.2763 0.2708 -0.0359 0.0722 -0.0309 364 VAL A CG1 2487 C CG2 . VAL A 329 ? 0.3204 0.2293 0.2331 -0.0237 0.0700 -0.0224 364 VAL A CG2 2488 N N . THR A 330 ? 0.4142 0.2734 0.2877 -0.0338 0.0951 -0.0368 365 THR A N 2489 C CA . THR A 330 ? 0.4601 0.3041 0.3196 -0.0406 0.1003 -0.0425 365 THR A CA 2490 C C . THR A 330 ? 0.5009 0.3466 0.3501 -0.0490 0.0972 -0.0469 365 THR A C 2491 O O . THR A 330 ? 0.4591 0.3144 0.3109 -0.0479 0.0936 -0.0453 365 THR A O 2492 C CB . THR A 330 ? 0.4797 0.3076 0.3340 -0.0359 0.1117 -0.0434 365 THR A CB 2493 O OG1 . THR A 330 ? 0.4765 0.3060 0.3296 -0.0333 0.1144 -0.0432 365 THR A OG1 2494 C CG2 . THR A 330 ? 0.4793 0.3072 0.3448 -0.0266 0.1145 -0.0380 365 THR A CG2 2495 N N . CYS A 331 ? 0.5233 0.3594 0.3603 -0.0576 0.0987 -0.0523 366 CYS A N 2496 C CA . CYS A 331 ? 0.5569 0.3950 0.3831 -0.0667 0.0952 -0.0565 366 CYS A CA 2497 C C . CYS A 331 ? 0.5577 0.3904 0.3757 -0.0661 0.1003 -0.0583 366 CYS A C 2498 O O . CYS A 331 ? 0.5598 0.3992 0.3723 -0.0712 0.0957 -0.0596 366 CYS A O 2499 C CB . CYS A 331 ? 0.6519 0.4800 0.4664 -0.0764 0.0966 -0.0621 366 CYS A CB 2500 S SG . CYS A 331 ? 0.7664 0.5685 0.5661 -0.0779 0.1101 -0.0676 366 CYS A SG 2501 N N . ASP A 332 ? 0.5378 0.3593 0.3554 -0.0595 0.1097 -0.0578 367 ASP A N 2502 C CA . ASP A 332 ? 0.5566 0.3736 0.3685 -0.0573 0.1154 -0.0587 367 ASP A CA 2503 C C . ASP A 332 ? 0.5203 0.3534 0.3419 -0.0529 0.1098 -0.0539 367 ASP A C 2504 O O . ASP A 332 ? 0.5203 0.3525 0.3353 -0.0540 0.1121 -0.0551 367 ASP A O 2505 C CB . ASP A 332 ? 0.6185 0.4212 0.4305 -0.0497 0.1271 -0.0583 367 ASP A CB 2506 C CG . ASP A 332 ? 0.7149 0.4969 0.5122 -0.0551 0.1352 -0.0644 367 ASP A CG 2507 O OD1 . ASP A 332 ? 0.7893 0.5629 0.5709 -0.0634 0.1374 -0.0703 367 ASP A OD1 2508 O OD2 . ASP A 332 ? 0.8127 0.5865 0.6135 -0.0513 0.1394 -0.0632 367 ASP A OD2 2509 N N . ARG A 333 ? 0.4763 0.3232 0.3127 -0.0482 0.1030 -0.0486 368 ARG A N 2510 C CA . ARG A 333 ? 0.4348 0.2964 0.2807 -0.0444 0.0975 -0.0441 368 ARG A CA 2511 C C . ARG A 333 ? 0.4128 0.2865 0.2594 -0.0503 0.0869 -0.0438 368 ARG A C 2512 O O . ARG A 333 ? 0.3868 0.2718 0.2449 -0.0476 0.0803 -0.0399 368 ARG A O 2513 C CB . ARG A 333 ? 0.4105 0.2788 0.2722 -0.0351 0.0977 -0.0383 368 ARG A CB 2514 C CG . ARG A 333 ? 0.4314 0.2898 0.2937 -0.0284 0.1080 -0.0376 368 ARG A CG 2515 C CD . ARG A 333 ? 0.4172 0.2860 0.2954 -0.0196 0.1071 -0.0313 368 ARG A CD 2516 N NE . ARG A 333 ? 0.3821 0.2549 0.2692 -0.0171 0.1032 -0.0286 368 ARG A NE 2517 C CZ . ARG A 333 ? 0.4047 0.2685 0.2927 -0.0134 0.1086 -0.0280 368 ARG A CZ 2518 N NH1 . ARG A 333 ? 0.4257 0.2748 0.3063 -0.0115 0.1187 -0.0302 368 ARG A NH1 2519 N NH2 . ARG A 333 ? 0.4010 0.2699 0.2971 -0.0114 0.1042 -0.0251 368 ARG A NH2 2520 N N . THR A 334 ? 0.3944 0.2654 0.2281 -0.0583 0.0856 -0.0478 369 THR A N 2521 C CA . THR A 334 ? 0.3875 0.2702 0.2208 -0.0639 0.0760 -0.0473 369 THR A CA 2522 C C . THR A 334 ? 0.3900 0.2760 0.2157 -0.0667 0.0745 -0.0474 369 THR A C 2523 O O . THR A 334 ? 0.4141 0.2900 0.2265 -0.0707 0.0801 -0.0515 369 THR A O 2524 C CB . THR A 334 ? 0.4092 0.2879 0.2341 -0.0723 0.0741 -0.0517 369 THR A CB 2525 O OG1 . THR A 334 ? 0.4098 0.2844 0.2413 -0.0697 0.0761 -0.0514 369 THR A OG1 2526 C CG2 . THR A 334 ? 0.3963 0.2895 0.2229 -0.0774 0.0636 -0.0503 369 THR A CG2 2527 N N . GLU A 335 ? 0.3861 0.2854 0.2198 -0.0645 0.0674 -0.0429 370 GLU A N 2528 C CA . GLU A 335 ? 0.3873 0.2918 0.2144 -0.0677 0.0641 -0.0422 370 GLU A CA 2529 C C . GLU A 335 ? 0.3836 0.2945 0.2047 -0.0755 0.0565 -0.0434 370 GLU A C 2530 O O . GLU A 335 ? 0.3700 0.2882 0.1989 -0.0757 0.0509 -0.0421 370 GLU A O 2531 C CB . GLU A 335 ? 0.3955 0.3109 0.2344 -0.0615 0.0602 -0.0362 370 GLU A CB 2532 C CG . GLU A 335 ? 0.4104 0.3222 0.2551 -0.0545 0.0670 -0.0343 370 GLU A CG 2533 C CD . GLU A 335 ? 0.4309 0.3410 0.2683 -0.0551 0.0703 -0.0340 370 GLU A CD 2534 O OE1 . GLU A 335 ? 0.4701 0.3786 0.2948 -0.0614 0.0689 -0.0362 370 GLU A OE1 2535 O OE2 . GLU A 335 ? 0.4471 0.3580 0.2914 -0.0494 0.0743 -0.0313 370 GLU A OE2 2536 N N . PHE A 336 ? 0.3824 0.2918 0.1901 -0.0817 0.0559 -0.0456 371 PHE A N 2537 C CA . PHE A 336 ? 0.3968 0.3141 0.1990 -0.0893 0.0482 -0.0463 371 PHE A CA 2538 C C . PHE A 336 ? 0.3898 0.3180 0.1916 -0.0893 0.0418 -0.0419 371 PHE A C 2539 O O . PHE A 336 ? 0.3829 0.3070 0.1765 -0.0896 0.0451 -0.0420 371 PHE A O 2540 C CB . PHE A 336 ? 0.4172 0.3239 0.2023 -0.0984 0.0520 -0.0529 371 PHE A CB 2541 C CG . PHE A 336 ? 0.4407 0.3355 0.2250 -0.0992 0.0583 -0.0572 371 PHE A CG 2542 C CD1 . PHE A 336 ? 0.4368 0.3363 0.2272 -0.1016 0.0541 -0.0575 371 PHE A CD1 2543 C CD2 . PHE A 336 ? 0.4631 0.3420 0.2411 -0.0970 0.0688 -0.0606 371 PHE A CD2 2544 C CE1 . PHE A 336 ? 0.4545 0.3426 0.2442 -0.1021 0.0599 -0.0611 371 PHE A CE1 2545 C CE2 . PHE A 336 ? 0.4757 0.3429 0.2532 -0.0970 0.0749 -0.0640 371 PHE A CE2 2546 C CZ . PHE A 336 ? 0.4629 0.3346 0.2462 -0.0997 0.0703 -0.0642 371 PHE A CZ 2547 N N . LEU A 337 ? 0.3775 0.3192 0.1872 -0.0893 0.0330 -0.0381 372 LEU A N 2548 C CA . LEU A 337 ? 0.3943 0.3464 0.2035 -0.0892 0.0266 -0.0334 372 LEU A CA 2549 C C . LEU A 337 ? 0.4088 0.3591 0.2010 -0.0971 0.0260 -0.0357 372 LEU A C 2550 O O . LEU A 337 ? 0.4300 0.3831 0.2182 -0.0961 0.0246 -0.0324 372 LEU A O 2551 C CB . LEU A 337 ? 0.3947 0.3612 0.2146 -0.0882 0.0177 -0.0291 372 LEU A CB 2552 C CG . LEU A 337 ? 0.4037 0.3738 0.2402 -0.0800 0.0170 -0.0257 372 LEU A CG 2553 C CD1 . LEU A 337 ? 0.3967 0.3809 0.2418 -0.0793 0.0085 -0.0214 372 LEU A CD1 2554 C CD2 . LEU A 337 ? 0.4060 0.3727 0.2472 -0.0731 0.0207 -0.0228 372 LEU A CD2 2555 N N . SER A 338 ? 0.4196 0.3649 0.2012 -0.1052 0.0271 -0.0413 373 SER A N 2556 C CA . SER A 338 ? 0.4463 0.3882 0.2095 -0.1140 0.0272 -0.0446 373 SER A CA 2557 C C . SER A 338 ? 0.4624 0.3924 0.2150 -0.1129 0.0353 -0.0465 373 SER A C 2558 O O . SER A 338 ? 0.4705 0.3999 0.2089 -0.1187 0.0345 -0.0475 373 SER A O 2559 C CB . SER A 338 ? 0.4488 0.3855 0.2024 -0.1234 0.0281 -0.0511 373 SER A CB 2560 O OG . SER A 338 ? 0.4511 0.3736 0.2058 -0.1213 0.0368 -0.0556 373 SER A OG 2561 N N . ASN A 339 ? 0.4428 0.3641 0.2024 -0.1056 0.0429 -0.0467 374 ASN A N 2562 C CA . ASN A 339 ? 0.4545 0.3670 0.2079 -0.1027 0.0506 -0.0471 374 ASN A CA 2563 C C . ASN A 339 ? 0.4372 0.3578 0.1969 -0.0971 0.0477 -0.0405 374 ASN A C 2564 O O . ASN A 339 ? 0.4535 0.3679 0.2083 -0.0950 0.0540 -0.0405 374 ASN A O 2565 C CB . ASN A 339 ? 0.4664 0.3670 0.2252 -0.0970 0.0604 -0.0496 374 ASN A CB 2566 C CG . ASN A 339 ? 0.5066 0.3939 0.2544 -0.1027 0.0664 -0.0568 374 ASN A CG 2567 O OD1 . ASN A 339 ? 0.5002 0.3836 0.2321 -0.1118 0.0659 -0.0612 374 ASN A OD1 2568 N ND2 . ASN A 339 ? 0.5340 0.4137 0.2897 -0.0976 0.0725 -0.0581 374 ASN A ND2 2569 N N . TYR A 340 ? 0.4063 0.3402 0.1768 -0.0947 0.0390 -0.0351 375 TYR A N 2570 C CA . TYR A 340 ? 0.4018 0.3436 0.1786 -0.0898 0.0354 -0.0285 375 TYR A CA 2571 C C . TYR A 340 ? 0.4120 0.3653 0.1850 -0.0935 0.0259 -0.0245 375 TYR A C 2572 O O . TYR A 340 ? 0.4306 0.3868 0.1999 -0.0926 0.0243 -0.0204 375 TYR A O 2573 C CB . TYR A 340 ? 0.3729 0.3196 0.1688 -0.0814 0.0342 -0.0245 375 TYR A CB 2574 C CG . TYR A 340 ? 0.3817 0.3196 0.1837 -0.0765 0.0426 -0.0269 375 TYR A CG 2575 C CD1 . TYR A 340 ? 0.3821 0.3138 0.1852 -0.0773 0.0461 -0.0314 375 TYR A CD1 2576 C CD2 . TYR A 340 ? 0.3925 0.3287 0.1995 -0.0710 0.0471 -0.0241 375 TYR A CD2 2577 C CE1 . TYR A 340 ? 0.3943 0.3183 0.2031 -0.0723 0.0538 -0.0328 375 TYR A CE1 2578 C CE2 . TYR A 340 ? 0.3952 0.3250 0.2086 -0.0664 0.0546 -0.0256 375 TYR A CE2 2579 C CZ . TYR A 340 ? 0.4055 0.3293 0.2198 -0.0667 0.0579 -0.0298 375 TYR A CZ 2580 O OH . TYR A 340 ? 0.4253 0.3433 0.2463 -0.0614 0.0653 -0.0305 375 TYR A OH 2581 N N . LEU A 341 ? 0.4347 0.3952 0.2096 -0.0973 0.0197 -0.0253 376 LEU A N 2582 C CA . LEU A 341 ? 0.4649 0.4386 0.2390 -0.0999 0.0102 -0.0207 376 LEU A CA 2583 C C . LEU A 341 ? 0.5044 0.4782 0.2623 -0.1102 0.0081 -0.0249 376 LEU A C 2584 O O . LEU A 341 ? 0.5239 0.4929 0.2784 -0.1152 0.0102 -0.0306 376 LEU A O 2585 C CB . LEU A 341 ? 0.4475 0.4317 0.2374 -0.0963 0.0041 -0.0179 376 LEU A CB 2586 C CG . LEU A 341 ? 0.4334 0.4177 0.2397 -0.0869 0.0057 -0.0145 376 LEU A CG 2587 C CD1 . LEU A 341 ? 0.4246 0.4188 0.2443 -0.0846 0.0001 -0.0125 376 LEU A CD1 2588 C CD2 . LEU A 341 ? 0.4363 0.4226 0.2446 -0.0819 0.0048 -0.0086 376 LEU A CD2 2589 N N . THR A 342 ? 0.5555 0.5344 0.3031 -0.1136 0.0039 -0.0218 377 THR A N 2590 C CA . THR A 342 ? 0.6197 0.6005 0.3511 -0.1241 0.0009 -0.0252 377 THR A CA 2591 C C . THR A 342 ? 0.6681 0.6638 0.4056 -0.1277 -0.0084 -0.0233 377 THR A C 2592 O O . THR A 342 ? 0.7297 0.7259 0.4571 -0.1371 -0.0099 -0.0281 377 THR A O 2593 C CB . THR A 342 ? 0.6506 0.6325 0.3685 -0.1265 -0.0005 -0.0220 377 THR A CB 2594 O OG1 . THR A 342 ? 0.6557 0.6496 0.3839 -0.1201 -0.0072 -0.0131 377 THR A OG1 2595 C CG2 . THR A 342 ? 0.6596 0.6264 0.3701 -0.1243 0.0096 -0.0249 377 THR A CG2 2596 N N . ASN A 343 ? 0.6878 0.6953 0.4416 -0.1205 -0.0141 -0.0166 378 ASN A N 2597 C CA . ASN A 343 ? 0.7046 0.7279 0.4667 -0.1224 -0.0228 -0.0137 378 ASN A CA 2598 C C . ASN A 343 ? 0.6747 0.6987 0.4533 -0.1177 -0.0216 -0.0149 378 ASN A C 2599 O O . ASN A 343 ? 0.6690 0.7043 0.4619 -0.1119 -0.0267 -0.0094 378 ASN A O 2600 C CB . ASN A 343 ? 0.7473 0.7847 0.5148 -0.1176 -0.0307 -0.0044 378 ASN A CB 2601 C CG . ASN A 343 ? 0.8456 0.8857 0.5963 -0.1235 -0.0338 -0.0024 378 ASN A CG 2602 O OD1 . ASN A 343 ? 0.9013 0.9373 0.6479 -0.1195 -0.0321 0.0013 378 ASN A OD1 2603 N ND2 . ASN A 343 ? 0.8781 0.9254 0.6187 -0.1334 -0.0386 -0.0049 378 ASN A ND2 2604 N N . VAL A 344 ? 0.6453 0.6570 0.4214 -0.1203 -0.0147 -0.0221 379 VAL A N 2605 C CA . VAL A 344 ? 0.6312 0.6426 0.4215 -0.1164 -0.0131 -0.0234 379 VAL A CA 2606 C C . VAL A 344 ? 0.6193 0.6443 0.4162 -0.1206 -0.0200 -0.0228 379 VAL A C 2607 O O . VAL A 344 ? 0.5691 0.5968 0.3796 -0.1162 -0.0200 -0.0222 379 VAL A O 2608 C CB . VAL A 344 ? 0.6658 0.6603 0.4519 -0.1179 -0.0038 -0.0308 379 VAL A CB 2609 C CG1 . VAL A 344 ? 0.6691 0.6520 0.4561 -0.1107 0.0034 -0.0304 379 VAL A CG1 2610 C CG2 . VAL A 344 ? 0.7039 0.6913 0.4725 -0.1291 -0.0016 -0.0376 379 VAL A CG2 2611 N N . ASP A 345 ? 0.5923 0.6259 0.3794 -0.1294 -0.0255 -0.0232 380 ASP A N 2612 C CA . ASP A 345 ? 0.6051 0.6539 0.3987 -0.1340 -0.0325 -0.0222 380 ASP A CA 2613 C C . ASP A 345 ? 0.5475 0.6136 0.3562 -0.1265 -0.0399 -0.0134 380 ASP A C 2614 O O . ASP A 345 ? 0.5273 0.6062 0.3459 -0.1275 -0.0446 -0.0117 380 ASP A O 2615 C CB . ASP A 345 ? 0.6629 0.7163 0.4408 -0.1467 -0.0363 -0.0255 380 ASP A CB 2616 C CG . ASP A 345 ? 0.7141 0.7497 0.4771 -0.1549 -0.0286 -0.0349 380 ASP A CG 2617 O OD1 . ASP A 345 ? 0.7540 0.7783 0.5220 -0.1527 -0.0221 -0.0390 380 ASP A OD1 2618 O OD2 . ASP A 345 ? 0.8254 0.8574 0.5708 -0.1636 -0.0287 -0.0381 380 ASP A OD2 2619 N N . ASP A 346 ? 0.5098 0.5760 0.3202 -0.1190 -0.0405 -0.0077 381 ASP A N 2620 C CA . ASP A 346 ? 0.5079 0.5878 0.3324 -0.1107 -0.0462 0.0006 381 ASP A CA 2621 C C . ASP A 346 ? 0.4761 0.5518 0.3164 -0.1009 -0.0426 0.0018 381 ASP A C 2622 O O . ASP A 346 ? 0.4592 0.5441 0.3111 -0.0936 -0.0462 0.0083 381 ASP A O 2623 C CB . ASP A 346 ? 0.5432 0.6246 0.3620 -0.1073 -0.0485 0.0065 381 ASP A CB 2624 C CG . ASP A 346 ? 0.5922 0.6798 0.3955 -0.1165 -0.0532 0.0065 381 ASP A CG 2625 O OD1 . ASP A 346 ? 0.6242 0.7178 0.4228 -0.1257 -0.0560 0.0026 381 ASP A OD1 2626 O OD2 . ASP A 346 ? 0.6336 0.7197 0.4290 -0.1149 -0.0540 0.0105 381 ASP A OD2 2627 N N . ILE A 347 ? 0.4544 0.5162 0.2947 -0.1006 -0.0353 -0.0040 382 ILE A N 2628 C CA . ILE A 347 ? 0.4507 0.5087 0.3050 -0.0918 -0.0320 -0.0028 382 ILE A CA 2629 C C . ILE A 347 ? 0.4151 0.4714 0.2750 -0.0941 -0.0297 -0.0075 382 ILE A C 2630 O O . ILE A 347 ? 0.4091 0.4616 0.2604 -0.1024 -0.0281 -0.0131 382 ILE A O 2631 C CB . ILE A 347 ? 0.4836 0.5267 0.3356 -0.0865 -0.0251 -0.0038 382 ILE A CB 2632 C CG1 . ILE A 347 ? 0.5210 0.5496 0.3620 -0.0918 -0.0181 -0.0112 382 ILE A CG1 2633 C CG2 . ILE A 347 ? 0.4892 0.5335 0.3363 -0.0837 -0.0270 0.0012 382 ILE A CG2 2634 C CD1 . ILE A 347 ? 0.5529 0.5687 0.3958 -0.0857 -0.0109 -0.0121 382 ILE A CD1 2635 N N . THR A 348 ? 0.3855 0.4438 0.2595 -0.0867 -0.0292 -0.0052 383 THR A N 2636 C CA . THR A 348 ? 0.3778 0.4324 0.2581 -0.0870 -0.0258 -0.0091 383 THR A CA 2637 C C . THR A 348 ? 0.3523 0.3938 0.2359 -0.0802 -0.0194 -0.0101 383 THR A C 2638 O O . THR A 348 ? 0.3560 0.3976 0.2445 -0.0734 -0.0197 -0.0060 383 THR A O 2639 C CB . THR A 348 ? 0.3761 0.4449 0.2702 -0.0839 -0.0306 -0.0053 383 THR A CB 2640 O OG1 . THR A 348 ? 0.4228 0.5051 0.3144 -0.0910 -0.0365 -0.0045 383 THR A OG1 2641 C CG2 . THR A 348 ? 0.3770 0.4414 0.2787 -0.0827 -0.0267 -0.0084 383 THR A CG2 2642 N N . LEU A 349 ? 0.3486 0.3790 0.2293 -0.0825 -0.0136 -0.0155 384 LEU A N 2643 C CA . LEU A 349 ? 0.3316 0.3504 0.2155 -0.0766 -0.0075 -0.0166 384 LEU A CA 2644 C C . LEU A 349 ? 0.3216 0.3391 0.2137 -0.0753 -0.0054 -0.0184 384 LEU A C 2645 O O . LEU A 349 ? 0.3208 0.3365 0.2092 -0.0813 -0.0043 -0.0222 384 LEU A O 2646 C CB . LEU A 349 ? 0.3477 0.3529 0.2194 -0.0800 -0.0013 -0.0211 384 LEU A CB 2647 C CG . LEU A 349 ? 0.3298 0.3232 0.2043 -0.0746 0.0055 -0.0225 384 LEU A CG 2648 C CD1 . LEU A 349 ? 0.3239 0.3188 0.2047 -0.0673 0.0051 -0.0179 384 LEU A CD1 2649 C CD2 . LEU A 349 ? 0.3610 0.3413 0.2233 -0.0788 0.0121 -0.0275 384 LEU A CD2 2650 N N . VAL A 350 ? 0.3131 0.3310 0.2157 -0.0678 -0.0048 -0.0156 385 VAL A N 2651 C CA . VAL A 350 ? 0.3229 0.3361 0.2316 -0.0656 -0.0013 -0.0175 385 VAL A CA 2652 C C . VAL A 350 ? 0.3288 0.3282 0.2321 -0.0643 0.0053 -0.0201 385 VAL A C 2653 O O . VAL A 350 ? 0.3121 0.3087 0.2170 -0.0593 0.0067 -0.0180 385 VAL A O 2654 C CB . VAL A 350 ? 0.3249 0.3439 0.2459 -0.0584 -0.0032 -0.0136 385 VAL A CB 2655 C CG1 . VAL A 350 ? 0.3233 0.3375 0.2495 -0.0567 0.0002 -0.0155 385 VAL A CG1 2656 C CG2 . VAL A 350 ? 0.3347 0.3677 0.2613 -0.0587 -0.0095 -0.0102 385 VAL A CG2 2657 N N . PRO A 351 ? 0.3322 0.3227 0.2287 -0.0688 0.0098 -0.0247 386 PRO A N 2658 C CA . PRO A 351 ? 0.3262 0.3038 0.2158 -0.0681 0.0164 -0.0272 386 PRO A CA 2659 C C . PRO A 351 ? 0.3252 0.2953 0.2206 -0.0631 0.0216 -0.0275 386 PRO A C 2660 O O . PRO A 351 ? 0.3120 0.2866 0.2163 -0.0602 0.0198 -0.0259 386 PRO A O 2661 C CB . PRO A 351 ? 0.3527 0.3246 0.2305 -0.0767 0.0183 -0.0321 386 PRO A CB 2662 C CG . PRO A 351 ? 0.3567 0.3343 0.2397 -0.0796 0.0157 -0.0327 386 PRO A CG 2663 C CD . PRO A 351 ? 0.3490 0.3405 0.2435 -0.0752 0.0094 -0.0278 386 PRO A CD 2664 N N . GLY A 352 ? 0.3328 0.2917 0.2227 -0.0619 0.0280 -0.0294 387 GLY A N 2665 C CA . GLY A 352 ? 0.3175 0.2683 0.2111 -0.0576 0.0335 -0.0298 387 GLY A CA 2666 C C . GLY A 352 ? 0.3035 0.2542 0.2034 -0.0502 0.0354 -0.0265 387 GLY A C 2667 O O . GLY A 352 ? 0.3065 0.2548 0.2023 -0.0495 0.0375 -0.0263 387 GLY A O 2668 N N . THR A 353 ? 0.2708 0.2249 0.1808 -0.0452 0.0346 -0.0239 388 THR A N 2669 C CA . THR A 353 ? 0.2633 0.2181 0.1801 -0.0387 0.0362 -0.0208 388 THR A CA 2670 C C . THR A 353 ? 0.2632 0.2272 0.1853 -0.0367 0.0310 -0.0175 388 THR A C 2671 O O . THR A 353 ? 0.2319 0.1977 0.1598 -0.0321 0.0316 -0.0148 388 THR A O 2672 C CB . THR A 353 ? 0.2519 0.2057 0.1760 -0.0347 0.0377 -0.0195 388 THR A CB 2673 O OG1 . THR A 353 ? 0.2627 0.2234 0.1913 -0.0359 0.0326 -0.0189 388 THR A OG1 2674 C CG2 . THR A 353 ? 0.2683 0.2110 0.1869 -0.0357 0.0441 -0.0221 388 THR A CG2 2675 N N A LEU A 354 ? 0.2597 0.2298 0.1800 -0.0401 0.0259 -0.0174 389 LEU A N 2676 N N B LEU A 354 ? 0.2650 0.2352 0.1853 -0.0401 0.0259 -0.0174 389 LEU A N 2677 C CA A LEU A 354 ? 0.2525 0.2296 0.1751 -0.0388 0.0215 -0.0145 389 LEU A CA 2678 C CA B LEU A 354 ? 0.2606 0.2378 0.1833 -0.0389 0.0214 -0.0145 389 LEU A CA 2679 C C A LEU A 354 ? 0.2639 0.2439 0.1790 -0.0442 0.0184 -0.0156 389 LEU A C 2680 C C B LEU A 354 ? 0.2668 0.2461 0.1813 -0.0443 0.0188 -0.0157 389 LEU A C 2681 O O A LEU A 354 ? 0.2822 0.2602 0.1922 -0.0489 0.0188 -0.0186 389 LEU A O 2682 O O B LEU A 354 ? 0.2774 0.2532 0.1855 -0.0491 0.0202 -0.0190 389 LEU A O 2683 C CB A LEU A 354 ? 0.2407 0.2248 0.1729 -0.0354 0.0174 -0.0117 389 LEU A CB 2684 C CB B LEU A 354 ? 0.2605 0.2451 0.1924 -0.0360 0.0170 -0.0120 389 LEU A CB 2685 C CG A LEU A 354 ? 0.2384 0.2273 0.1732 -0.0373 0.0142 -0.0124 389 LEU A CG 2686 C CG B LEU A 354 ? 0.2647 0.2530 0.1982 -0.0385 0.0146 -0.0132 389 LEU A CG 2687 C CD1 A LEU A 354 ? 0.2302 0.2271 0.1722 -0.0344 0.0095 -0.0093 389 LEU A CD1 2688 C CD1 B LEU A 354 ? 0.2713 0.2667 0.2023 -0.0420 0.0097 -0.0127 389 LEU A CD1 2689 C CD2 A LEU A 354 ? 0.2354 0.2198 0.1724 -0.0367 0.0175 -0.0141 389 LEU A CD2 2690 C CD2 B LEU A 354 ? 0.2626 0.2544 0.2052 -0.0345 0.0131 -0.0115 389 LEU A CD2 2691 N N . GLY A 355 ? 0.2486 0.2332 0.1628 -0.0439 0.0151 -0.0130 390 GLY A N 2692 C CA . GLY A 355 ? 0.2608 0.2500 0.1684 -0.0486 0.0112 -0.0130 390 GLY A CA 2693 C C . GLY A 355 ? 0.2460 0.2447 0.1597 -0.0460 0.0054 -0.0086 390 GLY A C 2694 O O . GLY A 355 ? 0.2457 0.2446 0.1641 -0.0415 0.0053 -0.0057 390 GLY A O 2695 N N . ARG A 356 ? 0.2498 0.2562 0.1637 -0.0489 0.0008 -0.0082 391 ARG A N 2696 C CA . ARG A 356 ? 0.2462 0.2620 0.1648 -0.0465 -0.0046 -0.0037 391 ARG A CA 2697 C C . ARG A 356 ? 0.2655 0.2869 0.1765 -0.0520 -0.0082 -0.0035 391 ARG A C 2698 O O . ARG A 356 ? 0.2638 0.2865 0.1712 -0.0574 -0.0085 -0.0067 391 ARG A O 2699 C CB . ARG A 356 ? 0.2473 0.2692 0.1762 -0.0436 -0.0068 -0.0025 391 ARG A CB 2700 C CG . ARG A 356 ? 0.2522 0.2685 0.1874 -0.0392 -0.0032 -0.0032 391 ARG A CG 2701 C CD . ARG A 356 ? 0.2515 0.2734 0.1965 -0.0347 -0.0055 -0.0007 391 ARG A CD 2702 N NE . ARG A 356 ? 0.2562 0.2857 0.2044 -0.0368 -0.0081 -0.0011 391 ARG A NE 2703 C CZ . ARG A 356 ? 0.2773 0.3060 0.2273 -0.0388 -0.0063 -0.0040 391 ARG A CZ 2704 N NH1 . ARG A 356 ? 0.2830 0.3031 0.2320 -0.0384 -0.0020 -0.0066 391 ARG A NH1 2705 N NH2 . ARG A 356 ? 0.2805 0.3176 0.2338 -0.0410 -0.0090 -0.0039 391 ARG A NH2 2706 N N . ILE A 357 ? 0.2685 0.2928 0.1765 -0.0509 -0.0108 0.0001 392 ILE A N 2707 C CA . ILE A 357 ? 0.2784 0.3083 0.1779 -0.0562 -0.0145 0.0008 392 ILE A CA 2708 C C . ILE A 357 ? 0.2724 0.3140 0.1777 -0.0532 -0.0206 0.0066 392 ILE A C 2709 O O . ILE A 357 ? 0.2649 0.3061 0.1753 -0.0472 -0.0210 0.0107 392 ILE A O 2710 C CB . ILE A 357 ? 0.2876 0.3102 0.1760 -0.0580 -0.0119 0.0004 392 ILE A CB 2711 C CG1 . ILE A 357 ? 0.2898 0.3011 0.1716 -0.0613 -0.0054 -0.0054 392 ILE A CG1 2712 C CG2 . ILE A 357 ? 0.3033 0.3327 0.1827 -0.0631 -0.0165 0.0021 392 ILE A CG2 2713 C CD1 . ILE A 357 ? 0.3064 0.3095 0.1789 -0.0619 -0.0013 -0.0059 392 ILE A CD1 2714 N N . ARG A 358 ? 0.3051 0.3568 0.2089 -0.0578 -0.0253 0.0070 393 ARG A N 2715 C CA . ARG A 358 ? 0.3283 0.3923 0.2357 -0.0555 -0.0314 0.0132 393 ARG A CA 2716 C C . ARG A 358 ? 0.3485 0.4206 0.2467 -0.0631 -0.0358 0.0131 393 ARG A C 2717 O O . ARG A 358 ? 0.3653 0.4328 0.2546 -0.0704 -0.0339 0.0077 393 ARG A O 2718 C CB . ARG A 358 ? 0.3275 0.4006 0.2483 -0.0514 -0.0336 0.0153 393 ARG A CB 2719 C CG . ARG A 358 ? 0.3283 0.4068 0.2508 -0.0571 -0.0343 0.0113 393 ARG A CG 2720 C CD . ARG A 358 ? 0.3371 0.4226 0.2730 -0.0526 -0.0350 0.0128 393 ARG A CD 2721 N NE . ARG A 358 ? 0.3425 0.4343 0.2793 -0.0590 -0.0359 0.0094 393 ARG A NE 2722 C CZ . ARG A 358 ? 0.3530 0.4379 0.2903 -0.0615 -0.0318 0.0042 393 ARG A CZ 2723 N NH1 . ARG A 358 ? 0.3303 0.4021 0.2677 -0.0580 -0.0264 0.0018 393 ARG A NH1 2724 N NH2 . ARG A 358 ? 0.3817 0.4733 0.3192 -0.0681 -0.0332 0.0017 393 ARG A NH2 2725 N N . ALA A 359 ? 0.3829 0.4667 0.2830 -0.0614 -0.0417 0.0193 394 ALA A N 2726 C CA . ALA A 359 ? 0.4152 0.5092 0.3070 -0.0686 -0.0470 0.0201 394 ALA A CA 2727 C C . ALA A 359 ? 0.4588 0.5615 0.3535 -0.0749 -0.0491 0.0166 394 ALA A C 2728 O O . ALA A 359 ? 0.4515 0.5604 0.3585 -0.0713 -0.0496 0.0177 394 ALA A O 2729 C CB . ALA A 359 ? 0.4342 0.5401 0.3293 -0.0642 -0.0529 0.0285 394 ALA A CB 2730 N N . LYS A 360 ? 0.4968 0.5997 0.3798 -0.0848 -0.0500 0.0124 395 LYS A N 2731 C CA . LYS A 360 ? 0.5771 0.6893 0.4622 -0.0920 -0.0525 0.0093 395 LYS A CA 2732 C C . LYS A 360 ? 0.6165 0.7497 0.5114 -0.0904 -0.0602 0.0160 395 LYS A C 2733 O O . LYS A 360 ? 0.6416 0.7839 0.5468 -0.0908 -0.0615 0.0158 395 LYS A O 2734 C CB . LYS A 360 ? 0.6391 0.7468 0.5084 -0.1036 -0.0519 0.0031 395 LYS A CB 2735 C CG . LYS A 360 ? 0.6770 0.7897 0.5482 -0.1115 -0.0525 -0.0014 395 LYS A CG 2736 C CD . LYS A 360 ? 0.7422 0.8492 0.5968 -0.1238 -0.0515 -0.0080 395 LYS A CD 2737 C CE . LYS A 360 ? 0.7880 0.8736 0.6352 -0.1254 -0.0425 -0.0156 395 LYS A CE 2738 N NZ . LYS A 360 ? 0.8460 0.9243 0.6759 -0.1373 -0.0408 -0.0222 395 LYS A NZ 2739 N N . SER A 361 ? 0.6624 0.8034 0.5544 -0.0883 -0.0651 0.0223 396 SER A N 2740 C CA . SER A 361 ? 0.7364 0.8975 0.6386 -0.0850 -0.0722 0.0301 396 SER A CA 2741 C C . SER A 361 ? 0.7697 0.9301 0.6777 -0.0738 -0.0725 0.0377 396 SER A C 2742 O O . SER A 361 ? 0.7433 0.8940 0.6417 -0.0724 -0.0711 0.0388 396 SER A O 2743 C CB . SER A 361 ? 0.7764 0.9511 0.6694 -0.0942 -0.0791 0.0315 396 SER A CB 2744 O OG . SER A 361 ? 0.8184 1.0139 0.7220 -0.0903 -0.0861 0.0399 396 SER A OG 2745 N N . ILE A 362 ? 0.8764 1.0467 0.7997 -0.0659 -0.0741 0.0429 397 ILE A N 2746 C CA . ILE A 362 ? 0.9794 1.1513 0.9091 -0.0552 -0.0751 0.0512 397 ILE A CA 2747 C C . ILE A 362 ? 1.0540 1.2371 0.9774 -0.0560 -0.0817 0.0583 397 ILE A C 2748 O O . ILE A 362 ? 1.1134 1.2915 1.0350 -0.0493 -0.0814 0.0639 397 ILE A O 2749 C CB . ILE A 362 ? 0.9894 1.1704 0.9367 -0.0467 -0.0753 0.0554 397 ILE A CB 2750 C CG1 . ILE A 362 ? 1.0135 1.2172 0.9687 -0.0502 -0.0815 0.0583 397 ILE A CG1 2751 C CG2 . ILE A 362 ? 0.9726 1.1410 0.9252 -0.0446 -0.0685 0.0491 397 ILE A CG2 2752 C CD1 . ILE A 362 ? 1.0236 1.2379 0.9961 -0.0409 -0.0817 0.0637 397 ILE A CD1 2753 N N . ASN A 363 ? 1.0802 1.2781 0.9997 -0.0647 -0.0876 0.0581 398 ASN A N 2754 C CA . ASN A 363 ? 1.1382 1.3486 1.0506 -0.0671 -0.0946 0.0647 398 ASN A CA 2755 C C . ASN A 363 ? 1.1905 1.3878 1.0843 -0.0720 -0.0932 0.0624 398 ASN A C 2756 O O . ASN A 363 ? 1.1872 1.3924 1.0737 -0.0731 -0.0985 0.0682 398 ASN A O 2757 C CB . ASN A 363 ? 1.1637 1.3946 1.0772 -0.0762 -0.1014 0.0646 398 ASN A CB 2758 C CG . ASN A 363 ? 1.2073 1.4541 1.1397 -0.0714 -0.1033 0.0679 398 ASN A CG 2759 O OD1 . ASN A 363 ? 1.2072 1.4544 1.1517 -0.0599 -0.1017 0.0735 398 ASN A OD1 2760 N ND2 . ASN A 363 ? 1.2439 1.5032 1.1784 -0.0805 -0.1062 0.0642 398 ASN A ND2 2761 N N . ASN A 364 ? 1.1788 1.3569 1.0651 -0.0750 -0.0861 0.0541 399 ASN A N 2762 C CA . ASN A 364 ? 1.1529 1.3166 1.0226 -0.0786 -0.0831 0.0514 399 ASN A CA 2763 C C . ASN A 364 ? 1.1232 1.2815 0.9928 -0.0694 -0.0825 0.0588 399 ASN A C 2764 O O . ASN A 364 ? 1.0737 1.2263 0.9543 -0.0600 -0.0791 0.0612 399 ASN A O 2765 C CB . ASN A 364 ? 1.1159 1.2606 0.9811 -0.0817 -0.0748 0.0416 399 ASN A CB 2766 C CG . ASN A 364 ? 1.0754 1.2072 0.9222 -0.0883 -0.0716 0.0370 399 ASN A CG 2767 O OD1 . ASN A 364 ? 1.0176 1.1427 0.8583 -0.0847 -0.0704 0.0406 399 ASN A OD1 2768 N ND2 . ASN A 364 ? 1.0731 1.2003 0.9107 -0.0982 -0.0696 0.0289 399 ASN A ND2 2769 N N . SER A 365 ? 1.1176 1.2777 0.9744 -0.0725 -0.0858 0.0626 400 SER A N 2770 C CA . SER A 365 ? 1.0856 1.2380 0.9386 -0.0655 -0.0844 0.0689 400 SER A CA 2771 C C . SER A 365 ? 1.0496 1.1834 0.8875 -0.0695 -0.0781 0.0634 400 SER A C 2772 O O . SER A 365 ? 0.9891 1.1143 0.8236 -0.0643 -0.0758 0.0677 400 SER A O 2773 C CB . SER A 365 ? 1.0829 1.2511 0.9325 -0.0649 -0.0926 0.0785 400 SER A CB 2774 O OG . SER A 365 ? 1.0651 1.2380 0.8989 -0.0760 -0.0962 0.0758 400 SER A OG 2775 N N . LYS A 366 ? 1.0286 1.1562 0.8580 -0.0785 -0.0751 0.0542 401 LYS A N 2776 C CA . LYS A 366 ? 0.9985 1.1091 0.8134 -0.0830 -0.0686 0.0481 401 LYS A CA 2777 C C . LYS A 366 ? 0.9946 1.0893 0.8167 -0.0776 -0.0601 0.0435 401 LYS A C 2778 O O . LYS A 366 ? 0.9791 1.0605 0.7944 -0.0764 -0.0545 0.0424 401 LYS A O 2779 C CB . LYS A 366 ? 0.9773 1.0882 0.7795 -0.0951 -0.0689 0.0403 401 LYS A CB 2780 C CG . LYS A 366 ? 1.0054 1.1077 0.7875 -0.1019 -0.0667 0.0378 401 LYS A CG 2781 C CD . LYS A 366 ? 1.0225 1.1046 0.7993 -0.1016 -0.0567 0.0310 401 LYS A CD 2782 C CE . LYS A 366 ? 1.0531 1.1267 0.8104 -0.1071 -0.0541 0.0296 401 LYS A CE 2783 N NZ . LYS A 366 ? 1.0689 1.1435 0.8244 -0.1012 -0.0558 0.0382 401 LYS A NZ 2784 N N . TYR A 367 ? 0.9264 1.0234 0.7622 -0.0748 -0.0592 0.0411 402 TYR A N 2785 C CA . TYR A 367 ? 0.8478 0.9319 0.6912 -0.0703 -0.0520 0.0367 402 TYR A CA 2786 C C . TYR A 367 ? 0.8142 0.8919 0.6635 -0.0611 -0.0496 0.0422 402 TYR A C 2787 O O . TYR A 367 ? 0.8919 0.9772 0.7516 -0.0544 -0.0531 0.0486 402 TYR A O 2788 C CB . TYR A 367 ? 0.8101 0.9007 0.6669 -0.0692 -0.0529 0.0343 402 TYR A CB 2789 C CG . TYR A 367 ? 0.7622 0.8420 0.6284 -0.0642 -0.0466 0.0305 402 TYR A CG 2790 C CD1 . TYR A 367 ? 0.7714 0.8409 0.6338 -0.0686 -0.0410 0.0225 402 TYR A CD1 2791 C CD2 . TYR A 367 ? 0.7208 0.8008 0.5995 -0.0551 -0.0462 0.0351 402 TYR A CD2 2792 C CE1 . TYR A 367 ? 0.7145 0.7753 0.5855 -0.0639 -0.0357 0.0197 402 TYR A CE1 2793 C CE2 . TYR A 367 ? 0.6821 0.7530 0.5687 -0.0511 -0.0409 0.0317 402 TYR A CE2 2794 C CZ . TYR A 367 ? 0.6760 0.7380 0.5589 -0.0555 -0.0359 0.0242 402 TYR A CZ 2795 O OH . TYR A 367 ? 0.5752 0.6294 0.4659 -0.0516 -0.0311 0.0214 402 TYR A OH 2796 N N . ASP A 368 ? 0.6883 0.7520 0.5309 -0.0609 -0.0435 0.0397 403 ASP A N 2797 C CA . ASP A 368 ? 0.6578 0.7137 0.5052 -0.0535 -0.0402 0.0437 403 ASP A CA 2798 C C . ASP A 368 ? 0.6261 0.6703 0.4785 -0.0522 -0.0330 0.0376 403 ASP A C 2799 O O . ASP A 368 ? 0.5704 0.6060 0.4145 -0.0566 -0.0281 0.0322 403 ASP A O 2800 C CB . ASP A 368 ? 0.6801 0.7310 0.5148 -0.0548 -0.0394 0.0472 403 ASP A CB 2801 C CG . ASP A 368 ? 0.7052 0.7483 0.5443 -0.0477 -0.0363 0.0521 403 ASP A CG 2802 O OD1 . ASP A 368 ? 0.7494 0.7894 0.6006 -0.0420 -0.0342 0.0521 403 ASP A OD1 2803 O OD2 . ASP A 368 ? 0.8178 0.8572 0.6473 -0.0482 -0.0359 0.0560 403 ASP A OD2 2804 N N . PRO A 369 ? 0.5803 0.6242 0.4462 -0.0460 -0.0322 0.0385 404 PRO A N 2805 C CA . PRO A 369 ? 0.5668 0.6013 0.4377 -0.0450 -0.0262 0.0329 404 PRO A CA 2806 C C . PRO A 369 ? 0.5476 0.5706 0.4139 -0.0441 -0.0204 0.0324 404 PRO A C 2807 O O . PRO A 369 ? 0.5124 0.5282 0.3793 -0.0452 -0.0151 0.0272 404 PRO A O 2808 C CB . PRO A 369 ? 0.5734 0.6113 0.4586 -0.0385 -0.0274 0.0352 404 PRO A CB 2809 C CG . PRO A 369 ? 0.5792 0.6224 0.4657 -0.0342 -0.0316 0.0430 404 PRO A CG 2810 C CD . PRO A 369 ? 0.6125 0.6634 0.4887 -0.0392 -0.0361 0.0450 404 PRO A CD 2811 N N . LYS A 370 ? 0.5481 0.5697 0.4097 -0.0423 -0.0212 0.0380 405 LYS A N 2812 C CA . LYS A 370 ? 0.5424 0.5541 0.3983 -0.0425 -0.0158 0.0378 405 LYS A CA 2813 C C . LYS A 370 ? 0.5083 0.5162 0.3517 -0.0490 -0.0126 0.0332 405 LYS A C 2814 O O . LYS A 370 ? 0.4709 0.4705 0.3127 -0.0496 -0.0064 0.0298 405 LYS A O 2815 C CB . LYS A 370 ? 0.5996 0.6105 0.4523 -0.0395 -0.0175 0.0453 405 LYS A CB 2816 C CG . LYS A 370 ? 0.6270 0.6373 0.4910 -0.0326 -0.0183 0.0496 405 LYS A CG 2817 C CD . LYS A 370 ? 0.6831 0.6910 0.5426 -0.0298 -0.0194 0.0572 405 LYS A CD 2818 C CE . LYS A 370 ? 0.7156 0.7223 0.5855 -0.0229 -0.0202 0.0616 405 LYS A CE 2819 N NZ . LYS A 370 ? 0.7386 0.7555 0.6160 -0.0199 -0.0255 0.0635 405 LYS A NZ 2820 N N . THR A 371 ? 0.5004 0.5145 0.3349 -0.0539 -0.0167 0.0330 406 THR A N 2821 C CA . THR A 371 ? 0.5123 0.5219 0.3333 -0.0607 -0.0135 0.0280 406 THR A CA 2822 C C . THR A 371 ? 0.4546 0.4599 0.2785 -0.0629 -0.0092 0.0203 406 THR A C 2823 O O . THR A 371 ? 0.4287 0.4257 0.2456 -0.0657 -0.0031 0.0157 406 THR A O 2824 C CB . THR A 371 ? 0.5559 0.5731 0.3649 -0.0664 -0.0191 0.0296 406 THR A CB 2825 O OG1 . THR A 371 ? 0.6198 0.6471 0.4345 -0.0677 -0.0247 0.0289 406 THR A OG1 2826 C CG2 . THR A 371 ? 0.5745 0.5952 0.3799 -0.0638 -0.0229 0.0378 406 THR A CG2 2827 N N . ILE A 372 ? 0.4164 0.4271 0.2511 -0.0611 -0.0120 0.0193 407 ILE A N 2828 C CA . ILE A 372 ? 0.3852 0.3918 0.2233 -0.0627 -0.0081 0.0126 407 ILE A CA 2829 C C . ILE A 372 ? 0.3523 0.3499 0.1960 -0.0587 -0.0013 0.0110 407 ILE A C 2830 O O . ILE A 372 ? 0.3552 0.3453 0.1942 -0.0610 0.0045 0.0060 407 ILE A O 2831 C CB . ILE A 372 ? 0.3883 0.4028 0.2373 -0.0612 -0.0124 0.0125 407 ILE A CB 2832 C CG1 . ILE A 372 ? 0.4252 0.4506 0.2698 -0.0656 -0.0193 0.0142 407 ILE A CG1 2833 C CG2 . ILE A 372 ? 0.3791 0.3881 0.2312 -0.0627 -0.0078 0.0060 407 ILE A CG2 2834 C CD1 . ILE A 372 ? 0.4657 0.4889 0.2949 -0.0740 -0.0187 0.0102 407 ILE A CD1 2835 N N . ILE A 373 ? 0.3459 0.3443 0.1994 -0.0528 -0.0020 0.0153 408 ILE A N 2836 C CA . ILE A 373 ? 0.3449 0.3366 0.2051 -0.0491 0.0036 0.0142 408 ILE A CA 2837 C C . ILE A 373 ? 0.3397 0.3242 0.1904 -0.0513 0.0093 0.0131 408 ILE A C 2838 O O . ILE A 373 ? 0.3191 0.2979 0.1704 -0.0515 0.0153 0.0092 408 ILE A O 2839 C CB . ILE A 373 ? 0.3758 0.3692 0.2459 -0.0435 0.0016 0.0193 408 ILE A CB 2840 C CG1 . ILE A 373 ? 0.3849 0.3844 0.2653 -0.0407 -0.0025 0.0197 408 ILE A CG1 2841 C CG2 . ILE A 373 ? 0.3793 0.3663 0.2545 -0.0409 0.0073 0.0186 408 ILE A CG2 2842 C CD1 . ILE A 373 ? 0.3975 0.3948 0.2859 -0.0395 0.0003 0.0154 408 ILE A CD1 2843 N N . ALA A 374 ? 0.3475 0.3328 0.1895 -0.0529 0.0075 0.0169 409 ALA A N 2844 C CA . ALA A 374 ? 0.3579 0.3368 0.1897 -0.0552 0.0128 0.0163 409 ALA A CA 2845 C C . ALA A 374 ? 0.3540 0.3281 0.1762 -0.0602 0.0173 0.0100 409 ALA A C 2846 O O . ALA A 374 ? 0.3435 0.3108 0.1634 -0.0603 0.0244 0.0074 409 ALA A O 2847 C CB . ALA A 374 ? 0.3724 0.3535 0.1953 -0.0565 0.0093 0.0217 409 ALA A CB 2848 N N . ALA A 375 ? 0.3412 0.3189 0.1586 -0.0642 0.0134 0.0075 410 ALA A N 2849 C CA . ALA A 375 ? 0.3492 0.3210 0.1562 -0.0696 0.0177 0.0010 410 ALA A CA 2850 C C . ALA A 375 ? 0.3359 0.3023 0.1505 -0.0675 0.0233 -0.0037 410 ALA A C 2851 O O . ALA A 375 ? 0.3415 0.3005 0.1481 -0.0708 0.0289 -0.0089 410 ALA A O 2852 C CB . ALA A 375 ? 0.3656 0.3432 0.1654 -0.0753 0.0117 -0.0003 410 ALA A CB 2853 N N . LEU A 376 ? 0.3035 0.2733 0.1329 -0.0622 0.0217 -0.0019 411 LEU A N 2854 C CA . LEU A 376 ? 0.3093 0.2749 0.1469 -0.0595 0.0264 -0.0053 411 LEU A CA 2855 C C . LEU A 376 ? 0.3046 0.2672 0.1500 -0.0545 0.0316 -0.0036 411 LEU A C 2856 O O . LEU A 376 ? 0.3048 0.2652 0.1582 -0.0515 0.0352 -0.0055 411 LEU A O 2857 C CB . LEU A 376 ? 0.2915 0.2633 0.1396 -0.0577 0.0212 -0.0049 411 LEU A CB 2858 C CG . LEU A 376 ? 0.2961 0.2719 0.1381 -0.0630 0.0164 -0.0069 411 LEU A CG 2859 C CD1 . LEU A 376 ? 0.2952 0.2786 0.1489 -0.0605 0.0111 -0.0053 411 LEU A CD1 2860 C CD2 . LEU A 376 ? 0.3099 0.2777 0.1429 -0.0678 0.0216 -0.0133 411 LEU A CD2 2861 N N . THR A 377 ? 0.3061 0.2690 0.1491 -0.0538 0.0321 0.0000 412 THR A N 2862 C CA . THR A 377 ? 0.3070 0.2689 0.1586 -0.0496 0.0361 0.0022 412 THR A CA 2863 C C . THR A 377 ? 0.3243 0.2797 0.1696 -0.0505 0.0445 0.0000 412 THR A C 2864 O O . THR A 377 ? 0.3245 0.2773 0.1584 -0.0536 0.0462 0.0004 412 THR A O 2865 C CB . THR A 377 ? 0.3130 0.2786 0.1668 -0.0481 0.0321 0.0080 412 THR A CB 2866 O OG1 . THR A 377 ? 0.3148 0.2859 0.1761 -0.0461 0.0254 0.0101 412 THR A OG1 2867 C CG2 . THR A 377 ? 0.3117 0.2761 0.1730 -0.0450 0.0364 0.0101 412 THR A CG2 2868 N N . CYS A 378 ? 0.3179 0.2710 0.1706 -0.0476 0.0498 -0.0023 413 CYS A N 2869 C CA . CYS A 378 ? 0.3369 0.2849 0.1874 -0.0468 0.0585 -0.0040 413 CYS A CA 2870 C C . CYS A 378 ? 0.3651 0.3062 0.1993 -0.0515 0.0627 -0.0074 413 CYS A C 2871 O O . CYS A 378 ? 0.3683 0.3069 0.1966 -0.0522 0.0675 -0.0065 413 CYS A O 2872 C CB . CYS A 378 ? 0.3406 0.2917 0.1974 -0.0445 0.0603 0.0003 413 CYS A CB 2873 S SG . CYS A 378 ? 0.3762 0.3347 0.2501 -0.0403 0.0553 0.0043 413 CYS A SG 2874 N N . LYS A 379 ? 0.3816 0.3197 0.2080 -0.0550 0.0608 -0.0113 414 LYS A N 2875 C CA . LYS A 379 ? 0.4117 0.3431 0.2209 -0.0606 0.0639 -0.0150 414 LYS A CA 2876 C C . LYS A 379 ? 0.4328 0.3544 0.2368 -0.0606 0.0735 -0.0201 414 LYS A C 2877 O O . LYS A 379 ? 0.4664 0.3813 0.2566 -0.0642 0.0786 -0.0227 414 LYS A O 2878 C CB . LYS A 379 ? 0.4246 0.3583 0.2262 -0.0658 0.0566 -0.0164 414 LYS A CB 2879 C CG . LYS A 379 ? 0.4353 0.3779 0.2382 -0.0663 0.0479 -0.0110 414 LYS A CG 2880 C CD . LYS A 379 ? 0.4637 0.4052 0.2561 -0.0684 0.0492 -0.0084 414 LYS A CD 2881 C CE . LYS A 379 ? 0.4707 0.4203 0.2648 -0.0680 0.0409 -0.0023 414 LYS A CE 2882 N NZ . LYS A 379 ? 0.4856 0.4333 0.2665 -0.0712 0.0421 -0.0002 414 LYS A NZ 2883 N N . LYS A 380 ? 0.4325 0.3528 0.2470 -0.0564 0.0764 -0.0215 415 LYS A N 2884 C CA . LYS A 380 ? 0.4508 0.3616 0.2627 -0.0547 0.0863 -0.0254 415 LYS A CA 2885 C C . LYS A 380 ? 0.4457 0.3603 0.2734 -0.0474 0.0902 -0.0222 415 LYS A C 2886 O O . LYS A 380 ? 0.3957 0.3182 0.2366 -0.0442 0.0847 -0.0190 415 LYS A O 2887 C CB . LYS A 380 ? 0.4827 0.3876 0.2912 -0.0569 0.0863 -0.0301 415 LYS A CB 2888 C CG . LYS A 380 ? 0.5287 0.4308 0.3214 -0.0650 0.0822 -0.0335 415 LYS A CG 2889 C CD . LYS A 380 ? 0.5824 0.4761 0.3695 -0.0681 0.0845 -0.0390 415 LYS A CD 2890 C CE . LYS A 380 ? 0.6590 0.5490 0.4285 -0.0773 0.0818 -0.0431 415 LYS A CE 2891 N NZ . LYS A 380 ? 0.7118 0.5897 0.4730 -0.0808 0.0873 -0.0495 415 LYS A NZ 2892 N N . PRO A 381 ? 0.4644 0.3741 0.2913 -0.0447 0.0998 -0.0230 416 PRO A N 2893 C CA . PRO A 381 ? 0.4797 0.3953 0.3226 -0.0379 0.1031 -0.0192 416 PRO A CA 2894 C C . PRO A 381 ? 0.5202 0.4387 0.3765 -0.0332 0.1014 -0.0185 416 PRO A C 2895 O O . PRO A 381 ? 0.5354 0.4627 0.4059 -0.0291 0.0991 -0.0143 416 PRO A O 2896 C CB . PRO A 381 ? 0.5091 0.4174 0.3470 -0.0360 0.1148 -0.0211 416 PRO A CB 2897 C CG . PRO A 381 ? 0.5174 0.4172 0.3358 -0.0424 0.1166 -0.0250 416 PRO A CG 2898 C CD . PRO A 381 ? 0.5069 0.4054 0.3186 -0.0475 0.1085 -0.0275 416 PRO A CD 2899 N N . ASP A 382 ? 0.5111 0.4218 0.3623 -0.0342 0.1027 -0.0226 417 ASP A N 2900 C CA . ASP A 382 ? 0.5335 0.4458 0.3960 -0.0299 0.1015 -0.0219 417 ASP A CA 2901 C C . ASP A 382 ? 0.4822 0.3973 0.3446 -0.0333 0.0922 -0.0225 417 ASP A C 2902 O O . ASP A 382 ? 0.5117 0.4248 0.3783 -0.0317 0.0918 -0.0236 417 ASP A O 2903 C CB . ASP A 382 ? 0.6055 0.5064 0.4640 -0.0274 0.1111 -0.0253 417 ASP A CB 2904 C CG . ASP A 382 ? 0.6985 0.5869 0.5392 -0.0337 0.1135 -0.0314 417 ASP A CG 2905 O OD1 . ASP A 382 ? 0.7375 0.6265 0.5675 -0.0400 0.1092 -0.0328 417 ASP A OD1 2906 O OD2 . ASP A 382 ? 0.8330 0.7109 0.6699 -0.0326 0.1198 -0.0347 417 ASP A OD2 2907 N N . GLN A 383 ? 0.4189 0.3392 0.2771 -0.0377 0.0849 -0.0215 418 GLN A N 2908 C CA . GLN A 383 ? 0.3848 0.3092 0.2433 -0.0408 0.0760 -0.0216 418 GLN A CA 2909 C C . GLN A 383 ? 0.3432 0.2731 0.2160 -0.0363 0.0728 -0.0193 418 GLN A C 2910 O O . GLN A 383 ? 0.3533 0.2899 0.2374 -0.0320 0.0722 -0.0155 418 GLN A O 2911 C CB . GLN A 383 ? 0.3748 0.3065 0.2317 -0.0433 0.0692 -0.0185 418 GLN A CB 2912 C CG . GLN A 383 ? 0.3683 0.3043 0.2229 -0.0471 0.0607 -0.0185 418 GLN A CG 2913 C CD . GLN A 383 ? 0.3588 0.3007 0.2106 -0.0490 0.0553 -0.0150 418 GLN A CD 2914 O OE1 . GLN A 383 ? 0.3915 0.3304 0.2330 -0.0517 0.0580 -0.0153 418 GLN A OE1 2915 N NE2 . GLN A 383 ? 0.3584 0.3081 0.2186 -0.0474 0.0483 -0.0116 418 GLN A NE2 2916 N N . HIS A 384 ? 0.3298 0.2572 0.2017 -0.0378 0.0707 -0.0218 419 HIS A N 2917 C CA . HIS A 384 ? 0.3069 0.2378 0.1909 -0.0336 0.0687 -0.0201 419 HIS A CA 2918 C C . HIS A 384 ? 0.2923 0.2316 0.1818 -0.0348 0.0597 -0.0182 419 HIS A C 2919 O O . HIS A 384 ? 0.2800 0.2205 0.1754 -0.0334 0.0576 -0.0183 419 HIS A O 2920 C CB . HIS A 384 ? 0.3199 0.2413 0.2002 -0.0337 0.0739 -0.0237 419 HIS A CB 2921 C CG . HIS A 384 ? 0.3648 0.2770 0.2404 -0.0315 0.0837 -0.0254 419 HIS A CG 2922 N ND1 . HIS A 384 ? 0.3726 0.2862 0.2581 -0.0247 0.0887 -0.0225 419 HIS A ND1 2923 C CD2 . HIS A 384 ? 0.3874 0.2893 0.2494 -0.0351 0.0897 -0.0296 419 HIS A CD2 2924 C CE1 . HIS A 384 ? 0.3839 0.2884 0.2628 -0.0236 0.0977 -0.0246 419 HIS A CE1 2925 N NE2 . HIS A 384 ? 0.4023 0.2989 0.2664 -0.0300 0.0987 -0.0292 419 HIS A NE2 2926 N N . PHE A 385 ? 0.2842 0.2290 0.1717 -0.0370 0.0547 -0.0163 420 PHE A N 2927 C CA . PHE A 385 ? 0.2692 0.2223 0.1631 -0.0368 0.0468 -0.0137 420 PHE A CA 2928 C C . PHE A 385 ? 0.2632 0.2211 0.1570 -0.0369 0.0440 -0.0102 420 PHE A C 2929 O O . PHE A 385 ? 0.2529 0.2078 0.1399 -0.0382 0.0476 -0.0104 420 PHE A O 2930 C CB . PHE A 385 ? 0.2794 0.2330 0.1674 -0.0415 0.0422 -0.0159 420 PHE A CB 2931 C CG . PHE A 385 ? 0.2961 0.2477 0.1714 -0.0469 0.0416 -0.0175 420 PHE A CG 2932 C CD1 . PHE A 385 ? 0.3225 0.2653 0.1868 -0.0505 0.0471 -0.0218 420 PHE A CD1 2933 C CD2 . PHE A 385 ? 0.3020 0.2603 0.1759 -0.0483 0.0357 -0.0145 420 PHE A CD2 2934 C CE1 . PHE A 385 ? 0.3405 0.2815 0.1918 -0.0560 0.0465 -0.0233 420 PHE A CE1 2935 C CE2 . PHE A 385 ? 0.3174 0.2746 0.1792 -0.0532 0.0349 -0.0154 420 PHE A CE2 2936 C CZ . PHE A 385 ? 0.3291 0.2780 0.1794 -0.0574 0.0401 -0.0199 420 PHE A CZ 2937 N N . LYS A 386 ? 0.2512 0.2159 0.1522 -0.0355 0.0380 -0.0071 421 LYS A N 2938 C CA . LYS A 386 ? 0.2450 0.2133 0.1461 -0.0353 0.0354 -0.0036 421 LYS A CA 2939 C C . LYS A 386 ? 0.2376 0.2110 0.1396 -0.0362 0.0281 -0.0019 421 LYS A C 2940 O O . LYS A 386 ? 0.2431 0.2196 0.1525 -0.0344 0.0253 -0.0018 421 LYS A O 2941 C CB . LYS A 386 ? 0.2446 0.2154 0.1556 -0.0315 0.0369 -0.0008 421 LYS A CB 2942 C CG . LYS A 386 ? 0.2412 0.2145 0.1523 -0.0316 0.0347 0.0029 421 LYS A CG 2943 C CD . LYS A 386 ? 0.2361 0.2117 0.1560 -0.0291 0.0364 0.0054 421 LYS A CD 2944 C CE . LYS A 386 ? 0.2515 0.2258 0.1736 -0.0278 0.0432 0.0045 421 LYS A CE 2945 N NZ . LYS A 386 ? 0.2650 0.2351 0.1771 -0.0301 0.0476 0.0037 421 LYS A NZ 2946 N N . PRO A 387 ? 0.2512 0.2259 0.1458 -0.0388 0.0253 -0.0003 422 PRO A N 2947 C CA . PRO A 387 ? 0.2484 0.2290 0.1446 -0.0389 0.0185 0.0022 422 PRO A CA 2948 C C . PRO A 387 ? 0.2488 0.2319 0.1526 -0.0352 0.0163 0.0064 422 PRO A C 2949 O O . PRO A 387 ? 0.2494 0.2301 0.1534 -0.0342 0.0192 0.0082 422 PRO A O 2950 C CB . PRO A 387 ? 0.2639 0.2446 0.1485 -0.0429 0.0169 0.0027 422 PRO A CB 2951 C CG . PRO A 387 ? 0.2750 0.2504 0.1544 -0.0433 0.0224 0.0028 422 PRO A CG 2952 C CD . PRO A 387 ? 0.2744 0.2455 0.1587 -0.0414 0.0282 -0.0002 422 PRO A CD 2953 N N . TYR A 388 ? 0.2388 0.2264 0.1484 -0.0334 0.0116 0.0080 423 TYR A N 2954 C CA . TYR A 388 ? 0.2387 0.2276 0.1544 -0.0301 0.0094 0.0118 423 TYR A CA 2955 C C . TYR A 388 ? 0.2496 0.2436 0.1659 -0.0293 0.0038 0.0144 423 TYR A C 2956 O O . TYR A 388 ? 0.2580 0.2560 0.1757 -0.0301 0.0016 0.0126 423 TYR A O 2957 C CB . TYR A 388 ? 0.2281 0.2171 0.1537 -0.0273 0.0103 0.0108 423 TYR A CB 2958 C CG . TYR A 388 ? 0.2224 0.2083 0.1508 -0.0268 0.0151 0.0095 423 TYR A CG 2959 C CD1 . TYR A 388 ? 0.2238 0.2081 0.1514 -0.0276 0.0188 0.0062 423 TYR A CD1 2960 C CD2 . TYR A 388 ? 0.2320 0.2169 0.1645 -0.0254 0.0160 0.0118 423 TYR A CD2 2961 C CE1 . TYR A 388 ? 0.2355 0.2182 0.1668 -0.0265 0.0232 0.0058 423 TYR A CE1 2962 C CE2 . TYR A 388 ? 0.2304 0.2145 0.1666 -0.0251 0.0201 0.0111 423 TYR A CE2 2963 C CZ . TYR A 388 ? 0.2288 0.2123 0.1649 -0.0253 0.0236 0.0084 423 TYR A CZ 2964 O OH . TYR A 388 ? 0.2422 0.2261 0.1832 -0.0244 0.0276 0.0083 423 TYR A OH 2965 N N . MET A 389 ? 0.2496 0.2438 0.1657 -0.0274 0.0019 0.0187 424 MET A N 2966 C CA . MET A 389 ? 0.2580 0.2567 0.1787 -0.0246 -0.0025 0.0217 424 MET A CA 2967 C C . MET A 389 ? 0.2391 0.2370 0.1693 -0.0217 -0.0016 0.0202 424 MET A C 2968 O O . MET A 389 ? 0.2365 0.2299 0.1693 -0.0212 0.0015 0.0193 424 MET A O 2969 C CB . MET A 389 ? 0.2735 0.2710 0.1917 -0.0227 -0.0041 0.0270 424 MET A CB 2970 C CG . MET A 389 ? 0.3141 0.3139 0.2226 -0.0254 -0.0060 0.0291 424 MET A CG 2971 S SD . MET A 389 ? 0.3637 0.3738 0.2714 -0.0266 -0.0117 0.0296 424 MET A SD 2972 C CE . MET A 389 ? 0.3742 0.3874 0.2897 -0.0203 -0.0151 0.0355 424 MET A CE 2973 N N . LYS A 390 ? 0.2252 0.2279 0.1604 -0.0201 -0.0044 0.0199 425 LYS A N 2974 C CA . LYS A 390 ? 0.2225 0.2244 0.1653 -0.0181 -0.0033 0.0178 425 LYS A CA 2975 C C . LYS A 390 ? 0.2257 0.2227 0.1722 -0.0154 -0.0019 0.0194 425 LYS A C 2976 O O . LYS A 390 ? 0.2164 0.2110 0.1668 -0.0153 0.0002 0.0171 425 LYS A O 2977 C CB . LYS A 390 ? 0.2146 0.2226 0.1620 -0.0168 -0.0062 0.0175 425 LYS A CB 2978 C CG . LYS A 390 ? 0.2138 0.2253 0.1635 -0.0134 -0.0093 0.0219 425 LYS A CG 2979 C CD . LYS A 390 ? 0.2088 0.2279 0.1637 -0.0124 -0.0118 0.0215 425 LYS A CD 2980 C CE . LYS A 390 ? 0.2110 0.2339 0.1697 -0.0078 -0.0143 0.0262 425 LYS A CE 2981 N NZ . LYS A 390 ? 0.2166 0.2468 0.1821 -0.0063 -0.0157 0.0256 425 LYS A NZ 2982 N N . GLN A 391 ? 0.2335 0.2286 0.1782 -0.0136 -0.0029 0.0235 426 GLN A N 2983 C CA . GLN A 391 ? 0.2523 0.2412 0.1992 -0.0119 -0.0011 0.0249 426 GLN A CA 2984 C C . GLN A 391 ? 0.2427 0.2274 0.1881 -0.0146 0.0022 0.0234 426 GLN A C 2985 O O . GLN A 391 ? 0.2312 0.2119 0.1796 -0.0143 0.0039 0.0232 426 GLN A O 2986 C CB . GLN A 391 ? 0.2860 0.2725 0.2309 -0.0092 -0.0025 0.0299 426 GLN A CB 2987 C CG . GLN A 391 ? 0.3336 0.3192 0.2710 -0.0109 -0.0027 0.0330 426 GLN A CG 2988 C CD . GLN A 391 ? 0.4065 0.3993 0.3404 -0.0111 -0.0062 0.0346 426 GLN A CD 2989 O OE1 . GLN A 391 ? 0.3962 0.3956 0.3330 -0.0114 -0.0083 0.0325 426 GLN A OE1 2990 N NE2 . GLN A 391 ? 0.4569 0.4488 0.3840 -0.0116 -0.0071 0.0387 426 GLN A NE2 2991 N N . HIS A 392 ? 0.2291 0.2149 0.1698 -0.0173 0.0035 0.0224 427 HIS A N 2992 C CA . HIS A 392 ? 0.2388 0.2219 0.1787 -0.0196 0.0073 0.0211 427 HIS A CA 2993 C C . HIS A 392 ? 0.2196 0.2046 0.1636 -0.0203 0.0093 0.0173 427 HIS A C 2994 O O . HIS A 392 ? 0.2230 0.2068 0.1679 -0.0216 0.0125 0.0166 427 HIS A O 2995 C CB . HIS A 392 ? 0.2584 0.2406 0.1904 -0.0218 0.0085 0.0224 427 HIS A CB 2996 C CG . HIS A 392 ? 0.3083 0.2880 0.2362 -0.0210 0.0070 0.0270 427 HIS A CG 2997 N ND1 . HIS A 392 ? 0.3444 0.3247 0.2642 -0.0224 0.0061 0.0291 427 HIS A ND1 2998 C CD2 . HIS A 392 ? 0.3322 0.3081 0.2622 -0.0190 0.0064 0.0299 427 HIS A CD2 2999 C CE1 . HIS A 392 ? 0.3717 0.3492 0.2894 -0.0208 0.0049 0.0337 427 HIS A CE1 3000 N NE2 . HIS A 392 ? 0.3799 0.3542 0.3037 -0.0187 0.0053 0.0342 427 HIS A NE2 3001 N N . LEU A 393 ? 0.2003 0.1884 0.1471 -0.0194 0.0077 0.0151 428 LEU A N 3002 C CA . LEU A 393 ? 0.1994 0.1885 0.1503 -0.0196 0.0096 0.0121 428 LEU A CA 3003 C C . LEU A 393 ? 0.1955 0.1837 0.1521 -0.0188 0.0105 0.0123 428 LEU A C 3004 O O . LEU A 393 ? 0.2051 0.1915 0.1631 -0.0179 0.0089 0.0139 428 LEU A O 3005 C CB . LEU A 393 ? 0.1935 0.1856 0.1466 -0.0188 0.0076 0.0102 428 LEU A CB 3006 C CG . LEU A 393 ? 0.1998 0.1936 0.1475 -0.0207 0.0069 0.0090 428 LEU A CG 3007 C CD1 . LEU A 393 ? 0.2061 0.2036 0.1569 -0.0200 0.0043 0.0078 428 LEU A CD1 3008 C CD2 . LEU A 393 ? 0.1953 0.1869 0.1399 -0.0226 0.0107 0.0066 428 LEU A CD2 3009 N N . PRO A 394 ? 0.2025 0.1917 0.1622 -0.0193 0.0130 0.0108 429 PRO A N 3010 C CA . PRO A 394 ? 0.1941 0.1840 0.1596 -0.0190 0.0133 0.0109 429 PRO A CA 3011 C C . PRO A 394 ? 0.1874 0.1770 0.1554 -0.0177 0.0104 0.0105 429 PRO A C 3012 O O . PRO A 394 ? 0.1947 0.1859 0.1632 -0.0165 0.0091 0.0091 429 PRO A O 3013 C CB . PRO A 394 ? 0.1946 0.1874 0.1634 -0.0188 0.0156 0.0094 429 PRO A CB 3014 C CG . PRO A 394 ? 0.2095 0.2012 0.1734 -0.0194 0.0182 0.0090 429 PRO A CG 3015 C CD . PRO A 394 ? 0.2049 0.1948 0.1630 -0.0199 0.0160 0.0091 429 PRO A CD 3016 N N . LYS A 395 ? 0.1819 0.1693 0.1513 -0.0182 0.0100 0.0115 430 LYS A N 3017 C CA . LYS A 395 ? 0.1829 0.1685 0.1536 -0.0168 0.0080 0.0111 430 LYS A CA 3018 C C . LYS A 395 ? 0.1805 0.1691 0.1550 -0.0163 0.0075 0.0089 430 LYS A C 3019 O O . LYS A 395 ? 0.1692 0.1575 0.1443 -0.0147 0.0061 0.0081 430 LYS A O 3020 C CB . LYS A 395 ? 0.1841 0.1650 0.1544 -0.0181 0.0083 0.0123 430 LYS A CB 3021 C CG . LYS A 395 ? 0.1896 0.1664 0.1555 -0.0182 0.0088 0.0150 430 LYS A CG 3022 C CD . LYS A 395 ? 0.1902 0.1661 0.1535 -0.0152 0.0069 0.0165 430 LYS A CD 3023 C CE . LYS A 395 ? 0.2047 0.1757 0.1684 -0.0132 0.0063 0.0172 430 LYS A CE 3024 N NZ . LYS A 395 ? 0.2119 0.1835 0.1742 -0.0098 0.0046 0.0194 430 LYS A NZ 3025 N N . ARG A 396 ? 0.1699 0.1618 0.1471 -0.0174 0.0089 0.0083 431 ARG A N 3026 C CA . ARG A 396 ? 0.1749 0.1698 0.1553 -0.0167 0.0085 0.0068 431 ARG A CA 3027 C C . ARG A 396 ? 0.1824 0.1781 0.1619 -0.0149 0.0080 0.0056 431 ARG A C 3028 O O . ARG A 396 ? 0.1975 0.1947 0.1789 -0.0142 0.0073 0.0044 431 ARG A O 3029 C CB . ARG A 396 ? 0.1784 0.1775 0.1621 -0.0174 0.0103 0.0072 431 ARG A CB 3030 C CG . ARG A 396 ? 0.1746 0.1743 0.1569 -0.0167 0.0127 0.0075 431 ARG A CG 3031 C CD . ARG A 396 ? 0.1804 0.1842 0.1666 -0.0168 0.0151 0.0085 431 ARG A CD 3032 N NE . ARG A 396 ? 0.1767 0.1794 0.1604 -0.0164 0.0182 0.0086 431 ARG A NE 3033 C CZ . ARG A 396 ? 0.1989 0.1999 0.1803 -0.0150 0.0199 0.0074 431 ARG A CZ 3034 N NH1 . ARG A 396 ? 0.2015 0.2023 0.1834 -0.0138 0.0187 0.0061 431 ARG A NH1 3035 N NH2 . ARG A 396 ? 0.2093 0.2083 0.1871 -0.0152 0.0230 0.0072 431 ARG A NH2 3036 N N . LEU A 397 ? 0.1774 0.1726 0.1538 -0.0148 0.0083 0.0058 432 LEU A N 3037 C CA . LEU A 397 ? 0.1890 0.1853 0.1643 -0.0141 0.0077 0.0045 432 LEU A CA 3038 C C . LEU A 397 ? 0.1936 0.1901 0.1693 -0.0129 0.0054 0.0045 432 LEU A C 3039 O O . LEU A 397 ? 0.1999 0.1984 0.1761 -0.0125 0.0049 0.0034 432 LEU A O 3040 C CB . LEU A 397 ? 0.1983 0.1942 0.1694 -0.0151 0.0087 0.0045 432 LEU A CB 3041 C CG . LEU A 397 ? 0.2011 0.1964 0.1714 -0.0159 0.0120 0.0042 432 LEU A CG 3042 C CD1 . LEU A 397 ? 0.2292 0.2229 0.1937 -0.0174 0.0129 0.0041 432 LEU A CD1 3043 C CD2 . LEU A 397 ? 0.2015 0.1974 0.1741 -0.0151 0.0137 0.0028 432 LEU A CD2 3044 N N . HIS A 398 ? 0.1882 0.1825 0.1637 -0.0122 0.0045 0.0059 433 HIS A N 3045 C CA . HIS A 398 ? 0.1809 0.1749 0.1570 -0.0103 0.0030 0.0064 433 HIS A CA 3046 C C . HIS A 398 ? 0.1824 0.1802 0.1579 -0.0097 0.0017 0.0066 433 HIS A C 3047 O O . HIS A 398 ? 0.1844 0.1847 0.1622 -0.0085 0.0009 0.0059 433 HIS A O 3048 C CB . HIS A 398 ? 0.1764 0.1700 0.1552 -0.0096 0.0031 0.0048 433 HIS A CB 3049 C CG . HIS A 398 ? 0.1832 0.1735 0.1622 -0.0107 0.0038 0.0046 433 HIS A CG 3050 N ND1 . HIS A 398 ? 0.2035 0.1889 0.1812 -0.0104 0.0039 0.0055 433 HIS A ND1 3051 C CD2 . HIS A 398 ? 0.1907 0.1821 0.1710 -0.0125 0.0045 0.0038 433 HIS A CD2 3052 C CE1 . HIS A 398 ? 0.2026 0.1861 0.1804 -0.0127 0.0045 0.0048 433 HIS A CE1 3053 N NE2 . HIS A 398 ? 0.2015 0.1895 0.1812 -0.0139 0.0046 0.0040 433 HIS A NE2 3054 N N . TYR A 399 ? 0.1777 0.1762 0.1498 -0.0110 0.0015 0.0075 434 TYR A N 3055 C CA . TYR A 399 ? 0.1791 0.1820 0.1497 -0.0120 0.0002 0.0072 434 TYR A CA 3056 C C . TYR A 399 ? 0.1892 0.1934 0.1568 -0.0117 -0.0016 0.0099 434 TYR A C 3057 O O . TYR A 399 ? 0.1991 0.2037 0.1621 -0.0139 -0.0017 0.0102 434 TYR A O 3058 C CB . TYR A 399 ? 0.1828 0.1853 0.1509 -0.0146 0.0020 0.0049 434 TYR A CB 3059 C CG . TYR A 399 ? 0.1794 0.1856 0.1461 -0.0164 0.0011 0.0036 434 TYR A CG 3060 C CD1 . TYR A 399 ? 0.1904 0.1991 0.1606 -0.0161 0.0007 0.0022 434 TYR A CD1 3061 C CD2 . TYR A 399 ? 0.1954 0.2024 0.1568 -0.0190 0.0006 0.0036 434 TYR A CD2 3062 C CE1 . TYR A 399 ? 0.1961 0.2084 0.1651 -0.0185 0.0000 0.0010 434 TYR A CE1 3063 C CE2 . TYR A 399 ? 0.1990 0.2095 0.1586 -0.0217 -0.0004 0.0021 434 TYR A CE2 3064 C CZ . TYR A 399 ? 0.1934 0.2068 0.1572 -0.0215 -0.0007 0.0008 434 TYR A CZ 3065 O OH . TYR A 399 ? 0.1997 0.2166 0.1617 -0.0249 -0.0016 -0.0007 434 TYR A OH 3066 N N . ALA A 400 ? 0.1819 0.1869 0.1520 -0.0087 -0.0031 0.0122 435 ALA A N 3067 C CA . ALA A 400 ? 0.1937 0.2003 0.1614 -0.0077 -0.0051 0.0158 435 ALA A CA 3068 C C . ALA A 400 ? 0.2003 0.2106 0.1718 -0.0039 -0.0069 0.0183 435 ALA A C 3069 O O . ALA A 400 ? 0.2034 0.2192 0.1742 -0.0034 -0.0094 0.0210 435 ALA A O 3070 C CB . ALA A 400 ? 0.2040 0.2044 0.1683 -0.0076 -0.0038 0.0178 435 ALA A CB 3071 N N . ASN A 401 ? 0.1823 0.1900 0.1580 -0.0013 -0.0056 0.0176 436 ASN A N 3072 C CA . ASN A 401 ? 0.1954 0.2049 0.1748 0.0030 -0.0063 0.0203 436 ASN A CA 3073 C C . ASN A 401 ? 0.1983 0.2167 0.1825 0.0037 -0.0076 0.0197 436 ASN A C 3074 O O . ASN A 401 ? 0.1888 0.2071 0.1770 0.0059 -0.0063 0.0186 436 ASN A O 3075 C CB . ASN A 401 ? 0.2005 0.2018 0.1810 0.0055 -0.0037 0.0198 436 ASN A CB 3076 C CG . ASN A 401 ? 0.2248 0.2260 0.2084 0.0108 -0.0035 0.0230 436 ASN A CG 3077 O OD1 . ASN A 401 ? 0.2244 0.2300 0.2084 0.0132 -0.0054 0.0270 436 ASN A OD1 3078 N ND2 . ASN A 401 ? 0.2334 0.2298 0.2191 0.0129 -0.0010 0.0213 436 ASN A ND2 3079 N N . ASN A 402 ? 0.1918 0.2179 0.1750 0.0015 -0.0102 0.0206 437 ASN A N 3080 C CA . ASN A 402 ? 0.1922 0.2279 0.1800 0.0013 -0.0118 0.0204 437 ASN A CA 3081 C C . ASN A 402 ? 0.2047 0.2487 0.1904 -0.0007 -0.0154 0.0229 437 ASN A C 3082 O O . ASN A 402 ? 0.1967 0.2382 0.1761 -0.0044 -0.0159 0.0220 437 ASN A O 3083 C CB . ASN A 402 ? 0.2009 0.2364 0.1890 -0.0022 -0.0103 0.0157 437 ASN A CB 3084 C CG . ASN A 402 ? 0.2003 0.2448 0.1939 -0.0022 -0.0111 0.0153 437 ASN A CG 3085 O OD1 . ASN A 402 ? 0.2126 0.2656 0.2066 -0.0045 -0.0137 0.0162 437 ASN A OD1 3086 N ND2 . ASN A 402 ? 0.1971 0.2400 0.1948 0.0000 -0.0089 0.0139 437 ASN A ND2 3087 N N . ARG A 403 ? 0.1995 0.2535 0.1903 0.0015 -0.0178 0.0260 438 ARG A N 3088 C CA . ARG A 403 ? 0.1990 0.2628 0.1879 -0.0008 -0.0219 0.0288 438 ARG A CA 3089 C C . ARG A 403 ? 0.1973 0.2650 0.1825 -0.0081 -0.0230 0.0248 438 ARG A C 3090 O O . ARG A 403 ? 0.1986 0.2720 0.1794 -0.0117 -0.0261 0.0260 438 ARG A O 3091 C CB . ARG A 403 ? 0.2080 0.2834 0.2045 0.0034 -0.0244 0.0335 438 ARG A CB 3092 C CG . ARG A 403 ? 0.2149 0.2983 0.2186 0.0028 -0.0240 0.0314 438 ARG A CG 3093 C CD . ARG A 403 ? 0.2453 0.3402 0.2578 0.0082 -0.0256 0.0366 438 ARG A CD 3094 N NE . ARG A 403 ? 0.2439 0.3465 0.2633 0.0072 -0.0246 0.0343 438 ARG A NE 3095 C CZ . ARG A 403 ? 0.2914 0.3935 0.3176 0.0122 -0.0214 0.0344 438 ARG A CZ 3096 N NH1 . ARG A 403 ? 0.3042 0.3987 0.3320 0.0192 -0.0188 0.0368 438 ARG A NH1 3097 N NH2 . ARG A 403 ? 0.2731 0.3827 0.3046 0.0099 -0.0207 0.0320 438 ARG A NH2 3098 N N . ARG A 404 ? 0.1892 0.2533 0.1754 -0.0102 -0.0203 0.0202 439 ARG A N 3099 C CA . ARG A 404 ? 0.1914 0.2562 0.1734 -0.0169 -0.0202 0.0161 439 ARG A CA 3100 C C . ARG A 404 ? 0.1980 0.2528 0.1716 -0.0200 -0.0182 0.0134 439 ARG A C 3101 O O . ARG A 404 ? 0.2156 0.2695 0.1845 -0.0254 -0.0176 0.0100 439 ARG A O 3102 C CB . ARG A 404 ? 0.1891 0.2536 0.1756 -0.0175 -0.0177 0.0127 439 ARG A CB 3103 C CG . ARG A 404 ? 0.1812 0.2566 0.1762 -0.0152 -0.0192 0.0149 439 ARG A CG 3104 C CD . ARG A 404 ? 0.1822 0.2554 0.1818 -0.0141 -0.0160 0.0122 439 ARG A CD 3105 N NE . ARG A 404 ? 0.1913 0.2752 0.1994 -0.0111 -0.0170 0.0148 439 ARG A NE 3106 C CZ . ARG A 404 ? 0.1907 0.2749 0.2040 -0.0092 -0.0143 0.0135 439 ARG A CZ 3107 N NH1 . ARG A 404 ? 0.1931 0.2677 0.2037 -0.0100 -0.0110 0.0099 439 ARG A NH1 3108 N NH2 . ARG A 404 ? 0.1961 0.2911 0.2175 -0.0063 -0.0150 0.0162 439 ARG A NH2 3109 N N . ILE A 405 ? 0.1925 0.2394 0.1644 -0.0168 -0.0165 0.0146 440 ILE A N 3110 C CA . ILE A 405 ? 0.1937 0.2321 0.1582 -0.0194 -0.0144 0.0126 440 ILE A CA 3111 C C . ILE A 405 ? 0.2079 0.2481 0.1665 -0.0206 -0.0167 0.0155 440 ILE A C 3112 O O . ILE A 405 ? 0.2092 0.2496 0.1688 -0.0168 -0.0180 0.0197 440 ILE A O 3113 C CB . ILE A 405 ? 0.1901 0.2195 0.1559 -0.0161 -0.0112 0.0123 440 ILE A CB 3114 C CG1 . ILE A 405 ? 0.1833 0.2112 0.1542 -0.0152 -0.0090 0.0095 440 ILE A CG1 3115 C CG2 . ILE A 405 ? 0.2021 0.2245 0.1614 -0.0186 -0.0088 0.0107 440 ILE A CG2 3116 C CD1 . ILE A 405 ? 0.1869 0.2082 0.1600 -0.0120 -0.0068 0.0096 440 ILE A CD1 3117 N N . GLU A 406 ? 0.2098 0.2505 0.1614 -0.0261 -0.0170 0.0133 441 GLU A N 3118 C CA . GLU A 406 ? 0.2390 0.2817 0.1832 -0.0283 -0.0194 0.0156 441 GLU A CA 3119 C C . GLU A 406 ? 0.2454 0.2799 0.1864 -0.0258 -0.0172 0.0174 441 GLU A C 3120 O O . GLU A 406 ? 0.2498 0.2764 0.1916 -0.0248 -0.0133 0.0151 441 GLU A O 3121 C CB . GLU A 406 ? 0.2515 0.2939 0.1874 -0.0353 -0.0190 0.0118 441 GLU A CB 3122 C CG . GLU A 406 ? 0.2604 0.3126 0.1980 -0.0393 -0.0222 0.0107 441 GLU A CG 3123 C CD . GLU A 406 ? 0.2682 0.3195 0.2117 -0.0396 -0.0199 0.0072 441 GLU A CD 3124 O OE1 . GLU A 406 ? 0.2649 0.3083 0.2113 -0.0365 -0.0161 0.0057 441 GLU A OE1 3125 O OE2 . GLU A 406 ? 0.2822 0.3414 0.2275 -0.0432 -0.0221 0.0063 441 GLU A OE2 3126 N N . ASP A 407 ? 0.2629 0.2998 0.2003 -0.0249 -0.0197 0.0218 442 ASP A N 3127 C CA . ASP A 407 ? 0.2746 0.3038 0.2083 -0.0230 -0.0176 0.0239 442 ASP A CA 3128 C C . ASP A 407 ? 0.2609 0.2826 0.1877 -0.0268 -0.0136 0.0200 442 ASP A C 3129 O O . ASP A 407 ? 0.2631 0.2776 0.1905 -0.0252 -0.0102 0.0197 442 ASP A O 3130 C CB . ASP A 407 ? 0.2911 0.3240 0.2203 -0.0221 -0.0210 0.0294 442 ASP A CB 3131 C CG . ASP A 407 ? 0.3311 0.3696 0.2676 -0.0165 -0.0239 0.0346 442 ASP A CG 3132 O OD1 . ASP A 407 ? 0.3656 0.4034 0.3104 -0.0128 -0.0228 0.0339 442 ASP A OD1 3133 O OD2 . ASP A 407 ? 0.3837 0.4270 0.3173 -0.0154 -0.0272 0.0397 442 ASP A OD2 3134 N N . ILE A 408 ? 0.2556 0.2790 0.1760 -0.0321 -0.0138 0.0170 443 ILE A N 3135 C CA . ILE A 408 ? 0.2576 0.2736 0.1705 -0.0356 -0.0095 0.0132 443 ILE A CA 3136 C C . ILE A 408 ? 0.2543 0.2668 0.1709 -0.0363 -0.0061 0.0085 443 ILE A C 3137 O O . ILE A 408 ? 0.2593 0.2757 0.1775 -0.0384 -0.0075 0.0063 443 ILE A O 3138 C CB . ILE A 408 ? 0.2746 0.2924 0.1765 -0.0414 -0.0108 0.0122 443 ILE A CB 3139 C CG1 . ILE A 408 ? 0.2937 0.3147 0.1910 -0.0406 -0.0141 0.0175 443 ILE A CG1 3140 C CG2 . ILE A 408 ? 0.2857 0.2946 0.1801 -0.0446 -0.0052 0.0078 443 ILE A CG2 3141 C CD1 . ILE A 408 ? 0.3220 0.3466 0.2081 -0.0465 -0.0166 0.0172 443 ILE A CD1 3142 N N . HIS A 409 ? 0.2443 0.2497 0.1625 -0.0344 -0.0016 0.0073 444 HIS A N 3143 C CA . HIS A 409 ? 0.2372 0.2387 0.1586 -0.0344 0.0020 0.0035 444 HIS A CA 3144 C C . HIS A 409 ? 0.2520 0.2463 0.1673 -0.0363 0.0073 0.0008 444 HIS A C 3145 O O . HIS A 409 ? 0.2669 0.2585 0.1791 -0.0357 0.0090 0.0025 444 HIS A O 3146 C CB . HIS A 409 ? 0.2304 0.2315 0.1614 -0.0297 0.0025 0.0047 444 HIS A CB 3147 C CG . HIS A 409 ? 0.2248 0.2245 0.1603 -0.0293 0.0046 0.0017 444 HIS A CG 3148 N ND1 . HIS A 409 ? 0.2359 0.2397 0.1748 -0.0298 0.0024 0.0007 444 HIS A ND1 3149 C CD2 . HIS A 409 ? 0.2264 0.2211 0.1631 -0.0286 0.0089 -0.0002 444 HIS A CD2 3150 C CE1 . HIS A 409 ? 0.2476 0.2484 0.1892 -0.0294 0.0053 -0.0017 444 HIS A CE1 3151 N NE2 . HIS A 409 ? 0.2381 0.2336 0.1787 -0.0285 0.0091 -0.0021 444 HIS A NE2 3152 N N . LEU A 410 ? 0.2365 0.2273 0.1503 -0.0382 0.0104 -0.0030 445 LEU A N 3153 C CA . LEU A 410 ? 0.2314 0.2147 0.1410 -0.0388 0.0166 -0.0055 445 LEU A CA 3154 C C . LEU A 410 ? 0.2399 0.2209 0.1574 -0.0353 0.0197 -0.0063 445 LEU A C 3155 O O . LEU A 410 ? 0.2219 0.2034 0.1426 -0.0354 0.0191 -0.0080 445 LEU A O 3156 C CB . LEU A 410 ? 0.2527 0.2319 0.1523 -0.0440 0.0187 -0.0095 445 LEU A CB 3157 C CG . LEU A 410 ? 0.2634 0.2462 0.1544 -0.0486 0.0148 -0.0091 445 LEU A CG 3158 C CD1 . LEU A 410 ? 0.2863 0.2635 0.1665 -0.0545 0.0177 -0.0139 445 LEU A CD1 3159 C CD2 . LEU A 410 ? 0.2648 0.2480 0.1518 -0.0479 0.0143 -0.0059 445 LEU A CD2 3160 N N . LEU A 411 ? 0.2357 0.2148 0.1566 -0.0324 0.0228 -0.0049 446 LEU A N 3161 C CA . LEU A 411 ? 0.2427 0.2203 0.1705 -0.0292 0.0260 -0.0053 446 LEU A CA 3162 C C . LEU A 411 ? 0.2474 0.2183 0.1698 -0.0301 0.0321 -0.0080 446 LEU A C 3163 O O . LEU A 411 ? 0.2477 0.2157 0.1657 -0.0305 0.0356 -0.0079 446 LEU A O 3164 C CB . LEU A 411 ? 0.2622 0.2421 0.1968 -0.0260 0.0263 -0.0022 446 LEU A CB 3165 C CG . LEU A 411 ? 0.2864 0.2709 0.2286 -0.0238 0.0221 0.0000 446 LEU A CG 3166 C CD1 . LEU A 411 ? 0.2868 0.2724 0.2344 -0.0218 0.0238 0.0021 446 LEU A CD1 3167 C CD2 . LEU A 411 ? 0.2738 0.2594 0.2207 -0.0227 0.0210 -0.0013 446 LEU A CD2 3168 N N . VAL A 412 ? 0.2380 0.2057 0.1603 -0.0304 0.0337 -0.0104 447 VAL A N 3169 C CA . VAL A 412 ? 0.2473 0.2070 0.1634 -0.0314 0.0400 -0.0134 447 VAL A CA 3170 C C . VAL A 412 ? 0.2532 0.2111 0.1760 -0.0265 0.0449 -0.0120 447 VAL A C 3171 O O . VAL A 412 ? 0.2427 0.2045 0.1742 -0.0233 0.0431 -0.0102 447 VAL A O 3172 C CB . VAL A 412 ? 0.2572 0.2132 0.1686 -0.0348 0.0398 -0.0166 447 VAL A CB 3173 C CG1 . VAL A 412 ? 0.2658 0.2114 0.1699 -0.0360 0.0470 -0.0200 447 VAL A CG1 3174 C CG2 . VAL A 412 ? 0.2684 0.2286 0.1743 -0.0398 0.0343 -0.0173 447 VAL A CG2 3175 N N . ASP A 413 ? 0.2563 0.2089 0.1752 -0.0257 0.0512 -0.0128 448 ASP A N 3176 C CA . ASP A 413 ? 0.2610 0.2127 0.1868 -0.0205 0.0563 -0.0112 448 ASP A CA 3177 C C . ASP A 413 ? 0.2583 0.2060 0.1863 -0.0188 0.0580 -0.0121 448 ASP A C 3178 O O . ASP A 413 ? 0.2510 0.1921 0.1715 -0.0221 0.0590 -0.0155 448 ASP A O 3179 C CB . ASP A 413 ? 0.2973 0.2427 0.2176 -0.0199 0.0638 -0.0123 448 ASP A CB 3180 C CG . ASP A 413 ? 0.3199 0.2694 0.2395 -0.0206 0.0636 -0.0105 448 ASP A CG 3181 O OD1 . ASP A 413 ? 0.3325 0.2892 0.2563 -0.0212 0.0577 -0.0082 448 ASP A OD1 3182 O OD2 . ASP A 413 ? 0.3379 0.2826 0.2523 -0.0204 0.0698 -0.0115 448 ASP A OD2 3183 N N . ARG A 414 ? 0.2564 0.2081 0.1942 -0.0139 0.0584 -0.0091 449 ARG A N 3184 C CA A ARG A 414 ? 0.2669 0.2143 0.2066 -0.0116 0.0608 -0.0093 449 ARG A CA 3185 C CA B ARG A 414 ? 0.2660 0.2135 0.2061 -0.0113 0.0610 -0.0092 449 ARG A CA 3186 C C . ARG A 414 ? 0.2821 0.2178 0.2137 -0.0117 0.0686 -0.0122 449 ARG A C 3187 O O . ARG A 414 ? 0.2717 0.2045 0.2003 -0.0108 0.0737 -0.0125 449 ARG A O 3188 C CB A ARG A 414 ? 0.2762 0.2301 0.2271 -0.0061 0.0607 -0.0051 449 ARG A CB 3189 C CB B ARG A 414 ? 0.2731 0.2271 0.2245 -0.0055 0.0615 -0.0048 449 ARG A CB 3190 C CG A ARG A 414 ? 0.2944 0.2491 0.2494 -0.0017 0.0664 -0.0027 449 ARG A CG 3191 C CG B ARG A 414 ? 0.2905 0.2450 0.2451 -0.0016 0.0674 -0.0027 449 ARG A CG 3192 C CD A ARG A 414 ? 0.2991 0.2638 0.2660 0.0025 0.0643 0.0018 449 ARG A CD 3193 C CD B ARG A 414 ? 0.2950 0.2587 0.2616 0.0034 0.0666 0.0020 449 ARG A CD 3194 N NE A ARG A 414 ? 0.3112 0.2850 0.2824 0.0009 0.0596 0.0035 449 ARG A NE 3195 N NE B ARG A 414 ? 0.3020 0.2651 0.2721 0.0059 0.0656 0.0033 449 ARG A NE 3196 C CZ A ARG A 414 ? 0.3123 0.2957 0.2929 0.0028 0.0563 0.0070 449 ARG A CZ 3197 C CZ B ARG A 414 ? 0.3144 0.2857 0.2942 0.0098 0.0639 0.0075 449 ARG A CZ 3198 N NH1 A ARG A 414 ? 0.3216 0.3080 0.3086 0.0067 0.0565 0.0097 449 ARG A NH1 3199 N NH1 B ARG A 414 ? 0.2955 0.2657 0.2771 0.0117 0.0629 0.0087 449 ARG A NH1 3200 N NH2 A ARG A 414 ? 0.3144 0.3041 0.2973 0.0005 0.0526 0.0079 449 ARG A NH2 3201 N NH2 B ARG A 414 ? 0.3069 0.2879 0.2941 0.0113 0.0629 0.0106 449 ARG A NH2 3202 N N . ARG A 415 ? 0.2751 0.2036 0.2024 -0.0133 0.0699 -0.0144 450 ARG A N 3203 C CA . ARG A 415 ? 0.3070 0.2221 0.2255 -0.0140 0.0775 -0.0176 450 ARG A CA 3204 C C . ARG A 415 ? 0.3072 0.2158 0.2128 -0.0212 0.0777 -0.0227 450 ARG A C 3205 O O . ARG A 415 ? 0.3162 0.2126 0.2129 -0.0231 0.0839 -0.0262 450 ARG A O 3206 C CB . ARG A 415 ? 0.3264 0.2375 0.2473 -0.0080 0.0856 -0.0158 450 ARG A CB 3207 C CG . ARG A 415 ? 0.3437 0.2625 0.2777 -0.0008 0.0853 -0.0103 450 ARG A CG 3208 C CD . ARG A 415 ? 0.4143 0.3300 0.3513 0.0053 0.0936 -0.0080 450 ARG A CD 3209 N NE . ARG A 415 ? 0.4998 0.4008 0.4298 0.0069 0.1017 -0.0102 450 ARG A NE 3210 C CZ . ARG A 415 ? 0.5720 0.4611 0.4925 0.0061 0.1098 -0.0136 450 ARG A CZ 3211 N NH1 . ARG A 415 ? 0.5792 0.4695 0.4954 0.0039 0.1112 -0.0153 450 ARG A NH1 3212 N NH2 . ARG A 415 ? 0.6218 0.4968 0.5362 0.0076 0.1170 -0.0153 450 ARG A NH2 3213 N N . TRP A 416 ? 0.2868 0.2032 0.1912 -0.0254 0.0710 -0.0230 451 TRP A N 3214 C CA . TRP A 416 ? 0.2965 0.2093 0.1889 -0.0324 0.0702 -0.0270 451 TRP A CA 3215 C C . TRP A 416 ? 0.2930 0.2112 0.1841 -0.0379 0.0627 -0.0282 451 TRP A C 3216 O O . TRP A 416 ? 0.2847 0.2112 0.1848 -0.0360 0.0573 -0.0255 451 TRP A O 3217 C CB . TRP A 416 ? 0.3107 0.2277 0.2013 -0.0324 0.0699 -0.0258 451 TRP A CB 3218 C CG . TRP A 416 ? 0.3228 0.2319 0.2102 -0.0294 0.0786 -0.0265 451 TRP A CG 3219 C CD1 . TRP A 416 ? 0.3216 0.2319 0.2179 -0.0225 0.0830 -0.0232 451 TRP A CD1 3220 C CD2 . TRP A 416 ? 0.3482 0.2467 0.2221 -0.0333 0.0846 -0.0307 451 TRP A CD2 3221 N NE1 . TRP A 416 ? 0.3489 0.2503 0.2391 -0.0211 0.0917 -0.0249 451 TRP A NE1 3222 C CE2 . TRP A 416 ? 0.3621 0.2552 0.2378 -0.0278 0.0931 -0.0298 451 TRP A CE2 3223 C CE3 . TRP A 416 ? 0.3661 0.2595 0.2264 -0.0411 0.0835 -0.0352 451 TRP A CE3 3224 C CZ2 . TRP A 416 ? 0.3969 0.2786 0.2608 -0.0295 0.1012 -0.0335 451 TRP A CZ2 3225 C CZ3 . TRP A 416 ? 0.3778 0.2599 0.2257 -0.0435 0.0910 -0.0390 451 TRP A CZ3 3226 C CH2 . TRP A 416 ? 0.4013 0.2770 0.2508 -0.0376 0.1001 -0.0383 451 TRP A CH2 3227 N N . HIS A 417 ? 0.3002 0.2136 0.1797 -0.0448 0.0627 -0.0322 452 HIS A N 3228 C CA . HIS A 417 ? 0.3011 0.2217 0.1786 -0.0507 0.0553 -0.0331 452 HIS A CA 3229 C C . HIS A 417 ? 0.3057 0.2299 0.1759 -0.0546 0.0526 -0.0336 452 HIS A C 3230 O O . HIS A 417 ? 0.3132 0.2306 0.1758 -0.0551 0.0577 -0.0351 452 HIS A O 3231 C CB . HIS A 417 ? 0.3302 0.2431 0.1995 -0.0570 0.0570 -0.0376 452 HIS A CB 3232 C CG . HIS A 417 ? 0.3279 0.2410 0.2045 -0.0552 0.0565 -0.0368 452 HIS A CG 3233 N ND1 . HIS A 417 ? 0.3528 0.2564 0.2232 -0.0595 0.0601 -0.0404 452 HIS A ND1 3234 C CD2 . HIS A 417 ? 0.3283 0.2494 0.2170 -0.0500 0.0530 -0.0328 452 HIS A CD2 3235 C CE1 . HIS A 417 ? 0.3394 0.2454 0.2181 -0.0567 0.0588 -0.0384 452 HIS A CE1 3236 N NE2 . HIS A 417 ? 0.3272 0.2440 0.2169 -0.0510 0.0545 -0.0339 452 HIS A NE2 3237 N N . VAL A 418 ? 0.3046 0.2393 0.1770 -0.0573 0.0447 -0.0320 453 VAL A N 3238 C CA A VAL A 418 ? 0.3170 0.2554 0.1808 -0.0625 0.0411 -0.0325 453 VAL A CA 3239 C CA B VAL A 418 ? 0.3156 0.2540 0.1794 -0.0625 0.0411 -0.0325 453 VAL A CA 3240 C C . VAL A 418 ? 0.3274 0.2696 0.1870 -0.0695 0.0365 -0.0348 453 VAL A C 3241 O O . VAL A 418 ? 0.3309 0.2802 0.1990 -0.0687 0.0322 -0.0332 453 VAL A O 3242 C CB A VAL A 418 ? 0.3114 0.2602 0.1819 -0.0589 0.0359 -0.0276 453 VAL A CB 3243 C CB B VAL A 418 ? 0.3087 0.2573 0.1787 -0.0590 0.0360 -0.0276 453 VAL A CB 3244 C CG1 A VAL A 418 ? 0.3173 0.2715 0.1796 -0.0642 0.0309 -0.0273 453 VAL A CG1 3245 C CG1 B VAL A 418 ? 0.2928 0.2524 0.1736 -0.0569 0.0290 -0.0243 453 VAL A CG1 3246 C CG2 A VAL A 418 ? 0.3136 0.2586 0.1863 -0.0536 0.0409 -0.0258 453 VAL A CG2 3247 C CG2 B VAL A 418 ? 0.3199 0.2700 0.1791 -0.0639 0.0339 -0.0281 453 VAL A CG2 3248 N N . ALA A 419 ? 0.3482 0.2855 0.1944 -0.0768 0.0377 -0.0387 454 ALA A N 3249 C CA . ALA A 419 ? 0.3740 0.3156 0.2148 -0.0849 0.0332 -0.0411 454 ALA A CA 3250 C C . ALA A 419 ? 0.4000 0.3473 0.2316 -0.0900 0.0288 -0.0407 454 ALA A C 3251 O O . ALA A 419 ? 0.3858 0.3309 0.2134 -0.0877 0.0307 -0.0395 454 ALA A O 3252 C CB . ALA A 419 ? 0.3950 0.3236 0.2264 -0.0904 0.0393 -0.0470 454 ALA A CB 3253 N N . ARG A 420 ? 0.4217 0.3770 0.2502 -0.0969 0.0229 -0.0415 455 ARG A N 3254 C CA . ARG A 420 ? 0.4771 0.4409 0.2984 -0.1015 0.0173 -0.0401 455 ARG A CA 3255 C C . ARG A 420 ? 0.4956 0.4486 0.2988 -0.1091 0.0218 -0.0453 455 ARG A C 3256 O O . ARG A 420 ? 0.4597 0.4127 0.2558 -0.1091 0.0216 -0.0440 455 ARG A O 3257 C CB . ARG A 420 ? 0.4984 0.4772 0.3242 -0.1058 0.0088 -0.0381 455 ARG A CB 3258 C CG . ARG A 420 ? 0.5429 0.5340 0.3663 -0.1070 0.0016 -0.0338 455 ARG A CG 3259 C CD . ARG A 420 ? 0.5711 0.5791 0.4029 -0.1087 -0.0067 -0.0303 455 ARG A CD 3260 N NE . ARG A 420 ? 0.5944 0.6031 0.4208 -0.1181 -0.0074 -0.0351 455 ARG A NE 3261 C CZ . ARG A 420 ? 0.6475 0.6635 0.4645 -0.1275 -0.0121 -0.0364 455 ARG A CZ 3262 N NH1 . ARG A 420 ? 0.6622 0.6863 0.4737 -0.1287 -0.0171 -0.0329 455 ARG A NH1 3263 N NH2 . ARG A 420 ? 0.6657 0.6812 0.4787 -0.1361 -0.0119 -0.0411 455 ARG A NH2 3264 N N . LYS A 421 ? 0.5380 0.4811 0.3335 -0.1153 0.0261 -0.0512 456 LYS A N 3265 C CA . LYS A 421 ? 0.6152 0.5465 0.3921 -0.1241 0.0308 -0.0574 456 LYS A CA 3266 C C . LYS A 421 ? 0.6025 0.5158 0.3747 -0.1249 0.0404 -0.0631 456 LYS A C 3267 O O . LYS A 421 ? 0.5590 0.4719 0.3411 -0.1220 0.0412 -0.0627 456 LYS A O 3268 C CB . LYS A 421 ? 0.6700 0.6098 0.4389 -0.1353 0.0241 -0.0596 456 LYS A CB 3269 C CG . LYS A 421 ? 0.6983 0.6563 0.4697 -0.1362 0.0143 -0.0542 456 LYS A CG 3270 C CD . LYS A 421 ? 0.7435 0.7071 0.5023 -0.1489 0.0094 -0.0575 456 LYS A CD 3271 C CE . LYS A 421 ? 0.7800 0.7608 0.5388 -0.1499 0.0001 -0.0519 456 LYS A CE 3272 N NZ . LYS A 421 ? 0.8238 0.8067 0.5652 -0.1622 -0.0030 -0.0554 456 LYS A NZ 3273 N N . PRO A 422 ? 0.6114 0.5093 0.3678 -0.1289 0.0480 -0.0684 457 PRO A N 3274 C CA . PRO A 422 ? 0.6473 0.5267 0.3987 -0.1291 0.0580 -0.0735 457 PRO A CA 3275 C C . PRO A 422 ? 0.7269 0.6028 0.4756 -0.1369 0.0576 -0.0777 457 PRO A C 3276 O O . PRO A 422 ? 0.7795 0.6425 0.5296 -0.1344 0.0648 -0.0799 457 PRO A O 3277 C CB . PRO A 422 ? 0.6606 0.5256 0.3940 -0.1330 0.0654 -0.0784 457 PRO A CB 3278 C CG . PRO A 422 ? 0.6406 0.5158 0.3752 -0.1296 0.0613 -0.0739 457 PRO A CG 3279 C CD . PRO A 422 ? 0.6267 0.5222 0.3706 -0.1312 0.0493 -0.0691 457 PRO A CD 3280 N N . LEU A 423 ? 0.7557 0.6432 0.5009 -0.1461 0.0495 -0.0783 458 LEU A N 3281 C CA . LEU A 423 ? 0.8531 0.7404 0.5982 -0.1536 0.0481 -0.0815 458 LEU A CA 3282 C C . LEU A 423 ? 0.8544 0.7468 0.6177 -0.1456 0.0472 -0.0773 458 LEU A C 3283 O O . LEU A 423 ? 0.8299 0.7146 0.5931 -0.1488 0.0506 -0.0803 458 LEU A O 3284 C CB . LEU A 423 ? 0.8978 0.8005 0.6381 -0.1644 0.0385 -0.0819 458 LEU A CB 3285 C CG . LEU A 423 ? 0.9661 0.8579 0.6843 -0.1770 0.0415 -0.0891 458 LEU A CG 3286 C CD1 . LEU A 423 ? 0.9666 0.8751 0.6786 -0.1850 0.0318 -0.0877 458 LEU A CD1 3287 C CD2 . LEU A 423 ? 0.9918 0.8715 0.7029 -0.1858 0.0461 -0.0955 458 LEU A CD2 3288 N N . ASP A 424 ? 0.8455 0.7499 0.6235 -0.1356 0.0430 -0.0707 459 ASP A N 3289 C CA . ASP A 424 ? 0.8462 0.7546 0.6407 -0.1271 0.0427 -0.0666 459 ASP A CA 3290 C C . ASP A 424 ? 0.8748 0.7661 0.6694 -0.1199 0.0527 -0.0677 459 ASP A C 3291 O O . ASP A 424 ? 0.8897 0.7746 0.6892 -0.1179 0.0563 -0.0681 459 ASP A O 3292 C CB . ASP A 424 ? 0.7907 0.7161 0.5994 -0.1191 0.0355 -0.0596 459 ASP A CB 3293 C CG . ASP A 424 ? 0.7855 0.7280 0.5938 -0.1247 0.0259 -0.0575 459 ASP A CG 3294 O OD1 . ASP A 424 ? 0.8234 0.7698 0.6267 -0.1341 0.0229 -0.0604 459 ASP A OD1 3295 O OD2 . ASP A 424 ? 0.7053 0.6576 0.5182 -0.1199 0.0214 -0.0528 459 ASP A OD2 3296 N N . LYS A 432 ? 0.9444 0.6532 0.7014 -0.0767 0.1581 -0.0821 467 LYS A N 3297 C CA . LYS A 432 ? 0.9296 0.6460 0.7021 -0.0694 0.1549 -0.0756 467 LYS A CA 3298 C C . LYS A 432 ? 0.8870 0.6221 0.6666 -0.0757 0.1422 -0.0745 467 LYS A C 3299 O O . LYS A 432 ? 0.8792 0.6108 0.6496 -0.0869 0.1399 -0.0794 467 LYS A O 3300 C CB . LYS A 432 ? 0.9605 0.6549 0.7269 -0.0681 0.1650 -0.0768 467 LYS A CB 3301 C CG . LYS A 432 ? 0.9699 0.6693 0.7487 -0.0630 0.1621 -0.0711 467 LYS A CG 3302 C CD . LYS A 432 ? 0.9571 0.6733 0.7545 -0.0504 0.1580 -0.0626 467 LYS A CD 3303 C CE . LYS A 432 ? 0.9370 0.6550 0.7445 -0.0451 0.1568 -0.0570 467 LYS A CE 3304 N NZ . LYS A 432 ? 0.9296 0.6624 0.7539 -0.0329 0.1538 -0.0489 467 LYS A NZ 3305 N N . CYS A 433 ? 0.8111 0.5660 0.6070 -0.0687 0.1343 -0.0680 468 CYS A N 3306 C CA . CYS A 433 ? 0.7318 0.5061 0.5354 -0.0735 0.1223 -0.0665 468 CYS A CA 3307 C C . CYS A 433 ? 0.6722 0.4477 0.4824 -0.0735 0.1201 -0.0642 468 CYS A C 3308 O O . CYS A 433 ? 0.6982 0.4648 0.5123 -0.0664 0.1260 -0.0611 468 CYS A O 3309 C CB . CYS A 433 ? 0.7457 0.5397 0.5628 -0.0663 0.1151 -0.0610 468 CYS A CB 3310 S SG . CYS A 433 ? 0.8323 0.6256 0.6443 -0.0637 0.1187 -0.0620 468 CYS A SG 3311 N N . PHE A 434 ? 0.5942 0.3820 0.4064 -0.0810 0.1115 -0.0651 469 PHE A N 3312 C CA . PHE A 434 ? 0.5803 0.3723 0.3996 -0.0816 0.1082 -0.0627 469 PHE A CA 3313 C C . PHE A 434 ? 0.5379 0.3443 0.3740 -0.0712 0.1034 -0.0554 469 PHE A C 3314 O O . PHE A 434 ? 0.5210 0.3275 0.3630 -0.0689 0.1032 -0.0525 469 PHE A O 3315 C CB . PHE A 434 ? 0.6008 0.4034 0.4179 -0.0928 0.1004 -0.0658 469 PHE A CB 3316 C CG . PHE A 434 ? 0.6501 0.4382 0.4512 -0.1046 0.1049 -0.0729 469 PHE A CG 3317 C CD1 . PHE A 434 ? 0.6650 0.4398 0.4615 -0.1085 0.1100 -0.0747 469 PHE A CD1 3318 C CD2 . PHE A 434 ? 0.6702 0.4577 0.4600 -0.1123 0.1039 -0.0779 469 PHE A CD2 3319 C CE1 . PHE A 434 ? 0.7114 0.4722 0.4926 -0.1202 0.1142 -0.0816 469 PHE A CE1 3320 C CE2 . PHE A 434 ? 0.6994 0.4736 0.4735 -0.1241 0.1078 -0.0848 469 PHE A CE2 3321 C CZ . PHE A 434 ? 0.7190 0.4797 0.4889 -0.1282 0.1130 -0.0868 469 PHE A CZ 3322 N N . PHE A 435 ? 0.4869 0.3055 0.3298 -0.0659 0.0994 -0.0526 470 PHE A N 3323 C CA . PHE A 435 ? 0.4695 0.3019 0.3274 -0.0570 0.0947 -0.0461 470 PHE A CA 3324 C C . PHE A 435 ? 0.4381 0.2693 0.2998 -0.0478 0.0988 -0.0430 470 PHE A C 3325 O O . PHE A 435 ? 0.4327 0.2577 0.2867 -0.0489 0.1028 -0.0459 470 PHE A O 3326 C CB . PHE A 435 ? 0.4723 0.3239 0.3369 -0.0600 0.0842 -0.0450 470 PHE A CB 3327 C CG . PHE A 435 ? 0.4921 0.3502 0.3544 -0.0610 0.0815 -0.0460 470 PHE A CG 3328 C CD1 . PHE A 435 ? 0.4992 0.3644 0.3694 -0.0530 0.0805 -0.0420 470 PHE A CD1 3329 C CD2 . PHE A 435 ? 0.5271 0.3840 0.3788 -0.0702 0.0799 -0.0510 470 PHE A CD2 3330 C CE1 . PHE A 435 ? 0.4942 0.3644 0.3617 -0.0540 0.0785 -0.0427 470 PHE A CE1 3331 C CE2 . PHE A 435 ? 0.5402 0.4027 0.3890 -0.0710 0.0776 -0.0515 470 PHE A CE2 3332 C CZ . PHE A 435 ? 0.4931 0.3617 0.3497 -0.0628 0.0771 -0.0474 470 PHE A CZ 3333 N N . GLN A 436 ? 0.4041 0.2411 0.2773 -0.0391 0.0982 -0.0373 471 GLN A N 3334 C CA . GLN A 436 ? 0.4069 0.2453 0.2862 -0.0299 0.1015 -0.0333 471 GLN A CA 3335 C C . GLN A 436 ? 0.3659 0.2221 0.2589 -0.0243 0.0942 -0.0279 471 GLN A C 3336 O O . GLN A 436 ? 0.3654 0.2252 0.2649 -0.0171 0.0961 -0.0242 471 GLN A O 3337 C CB . GLN A 436 ? 0.4521 0.2770 0.3311 -0.0236 0.1101 -0.0310 471 GLN A CB 3338 C CG . GLN A 436 ? 0.5125 0.3170 0.3773 -0.0282 0.1190 -0.0363 471 GLN A CG 3339 C CD . GLN A 436 ? 0.5991 0.3899 0.4642 -0.0203 0.1284 -0.0333 471 GLN A CD 3340 O OE1 . GLN A 436 ? 0.6450 0.4347 0.5137 -0.0125 0.1333 -0.0305 471 GLN A OE1 3341 N NE2 . GLN A 436 ? 0.6459 0.4262 0.5075 -0.0220 0.1312 -0.0335 471 GLN A NE2 3342 N N . GLY A 437 ? 0.3383 0.2055 0.2358 -0.0277 0.0863 -0.0274 472 GLY A N 3343 C CA . GLY A 437 ? 0.3104 0.1935 0.2195 -0.0234 0.0794 -0.0230 472 GLY A CA 3344 C C . GLY A 437 ? 0.2973 0.1917 0.2073 -0.0291 0.0712 -0.0246 472 GLY A C 3345 O O . GLY A 437 ? 0.2980 0.1904 0.2022 -0.0361 0.0697 -0.0281 472 GLY A O 3346 N N . ASP A 438 ? 0.2698 0.1764 0.1872 -0.0262 0.0661 -0.0218 473 ASP A N 3347 C CA . ASP A 438 ? 0.2565 0.1746 0.1768 -0.0298 0.0583 -0.0221 473 ASP A CA 3348 C C . ASP A 438 ? 0.2389 0.1683 0.1692 -0.0245 0.0540 -0.0178 473 ASP A C 3349 O O . ASP A 438 ? 0.2309 0.1603 0.1658 -0.0187 0.0567 -0.0149 473 ASP A O 3350 C CB . ASP A 438 ? 0.2685 0.1864 0.1808 -0.0360 0.0570 -0.0258 473 ASP A CB 3351 C CG . ASP A 438 ? 0.2679 0.1946 0.1804 -0.0416 0.0502 -0.0270 473 ASP A CG 3352 O OD1 . ASP A 438 ? 0.2666 0.2004 0.1861 -0.0405 0.0462 -0.0250 473 ASP A OD1 3353 O OD2 . ASP A 438 ? 0.2770 0.2044 0.1827 -0.0471 0.0486 -0.0297 473 ASP A OD2 3354 N N . HIS A 439 ? 0.2325 0.1717 0.1663 -0.0266 0.0474 -0.0175 474 HIS A N 3355 C CA . HIS A 439 ? 0.2232 0.1726 0.1654 -0.0229 0.0428 -0.0142 474 HIS A CA 3356 C C . HIS A 439 ? 0.2150 0.1720 0.1569 -0.0264 0.0372 -0.0150 474 HIS A C 3357 O O . HIS A 439 ? 0.2280 0.1839 0.1642 -0.0315 0.0362 -0.0178 474 HIS A O 3358 C CB . HIS A 439 ? 0.2159 0.1682 0.1641 -0.0203 0.0413 -0.0119 474 HIS A CB 3359 C CG . HIS A 439 ? 0.2259 0.1778 0.1719 -0.0246 0.0397 -0.0139 474 HIS A CG 3360 N ND1 . HIS A 439 ? 0.2236 0.1840 0.1723 -0.0269 0.0343 -0.0142 474 HIS A ND1 3361 C CD2 . HIS A 439 ? 0.2295 0.1736 0.1707 -0.0273 0.0432 -0.0158 474 HIS A CD2 3362 C CE1 . HIS A 439 ? 0.2309 0.1898 0.1772 -0.0309 0.0343 -0.0160 474 HIS A CE1 3363 N NE2 . HIS A 439 ? 0.2316 0.1805 0.1731 -0.0316 0.0396 -0.0172 474 HIS A NE2 3364 N N . GLY A 440 ? 0.2093 0.1739 0.1571 -0.0236 0.0334 -0.0124 475 GLY A N 3365 C CA . GLY A 440 ? 0.2052 0.1767 0.1534 -0.0257 0.0284 -0.0123 475 GLY A CA 3366 C C . GLY A 440 ? 0.2077 0.1820 0.1576 -0.0235 0.0277 -0.0104 475 GLY A C 3367 O O . GLY A 440 ? 0.2241 0.2041 0.1760 -0.0236 0.0236 -0.0092 475 GLY A O 3368 N N . PHE A 441 ? 0.2109 0.1810 0.1605 -0.0211 0.0321 -0.0098 476 PHE A N 3369 C CA . PHE A 441 ? 0.2031 0.1754 0.1544 -0.0192 0.0325 -0.0080 476 PHE A CA 3370 C C . PHE A 441 ? 0.1914 0.1707 0.1503 -0.0167 0.0287 -0.0051 476 PHE A C 3371 O O . PHE A 441 ? 0.1846 0.1666 0.1478 -0.0156 0.0265 -0.0044 476 PHE A O 3372 C CB . PHE A 441 ? 0.2146 0.1822 0.1661 -0.0164 0.0384 -0.0074 476 PHE A CB 3373 C CG . PHE A 441 ? 0.2242 0.1828 0.1676 -0.0184 0.0434 -0.0104 476 PHE A CG 3374 C CD1 . PHE A 441 ? 0.2272 0.1827 0.1628 -0.0219 0.0445 -0.0126 476 PHE A CD1 3375 C CD2 . PHE A 441 ? 0.2249 0.1776 0.1679 -0.0171 0.0472 -0.0111 476 PHE A CD2 3376 C CE1 . PHE A 441 ? 0.2433 0.1899 0.1704 -0.0245 0.0493 -0.0159 476 PHE A CE1 3377 C CE2 . PHE A 441 ? 0.2380 0.1808 0.1727 -0.0193 0.0524 -0.0142 476 PHE A CE2 3378 C CZ . PHE A 441 ? 0.2462 0.1858 0.1726 -0.0233 0.0534 -0.0168 476 PHE A CZ 3379 N N . ASP A 442 ? 0.2009 0.1825 0.1605 -0.0163 0.0283 -0.0037 477 ASP A N 3380 C CA . ASP A 442 ? 0.1858 0.1726 0.1517 -0.0145 0.0259 -0.0011 477 ASP A CA 3381 C C . ASP A 442 ? 0.1788 0.1678 0.1507 -0.0119 0.0257 0.0000 477 ASP A C 3382 O O . ASP A 442 ? 0.1726 0.1599 0.1458 -0.0099 0.0293 0.0005 477 ASP A O 3383 C CB . ASP A 442 ? 0.1972 0.1843 0.1633 -0.0139 0.0286 0.0001 477 ASP A CB 3384 C CG . ASP A 442 ? 0.1961 0.1883 0.1677 -0.0133 0.0262 0.0026 477 ASP A CG 3385 O OD1 . ASP A 442 ? 0.1849 0.1801 0.1610 -0.0125 0.0234 0.0033 477 ASP A OD1 3386 O OD2 . ASP A 442 ? 0.2082 0.2008 0.1791 -0.0139 0.0276 0.0037 477 ASP A OD2 3387 N N . ASN A 443 ? 0.1747 0.1675 0.1500 -0.0119 0.0218 0.0006 478 ASN A N 3388 C CA . ASN A 443 ? 0.1843 0.1792 0.1640 -0.0100 0.0211 0.0016 478 ASN A CA 3389 C C . ASN A 443 ? 0.1863 0.1851 0.1712 -0.0081 0.0220 0.0041 478 ASN A C 3390 O O . ASN A 443 ? 0.1975 0.1986 0.1857 -0.0065 0.0214 0.0053 478 ASN A O 3391 C CB . ASN A 443 ? 0.1814 0.1784 0.1620 -0.0108 0.0172 0.0012 478 ASN A CB 3392 C CG . ASN A 443 ? 0.1864 0.1860 0.1689 -0.0113 0.0146 0.0021 478 ASN A CG 3393 O OD1 . ASN A 443 ? 0.1925 0.1917 0.1738 -0.0120 0.0152 0.0027 478 ASN A OD1 3394 N ND2 . ASN A 443 ? 0.1854 0.1867 0.1697 -0.0112 0.0121 0.0021 478 ASN A ND2 3395 N N . LYS A 444 ? 0.2129 0.2130 0.1987 -0.0082 0.0234 0.0052 479 LYS A N 3396 C CA . LYS A 444 ? 0.2279 0.2328 0.2194 -0.0063 0.0248 0.0078 479 LYS A CA 3397 C C . LYS A 444 ? 0.2228 0.2260 0.2150 -0.0035 0.0299 0.0087 479 LYS A C 3398 O O . LYS A 444 ? 0.2513 0.2596 0.2492 -0.0012 0.0311 0.0115 479 LYS A O 3399 C CB . LYS A 444 ? 0.2480 0.2566 0.2416 -0.0080 0.0237 0.0090 479 LYS A CB 3400 C CG . LYS A 444 ? 0.2907 0.2972 0.2817 -0.0086 0.0270 0.0088 479 LYS A CG 3401 C CD . LYS A 444 ? 0.3243 0.3349 0.3181 -0.0105 0.0257 0.0104 479 LYS A CD 3402 C CE . LYS A 444 ? 0.3594 0.3681 0.3504 -0.0113 0.0290 0.0106 479 LYS A CE 3403 N NZ . LYS A 444 ? 0.3888 0.4020 0.3850 -0.0093 0.0331 0.0126 479 LYS A NZ 3404 N N . VAL A 445 ? 0.2258 0.2221 0.2123 -0.0037 0.0328 0.0065 480 VAL A N 3405 C CA . VAL A 445 ? 0.2439 0.2360 0.2295 -0.0010 0.0385 0.0069 480 VAL A CA 3406 C C . VAL A 445 ? 0.2362 0.2291 0.2256 0.0022 0.0392 0.0089 480 VAL A C 3407 O O . VAL A 445 ? 0.2214 0.2132 0.2095 0.0013 0.0365 0.0080 480 VAL A O 3408 C CB . VAL A 445 ? 0.2473 0.2306 0.2241 -0.0033 0.0411 0.0033 480 VAL A CB 3409 C CG1 . VAL A 445 ? 0.2758 0.2523 0.2505 -0.0007 0.0473 0.0031 480 VAL A CG1 3410 C CG2 . VAL A 445 ? 0.2652 0.2481 0.2383 -0.0057 0.0414 0.0023 480 VAL A CG2 3411 N N . ASN A 446 ? 0.2439 0.2391 0.2381 0.0061 0.0429 0.0119 481 ASN A N 3412 C CA . ASN A 446 ? 0.2685 0.2653 0.2668 0.0100 0.0436 0.0148 481 ASN A CA 3413 C C . ASN A 446 ? 0.2519 0.2397 0.2445 0.0100 0.0453 0.0130 481 ASN A C 3414 O O . ASN A 446 ? 0.2373 0.2265 0.2311 0.0104 0.0426 0.0141 481 ASN A O 3415 C CB . ASN A 446 ? 0.3558 0.3552 0.3595 0.0149 0.0487 0.0185 481 ASN A CB 3416 C CG . ASN A 446 ? 0.4428 0.4548 0.4553 0.0157 0.0460 0.0221 481 ASN A CG 3417 O OD1 . ASN A 446 ? 0.5798 0.5976 0.5937 0.0124 0.0403 0.0219 481 ASN A OD1 3418 N ND2 . ASN A 446 ? 0.5243 0.5405 0.5427 0.0201 0.0503 0.0257 481 ASN A ND2 3419 N N . SER A 447 ? 0.2262 0.2045 0.2121 0.0090 0.0497 0.0100 482 SER A N 3420 C CA . SER A 447 ? 0.2380 0.2068 0.2179 0.0083 0.0520 0.0080 482 SER A CA 3421 C C . SER A 447 ? 0.2248 0.1943 0.2021 0.0041 0.0468 0.0056 482 SER A C 3422 O O . SER A 447 ? 0.2235 0.1878 0.1980 0.0037 0.0476 0.0050 482 SER A O 3423 C CB . SER A 447 ? 0.2537 0.2121 0.2260 0.0069 0.0578 0.0046 482 SER A CB 3424 O OG . SER A 447 ? 0.2549 0.2145 0.2234 0.0025 0.0555 0.0017 482 SER A OG 3425 N N . MET A 448 ? 0.2194 0.1951 0.1978 0.0012 0.0417 0.0047 483 MET A N 3426 C CA . MET A 448 ? 0.2060 0.1830 0.1825 -0.0022 0.0371 0.0027 483 MET A CA 3427 C C . MET A 448 ? 0.1982 0.1812 0.1795 -0.0009 0.0333 0.0049 483 MET A C 3428 O O . MET A 448 ? 0.1866 0.1699 0.1665 -0.0031 0.0305 0.0035 483 MET A O 3429 C CB . MET A 448 ? 0.2198 0.1997 0.1947 -0.0054 0.0339 0.0009 483 MET A CB 3430 C CG . MET A 448 ? 0.2233 0.1973 0.1914 -0.0081 0.0365 -0.0019 483 MET A CG 3431 S SD . MET A 448 ? 0.2337 0.1994 0.1946 -0.0114 0.0386 -0.0054 483 MET A SD 3432 C CE . MET A 448 ? 0.2468 0.2033 0.2054 -0.0083 0.0463 -0.0049 483 MET A CE 3433 N N . GLN A 449 ? 0.1894 0.1775 0.1763 0.0023 0.0334 0.0085 484 GLN A N 3434 C CA . GLN A 449 ? 0.2024 0.1964 0.1930 0.0031 0.0297 0.0106 484 GLN A CA 3435 C C . GLN A 449 ? 0.2035 0.1932 0.1919 0.0040 0.0309 0.0110 484 GLN A C 3436 O O . GLN A 449 ? 0.2314 0.2143 0.2173 0.0056 0.0354 0.0113 484 GLN A O 3437 C CB . GLN A 449 ? 0.2091 0.2107 0.2061 0.0061 0.0293 0.0147 484 GLN A CB 3438 C CG . GLN A 449 ? 0.2093 0.2153 0.2089 0.0050 0.0287 0.0146 484 GLN A CG 3439 C CD . GLN A 449 ? 0.2260 0.2321 0.2229 0.0008 0.0251 0.0115 484 GLN A CD 3440 O OE1 . GLN A 449 ? 0.2261 0.2356 0.2237 -0.0007 0.0211 0.0113 484 GLN A OE1 3441 N NE2 . GLN A 449 ? 0.1984 0.2003 0.1917 -0.0006 0.0267 0.0093 484 GLN A NE2 3442 N N . THR A 450 ? 0.2048 0.1980 0.1937 0.0029 0.0271 0.0112 485 THR A N 3443 C CA . THR A 450 ? 0.2095 0.1992 0.1959 0.0031 0.0279 0.0115 485 THR A CA 3444 C C . THR A 450 ? 0.2103 0.2059 0.1996 0.0049 0.0253 0.0149 485 THR A C 3445 O O . THR A 450 ? 0.2197 0.2220 0.2133 0.0065 0.0238 0.0175 485 THR A O 3446 C CB . THR A 450 ? 0.2083 0.1949 0.1907 -0.0007 0.0267 0.0077 485 THR A CB 3447 O OG1 . THR A 450 ? 0.2304 0.2126 0.2101 -0.0008 0.0285 0.0079 485 THR A OG1 3448 C CG2 . THR A 450 ? 0.2168 0.2094 0.2007 -0.0026 0.0221 0.0066 485 THR A CG2 3449 N N . VAL A 451 ? 0.2143 0.2078 0.2011 0.0045 0.0251 0.0152 486 VAL A N 3450 C CA . VAL A 451 ? 0.2345 0.2327 0.2227 0.0065 0.0232 0.0189 486 VAL A CA 3451 C C . VAL A 451 ? 0.2107 0.2126 0.1973 0.0036 0.0192 0.0174 486 VAL A C 3452 O O . VAL A 451 ? 0.2054 0.2047 0.1894 0.0008 0.0189 0.0138 486 VAL A O 3453 C CB . VAL A 451 ? 0.2463 0.2389 0.2324 0.0092 0.0268 0.0217 486 VAL A CB 3454 C CG1 . VAL A 451 ? 0.2738 0.2632 0.2621 0.0131 0.0311 0.0241 486 VAL A CG1 3455 C CG2 . VAL A 451 ? 0.2632 0.2480 0.2442 0.0064 0.0288 0.0185 486 VAL A CG2 3456 N N . PHE A 452 ? 0.2081 0.2165 0.1962 0.0044 0.0164 0.0203 487 PHE A N 3457 C CA . PHE A 452 ? 0.1979 0.2087 0.1832 0.0021 0.0134 0.0194 487 PHE A CA 3458 C C . PHE A 452 ? 0.1887 0.2036 0.1736 0.0040 0.0121 0.0240 487 PHE A C 3459 O O . PHE A 452 ? 0.1941 0.2155 0.1829 0.0059 0.0107 0.0276 487 PHE A O 3460 C CB . PHE A 452 ? 0.1812 0.1965 0.1673 -0.0007 0.0099 0.0169 487 PHE A CB 3461 C CG . PHE A 452 ? 0.2046 0.2218 0.1871 -0.0029 0.0073 0.0160 487 PHE A CG 3462 C CD1 . PHE A 452 ? 0.2202 0.2330 0.1990 -0.0045 0.0081 0.0129 487 PHE A CD1 3463 C CD2 . PHE A 452 ? 0.2183 0.2419 0.2009 -0.0033 0.0043 0.0187 487 PHE A CD2 3464 C CE1 . PHE A 452 ? 0.2336 0.2476 0.2085 -0.0063 0.0065 0.0120 487 PHE A CE1 3465 C CE2 . PHE A 452 ? 0.2345 0.2590 0.2123 -0.0056 0.0023 0.0178 487 PHE A CE2 3466 C CZ . PHE A 452 ? 0.2338 0.2531 0.2077 -0.0070 0.0036 0.0143 487 PHE A CZ 3467 N N . VAL A 453 ? 0.1952 0.2072 0.1757 0.0034 0.0126 0.0241 488 VAL A N 3468 C CA . VAL A 453 ? 0.2089 0.2252 0.1874 0.0042 0.0106 0.0279 488 VAL A CA 3469 C C . VAL A 453 ? 0.2030 0.2181 0.1761 0.0007 0.0092 0.0247 488 VAL A C 3470 O O . VAL A 453 ? 0.2131 0.2224 0.1839 -0.0005 0.0116 0.0216 488 VAL A O 3471 C CB . VAL A 453 ? 0.2314 0.2437 0.2088 0.0080 0.0138 0.0325 488 VAL A CB 3472 C CG1 . VAL A 453 ? 0.2513 0.2684 0.2260 0.0088 0.0114 0.0370 488 VAL A CG1 3473 C CG2 . VAL A 453 ? 0.2240 0.2359 0.2065 0.0121 0.0163 0.0354 488 VAL A CG2 3474 N N . GLY A 454 ? 0.2060 0.2270 0.1770 -0.0009 0.0056 0.0256 489 GLY A N 3475 C CA . GLY A 454 ? 0.2179 0.2377 0.1826 -0.0037 0.0048 0.0235 489 GLY A CA 3476 C C . GLY A 454 ? 0.2322 0.2552 0.1933 -0.0028 0.0035 0.0283 489 GLY A C 3477 O O . GLY A 454 ? 0.2484 0.2786 0.2115 -0.0018 0.0005 0.0323 489 GLY A O 3478 N N . TYR A 455 ? 0.2367 0.2551 0.1923 -0.0032 0.0055 0.0282 490 TYR A N 3479 C CA . TYR A 455 ? 0.2358 0.2565 0.1869 -0.0022 0.0046 0.0331 490 TYR A CA 3480 C C . TYR A 455 ? 0.2459 0.2639 0.1893 -0.0055 0.0050 0.0301 490 TYR A C 3481 O O . TYR A 455 ? 0.2459 0.2578 0.1882 -0.0064 0.0085 0.0266 490 TYR A O 3482 C CB . TYR A 455 ? 0.2523 0.2681 0.2044 0.0018 0.0082 0.0375 490 TYR A CB 3483 C CG . TYR A 455 ? 0.2586 0.2758 0.2057 0.0033 0.0077 0.0432 490 TYR A CG 3484 C CD1 . TYR A 455 ? 0.2703 0.2824 0.2104 0.0016 0.0098 0.0425 490 TYR A CD1 3485 C CD2 . TYR A 455 ? 0.2663 0.2905 0.2159 0.0065 0.0050 0.0497 490 TYR A CD2 3486 C CE1 . TYR A 455 ? 0.2847 0.2977 0.2194 0.0029 0.0093 0.0481 490 TYR A CE1 3487 C CE2 . TYR A 455 ? 0.2876 0.3136 0.2325 0.0082 0.0043 0.0556 490 TYR A CE2 3488 C CZ . TYR A 455 ? 0.2901 0.3100 0.2271 0.0064 0.0064 0.0548 490 TYR A CZ 3489 O OH . TYR A 455 ? 0.3279 0.3492 0.2595 0.0080 0.0057 0.0610 490 TYR A OH 3490 N N . GLY A 456 ? 0.2473 0.2702 0.1852 -0.0075 0.0017 0.0317 491 GLY A N 3491 C CA . GLY A 456 ? 0.2583 0.2785 0.1878 -0.0106 0.0025 0.0292 491 GLY A CA 3492 C C . GLY A 456 ? 0.2649 0.2905 0.1890 -0.0144 -0.0016 0.0279 491 GLY A C 3493 O O . GLY A 456 ? 0.2536 0.2858 0.1808 -0.0151 -0.0055 0.0292 491 GLY A O 3494 N N . PRO A 457 ? 0.2673 0.2900 0.1828 -0.0175 -0.0006 0.0251 492 PRO A N 3495 C CA . PRO A 457 ? 0.2877 0.3145 0.1963 -0.0219 -0.0044 0.0236 492 PRO A CA 3496 C C . PRO A 457 ? 0.2805 0.3085 0.1916 -0.0247 -0.0064 0.0188 492 PRO A C 3497 O O . PRO A 457 ? 0.2650 0.2985 0.1727 -0.0282 -0.0107 0.0190 492 PRO A O 3498 C CB . PRO A 457 ? 0.3003 0.3212 0.1993 -0.0243 -0.0011 0.0202 492 PRO A CB 3499 C CG . PRO A 457 ? 0.2904 0.3047 0.1939 -0.0218 0.0041 0.0180 492 PRO A CG 3500 C CD . PRO A 457 ? 0.2916 0.3072 0.2033 -0.0175 0.0042 0.0228 492 PRO A CD 3501 N N . THR A 458 ? 0.2744 0.2975 0.1912 -0.0236 -0.0035 0.0148 493 THR A N 3502 C CA . THR A 458 ? 0.2669 0.2893 0.1850 -0.0262 -0.0047 0.0101 493 THR A CA 3503 C C . THR A 458 ? 0.2602 0.2880 0.1868 -0.0251 -0.0075 0.0123 493 THR A C 3504 O O . THR A 458 ? 0.2696 0.2991 0.1965 -0.0281 -0.0098 0.0100 493 THR A O 3505 C CB . THR A 458 ? 0.2694 0.2841 0.1883 -0.0257 -0.0002 0.0047 493 THR A CB 3506 O OG1 . THR A 458 ? 0.2863 0.2970 0.1984 -0.0261 0.0029 0.0034 493 THR A OG1 3507 C CG2 . THR A 458 ? 0.2814 0.2937 0.1985 -0.0290 -0.0010 -0.0002 493 THR A CG2 3508 N N . PHE A 459 ? 0.2535 0.2837 0.1866 -0.0209 -0.0070 0.0169 494 PHE A N 3509 C CA . PHE A 459 ? 0.2363 0.2722 0.1776 -0.0191 -0.0091 0.0198 494 PHE A CA 3510 C C . PHE A 459 ? 0.2551 0.3007 0.1955 -0.0203 -0.0138 0.0247 494 PHE A C 3511 O O . PHE A 459 ? 0.2523 0.2997 0.1865 -0.0207 -0.0148 0.0274 494 PHE A O 3512 C CB . PHE A 459 ? 0.2330 0.2664 0.1808 -0.0141 -0.0060 0.0226 494 PHE A CB 3513 C CG . PHE A 459 ? 0.2301 0.2568 0.1810 -0.0134 -0.0026 0.0182 494 PHE A CG 3514 C CD1 . PHE A 459 ? 0.2263 0.2535 0.1817 -0.0143 -0.0034 0.0157 494 PHE A CD1 3515 C CD2 . PHE A 459 ? 0.2179 0.2381 0.1669 -0.0123 0.0012 0.0166 494 PHE A CD2 3516 C CE1 . PHE A 459 ? 0.2287 0.2504 0.1867 -0.0136 -0.0006 0.0120 494 PHE A CE1 3517 C CE2 . PHE A 459 ? 0.2343 0.2499 0.1865 -0.0120 0.0038 0.0128 494 PHE A CE2 3518 C CZ . PHE A 459 ? 0.2199 0.2363 0.1764 -0.0125 0.0027 0.0107 494 PHE A CZ 3519 N N . LYS A 460 ? 0.2448 0.2973 0.1914 -0.0208 -0.0166 0.0262 495 LYS A N 3520 C CA . LYS A 460 ? 0.2651 0.3291 0.2130 -0.0215 -0.0212 0.0316 495 LYS A CA 3521 C C . LYS A 460 ? 0.2619 0.3294 0.2137 -0.0155 -0.0204 0.0388 495 LYS A C 3522 O O . LYS A 460 ? 0.2551 0.3159 0.2101 -0.0110 -0.0161 0.0393 495 LYS A O 3523 C CB . LYS A 460 ? 0.2732 0.3444 0.2278 -0.0236 -0.0240 0.0315 495 LYS A CB 3524 C CG . LYS A 460 ? 0.2889 0.3574 0.2382 -0.0303 -0.0254 0.0252 495 LYS A CG 3525 C CD . LYS A 460 ? 0.3141 0.3905 0.2698 -0.0329 -0.0283 0.0258 495 LYS A CD 3526 C CE . LYS A 460 ? 0.3449 0.4186 0.2943 -0.0403 -0.0300 0.0200 495 LYS A CE 3527 N NZ . LYS A 460 ? 0.3738 0.4527 0.3306 -0.0424 -0.0314 0.0199 495 LYS A NZ 3528 N N . TYR A 461 ? 0.2803 0.3580 0.2312 -0.0158 -0.0246 0.0444 496 TYR A N 3529 C CA . TYR A 461 ? 0.2646 0.3468 0.2186 -0.0101 -0.0245 0.0524 496 TYR A CA 3530 C C . TYR A 461 ? 0.2569 0.3484 0.2225 -0.0065 -0.0255 0.0571 496 TYR A C 3531 O O . TYR A 461 ? 0.2447 0.3458 0.2135 -0.0102 -0.0296 0.0568 496 TYR A O 3532 C CB . TYR A 461 ? 0.2932 0.3829 0.2397 -0.0127 -0.0290 0.0563 496 TYR A CB 3533 C CG . TYR A 461 ? 0.2918 0.3878 0.2408 -0.0069 -0.0297 0.0656 496 TYR A CG 3534 C CD1 . TYR A 461 ? 0.3056 0.3925 0.2534 -0.0014 -0.0248 0.0682 496 TYR A CD1 3535 C CD2 . TYR A 461 ? 0.3113 0.4228 0.2635 -0.0070 -0.0354 0.0722 496 TYR A CD2 3536 C CE1 . TYR A 461 ? 0.3120 0.4033 0.2615 0.0041 -0.0250 0.0771 496 TYR A CE1 3537 C CE2 . TYR A 461 ? 0.3263 0.4439 0.2809 -0.0010 -0.0360 0.0814 496 TYR A CE2 3538 C CZ . TYR A 461 ? 0.3280 0.4346 0.2811 0.0047 -0.0306 0.0839 496 TYR A CZ 3539 O OH . TYR A 461 ? 0.3802 0.4913 0.3352 0.0112 -0.0306 0.0934 496 TYR A OH 3540 N N . ARG A 462 ? 0.2652 0.3533 0.2367 0.0004 -0.0214 0.0611 497 ARG A N 3541 C CA . ARG A 462 ? 0.2776 0.3739 0.2602 0.0053 -0.0213 0.0665 497 ARG A CA 3542 C C . ARG A 462 ? 0.2701 0.3722 0.2587 0.0017 -0.0231 0.0630 497 ARG A C 3543 O O . ARG A 462 ? 0.2619 0.3777 0.2564 0.0010 -0.0271 0.0670 497 ARG A O 3544 C CB . ARG A 462 ? 0.3048 0.4142 0.2896 0.0081 -0.0252 0.0754 497 ARG A CB 3545 C CG . ARG A 462 ? 0.3374 0.4419 0.3173 0.0128 -0.0231 0.0807 497 ARG A CG 3546 C CD . ARG A 462 ? 0.3817 0.5009 0.3654 0.0163 -0.0273 0.0905 497 ARG A CD 3547 N NE . ARG A 462 ? 0.4625 0.5769 0.4432 0.0224 -0.0246 0.0971 497 ARG A NE 3548 C CZ . ARG A 462 ? 0.5362 0.6437 0.5220 0.0303 -0.0188 0.1013 497 ARG A CZ 3549 N NH1 . ARG A 462 ? 0.5644 0.6687 0.5585 0.0332 -0.0148 0.0992 497 ARG A NH1 3550 N NH2 . ARG A 462 ? 0.5764 0.6791 0.5582 0.0353 -0.0166 0.1074 497 ARG A NH2 3551 N N . THR A 463 ? 0.2485 0.3406 0.2356 -0.0005 -0.0202 0.0559 498 THR A N 3552 C CA . THR A 463 ? 0.2400 0.3350 0.2305 -0.0049 -0.0218 0.0516 498 THR A CA 3553 C C . THR A 463 ? 0.2330 0.3208 0.2291 -0.0019 -0.0170 0.0491 498 THR A C 3554 O O . THR A 463 ? 0.2215 0.2976 0.2142 -0.0003 -0.0129 0.0458 498 THR A O 3555 C CB . THR A 463 ? 0.2558 0.3461 0.2373 -0.0122 -0.0238 0.0448 498 THR A CB 3556 O OG1 . THR A 463 ? 0.2662 0.3643 0.2422 -0.0159 -0.0287 0.0469 498 THR A OG1 3557 C CG2 . THR A 463 ? 0.2636 0.3549 0.2480 -0.0167 -0.0248 0.0402 498 THR A CG2 3558 N N . LYS A 464 ? 0.2329 0.3286 0.2371 -0.0014 -0.0176 0.0508 499 LYS A N 3559 C CA . LYS A 464 ? 0.2417 0.3320 0.2508 0.0003 -0.0135 0.0483 499 LYS A CA 3560 C C . LYS A 464 ? 0.2332 0.3225 0.2407 -0.0060 -0.0153 0.0425 499 LYS A C 3561 O O . LYS A 464 ? 0.2334 0.3313 0.2409 -0.0108 -0.0197 0.0426 499 LYS A O 3562 C CB . LYS A 464 ? 0.2710 0.3707 0.2902 0.0052 -0.0124 0.0543 499 LYS A CB 3563 C CG . LYS A 464 ? 0.2985 0.3927 0.3223 0.0075 -0.0077 0.0522 499 LYS A CG 3564 C CD . LYS A 464 ? 0.3569 0.4615 0.3909 0.0125 -0.0064 0.0585 499 LYS A CD 3565 C CE . LYS A 464 ? 0.3962 0.4953 0.4342 0.0149 -0.0012 0.0566 499 LYS A CE 3566 N NZ . LYS A 464 ? 0.4228 0.5333 0.4713 0.0198 0.0002 0.0630 499 LYS A NZ 3567 N N . VAL A 465 ? 0.2101 0.2889 0.2159 -0.0061 -0.0120 0.0375 500 VAL A N 3568 C CA . VAL A 465 ? 0.2187 0.2945 0.2225 -0.0114 -0.0129 0.0322 500 VAL A CA 3569 C C . VAL A 465 ? 0.2135 0.2863 0.2225 -0.0092 -0.0094 0.0314 500 VAL A C 3570 O O . VAL A 465 ? 0.2128 0.2820 0.2241 -0.0042 -0.0057 0.0331 500 VAL A O 3571 C CB . VAL A 465 ? 0.2352 0.3003 0.2303 -0.0140 -0.0124 0.0267 500 VAL A CB 3572 C CG1 . VAL A 465 ? 0.2565 0.3240 0.2456 -0.0160 -0.0153 0.0275 500 VAL A CG1 3573 C CG2 . VAL A 465 ? 0.2253 0.2803 0.2192 -0.0102 -0.0080 0.0250 500 VAL A CG2 3574 N N . PRO A 466 ? 0.2178 0.2914 0.2279 -0.0132 -0.0103 0.0287 501 PRO A N 3575 C CA . PRO A 466 ? 0.2112 0.2820 0.2256 -0.0112 -0.0069 0.0282 501 PRO A CA 3576 C C . PRO A 466 ? 0.1959 0.2546 0.2063 -0.0091 -0.0032 0.0247 501 PRO A C 3577 O O . PRO A 466 ? 0.1849 0.2370 0.1892 -0.0102 -0.0036 0.0217 501 PRO A O 3578 C CB . PRO A 466 ? 0.2371 0.3099 0.2517 -0.0168 -0.0089 0.0257 501 PRO A CB 3579 C CG . PRO A 466 ? 0.2508 0.3312 0.2638 -0.0213 -0.0134 0.0265 501 PRO A CG 3580 C CD . PRO A 466 ? 0.2286 0.3062 0.2363 -0.0197 -0.0142 0.0267 501 PRO A CD 3581 N N . PRO A 467 ? 0.1989 0.2551 0.2126 -0.0062 0.0002 0.0251 502 PRO A N 3582 C CA . PRO A 467 ? 0.1938 0.2393 0.2033 -0.0053 0.0032 0.0215 502 PRO A CA 3583 C C . PRO A 467 ? 0.1945 0.2350 0.1995 -0.0093 0.0016 0.0171 502 PRO A C 3584 O O . PRO A 467 ? 0.1912 0.2347 0.1970 -0.0127 -0.0003 0.0165 502 PRO A O 3585 C CB . PRO A 467 ? 0.2075 0.2526 0.2209 -0.0030 0.0067 0.0225 502 PRO A CB 3586 C CG . PRO A 467 ? 0.2345 0.2892 0.2546 -0.0006 0.0068 0.0274 502 PRO A CG 3587 C CD . PRO A 467 ? 0.2165 0.2795 0.2374 -0.0041 0.0019 0.0285 502 PRO A CD 3588 N N . PHE A 468 ? 0.1760 0.2087 0.1763 -0.0090 0.0027 0.0142 503 PHE A N 3589 C CA . PHE A 468 ? 0.1774 0.2052 0.1738 -0.0118 0.0016 0.0105 503 PHE A CA 3590 C C . PHE A 468 ? 0.1731 0.1942 0.1675 -0.0103 0.0040 0.0084 503 PHE A C 3591 O O . PHE A 468 ? 0.1715 0.1911 0.1664 -0.0077 0.0063 0.0094 503 PHE A O 3592 C CB . PHE A 468 ? 0.1871 0.2148 0.1795 -0.0139 -0.0006 0.0092 503 PHE A CB 3593 C CG . PHE A 468 ? 0.1900 0.2156 0.1800 -0.0118 0.0003 0.0095 503 PHE A CG 3594 C CD1 . PHE A 468 ? 0.1889 0.2083 0.1762 -0.0111 0.0020 0.0069 503 PHE A CD1 3595 C CD2 . PHE A 468 ? 0.2111 0.2413 0.2020 -0.0104 -0.0002 0.0128 503 PHE A CD2 3596 C CE1 . PHE A 468 ? 0.1994 0.2168 0.1846 -0.0096 0.0032 0.0072 503 PHE A CE1 3597 C CE2 . PHE A 468 ? 0.2242 0.2515 0.2124 -0.0085 0.0009 0.0132 503 PHE A CE2 3598 C CZ . PHE A 468 ? 0.2139 0.2347 0.1992 -0.0084 0.0028 0.0103 503 PHE A CZ 3599 N N . GLU A 469 ? 0.1760 0.1930 0.1678 -0.0119 0.0035 0.0057 504 GLU A N 3600 C CA . GLU A 469 ? 0.1808 0.1929 0.1710 -0.0109 0.0051 0.0039 504 GLU A CA 3601 C C . GLU A 469 ? 0.1862 0.1958 0.1737 -0.0105 0.0052 0.0023 504 GLU A C 3602 O O . GLU A 469 ? 0.1903 0.1999 0.1760 -0.0115 0.0040 0.0015 504 GLU A O 3603 C CB . GLU A 469 ? 0.1929 0.2026 0.1822 -0.0123 0.0046 0.0026 504 GLU A CB 3604 C CG . GLU A 469 ? 0.2172 0.2291 0.2089 -0.0130 0.0048 0.0041 504 GLU A CG 3605 C CD . GLU A 469 ? 0.2286 0.2373 0.2191 -0.0141 0.0049 0.0033 504 GLU A CD 3606 O OE1 . GLU A 469 ? 0.2345 0.2396 0.2226 -0.0146 0.0041 0.0018 504 GLU A OE1 3607 O OE2 . GLU A 469 ? 0.2652 0.2749 0.2571 -0.0142 0.0061 0.0045 504 GLU A OE2 3608 N N . ASN A 470 ? 0.1672 0.1745 0.1542 -0.0094 0.0069 0.0018 505 ASN A N 3609 C CA . ASN A 470 ? 0.1792 0.1852 0.1644 -0.0093 0.0074 0.0005 505 ASN A CA 3610 C C . ASN A 470 ? 0.1680 0.1728 0.1521 -0.0099 0.0065 -0.0014 505 ASN A C 3611 O O . ASN A 470 ? 0.1825 0.1870 0.1652 -0.0098 0.0068 -0.0023 505 ASN A O 3612 C CB . ASN A 470 ? 0.1970 0.2011 0.1818 -0.0088 0.0096 0.0003 505 ASN A CB 3613 C CG . ASN A 470 ? 0.2164 0.2193 0.2012 -0.0094 0.0098 -0.0008 505 ASN A CG 3614 O OD1 . ASN A 470 ? 0.2160 0.2194 0.2012 -0.0097 0.0086 -0.0010 505 ASN A OD1 3615 N ND2 . ASN A 470 ? 0.2407 0.2420 0.2244 -0.0100 0.0114 -0.0015 505 ASN A ND2 3616 N N . ILE A 471 ? 0.1566 0.1606 0.1411 -0.0103 0.0057 -0.0018 506 ILE A N 3617 C CA . ILE A 471 ? 0.1706 0.1726 0.1540 -0.0102 0.0052 -0.0033 506 ILE A CA 3618 C C . ILE A 471 ? 0.1829 0.1839 0.1640 -0.0111 0.0048 -0.0042 506 ILE A C 3619 O O . ILE A 471 ? 0.1921 0.1907 0.1717 -0.0107 0.0054 -0.0057 506 ILE A O 3620 C CB . ILE A 471 ? 0.1775 0.1776 0.1612 -0.0103 0.0047 -0.0030 506 ILE A CB 3621 C CG1 . ILE A 471 ? 0.1815 0.1816 0.1651 -0.0120 0.0039 -0.0022 506 ILE A CG1 3622 C CG2 . ILE A 471 ? 0.1761 0.1771 0.1608 -0.0097 0.0050 -0.0024 506 ILE A CG2 3623 C CD1 . ILE A 471 ? 0.1861 0.1833 0.1691 -0.0126 0.0036 -0.0020 506 ILE A CD1 3624 N N . GLU A 472 ? 0.1783 0.1813 0.1590 -0.0123 0.0039 -0.0032 507 GLU A N 3625 C CA . GLU A 472 ? 0.1819 0.1846 0.1596 -0.0141 0.0030 -0.0040 507 GLU A CA 3626 C C . GLU A 472 ? 0.1840 0.1870 0.1594 -0.0136 0.0038 -0.0044 507 GLU A C 3627 O O . GLU A 472 ? 0.1876 0.1895 0.1593 -0.0151 0.0035 -0.0057 507 GLU A O 3628 C CB . GLU A 472 ? 0.1788 0.1853 0.1573 -0.0159 0.0013 -0.0023 507 GLU A CB 3629 C CG . GLU A 472 ? 0.1870 0.1937 0.1676 -0.0171 0.0006 -0.0017 507 GLU A CG 3630 C CD . GLU A 472 ? 0.1976 0.1990 0.1753 -0.0188 0.0007 -0.0039 507 GLU A CD 3631 O OE1 . GLU A 472 ? 0.2166 0.2150 0.1903 -0.0201 0.0007 -0.0059 507 GLU A OE1 3632 O OE2 . GLU A 472 ? 0.2329 0.2325 0.2120 -0.0187 0.0011 -0.0035 507 GLU A OE2 3633 N N . LEU A 473 ? 0.1915 0.1958 0.1687 -0.0119 0.0050 -0.0035 508 LEU A N 3634 C CA . LEU A 473 ? 0.1959 0.2007 0.1709 -0.0117 0.0059 -0.0032 508 LEU A CA 3635 C C . LEU A 473 ? 0.2008 0.2034 0.1736 -0.0116 0.0074 -0.0055 508 LEU A C 3636 O O . LEU A 473 ? 0.2244 0.2268 0.1937 -0.0122 0.0079 -0.0059 508 LEU A O 3637 C CB . LEU A 473 ? 0.2432 0.2490 0.2201 -0.0105 0.0071 -0.0014 508 LEU A CB 3638 C CG . LEU A 473 ? 0.2698 0.2780 0.2475 -0.0101 0.0063 0.0014 508 LEU A CG 3639 C CD1 . LEU A 473 ? 0.2849 0.2920 0.2636 -0.0085 0.0085 0.0031 508 LEU A CD1 3640 C CD2 . LEU A 473 ? 0.2830 0.2934 0.2576 -0.0111 0.0048 0.0025 508 LEU A CD2 3641 N N . TYR A 474 ? 0.1888 0.1902 0.1637 -0.0105 0.0083 -0.0067 509 TYR A N 3642 C CA . TYR A 474 ? 0.1840 0.1841 0.1579 -0.0097 0.0102 -0.0086 509 TYR A CA 3643 C C . TYR A 474 ? 0.1837 0.1805 0.1526 -0.0108 0.0105 -0.0104 509 TYR A C 3644 O O . TYR A 474 ? 0.2043 0.2005 0.1704 -0.0108 0.0123 -0.0114 509 TYR A O 3645 C CB . TYR A 474 ? 0.1832 0.1832 0.1606 -0.0080 0.0107 -0.0090 509 TYR A CB 3646 C CG . TYR A 474 ? 0.1732 0.1724 0.1509 -0.0063 0.0129 -0.0104 509 TYR A CG 3647 C CD1 . TYR A 474 ? 0.1857 0.1879 0.1651 -0.0055 0.0147 -0.0105 509 TYR A CD1 3648 C CD2 . TYR A 474 ? 0.1722 0.1671 0.1483 -0.0053 0.0135 -0.0115 509 TYR A CD2 3649 C CE1 . TYR A 474 ? 0.1709 0.1732 0.1514 -0.0035 0.0172 -0.0116 509 TYR A CE1 3650 C CE2 . TYR A 474 ? 0.1731 0.1668 0.1498 -0.0029 0.0161 -0.0126 509 TYR A CE2 3651 C CZ . TYR A 474 ? 0.1804 0.1783 0.1596 -0.0018 0.0180 -0.0126 509 TYR A CZ 3652 O OH . TYR A 474 ? 0.1751 0.1723 0.1555 0.0009 0.0210 -0.0134 509 TYR A OH 3653 N N . ASN A 475 ? 0.1735 0.1679 0.1407 -0.0121 0.0091 -0.0109 510 ASN A N 3654 C CA . ASN A 475 ? 0.1907 0.1813 0.1521 -0.0142 0.0093 -0.0129 510 ASN A CA 3655 C C . ASN A 475 ? 0.1984 0.1913 0.1557 -0.0162 0.0085 -0.0124 510 ASN A C 3656 O O . ASN A 475 ? 0.2066 0.1968 0.1586 -0.0171 0.0099 -0.0143 510 ASN A O 3657 C CB . ASN A 475 ? 0.1948 0.1830 0.1548 -0.0165 0.0075 -0.0133 510 ASN A CB 3658 C CG . ASN A 475 ? 0.2014 0.1848 0.1628 -0.0149 0.0089 -0.0143 510 ASN A CG 3659 O OD1 . ASN A 475 ? 0.1995 0.1801 0.1611 -0.0124 0.0115 -0.0154 510 ASN A OD1 3660 N ND2 . ASN A 475 ? 0.1944 0.1773 0.1572 -0.0163 0.0073 -0.0134 510 ASN A ND2 3661 N N . VAL A 476 ? 0.1911 0.1887 0.1506 -0.0164 0.0065 -0.0096 511 VAL A N 3662 C CA . VAL A 476 ? 0.2135 0.2139 0.1695 -0.0178 0.0054 -0.0081 511 VAL A CA 3663 C C . VAL A 476 ? 0.2082 0.2082 0.1628 -0.0165 0.0079 -0.0082 511 VAL A C 3664 O O . VAL A 476 ? 0.2399 0.2394 0.1887 -0.0179 0.0083 -0.0086 511 VAL A O 3665 C CB . VAL A 476 ? 0.2173 0.2229 0.1772 -0.0174 0.0032 -0.0045 511 VAL A CB 3666 C CG1 . VAL A 476 ? 0.2382 0.2470 0.1950 -0.0178 0.0024 -0.0020 511 VAL A CG1 3667 C CG2 . VAL A 476 ? 0.2383 0.2456 0.2000 -0.0191 0.0008 -0.0041 511 VAL A CG2 3668 N N . MET A 477 ? 0.1992 0.1996 0.1585 -0.0142 0.0097 -0.0077 512 MET A N 3669 C CA . MET A 477 ? 0.2100 0.2103 0.1685 -0.0133 0.0123 -0.0078 512 MET A CA 3670 C C . MET A 477 ? 0.2225 0.2199 0.1776 -0.0134 0.0148 -0.0108 512 MET A C 3671 O O . MET A 477 ? 0.2176 0.2146 0.1687 -0.0139 0.0167 -0.0111 512 MET A O 3672 C CB . MET A 477 ? 0.2108 0.2126 0.1749 -0.0118 0.0135 -0.0069 512 MET A CB 3673 C CG . MET A 477 ? 0.2261 0.2293 0.1924 -0.0115 0.0122 -0.0041 512 MET A CG 3674 S SD . MET A 477 ? 0.2481 0.2517 0.2189 -0.0108 0.0140 -0.0036 512 MET A SD 3675 C CE . MET A 477 ? 0.2539 0.2582 0.2289 -0.0102 0.0131 -0.0054 512 MET A CE 3676 N N . CYS A 478 ? 0.2107 0.2054 0.1666 -0.0129 0.0152 -0.0129 513 CYS A N 3677 C CA . CYS A 478 ? 0.2223 0.2131 0.1745 -0.0125 0.0180 -0.0158 513 CYS A CA 3678 C C . CYS A 478 ? 0.2344 0.2224 0.1780 -0.0155 0.0176 -0.0171 513 CYS A C 3679 O O . CYS A 478 ? 0.2527 0.2388 0.1914 -0.0159 0.0203 -0.0186 513 CYS A O 3680 C CB . CYS A 478 ? 0.2273 0.2146 0.1818 -0.0110 0.0187 -0.0173 513 CYS A CB 3681 S SG . CYS A 478 ? 0.2260 0.2174 0.1896 -0.0073 0.0198 -0.0160 513 CYS A SG 3682 N N . ASP A 479 ? 0.2328 0.2211 0.1744 -0.0180 0.0141 -0.0165 514 ASP A N 3683 C CA . ASP A 479 ? 0.2625 0.2496 0.1957 -0.0217 0.0128 -0.0174 514 ASP A CA 3684 C C . ASP A 479 ? 0.2529 0.2432 0.1830 -0.0220 0.0130 -0.0155 514 ASP A C 3685 O O . ASP A 479 ? 0.2625 0.2502 0.1845 -0.0241 0.0143 -0.0172 514 ASP A O 3686 C CB . ASP A 479 ? 0.2882 0.2779 0.2216 -0.0245 0.0084 -0.0160 514 ASP A CB 3687 C CG . ASP A 479 ? 0.3272 0.3123 0.2611 -0.0255 0.0083 -0.0183 514 ASP A CG 3688 O OD1 . ASP A 479 ? 0.3491 0.3278 0.2812 -0.0245 0.0116 -0.0213 514 ASP A OD1 3689 O OD2 . ASP A 479 ? 0.3588 0.3469 0.2953 -0.0272 0.0052 -0.0168 514 ASP A OD2 3690 N N . LEU A 480 ? 0.2474 0.2421 0.1829 -0.0202 0.0122 -0.0120 515 LEU A N 3691 C CA . LEU A 480 ? 0.2621 0.2593 0.1949 -0.0202 0.0124 -0.0094 515 LEU A CA 3692 C C . LEU A 480 ? 0.2793 0.2740 0.2094 -0.0195 0.0168 -0.0112 515 LEU A C 3693 O O . LEU A 480 ? 0.2758 0.2711 0.2008 -0.0204 0.0176 -0.0097 515 LEU A O 3694 C CB . LEU A 480 ? 0.2722 0.2730 0.2114 -0.0182 0.0115 -0.0056 515 LEU A CB 3695 C CG . LEU A 480 ? 0.2972 0.3018 0.2389 -0.0184 0.0076 -0.0027 515 LEU A CG 3696 C CD1 . LEU A 480 ? 0.3067 0.3128 0.2552 -0.0158 0.0081 0.0000 515 LEU A CD1 3697 C CD2 . LEU A 480 ? 0.3152 0.3229 0.2513 -0.0203 0.0051 -0.0001 515 LEU A CD2 3698 N N . LEU A 481 ? 0.2519 0.2443 0.1854 -0.0178 0.0198 -0.0139 516 LEU A N 3699 C CA . LEU A 481 ? 0.2419 0.2331 0.1745 -0.0167 0.0244 -0.0155 516 LEU A CA 3700 C C . LEU A 481 ? 0.2655 0.2515 0.1929 -0.0169 0.0274 -0.0194 516 LEU A C 3701 O O . LEU A 481 ? 0.2600 0.2450 0.1868 -0.0156 0.0318 -0.0209 516 LEU A O 3702 C CB . LEU A 481 ? 0.2399 0.2339 0.1817 -0.0140 0.0260 -0.0147 516 LEU A CB 3703 C CG . LEU A 481 ? 0.2381 0.2357 0.1838 -0.0140 0.0246 -0.0113 516 LEU A CG 3704 C CD1 . LEU A 481 ? 0.2350 0.2353 0.1893 -0.0123 0.0252 -0.0111 516 LEU A CD1 3705 C CD2 . LEU A 481 ? 0.2478 0.2456 0.1894 -0.0150 0.0271 -0.0101 516 LEU A CD2 3706 N N . GLY A 482 ? 0.2562 0.2387 0.1795 -0.0188 0.0253 -0.0212 517 GLY A N 3707 C CA . GLY A 482 ? 0.2696 0.2453 0.1868 -0.0194 0.0282 -0.0253 517 GLY A CA 3708 C C . GLY A 482 ? 0.2686 0.2421 0.1922 -0.0155 0.0314 -0.0267 517 GLY A C 3709 O O . GLY A 482 ? 0.2817 0.2500 0.2020 -0.0143 0.0359 -0.0296 517 GLY A O 3710 N N . LEU A 483 ? 0.2504 0.2278 0.1831 -0.0135 0.0292 -0.0244 518 LEU A N 3711 C CA . LEU A 483 ? 0.2583 0.2353 0.1979 -0.0096 0.0315 -0.0248 518 LEU A CA 3712 C C . LEU A 483 ? 0.2670 0.2389 0.2064 -0.0096 0.0300 -0.0258 518 LEU A C 3713 O O . LEU A 483 ? 0.2671 0.2393 0.2052 -0.0124 0.0260 -0.0249 518 LEU A O 3714 C CB . LEU A 483 ? 0.2463 0.2309 0.1953 -0.0077 0.0300 -0.0217 518 LEU A CB 3715 C CG . LEU A 483 ? 0.2484 0.2381 0.1990 -0.0077 0.0316 -0.0203 518 LEU A CG 3716 C CD1 . LEU A 483 ? 0.2339 0.2298 0.1926 -0.0071 0.0294 -0.0175 518 LEU A CD1 3717 C CD2 . LEU A 483 ? 0.2599 0.2492 0.2110 -0.0054 0.0369 -0.0220 518 LEU A CD2 3718 N N . LYS A 484 ? 0.2739 0.2413 0.2149 -0.0064 0.0335 -0.0272 519 LYS A N 3719 C CA . LYS A 484 ? 0.2874 0.2502 0.2298 -0.0056 0.0325 -0.0274 519 LYS A CA 3720 C C . LYS A 484 ? 0.2700 0.2397 0.2221 -0.0031 0.0298 -0.0239 519 LYS A C 3721 O O . LYS A 484 ? 0.2461 0.2207 0.2049 0.0004 0.0316 -0.0225 519 LYS A O 3722 C CB . LYS A 484 ? 0.3408 0.2952 0.2808 -0.0025 0.0378 -0.0298 519 LYS A CB 3723 C CG . LYS A 484 ? 0.4014 0.3486 0.3406 -0.0023 0.0372 -0.0301 519 LYS A CG 3724 C CD . LYS A 484 ? 0.4717 0.4106 0.4103 0.0021 0.0428 -0.0315 519 LYS A CD 3725 C CE . LYS A 484 ? 0.5194 0.4516 0.4583 0.0027 0.0422 -0.0309 519 LYS A CE 3726 N NZ . LYS A 484 ? 0.6458 0.5673 0.5821 0.0070 0.0483 -0.0325 519 LYS A NZ 3727 N N . PRO A 485 ? 0.2499 0.2208 0.2030 -0.0054 0.0256 -0.0225 520 PRO A N 3728 C CA . PRO A 485 ? 0.2389 0.2154 0.2000 -0.0034 0.0233 -0.0196 520 PRO A CA 3729 C C . PRO A 485 ? 0.2409 0.2152 0.2062 0.0006 0.0251 -0.0189 520 PRO A C 3730 O O . PRO A 485 ? 0.2500 0.2161 0.2113 0.0010 0.0270 -0.0205 520 PRO A O 3731 C CB . PRO A 485 ? 0.2461 0.2228 0.2061 -0.0067 0.0192 -0.0186 520 PRO A CB 3732 C CG . PRO A 485 ? 0.2578 0.2306 0.2100 -0.0107 0.0188 -0.0207 520 PRO A CG 3733 C CD . PRO A 485 ? 0.2638 0.2309 0.2107 -0.0099 0.0229 -0.0236 520 PRO A CD 3734 N N . ALA A 486 ? 0.2204 0.2016 0.1931 0.0033 0.0245 -0.0164 521 ALA A N 3735 C CA . ALA A 486 ? 0.2230 0.2039 0.2003 0.0072 0.0251 -0.0147 521 ALA A CA 3736 C C . ALA A 486 ? 0.2372 0.2147 0.2131 0.0054 0.0221 -0.0138 521 ALA A C 3737 O O . ALA A 486 ? 0.2263 0.2050 0.2003 0.0017 0.0193 -0.0139 521 ALA A O 3738 C CB . ALA A 486 ? 0.2195 0.2104 0.2048 0.0094 0.0243 -0.0121 521 ALA A CB 3739 N N . PRO A 487 ? 0.2348 0.2080 0.2118 0.0083 0.0230 -0.0126 522 PRO A N 3740 C CA . PRO A 487 ? 0.2404 0.2100 0.2158 0.0064 0.0206 -0.0116 522 PRO A CA 3741 C C . PRO A 487 ? 0.2177 0.1949 0.1966 0.0045 0.0167 -0.0096 522 PRO A C 3742 O O . PRO A 487 ? 0.2106 0.1951 0.1947 0.0064 0.0159 -0.0077 522 PRO A O 3743 C CB . PRO A 487 ? 0.2583 0.2237 0.2356 0.0109 0.0225 -0.0097 522 PRO A CB 3744 C CG . PRO A 487 ? 0.2684 0.2312 0.2457 0.0146 0.0269 -0.0110 522 PRO A CG 3745 C CD . PRO A 487 ? 0.2521 0.2242 0.2324 0.0138 0.0264 -0.0115 522 PRO A CD 3746 N N . ASN A 488 ? 0.1992 0.1749 0.1752 0.0006 0.0146 -0.0100 523 ASN A N 3747 C CA . ASN A 488 ? 0.1891 0.1714 0.1680 -0.0009 0.0117 -0.0084 523 ASN A CA 3748 C C . ASN A 488 ? 0.1994 0.1792 0.1764 -0.0038 0.0099 -0.0079 523 ASN A C 3749 O O . ASN A 488 ? 0.2011 0.1742 0.1746 -0.0049 0.0107 -0.0088 523 ASN A O 3750 C CB . ASN A 488 ? 0.1827 0.1701 0.1620 -0.0024 0.0114 -0.0092 523 ASN A CB 3751 C CG . ASN A 488 ? 0.1872 0.1719 0.1617 -0.0056 0.0111 -0.0109 523 ASN A CG 3752 O OD1 . ASN A 488 ? 0.1983 0.1847 0.1724 -0.0081 0.0091 -0.0102 523 ASN A OD1 3753 N ND2 . ASN A 488 ? 0.1925 0.1735 0.1635 -0.0056 0.0132 -0.0130 523 ASN A ND2 3754 N N . ASN A 489 ? 0.1926 0.1775 0.1717 -0.0051 0.0080 -0.0066 524 ASN A N 3755 C CA . ASN A 489 ? 0.1944 0.1781 0.1726 -0.0074 0.0066 -0.0057 524 ASN A CA 3756 C C . ASN A 489 ? 0.2011 0.1861 0.1778 -0.0108 0.0056 -0.0064 524 ASN A C 3757 O O . ASN A 489 ? 0.1912 0.1763 0.1680 -0.0129 0.0047 -0.0055 524 ASN A O 3758 C CB . ASN A 489 ? 0.1832 0.1709 0.1642 -0.0067 0.0056 -0.0036 524 ASN A CB 3759 C CG . ASN A 489 ? 0.1909 0.1784 0.1734 -0.0036 0.0059 -0.0022 524 ASN A CG 3760 O OD1 . ASN A 489 ? 0.1920 0.1848 0.1770 -0.0025 0.0053 -0.0014 524 ASN A OD1 3761 N ND2 . ASN A 489 ? 0.1932 0.1748 0.1740 -0.0024 0.0069 -0.0018 524 ASN A ND2 3762 N N . GLY A 490 ? 0.1894 0.1761 0.1651 -0.0113 0.0058 -0.0076 525 GLY A N 3763 C CA . GLY A 490 ? 0.2003 0.1881 0.1739 -0.0145 0.0047 -0.0081 525 GLY A CA 3764 C C . GLY A 490 ? 0.2111 0.1933 0.1807 -0.0172 0.0048 -0.0096 525 GLY A C 3765 O O . GLY A 490 ? 0.2383 0.2140 0.2060 -0.0162 0.0065 -0.0106 525 GLY A O 3766 N N . THR A 491 ? 0.2154 0.2001 0.1837 -0.0208 0.0031 -0.0096 526 THR A N 3767 C CA . THR A 491 ? 0.2213 0.2014 0.1850 -0.0249 0.0029 -0.0114 526 THR A CA 3768 C C . THR A 491 ? 0.2310 0.2128 0.1909 -0.0269 0.0022 -0.0129 526 THR A C 3769 O O . THR A 491 ? 0.2098 0.1987 0.1709 -0.0286 0.0000 -0.0114 526 THR A O 3770 C CB . THR A 491 ? 0.2353 0.2188 0.2013 -0.0281 0.0011 -0.0098 526 THR A CB 3771 O OG1 . THR A 491 ? 0.2171 0.1981 0.1856 -0.0261 0.0022 -0.0085 526 THR A OG1 3772 C CG2 . THR A 491 ? 0.2307 0.2105 0.1919 -0.0336 0.0006 -0.0117 526 THR A CG2 3773 N N . HIS A 492 ? 0.2182 0.1938 0.1734 -0.0261 0.0044 -0.0155 527 HIS A N 3774 C CA . HIS A 492 ? 0.2295 0.2063 0.1804 -0.0274 0.0044 -0.0169 527 HIS A CA 3775 C C . HIS A 492 ? 0.2304 0.2081 0.1765 -0.0334 0.0020 -0.0179 527 HIS A C 3776 O O . HIS A 492 ? 0.2303 0.2017 0.1722 -0.0369 0.0026 -0.0201 527 HIS A O 3777 C CB . HIS A 492 ? 0.2415 0.2105 0.1882 -0.0254 0.0079 -0.0197 527 HIS A CB 3778 C CG . HIS A 492 ? 0.2606 0.2315 0.2042 -0.0251 0.0087 -0.0206 527 HIS A CG 3779 N ND1 . HIS A 492 ? 0.2881 0.2534 0.2282 -0.0230 0.0124 -0.0230 527 HIS A ND1 3780 C CD2 . HIS A 492 ? 0.2694 0.2471 0.2126 -0.0263 0.0065 -0.0192 527 HIS A CD2 3781 C CE1 . HIS A 492 ? 0.2964 0.2648 0.2338 -0.0235 0.0125 -0.0232 527 HIS A CE1 3782 N NE2 . HIS A 492 ? 0.2825 0.2583 0.2216 -0.0254 0.0088 -0.0208 527 HIS A NE2 3783 N N . GLY A 493 ? 0.2245 0.2102 0.1711 -0.0347 -0.0005 -0.0161 528 GLY A N 3784 C CA . GLY A 493 ? 0.2258 0.2159 0.1696 -0.0403 -0.0036 -0.0160 528 GLY A CA 3785 C C . GLY A 493 ? 0.2251 0.2252 0.1763 -0.0402 -0.0065 -0.0119 528 GLY A C 3786 O O . GLY A 493 ? 0.2500 0.2575 0.2010 -0.0436 -0.0096 -0.0104 528 GLY A O 3787 N N . SER A 494 ? 0.2106 0.2112 0.1683 -0.0365 -0.0054 -0.0101 529 SER A N 3788 C CA . SER A 494 ? 0.2103 0.2198 0.1749 -0.0361 -0.0073 -0.0063 529 SER A CA 3789 C C . SER A 494 ? 0.2179 0.2353 0.1852 -0.0336 -0.0085 -0.0031 529 SER A C 3790 O O . SER A 494 ? 0.2090 0.2345 0.1814 -0.0336 -0.0102 0.0001 529 SER A O 3791 C CB . SER A 494 ? 0.2021 0.2097 0.1718 -0.0329 -0.0055 -0.0053 529 SER A CB 3792 O OG . SER A 494 ? 0.2087 0.2149 0.1801 -0.0280 -0.0036 -0.0048 529 SER A OG 3793 N N . LEU A 495 ? 0.2040 0.2189 0.1684 -0.0312 -0.0073 -0.0038 530 LEU A N 3794 C CA . LEU A 495 ? 0.2220 0.2429 0.1879 -0.0289 -0.0081 -0.0007 530 LEU A CA 3795 C C . LEU A 495 ? 0.2285 0.2504 0.1877 -0.0315 -0.0096 -0.0014 530 LEU A C 3796 O O . LEU A 495 ? 0.2618 0.2866 0.2206 -0.0294 -0.0096 0.0009 530 LEU A O 3797 C CB . LEU A 495 ? 0.2234 0.2412 0.1916 -0.0240 -0.0052 -0.0003 530 LEU A CB 3798 C CG . LEU A 495 ? 0.2083 0.2261 0.1826 -0.0212 -0.0038 0.0008 530 LEU A CG 3799 C CD1 . LEU A 495 ? 0.2302 0.2459 0.2057 -0.0175 -0.0015 0.0014 530 LEU A CD1 3800 C CD2 . LEU A 495 ? 0.2178 0.2428 0.1970 -0.0213 -0.0054 0.0043 530 LEU A CD2 3801 N N . ASN A 496 ? 0.2404 0.2597 0.1938 -0.0365 -0.0107 -0.0043 531 ASN A N 3802 C CA . ASN A 496 ? 0.2660 0.2866 0.2119 -0.0399 -0.0124 -0.0051 531 ASN A CA 3803 C C . ASN A 496 ? 0.2566 0.2885 0.2048 -0.0403 -0.0161 -0.0003 531 ASN A C 3804 O O . ASN A 496 ? 0.2574 0.2914 0.2009 -0.0406 -0.0170 0.0007 531 ASN A O 3805 C CB . ASN A 496 ? 0.2842 0.2993 0.2226 -0.0460 -0.0128 -0.0095 531 ASN A CB 3806 C CG . ASN A 496 ? 0.3042 0.3073 0.2370 -0.0451 -0.0086 -0.0142 531 ASN A CG 3807 O OD1 . ASN A 496 ? 0.3145 0.3141 0.2501 -0.0400 -0.0056 -0.0142 531 ASN A OD1 3808 N ND2 . ASN A 496 ? 0.3603 0.3569 0.2851 -0.0502 -0.0082 -0.0182 531 ASN A ND2 3809 N N . HIS A 497 ? 0.2534 0.2930 0.2092 -0.0400 -0.0179 0.0029 532 HIS A N 3810 C CA . HIS A 497 ? 0.2563 0.3079 0.2162 -0.0394 -0.0212 0.0083 532 HIS A CA 3811 C C . HIS A 497 ? 0.2543 0.3074 0.2170 -0.0332 -0.0197 0.0124 532 HIS A C 3812 O O . HIS A 497 ? 0.2619 0.3242 0.2278 -0.0318 -0.0219 0.0174 532 HIS A O 3813 C CB . HIS A 497 ? 0.2710 0.3302 0.2390 -0.0404 -0.0228 0.0107 532 HIS A CB 3814 C CG . HIS A 497 ? 0.2557 0.3120 0.2309 -0.0355 -0.0195 0.0115 532 HIS A CG 3815 N ND1 . HIS A 497 ? 0.2687 0.3161 0.2433 -0.0358 -0.0169 0.0076 532 HIS A ND1 3816 C CD2 . HIS A 497 ? 0.2590 0.3199 0.2416 -0.0302 -0.0182 0.0157 532 HIS A CD2 3817 C CE1 . HIS A 497 ? 0.2416 0.2886 0.2225 -0.0313 -0.0145 0.0093 532 HIS A CE1 3818 N NE2 . HIS A 497 ? 0.2332 0.2879 0.2188 -0.0280 -0.0151 0.0140 532 HIS A NE2 3819 N N . LEU A 498 ? 0.2305 0.2748 0.1924 -0.0295 -0.0158 0.0104 533 LEU A N 3820 C CA . LEU A 498 ? 0.2393 0.2831 0.2022 -0.0246 -0.0139 0.0134 533 LEU A CA 3821 C C . LEU A 498 ? 0.2502 0.2928 0.2050 -0.0259 -0.0143 0.0132 533 LEU A C 3822 O O . LEU A 498 ? 0.2490 0.2925 0.2037 -0.0226 -0.0135 0.0167 533 LEU A O 3823 C CB . LEU A 498 ? 0.2360 0.2718 0.2011 -0.0211 -0.0097 0.0113 533 LEU A CB 3824 C CG . LEU A 498 ? 0.2360 0.2730 0.2089 -0.0179 -0.0083 0.0131 533 LEU A CG 3825 C CD1 . LEU A 498 ? 0.2613 0.3017 0.2377 -0.0205 -0.0100 0.0125 533 LEU A CD1 3826 C CD2 . LEU A 498 ? 0.2425 0.2717 0.2158 -0.0155 -0.0046 0.0106 533 LEU A CD2 3827 N N . LEU A 499 ? 0.2623 0.3016 0.2097 -0.0307 -0.0152 0.0091 534 LEU A N 3828 C CA . LEU A 499 ? 0.2690 0.3044 0.2077 -0.0318 -0.0142 0.0075 534 LEU A CA 3829 C C . LEU A 499 ? 0.2858 0.3271 0.2178 -0.0366 -0.0183 0.0085 534 LEU A C 3830 O O . LEU A 499 ? 0.2907 0.3351 0.2220 -0.0413 -0.0211 0.0071 534 LEU A O 3831 C CB . LEU A 499 ? 0.2957 0.3209 0.2298 -0.0330 -0.0108 0.0015 534 LEU A CB 3832 C CG . LEU A 499 ? 0.3133 0.3334 0.2538 -0.0288 -0.0072 0.0003 534 LEU A CG 3833 C CD1 . LEU A 499 ? 0.3530 0.3644 0.2894 -0.0297 -0.0041 -0.0049 534 LEU A CD1 3834 C CD2 . LEU A 499 ? 0.3148 0.3354 0.2583 -0.0243 -0.0051 0.0035 534 LEU A CD2 3835 N N . ARG A 500 ? 0.2965 0.3393 0.2234 -0.0359 -0.0186 0.0110 535 ARG A N 3836 C CA . ARG A 500 ? 0.3398 0.3872 0.2578 -0.0408 -0.0222 0.0116 535 ARG A CA 3837 C C . ARG A 500 ? 0.3670 0.4063 0.2751 -0.0463 -0.0209 0.0047 535 ARG A C 3838 O O . ARG A 500 ? 0.3676 0.4100 0.2696 -0.0524 -0.0244 0.0032 535 ARG A O 3839 C CB . ARG A 500 ? 0.3470 0.3961 0.2611 -0.0382 -0.0219 0.0159 535 ARG A CB 3840 C CG . ARG A 500 ? 0.3807 0.4329 0.2834 -0.0434 -0.0251 0.0160 535 ARG A CG 3841 C CD . ARG A 500 ? 0.4171 0.4697 0.3151 -0.0406 -0.0242 0.0202 535 ARG A CD 3842 N NE . ARG A 500 ? 0.4306 0.4910 0.3372 -0.0353 -0.0258 0.0279 535 ARG A NE 3843 C CZ . ARG A 500 ? 0.4206 0.4928 0.3289 -0.0357 -0.0309 0.0339 535 ARG A CZ 3844 N NH1 . ARG A 500 ? 0.4249 0.5042 0.3265 -0.0421 -0.0359 0.0335 535 ARG A NH1 3845 N NH2 . ARG A 500 ? 0.4317 0.5091 0.3486 -0.0296 -0.0309 0.0407 535 ARG A NH2 3846 N N . THR A 501 ? 0.3641 0.3930 0.2699 -0.0442 -0.0159 0.0006 536 THR A N 3847 C CA . THR A 501 ? 0.4596 0.4796 0.3563 -0.0484 -0.0135 -0.0058 536 THR A CA 3848 C C . THR A 501 ? 0.4713 0.4834 0.3734 -0.0458 -0.0095 -0.0095 536 THR A C 3849 O O . THR A 501 ? 0.4677 0.4778 0.3758 -0.0405 -0.0065 -0.0085 536 THR A O 3850 C CB . THR A 501 ? 0.5186 0.5340 0.4053 -0.0489 -0.0109 -0.0072 536 THR A CB 3851 O OG1 . THR A 501 ? 0.5523 0.5671 0.4439 -0.0430 -0.0078 -0.0044 536 THR A OG1 3852 C CG2 . THR A 501 ? 0.5789 0.6013 0.4574 -0.0532 -0.0154 -0.0045 536 THR A CG2 3853 N N . ASN A 502 ? 0.4812 0.4891 0.3809 -0.0498 -0.0098 -0.0136 537 ASN A N 3854 C CA . ASN A 502 ? 0.4815 0.4811 0.3848 -0.0478 -0.0061 -0.0171 537 ASN A CA 3855 C C . ASN A 502 ? 0.5500 0.5387 0.4440 -0.0495 -0.0019 -0.0228 537 ASN A C 3856 O O . ASN A 502 ? 0.5677 0.5538 0.4514 -0.0550 -0.0027 -0.0256 537 ASN A O 3857 C CB . ASN A 502 ? 0.4755 0.4770 0.3830 -0.0506 -0.0087 -0.0173 537 ASN A CB 3858 C CG . ASN A 502 ? 0.4796 0.4897 0.3983 -0.0470 -0.0109 -0.0122 537 ASN A CG 3859 O OD1 . ASN A 502 ? 0.4748 0.4828 0.4005 -0.0420 -0.0084 -0.0115 537 ASN A OD1 3860 N ND2 . ASN A 502 ? 0.4388 0.4591 0.3595 -0.0494 -0.0155 -0.0084 537 ASN A ND2 3861 N N . THR A 503 ? 0.5699 0.5522 0.4674 -0.0448 0.0027 -0.0244 538 THR A N 3862 C CA . THR A 503 ? 0.6396 0.6110 0.5301 -0.0451 0.0077 -0.0296 538 THR A CA 3863 C C . THR A 503 ? 0.5494 0.5137 0.4430 -0.0444 0.0096 -0.0321 538 THR A C 3864 O O . THR A 503 ? 0.5788 0.5331 0.4662 -0.0450 0.0137 -0.0364 538 THR A O 3865 C CB . THR A 503 ? 0.6955 0.6652 0.5870 -0.0401 0.0123 -0.0296 538 THR A CB 3866 O OG1 . THR A 503 ? 0.7926 0.7520 0.6772 -0.0402 0.0176 -0.0345 538 THR A OG1 3867 C CG2 . THR A 503 ? 0.6919 0.6654 0.5956 -0.0341 0.0131 -0.0265 538 THR A CG2 3868 N N . PHE A 504 ? 0.4822 0.4512 0.3849 -0.0430 0.0070 -0.0292 539 PHE A N 3869 C CA . PHE A 504 ? 0.4542 0.4169 0.3592 -0.0429 0.0083 -0.0310 539 PHE A CA 3870 C C . PHE A 504 ? 0.4471 0.4120 0.3504 -0.0491 0.0042 -0.0310 539 PHE A C 3871 O O . PHE A 504 ? 0.4884 0.4634 0.3970 -0.0499 0.0000 -0.0272 539 PHE A O 3872 C CB . PHE A 504 ? 0.4164 0.3822 0.3326 -0.0371 0.0087 -0.0279 539 PHE A CB 3873 C CG . PHE A 504 ? 0.3663 0.3252 0.2844 -0.0365 0.0103 -0.0293 539 PHE A CG 3874 C CD1 . PHE A 504 ? 0.3781 0.3269 0.2932 -0.0340 0.0152 -0.0322 539 PHE A CD1 3875 C CD2 . PHE A 504 ? 0.3464 0.3086 0.2691 -0.0384 0.0073 -0.0274 539 PHE A CD2 3876 C CE1 . PHE A 504 ? 0.3918 0.3333 0.3082 -0.0331 0.0170 -0.0330 539 PHE A CE1 3877 C CE2 . PHE A 504 ? 0.3396 0.2947 0.2633 -0.0380 0.0090 -0.0284 539 PHE A CE2 3878 C CZ . PHE A 504 ? 0.3582 0.3026 0.2785 -0.0353 0.0138 -0.0311 539 PHE A CZ 3879 N N . ARG A 505 ? 0.4323 0.3875 0.3284 -0.0533 0.0060 -0.0351 540 ARG A N 3880 C CA . ARG A 505 ? 0.4522 0.4087 0.3464 -0.0599 0.0026 -0.0356 540 ARG A CA 3881 C C . ARG A 505 ? 0.4153 0.3637 0.3128 -0.0584 0.0051 -0.0365 540 ARG A C 3882 O O . ARG A 505 ? 0.4135 0.3496 0.3061 -0.0572 0.0099 -0.0400 540 ARG A O 3883 C CB . ARG A 505 ? 0.5302 0.4820 0.4115 -0.0676 0.0022 -0.0398 540 ARG A CB 3884 C CG . ARG A 505 ? 0.6227 0.5856 0.5014 -0.0701 -0.0020 -0.0375 540 ARG A CG 3885 C CD . ARG A 505 ? 0.7108 0.6851 0.5915 -0.0763 -0.0083 -0.0349 540 ARG A CD 3886 N NE . ARG A 505 ? 0.7353 0.7193 0.6292 -0.0726 -0.0109 -0.0297 540 ARG A NE 3887 C CZ . ARG A 505 ? 0.7645 0.7616 0.6662 -0.0695 -0.0144 -0.0242 540 ARG A CZ 3888 N NH1 . ARG A 505 ? 0.8331 0.8360 0.7313 -0.0692 -0.0161 -0.0224 540 ARG A NH1 3889 N NH2 . ARG A 505 ? 0.6933 0.6972 0.6062 -0.0665 -0.0157 -0.0204 540 ARG A NH2 3890 N N . PRO A 506 ? 0.3701 0.4297 0.2972 -0.0390 0.0274 -0.0502 541 PRO A N 3891 C CA . PRO A 506 ? 0.3615 0.4115 0.2963 -0.0345 0.0288 -0.0526 541 PRO A CA 3892 C C . PRO A 506 ? 0.3832 0.4271 0.3152 -0.0367 0.0303 -0.0601 541 PRO A C 3893 O O . PRO A 506 ? 0.3776 0.4253 0.3028 -0.0420 0.0284 -0.0620 541 PRO A O 3894 C CB . PRO A 506 ? 0.3481 0.3956 0.2881 -0.0328 0.0237 -0.0451 541 PRO A CB 3895 C CG . PRO A 506 ? 0.3504 0.4045 0.2845 -0.0371 0.0193 -0.0413 541 PRO A CG 3896 C CD . PRO A 506 ? 0.3669 0.4289 0.2930 -0.0406 0.0213 -0.0429 541 PRO A CD 3897 N N . THR A 507 ? 0.3872 0.4217 0.3243 -0.0326 0.0338 -0.0640 542 THR A N 3898 C CA . THR A 507 ? 0.3955 0.4213 0.3301 -0.0345 0.0360 -0.0713 542 THR A CA 3899 C C . THR A 507 ? 0.3751 0.3897 0.3167 -0.0306 0.0352 -0.0693 542 THR A C 3900 O O . THR A 507 ? 0.3606 0.3729 0.3090 -0.0248 0.0357 -0.0656 542 THR A O 3901 C CB . THR A 507 ? 0.4500 0.4733 0.3817 -0.0334 0.0427 -0.0796 542 THR A CB 3902 O OG1 . THR A 507 ? 0.4729 0.4951 0.4122 -0.0262 0.0457 -0.0780 542 THR A OG1 3903 C CG2 . THR A 507 ? 0.4696 0.5041 0.3926 -0.0384 0.0438 -0.0821 542 THR A CG2 3904 N N . MET A 508 ? 0.3630 0.3716 0.3027 -0.0343 0.0338 -0.0717 543 MET A N 3905 C CA . MET A 508 ? 0.4024 0.4003 0.3474 -0.0318 0.0331 -0.0698 543 MET A CA 3906 C C . MET A 508 ? 0.3830 0.3692 0.3308 -0.0264 0.0384 -0.0737 543 MET A C 3907 O O . MET A 508 ? 0.4088 0.3911 0.3522 -0.0275 0.0429 -0.0811 543 MET A O 3908 C CB . MET A 508 ? 0.4341 0.4296 0.3753 -0.0385 0.0312 -0.0726 543 MET A CB 3909 C CG . MET A 508 ? 0.4587 0.4454 0.4041 -0.0381 0.0299 -0.0701 543 MET A CG 3910 S SD . MET A 508 ? 0.4910 0.4795 0.4313 -0.0478 0.0279 -0.0744 543 MET A SD 3911 C CE . MET A 508 ? 0.4840 0.4904 0.4260 -0.0494 0.0213 -0.0673 543 MET A CE 3912 N N . PRO A 509 ? 0.3847 0.3655 0.3395 -0.0204 0.0379 -0.0687 544 PRO A N 3913 C CA . PRO A 509 ? 0.3883 0.3586 0.3464 -0.0140 0.0426 -0.0715 544 PRO A CA 3914 C C . PRO A 509 ? 0.4054 0.3601 0.3597 -0.0161 0.0457 -0.0774 544 PRO A C 3915 O O . PRO A 509 ? 0.3529 0.3039 0.3044 -0.0218 0.0434 -0.0772 544 PRO A O 3916 C CB . PRO A 509 ? 0.3854 0.3552 0.3510 -0.0082 0.0400 -0.0637 544 PRO A CB 3917 C CG . PRO A 509 ? 0.3763 0.3510 0.3416 -0.0125 0.0347 -0.0583 544 PRO A CG 3918 C CD . PRO A 509 ? 0.3593 0.3436 0.3191 -0.0188 0.0333 -0.0605 544 PRO A CD 3919 N N . ASP A 510 ? 0.4212 0.3669 0.3754 -0.0119 0.0513 -0.0829 545 ASP A N 3920 C CA . ASP A 510 ? 0.4461 0.3745 0.3961 -0.0138 0.0549 -0.0889 545 ASP A CA 3921 C C . ASP A 510 ? 0.4023 0.3185 0.3564 -0.0104 0.0535 -0.0832 545 ASP A C 3922 O O . ASP A 510 ? 0.3923 0.3102 0.3532 -0.0031 0.0522 -0.0769 545 ASP A O 3923 C CB . ASP A 510 ? 0.5194 0.4403 0.4682 -0.0093 0.0619 -0.0967 545 ASP A CB 3924 C CG . ASP A 510 ? 0.6023 0.5285 0.5428 -0.0162 0.0647 -0.1055 545 ASP A CG 3925 O OD1 . ASP A 510 ? 0.6258 0.5672 0.5634 -0.0218 0.0609 -0.1039 545 ASP A OD1 3926 O OD2 . ASP A 510 ? 0.7068 0.6215 0.6431 -0.0160 0.0708 -0.1142 545 ASP A OD2 3927 N N . GLU A 511 ? 0.4266 0.3312 0.3761 -0.0165 0.0535 -0.0853 546 GLU A N 3928 C CA . GLU A 511 ? 0.4335 0.3241 0.3852 -0.0140 0.0531 -0.0805 546 GLU A CA 3929 C C . GLU A 511 ? 0.4243 0.3009 0.3786 -0.0048 0.0579 -0.0816 546 GLU A C 3930 O O . GLU A 511 ? 0.4521 0.3219 0.4033 -0.0038 0.0632 -0.0895 546 GLU A O 3931 C CB . GLU A 511 ? 0.4829 0.3631 0.4285 -0.0233 0.0532 -0.0835 546 GLU A CB 3932 C CG . GLU A 511 ? 0.5340 0.3980 0.4806 -0.0211 0.0535 -0.0786 546 GLU A CG 3933 C CD . GLU A 511 ? 0.6134 0.4756 0.5569 -0.0304 0.0511 -0.0772 546 GLU A CD 3934 O OE1 . GLU A 511 ? 0.6554 0.5183 0.5935 -0.0396 0.0520 -0.0838 546 GLU A OE1 3935 O OE2 . GLU A 511 ? 0.5252 0.3852 0.4716 -0.0287 0.0486 -0.0696 546 GLU A OE2 3936 N N . VAL A 512 ? 0.3978 0.2706 0.3577 0.0020 0.0561 -0.0738 547 VAL A N 3937 C CA . VAL A 512 ? 0.4275 0.2889 0.3913 0.0122 0.0597 -0.0730 547 VAL A CA 3938 C C . VAL A 512 ? 0.4343 0.2722 0.3940 0.0116 0.0621 -0.0729 547 VAL A C 3939 O O . VAL A 512 ? 0.4640 0.2867 0.4220 0.0154 0.0675 -0.0781 547 VAL A O 3940 C CB . VAL A 512 ? 0.4102 0.2828 0.3828 0.0208 0.0561 -0.0643 547 VAL A CB 3941 C CG1 . VAL A 512 ? 0.4473 0.3079 0.4246 0.0318 0.0591 -0.0622 547 VAL A CG1 3942 C CG2 . VAL A 512 ? 0.4074 0.3009 0.3837 0.0216 0.0551 -0.0654 547 VAL A CG2 3943 N N . SER A 513 ? 0.4424 0.2769 0.4004 0.0069 0.0584 -0.0671 548 SER A N 3944 C CA . SER A 513 ? 0.4753 0.2875 0.4286 0.0051 0.0606 -0.0661 548 SER A CA 3945 C C . SER A 513 ? 0.4926 0.3005 0.4383 -0.0077 0.0613 -0.0717 548 SER A C 3946 O O . SER A 513 ? 0.5188 0.3416 0.4644 -0.0145 0.0573 -0.0705 548 SER A O 3947 C CB . SER A 513 ? 0.4704 0.2817 0.4266 0.0084 0.0564 -0.0553 548 SER A CB 3948 O OG . SER A 513 ? 0.4902 0.3031 0.4531 0.0204 0.0561 -0.0504 548 SER A OG 3949 N N . ARG A 514 ? 0.5276 0.3151 0.4670 -0.0109 0.0664 -0.0779 549 ARG A N 3950 C CA . ARG A 514 ? 0.5597 0.3422 0.4916 -0.0240 0.0673 -0.0836 549 ARG A CA 3951 C C . ARG A 514 ? 0.5389 0.3067 0.4680 -0.0279 0.0668 -0.0778 549 ARG A C 3952 O O . ARG A 514 ? 0.5564 0.3059 0.4853 -0.0211 0.0691 -0.0736 549 ARG A O 3953 C CB . ARG A 514 ? 0.6197 0.3882 0.5451 -0.0272 0.0737 -0.0949 549 ARG A CB 3954 C CG . ARG A 514 ? 0.6632 0.4477 0.5893 -0.0265 0.0745 -0.1020 549 ARG A CG 3955 C CD . ARG A 514 ? 0.7208 0.5248 0.6443 -0.0378 0.0704 -0.1047 549 ARG A CD 3956 N NE . ARG A 514 ? 0.7760 0.5698 0.6906 -0.0500 0.0732 -0.1133 549 ARG A NE 3957 C CZ . ARG A 514 ? 0.8522 0.6556 0.7614 -0.0586 0.0736 -0.1218 549 ARG A CZ 3958 N NH1 . ARG A 514 ? 0.8595 0.6829 0.7705 -0.0567 0.0715 -0.1231 549 ARG A NH1 3959 N NH2 . ARG A 514 ? 0.9084 0.7013 0.8097 -0.0701 0.0761 -0.1292 549 ARG A NH2 3960 N N . PRO A 515 ? 0.5224 0.2981 0.4492 -0.0387 0.0640 -0.0773 550 PRO A N 3961 C CA . PRO A 515 ? 0.5242 0.2875 0.4482 -0.0430 0.0637 -0.0714 550 PRO A CA 3962 C C . PRO A 515 ? 0.5492 0.2868 0.4650 -0.0496 0.0693 -0.0766 550 PRO A C 3963 O O . PRO A 515 ? 0.5440 0.2768 0.4552 -0.0553 0.0728 -0.0865 550 PRO A O 3964 C CB . PRO A 515 ? 0.5170 0.2994 0.4419 -0.0529 0.0596 -0.0707 550 PRO A CB 3965 C CG . PRO A 515 ? 0.5138 0.3099 0.4381 -0.0577 0.0594 -0.0794 550 PRO A CG 3966 C CD . PRO A 515 ? 0.5004 0.2957 0.4266 -0.0479 0.0614 -0.0823 550 PRO A CD 3967 N N . ASN A 516 ? 0.5496 0.2708 0.4628 -0.0497 0.0701 -0.0698 551 ASN A N 3968 C CA . ASN A 516 ? 0.5881 0.2860 0.4928 -0.0590 0.0747 -0.0732 551 ASN A CA 3969 C C . ASN A 516 ? 0.5582 0.2681 0.4611 -0.0731 0.0725 -0.0738 551 ASN A C 3970 O O . ASN A 516 ? 0.5204 0.2523 0.4289 -0.0732 0.0674 -0.0688 551 ASN A O 3971 C CB . ASN A 516 ? 0.6398 0.3146 0.5422 -0.0525 0.0764 -0.0645 551 ASN A CB 3972 C CG . ASN A 516 ? 0.6827 0.3484 0.5887 -0.0369 0.0779 -0.0625 551 ASN A CG 3973 O OD1 . ASN A 516 ? 0.7110 0.3658 0.6153 -0.0343 0.0826 -0.0705 551 ASN A OD1 3974 N ND2 . ASN A 516 ? 0.7100 0.3818 0.6214 -0.0267 0.0741 -0.0520 551 ASN A ND2 3975 N N . TYR A 517 ? 0.5573 0.2533 0.4528 -0.0852 0.0764 -0.0804 552 TYR A N 3976 C CA . TYR A 517 ? 0.5497 0.2568 0.4438 -0.0993 0.0748 -0.0813 552 TYR A CA 3977 C C . TYR A 517 ? 0.5704 0.2518 0.4567 -0.1069 0.0791 -0.0793 552 TYR A C 3978 O O . TYR A 517 ? 0.5787 0.2477 0.4583 -0.1178 0.0832 -0.0874 552 TYR A O 3979 C CB . TYR A 517 ? 0.5617 0.2813 0.4544 -0.1092 0.0750 -0.0925 552 TYR A CB 3980 C CG . TYR A 517 ? 0.5567 0.3020 0.4559 -0.1033 0.0707 -0.0943 552 TYR A CG 3981 C CD1 . TYR A 517 ? 0.5791 0.3209 0.4788 -0.0936 0.0723 -0.0979 552 TYR A CD1 3982 C CD2 . TYR A 517 ? 0.5339 0.3069 0.4387 -0.1077 0.0654 -0.0926 552 TYR A CD2 3983 C CE1 . TYR A 517 ? 0.5724 0.3374 0.4773 -0.0890 0.0686 -0.0992 552 TYR A CE1 3984 C CE2 . TYR A 517 ? 0.5401 0.3352 0.4502 -0.1025 0.0615 -0.0936 552 TYR A CE2 3985 C CZ . TYR A 517 ? 0.5605 0.3514 0.4701 -0.0937 0.0631 -0.0969 552 TYR A CZ 3986 O OH . TYR A 517 ? 0.5713 0.3840 0.4854 -0.0895 0.0594 -0.0975 552 TYR A OH 3987 N N . PRO A 518 ? 0.5723 0.2454 0.4588 -0.1017 0.0783 -0.0685 553 PRO A N 3988 C CA . PRO A 518 ? 0.6067 0.2520 0.4847 -0.1078 0.0828 -0.0655 553 PRO A CA 3989 C C . PRO A 518 ? 0.6252 0.2758 0.4998 -0.1248 0.0835 -0.0673 553 PRO A C 3990 O O . PRO A 518 ? 0.6222 0.2983 0.5026 -0.1283 0.0794 -0.0647 553 PRO A O 3991 C CB . PRO A 518 ? 0.6053 0.2461 0.4851 -0.0965 0.0805 -0.0526 553 PRO A CB 3992 C CG . PRO A 518 ? 0.5677 0.2402 0.4568 -0.0917 0.0743 -0.0491 553 PRO A CG 3993 C CD . PRO A 518 ? 0.5549 0.2430 0.4485 -0.0905 0.0733 -0.0586 553 PRO A CD 3994 N N . GLY A 519 ? 0.6857 0.3120 0.5513 -0.1353 0.0891 -0.0719 554 GLY A N 3995 C CA . GLY A 519 ? 0.7284 0.3572 0.5901 -0.1526 0.0906 -0.0737 554 GLY A CA 3996 C C . GLY A 519 ? 0.7764 0.3916 0.6338 -0.1540 0.0917 -0.0627 554 GLY A C 3997 O O . GLY A 519 ? 0.7641 0.3656 0.6207 -0.1415 0.0913 -0.0537 554 GLY A O 3998 N N . ILE A 520 ? 0.8130 0.4335 0.6679 -0.1696 0.0930 -0.0633 555 ILE A N 3999 C CA . ILE A 520 ? 0.8441 0.4502 0.6930 -0.1747 0.0953 -0.0541 555 ILE A CA 4000 C C . ILE A 520 ? 0.8837 0.4487 0.7210 -0.1758 0.1014 -0.0536 555 ILE A C 4001 O O . ILE A 520 ? 0.9044 0.4549 0.7348 -0.1895 0.1062 -0.0612 555 ILE A O 4002 C CB . ILE A 520 ? 0.8567 0.4799 0.7061 -0.1926 0.0960 -0.0564 555 ILE A CB 4003 C CG1 . ILE A 520 ? 0.8410 0.5031 0.7022 -0.1892 0.0901 -0.0545 555 ILE A CG1 4004 C CG2 . ILE A 520 ? 0.8693 0.4717 0.7096 -0.2008 0.1001 -0.0484 555 ILE A CG2 4005 C CD1 . ILE A 520 ? 0.8436 0.5281 0.7081 -0.2050 0.0903 -0.0577 555 ILE A CD1 4006 N N . MET A 521 ? 0.9132 0.4599 0.7484 -0.1611 0.1012 -0.0447 556 MET A N 4007 C CA . MET A 521 ? 1.0037 0.5104 0.8290 -0.1583 0.1067 -0.0433 556 MET A CA 4008 C C . MET A 521 ? 1.0226 0.5076 0.8404 -0.1559 0.1079 -0.0296 556 MET A C 4009 O O . MET A 521 ? 1.0409 0.4922 0.8479 -0.1614 0.1135 -0.0287 556 MET A O 4010 C CB . MET A 521 ? 1.0597 0.5587 0.8886 -0.1420 0.1064 -0.0466 556 MET A CB 4011 C CG . MET A 521 ? 1.0771 0.5934 0.9150 -0.1239 0.1005 -0.0382 556 MET A CG 4012 S SD . MET A 521 ? 1.2528 0.7627 1.0956 -0.1070 0.1011 -0.0443 556 MET A SD 4013 C CE . MET A 521 ? 1.1427 0.6962 0.9992 -0.0985 0.0933 -0.0440 556 MET A CE 4014 N N . TYR A 522 ? 0.9930 0.4960 0.8155 -0.1481 0.1028 -0.0191 557 TYR A N 4015 C CA . TYR A 522 ? 1.0138 0.4985 0.8287 -0.1451 0.1032 -0.0052 557 TYR A CA 4016 C C . TYR A 522 ? 1.0069 0.4963 0.8162 -0.1619 0.1049 -0.0016 557 TYR A C 4017 O O . TYR A 522 ? 0.9953 0.5105 0.8098 -0.1731 0.1042 -0.0083 557 TYR A O 4018 C CB . TYR A 522 ? 0.9982 0.4983 0.8197 -0.1281 0.0969 0.0046 557 TYR A CB 4019 C CG . TYR A 522 ? 1.0118 0.5098 0.8399 -0.1106 0.0950 0.0025 557 TYR A CG 4020 C CD1 . TYR A 522 ? 1.0331 0.4999 0.8562 -0.1000 0.0975 0.0072 557 TYR A CD1 4021 C CD2 . TYR A 522 ? 0.9837 0.5116 0.8233 -0.1044 0.0907 -0.0036 557 TYR A CD2 4022 C CE1 . TYR A 522 ? 1.0317 0.4985 0.8618 -0.0837 0.0961 0.0051 557 TYR A CE1 4023 C CE2 . TYR A 522 ? 0.9824 0.5099 0.8282 -0.0892 0.0892 -0.0056 557 TYR A CE2 4024 C CZ . TYR A 522 ? 1.0151 0.5129 0.8565 -0.0788 0.0920 -0.0014 557 TYR A CZ 4025 O OH . TYR A 522 ? 1.0279 0.5274 0.8764 -0.0635 0.0909 -0.0037 557 TYR A OH 4026 N N . LEU A 523 ? 1.0253 0.4895 0.8239 -0.1634 0.1075 0.0090 558 LEU A N 4027 C CA . LEU A 523 ? 1.0173 0.4847 0.8096 -0.1782 0.1094 0.0145 558 LEU A CA 4028 C C . LEU A 523 ? 0.9745 0.4582 0.7686 -0.1691 0.1043 0.0267 558 LEU A C 4029 O O . LEU A 523 ? 0.9244 0.4024 0.7198 -0.1525 0.1007 0.0340 558 LEU A O 4030 C CB . LEU A 523 ? 1.0663 0.4935 0.8436 -0.1874 0.1160 0.0188 558 LEU A CB 4031 C CG . LEU A 523 ? 1.0996 0.5019 0.8714 -0.1976 0.1222 0.0077 558 LEU A CG 4032 C CD1 . LEU A 523 ? 1.1294 0.4892 0.8856 -0.2041 0.1283 0.0151 558 LEU A CD1 4033 C CD2 . LEU A 523 ? 1.0915 0.5167 0.8676 -0.2159 0.1238 -0.0047 558 LEU A CD2 4034 N N . GLN A 524 ? 0.9917 0.4962 0.7859 -0.1804 0.1042 0.0287 559 GLN A N 4035 C CA . GLN A 524 ? 0.9954 0.5138 0.7888 -0.1752 0.1005 0.0401 559 GLN A CA 4036 C C . GLN A 524 ? 0.9961 0.4866 0.7791 -0.1653 0.1000 0.0540 559 GLN A C 4037 O O . GLN A 524 ? 0.9676 0.4681 0.7535 -0.1517 0.0947 0.0617 559 GLN A O 4038 C CB . GLN A 524 ? 1.0314 0.5644 0.8217 -0.1923 0.1033 0.0408 559 GLN A CB 4039 C CG . GLN A 524 ? 1.0401 0.6110 0.8430 -0.1982 0.1017 0.0307 559 GLN A CG 4040 C CD . GLN A 524 ? 1.0465 0.6461 0.8590 -0.1852 0.0954 0.0331 559 GLN A CD 4041 O OE1 . GLN A 524 ? 1.0835 0.7008 0.9071 -0.1776 0.0918 0.0258 559 GLN A OE1 4042 N NE2 . GLN A 524 ? 1.0708 0.6748 0.8785 -0.1832 0.0941 0.0434 559 GLN A NE2 4043 N N . SER A 525 ? 1.0085 0.4640 0.7794 -0.1722 0.1054 0.0573 560 SER A N 4044 C CA . SER A 525 ? 1.0239 0.4494 0.7834 -0.1641 0.1055 0.0714 560 SER A CA 4045 C C . SER A 525 ? 1.0144 0.4333 0.7787 -0.1422 0.1006 0.0762 560 SER A C 4046 O O . SER A 525 ? 1.0205 0.4274 0.7785 -0.1329 0.0981 0.0895 560 SER A O 4047 C CB . SER A 525 ? 1.0644 0.4508 0.8107 -0.1756 0.1128 0.0719 560 SER A CB 4048 O OG . SER A 525 ? 1.0617 0.4421 0.8121 -0.1815 0.1166 0.0576 560 SER A OG 4049 N N . GLU A 526 ? 1.0122 0.4409 0.7878 -0.1341 0.0991 0.0656 561 GLU A N 4050 C CA . GLU A 526 ? 1.0442 0.4697 0.8260 -0.1136 0.0949 0.0688 561 GLU A CA 4051 C C . GLU A 526 ? 0.9966 0.4529 0.7864 -0.1020 0.0872 0.0750 561 GLU A C 4052 O O . GLU A 526 ? 1.0022 0.4562 0.7961 -0.0853 0.0833 0.0805 561 GLU A O 4053 C CB . GLU A 526 ? 1.0719 0.4976 0.8624 -0.1098 0.0966 0.0548 561 GLU A CB 4054 C CG . GLU A 526 ? 1.1411 0.5351 0.9236 -0.1202 0.1042 0.0475 561 GLU A CG 4055 C CD . GLU A 526 ? 1.1593 0.5550 0.9496 -0.1166 0.1058 0.0332 561 GLU A CD 4056 O OE1 . GLU A 526 ? 1.1752 0.5679 0.9714 -0.0995 0.1037 0.0340 561 GLU A OE1 4057 O OE2 . GLU A 526 ? 1.1350 0.5361 0.9255 -0.1310 0.1092 0.0214 561 GLU A OE2 4058 N N . PHE A 527 ? 0.9504 0.4352 0.7427 -0.1107 0.0853 0.0740 562 PHE A N 4059 C CA . PHE A 527 ? 0.9174 0.4328 0.7177 -0.1013 0.0785 0.0775 562 PHE A CA 4060 C C . PHE A 527 ? 0.9364 0.4512 0.7275 -0.1006 0.0760 0.0919 562 PHE A C 4061 O O . PHE A 527 ? 0.9222 0.4308 0.7036 -0.1138 0.0794 0.0957 562 PHE A O 4062 C CB . PHE A 527 ? 0.8648 0.4132 0.6743 -0.1097 0.0779 0.0670 562 PHE A CB 4063 C CG . PHE A 527 ? 0.8371 0.3920 0.6565 -0.1087 0.0788 0.0535 562 PHE A CG 4064 C CD1 . PHE A 527 ? 0.8296 0.3728 0.6464 -0.1214 0.0844 0.0444 562 PHE A CD1 4065 C CD2 . PHE A 527 ? 0.7914 0.3652 0.6221 -0.0960 0.0741 0.0497 562 PHE A CD2 4066 C CE1 . PHE A 527 ? 0.8200 0.3702 0.6449 -0.1210 0.0850 0.0320 562 PHE A CE1 4067 C CE2 . PHE A 527 ? 0.7736 0.3538 0.6124 -0.0956 0.0750 0.0377 562 PHE A CE2 4068 C CZ . PHE A 527 ? 0.7891 0.3577 0.6248 -0.1079 0.0804 0.0288 562 PHE A CZ 4069 N N . ASP A 528 ? 0.9531 0.4755 0.7474 -0.0856 0.0699 0.0997 563 ASP A N 4070 C CA . ASP A 528 ? 0.9711 0.4956 0.7570 -0.0830 0.0663 0.1136 563 ASP A CA 4071 C C . ASP A 528 ? 0.9329 0.4908 0.7282 -0.0749 0.0596 0.1131 563 ASP A C 4072 O O . ASP A 528 ? 0.9344 0.4949 0.7306 -0.0620 0.0542 0.1215 563 ASP A O 4073 C CB . ASP A 528 ? 1.0202 0.5148 0.7985 -0.0719 0.0653 0.1258 563 ASP A CB 4074 C CG . ASP A 528 ? 1.0533 0.5414 0.8181 -0.0739 0.0633 0.1412 563 ASP A CG 4075 O OD1 . ASP A 528 ? 1.0457 0.5589 0.8103 -0.0757 0.0595 0.1442 563 ASP A OD1 4076 O OD2 . ASP A 528 ? 1.1047 0.5615 0.8582 -0.0737 0.0658 0.1505 563 ASP A OD2 4077 N N . LEU A 529 ? 0.8995 0.4831 0.7021 -0.0827 0.0602 0.1030 564 LEU A N 4078 C CA . LEU A 529 ? 0.8597 0.4748 0.6721 -0.0764 0.0548 0.1000 564 LEU A CA 4079 C C . LEU A 529 ? 0.8346 0.4663 0.6410 -0.0807 0.0525 0.1067 564 LEU A C 4080 O O . LEU A 529 ? 0.8100 0.4660 0.6231 -0.0758 0.0481 0.1049 564 LEU A O 4081 C CB . LEU A 529 ? 0.8308 0.4650 0.6548 -0.0813 0.0564 0.0856 564 LEU A CB 4082 C CG . LEU A 529 ? 0.8442 0.4655 0.6737 -0.0802 0.0595 0.0764 564 LEU A CG 4083 C CD1 . LEU A 529 ? 0.7942 0.4382 0.6340 -0.0860 0.0603 0.0635 564 LEU A CD1 4084 C CD2 . LEU A 529 ? 0.8598 0.4720 0.6940 -0.0641 0.0564 0.0788 564 LEU A CD2 4085 N N . GLY A 530 ? 0.8394 0.4579 0.6327 -0.0905 0.0557 0.1141 565 GLY A N 4086 C CA . GLY A 530 ? 0.8389 0.4729 0.6251 -0.0968 0.0547 0.1194 565 GLY A CA 4087 C C . GLY A 530 ? 0.8216 0.4817 0.6142 -0.1065 0.0571 0.1091 565 GLY A C 4088 O O . GLY A 530 ? 0.8015 0.4792 0.5911 -0.1093 0.0558 0.1114 565 GLY A O 4089 N N . CYS A 531 ? 0.8295 0.4920 0.6307 -0.1117 0.0607 0.0978 566 CYS A N 4090 C CA . CYS A 531 ? 0.8539 0.5413 0.6630 -0.1200 0.0629 0.0875 566 CYS A CA 4091 C C . CYS A 531 ? 0.8783 0.5621 0.6802 -0.1363 0.0694 0.0869 566 CYS A C 4092 O O . CYS A 531 ? 0.9197 0.5790 0.7126 -0.1424 0.0730 0.0911 566 CYS A O 4093 C CB . CYS A 531 ? 0.8581 0.5527 0.6807 -0.1170 0.0627 0.0758 566 CYS A CB 4094 S SG . CYS A 531 ? 0.8632 0.5639 0.6957 -0.0990 0.0559 0.0749 566 CYS A SG 4095 N N . THR A 532 ? 0.8854 0.5937 0.6917 -0.1433 0.0710 0.0814 567 THR A N 4096 C CA . THR A 532 ? 0.9427 0.6535 0.7433 -0.1588 0.0773 0.0807 567 THR A CA 4097 C C . THR A 532 ? 0.9427 0.6804 0.7561 -0.1643 0.0793 0.0689 567 THR A C 4098 O O . THR A 532 ? 0.9243 0.6822 0.7475 -0.1561 0.0756 0.0642 567 THR A O 4099 C CB . THR A 532 ? 0.9612 0.6738 0.7492 -0.1620 0.0777 0.0905 567 THR A CB 4100 O OG1 . THR A 532 ? 1.0240 0.7433 0.8080 -0.1773 0.0842 0.0886 567 THR A OG1 4101 C CG2 . THR A 532 ? 0.9388 0.6738 0.7310 -0.1530 0.0729 0.0904 567 THR A CG2 4102 N N . CYS A 533 ? 0.9264 0.6644 0.7400 -0.1779 0.0850 0.0643 568 CYS A N 4103 C CA . CYS A 533 ? 0.9280 0.6926 0.7540 -0.1838 0.0872 0.0537 568 CYS A CA 4104 C C . CYS A 533 ? 0.9726 0.7475 0.7938 -0.1976 0.0931 0.0546 568 CYS A C 4105 O O . CYS A 533 ? 1.0002 0.7572 0.8085 -0.2063 0.0969 0.0616 568 CYS A O 4106 C CB . CYS A 533 ? 0.9437 0.7043 0.7776 -0.1873 0.0881 0.0451 568 CYS A CB 4107 S SG . CYS A 533 ? 0.9426 0.7378 0.7945 -0.1901 0.0882 0.0322 568 CYS A SG 4108 N N . LYS A 536 ? 1.4164 1.1241 1.1671 -0.2479 0.1149 0.0939 571 LYS A N 4109 C CA . LYS A 536 ? 1.3977 1.1200 1.1419 -0.2607 0.1209 0.0957 571 LYS A CA 4110 C C . LYS A 536 ? 1.3637 1.1058 1.1193 -0.2739 0.1270 0.0845 571 LYS A C 4111 O O . LYS A 536 ? 1.2947 1.0365 1.0433 -0.2895 0.1339 0.0861 571 LYS A O 4112 C CB . LYS A 536 ? 1.3705 1.1154 1.1154 -0.2525 0.1181 0.0967 571 LYS A CB 4113 C CG . LYS A 536 ? 1.3771 1.1091 1.1151 -0.2373 0.1105 0.1054 571 LYS A CG 4114 C CD . LYS A 536 ? 1.4222 1.1237 1.1403 -0.2401 0.1107 0.1198 571 LYS A CD 4115 C CE . LYS A 536 ? 1.4371 1.1127 1.1544 -0.2275 0.1046 0.1251 571 LYS A CE 4116 N NZ . LYS A 536 ? 1.4369 1.1223 1.1599 -0.2105 0.0966 0.1258 571 LYS A NZ 4117 N N . VAL A 537 ? 1.3372 1.0978 1.1106 -0.2674 0.1241 0.0735 572 VAL A N 4118 C CA . VAL A 537 ? 1.3225 1.1000 1.1088 -0.2779 0.1281 0.0625 572 VAL A CA 4119 C C . VAL A 537 ? 1.3130 1.0736 1.1044 -0.2768 0.1259 0.0578 572 VAL A C 4120 O O . VAL A 537 ? 1.3642 1.1262 1.1593 -0.2898 0.1301 0.0519 572 VAL A O 4121 C CB . VAL A 537 ? 1.2745 1.0902 1.0780 -0.2732 0.1275 0.0529 572 VAL A CB 4122 C CG1 . VAL A 537 ? 1.2746 1.1072 1.0728 -0.2770 0.1315 0.0561 572 VAL A CG1 4123 C CG2 . VAL A 537 ? 1.2241 1.0453 1.0374 -0.2551 0.1197 0.0498 572 VAL A CG2 4124 N N . GLU A 538 ? 1.2637 1.0092 1.0551 -0.2618 0.1194 0.0601 573 GLU A N 4125 C CA . GLU A 538 ? 1.2290 0.9595 1.0255 -0.2582 0.1168 0.0550 573 GLU A CA 4126 C C . GLU A 538 ? 1.1584 0.9159 0.9729 -0.2600 0.1163 0.0419 573 GLU A C 4127 O O . GLU A 538 ? 1.1153 0.8712 0.9323 -0.2722 0.1199 0.0358 573 GLU A O 4128 C CB . GLU A 538 ? 1.2820 0.9793 1.0656 -0.2693 0.1212 0.0592 573 GLU A CB 4129 C CG . GLU A 538 ? 1.3170 0.9856 1.0829 -0.2656 0.1208 0.0731 573 GLU A CG 4130 C CD . GLU A 538 ? 1.3693 1.0018 1.1222 -0.2754 0.1251 0.0777 573 GLU A CD 4131 O OE1 . GLU A 538 ? 1.3733 0.9913 1.1300 -0.2744 0.1246 0.0718 573 GLU A OE1 4132 O OE2 . GLU A 538 ? 1.4007 1.0185 1.1389 -0.2843 0.1291 0.0872 573 GLU A OE2 4133 N N . PRO A 539 ? 1.0399 0.8221 0.8665 -0.2479 0.1117 0.0377 574 PRO A N 4134 C CA . PRO A 539 ? 0.9803 0.7884 0.8238 -0.2480 0.1105 0.0264 574 PRO A CA 4135 C C . PRO A 539 ? 0.9417 0.7360 0.7889 -0.2441 0.1073 0.0212 574 PRO A C 4136 O O . PRO A 539 ? 0.8717 0.6486 0.7153 -0.2319 0.1030 0.0248 574 PRO A O 4137 C CB . PRO A 539 ? 0.9601 0.7912 0.8124 -0.2343 0.1062 0.0254 574 PRO A CB 4138 C CG . PRO A 539 ? 0.9666 0.7856 0.8063 -0.2288 0.1056 0.0356 574 PRO A CG 4139 C CD . PRO A 539 ? 1.0182 0.8029 0.8430 -0.2330 0.1068 0.0432 574 PRO A CD 4140 N N . LYS A 540 ? 0.9041 0.7071 0.7583 -0.2549 0.1095 0.0128 575 LYS A N 4141 C CA . LYS A 540 ? 0.9056 0.6968 0.7626 -0.2536 0.1073 0.0067 575 LYS A CA 4142 C C . LYS A 540 ? 0.8937 0.7082 0.7628 -0.2637 0.1082 -0.0039 575 LYS A C 4143 O O . LYS A 540 ? 0.8738 0.7034 0.7452 -0.2772 0.1128 -0.0060 575 LYS A O 4144 C CB . LYS A 540 ? 0.9437 0.6966 0.7856 -0.2594 0.1103 0.0114 575 LYS A CB 4145 C CG . LYS A 540 ? 0.9514 0.6956 0.7843 -0.2782 0.1174 0.0136 575 LYS A CG 4146 C CD . LYS A 540 ? 0.9595 0.7019 0.7950 -0.2927 0.1204 0.0044 575 LYS A CD 4147 C CE . LYS A 540 ? 0.9984 0.7211 0.8212 -0.3110 0.1276 0.0079 575 LYS A CE 4148 N NZ . LYS A 540 ? 0.9885 0.7373 0.8149 -0.3228 0.1319 0.0082 575 LYS A NZ 4149 N N . ASN A 541 ? 0.8842 0.7028 0.7610 -0.2569 0.1038 -0.0106 576 ASN A N 4150 C CA . ASN A 541 ? 0.8549 0.6919 0.7416 -0.2661 0.1039 -0.0206 576 ASN A CA 4151 C C . ASN A 541 ? 0.8764 0.6863 0.7530 -0.2789 0.1076 -0.0231 576 ASN A C 4152 O O . ASN A 541 ? 0.8390 0.6293 0.7120 -0.2739 0.1057 -0.0256 576 ASN A O 4153 C CB . ASN A 541 ? 0.8642 0.7167 0.7622 -0.2534 0.0974 -0.0262 576 ASN A CB 4154 C CG . ASN A 541 ? 0.8675 0.7422 0.7760 -0.2623 0.0966 -0.0362 576 ASN A CG 4155 O OD1 . ASN A 541 ? 0.8635 0.7455 0.7725 -0.2782 0.1007 -0.0394 576 ASN A OD1 4156 N ND2 . ASN A 541 ? 0.8708 0.7571 0.7876 -0.2526 0.0912 -0.0409 576 ASN A ND2 4157 N N . LYS A 542 ? 0.8812 0.6897 0.7529 -0.2956 0.1136 -0.0224 577 LYS A N 4158 C CA . LYS A 542 ? 0.9055 0.6904 0.7676 -0.3114 0.1183 -0.0253 577 LYS A CA 4159 C C . LYS A 542 ? 0.8681 0.6569 0.7360 -0.3152 0.1160 -0.0364 577 LYS A C 4160 O O . LYS A 542 ? 0.8269 0.5871 0.6852 -0.3209 0.1182 -0.0390 577 LYS A O 4161 C CB . LYS A 542 ? 0.9543 0.7503 0.8151 -0.3298 0.1245 -0.0246 577 LYS A CB 4162 C CG . LYS A 542 ? 1.0027 0.7794 0.8547 -0.3494 0.1301 -0.0285 577 LYS A CG 4163 C CD . LYS A 542 ? 1.0463 0.7762 0.8807 -0.3485 0.1325 -0.0226 577 LYS A CD 4164 C CE . LYS A 542 ? 1.0800 0.7913 0.9052 -0.3700 0.1389 -0.0264 577 LYS A CE 4165 N NZ . LYS A 542 ? 1.1295 0.7942 0.9392 -0.3687 0.1410 -0.0235 577 LYS A NZ 4166 N N . LEU A 543 ? 0.8197 0.6439 0.7028 -0.3117 0.1118 -0.0428 578 LEU A N 4167 C CA . LEU A 543 ? 0.8002 0.6344 0.6900 -0.3141 0.1086 -0.0529 578 LEU A CA 4168 C C . LEU A 543 ? 0.7733 0.5828 0.6575 -0.3022 0.1054 -0.0544 578 LEU A C 4169 O O . LEU A 543 ? 0.7356 0.5398 0.6187 -0.3086 0.1052 -0.0627 578 LEU A O 4170 C CB . LEU A 543 ? 0.8065 0.6836 0.7139 -0.3088 0.1038 -0.0570 578 LEU A CB 4171 C CG . LEU A 543 ? 0.8217 0.7206 0.7384 -0.3154 0.1007 -0.0673 578 LEU A CG 4172 C CD1 . LEU A 543 ? 0.8312 0.7325 0.7457 -0.3378 0.1055 -0.0729 578 LEU A CD1 4173 C CD2 . LEU A 543 ? 0.8034 0.7424 0.7370 -0.3063 0.0957 -0.0683 578 LEU A CD2 4174 N N . GLU A 544 ? 0.7327 0.5283 0.6134 -0.2855 0.1032 -0.0468 579 GLU A N 4175 C CA . GLU A 544 ? 0.7435 0.5167 0.6197 -0.2729 0.1005 -0.0476 579 GLU A CA 4176 C C . GLU A 544 ? 0.7445 0.4812 0.6075 -0.2817 0.1051 -0.0502 579 GLU A C 4177 O O . GLU A 544 ? 0.7280 0.4536 0.5896 -0.2778 0.1038 -0.0563 579 GLU A O 4178 C CB . GLU A 544 ? 0.7436 0.5068 0.6173 -0.2552 0.0980 -0.0378 579 GLU A CB 4179 C CG . GLU A 544 ? 0.7679 0.5628 0.6542 -0.2433 0.0928 -0.0367 579 GLU A CG 4180 C CD . GLU A 544 ? 0.7801 0.5659 0.6641 -0.2261 0.0898 -0.0282 579 GLU A CD 4181 O OE1 . GLU A 544 ? 0.8130 0.5696 0.6879 -0.2200 0.0904 -0.0244 579 GLU A OE1 4182 O OE2 . GLU A 544 ? 0.7575 0.5660 0.6492 -0.2187 0.0870 -0.0254 579 GLU A OE2 4183 N N . GLU A 545 ? 0.7632 0.4812 0.6162 -0.2937 0.1108 -0.0458 580 GLU A N 4184 C CA . GLU A 545 ? 0.7892 0.4703 0.6287 -0.3035 0.1161 -0.0477 580 GLU A CA 4185 C C . GLU A 545 ? 0.7619 0.4491 0.6032 -0.3183 0.1174 -0.0605 580 GLU A C 4186 O O . GLU A 545 ? 0.8131 0.4708 0.6448 -0.3229 0.1205 -0.0650 580 GLU A O 4187 C CB . GLU A 545 ? 0.8516 0.5150 0.6805 -0.3149 0.1220 -0.0397 580 GLU A CB 4188 C CG . GLU A 545 ? 0.8788 0.5308 0.7026 -0.3016 0.1211 -0.0266 580 GLU A CG 4189 C CD . GLU A 545 ? 0.9405 0.5933 0.7584 -0.3131 0.1256 -0.0189 580 GLU A CD 4190 O OE1 . GLU A 545 ? 0.9397 0.5785 0.7496 -0.3310 0.1314 -0.0208 580 GLU A OE1 4191 O OE2 . GLU A 545 ? 0.9762 0.6437 0.7969 -0.3047 0.1235 -0.0112 580 GLU A OE2 4192 N N . PHE A 546 ? 0.6957 0.4210 0.5492 -0.3259 0.1151 -0.0662 581 PHE A N 4193 C CA . PHE A 546 ? 0.6670 0.4052 0.5238 -0.3401 0.1151 -0.0784 581 PHE A CA 4194 C C . PHE A 546 ? 0.6470 0.4028 0.5125 -0.3290 0.1089 -0.0853 581 PHE A C 4195 O O . PHE A 546 ? 0.6455 0.4087 0.5121 -0.3389 0.1083 -0.0955 581 PHE A O 4196 C CB . PHE A 546 ? 0.6453 0.4183 0.5116 -0.3548 0.1158 -0.0806 581 PHE A CB 4197 C CG . PHE A 546 ? 0.6631 0.4231 0.5213 -0.3688 0.1225 -0.0750 581 PHE A CG 4198 C CD1 . PHE A 546 ? 0.6897 0.4134 0.5330 -0.3821 0.1286 -0.0764 581 PHE A CD1 4199 C CD2 . PHE A 546 ? 0.6442 0.4278 0.5093 -0.3691 0.1231 -0.0685 581 PHE A CD2 4200 C CE1 . PHE A 546 ? 0.7139 0.4245 0.5489 -0.3956 0.1350 -0.0708 581 PHE A CE1 4201 C CE2 . PHE A 546 ? 0.6632 0.4353 0.5201 -0.3827 0.1296 -0.0633 581 PHE A CE2 4202 C CZ . PHE A 546 ? 0.7078 0.4434 0.5495 -0.3962 0.1354 -0.0641 581 PHE A CZ 4203 N N . ASN A 547 ? 0.6185 0.3809 0.4894 -0.3094 0.1042 -0.0798 582 ASN A N 4204 C CA . ASN A 547 ? 0.6090 0.3918 0.4889 -0.2987 0.0980 -0.0852 582 ASN A CA 4205 C C . ASN A 547 ? 0.6221 0.3761 0.4939 -0.2892 0.0981 -0.0877 582 ASN A C 4206 O O . ASN A 547 ? 0.6275 0.3697 0.4983 -0.2727 0.0965 -0.0812 582 ASN A O 4207 C CB . ASN A 547 ? 0.5964 0.4059 0.4878 -0.2840 0.0930 -0.0786 582 ASN A CB 4208 C CG . ASN A 547 ? 0.5875 0.4209 0.4887 -0.2740 0.0865 -0.0835 582 ASN A CG 4209 O OD1 . ASN A 547 ? 0.6281 0.4620 0.5282 -0.2790 0.0855 -0.0922 582 ASN A OD1 4210 N ND2 . ASN A 547 ? 0.5901 0.4429 0.5003 -0.2604 0.0823 -0.0780 582 ASN A ND2 4211 N N . LYS A 548 ? 0.6432 0.3874 0.5096 -0.3000 0.1000 -0.0978 583 LYS A N 4212 C CA . LYS A 548 ? 0.6677 0.3840 0.5260 -0.2927 0.1012 -0.1021 583 LYS A CA 4213 C C . LYS A 548 ? 0.6432 0.3748 0.5089 -0.2753 0.0953 -0.1026 583 LYS A C 4214 O O . LYS A 548 ? 0.6498 0.3588 0.5107 -0.2628 0.0960 -0.1010 583 LYS A O 4215 C CB . LYS A 548 ? 0.7010 0.4069 0.5520 -0.3095 0.1046 -0.1142 583 LYS A CB 4216 C CG . LYS A 548 ? 0.7429 0.4247 0.5836 -0.3266 0.1116 -0.1139 583 LYS A CG 4217 C CD . LYS A 548 ? 0.7861 0.4435 0.6157 -0.3398 0.1163 -0.1252 583 LYS A CD 4218 C CE . LYS A 548 ? 0.8292 0.4613 0.6481 -0.3576 0.1235 -0.1246 583 LYS A CE 4219 N NZ . LYS A 548 ? 0.8457 0.4999 0.6669 -0.3800 0.1241 -0.1333 583 LYS A NZ 4220 N N . ARG A 549 ? 0.6256 0.3954 0.5034 -0.2743 0.0897 -0.1042 584 ARG A N 4221 C CA . ARG A 549 ? 0.6295 0.4163 0.5145 -0.2593 0.0839 -0.1049 584 ARG A CA 4222 C C . ARG A 549 ? 0.5986 0.3947 0.4906 -0.2429 0.0807 -0.0942 584 ARG A C 4223 O O . ARG A 549 ? 0.5857 0.4001 0.4851 -0.2313 0.0756 -0.0937 584 ARG A O 4224 C CB . ARG A 549 ? 0.6436 0.4664 0.5375 -0.2662 0.0792 -0.1120 584 ARG A CB 4225 C CG . ARG A 549 ? 0.6844 0.5055 0.5725 -0.2841 0.0813 -0.1235 584 ARG A CG 4226 C CD . ARG A 549 ? 0.7390 0.5546 0.6224 -0.2813 0.0801 -0.1323 584 ARG A CD 4227 N NE . ARG A 549 ? 0.7740 0.6137 0.6660 -0.2672 0.0736 -0.1307 584 ARG A NE 4228 C CZ . ARG A 549 ? 0.8023 0.6445 0.6918 -0.2642 0.0715 -0.1377 584 ARG A CZ 4229 N NH1 . ARG A 549 ? 0.8223 0.6458 0.7011 -0.2743 0.0754 -0.1477 584 ARG A NH1 4230 N NH2 . ARG A 549 ? 0.8068 0.6705 0.7039 -0.2515 0.0657 -0.1348 584 ARG A NH2 4231 N N . LEU A 550 ? 0.5971 0.3807 0.4862 -0.2425 0.0835 -0.0858 585 LEU A N 4232 C CA . LEU A 550 ? 0.5950 0.3858 0.4892 -0.2280 0.0807 -0.0759 585 LEU A CA 4233 C C . LEU A 550 ? 0.5796 0.3589 0.4729 -0.2110 0.0784 -0.0742 585 LEU A C 4234 O O . LEU A 550 ? 0.5861 0.3372 0.4708 -0.2092 0.0814 -0.0761 585 LEU A O 4235 C CB . LEU A 550 ? 0.6148 0.3873 0.5024 -0.2307 0.0849 -0.0673 585 LEU A CB 4236 C CG . LEU A 550 ? 0.6155 0.3930 0.5063 -0.2175 0.0826 -0.0569 585 LEU A CG 4237 C CD1 . LEU A 550 ? 0.6141 0.4286 0.5173 -0.2163 0.0788 -0.0563 585 LEU A CD1 4238 C CD2 . LEU A 550 ? 0.6455 0.4005 0.5269 -0.2219 0.0872 -0.0489 585 LEU A CD2 4239 N N . HIS A 551 ? 0.5562 0.3578 0.4587 -0.1992 0.0732 -0.0711 586 HIS A N 4240 C CA . HIS A 551 ? 0.5569 0.3527 0.4602 -0.1829 0.0705 -0.0690 586 HIS A CA 4241 C C . HIS A 551 ? 0.5655 0.3563 0.4667 -0.1818 0.0702 -0.0776 586 HIS A C 4242 O O . HIS A 551 ? 0.5727 0.3515 0.4723 -0.1700 0.0698 -0.0765 586 HIS A O 4243 C CB . HIS A 551 ? 0.5802 0.3492 0.4768 -0.1744 0.0729 -0.0606 586 HIS A CB 4244 C CG . HIS A 551 ? 0.5816 0.3566 0.4796 -0.1740 0.0727 -0.0516 586 HIS A CG 4245 N ND1 . HIS A 551 ? 0.6261 0.3773 0.5156 -0.1747 0.0762 -0.0445 586 HIS A ND1 4246 C CD2 . HIS A 551 ? 0.5566 0.3583 0.4627 -0.1734 0.0699 -0.0488 586 HIS A CD2 4247 C CE1 . HIS A 551 ? 0.5939 0.3577 0.4859 -0.1747 0.0754 -0.0378 586 HIS A CE1 4248 N NE2 . HIS A 551 ? 0.5763 0.3704 0.4785 -0.1740 0.0718 -0.0407 586 HIS A NE2 4249 N N . THR A 552 ? 0.5743 0.3753 0.4755 -0.1942 0.0705 -0.0865 587 THR A N 4250 C CA . THR A 552 ? 0.5686 0.3710 0.4684 -0.1934 0.0695 -0.0951 587 THR A CA 4251 C C . THR A 552 ? 0.5461 0.3796 0.4559 -0.1857 0.0632 -0.0945 587 THR A C 4252 O O . THR A 552 ? 0.5297 0.3854 0.4474 -0.1856 0.0602 -0.0900 587 THR A O 4253 C CB . THR A 552 ? 0.5757 0.3773 0.4705 -0.2107 0.0719 -0.1052 587 THR A CB 4254 O OG1 . THR A 552 ? 0.5536 0.3834 0.4556 -0.2208 0.0694 -0.1056 587 THR A OG1 4255 C CG2 . THR A 552 ? 0.6095 0.3773 0.4933 -0.2189 0.0787 -0.1063 587 THR A CG2 4256 N N . LYS A 553 ? 0.5749 0.4095 0.4838 -0.1795 0.0616 -0.0992 588 LYS A N 4257 C CA . LYS A 553 ? 0.5852 0.4477 0.5022 -0.1729 0.0557 -0.0989 588 LYS A CA 4258 C C . LYS A 553 ? 0.5708 0.4626 0.4950 -0.1820 0.0522 -0.1001 588 LYS A C 4259 O O . LYS A 553 ? 0.5744 0.4854 0.5072 -0.1762 0.0486 -0.0940 588 LYS A O 4260 C CB . LYS A 553 ? 0.6241 0.4847 0.5371 -0.1706 0.0554 -0.1063 588 LYS A CB 4261 C CG . LYS A 553 ? 0.6619 0.5489 0.5822 -0.1626 0.0494 -0.1046 588 LYS A CG 4262 C CD . LYS A 553 ? 0.7134 0.6031 0.6293 -0.1633 0.0488 -0.1126 588 LYS A CD 4263 C CE . LYS A 553 ? 0.7344 0.6024 0.6452 -0.1531 0.0521 -0.1133 588 LYS A CE 4264 N NZ . LYS A 553 ? 0.7583 0.6380 0.6684 -0.1488 0.0498 -0.1174 588 LYS A NZ 4265 N N . GLY A 554 ? 0.6120 0.5077 0.5328 -0.1962 0.0532 -0.1083 589 GLY A N 4266 C CA . GLY A 554 ? 0.5971 0.5236 0.5255 -0.2050 0.0493 -0.1101 589 GLY A CA 4267 C C . GLY A 554 ? 0.5701 0.5225 0.5068 -0.1948 0.0429 -0.1073 589 GLY A C 4268 O O . GLY A 554 ? 0.5640 0.5137 0.4974 -0.1885 0.0414 -0.1098 589 GLY A O 4269 N N . SER A 555 ? 0.5783 0.5547 0.5255 -0.1931 0.0395 -0.1021 590 SER A N 4270 C CA . SER A 555 ? 0.5689 0.5688 0.5247 -0.1826 0.0336 -0.0979 590 SER A CA 4271 C C . SER A 555 ? 0.5614 0.5556 0.5209 -0.1680 0.0335 -0.0892 590 SER A C 4272 O O . SER A 555 ? 0.5858 0.5992 0.5533 -0.1599 0.0292 -0.0848 590 SER A O 4273 C CB . SER A 555 ? 0.5553 0.5865 0.5213 -0.1889 0.0300 -0.0977 590 SER A CB 4274 O OG . SER A 555 ? 0.5640 0.5987 0.5363 -0.1882 0.0319 -0.0921 590 SER A OG 4275 N N . THR A 556 ? 0.5478 0.5161 0.5013 -0.1648 0.0379 -0.0866 591 THR A N 4276 C CA . THR A 556 ? 0.5132 0.4754 0.4691 -0.1521 0.0378 -0.0786 591 THR A CA 4277 C C . THR A 556 ? 0.5025 0.4693 0.4599 -0.1402 0.0342 -0.0771 591 THR A C 4278 O O . THR A 556 ? 0.4511 0.4304 0.4151 -0.1315 0.0312 -0.0716 591 THR A O 4279 C CB . THR A 556 ? 0.5212 0.4537 0.4692 -0.1508 0.0427 -0.0762 591 THR A CB 4280 O OG1 . THR A 556 ? 0.5487 0.4768 0.4952 -0.1615 0.0462 -0.0760 591 THR A OG1 4281 C CG2 . THR A 556 ? 0.4935 0.4208 0.4434 -0.1376 0.0420 -0.0682 591 THR A CG2 4282 N N . LYS A 557 ? 0.5138 0.4693 0.4646 -0.1401 0.0350 -0.0822 592 LYS A N 4283 C CA . LYS A 557 ? 0.5400 0.4988 0.4911 -0.1297 0.0323 -0.0812 592 LYS A CA 4284 C C . LYS A 557 ? 0.5389 0.5252 0.4966 -0.1290 0.0267 -0.0809 592 LYS A C 4285 O O . LYS A 557 ? 0.5238 0.5189 0.4861 -0.1191 0.0237 -0.0757 592 LYS A O 4286 C CB . LYS A 557 ? 0.5800 0.5220 0.5223 -0.1310 0.0350 -0.0879 592 LYS A CB 4287 C CG . LYS A 557 ? 0.5891 0.5343 0.5309 -0.1215 0.0330 -0.0877 592 LYS A CG 4288 C CD . LYS A 557 ? 0.5911 0.5188 0.5243 -0.1225 0.0368 -0.0949 592 LYS A CD 4289 C CE . LYS A 557 ? 0.6168 0.5167 0.5456 -0.1198 0.0422 -0.0941 592 LYS A CE 4290 N NZ . LYS A 557 ? 0.5543 0.4490 0.4875 -0.1086 0.0417 -0.0852 592 LYS A NZ 4291 N N . GLU A 558 ? 0.5226 0.5225 0.4808 -0.1397 0.0254 -0.0860 593 GLU A N 4292 C CA . GLU A 558 ? 0.5407 0.5686 0.5058 -0.1400 0.0198 -0.0852 593 GLU A CA 4293 C C . GLU A 558 ? 0.4947 0.5367 0.4700 -0.1325 0.0175 -0.0774 593 GLU A C 4294 O O . GLU A 558 ? 0.4752 0.5296 0.4548 -0.1242 0.0135 -0.0735 593 GLU A O 4295 C CB . GLU A 558 ? 0.6411 0.6813 0.6060 -0.1540 0.0192 -0.0915 593 GLU A CB 4296 C CG . GLU A 558 ? 0.7161 0.7854 0.6867 -0.1555 0.0130 -0.0917 593 GLU A CG 4297 C CD . GLU A 558 ? 0.8321 0.9127 0.8015 -0.1706 0.0126 -0.0988 593 GLU A CD 4298 O OE1 . GLU A 558 ? 0.8834 0.9693 0.8470 -0.1758 0.0104 -0.1045 593 GLU A OE1 4299 O OE2 . GLU A 558 ? 0.8859 0.9699 0.8595 -0.1780 0.0145 -0.0991 593 GLU A OE2 4300 N N . ARG A 559 ? 0.4075 0.4464 0.3859 -0.1356 0.0203 -0.0753 594 ARG A N 4301 C CA . ARG A 559 ? 0.3999 0.4538 0.3881 -0.1303 0.0188 -0.0693 594 ARG A CA 4302 C C . ARG A 559 ? 0.3393 0.3825 0.3279 -0.1181 0.0195 -0.0628 594 ARG A C 4303 O O . ARG A 559 ? 0.3218 0.3780 0.3174 -0.1106 0.0169 -0.0584 594 ARG A O 4304 C CB . ARG A 559 ? 0.4291 0.4860 0.4202 -0.1396 0.0220 -0.0700 594 ARG A CB 4305 C CG . ARG A 559 ? 0.4787 0.5520 0.4718 -0.1520 0.0206 -0.0759 594 ARG A CG 4306 C CD . ARG A 559 ? 0.5302 0.6088 0.5270 -0.1621 0.0239 -0.0767 594 ARG A CD 4307 N NE . ARG A 559 ? 0.5746 0.6265 0.5623 -0.1677 0.0297 -0.0778 594 ARG A NE 4308 C CZ . ARG A 559 ? 0.6000 0.6411 0.5872 -0.1658 0.0335 -0.0732 594 ARG A CZ 4309 N NH1 . ARG A 559 ? 0.5951 0.6495 0.5907 -0.1586 0.0328 -0.0678 594 ARG A NH1 4310 N NH2 . ARG A 559 ? 0.5900 0.6060 0.5679 -0.1714 0.0384 -0.0740 594 ARG A NH2 4311 N N . HIS A 560 ? 0.3447 0.3644 0.3258 -0.1165 0.0230 -0.0626 595 HIS A N 4312 C CA . HIS A 560 ? 0.3557 0.3643 0.3365 -0.1068 0.0240 -0.0568 595 HIS A CA 4313 C C . HIS A 560 ? 0.3572 0.3563 0.3342 -0.0979 0.0229 -0.0556 595 HIS A C 4314 O O . HIS A 560 ? 0.3310 0.3270 0.3096 -0.0893 0.0225 -0.0505 595 HIS A O 4315 C CB . HIS A 560 ? 0.3606 0.3515 0.3368 -0.1109 0.0287 -0.0556 595 HIS A CB 4316 C CG . HIS A 560 ? 0.3832 0.3845 0.3635 -0.1192 0.0303 -0.0558 595 HIS A CG 4317 N ND1 . HIS A 560 ? 0.3738 0.3946 0.3629 -0.1165 0.0287 -0.0529 595 HIS A ND1 4318 C CD2 . HIS A 560 ? 0.3900 0.3856 0.3671 -0.1305 0.0337 -0.0588 595 HIS A CD2 4319 C CE1 . HIS A 560 ? 0.3799 0.4082 0.3717 -0.1255 0.0309 -0.0542 595 HIS A CE1 4320 N NE2 . HIS A 560 ? 0.3977 0.4110 0.3822 -0.1345 0.0340 -0.0577 595 HIS A NE2 4321 N N . LEU A 561 ? 0.3600 0.3556 0.3324 -0.1001 0.0225 -0.0605 596 LEU A N 4322 C CA . LEU A 561 ? 0.3831 0.3733 0.3525 -0.0922 0.0215 -0.0601 596 LEU A CA 4323 C C . LEU A 561 ? 0.3805 0.3883 0.3517 -0.0924 0.0174 -0.0621 596 LEU A C 4324 O O . LEU A 561 ? 0.3847 0.3916 0.3508 -0.0971 0.0175 -0.0677 596 LEU A O 4325 C CB . LEU A 561 ? 0.4349 0.4043 0.3964 -0.0935 0.0252 -0.0643 596 LEU A CB 4326 C CG . LEU A 561 ? 0.4651 0.4143 0.4237 -0.0879 0.0284 -0.0609 596 LEU A CG 4327 C CD1 . LEU A 561 ? 0.5148 0.4465 0.4661 -0.0898 0.0319 -0.0665 596 LEU A CD1 4328 C CD2 . LEU A 561 ? 0.4357 0.3871 0.3974 -0.0770 0.0265 -0.0552 596 LEU A CD2 4329 N N . LEU A 562 ? 0.3197 0.3429 0.2975 -0.0871 0.0139 -0.0573 597 LEU A N 4330 C CA . LEU A 562 ? 0.3162 0.3577 0.2962 -0.0872 0.0095 -0.0577 597 LEU A CA 4331 C C . LEU A 562 ? 0.2977 0.3362 0.2726 -0.0828 0.0084 -0.0585 597 LEU A C 4332 O O . LEU A 562 ? 0.3046 0.3553 0.2781 -0.0855 0.0054 -0.0606 597 LEU A O 4333 C CB . LEU A 562 ? 0.2914 0.3487 0.2801 -0.0819 0.0063 -0.0520 597 LEU A CB 4334 C CG . LEU A 562 ? 0.3033 0.3685 0.2983 -0.0863 0.0073 -0.0515 597 LEU A CG 4335 C CD1 . LEU A 562 ? 0.2820 0.3624 0.2857 -0.0796 0.0045 -0.0462 597 LEU A CD1 4336 C CD2 . LEU A 562 ? 0.3112 0.3863 0.3063 -0.0972 0.0068 -0.0569 597 LEU A CD2 4337 N N . TYR A 563 ? 0.2934 0.3172 0.2656 -0.0765 0.0108 -0.0568 598 TYR A N 4338 C CA . TYR A 563 ? 0.2912 0.3132 0.2597 -0.0714 0.0101 -0.0566 598 TYR A CA 4339 C C . TYR A 563 ? 0.3150 0.3195 0.2771 -0.0719 0.0145 -0.0612 598 TYR A C 4340 O O . TYR A 563 ? 0.3065 0.3061 0.2664 -0.0662 0.0153 -0.0606 598 TYR A O 4341 C CB . TYR A 563 ? 0.2879 0.3117 0.2607 -0.0623 0.0086 -0.0496 598 TYR A CB 4342 C CG . TYR A 563 ? 0.2618 0.2974 0.2416 -0.0611 0.0060 -0.0452 598 TYR A CG 4343 C CD1 . TYR A 563 ? 0.2659 0.3188 0.2487 -0.0625 0.0020 -0.0443 598 TYR A CD1 4344 C CD2 . TYR A 563 ? 0.2556 0.2857 0.2391 -0.0588 0.0077 -0.0421 598 TYR A CD2 4345 C CE1 . TYR A 563 ? 0.2535 0.3177 0.2438 -0.0607 0.0001 -0.0405 598 TYR A CE1 4346 C CE2 . TYR A 563 ? 0.2412 0.2824 0.2313 -0.0578 0.0060 -0.0389 598 TYR A CE2 4347 C CZ . TYR A 563 ? 0.2380 0.2961 0.2320 -0.0583 0.0024 -0.0382 598 TYR A CZ 4348 O OH . TYR A 563 ? 0.2270 0.2960 0.2285 -0.0563 0.0012 -0.0351 598 TYR A OH 4349 N N . GLY A 564 ? 0.3123 0.3075 0.2712 -0.0788 0.0174 -0.0661 599 GLY A N 4350 C CA . GLY A 564 ? 0.3374 0.3142 0.2904 -0.0791 0.0220 -0.0707 599 GLY A CA 4351 C C . GLY A 564 ? 0.3562 0.3176 0.3106 -0.0730 0.0246 -0.0665 599 GLY A C 4352 O O . GLY A 564 ? 0.3307 0.2958 0.2900 -0.0677 0.0229 -0.0601 599 GLY A O 4353 N N . ARG A 565 ? 0.3684 0.3120 0.3180 -0.0737 0.0289 -0.0703 600 ARG A N 4354 C CA . ARG A 565 ? 0.4058 0.3337 0.3558 -0.0681 0.0313 -0.0663 600 ARG A CA 4355 C C . ARG A 565 ? 0.3647 0.2947 0.3175 -0.0579 0.0304 -0.0624 600 ARG A C 4356 O O . ARG A 565 ? 0.3351 0.2685 0.2862 -0.0559 0.0307 -0.0657 600 ARG A O 4357 C CB . ARG A 565 ? 0.4877 0.3957 0.4315 -0.0714 0.0363 -0.0719 600 ARG A CB 4358 C CG . ARG A 565 ? 0.5572 0.4466 0.5004 -0.0667 0.0390 -0.0679 600 ARG A CG 4359 C CD . ARG A 565 ? 0.6127 0.4815 0.5492 -0.0711 0.0441 -0.0740 600 ARG A CD 4360 N NE . ARG A 565 ? 0.6183 0.4838 0.5514 -0.0695 0.0466 -0.0810 600 ARG A NE 4361 C CZ . ARG A 565 ? 0.6263 0.4879 0.5608 -0.0597 0.0479 -0.0802 600 ARG A CZ 4362 N NH1 . ARG A 565 ? 0.6516 0.5126 0.5910 -0.0506 0.0465 -0.0725 600 ARG A NH1 4363 N NH2 . ARG A 565 ? 0.6679 0.5273 0.5989 -0.0594 0.0507 -0.0876 600 ARG A NH2 4364 N N . PRO A 566 ? 0.3464 0.2753 0.3030 -0.0521 0.0292 -0.0555 601 PRO A N 4365 C CA . PRO A 566 ? 0.3395 0.2697 0.2985 -0.0432 0.0286 -0.0523 601 PRO A CA 4366 C C . PRO A 566 ? 0.3653 0.2814 0.3214 -0.0394 0.0326 -0.0558 601 PRO A C 4367 O O . PRO A 566 ? 0.4128 0.3136 0.3658 -0.0414 0.0356 -0.0575 601 PRO A O 4368 C CB . PRO A 566 ? 0.3345 0.2627 0.2967 -0.0392 0.0273 -0.0451 601 PRO A CB 4369 C CG . PRO A 566 ? 0.3378 0.2690 0.3002 -0.0458 0.0265 -0.0443 601 PRO A CG 4370 C CD . PRO A 566 ? 0.3419 0.2683 0.3003 -0.0536 0.0288 -0.0507 601 PRO A CD 4371 N N . ALA A 567 ? 0.3326 0.2535 0.2897 -0.0342 0.0329 -0.0570 602 ALA A N 4372 C CA . ALA A 567 ? 0.3479 0.2571 0.3038 -0.0290 0.0369 -0.0600 602 ALA A CA 4373 C C . ALA A 567 ? 0.3403 0.2447 0.3006 -0.0203 0.0366 -0.0535 602 ALA A C 4374 O O . ALA A 567 ? 0.3279 0.2432 0.2925 -0.0170 0.0333 -0.0480 602 ALA A O 4375 C CB . ALA A 567 ? 0.3519 0.2694 0.3068 -0.0278 0.0381 -0.0648 602 ALA A CB 4376 N N . VAL A 568 ? 0.3313 0.2194 0.2905 -0.0167 0.0401 -0.0542 603 VAL A N 4377 C CA . VAL A 568 ? 0.3390 0.2226 0.3023 -0.0079 0.0398 -0.0481 603 VAL A CA 4378 C C . VAL A 568 ? 0.3391 0.2266 0.3058 -0.0005 0.0419 -0.0507 603 VAL A C 4379 O O . VAL A 568 ? 0.3548 0.2328 0.3191 0.0004 0.0463 -0.0569 603 VAL A O 4380 C CB . VAL A 568 ? 0.3696 0.2332 0.3299 -0.0072 0.0421 -0.0463 603 VAL A CB 4381 C CG1 . VAL A 568 ? 0.3971 0.2570 0.3616 0.0024 0.0412 -0.0392 603 VAL A CG1 4382 C CG2 . VAL A 568 ? 0.3788 0.2406 0.3358 -0.0155 0.0404 -0.0442 603 VAL A CG2 4383 N N . LEU A 569 ? 0.3058 0.2071 0.2780 0.0042 0.0390 -0.0461 604 LEU A N 4384 C CA . LEU A 569 ? 0.3132 0.2229 0.2895 0.0103 0.0407 -0.0482 604 LEU A CA 4385 C C . LEU A 569 ? 0.3370 0.2427 0.3191 0.0203 0.0417 -0.0443 604 LEU A C 4386 O O . LEU A 569 ? 0.3513 0.2676 0.3387 0.0257 0.0422 -0.0443 604 LEU A O 4387 C CB . LEU A 569 ? 0.3064 0.2349 0.2851 0.0083 0.0372 -0.0461 604 LEU A CB 4388 C CG . LEU A 569 ? 0.3083 0.2433 0.2822 -0.0003 0.0357 -0.0490 604 LEU A CG 4389 C CD1 . LEU A 569 ? 0.3063 0.2580 0.2825 -0.0004 0.0334 -0.0472 604 LEU A CD1 4390 C CD2 . LEU A 569 ? 0.3297 0.2581 0.2979 -0.0049 0.0394 -0.0571 604 LEU A CD2 4391 N N . TYR A 570 ? 0.3348 0.2254 0.3157 0.0227 0.0420 -0.0410 605 TYR A N 4392 C CA . TYR A 570 ? 0.3504 0.2355 0.3364 0.0328 0.0429 -0.0371 605 TYR A CA 4393 C C . TYR A 570 ? 0.3687 0.2309 0.3502 0.0340 0.0468 -0.0389 605 TYR A C 4394 O O . TYR A 570 ? 0.3702 0.2225 0.3449 0.0259 0.0482 -0.0426 605 TYR A O 4395 C CB . TYR A 570 ? 0.3376 0.2302 0.3272 0.0355 0.0377 -0.0278 605 TYR A CB 4396 C CG . TYR A 570 ? 0.3413 0.2256 0.3255 0.0299 0.0351 -0.0231 605 TYR A CG 4397 C CD1 . TYR A 570 ? 0.3187 0.2097 0.2994 0.0209 0.0329 -0.0239 605 TYR A CD1 4398 C CD2 . TYR A 570 ? 0.3544 0.2248 0.3374 0.0339 0.0349 -0.0175 605 TYR A CD2 4399 C CE1 . TYR A 570 ? 0.3199 0.2046 0.2963 0.0159 0.0311 -0.0200 605 TYR A CE1 4400 C CE2 . TYR A 570 ? 0.3583 0.2216 0.3358 0.0283 0.0329 -0.0132 605 TYR A CE2 4401 C CZ . TYR A 570 ? 0.3387 0.2098 0.3133 0.0192 0.0312 -0.0147 605 TYR A CZ 4402 O OH . TYR A 570 ? 0.3655 0.2305 0.3352 0.0139 0.0298 -0.0106 605 TYR A OH 4403 N N . ARG A 571 ? 0.3957 0.2497 0.3814 0.0440 0.0486 -0.0362 606 ARG A N 4404 C CA . ARG A 571 ? 0.4250 0.2548 0.4064 0.0462 0.0529 -0.0378 606 ARG A CA 4405 C C . ARG A 571 ? 0.4193 0.2372 0.3969 0.0448 0.0500 -0.0296 606 ARG A C 4406 O O . ARG A 571 ? 0.4207 0.2440 0.4026 0.0509 0.0462 -0.0211 606 ARG A O 4407 C CB . ARG A 571 ? 0.4915 0.3164 0.4791 0.0586 0.0567 -0.0388 606 ARG A CB 4408 C CG . ARG A 571 ? 0.5457 0.3788 0.5352 0.0591 0.0612 -0.0486 606 ARG A CG 4409 C CD . ARG A 571 ? 0.6248 0.4530 0.6211 0.0718 0.0658 -0.0502 606 ARG A CD 4410 N NE . ARG A 571 ? 0.6785 0.5214 0.6849 0.0812 0.0617 -0.0416 606 ARG A NE 4411 C CZ . ARG A 571 ? 0.7641 0.6295 0.7788 0.0851 0.0608 -0.0419 606 ARG A CZ 4412 N NH1 . ARG A 571 ? 0.7776 0.6537 0.7917 0.0808 0.0640 -0.0502 606 ARG A NH1 4413 N NH2 . ARG A 571 ? 0.7972 0.6751 0.8207 0.0929 0.0566 -0.0336 606 ARG A NH2 4414 N N . THR A 572 ? 0.4334 0.2363 0.4028 0.0361 0.0518 -0.0321 607 THR A N 4415 C CA . THR A 572 ? 0.4473 0.2379 0.4118 0.0333 0.0498 -0.0248 607 THR A CA 4416 C C . THR A 572 ? 0.4773 0.2465 0.4330 0.0251 0.0542 -0.0298 607 THR A C 4417 O O . THR A 572 ? 0.4793 0.2445 0.4326 0.0212 0.0583 -0.0392 607 THR A O 4418 C CB . THR A 572 ? 0.4349 0.2425 0.3996 0.0271 0.0442 -0.0198 607 THR A CB 4419 O OG1 . THR A 572 ? 0.4397 0.2381 0.4009 0.0271 0.0420 -0.0111 607 THR A OG1 4420 C CG2 . THR A 572 ? 0.4211 0.2343 0.3815 0.0150 0.0445 -0.0260 607 THR A CG2 4421 N N . SER A 573 ? 0.4813 0.2369 0.4317 0.0219 0.0535 -0.0236 608 SER A N 4422 C CA . SER A 573 ? 0.5140 0.2490 0.4556 0.0128 0.0575 -0.0274 608 SER A CA 4423 C C . SER A 573 ? 0.4902 0.2329 0.4280 0.0015 0.0546 -0.0251 608 SER A C 4424 O O . SER A 573 ? 0.4831 0.2291 0.4209 0.0026 0.0510 -0.0162 608 SER A O 4425 C CB . SER A 573 ? 0.5478 0.2570 0.4856 0.0187 0.0600 -0.0217 608 SER A CB 4426 O OG . SER A 573 ? 0.6395 0.3403 0.5811 0.0294 0.0637 -0.0251 608 SER A OG 4427 N N . TYR A 574 ? 0.4743 0.2204 0.4089 -0.0093 0.0562 -0.0331 609 TYR A N 4428 C CA . TYR A 574 ? 0.4541 0.2097 0.3863 -0.0201 0.0538 -0.0318 609 TYR A CA 4429 C C . TYR A 574 ? 0.4664 0.2137 0.3924 -0.0326 0.0573 -0.0396 609 TYR A C 4430 O O . TYR A 574 ? 0.4833 0.2216 0.4071 -0.0337 0.0612 -0.0478 609 TYR A O 4431 C CB . TYR A 574 ? 0.4324 0.2154 0.3710 -0.0195 0.0490 -0.0312 609 TYR A CB 4432 C CG . TYR A 574 ? 0.4157 0.2120 0.3561 -0.0237 0.0493 -0.0401 609 TYR A CG 4433 C CD1 . TYR A 574 ? 0.4192 0.2178 0.3624 -0.0174 0.0509 -0.0450 609 TYR A CD1 4434 C CD2 . TYR A 574 ? 0.4130 0.2208 0.3523 -0.0341 0.0480 -0.0432 609 TYR A CD2 4435 C CE1 . TYR A 574 ? 0.4146 0.2260 0.3583 -0.0219 0.0511 -0.0526 609 TYR A CE1 4436 C CE2 . TYR A 574 ? 0.4049 0.2258 0.3453 -0.0379 0.0477 -0.0504 609 TYR A CE2 4437 C CZ . TYR A 574 ? 0.4164 0.2388 0.3584 -0.0320 0.0491 -0.0549 609 TYR A CZ 4438 O OH . TYR A 574 ? 0.4182 0.2537 0.3602 -0.0367 0.0487 -0.0616 609 TYR A OH 4439 N N . ASP A 575 ? 0.4668 0.2169 0.3899 -0.0422 0.0563 -0.0373 610 ASP A N 4440 C CA . ASP A 575 ? 0.4806 0.2239 0.3980 -0.0554 0.0593 -0.0436 610 ASP A CA 4441 C C . ASP A 575 ? 0.4624 0.2301 0.3833 -0.0634 0.0561 -0.0461 610 ASP A C 4442 O O . ASP A 575 ? 0.4529 0.2356 0.3779 -0.0613 0.0522 -0.0399 610 ASP A O 4443 C CB . ASP A 575 ? 0.5107 0.2353 0.4214 -0.0610 0.0615 -0.0383 610 ASP A CB 4444 C CG . ASP A 575 ? 0.5541 0.2546 0.4615 -0.0519 0.0638 -0.0327 610 ASP A CG 4445 O OD1 . ASP A 575 ? 0.5749 0.2629 0.4819 -0.0460 0.0668 -0.0372 610 ASP A OD1 4446 O OD2 . ASP A 575 ? 0.5652 0.2591 0.4700 -0.0509 0.0628 -0.0236 610 ASP A OD2 4447 N N . ILE A 576 ? 0.4503 0.2215 0.3692 -0.0728 0.0576 -0.0548 611 ILE A N 4448 C CA . ILE A 576 ? 0.4402 0.2327 0.3619 -0.0819 0.0549 -0.0570 611 ILE A CA 4449 C C . ILE A 576 ? 0.4400 0.2247 0.3574 -0.0927 0.0570 -0.0557 611 ILE A C 4450 O O . ILE A 576 ? 0.4529 0.2175 0.3634 -0.0991 0.0614 -0.0595 611 ILE A O 4451 C CB . ILE A 576 ? 0.4464 0.2487 0.3679 -0.0876 0.0552 -0.0669 611 ILE A CB 4452 C CG1 . ILE A 576 ? 0.4607 0.2715 0.3860 -0.0775 0.0535 -0.0682 611 ILE A CG1 4453 C CG2 . ILE A 576 ? 0.4279 0.2527 0.3529 -0.0969 0.0521 -0.0686 611 ILE A CG2 4454 C CD1 . ILE A 576 ? 0.4334 0.2649 0.3660 -0.0708 0.0485 -0.0621 611 ILE A CD1 4455 N N . LEU A 577 ? 0.4101 0.2106 0.3313 -0.0953 0.0542 -0.0508 612 LEU A N 4456 C CA . LEU A 577 ? 0.4256 0.2226 0.3436 -0.1060 0.0562 -0.0490 612 LEU A CA 4457 C C . LEU A 577 ? 0.4095 0.2320 0.3331 -0.1141 0.0538 -0.0525 612 LEU A C 4458 O O . LEU A 577 ? 0.3810 0.2237 0.3114 -0.1089 0.0499 -0.0498 612 LEU A O 4459 C CB . LEU A 577 ? 0.4322 0.2240 0.3493 -0.1014 0.0557 -0.0390 612 LEU A CB 4460 C CG . LEU A 577 ? 0.4358 0.2055 0.3485 -0.0917 0.0569 -0.0334 612 LEU A CG 4461 C CD1 . LEU A 577 ? 0.4453 0.2150 0.3569 -0.0885 0.0555 -0.0235 612 LEU A CD1 4462 C CD2 . LEU A 577 ? 0.4733 0.2152 0.3777 -0.0964 0.0620 -0.0363 612 LEU A CD2 4463 N N . TYR A 578 ? 0.4153 0.2365 0.3360 -0.1269 0.0563 -0.0583 613 TYR A N 4464 C CA . TYR A 578 ? 0.4158 0.2615 0.3422 -0.1353 0.0542 -0.0619 613 TYR A CA 4465 C C . TYR A 578 ? 0.4224 0.2723 0.3493 -0.1433 0.0557 -0.0578 613 TYR A C 4466 O O . TYR A 578 ? 0.4385 0.2684 0.3585 -0.1483 0.0597 -0.0555 613 TYR A O 4467 C CB . TYR A 578 ? 0.4289 0.2736 0.3521 -0.1458 0.0557 -0.0715 613 TYR A CB 4468 C CG . TYR A 578 ? 0.4398 0.2818 0.3616 -0.1400 0.0549 -0.0769 613 TYR A CG 4469 C CD1 . TYR A 578 ? 0.4369 0.3010 0.3651 -0.1338 0.0502 -0.0776 613 TYR A CD1 4470 C CD2 . TYR A 578 ? 0.4842 0.3012 0.3977 -0.1409 0.0591 -0.0817 613 TYR A CD2 4471 C CE1 . TYR A 578 ? 0.4288 0.2913 0.3551 -0.1293 0.0497 -0.0826 613 TYR A CE1 4472 C CE2 . TYR A 578 ? 0.4795 0.2948 0.3915 -0.1358 0.0590 -0.0873 613 TYR A CE2 4473 C CZ . TYR A 578 ? 0.4599 0.2985 0.3782 -0.1303 0.0543 -0.0877 613 TYR A CZ 4474 O OH . TYR A 578 ? 0.4627 0.3002 0.3788 -0.1260 0.0545 -0.0933 613 TYR A OH 4475 N N . HIS A 579 ? 0.3861 0.2619 0.3213 -0.1441 0.0528 -0.0568 614 HIS A N 4476 C CA . HIS A 579 ? 0.3896 0.2746 0.3269 -0.1527 0.0544 -0.0545 614 HIS A CA 4477 C C . HIS A 579 ? 0.3753 0.2896 0.3218 -0.1572 0.0516 -0.0585 614 HIS A C 4478 O O . HIS A 579 ? 0.3911 0.3191 0.3426 -0.1513 0.0476 -0.0608 614 HIS A O 4479 C CB . HIS A 579 ? 0.3781 0.2635 0.3164 -0.1451 0.0541 -0.0460 614 HIS A CB 4480 C CG . HIS A 579 ? 0.3881 0.2513 0.3201 -0.1353 0.0545 -0.0408 614 HIS A CG 4481 N ND1 . HIS A 579 ? 0.3779 0.2406 0.3118 -0.1239 0.0514 -0.0408 614 HIS A ND1 4482 C CD2 . HIS A 579 ? 0.4098 0.2513 0.3338 -0.1352 0.0574 -0.0352 614 HIS A CD2 4483 C CE1 . HIS A 579 ? 0.3905 0.2336 0.3188 -0.1169 0.0524 -0.0357 614 HIS A CE1 4484 N NE2 . HIS A 579 ? 0.4171 0.2468 0.3393 -0.1232 0.0557 -0.0320 614 HIS A NE2 4485 N N . THR A 580 ? 0.3777 0.3030 0.3271 -0.1671 0.0535 -0.0586 615 THR A N 4486 C CA . THR A 580 ? 0.3696 0.3253 0.3294 -0.1709 0.0509 -0.0615 615 THR A CA 4487 C C . THR A 580 ? 0.3394 0.3134 0.3078 -0.1582 0.0464 -0.0581 615 THR A C 4488 O O . THR A 580 ? 0.3328 0.3265 0.3081 -0.1566 0.0425 -0.0611 615 THR A O 4489 C CB . THR A 580 ? 0.3708 0.3357 0.3331 -0.1814 0.0543 -0.0605 615 THR A CB 4490 O OG1 . THR A 580 ? 0.4195 0.3663 0.3733 -0.1942 0.0586 -0.0637 615 THR A OG1 4491 C CG2 . THR A 580 ? 0.3593 0.3571 0.3336 -0.1853 0.0516 -0.0637 615 THR A CG2 4492 N N . ASP A 581 ? 0.3424 0.3098 0.3099 -0.1495 0.0469 -0.0517 616 ASP A N 4493 C CA . ASP A 581 ? 0.3251 0.3092 0.3004 -0.1388 0.0436 -0.0485 616 ASP A CA 4494 C C . ASP A 581 ? 0.3227 0.2971 0.2956 -0.1264 0.0407 -0.0460 616 ASP A C 4495 O O . ASP A 581 ? 0.2940 0.2809 0.2728 -0.1178 0.0378 -0.0438 616 ASP A O 4496 C CB . ASP A 581 ? 0.3267 0.3143 0.3035 -0.1382 0.0462 -0.0435 616 ASP A CB 4497 C CG . ASP A 581 ? 0.3401 0.3429 0.3217 -0.1492 0.0489 -0.0457 616 ASP A CG 4498 O OD1 . ASP A 581 ? 0.3462 0.3638 0.3332 -0.1559 0.0477 -0.0508 616 ASP A OD1 4499 O OD2 . ASP A 581 ? 0.3456 0.3465 0.3256 -0.1515 0.0525 -0.0422 616 ASP A OD2 4500 N N . PHE A 582 ? 0.3258 0.2780 0.2903 -0.1254 0.0419 -0.0463 617 PHE A N 4501 C CA . PHE A 582 ? 0.3215 0.2652 0.2842 -0.1140 0.0397 -0.0439 617 PHE A CA 4502 C C . PHE A 582 ? 0.3368 0.2594 0.2919 -0.1140 0.0411 -0.0464 617 PHE A C 4503 O O . PHE A 582 ? 0.3478 0.2560 0.2970 -0.1224 0.0446 -0.0487 617 PHE A O 4504 C CB . PHE A 582 ? 0.3099 0.2486 0.2717 -0.1065 0.0399 -0.0370 617 PHE A CB 4505 C CG . PHE A 582 ? 0.3341 0.2533 0.2880 -0.1101 0.0436 -0.0333 617 PHE A CG 4506 C CD1 . PHE A 582 ? 0.3361 0.2579 0.2892 -0.1191 0.0467 -0.0325 617 PHE A CD1 4507 C CD2 . PHE A 582 ? 0.3474 0.2465 0.2949 -0.1039 0.0439 -0.0300 617 PHE A CD2 4508 C CE1 . PHE A 582 ? 0.3579 0.2612 0.3028 -0.1225 0.0501 -0.0284 617 PHE A CE1 4509 C CE2 . PHE A 582 ? 0.3667 0.2475 0.3065 -0.1064 0.0470 -0.0255 617 PHE A CE2 4510 C CZ . PHE A 582 ? 0.3644 0.2466 0.3023 -0.1160 0.0501 -0.0245 617 PHE A CZ 4511 N N . GLU A 583 ? 0.3211 0.2418 0.2765 -0.1048 0.0387 -0.0463 618 GLU A N 4512 C CA . GLU A 583 ? 0.3472 0.2483 0.2963 -0.1021 0.0403 -0.0483 618 GLU A CA 4513 C C . GLU A 583 ? 0.3409 0.2342 0.2895 -0.0905 0.0393 -0.0426 618 GLU A C 4514 O O . GLU A 583 ? 0.3282 0.2351 0.2820 -0.0840 0.0362 -0.0395 618 GLU A O 4515 C CB . GLU A 583 ? 0.3615 0.2702 0.3115 -0.1030 0.0387 -0.0550 618 GLU A CB 4516 C CG . GLU A 583 ? 0.3883 0.2777 0.3321 -0.1002 0.0410 -0.0584 618 GLU A CG 4517 C CD . GLU A 583 ? 0.4293 0.3254 0.3721 -0.1037 0.0403 -0.0662 618 GLU A CD 4518 O OE1 . GLU A 583 ? 0.4281 0.3400 0.3733 -0.1118 0.0387 -0.0698 618 GLU A OE1 4519 O OE2 . GLU A 583 ? 0.4182 0.3045 0.3579 -0.0984 0.0414 -0.0687 618 GLU A OE2 4520 N N . SER A 584 ? 0.3473 0.2193 0.2901 -0.0878 0.0418 -0.0413 619 SER A N 4521 C CA . SER A 584 ? 0.3576 0.2229 0.3003 -0.0767 0.0406 -0.0358 619 SER A CA 4522 C C . SER A 584 ? 0.3661 0.2153 0.3055 -0.0715 0.0422 -0.0380 619 SER A C 4523 O O . SER A 584 ? 0.3795 0.2153 0.3142 -0.0768 0.0455 -0.0429 619 SER A O 4524 C CB . SER A 584 ? 0.3788 0.2355 0.3185 -0.0761 0.0414 -0.0285 619 SER A CB 4525 O OG . SER A 584 ? 0.3966 0.2334 0.3292 -0.0821 0.0453 -0.0284 619 SER A OG 4526 N N . GLY A 585 ? 0.3571 0.2082 0.2992 -0.0611 0.0402 -0.0346 620 GLY A N 4527 C CA . GLY A 585 ? 0.3745 0.2115 0.3148 -0.0535 0.0418 -0.0350 620 GLY A CA 4528 C C . GLY A 585 ? 0.3833 0.2095 0.3221 -0.0473 0.0415 -0.0267 620 GLY A C 4529 O O . GLY A 585 ? 0.3650 0.2013 0.3075 -0.0408 0.0383 -0.0216 620 GLY A O 4530 N N . TYR A 586 ? 0.3938 0.1993 0.3264 -0.0498 0.0448 -0.0254 621 TYR A N 4531 C CA . TYR A 586 ? 0.4051 0.1988 0.3346 -0.0454 0.0446 -0.0167 621 TYR A CA 4532 C C . TYR A 586 ? 0.4184 0.2007 0.3487 -0.0341 0.0449 -0.0143 621 TYR A C 4533 O O . TYR A 586 ? 0.4596 0.2255 0.3872 -0.0333 0.0486 -0.0184 621 TYR A O 4534 C CB . TYR A 586 ? 0.4259 0.2024 0.3479 -0.0544 0.0482 -0.0155 621 TYR A CB 4535 C CG . TYR A 586 ? 0.4421 0.2053 0.3594 -0.0505 0.0480 -0.0059 621 TYR A CG 4536 C CD1 . TYR A 586 ? 0.4265 0.2007 0.3437 -0.0513 0.0452 0.0006 621 TYR A CD1 4537 C CD2 . TYR A 586 ? 0.4613 0.2009 0.3739 -0.0455 0.0504 -0.0031 621 TYR A CD2 4538 C CE1 . TYR A 586 ? 0.4369 0.1999 0.3489 -0.0480 0.0447 0.0098 621 TYR A CE1 4539 C CE2 . TYR A 586 ? 0.4793 0.2071 0.3873 -0.0416 0.0497 0.0067 621 TYR A CE2 4540 C CZ . TYR A 586 ? 0.4651 0.2053 0.3725 -0.0430 0.0466 0.0133 621 TYR A CZ 4541 O OH . TYR A 586 ? 0.4856 0.2150 0.3874 -0.0395 0.0456 0.0233 621 TYR A OH 4542 N N . SER A 587 ? 0.4110 0.2020 0.3451 -0.0254 0.0413 -0.0080 622 SER A N 4543 C CA . SER A 587 ? 0.4218 0.2045 0.3578 -0.0140 0.0411 -0.0046 622 SER A CA 4544 C C . SER A 587 ? 0.4593 0.2199 0.3893 -0.0118 0.0428 0.0022 622 SER A C 4545 O O . SER A 587 ? 0.4610 0.2214 0.3875 -0.0133 0.0407 0.0098 622 SER A O 4546 C CB . SER A 587 ? 0.3940 0.1947 0.3363 -0.0064 0.0364 -0.0001 622 SER A CB 4547 O OG . SER A 587 ? 0.3924 0.1871 0.3376 0.0046 0.0361 0.0035 622 SER A OG 4548 N N . GLU A 588 ? 0.5021 0.2437 0.4303 -0.0078 0.0465 -0.0001 623 GLU A N 4549 C CA . GLU A 588 ? 0.5441 0.2631 0.4670 -0.0034 0.0480 0.0072 623 GLU A CA 4550 C C . GLU A 588 ? 0.5504 0.2745 0.4779 0.0095 0.0440 0.0159 623 GLU A C 4551 O O . GLU A 588 ? 0.5930 0.3023 0.5162 0.0137 0.0437 0.0244 623 GLU A O 4552 C CB . GLU A 588 ? 0.5822 0.2772 0.5013 -0.0033 0.0538 0.0014 623 GLU A CB 4553 C CG . GLU A 588 ? 0.5954 0.2821 0.5077 -0.0178 0.0576 -0.0051 623 GLU A CG 4554 C CD . GLU A 588 ? 0.6339 0.2921 0.5399 -0.0196 0.0637 -0.0096 623 GLU A CD 4555 O OE1 . GLU A 588 ? 0.6261 0.2721 0.5341 -0.0088 0.0657 -0.0100 623 GLU A OE1 4556 O OE2 . GLU A 588 ? 0.6475 0.2961 0.5467 -0.0321 0.0667 -0.0132 623 GLU A OE2 4557 N N . ILE A 589 ? 0.5066 0.2522 0.4425 0.0152 0.0408 0.0143 624 ILE A N 4558 C CA . ILE A 589 ? 0.5094 0.2643 0.4508 0.0264 0.0365 0.0219 624 ILE A CA 4559 C C . ILE A 589 ? 0.4971 0.2665 0.4368 0.0230 0.0314 0.0289 624 ILE A C 4560 O O . ILE A 589 ? 0.5073 0.2730 0.4447 0.0277 0.0287 0.0383 624 ILE A O 4561 C CB . ILE A 589 ? 0.5036 0.2746 0.4547 0.0337 0.0359 0.0165 624 ILE A CB 4562 C CG1 . ILE A 589 ? 0.5274 0.2845 0.4794 0.0365 0.0416 0.0084 624 ILE A CG1 4563 C CG2 . ILE A 589 ? 0.5139 0.2958 0.4715 0.0449 0.0315 0.0243 624 ILE A CG2 4564 C CD1 . ILE A 589 ? 0.5776 0.3096 0.5268 0.0439 0.0447 0.0123 624 ILE A CD1 4565 N N . PHE A 590 ? 0.4860 0.2716 0.4265 0.0148 0.0303 0.0245 625 PHE A N 4566 C CA . PHE A 590 ? 0.4749 0.2736 0.4135 0.0110 0.0264 0.0298 625 PHE A CA 4567 C C . PHE A 590 ? 0.4563 0.2446 0.3858 0.0015 0.0280 0.0325 625 PHE A C 4568 O O . PHE A 590 ? 0.4408 0.2383 0.3676 -0.0019 0.0255 0.0370 625 PHE A O 4569 C CB . PHE A 590 ? 0.4880 0.3089 0.4321 0.0076 0.0245 0.0242 625 PHE A CB 4570 C CG . PHE A 590 ? 0.5315 0.3661 0.4841 0.0159 0.0223 0.0226 625 PHE A CG 4571 C CD1 . PHE A 590 ? 0.5993 0.4321 0.5554 0.0262 0.0206 0.0278 625 PHE A CD1 4572 C CD2 . PHE A 590 ? 0.6089 0.4594 0.5661 0.0130 0.0219 0.0163 625 PHE A CD2 4573 C CE1 . PHE A 590 ? 0.6058 0.4532 0.5702 0.0329 0.0189 0.0260 625 PHE A CE1 4574 C CE2 . PHE A 590 ? 0.6285 0.4920 0.5930 0.0194 0.0201 0.0149 625 PHE A CE2 4575 C CZ . PHE A 590 ? 0.6417 0.5042 0.6101 0.0291 0.0188 0.0195 625 PHE A CZ 4576 N N . LEU A 591 ? 0.4770 0.2469 0.4018 -0.0033 0.0326 0.0295 626 LEU A N 4577 C CA . LEU A 591 ? 0.4824 0.2416 0.3985 -0.0135 0.0350 0.0317 626 LEU A CA 4578 C C . LEU A 591 ? 0.4624 0.2388 0.3791 -0.0234 0.0347 0.0276 626 LEU A C 4579 O O . LEU A 591 ? 0.4680 0.2440 0.3789 -0.0302 0.0350 0.0315 626 LEU A O 4580 C CB . LEU A 591 ? 0.5115 0.2612 0.4209 -0.0106 0.0331 0.0430 626 LEU A CB 4581 C CG . LEU A 591 ? 0.5350 0.2710 0.4450 0.0013 0.0321 0.0491 626 LEU A CG 4582 C CD1 . LEU A 591 ? 0.5584 0.2877 0.4611 0.0032 0.0295 0.0611 626 LEU A CD1 4583 C CD2 . LEU A 591 ? 0.5595 0.2725 0.4675 0.0015 0.0374 0.0448 626 LEU A CD2 4584 N N . MET A 592 ? 0.4144 0.2060 0.3380 -0.0241 0.0342 0.0198 627 MET A N 4585 C CA . MET A 592 ? 0.3933 0.2014 0.3186 -0.0322 0.0339 0.0158 627 MET A CA 4586 C C . MET A 592 ? 0.3748 0.1928 0.3065 -0.0328 0.0344 0.0069 627 MET A C 4587 O O . MET A 592 ? 0.3851 0.1997 0.3200 -0.0262 0.0345 0.0043 627 MET A O 4588 C CB . MET A 592 ? 0.3798 0.2040 0.3068 -0.0296 0.0299 0.0204 627 MET A CB 4589 C CG . MET A 592 ? 0.3638 0.2000 0.2976 -0.0206 0.0264 0.0202 627 MET A CG 4590 S SD . MET A 592 ? 0.3545 0.2070 0.2884 -0.0188 0.0220 0.0256 627 MET A SD 4591 C CE . MET A 592 ? 0.3998 0.2385 0.3261 -0.0152 0.0207 0.0360 627 MET A CE 4592 N N . PRO A 593 ? 0.3550 0.1859 0.2887 -0.0404 0.0347 0.0022 628 PRO A N 4593 C CA . PRO A 593 ? 0.3444 0.1859 0.2836 -0.0406 0.0345 -0.0052 628 PRO A CA 4594 C C . PRO A 593 ? 0.3347 0.1892 0.2799 -0.0322 0.0311 -0.0048 628 PRO A C 4595 O O . PRO A 593 ? 0.3135 0.1761 0.2598 -0.0289 0.0283 0.0000 628 PRO A O 4596 C CB . PRO A 593 ? 0.3388 0.1931 0.2794 -0.0495 0.0348 -0.0085 628 PRO A CB 4597 C CG . PRO A 593 ? 0.3399 0.1840 0.2743 -0.0562 0.0373 -0.0048 628 PRO A CG 4598 C CD . PRO A 593 ? 0.3546 0.1898 0.2853 -0.0494 0.0359 0.0031 628 PRO A CD 4599 N N . LEU A 594 ? 0.3359 0.1921 0.2844 -0.0295 0.0315 -0.0102 629 LEU A N 4600 C CA . LEU A 594 ? 0.3278 0.1989 0.2820 -0.0240 0.0288 -0.0113 629 LEU A CA 4601 C C . LEU A 594 ? 0.3004 0.1874 0.2574 -0.0293 0.0275 -0.0146 629 LEU A C 4602 O O . LEU A 594 ? 0.2665 0.1665 0.2273 -0.0263 0.0248 -0.0136 629 LEU A O 4603 C CB . LEU A 594 ? 0.3409 0.2082 0.2970 -0.0196 0.0303 -0.0160 629 LEU A CB 4604 C CG . LEU A 594 ? 0.3744 0.2248 0.3285 -0.0134 0.0323 -0.0137 629 LEU A CG 4605 C CD1 . LEU A 594 ? 0.3856 0.2339 0.3420 -0.0093 0.0346 -0.0196 629 LEU A CD1 4606 C CD2 . LEU A 594 ? 0.3797 0.2329 0.3357 -0.0060 0.0293 -0.0058 629 LEU A CD2 4607 N N . TRP A 595 ? 0.2994 0.1853 0.2547 -0.0372 0.0294 -0.0188 630 TRP A N 4608 C CA . TRP A 595 ? 0.2895 0.1906 0.2479 -0.0422 0.0282 -0.0216 630 TRP A CA 4609 C C . TRP A 595 ? 0.2894 0.1874 0.2452 -0.0513 0.0305 -0.0236 630 TRP A C 4610 O O . TRP A 595 ? 0.2956 0.1793 0.2470 -0.0548 0.0334 -0.0254 630 TRP A O 4611 C CB . TRP A 595 ? 0.2859 0.1958 0.2472 -0.0413 0.0274 -0.0270 630 TRP A CB 4612 C CG . TRP A 595 ? 0.2981 0.1979 0.2562 -0.0439 0.0301 -0.0326 630 TRP A CG 4613 C CD1 . TRP A 595 ? 0.3139 0.2045 0.2709 -0.0385 0.0315 -0.0341 630 TRP A CD1 4614 C CD2 . TRP A 595 ? 0.3119 0.2102 0.2677 -0.0527 0.0319 -0.0380 630 TRP A CD2 4615 N NE1 . TRP A 595 ? 0.3309 0.2129 0.2843 -0.0433 0.0345 -0.0404 630 TRP A NE1 4616 C CE2 . TRP A 595 ? 0.3176 0.2041 0.2698 -0.0525 0.0346 -0.0429 630 TRP A CE2 4617 C CE3 . TRP A 595 ? 0.2935 0.2002 0.2501 -0.0609 0.0317 -0.0393 630 TRP A CE3 4618 C CZ2 . TRP A 595 ? 0.3338 0.2157 0.2824 -0.0610 0.0370 -0.0494 630 TRP A CZ2 4619 C CZ3 . TRP A 595 ? 0.3071 0.2107 0.2608 -0.0694 0.0337 -0.0454 630 TRP A CZ3 4620 C CH2 . TRP A 595 ? 0.3222 0.2129 0.2714 -0.0697 0.0363 -0.0505 630 TRP A CH2 4621 N N . THR A 596 ? 0.2890 0.2003 0.2478 -0.0550 0.0295 -0.0234 631 THR A N 4622 C CA . THR A 596 ? 0.2943 0.2080 0.2525 -0.0641 0.0314 -0.0255 631 THR A CA 4623 C C . THR A 596 ? 0.2735 0.2066 0.2379 -0.0659 0.0294 -0.0287 631 THR A C 4624 O O . THR A 596 ? 0.2766 0.2205 0.2450 -0.0612 0.0272 -0.0264 631 THR A O 4625 C CB . THR A 596 ? 0.3129 0.2244 0.2690 -0.0660 0.0326 -0.0204 631 THR A CB 4626 O OG1 . THR A 596 ? 0.3377 0.2311 0.2876 -0.0639 0.0340 -0.0162 631 THR A OG1 4627 C CG2 . THR A 596 ? 0.3265 0.2435 0.2831 -0.0757 0.0349 -0.0226 631 THR A CG2 4628 N N . SER A 597 ? 0.2749 0.2121 0.2399 -0.0728 0.0301 -0.0339 632 SER A N 4629 C CA . SER A 597 ? 0.2736 0.2293 0.2443 -0.0739 0.0276 -0.0368 632 SER A CA 4630 C C . SER A 597 ? 0.2784 0.2443 0.2519 -0.0828 0.0286 -0.0390 632 SER A C 4631 O O . SER A 597 ? 0.2858 0.2432 0.2554 -0.0907 0.0313 -0.0416 632 SER A O 4632 C CB . SER A 597 ? 0.2764 0.2310 0.2455 -0.0737 0.0266 -0.0415 632 SER A CB 4633 O OG . SER A 597 ? 0.2902 0.2630 0.2641 -0.0744 0.0236 -0.0435 632 SER A OG 4634 N N . TYR A 598 ? 0.2592 0.2432 0.2396 -0.0814 0.0265 -0.0380 633 TYR A N 4635 C CA . TYR A 598 ? 0.2582 0.2556 0.2433 -0.0888 0.0274 -0.0399 633 TYR A CA 4636 C C . TYR A 598 ? 0.2540 0.2727 0.2477 -0.0853 0.0242 -0.0395 633 TYR A C 4637 O O . TYR A 598 ? 0.2437 0.2651 0.2395 -0.0769 0.0222 -0.0365 633 TYR A O 4638 C CB . TYR A 598 ? 0.2530 0.2446 0.2364 -0.0919 0.0309 -0.0369 633 TYR A CB 4639 C CG . TYR A 598 ? 0.2447 0.2375 0.2295 -0.0843 0.0307 -0.0320 633 TYR A CG 4640 C CD1 . TYR A 598 ? 0.2496 0.2276 0.2288 -0.0782 0.0306 -0.0284 633 TYR A CD1 4641 C CD2 . TYR A 598 ? 0.2475 0.2564 0.2391 -0.0835 0.0308 -0.0313 633 TYR A CD2 4642 C CE1 . TYR A 598 ? 0.2478 0.2275 0.2276 -0.0725 0.0304 -0.0244 633 TYR A CE1 4643 C CE2 . TYR A 598 ? 0.2358 0.2451 0.2279 -0.0775 0.0312 -0.0277 633 TYR A CE2 4644 C CZ . TYR A 598 ? 0.2443 0.2390 0.2301 -0.0725 0.0309 -0.0244 633 TYR A CZ 4645 O OH . TYR A 598 ? 0.2264 0.2225 0.2122 -0.0677 0.0312 -0.0215 633 TYR A OH 4646 N N . THR A 599 ? 0.2650 0.2988 0.2637 -0.0919 0.0238 -0.0425 634 THR A N 4647 C CA . THR A 599 ? 0.2605 0.3159 0.2681 -0.0888 0.0205 -0.0422 634 THR A CA 4648 C C . THR A 599 ? 0.2614 0.3292 0.2757 -0.0920 0.0227 -0.0416 634 THR A C 4649 O O . THR A 599 ? 0.2738 0.3398 0.2866 -0.1011 0.0258 -0.0437 634 THR A O 4650 C CB . THR A 599 ? 0.2722 0.3387 0.2810 -0.0935 0.0174 -0.0463 634 THR A CB 4651 O OG1 . THR A 599 ? 0.2723 0.3271 0.2743 -0.0905 0.0160 -0.0472 634 THR A OG1 4652 C CG2 . THR A 599 ? 0.2697 0.3597 0.2882 -0.0896 0.0135 -0.0448 634 THR A CG2 4653 N N . ILE A 600 ? 0.2487 0.3287 0.2702 -0.0846 0.0215 -0.0388 635 ILE A N 4654 C CA . ILE A 600 ? 0.2458 0.3390 0.2748 -0.0854 0.0239 -0.0382 635 ILE A CA 4655 C C . ILE A 600 ? 0.2443 0.3603 0.2840 -0.0814 0.0202 -0.0382 635 ILE A C 4656 O O . ILE A 600 ? 0.2267 0.3439 0.2679 -0.0726 0.0172 -0.0357 635 ILE A O 4657 C CB . ILE A 600 ? 0.2473 0.3319 0.2746 -0.0786 0.0264 -0.0347 635 ILE A CB 4658 C CG1 . ILE A 600 ? 0.2529 0.3157 0.2696 -0.0816 0.0293 -0.0336 635 ILE A CG1 4659 C CG2 . ILE A 600 ? 0.2469 0.3465 0.2823 -0.0792 0.0294 -0.0348 635 ILE A CG2 4660 C CD1 . ILE A 600 ? 0.2704 0.3295 0.2839 -0.0924 0.0331 -0.0353 635 ILE A CD1 4661 N N . SER A 601 ? 0.2487 0.3829 0.2957 -0.0881 0.0204 -0.0407 636 SER A N 4662 C CA . SER A 601 ? 0.2454 0.4035 0.3035 -0.0843 0.0165 -0.0403 636 SER A CA 4663 C C . SER A 601 ? 0.2312 0.3985 0.2979 -0.0754 0.0181 -0.0375 636 SER A C 4664 O O . SER A 601 ? 0.2274 0.3871 0.2925 -0.0756 0.0229 -0.0372 636 SER A O 4665 C CB . SER A 601 ? 0.2590 0.4356 0.3228 -0.0949 0.0160 -0.0441 636 SER A CB 4666 O OG . SER A 601 ? 0.2801 0.4675 0.3510 -0.0982 0.0203 -0.0447 636 SER A OG 4667 N N . LYS A 602 ? 0.2417 0.4251 0.3173 -0.0677 0.0143 -0.0354 637 LYS A N 4668 C CA . LYS A 602 ? 0.2469 0.4407 0.3322 -0.0586 0.0159 -0.0332 637 LYS A CA 4669 C C . LYS A 602 ? 0.2570 0.4621 0.3492 -0.0635 0.0213 -0.0355 637 LYS A C 4670 O O . LYS A 602 ? 0.2645 0.4677 0.3591 -0.0580 0.0253 -0.0347 637 LYS A O 4671 C CB . LYS A 602 ? 0.2689 0.4826 0.3643 -0.0517 0.0106 -0.0309 637 LYS A CB 4672 C CG . LYS A 602 ? 0.2847 0.5072 0.3901 -0.0402 0.0117 -0.0281 637 LYS A CG 4673 C CD . LYS A 602 ? 0.2952 0.5408 0.4121 -0.0345 0.0064 -0.0256 637 LYS A CD 4674 C CE . LYS A 602 ? 0.3236 0.5792 0.4521 -0.0235 0.0087 -0.0236 637 LYS A CE 4675 N NZ . LYS A 602 ? 0.3545 0.6327 0.4952 -0.0161 0.0034 -0.0202 637 LYS A NZ 4676 N N . GLN A 603 ? 0.2668 0.4837 0.3615 -0.0742 0.0216 -0.0386 638 GLN A N 4677 C CA . GLN A 603 ? 0.3183 0.5505 0.4209 -0.0803 0.0264 -0.0410 638 GLN A CA 4678 C C . GLN A 603 ? 0.3342 0.5496 0.4267 -0.0902 0.0320 -0.0429 638 GLN A C 4679 O O . GLN A 603 ? 0.3211 0.5476 0.4183 -0.0976 0.0364 -0.0450 638 GLN A O 4680 C CB . GLN A 603 ? 0.3336 0.5908 0.4455 -0.0875 0.0232 -0.0433 638 GLN A CB 4681 C CG . GLN A 603 ? 0.3815 0.6581 0.5037 -0.0783 0.0168 -0.0408 638 GLN A CG 4682 C CD . GLN A 603 ? 0.4432 0.7122 0.5576 -0.0783 0.0104 -0.0398 638 GLN A CD 4683 O OE1 . GLN A 603 ? 0.4640 0.7128 0.5655 -0.0848 0.0107 -0.0416 638 GLN A OE1 4684 N NE2 . GLN A 603 ? 0.4751 0.7607 0.5974 -0.0706 0.0045 -0.0369 638 GLN A NE2 4685 N N . ALA A 604 ? 0.3281 0.5175 0.4071 -0.0904 0.0320 -0.0418 639 ALA A N 4686 C CA . ALA A 604 ? 0.3384 0.5096 0.4067 -0.0990 0.0367 -0.0425 639 ALA A CA 4687 C C . ALA A 604 ? 0.3404 0.5121 0.4098 -0.0979 0.0427 -0.0418 639 ALA A C 4688 O O . ALA A 604 ? 0.3229 0.4978 0.3966 -0.0879 0.0433 -0.0402 639 ALA A O 4689 C CB . ALA A 604 ? 0.3858 0.5306 0.4410 -0.0963 0.0351 -0.0406 639 ALA A CB 4690 N N . GLU A 605 ? 0.3605 0.5274 0.4249 -0.1087 0.0474 -0.0430 640 GLU A N 4691 C CA . GLU A 605 ? 0.4010 0.5689 0.4651 -0.1104 0.0537 -0.0426 640 GLU A CA 4692 C C . GLU A 605 ? 0.3773 0.5185 0.4266 -0.1105 0.0559 -0.0398 640 GLU A C 4693 O O . GLU A 605 ? 0.3745 0.4974 0.4136 -0.1153 0.0544 -0.0389 640 GLU A O 4694 C CB . GLU A 605 ? 0.4429 0.6240 0.5107 -0.1236 0.0579 -0.0453 640 GLU A CB 4695 C CG . GLU A 605 ? 0.5081 0.7174 0.5905 -0.1258 0.0554 -0.0483 640 GLU A CG 4696 C CD . GLU A 605 ? 0.5613 0.7920 0.6577 -0.1144 0.0552 -0.0481 640 GLU A CD 4697 O OE1 . GLU A 605 ? 0.6169 0.8432 0.7143 -0.1024 0.0512 -0.0461 640 GLU A OE1 4698 O OE2 . GLU A 605 ? 0.5756 0.8276 0.6824 -0.1174 0.0593 -0.0501 640 GLU A OE2 4699 N N . VAL A 606 ? 0.3627 0.5020 0.4107 -0.1049 0.0592 -0.0384 641 VAL A N 4700 C CA . VAL A 606 ? 0.3714 0.4890 0.4058 -0.1057 0.0616 -0.0355 641 VAL A CA 4701 C C . VAL A 606 ? 0.3705 0.4908 0.4018 -0.1164 0.0680 -0.0359 641 VAL A C 4702 O O . VAL A 606 ? 0.3626 0.5029 0.4033 -0.1179 0.0718 -0.0384 641 VAL A O 4703 C CB . VAL A 606 ? 0.4072 0.5205 0.4402 -0.0947 0.0617 -0.0341 641 VAL A CB 4704 C CG1 . VAL A 606 ? 0.4124 0.5038 0.4308 -0.0959 0.0631 -0.0307 641 VAL A CG1 4705 C CG2 . VAL A 606 ? 0.4086 0.5216 0.4460 -0.0845 0.0558 -0.0338 641 VAL A CG2 4706 N N . SER A 607 ? 0.3847 0.4856 0.4032 -0.1238 0.0693 -0.0333 642 SER A N 4707 C CA . SER A 607 ? 0.4100 0.5100 0.4230 -0.1345 0.0755 -0.0326 642 SER A CA 4708 C C . SER A 607 ? 0.4553 0.5333 0.4533 -0.1337 0.0769 -0.0279 642 SER A C 4709 O O . SER A 607 ? 0.5007 0.5631 0.4926 -0.1268 0.0727 -0.0254 642 SER A O 4710 C CB . SER A 607 ? 0.4291 0.5277 0.4409 -0.1470 0.0762 -0.0339 642 SER A CB 4711 O OG . SER A 607 ? 0.4496 0.5269 0.4529 -0.1470 0.0721 -0.0321 642 SER A OG 4712 N N . SER A 608 ? 0.4770 0.5554 0.4693 -0.1406 0.0827 -0.0267 643 SER A N 4713 C CA . SER A 608 ? 0.5218 0.5817 0.4995 -0.1400 0.0840 -0.0218 643 SER A CA 4714 C C . SER A 608 ? 0.5589 0.5972 0.5247 -0.1478 0.0834 -0.0175 643 SER A C 4715 O O . SER A 608 ? 0.6026 0.6417 0.5712 -0.1555 0.0837 -0.0192 643 SER A O 4716 C CB . SER A 608 ? 0.5429 0.6130 0.5188 -0.1440 0.0907 -0.0222 643 SER A CB 4717 O OG . SER A 608 ? 0.5780 0.6626 0.5599 -0.1545 0.0955 -0.0248 643 SER A OG 4718 N N . ILE A 609 ? 0.5716 0.5908 0.5243 -0.1456 0.0826 -0.0121 644 ILE A N 4719 C CA . ILE A 609 ? 0.5882 0.5851 0.5282 -0.1525 0.0828 -0.0069 644 ILE A CA 4720 C C . ILE A 609 ? 0.6085 0.6072 0.5417 -0.1640 0.0895 -0.0049 644 ILE A C 4721 O O . ILE A 609 ? 0.6049 0.6088 0.5340 -0.1629 0.0923 -0.0035 644 ILE A O 4722 C CB . ILE A 609 ? 0.5762 0.5532 0.5055 -0.1446 0.0786 -0.0011 644 ILE A CB 4723 C CG1 . ILE A 609 ? 0.5767 0.5523 0.5128 -0.1342 0.0724 -0.0032 644 ILE A CG1 4724 C CG2 . ILE A 609 ? 0.5954 0.5492 0.5113 -0.1510 0.0793 0.0050 644 ILE A CG2 4725 C CD1 . ILE A 609 ? 0.5936 0.5559 0.5224 -0.1251 0.0682 0.0013 644 ILE A CD1 4726 N N . PRO A 610 ? 0.6315 0.6261 0.5630 -0.1757 0.0925 -0.0050 645 PRO A N 4727 C CA . PRO A 610 ? 0.6432 0.6394 0.5675 -0.1874 0.0993 -0.0027 645 PRO A CA 4728 C C . PRO A 610 ? 0.6803 0.6566 0.5874 -0.1875 0.1000 0.0053 645 PRO A C 4729 O O . PRO A 610 ? 0.6931 0.6498 0.5928 -0.1810 0.0952 0.0099 645 PRO A O 4730 C CB . PRO A 610 ? 0.6577 0.6486 0.5822 -0.1997 0.1014 -0.0040 645 PRO A CB 4731 C CG . PRO A 610 ? 0.6503 0.6486 0.5870 -0.1947 0.0966 -0.0097 645 PRO A CG 4732 C CD . PRO A 610 ? 0.6313 0.6224 0.5678 -0.1799 0.0905 -0.0081 645 PRO A CD 4733 N N . GLU A 611 ? 0.7156 0.6987 0.6169 -0.1949 0.1060 0.0069 646 GLU A N 4734 C CA . GLU A 611 ? 0.7516 0.7195 0.6358 -0.1965 0.1073 0.0148 646 GLU A CA 4735 C C . GLU A 611 ? 0.7631 0.7019 0.6346 -0.1990 0.1046 0.0224 646 GLU A C 4736 O O . GLU A 611 ? 0.7593 0.6825 0.6209 -0.1920 0.1006 0.0287 646 GLU A O 4737 C CB . GLU A 611 ? 0.8184 0.7978 0.6982 -0.2082 0.1154 0.0149 646 GLU A CB 4738 C CG . GLU A 611 ? 0.8895 0.8602 0.7526 -0.2093 0.1173 0.0219 646 GLU A CG 4739 C CD . GLU A 611 ? 0.9553 0.9405 0.8151 -0.2209 0.1260 0.0208 646 GLU A CD 4740 O OE1 . GLU A 611 ? 0.9888 0.9729 0.8475 -0.2334 0.1307 0.0214 646 GLU A OE1 4741 O OE2 . GLU A 611 ? 0.9735 0.9711 0.8314 -0.2179 0.1286 0.0192 646 GLU A OE2 4742 N N . HIS A 612 ? 0.7773 0.7096 0.6497 -0.2088 0.1070 0.0215 647 HIS A N 4743 C CA . HIS A 612 ? 0.8035 0.7068 0.6643 -0.2123 0.1056 0.0279 647 HIS A CA 4744 C C . HIS A 612 ? 0.7479 0.6361 0.6106 -0.2005 0.0985 0.0285 647 HIS A C 4745 O O . HIS A 612 ? 0.7431 0.6059 0.5948 -0.1996 0.0967 0.0353 647 HIS A O 4746 C CB . HIS A 612 ? 0.8819 0.7822 0.7430 -0.2273 0.1107 0.0257 647 HIS A CB 4747 C CG . HIS A 612 ? 0.9429 0.8614 0.8207 -0.2287 0.1101 0.0159 647 HIS A CG 4748 N ND1 . HIS A 612 ? 0.9748 0.9229 0.8650 -0.2330 0.1137 0.0092 647 HIS A ND1 4749 C CD2 . HIS A 612 ? 0.9821 0.8938 0.8658 -0.2266 0.1065 0.0119 647 HIS A CD2 4750 C CE1 . HIS A 612 ? 0.9742 0.9334 0.8774 -0.2332 0.1116 0.0021 647 HIS A CE1 4751 N NE2 . HIS A 612 ? 0.9655 0.9030 0.8646 -0.2299 0.1073 0.0033 647 HIS A NE2 4752 N N . LEU A 613 ? 0.6917 0.5953 0.5682 -0.1915 0.0947 0.0217 648 LEU A N 4753 C CA . LEU A 613 ? 0.6676 0.5600 0.5469 -0.1803 0.0883 0.0215 648 LEU A CA 4754 C C . LEU A 613 ? 0.6447 0.5391 0.5235 -0.1670 0.0834 0.0241 648 LEU A C 4755 O O . LEU A 613 ? 0.6020 0.4878 0.4827 -0.1577 0.0783 0.0244 648 LEU A O 4756 C CB . LEU A 613 ? 0.6494 0.5553 0.5433 -0.1795 0.0867 0.0126 648 LEU A CB 4757 C CG . LEU A 613 ? 0.6835 0.5875 0.5794 -0.1922 0.0902 0.0087 648 LEU A CG 4758 C CD1 . LEU A 613 ? 0.6653 0.5801 0.5741 -0.1887 0.0868 0.0009 648 LEU A CD1 4759 C CD2 . LEU A 613 ? 0.7241 0.5979 0.6065 -0.1980 0.0916 0.0144 648 LEU A CD2 4760 N N . THR A 614 ? 0.6648 0.5704 0.5404 -0.1666 0.0852 0.0257 649 THR A N 4761 C CA . THR A 614 ? 0.6621 0.5717 0.5371 -0.1553 0.0809 0.0272 649 THR A CA 4762 C C . THR A 614 ? 0.6517 0.5407 0.5191 -0.1473 0.0753 0.0339 649 THR A C 4763 O O . THR A 614 ? 0.6660 0.5571 0.5395 -0.1370 0.0703 0.0321 649 THR A O 4764 C CB . THR A 614 ? 0.6964 0.6148 0.5638 -0.1586 0.0844 0.0296 649 THR A CB 4765 O OG1 . THR A 614 ? 0.7316 0.6672 0.6049 -0.1675 0.0908 0.0242 649 THR A OG1 4766 C CG2 . THR A 614 ? 0.6996 0.6279 0.5696 -0.1483 0.0809 0.0279 649 THR A CG2 4767 N N . ASN A 615 ? 0.6305 0.4999 0.4850 -0.1521 0.0764 0.0418 650 ASN A N 4768 C CA . ASN A 615 ? 0.6410 0.4904 0.4879 -0.1444 0.0715 0.0493 650 ASN A CA 4769 C C . ASN A 615 ? 0.6357 0.4647 0.4819 -0.1461 0.0715 0.0503 650 ASN A C 4770 O O . ASN A 615 ? 0.6242 0.4325 0.4616 -0.1426 0.0694 0.0579 650 ASN A O 4771 C CB . ASN A 615 ? 0.6973 0.5388 0.5290 -0.1465 0.0718 0.0589 650 ASN A CB 4772 C CG . ASN A 615 ? 0.7102 0.5696 0.5416 -0.1430 0.0708 0.0577 650 ASN A CG 4773 O OD1 . ASN A 615 ? 0.7879 0.6581 0.6281 -0.1342 0.0670 0.0531 650 ASN A OD1 4774 N ND2 . ASN A 615 ? 0.7634 0.6255 0.5840 -0.1503 0.0745 0.0616 650 ASN A ND2 4775 N N . CYS A 616 ? 0.6060 0.4413 0.4618 -0.1509 0.0738 0.0423 651 CYS A N 4776 C CA . CYS A 616 ? 0.6309 0.4480 0.4857 -0.1547 0.0749 0.0415 651 CYS A CA 4777 C C . CYS A 616 ? 0.5726 0.3820 0.4328 -0.1431 0.0697 0.0399 651 CYS A C 4778 O O . CYS A 616 ? 0.5362 0.3618 0.4072 -0.1365 0.0668 0.0340 651 CYS A O 4779 C CB . CYS A 616 ? 0.6901 0.5191 0.5529 -0.1654 0.0791 0.0331 651 CYS A CB 4780 S SG . CYS A 616 ? 0.7556 0.5654 0.6193 -0.1698 0.0800 0.0291 651 CYS A SG 4781 N N . VAL A 617 ? 0.5486 0.3330 0.4011 -0.1405 0.0689 0.0455 652 VAL A N 4782 C CA . VAL A 617 ? 0.5458 0.3212 0.4035 -0.1309 0.0654 0.0431 652 VAL A CA 4783 C C . VAL A 617 ? 0.5672 0.3184 0.4193 -0.1370 0.0688 0.0431 652 VAL A C 4784 O O . VAL A 617 ? 0.5571 0.2892 0.3976 -0.1418 0.0713 0.0507 652 VAL A O 4785 C CB . VAL A 617 ? 0.5592 0.3287 0.4143 -0.1177 0.0601 0.0501 652 VAL A CB 4786 C CG1 . VAL A 617 ? 0.5552 0.3152 0.4159 -0.1083 0.0574 0.0472 652 VAL A CG1 4787 C CG2 . VAL A 617 ? 0.5303 0.3230 0.3901 -0.1126 0.0570 0.0495 652 VAL A CG2 4788 N N . ARG A 618 ? 0.5434 0.2948 0.4031 -0.1371 0.0689 0.0347 653 ARG A N 4789 C CA . ARG A 618 ? 0.5863 0.3163 0.4413 -0.1447 0.0728 0.0324 653 ARG A CA 4790 C C . ARG A 618 ? 0.5846 0.2966 0.4402 -0.1346 0.0708 0.0315 653 ARG A C 4791 O O . ARG A 618 ? 0.5500 0.2745 0.4146 -0.1258 0.0672 0.0267 653 ARG A O 4792 C CB . ARG A 618 ? 0.5920 0.3373 0.4541 -0.1562 0.0757 0.0223 653 ARG A CB 4793 C CG . ARG A 618 ? 0.5999 0.3642 0.4627 -0.1661 0.0784 0.0225 653 ARG A CG 4794 C CD . ARG A 618 ? 0.6056 0.3891 0.4775 -0.1763 0.0805 0.0127 653 ARG A CD 4795 N NE . ARG A 618 ? 0.6264 0.3930 0.4950 -0.1855 0.0836 0.0081 653 ARG A NE 4796 C CZ . ARG A 618 ? 0.6339 0.4031 0.5088 -0.1852 0.0824 -0.0002 653 ARG A CZ 4797 N NH1 . ARG A 618 ? 0.6231 0.4117 0.5087 -0.1761 0.0778 -0.0049 653 ARG A NH1 4798 N NH2 . ARG A 618 ? 0.6703 0.4222 0.5402 -0.1951 0.0859 -0.0042 653 ARG A NH2 4799 N N . PRO A 619 ? 0.6178 0.3001 0.4638 -0.1361 0.0736 0.0358 654 PRO A N 4800 C CA . PRO A 619 ? 0.6320 0.2968 0.4792 -0.1271 0.0727 0.0334 654 PRO A CA 4801 C C . PRO A 619 ? 0.6190 0.2913 0.4737 -0.1317 0.0741 0.0209 654 PRO A C 4802 O O . PRO A 619 ? 0.6023 0.2825 0.4576 -0.1449 0.0771 0.0153 654 PRO A O 4803 C CB . PRO A 619 ? 0.6796 0.3107 0.5143 -0.1306 0.0767 0.0400 654 PRO A CB 4804 C CG . PRO A 619 ? 0.7050 0.3371 0.5315 -0.1368 0.0776 0.0491 654 PRO A CG 4805 C CD . PRO A 619 ? 0.6693 0.3317 0.5026 -0.1453 0.0777 0.0433 654 PRO A CD 4806 N N . ASP A 620 ? 0.6201 0.2922 0.4808 -0.1210 0.0716 0.0168 655 ASP A N 4807 C CA . ASP A 620 ? 0.6001 0.2791 0.4671 -0.1241 0.0724 0.0051 655 ASP A CA 4808 C C . ASP A 620 ? 0.6267 0.2753 0.4871 -0.1246 0.0764 0.0025 655 ASP A C 4809 O O . ASP A 620 ? 0.6249 0.2601 0.4851 -0.1123 0.0753 0.0049 655 ASP A O 4810 C CB . ASP A 620 ? 0.5670 0.2670 0.4445 -0.1126 0.0675 0.0017 655 ASP A CB 4811 C CG . ASP A 620 ? 0.5470 0.2590 0.4308 -0.1171 0.0678 -0.0098 655 ASP A CG 4812 O OD1 . ASP A 620 ? 0.5506 0.2477 0.4302 -0.1251 0.0717 -0.0158 655 ASP A OD1 4813 O OD2 . ASP A 620 ? 0.5191 0.2555 0.4117 -0.1130 0.0641 -0.0129 655 ASP A OD2 4814 N N . VAL A 621 ? 0.6461 0.2845 0.5013 -0.1390 0.0811 -0.0025 656 VAL A N 4815 C CA . VAL A 621 ? 0.6923 0.2994 0.5398 -0.1417 0.0859 -0.0059 656 VAL A CA 4816 C C . VAL A 621 ? 0.6858 0.2914 0.5381 -0.1349 0.0857 -0.0153 656 VAL A C 4817 O O . VAL A 621 ? 0.7139 0.2929 0.5600 -0.1357 0.0899 -0.0187 656 VAL A O 4818 C CB . VAL A 621 ? 0.7170 0.3142 0.5574 -0.1607 0.0913 -0.0101 656 VAL A CB 4819 C CG1 . VAL A 621 ? 0.7273 0.3201 0.5608 -0.1672 0.0927 0.0000 656 VAL A CG1 4820 C CG2 . VAL A 621 ? 0.7163 0.3406 0.5642 -0.1715 0.0907 -0.0208 656 VAL A CG2 4821 N N . ARG A 622 ? 0.6316 0.2645 0.4941 -0.1290 0.0813 -0.0198 657 ARG A N 4822 C CA . ARG A 622 ? 0.6255 0.2583 0.4924 -0.1205 0.0807 -0.0271 657 ARG A CA 4823 C C . ARG A 622 ? 0.6438 0.2690 0.5130 -0.1027 0.0784 -0.0208 657 ARG A C 4824 O O . ARG A 622 ? 0.6315 0.2516 0.5031 -0.0952 0.0792 -0.0263 657 ARG A O 4825 C CB . ARG A 622 ? 0.5963 0.2614 0.4728 -0.1219 0.0770 -0.0342 657 ARG A CB 4826 C CG . ARG A 622 ? 0.5854 0.2622 0.4618 -0.1382 0.0785 -0.0421 657 ARG A CG 4827 C CD . ARG A 622 ? 0.5594 0.2708 0.4460 -0.1374 0.0736 -0.0454 657 ARG A CD 4828 N NE . ARG A 622 ? 0.5281 0.2558 0.4191 -0.1334 0.0703 -0.0368 657 ARG A NE 4829 C CZ . ARG A 622 ? 0.4887 0.2454 0.3881 -0.1330 0.0664 -0.0376 657 ARG A CZ 4830 N NH1 . ARG A 622 ? 0.4668 0.2412 0.3718 -0.1359 0.0647 -0.0457 657 ARG A NH1 4831 N NH2 . ARG A 622 ? 0.4604 0.2280 0.3623 -0.1295 0.0644 -0.0301 657 ARG A NH2 4832 N N . VAL A 623 ? 0.6510 0.2777 0.5198 -0.0961 0.0756 -0.0095 658 VAL A N 4833 C CA . VAL A 623 ? 0.6553 0.2824 0.5282 -0.0794 0.0722 -0.0030 658 VAL A CA 4834 C C . VAL A 623 ? 0.7113 0.3136 0.5761 -0.0753 0.0734 0.0080 658 VAL A C 4835 O O . VAL A 623 ? 0.7103 0.3099 0.5690 -0.0834 0.0739 0.0141 658 VAL A O 4836 C CB . VAL A 623 ? 0.6346 0.2931 0.5157 -0.0749 0.0662 0.0002 658 VAL A CB 4837 C CG1 . VAL A 623 ? 0.6334 0.2936 0.5183 -0.0590 0.0624 0.0076 658 VAL A CG1 4838 C CG2 . VAL A 623 ? 0.6059 0.2879 0.4946 -0.0785 0.0649 -0.0099 658 VAL A CG2 4839 N N . SER A 624 ? 0.7438 0.3291 0.6087 -0.0623 0.0738 0.0110 659 SER A N 4840 C CA . SER A 624 ? 0.7855 0.3441 0.6423 -0.0576 0.0751 0.0218 659 SER A CA 4841 C C . SER A 624 ? 0.7768 0.3490 0.6333 -0.0540 0.0699 0.0336 659 SER A C 4842 O O . SER A 624 ? 0.7474 0.3475 0.6120 -0.0499 0.0651 0.0332 659 SER A O 4843 C CB . SER A 624 ? 0.8251 0.3658 0.6840 -0.0423 0.0761 0.0229 659 SER A CB 4844 O OG . SER A 624 ? 0.8461 0.4044 0.7130 -0.0282 0.0703 0.0294 659 SER A OG 4845 N N . PRO A 625 ? 0.7523 0.3047 0.5990 -0.0559 0.0711 0.0440 660 PRO A N 4846 C CA . PRO A 625 ? 0.7506 0.3122 0.5951 -0.0513 0.0662 0.0564 660 PRO A CA 4847 C C . PRO A 625 ? 0.7236 0.2985 0.5766 -0.0346 0.0605 0.0609 660 PRO A C 4848 O O . PRO A 625 ? 0.7302 0.3287 0.5867 -0.0327 0.0556 0.0646 660 PRO A O 4849 C CB . PRO A 625 ? 0.7718 0.3013 0.6036 -0.0531 0.0692 0.0664 660 PRO A CB 4850 C CG . PRO A 625 ? 0.7988 0.3092 0.6250 -0.0661 0.0761 0.0581 660 PRO A CG 4851 C CD . PRO A 625 ? 0.7964 0.3163 0.6319 -0.0646 0.0773 0.0443 660 PRO A CD 4852 N N . GLY A 626 ? 0.7505 0.3106 0.6068 -0.0228 0.0616 0.0600 661 GLY A N 4853 C CA . GLY A 626 ? 0.7334 0.3057 0.5987 -0.0065 0.0567 0.0638 661 GLY A CA 4854 C C . GLY A 626 ? 0.7071 0.3111 0.5841 -0.0044 0.0534 0.0559 661 GLY A C 4855 O O . GLY A 626 ? 0.6945 0.3147 0.5784 0.0063 0.0483 0.0604 661 GLY A O 4856 N N . PHE A 627 ? 0.6975 0.3105 0.5766 -0.0146 0.0561 0.0444 662 PHE A N 4857 C CA . PHE A 627 ? 0.6699 0.3127 0.5589 -0.0141 0.0530 0.0371 662 PHE A CA 4858 C C . PHE A 627 ? 0.6447 0.3078 0.5327 -0.0253 0.0510 0.0366 662 PHE A C 4859 O O . PHE A 627 ? 0.5996 0.2839 0.4943 -0.0283 0.0498 0.0291 662 PHE A O 4860 C CB . PHE A 627 ? 0.7009 0.3422 0.5942 -0.0157 0.0569 0.0243 662 PHE A CB 4861 C CG . PHE A 627 ? 0.7400 0.3674 0.6368 -0.0029 0.0588 0.0231 662 PHE A CG 4862 C CD1 . PHE A 627 ? 0.7419 0.3811 0.6466 0.0110 0.0546 0.0282 662 PHE A CD1 4863 C CD2 . PHE A 627 ? 0.8028 0.4064 0.6955 -0.0052 0.0649 0.0162 662 PHE A CD2 4864 C CE1 . PHE A 627 ? 0.7772 0.4054 0.6864 0.0234 0.0567 0.0268 662 PHE A CE1 4865 C CE2 . PHE A 627 ? 0.8128 0.4036 0.7091 0.0071 0.0673 0.0144 662 PHE A CE2 4866 C CZ . PHE A 627 ? 0.7976 0.4012 0.7026 0.0218 0.0633 0.0199 662 PHE A CZ 4867 N N . SER A 628 ? 0.6255 0.2826 0.5054 -0.0310 0.0507 0.0448 663 SER A N 4868 C CA . SER A 628 ? 0.6010 0.2756 0.4793 -0.0413 0.0496 0.0449 663 SER A CA 4869 C C . SER A 628 ? 0.5902 0.2762 0.4673 -0.0357 0.0446 0.0550 663 SER A C 4870 O O . SER A 628 ? 0.6284 0.3030 0.5028 -0.0265 0.0425 0.0638 663 SER A O 4871 C CB . SER A 628 ? 0.6314 0.2896 0.4999 -0.0548 0.0545 0.0452 663 SER A CB 4872 O OG . SER A 628 ? 0.6345 0.2828 0.5034 -0.0614 0.0592 0.0352 663 SER A OG 4873 N N . GLN A 629 ? 0.5489 0.2573 0.4279 -0.0411 0.0425 0.0538 664 GLN A N 4874 C CA . GLN A 629 ? 0.5481 0.2668 0.4237 -0.0388 0.0384 0.0627 664 GLN A CA 4875 C C . GLN A 629 ? 0.5932 0.2962 0.4565 -0.0464 0.0408 0.0705 664 GLN A C 4876 O O . GLN A 629 ? 0.5955 0.2840 0.4540 -0.0555 0.0457 0.0678 664 GLN A O 4877 C CB . GLN A 629 ? 0.5206 0.2658 0.4011 -0.0432 0.0365 0.0581 664 GLN A CB 4878 C CG . GLN A 629 ? 0.4976 0.2600 0.3894 -0.0364 0.0338 0.0513 664 GLN A CG 4879 C CD . GLN A 629 ? 0.4819 0.2677 0.3779 -0.0410 0.0325 0.0468 664 GLN A CD 4880 O OE1 . GLN A 629 ? 0.4968 0.2901 0.3883 -0.0441 0.0314 0.0512 664 GLN A OE1 4881 N NE2 . GLN A 629 ? 0.4540 0.2511 0.3583 -0.0413 0.0329 0.0380 664 GLN A NE2 4882 N N . ASN A 630 ? 0.6406 0.3477 0.4985 -0.0437 0.0372 0.0801 665 ASN A N 4883 C CA . ASN A 630 ? 0.6981 0.3928 0.5432 -0.0514 0.0392 0.0884 665 ASN A CA 4884 C C . ASN A 630 ? 0.6795 0.3943 0.5213 -0.0567 0.0372 0.0907 665 ASN A C 4885 O O . ASN A 630 ? 0.6569 0.3898 0.5034 -0.0503 0.0325 0.0912 665 ASN A O 4886 C CB . ASN A 630 ? 0.7296 0.4020 0.5677 -0.0432 0.0376 0.0997 665 ASN A CB 4887 C CG . ASN A 630 ? 0.7623 0.4464 0.6005 -0.0333 0.0310 0.1084 665 ASN A CG 4888 O OD1 . ASN A 630 ? 0.7915 0.4797 0.6207 -0.0372 0.0292 0.1162 665 ASN A OD1 4889 N ND2 . ASN A 630 ? 0.7646 0.4542 0.6124 -0.0209 0.0273 0.1073 665 ASN A ND2 4890 N N . CYS A 631 ? 0.6838 0.3952 0.5174 -0.0689 0.0414 0.0917 666 CYS A N 4891 C CA . CYS A 631 ? 0.6882 0.4179 0.5182 -0.0753 0.0410 0.0924 666 CYS A CA 4892 C C . CYS A 631 ? 0.6868 0.4161 0.5073 -0.0712 0.0369 0.1041 666 CYS A C 4893 O O . CYS A 631 ? 0.6587 0.4065 0.4778 -0.0730 0.0350 0.1042 666 CYS A O 4894 C CB . CYS A 631 ? 0.7310 0.4587 0.5561 -0.0899 0.0474 0.0891 666 CYS A CB 4895 S SG . CYS A 631 ? 0.8071 0.5426 0.6448 -0.0949 0.0510 0.0747 666 CYS A SG 4896 N N . LEU A 632 ? 0.6906 0.3991 0.5044 -0.0653 0.0353 0.1139 667 LEU A N 4897 C CA . LEU A 632 ? 0.6901 0.3977 0.4945 -0.0607 0.0306 0.1262 667 LEU A CA 4898 C C . LEU A 632 ? 0.6506 0.3780 0.4629 -0.0499 0.0237 0.1261 667 LEU A C 4899 O O . LEU A 632 ? 0.6444 0.3833 0.4505 -0.0499 0.0200 0.1319 667 LEU A O 4900 C CB . LEU A 632 ? 0.7268 0.4061 0.5230 -0.0562 0.0306 0.1370 667 LEU A CB 4901 C CG . LEU A 632 ? 0.7493 0.4239 0.5347 -0.0508 0.0255 0.1518 667 LEU A CG 4902 C CD1 . LEU A 632 ? 0.7528 0.4372 0.5258 -0.0618 0.0263 0.1560 667 LEU A CD1 4903 C CD2 . LEU A 632 ? 0.7815 0.4249 0.5596 -0.0467 0.0268 0.1614 667 LEU A CD2 4904 N N . ALA A 633 ? 0.6150 0.3471 0.4405 -0.0417 0.0223 0.1190 668 ALA A N 4905 C CA . ALA A 633 ? 0.5997 0.3519 0.4338 -0.0329 0.0165 0.1175 668 ALA A CA 4906 C C . ALA A 633 ? 0.5628 0.3378 0.3969 -0.0398 0.0162 0.1122 668 ALA A C 4907 O O . ALA A 633 ? 0.5861 0.3747 0.4180 -0.0370 0.0114 0.1161 668 ALA A O 4908 C CB . ALA A 633 ? 0.5961 0.3502 0.4441 -0.0253 0.0165 0.1091 668 ALA A CB 4909 N N . TYR A 634 ? 0.5364 0.3154 0.3726 -0.0490 0.0214 0.1033 669 TYR A N 4910 C CA . TYR A 634 ? 0.5269 0.3260 0.3635 -0.0555 0.0222 0.0977 669 TYR A CA 4911 C C . TYR A 634 ? 0.5564 0.3569 0.3792 -0.0621 0.0223 0.1051 669 TYR A C 4912 O O . TYR A 634 ? 0.5508 0.3678 0.3719 -0.0630 0.0201 0.1042 669 TYR A O 4913 C CB . TYR A 634 ? 0.5117 0.3148 0.3546 -0.0631 0.0278 0.0870 669 TYR A CB 4914 C CG . TYR A 634 ? 0.4825 0.2899 0.3387 -0.0571 0.0271 0.0788 669 TYR A CG 4915 C CD1 . TYR A 634 ? 0.4574 0.2829 0.3219 -0.0521 0.0237 0.0739 669 TYR A CD1 4916 C CD2 . TYR A 634 ? 0.4848 0.2777 0.3446 -0.0569 0.0298 0.0759 669 TYR A CD2 4917 C CE1 . TYR A 634 ? 0.4610 0.2907 0.3370 -0.0470 0.0231 0.0668 669 TYR A CE1 4918 C CE2 . TYR A 634 ? 0.4870 0.2846 0.3582 -0.0518 0.0293 0.0682 669 TYR A CE2 4919 C CZ . TYR A 634 ? 0.4803 0.2966 0.3596 -0.0467 0.0259 0.0639 669 TYR A CZ 4920 O OH . TYR A 634 ? 0.4509 0.2720 0.3406 -0.0421 0.0254 0.0568 669 TYR A OH 4921 N N . LYS A 635 ? 0.6217 0.4047 0.4339 -0.0675 0.0253 0.1121 670 LYS A N 4922 C CA . LYS A 635 ? 0.6434 0.4262 0.4407 -0.0735 0.0251 0.1207 670 LYS A CA 4923 C C . LYS A 635 ? 0.6383 0.4274 0.4312 -0.0654 0.0177 0.1292 670 LYS A C 4924 O O . LYS A 635 ? 0.6572 0.4594 0.4427 -0.0694 0.0162 0.1309 670 LYS A O 4925 C CB . LYS A 635 ? 0.7276 0.4872 0.5135 -0.0794 0.0289 0.1287 670 LYS A CB 4926 C CG . LYS A 635 ? 0.7926 0.5522 0.5741 -0.0933 0.0364 0.1239 670 LYS A CG 4927 C CD . LYS A 635 ? 0.8322 0.5883 0.6247 -0.0962 0.0411 0.1137 670 LYS A CD 4928 C CE . LYS A 635 ? 0.8932 0.6412 0.6788 -0.1100 0.0484 0.1128 670 LYS A CE 4929 N NZ . LYS A 635 ? 0.9386 0.6772 0.7325 -0.1129 0.0523 0.1053 670 LYS A NZ 4930 N N . ASN A 636 ? 0.6378 0.4181 0.4353 -0.0544 0.0132 0.1343 671 ASN A N 4931 C CA . ASN A 636 ? 0.6569 0.4430 0.4511 -0.0461 0.0057 0.1436 671 ASN A CA 4932 C C . ASN A 636 ? 0.6401 0.4497 0.4438 -0.0415 0.0012 0.1371 671 ASN A C 4933 O O . ASN A 636 ? 0.6379 0.4586 0.4368 -0.0389 -0.0043 0.1429 671 ASN A O 4934 C CB . ASN A 636 ? 0.6853 0.4539 0.4822 -0.0350 0.0027 0.1516 671 ASN A CB 4935 C CG . ASN A 636 ? 0.7120 0.4545 0.4979 -0.0391 0.0067 0.1596 671 ASN A CG 4936 O OD1 . ASN A 636 ? 0.7175 0.4567 0.4908 -0.0496 0.0099 0.1629 671 ASN A OD1 4937 N ND2 . ASN A 636 ? 0.7309 0.4543 0.5213 -0.0311 0.0071 0.1623 671 ASN A ND2 4938 N N . ASP A 637 ? 0.5953 0.4121 0.4118 -0.0408 0.0036 0.1255 672 ASP A N 4939 C CA . ASP A 637 ? 0.5655 0.4036 0.3905 -0.0381 0.0005 0.1184 672 ASP A CA 4940 C C . ASP A 637 ? 0.5548 0.4058 0.3740 -0.0482 0.0034 0.1130 672 ASP A C 4941 O O . ASP A 637 ? 0.5508 0.4026 0.3735 -0.0545 0.0091 0.1045 672 ASP A O 4942 C CB . ASP A 637 ? 0.5424 0.3827 0.3827 -0.0335 0.0020 0.1086 672 ASP A CB 4943 C CG . ASP A 637 ? 0.5237 0.3831 0.3728 -0.0285 -0.0023 0.1039 672 ASP A CG 4944 O OD1 . ASP A 637 ? 0.5104 0.3839 0.3551 -0.0330 -0.0037 0.1023 672 ASP A OD1 4945 O OD2 . ASP A 637 ? 0.5070 0.3671 0.3671 -0.0205 -0.0041 0.1015 672 ASP A OD2 4946 N N . LYS A 638 ? 0.5673 0.4290 0.3779 -0.0496 -0.0005 0.1176 673 LYS A N 4947 C CA . LYS A 638 ? 0.5699 0.4432 0.3729 -0.0591 0.0023 0.1130 673 LYS A CA 4948 C C . LYS A 638 ? 0.5411 0.4301 0.3542 -0.0595 0.0034 0.1010 673 LYS A C 4949 O O . LYS A 638 ? 0.5336 0.4304 0.3430 -0.0670 0.0075 0.0949 673 LYS A O 4950 C CB . LYS A 638 ? 0.6006 0.4803 0.3900 -0.0608 -0.0025 0.1217 673 LYS A CB 4951 C CG . LYS A 638 ? 0.6439 0.5086 0.4208 -0.0609 -0.0039 0.1351 673 LYS A CG 4952 C CD . LYS A 638 ? 0.6752 0.5244 0.4470 -0.0684 0.0035 0.1351 673 LYS A CD 4953 C CE . LYS A 638 ? 0.7421 0.5749 0.4999 -0.0694 0.0023 0.1489 673 LYS A CE 4954 N NZ . LYS A 638 ? 0.7673 0.5807 0.5247 -0.0736 0.0088 0.1491 673 LYS A NZ 4955 N N . GLN A 639 ? 0.5159 0.4092 0.3415 -0.0515 0.0000 0.0977 674 GLN A N 4956 C CA . GLN A 639 ? 0.4933 0.3995 0.3287 -0.0513 0.0009 0.0869 674 GLN A CA 4957 C C . GLN A 639 ? 0.4501 0.3516 0.2966 -0.0509 0.0057 0.0791 674 GLN A C 4958 O O . GLN A 639 ? 0.4310 0.3420 0.2844 -0.0520 0.0075 0.0703 674 GLN A O 4959 C CB . GLN A 639 ? 0.5182 0.4343 0.3602 -0.0438 -0.0056 0.0877 674 GLN A CB 4960 C CG . GLN A 639 ? 0.5882 0.5153 0.4206 -0.0458 -0.0104 0.0921 674 GLN A CG 4961 C CD . GLN A 639 ? 0.6927 0.6123 0.5132 -0.0457 -0.0133 0.1043 674 GLN A CD 4962 O OE1 . GLN A 639 ? 0.8179 0.7276 0.6412 -0.0388 -0.0158 0.1115 674 GLN A OE1 4963 N NE2 . GLN A 639 ? 0.7255 0.6490 0.5321 -0.0533 -0.0128 0.1067 674 GLN A NE2 4964 N N . MET A 640 ? 0.4361 0.3231 0.2841 -0.0494 0.0076 0.0821 675 MET A N 4965 C CA . MET A 640 ? 0.4162 0.2991 0.2752 -0.0482 0.0110 0.0749 675 MET A CA 4966 C C . MET A 640 ? 0.4175 0.2921 0.2733 -0.0561 0.0173 0.0728 675 MET A C 4967 O O . MET A 640 ? 0.4338 0.2968 0.2802 -0.0596 0.0187 0.0798 675 MET A O 4968 C CB . MET A 640 ? 0.4225 0.2961 0.2879 -0.0393 0.0080 0.0783 675 MET A CB 4969 C CG . MET A 640 ? 0.4212 0.2929 0.2981 -0.0372 0.0106 0.0704 675 MET A CG 4970 S SD . MET A 640 ? 0.4072 0.2973 0.2946 -0.0362 0.0100 0.0604 675 MET A SD 4971 C CE . MET A 640 ? 0.4091 0.3070 0.2993 -0.0275 0.0031 0.0648 675 MET A CE 4972 N N . SER A 641 ? 0.3890 0.2701 0.2526 -0.0592 0.0212 0.0637 676 SER A N 4973 C CA . SER A 641 ? 0.3927 0.2680 0.2562 -0.0663 0.0269 0.0607 676 SER A CA 4974 C C . SER A 641 ? 0.3904 0.2616 0.2647 -0.0631 0.0276 0.0554 676 SER A C 4975 O O . SER A 641 ? 0.3807 0.2485 0.2597 -0.0553 0.0239 0.0566 676 SER A O 4976 C CB . SER A 641 ? 0.3944 0.2828 0.2574 -0.0733 0.0310 0.0548 676 SER A CB 4977 O OG . SER A 641 ? 0.4044 0.2889 0.2669 -0.0809 0.0366 0.0527 676 SER A OG 4978 N N . TYR A 642 ? 0.3987 0.2710 0.2769 -0.0691 0.0323 0.0495 677 TYR A N 4979 C CA . TYR A 642 ? 0.3887 0.2585 0.2763 -0.0673 0.0330 0.0439 677 TYR A CA 4980 C C . TYR A 642 ? 0.3790 0.2617 0.2739 -0.0722 0.0364 0.0356 677 TYR A C 4981 O O . TYR A 642 ? 0.3789 0.2686 0.2707 -0.0787 0.0397 0.0346 677 TYR A O 4982 C CB . TYR A 642 ? 0.4218 0.2726 0.3053 -0.0695 0.0349 0.0473 677 TYR A CB 4983 C CG . TYR A 642 ? 0.4336 0.2796 0.3104 -0.0802 0.0401 0.0482 677 TYR A CG 4984 C CD1 . TYR A 642 ? 0.4623 0.3011 0.3273 -0.0840 0.0409 0.0561 677 TYR A CD1 4985 C CD2 . TYR A 642 ? 0.4319 0.2820 0.3143 -0.0871 0.0442 0.0411 677 TYR A CD2 4986 C CE1 . TYR A 642 ? 0.4886 0.3234 0.3472 -0.0945 0.0460 0.0569 677 TYR A CE1 4987 C CE2 . TYR A 642 ? 0.4594 0.3069 0.3363 -0.0976 0.0491 0.0417 677 TYR A CE2 4988 C CZ . TYR A 642 ? 0.4829 0.3224 0.3479 -0.1014 0.0503 0.0496 677 TYR A CZ 4989 O OH . TYR A 642 ? 0.5046 0.3418 0.3639 -0.1125 0.0556 0.0502 677 TYR A OH 4990 N N . GLY A 643 ? 0.3524 0.2389 0.2569 -0.0688 0.0355 0.0298 678 GLY A N 4991 C CA . GLY A 643 ? 0.3279 0.2262 0.2404 -0.0725 0.0380 0.0223 678 GLY A CA 4992 C C . GLY A 643 ? 0.3256 0.2168 0.2422 -0.0739 0.0389 0.0190 678 GLY A C 4993 O O . GLY A 643 ? 0.3310 0.2068 0.2437 -0.0722 0.0382 0.0224 678 GLY A O 4994 N N . PHE A 644 ? 0.3173 0.2199 0.2418 -0.0769 0.0404 0.0125 679 PHE A N 4995 C CA . PHE A 644 ? 0.3283 0.2274 0.2571 -0.0793 0.0411 0.0080 679 PHE A CA 4996 C C . PHE A 644 ? 0.3119 0.2231 0.2501 -0.0740 0.0384 0.0027 679 PHE A C 4997 O O . PHE A 644 ? 0.2878 0.2132 0.2307 -0.0718 0.0376 0.0010 679 PHE A O 4998 C CB . PHE A 644 ? 0.3439 0.2466 0.2730 -0.0896 0.0454 0.0052 679 PHE A CB 4999 C CG . PHE A 644 ? 0.3693 0.2580 0.2883 -0.0962 0.0486 0.0104 679 PHE A CG 5000 C CD1 . PHE A 644 ? 0.3952 0.2637 0.3081 -0.0969 0.0490 0.0133 679 PHE A CD1 5001 C CD2 . PHE A 644 ? 0.3969 0.2918 0.3121 -0.1012 0.0513 0.0127 679 PHE A CD2 5002 C CE1 . PHE A 644 ? 0.4454 0.2993 0.3483 -0.1028 0.0519 0.0189 679 PHE A CE1 5003 C CE2 . PHE A 644 ? 0.4312 0.3131 0.3363 -0.1075 0.0542 0.0181 679 PHE A CE2 5004 C CZ . PHE A 644 ? 0.4576 0.3184 0.3563 -0.1084 0.0544 0.0216 679 PHE A CZ 5005 N N . LEU A 645 ? 0.3049 0.2098 0.2451 -0.0721 0.0374 0.0001 680 LEU A N 5006 C CA . LEU A 645 ? 0.3009 0.2167 0.2489 -0.0677 0.0349 -0.0044 680 LEU A CA 5007 C C . LEU A 645 ? 0.3148 0.2437 0.2690 -0.0735 0.0361 -0.0099 680 LEU A C 5008 O O . LEU A 645 ? 0.2913 0.2351 0.2518 -0.0709 0.0347 -0.0119 680 LEU A O 5009 C CB . LEU A 645 ? 0.3014 0.2072 0.2491 -0.0628 0.0332 -0.0052 680 LEU A CB 5010 C CG . LEU A 645 ? 0.3100 0.2088 0.2550 -0.0547 0.0309 -0.0002 680 LEU A CG 5011 C CD1 . LEU A 645 ? 0.3241 0.2122 0.2690 -0.0506 0.0304 -0.0015 680 LEU A CD1 5012 C CD2 . LEU A 645 ? 0.3056 0.2180 0.2551 -0.0492 0.0279 -0.0001 680 LEU A CD2 5013 N N . PHE A 646 ? 0.3159 0.2398 0.2683 -0.0814 0.0388 -0.0122 681 PHE A N 5014 C CA . PHE A 646 ? 0.3184 0.2573 0.2766 -0.0882 0.0402 -0.0165 681 PHE A CA 5015 C C . PHE A 646 ? 0.3352 0.2796 0.2922 -0.0925 0.0432 -0.0140 681 PHE A C 5016 O O . PHE A 646 ? 0.3507 0.2824 0.3000 -0.0971 0.0458 -0.0106 681 PHE A O 5017 C CB . PHE A 646 ? 0.3204 0.2546 0.2777 -0.0967 0.0421 -0.0206 681 PHE A CB 5018 C CG . PHE A 646 ? 0.3187 0.2711 0.2827 -0.1038 0.0433 -0.0246 681 PHE A CG 5019 C CD1 . PHE A 646 ? 0.2963 0.2663 0.2688 -0.1009 0.0403 -0.0283 681 PHE A CD1 5020 C CD2 . PHE A 646 ? 0.3383 0.2916 0.3005 -0.1129 0.0472 -0.0242 681 PHE A CD2 5021 C CE1 . PHE A 646 ? 0.2854 0.2746 0.2655 -0.1062 0.0410 -0.0313 681 PHE A CE1 5022 C CE2 . PHE A 646 ? 0.3236 0.2965 0.2935 -0.1191 0.0482 -0.0278 681 PHE A CE2 5023 C CZ . PHE A 646 ? 0.3059 0.2971 0.2851 -0.1153 0.0450 -0.0313 681 PHE A CZ 5024 N N . PRO A 647 ? 0.3325 0.2953 0.2968 -0.0912 0.0430 -0.0157 682 PRO A N 5025 C CA . PRO A 647 ? 0.3612 0.3302 0.3244 -0.0947 0.0463 -0.0140 682 PRO A CA 5026 C C . PRO A 647 ? 0.3673 0.3406 0.3310 -0.1058 0.0505 -0.0160 682 PRO A C 5027 O O . PRO A 647 ? 0.3510 0.3375 0.3225 -0.1090 0.0503 -0.0205 682 PRO A O 5028 C CB . PRO A 647 ? 0.3337 0.3208 0.3057 -0.0892 0.0451 -0.0163 682 PRO A CB 5029 C CG . PRO A 647 ? 0.3525 0.3468 0.3316 -0.0862 0.0418 -0.0197 682 PRO A CG 5030 C CD . PRO A 647 ? 0.3479 0.3260 0.3212 -0.0862 0.0401 -0.0192 682 PRO A CD 5031 N N . PRO A 648 ? 0.4105 0.3740 0.3660 -0.1118 0.0541 -0.0124 683 PRO A N 5032 C CA . PRO A 648 ? 0.4220 0.3909 0.3780 -0.1232 0.0585 -0.0142 683 PRO A CA 5033 C C . PRO A 648 ? 0.3953 0.3893 0.3622 -0.1245 0.0602 -0.0182 683 PRO A C 5034 O O . PRO A 648 ? 0.3840 0.3876 0.3554 -0.1332 0.0626 -0.0215 683 PRO A O 5035 C CB . PRO A 648 ? 0.4673 0.4228 0.4120 -0.1272 0.0619 -0.0085 683 PRO A CB 5036 C CG . PRO A 648 ? 0.4616 0.3996 0.3989 -0.1190 0.0585 -0.0037 683 PRO A CG 5037 C CD . PRO A 648 ? 0.4415 0.3891 0.3865 -0.1089 0.0541 -0.0063 683 PRO A CD 5038 N N . TYR A 649 ? 0.3626 0.3666 0.3339 -0.1160 0.0589 -0.0181 684 TYR A N 5039 C CA . TYR A 649 ? 0.3631 0.3902 0.3455 -0.1149 0.0604 -0.0217 684 TYR A CA 5040 C C . TYR A 649 ? 0.3376 0.3798 0.3314 -0.1148 0.0579 -0.0262 684 TYR A C 5041 O O . TYR A 649 ? 0.3281 0.3903 0.3315 -0.1165 0.0597 -0.0291 684 TYR A O 5042 C CB . TYR A 649 ? 0.3814 0.4131 0.3658 -0.1046 0.0592 -0.0210 684 TYR A CB 5043 C CG . TYR A 649 ? 0.4347 0.4532 0.4079 -0.1033 0.0606 -0.0167 684 TYR A CG 5044 C CD1 . TYR A 649 ? 0.4826 0.5039 0.4513 -0.1091 0.0658 -0.0157 684 TYR A CD1 5045 C CD2 . TYR A 649 ? 0.4714 0.4759 0.4383 -0.0963 0.0566 -0.0135 684 TYR A CD2 5046 C CE1 . TYR A 649 ? 0.5197 0.5298 0.4772 -0.1083 0.0667 -0.0115 684 TYR A CE1 5047 C CE2 . TYR A 649 ? 0.5188 0.5127 0.4754 -0.0954 0.0572 -0.0093 684 TYR A CE2 5048 C CZ . TYR A 649 ? 0.5329 0.5295 0.4845 -0.1014 0.0621 -0.0082 684 TYR A CZ 5049 O OH . TYR A 649 ? 0.5716 0.5588 0.5122 -0.1009 0.0624 -0.0039 684 TYR A OH 5050 N N . LEU A 650 ? 0.3212 0.3551 0.3139 -0.1122 0.0535 -0.0267 685 LEU A N 5051 C CA . LEU A 650 ? 0.3267 0.3746 0.3288 -0.1121 0.0505 -0.0307 685 LEU A CA 5052 C C . LEU A 650 ? 0.3257 0.3696 0.3256 -0.1225 0.0509 -0.0334 685 LEU A C 5053 O O . LEU A 650 ? 0.3354 0.3873 0.3404 -0.1227 0.0477 -0.0366 685 LEU A O 5054 C CB . LEU A 650 ? 0.3350 0.3803 0.3384 -0.1016 0.0453 -0.0303 685 LEU A CB 5055 C CG . LEU A 650 ? 0.3401 0.3894 0.3460 -0.0917 0.0448 -0.0283 685 LEU A CG 5056 C CD1 . LEU A 650 ? 0.3383 0.3832 0.3444 -0.0826 0.0400 -0.0275 685 LEU A CD1 5057 C CD2 . LEU A 650 ? 0.3403 0.4116 0.3573 -0.0907 0.0464 -0.0304 685 LEU A CD2 5058 N N . SER A 651 ? 0.3177 0.3494 0.3097 -0.1315 0.0550 -0.0321 686 SER A N 5059 C CA . SER A 651 ? 0.3385 0.3655 0.3279 -0.1431 0.0564 -0.0351 686 SER A CA 5060 C C . SER A 651 ? 0.3365 0.3889 0.3374 -0.1492 0.0562 -0.0400 686 SER A C 5061 O O . SER A 651 ? 0.3380 0.4104 0.3478 -0.1476 0.0576 -0.0402 686 SER A O 5062 C CB . SER A 651 ? 0.3658 0.3781 0.3456 -0.1523 0.0616 -0.0323 686 SER A CB 5063 O OG . SER A 651 ? 0.3654 0.3932 0.3496 -0.1549 0.0653 -0.0316 686 SER A OG 5064 N N . SER A 652 ? 0.3418 0.3938 0.3426 -0.1563 0.0548 -0.0440 687 SER A N 5065 C CA . SER A 652 ? 0.3417 0.4186 0.3532 -0.1627 0.0536 -0.0488 687 SER A CA 5066 C C . SER A 652 ? 0.3539 0.4382 0.3664 -0.1766 0.0588 -0.0505 687 SER A C 5067 O O . SER A 652 ? 0.3455 0.4552 0.3690 -0.1815 0.0585 -0.0537 687 SER A O 5068 C CB . SER A 652 ? 0.3551 0.4287 0.3648 -0.1656 0.0498 -0.0530 687 SER A CB 5069 O OG . SER A 652 ? 0.3812 0.4294 0.3788 -0.1733 0.0523 -0.0539 687 SER A OG 5070 N N . SER A 653 ? 0.3648 0.4275 0.3660 -0.1830 0.0634 -0.0479 688 SER A N 5071 C CA . SER A 653 ? 0.3919 0.4587 0.3922 -0.1969 0.0690 -0.0487 688 SER A CA 5072 C C . SER A 653 ? 0.4077 0.4502 0.3951 -0.1987 0.0735 -0.0433 688 SER A C 5073 O O . SER A 653 ? 0.3891 0.4091 0.3675 -0.1910 0.0719 -0.0396 688 SER A O 5074 C CB . SER A 653 ? 0.4044 0.4685 0.4025 -0.2105 0.0692 -0.0539 688 SER A CB 5075 O OG . SER A 653 ? 0.4108 0.4434 0.3955 -0.2114 0.0693 -0.0530 688 SER A OG 5076 N N . PRO A 654 ? 0.4428 0.4902 0.4291 -0.2092 0.0793 -0.0424 689 PRO A N 5077 C CA . PRO A 654 ? 0.4664 0.4892 0.4386 -0.2126 0.0836 -0.0366 689 PRO A CA 5078 C C . PRO A 654 ? 0.4946 0.4860 0.4538 -0.2168 0.0834 -0.0355 689 PRO A C 5079 O O . PRO A 654 ? 0.5227 0.4902 0.4708 -0.2117 0.0837 -0.0298 689 PRO A O 5080 C CB . PRO A 654 ? 0.4826 0.5192 0.4570 -0.2261 0.0899 -0.0374 689 PRO A CB 5081 C CG . PRO A 654 ? 0.4600 0.5320 0.4517 -0.2239 0.0886 -0.0421 689 PRO A CG 5082 C CD . PRO A 654 ? 0.4452 0.5217 0.4431 -0.2181 0.0821 -0.0461 689 PRO A CD 5083 N N . GLU A 655 ? 0.4903 0.4827 0.4514 -0.2256 0.0827 -0.0412 690 GLU A N 5084 C CA . GLU A 655 ? 0.5180 0.4815 0.4679 -0.2292 0.0825 -0.0419 690 GLU A CA 5085 C C . GLU A 655 ? 0.4904 0.4391 0.4372 -0.2140 0.0778 -0.0398 690 GLU A C 5086 O O . GLU A 655 ? 0.4864 0.4079 0.4220 -0.2103 0.0786 -0.0350 690 GLU A O 5087 C CB . GLU A 655 ? 0.5442 0.5162 0.4982 -0.2405 0.0820 -0.0499 690 GLU A CB 5088 C CG . GLU A 655 ? 0.5960 0.5774 0.5509 -0.2585 0.0872 -0.0525 690 GLU A CG 5089 C CD . GLU A 655 ? 0.6117 0.6315 0.5820 -0.2604 0.0872 -0.0548 690 GLU A CD 5090 O OE1 . GLU A 655 ? 0.5820 0.6213 0.5626 -0.2476 0.0829 -0.0547 690 GLU A OE1 5091 O OE2 . GLU A 655 ? 0.6403 0.6710 0.6125 -0.2750 0.0917 -0.0567 690 GLU A OE2 5092 N N . ALA A 656 ? 0.4548 0.4227 0.4119 -0.2051 0.0728 -0.0430 691 ALA A N 5093 C CA . ALA A 656 ? 0.4421 0.3998 0.3977 -0.1912 0.0682 -0.0417 691 ALA A CA 5094 C C . ALA A 656 ? 0.4382 0.3870 0.3897 -0.1800 0.0679 -0.0343 691 ALA A C 5095 O O . ALA A 656 ? 0.4340 0.3650 0.3798 -0.1711 0.0658 -0.0317 691 ALA A O 5096 C CB . ALA A 656 ? 0.4179 0.3994 0.3852 -0.1851 0.0631 -0.0463 691 ALA A CB 5097 N N . LYS A 657 ? 0.4248 0.3861 0.3790 -0.1807 0.0703 -0.0313 692 LYS A N 5098 C CA . LYS A 657 ? 0.4379 0.3921 0.3875 -0.1711 0.0701 -0.0248 692 LYS A CA 5099 C C . LYS A 657 ? 0.4483 0.3719 0.3838 -0.1708 0.0714 -0.0189 692 LYS A C 5100 O O . LYS A 657 ? 0.4177 0.3321 0.3494 -0.1603 0.0690 -0.0143 692 LYS A O 5101 C CB . LYS A 657 ? 0.4455 0.4175 0.3990 -0.1737 0.0734 -0.0233 692 LYS A CB 5102 C CG . LYS A 657 ? 0.4509 0.4236 0.4030 -0.1624 0.0721 -0.0188 692 LYS A CG 5103 C CD . LYS A 657 ? 0.4774 0.4633 0.4303 -0.1664 0.0767 -0.0173 692 LYS A CD 5104 C CE . LYS A 657 ? 0.4762 0.4920 0.4437 -0.1659 0.0772 -0.0226 692 LYS A CE 5105 N NZ . LYS A 657 ? 0.4996 0.5249 0.4734 -0.1524 0.0737 -0.0228 692 LYS A NZ 5106 N N . TYR A 658 ? 0.4672 0.3752 0.3953 -0.1823 0.0751 -0.0191 693 TYR A N 5107 C CA . TYR A 658 ? 0.4982 0.3752 0.4129 -0.1821 0.0765 -0.0134 693 TYR A CA 5108 C C . TYR A 658 ? 0.4823 0.3438 0.3949 -0.1705 0.0724 -0.0129 693 TYR A C 5109 O O . TYR A 658 ? 0.4803 0.3225 0.3847 -0.1643 0.0719 -0.0063 693 TYR A O 5110 C CB . TYR A 658 ? 0.5515 0.4136 0.4589 -0.1972 0.0815 -0.0147 693 TYR A CB 5111 C CG . TYR A 658 ? 0.5848 0.4512 0.4882 -0.2075 0.0865 -0.0109 693 TYR A CG 5112 C CD1 . TYR A 658 ? 0.5845 0.4779 0.4972 -0.2161 0.0888 -0.0156 693 TYR A CD1 5113 C CD2 . TYR A 658 ? 0.6226 0.4675 0.5131 -0.2082 0.0890 -0.0024 693 TYR A CD2 5114 C CE1 . TYR A 658 ? 0.6241 0.5231 0.5334 -0.2255 0.0939 -0.0124 693 TYR A CE1 5115 C CE2 . TYR A 658 ? 0.6493 0.4987 0.5352 -0.2180 0.0939 0.0012 693 TYR A CE2 5116 C CZ . TYR A 658 ? 0.6509 0.5275 0.5463 -0.2269 0.0966 -0.0040 693 TYR A CZ 5117 O OH . TYR A 658 ? 0.6592 0.5414 0.5502 -0.2368 0.1020 -0.0008 693 TYR A OH 5118 N N . ASP A 659 ? 0.4780 0.3490 0.3983 -0.1677 0.0694 -0.0196 694 ASP A N 5119 C CA . ASP A 659 ? 0.4784 0.3381 0.3981 -0.1568 0.0657 -0.0202 694 ASP A CA 5120 C C . ASP A 659 ? 0.4408 0.3048 0.3623 -0.1431 0.0621 -0.0151 694 ASP A C 5121 O O . ASP A 659 ? 0.4451 0.2942 0.3629 -0.1341 0.0600 -0.0122 694 ASP A O 5122 C CB . ASP A 659 ? 0.4830 0.3571 0.4110 -0.1570 0.0631 -0.0284 694 ASP A CB 5123 C CG . ASP A 659 ? 0.5424 0.4093 0.4676 -0.1696 0.0660 -0.0347 694 ASP A CG 5124 O OD1 . ASP A 659 ? 0.5830 0.4270 0.4986 -0.1765 0.0699 -0.0328 694 ASP A OD1 5125 O OD2 . ASP A 659 ? 0.5385 0.4227 0.4709 -0.1729 0.0641 -0.0415 694 ASP A OD2 5126 N N . ALA A 660 ? 0.4173 0.3026 0.3452 -0.1415 0.0613 -0.0144 695 ALA A N 5127 C CA . ALA A 660 ? 0.3908 0.2817 0.3205 -0.1299 0.0580 -0.0106 695 ALA A CA 5128 C C . ALA A 660 ? 0.4043 0.2785 0.3240 -0.1269 0.0588 -0.0023 695 ALA A C 5129 O O . ALA A 660 ? 0.3911 0.2646 0.3104 -0.1169 0.0556 0.0011 695 ALA A O 5130 C CB . ALA A 660 ? 0.3795 0.2963 0.3183 -0.1292 0.0575 -0.0127 695 ALA A CB 5131 N N . PHE A 661 ? 0.4226 0.2834 0.3338 -0.1359 0.0628 0.0009 696 PHE A N 5132 C CA . PHE A 661 ? 0.4444 0.2876 0.3447 -0.1337 0.0634 0.0096 696 PHE A CA 5133 C C . PHE A 661 ? 0.4595 0.2760 0.3525 -0.1303 0.0630 0.0128 696 PHE A C 5134 O O . PHE A 661 ? 0.4699 0.2695 0.3532 -0.1290 0.0635 0.0207 696 PHE A O 5135 C CB . PHE A 661 ? 0.4719 0.3159 0.3662 -0.1449 0.0683 0.0126 696 PHE A CB 5136 C CG . PHE A 661 ? 0.4809 0.3508 0.3823 -0.1466 0.0691 0.0099 696 PHE A CG 5137 C CD1 . PHE A 661 ? 0.4903 0.3678 0.3907 -0.1394 0.0673 0.0136 696 PHE A CD1 5138 C CD2 . PHE A 661 ? 0.5099 0.3970 0.4194 -0.1551 0.0717 0.0033 696 PHE A CD2 5139 C CE1 . PHE A 661 ? 0.4991 0.3992 0.4059 -0.1404 0.0687 0.0106 696 PHE A CE1 5140 C CE2 . PHE A 661 ? 0.5032 0.4144 0.4202 -0.1554 0.0728 0.0007 696 PHE A CE2 5141 C CZ . PHE A 661 ? 0.4948 0.4117 0.4104 -0.1479 0.0715 0.0042 696 PHE A CZ 5142 N N . LEU A 662 ? 0.4485 0.2610 0.3458 -0.1284 0.0620 0.0069 697 LEU A N 5143 C CA . LEU A 662 ? 0.4635 0.2516 0.3551 -0.1232 0.0617 0.0091 697 LEU A CA 5144 C C . LEU A 662 ? 0.4495 0.2351 0.3409 -0.1094 0.0574 0.0151 697 LEU A C 5145 O O . LEU A 662 ? 0.4170 0.2212 0.3155 -0.1026 0.0539 0.0138 697 LEU A O 5146 C CB . LEU A 662 ? 0.4706 0.2571 0.3670 -0.1239 0.0618 0.0005 697 LEU A CB 5147 C CG . LEU A 662 ? 0.4874 0.2726 0.3829 -0.1381 0.0659 -0.0058 697 LEU A CG 5148 C CD1 . LEU A 662 ? 0.4843 0.2782 0.3867 -0.1382 0.0645 -0.0152 697 LEU A CD1 5149 C CD2 . LEU A 662 ? 0.5294 0.2851 0.4136 -0.1439 0.0701 -0.0025 697 LEU A CD2 5150 N N . VAL A 663 ? 0.4729 0.2355 0.3561 -0.1055 0.0578 0.0218 698 VAL A N 5151 C CA . VAL A 663 ? 0.4745 0.2329 0.3570 -0.0926 0.0538 0.0283 698 VAL A CA 5152 C C . VAL A 663 ? 0.4507 0.2167 0.3422 -0.0828 0.0506 0.0231 698 VAL A C 5153 O O . VAL A 663 ? 0.4431 0.2155 0.3374 -0.0726 0.0466 0.0266 698 VAL A O 5154 C CB . VAL A 663 ? 0.5056 0.2359 0.3780 -0.0905 0.0552 0.0363 698 VAL A CB 5155 C CG1 . VAL A 663 ? 0.5285 0.2395 0.4007 -0.0899 0.0578 0.0314 698 VAL A CG1 5156 C CG2 . VAL A 663 ? 0.5053 0.2339 0.3760 -0.0784 0.0508 0.0450 698 VAL A CG2 5157 N N . THR A 664 ? 0.4428 0.2090 0.3382 -0.0866 0.0524 0.0145 699 THR A N 5158 C CA . THR A 664 ? 0.4305 0.2049 0.3339 -0.0792 0.0501 0.0086 699 THR A CA 5159 C C . THR A 664 ? 0.4005 0.2019 0.3124 -0.0785 0.0471 0.0046 699 THR A C 5160 O O . THR A 664 ? 0.3895 0.1991 0.3077 -0.0726 0.0450 0.0003 699 THR A O 5161 C CB . THR A 664 ? 0.4499 0.2130 0.3528 -0.0841 0.0533 0.0008 699 THR A CB 5162 O OG1 . THR A 664 ? 0.4521 0.2187 0.3534 -0.0976 0.0564 -0.0033 699 THR A OG1 5163 C CG2 . THR A 664 ? 0.4816 0.2169 0.3775 -0.0804 0.0557 0.0043 699 THR A CG2 5164 N N . ASN A 665 ? 0.3834 0.1978 0.2956 -0.0846 0.0475 0.0059 700 ASN A N 5165 C CA . ASN A 665 ? 0.3611 0.1999 0.2811 -0.0834 0.0451 0.0030 700 ASN A CA 5166 C C . ASN A 665 ? 0.3683 0.2136 0.2871 -0.0778 0.0426 0.0094 700 ASN A C 5167 O O . ASN A 665 ? 0.3509 0.2142 0.2751 -0.0761 0.0408 0.0077 700 ASN A O 5168 C CB . ASN A 665 ? 0.3626 0.2128 0.2848 -0.0945 0.0478 -0.0013 700 ASN A CB 5169 C CG . ASN A 665 ? 0.3347 0.2097 0.2660 -0.0932 0.0457 -0.0051 700 ASN A CG 5170 O OD1 . ASN A 665 ? 0.3254 0.2089 0.2626 -0.0866 0.0427 -0.0079 700 ASN A OD1 5171 N ND2 . ASN A 665 ? 0.3266 0.2130 0.2590 -0.0996 0.0477 -0.0051 700 ASN A ND2 5172 N N . MET A 666 ? 0.3907 0.2213 0.3019 -0.0749 0.0424 0.0168 701 MET A N 5173 C CA . MET A 666 ? 0.3917 0.2285 0.3000 -0.0714 0.0402 0.0231 701 MET A CA 5174 C C . MET A 666 ? 0.3767 0.2166 0.2883 -0.0602 0.0357 0.0253 701 MET A C 5175 O O . MET A 666 ? 0.3973 0.2278 0.3105 -0.0542 0.0347 0.0250 701 MET A O 5176 C CB . MET A 666 ? 0.4478 0.2697 0.3452 -0.0759 0.0423 0.0308 701 MET A CB 5177 C CG . MET A 666 ? 0.4866 0.2915 0.3784 -0.0682 0.0402 0.0384 701 MET A CG 5178 S SD . MET A 666 ? 0.5754 0.3601 0.4535 -0.0742 0.0429 0.0478 701 MET A SD 5179 C CE . MET A 666 ? 0.4827 0.2857 0.3577 -0.0787 0.0424 0.0502 701 MET A CE 5180 N N . VAL A 667 ? 0.3470 0.2007 0.2599 -0.0575 0.0332 0.0268 702 VAL A N 5181 C CA . VAL A 667 ? 0.3383 0.1968 0.2543 -0.0481 0.0289 0.0288 702 VAL A CA 5182 C C . VAL A 667 ? 0.3429 0.2066 0.2535 -0.0473 0.0268 0.0348 702 VAL A C 5183 O O . VAL A 667 ? 0.3452 0.2153 0.2528 -0.0536 0.0287 0.0344 702 VAL A O 5184 C CB . VAL A 667 ? 0.3237 0.1972 0.2491 -0.0452 0.0274 0.0220 702 VAL A CB 5185 C CG1 . VAL A 667 ? 0.3364 0.2045 0.2663 -0.0440 0.0284 0.0170 702 VAL A CG1 5186 C CG2 . VAL A 667 ? 0.3088 0.1964 0.2368 -0.0511 0.0290 0.0178 702 VAL A CG2 5187 N N . PRO A 668 ? 0.3407 0.2028 0.2503 -0.0398 0.0229 0.0401 703 PRO A N 5188 C CA . PRO A 668 ? 0.3373 0.2046 0.2407 -0.0396 0.0205 0.0459 703 PRO A CA 5189 C C . PRO A 668 ? 0.3192 0.2042 0.2263 -0.0403 0.0194 0.0415 703 PRO A C 5190 O O . PRO A 668 ? 0.3066 0.1997 0.2217 -0.0361 0.0177 0.0370 703 PRO A O 5191 C CB . PRO A 668 ? 0.3492 0.2112 0.2523 -0.0308 0.0163 0.0522 703 PRO A CB 5192 C CG . PRO A 668 ? 0.3558 0.2166 0.2678 -0.0253 0.0162 0.0474 703 PRO A CG 5193 C CD . PRO A 668 ? 0.3501 0.2057 0.2638 -0.0314 0.0207 0.0411 703 PRO A CD 5194 N N . MET A 669 ? 0.3164 0.2065 0.2173 -0.0460 0.0208 0.0425 704 MET A N 5195 C CA . MET A 669 ? 0.3041 0.2090 0.2075 -0.0474 0.0207 0.0379 704 MET A CA 5196 C C . MET A 669 ? 0.3141 0.2224 0.2080 -0.0502 0.0199 0.0423 704 MET A C 5197 O O . MET A 669 ? 0.3098 0.2128 0.1956 -0.0558 0.0226 0.0457 704 MET A O 5198 C CB . MET A 669 ? 0.3011 0.2118 0.2091 -0.0527 0.0251 0.0310 704 MET A CB 5199 C CG . MET A 669 ? 0.3091 0.2201 0.2267 -0.0501 0.0252 0.0258 704 MET A CG 5200 S SD . MET A 669 ? 0.3012 0.2241 0.2262 -0.0547 0.0289 0.0178 704 MET A SD 5201 C CE . MET A 669 ? 0.2891 0.2123 0.2232 -0.0493 0.0266 0.0138 704 MET A CE 5202 N N . TYR A 670 ? 0.3042 0.2212 0.1983 -0.0469 0.0164 0.0423 705 TYR A N 5203 C CA . TYR A 670 ? 0.3155 0.2388 0.2012 -0.0506 0.0161 0.0439 705 TYR A CA 5204 C C . TYR A 670 ? 0.3089 0.2370 0.1932 -0.0574 0.0216 0.0386 705 TYR A C 5205 O O . TYR A 670 ? 0.2848 0.2173 0.1775 -0.0574 0.0241 0.0320 705 TYR A O 5206 C CB . TYR A 670 ? 0.3110 0.2445 0.1992 -0.0471 0.0123 0.0419 705 TYR A CB 5207 C CG . TYR A 670 ? 0.3355 0.2680 0.2250 -0.0406 0.0066 0.0474 705 TYR A CG 5208 C CD1 . TYR A 670 ? 0.3700 0.2985 0.2510 -0.0400 0.0034 0.0559 705 TYR A CD1 5209 C CD2 . TYR A 670 ? 0.3254 0.2618 0.2249 -0.0349 0.0043 0.0443 705 TYR A CD2 5210 C CE1 . TYR A 670 ? 0.3847 0.3140 0.2683 -0.0332 -0.0018 0.0611 705 TYR A CE1 5211 C CE2 . TYR A 670 ? 0.3480 0.2853 0.2498 -0.0288 -0.0005 0.0491 705 TYR A CE2 5212 C CZ . TYR A 670 ? 0.3729 0.3070 0.2672 -0.0277 -0.0036 0.0574 705 TYR A CZ 5213 O OH . TYR A 670 ? 0.4250 0.3617 0.3227 -0.0209 -0.0085 0.0624 705 TYR A OH 5214 N N . PRO A 671 ? 0.3252 0.2531 0.1989 -0.0631 0.0236 0.0416 706 PRO A N 5215 C CA . PRO A 671 ? 0.3307 0.2650 0.2031 -0.0694 0.0293 0.0362 706 PRO A CA 5216 C C . PRO A 671 ? 0.3142 0.2596 0.1934 -0.0677 0.0302 0.0281 706 PRO A C 5217 O O . PRO A 671 ? 0.3145 0.2648 0.1997 -0.0695 0.0346 0.0222 706 PRO A O 5218 C CB . PRO A 671 ? 0.3421 0.2759 0.2006 -0.0746 0.0299 0.0412 706 PRO A CB 5219 C CG . PRO A 671 ? 0.3585 0.2819 0.2110 -0.0721 0.0254 0.0508 706 PRO A CG 5220 C CD . PRO A 671 ? 0.3428 0.2645 0.2051 -0.0639 0.0208 0.0506 706 PRO A CD 5221 N N . ALA A 672 ? 0.3020 0.2513 0.1807 -0.0640 0.0261 0.0280 707 ALA A N 5222 C CA . ALA A 672 ? 0.2977 0.2551 0.1823 -0.0623 0.0268 0.0207 707 ALA A CA 5223 C C . ALA A 672 ? 0.2834 0.2414 0.1807 -0.0582 0.0273 0.0165 707 ALA A C 5224 O O . ALA A 672 ? 0.2674 0.2309 0.1703 -0.0584 0.0307 0.0103 707 ALA A O 5225 C CB . ALA A 672 ? 0.3070 0.2674 0.1886 -0.0598 0.0218 0.0219 707 ALA A CB 5226 N N . PHE A 673 ? 0.2866 0.2390 0.1881 -0.0544 0.0241 0.0199 708 PHE A N 5227 C CA . PHE A 673 ? 0.2737 0.2266 0.1861 -0.0510 0.0243 0.0162 708 PHE A CA 5228 C C . PHE A 673 ? 0.2785 0.2315 0.1943 -0.0545 0.0288 0.0135 708 PHE A C 5229 O O . PHE A 673 ? 0.2550 0.2129 0.1794 -0.0531 0.0301 0.0087 708 PHE A O 5230 C CB . PHE A 673 ? 0.2735 0.2206 0.1891 -0.0460 0.0202 0.0198 708 PHE A CB 5231 C CG . PHE A 673 ? 0.2575 0.2062 0.1832 -0.0429 0.0203 0.0156 708 PHE A CG 5232 C CD1 . PHE A 673 ? 0.2481 0.2034 0.1793 -0.0399 0.0190 0.0117 708 PHE A CD1 5233 C CD2 . PHE A 673 ? 0.2616 0.2053 0.1905 -0.0440 0.0220 0.0151 708 PHE A CD2 5234 C CE1 . PHE A 673 ? 0.2444 0.2016 0.1839 -0.0373 0.0191 0.0082 708 PHE A CE1 5235 C CE2 . PHE A 673 ? 0.2659 0.2123 0.2032 -0.0417 0.0220 0.0109 708 PHE A CE2 5236 C CZ . PHE A 673 ? 0.2486 0.2022 0.1913 -0.0383 0.0205 0.0078 708 PHE A CZ 5237 N N . LYS A 674 ? 0.2953 0.2432 0.2046 -0.0594 0.0311 0.0171 709 LYS A N 5238 C CA . LYS A 674 ? 0.2908 0.2398 0.2029 -0.0643 0.0357 0.0146 709 LYS A CA 5239 C C . LYS A 674 ? 0.2739 0.2344 0.1904 -0.0659 0.0398 0.0084 709 LYS A C 5240 O O . LYS A 674 ? 0.2518 0.2175 0.1757 -0.0675 0.0426 0.0046 709 LYS A O 5241 C CB . LYS A 674 ? 0.3169 0.2583 0.2194 -0.0703 0.0379 0.0198 709 LYS A CB 5242 C CG . LYS A 674 ? 0.3469 0.2753 0.2471 -0.0687 0.0352 0.0253 709 LYS A CG 5243 C CD . LYS A 674 ? 0.3899 0.3084 0.2794 -0.0742 0.0369 0.0318 709 LYS A CD 5244 C CE . LYS A 674 ? 0.4062 0.3259 0.2961 -0.0821 0.0427 0.0292 709 LYS A CE 5245 N NZ . LYS A 674 ? 0.4590 0.3675 0.3373 -0.0880 0.0445 0.0361 709 LYS A NZ 5246 N N . ARG A 675 ? 0.2696 0.2345 0.1817 -0.0655 0.0401 0.0071 710 ARG A N 5247 C CA . ARG A 675 ? 0.2755 0.2502 0.1923 -0.0656 0.0441 0.0007 710 ARG A CA 5248 C C . ARG A 675 ? 0.2570 0.2363 0.1859 -0.0602 0.0428 -0.0034 710 ARG A C 5249 O O . ARG A 675 ? 0.2535 0.2406 0.1900 -0.0603 0.0462 -0.0076 710 ARG A O 5250 C CB . ARG A 675 ? 0.2975 0.2743 0.2070 -0.0658 0.0446 -0.0006 710 ARG A CB 5251 C CG . ARG A 675 ? 0.3078 0.2826 0.2048 -0.0721 0.0468 0.0028 710 ARG A CG 5252 C CD . ARG A 675 ? 0.3239 0.3015 0.2132 -0.0729 0.0472 0.0006 710 ARG A CD 5253 N NE . ARG A 675 ? 0.3296 0.3148 0.2238 -0.0725 0.0526 -0.0070 710 ARG A NE 5254 C CZ . ARG A 675 ? 0.3274 0.3147 0.2191 -0.0713 0.0536 -0.0116 710 ARG A CZ 5255 N NH1 . ARG A 675 ? 0.3451 0.3289 0.2294 -0.0711 0.0493 -0.0098 710 ARG A NH1 5256 N NH2 . ARG A 675 ? 0.3430 0.3362 0.2402 -0.0702 0.0591 -0.0184 710 ARG A NH2 5257 N N . VAL A 676 ? 0.2430 0.2180 0.1735 -0.0555 0.0379 -0.0017 711 VAL A N 5258 C CA . VAL A 676 ? 0.2414 0.2195 0.1818 -0.0504 0.0360 -0.0047 711 VAL A CA 5259 C C . VAL A 676 ? 0.2314 0.2101 0.1782 -0.0512 0.0363 -0.0048 711 VAL A C 5260 O O . VAL A 676 ? 0.2280 0.2143 0.1830 -0.0503 0.0379 -0.0085 711 VAL A O 5261 C CB . VAL A 676 ? 0.2232 0.1968 0.1625 -0.0462 0.0310 -0.0025 711 VAL A CB 5262 C CG1 . VAL A 676 ? 0.2207 0.1969 0.1691 -0.0415 0.0291 -0.0049 711 VAL A CG1 5263 C CG2 . VAL A 676 ? 0.2437 0.2179 0.1766 -0.0463 0.0307 -0.0032 711 VAL A CG2 5264 N N . TRP A 677 ? 0.2314 0.2021 0.1742 -0.0530 0.0347 -0.0008 712 TRP A N 5265 C CA . TRP A 677 ? 0.2300 0.1988 0.1774 -0.0544 0.0346 -0.0011 712 TRP A CA 5266 C C . TRP A 677 ? 0.2516 0.2272 0.2023 -0.0597 0.0390 -0.0038 712 TRP A C 5267 O O . TRP A 677 ? 0.2670 0.2487 0.2256 -0.0596 0.0391 -0.0069 712 TRP A O 5268 C CB . TRP A 677 ? 0.2476 0.2042 0.1888 -0.0552 0.0328 0.0037 712 TRP A CB 5269 C CG . TRP A 677 ? 0.2526 0.2051 0.1980 -0.0556 0.0322 0.0027 712 TRP A CG 5270 C CD1 . TRP A 677 ? 0.2721 0.2182 0.2151 -0.0611 0.0345 0.0036 712 TRP A CD1 5271 C CD2 . TRP A 677 ? 0.2597 0.2137 0.2115 -0.0511 0.0295 0.0004 712 TRP A CD2 5272 N NE1 . TRP A 677 ? 0.2862 0.2298 0.2338 -0.0603 0.0334 0.0013 712 TRP A NE1 5273 C CE2 . TRP A 677 ? 0.2713 0.2201 0.2242 -0.0541 0.0303 -0.0005 712 TRP A CE2 5274 C CE3 . TRP A 677 ? 0.2619 0.2210 0.2180 -0.0455 0.0268 -0.0010 712 TRP A CE3 5275 C CZ2 . TRP A 677 ? 0.2812 0.2302 0.2390 -0.0515 0.0285 -0.0031 712 TRP A CZ2 5276 C CZ3 . TRP A 677 ? 0.2786 0.2381 0.2397 -0.0428 0.0249 -0.0030 712 TRP A CZ3 5277 C CH2 . TRP A 677 ? 0.2844 0.2392 0.2462 -0.0457 0.0257 -0.0042 712 TRP A CH2 5278 N N . ALA A 678 ? 0.2556 0.2317 0.2004 -0.0645 0.0425 -0.0027 713 ALA A N 5279 C CA . ALA A 678 ? 0.2689 0.2527 0.2169 -0.0702 0.0471 -0.0052 713 ALA A CA 5280 C C . ALA A 678 ? 0.2596 0.2576 0.2179 -0.0674 0.0488 -0.0106 713 ALA A C 5281 O O . ALA A 678 ? 0.2601 0.2668 0.2259 -0.0700 0.0506 -0.0132 713 ALA A O 5282 C CB . ALA A 678 ? 0.2733 0.2550 0.2120 -0.0760 0.0508 -0.0029 713 ALA A CB 5283 N N . TYR A 679 ? 0.2555 0.2559 0.2142 -0.0620 0.0481 -0.0121 714 TYR A N 5284 C CA . TYR A 679 ? 0.2505 0.2624 0.2188 -0.0578 0.0495 -0.0166 714 TYR A CA 5285 C C . TYR A 679 ? 0.2333 0.2480 0.2103 -0.0538 0.0458 -0.0174 714 TYR A C 5286 O O . TYR A 679 ? 0.2387 0.2646 0.2250 -0.0533 0.0469 -0.0201 714 TYR A O 5287 C CB . TYR A 679 ? 0.2688 0.2795 0.2340 -0.0535 0.0498 -0.0180 714 TYR A CB 5288 C CG . TYR A 679 ? 0.2935 0.3145 0.2680 -0.0488 0.0523 -0.0225 714 TYR A CG 5289 C CD1 . TYR A 679 ? 0.3137 0.3444 0.2912 -0.0509 0.0581 -0.0259 714 TYR A CD1 5290 C CD2 . TYR A 679 ? 0.2939 0.3147 0.2741 -0.0422 0.0492 -0.0233 714 TYR A CD2 5291 C CE1 . TYR A 679 ? 0.3332 0.3733 0.3203 -0.0454 0.0604 -0.0299 714 TYR A CE1 5292 C CE2 . TYR A 679 ? 0.3086 0.3374 0.2971 -0.0372 0.0512 -0.0267 714 TYR A CE2 5293 C CZ . TYR A 679 ? 0.3315 0.3698 0.3239 -0.0383 0.0567 -0.0300 714 TYR A CZ 5294 O OH . TYR A 679 ? 0.3809 0.4267 0.3824 -0.0318 0.0586 -0.0331 714 TYR A OH 5295 N N . PHE A 680 ? 0.2255 0.2313 0.1996 -0.0513 0.0413 -0.0149 715 PHE A N 5296 C CA . PHE A 680 ? 0.2231 0.2307 0.2036 -0.0484 0.0379 -0.0155 715 PHE A CA 5297 C C . PHE A 680 ? 0.2391 0.2516 0.2237 -0.0536 0.0389 -0.0166 715 PHE A C 5298 O O . PHE A 680 ? 0.2189 0.2421 0.2122 -0.0524 0.0384 -0.0190 715 PHE A O 5299 C CB . PHE A 680 ? 0.2221 0.2186 0.1976 -0.0460 0.0338 -0.0126 715 PHE A CB 5300 C CG . PHE A 680 ? 0.2204 0.2172 0.2003 -0.0448 0.0309 -0.0132 715 PHE A CG 5301 C CD1 . PHE A 680 ? 0.2276 0.2327 0.2148 -0.0408 0.0294 -0.0152 715 PHE A CD1 5302 C CD2 . PHE A 680 ? 0.2442 0.2328 0.2206 -0.0476 0.0300 -0.0117 715 PHE A CD2 5303 C CE1 . PHE A 680 ? 0.2317 0.2379 0.2221 -0.0402 0.0267 -0.0158 715 PHE A CE1 5304 C CE2 . PHE A 680 ? 0.2518 0.2408 0.2316 -0.0468 0.0278 -0.0130 715 PHE A CE2 5305 C CZ . PHE A 680 ? 0.2411 0.2395 0.2276 -0.0435 0.0261 -0.0151 715 PHE A CZ 5306 N N . GLN A 681 ? 0.2369 0.2420 0.2151 -0.0596 0.0405 -0.0147 716 GLN A N 5307 C CA A GLN A 681 ? 0.2490 0.2559 0.2293 -0.0658 0.0415 -0.0157 716 GLN A CA 5308 C CA B GLN A 681 ? 0.2590 0.2655 0.2390 -0.0661 0.0417 -0.0156 716 GLN A CA 5309 C C . GLN A 681 ? 0.2586 0.2798 0.2453 -0.0703 0.0454 -0.0186 716 GLN A C 5310 O O . GLN A 681 ? 0.2728 0.3028 0.2663 -0.0730 0.0451 -0.0210 716 GLN A O 5311 C CB A GLN A 681 ? 0.2547 0.2468 0.2255 -0.0707 0.0421 -0.0123 716 GLN A CB 5312 C CB B GLN A 681 ? 0.2772 0.2697 0.2472 -0.0716 0.0430 -0.0121 716 GLN A CB 5313 C CG A GLN A 681 ? 0.2493 0.2291 0.2164 -0.0664 0.0382 -0.0101 716 GLN A CG 5314 C CG B GLN A 681 ? 0.2876 0.2654 0.2514 -0.0679 0.0395 -0.0088 716 GLN A CG 5315 C CD A GLN A 681 ? 0.2621 0.2277 0.2219 -0.0710 0.0390 -0.0074 716 GLN A CD 5316 C CD B GLN A 681 ? 0.3029 0.2768 0.2694 -0.0676 0.0372 -0.0102 716 GLN A CD 5317 O OE1 A GLN A 681 ? 0.2756 0.2360 0.2289 -0.0755 0.0416 -0.0046 716 GLN A OE1 5318 O OE1 B GLN A 681 ? 0.3073 0.2893 0.2805 -0.0642 0.0350 -0.0130 716 GLN A OE1 5319 N NE2 A GLN A 681 ? 0.2754 0.2339 0.2356 -0.0701 0.0370 -0.0081 716 GLN A NE2 5320 N NE2 B GLN A 681 ? 0.3207 0.2815 0.2812 -0.0713 0.0378 -0.0083 716 GLN A NE2 5321 N N . ARG A 682 ? 0.2582 0.2828 0.2428 -0.0713 0.0492 -0.0185 717 ARG A N 5322 C CA . ARG A 682 ? 0.2885 0.3272 0.2790 -0.0758 0.0538 -0.0213 717 ARG A CA 5323 C C . ARG A 682 ? 0.2700 0.3246 0.2721 -0.0695 0.0539 -0.0247 717 ARG A C 5324 O O . ARG A 682 ? 0.2772 0.3468 0.2882 -0.0721 0.0558 -0.0272 717 ARG A O 5325 C CB . ARG A 682 ? 0.3214 0.3571 0.3038 -0.0802 0.0586 -0.0200 717 ARG A CB 5326 C CG . ARG A 682 ? 0.3861 0.4374 0.3744 -0.0852 0.0643 -0.0230 717 ARG A CG 5327 C CD . ARG A 682 ? 0.4274 0.4748 0.4058 -0.0902 0.0692 -0.0215 717 ARG A CD 5328 N NE . ARG A 682 ? 0.4827 0.5268 0.4570 -0.0837 0.0691 -0.0218 717 ARG A NE 5329 C CZ . ARG A 682 ? 0.5113 0.5665 0.4915 -0.0791 0.0721 -0.0258 717 ARG A CZ 5330 N NH1 . ARG A 682 ? 0.5140 0.5863 0.5061 -0.0791 0.0755 -0.0297 717 ARG A NH1 5331 N NH2 . ARG A 682 ? 0.5333 0.5824 0.5077 -0.0743 0.0719 -0.0260 717 ARG A NH2 5332 N N . VAL A 683 ? 0.2486 0.3001 0.2507 -0.0614 0.0518 -0.0245 718 VAL A N 5333 C CA . VAL A 683 ? 0.2386 0.3022 0.2504 -0.0545 0.0523 -0.0271 718 VAL A CA 5334 C C . VAL A 683 ? 0.2245 0.2886 0.2417 -0.0480 0.0469 -0.0266 718 VAL A C 5335 O O . VAL A 683 ? 0.2348 0.3122 0.2622 -0.0455 0.0460 -0.0280 718 VAL A O 5336 C CB . VAL A 683 ? 0.2442 0.3042 0.2518 -0.0507 0.0554 -0.0280 718 VAL A CB 5337 C CG1 . VAL A 683 ? 0.2516 0.3221 0.2692 -0.0429 0.0565 -0.0308 718 VAL A CG1 5338 C CG2 . VAL A 683 ? 0.2561 0.3175 0.2582 -0.0575 0.0610 -0.0287 718 VAL A CG2 5339 N N . LEU A 684 ? 0.2113 0.2620 0.2216 -0.0453 0.0434 -0.0243 719 LEU A N 5340 C CA . LEU A 684 ? 0.2086 0.2592 0.2228 -0.0388 0.0390 -0.0237 719 LEU A CA 5341 C C . LEU A 684 ? 0.2002 0.2552 0.2183 -0.0406 0.0355 -0.0235 719 LEU A C 5342 O O . LEU A 684 ? 0.2105 0.2735 0.2356 -0.0360 0.0329 -0.0236 719 LEU A O 5343 C CB . LEU A 684 ? 0.2149 0.2515 0.2210 -0.0357 0.0368 -0.0217 719 LEU A CB 5344 C CG . LEU A 684 ? 0.2341 0.2667 0.2361 -0.0335 0.0398 -0.0224 719 LEU A CG 5345 C CD1 . LEU A 684 ? 0.2404 0.2605 0.2345 -0.0318 0.0370 -0.0203 719 LEU A CD1 5346 C CD2 . LEU A 684 ? 0.2535 0.2944 0.2633 -0.0276 0.0416 -0.0247 719 LEU A CD2 5347 N N . VAL A 685 ? 0.2009 0.2505 0.2143 -0.0473 0.0353 -0.0231 720 VAL A N 5348 C CA . VAL A 685 ? 0.2024 0.2557 0.2187 -0.0498 0.0323 -0.0238 720 VAL A CA 5349 C C . VAL A 685 ? 0.2081 0.2803 0.2351 -0.0507 0.0327 -0.0260 720 VAL A C 5350 O O . VAL A 685 ? 0.1885 0.2689 0.2209 -0.0481 0.0292 -0.0263 720 VAL A O 5351 C CB . VAL A 685 ? 0.2267 0.2697 0.2359 -0.0574 0.0330 -0.0237 720 VAL A CB 5352 C CG1 . VAL A 685 ? 0.2270 0.2761 0.2397 -0.0613 0.0307 -0.0258 720 VAL A CG1 5353 C CG2 . VAL A 685 ? 0.2269 0.2529 0.2273 -0.0550 0.0314 -0.0211 720 VAL A CG2 5354 N N . LYS A 686 ? 0.1991 0.2794 0.2292 -0.0545 0.0370 -0.0274 721 LYS A N 5355 C CA . LYS A 686 ? 0.2237 0.3247 0.2655 -0.0549 0.0378 -0.0295 721 LYS A CA 5356 C C . LYS A 686 ? 0.2103 0.3197 0.2599 -0.0448 0.0359 -0.0289 721 LYS A C 5357 O O . LYS A 686 ? 0.1955 0.3186 0.2536 -0.0426 0.0329 -0.0291 721 LYS A O 5358 C CB . LYS A 686 ? 0.2435 0.3516 0.2871 -0.0603 0.0435 -0.0312 721 LYS A CB 5359 C CG . LYS A 686 ? 0.2747 0.4061 0.3319 -0.0590 0.0453 -0.0334 721 LYS A CG 5360 C CD . LYS A 686 ? 0.2787 0.4247 0.3436 -0.0624 0.0415 -0.0344 721 LYS A CD 5361 C CE . LYS A 686 ? 0.3108 0.4820 0.3900 -0.0615 0.0433 -0.0364 721 LYS A CE 5362 N NZ . LYS A 686 ? 0.3102 0.4974 0.3971 -0.0641 0.0387 -0.0370 721 LYS A NZ 5363 N N . LYS A 687 ? 0.2075 0.3082 0.2538 -0.0388 0.0375 -0.0280 722 LYS A N 5364 C CA . LYS A 687 ? 0.2119 0.3166 0.2642 -0.0291 0.0361 -0.0272 722 LYS A CA 5365 C C . LYS A 687 ? 0.2124 0.3163 0.2653 -0.0258 0.0301 -0.0250 722 LYS A C 5366 O O . LYS A 687 ? 0.1978 0.3144 0.2596 -0.0209 0.0278 -0.0243 722 LYS A O 5367 C CB . LYS A 687 ? 0.2381 0.3295 0.2839 -0.0247 0.0385 -0.0269 722 LYS A CB 5368 C CG . LYS A 687 ? 0.2637 0.3568 0.3149 -0.0149 0.0379 -0.0264 722 LYS A CG 5369 C CD . LYS A 687 ? 0.3219 0.3995 0.3646 -0.0125 0.0401 -0.0266 722 LYS A CD 5370 C CE . LYS A 687 ? 0.3779 0.4524 0.4237 -0.0035 0.0394 -0.0259 722 LYS A CE 5371 N NZ . LYS A 687 ? 0.4441 0.5016 0.4794 -0.0034 0.0400 -0.0258 722 LYS A NZ 5372 N N . TYR A 688 ? 0.2038 0.2936 0.2474 -0.0284 0.0277 -0.0238 723 TYR A N 5373 C CA . TYR A 688 ? 0.1965 0.2847 0.2392 -0.0260 0.0226 -0.0220 723 TYR A CA 5374 C C . TYR A 688 ? 0.1869 0.2900 0.2358 -0.0295 0.0199 -0.0229 723 TYR A C 5375 O O . TYR A 688 ? 0.1773 0.2889 0.2311 -0.0250 0.0161 -0.0212 723 TYR A O 5376 C CB . TYR A 688 ? 0.2020 0.2734 0.2341 -0.0284 0.0212 -0.0211 723 TYR A CB 5377 C CG . TYR A 688 ? 0.2165 0.2744 0.2422 -0.0255 0.0232 -0.0201 723 TYR A CG 5378 C CD1 . TYR A 688 ? 0.2379 0.2964 0.2663 -0.0195 0.0246 -0.0197 723 TYR A CD1 5379 C CD2 . TYR A 688 ? 0.2572 0.3019 0.2741 -0.0290 0.0236 -0.0196 723 TYR A CD2 5380 C CE1 . TYR A 688 ? 0.2672 0.3140 0.2891 -0.0181 0.0264 -0.0194 723 TYR A CE1 5381 C CE2 . TYR A 688 ? 0.2530 0.2874 0.2641 -0.0270 0.0248 -0.0186 723 TYR A CE2 5382 C CZ . TYR A 688 ? 0.2764 0.3121 0.2897 -0.0221 0.0262 -0.0187 723 TYR A CZ 5383 O OH . TYR A 688 ? 0.3504 0.3764 0.3574 -0.0210 0.0275 -0.0183 723 TYR A OH 5384 N N . ALA A 689 ? 0.1746 0.2807 0.2228 -0.0380 0.0216 -0.0253 724 ALA A N 5385 C CA . ALA A 689 ? 0.1844 0.3060 0.2385 -0.0430 0.0194 -0.0269 724 ALA A CA 5386 C C . ALA A 689 ? 0.1760 0.3181 0.2426 -0.0378 0.0187 -0.0264 724 ALA A C 5387 O O . ALA A 689 ? 0.1897 0.3443 0.2615 -0.0365 0.0143 -0.0256 724 ALA A O 5388 C CB . ALA A 689 ? 0.1829 0.3041 0.2345 -0.0535 0.0226 -0.0298 724 ALA A CB 5389 N N . SER A 690 ? 0.1814 0.3271 0.2529 -0.0343 0.0229 -0.0267 725 SER A N 5390 C CA . SER A 690 ? 0.1984 0.3631 0.2827 -0.0280 0.0229 -0.0262 725 SER A CA 5391 C C . SER A 690 ? 0.2092 0.3737 0.2965 -0.0170 0.0191 -0.0226 725 SER A C 5392 O O . SER A 690 ? 0.2334 0.4152 0.3314 -0.0118 0.0169 -0.0212 725 SER A O 5393 C CB . SER A 690 ? 0.2246 0.3922 0.3127 -0.0271 0.0293 -0.0282 725 SER A CB 5394 O OG . SER A 690 ? 0.2417 0.4094 0.3264 -0.0377 0.0329 -0.0309 725 SER A OG 5395 N N . GLU A 691 ? 0.1923 0.3377 0.2702 -0.0137 0.0183 -0.0208 726 GLU A N 5396 C CA . GLU A 691 ? 0.2033 0.3452 0.2822 -0.0044 0.0152 -0.0171 726 GLU A CA 5397 C C . GLU A 691 ? 0.2057 0.3493 0.2818 -0.0052 0.0091 -0.0146 726 GLU A C 5398 O O . GLU A 691 ? 0.2275 0.3756 0.3073 0.0018 0.0057 -0.0109 726 GLU A O 5399 C CB . GLU A 691 ? 0.2159 0.3370 0.2859 -0.0011 0.0176 -0.0165 726 GLU A CB 5400 C CG . GLU A 691 ? 0.2241 0.3429 0.2962 0.0011 0.0236 -0.0188 726 GLU A CG 5401 C CD . GLU A 691 ? 0.2494 0.3482 0.3117 0.0028 0.0257 -0.0188 726 GLU A CD 5402 O OE1 . GLU A 691 ? 0.2649 0.3515 0.3177 -0.0013 0.0239 -0.0181 726 GLU A OE1 5403 O OE2 . GLU A 691 ? 0.3088 0.4048 0.3731 0.0081 0.0294 -0.0198 726 GLU A OE2 5404 N N . ARG A 692 ? 0.1951 0.3345 0.2643 -0.0137 0.0080 -0.0165 727 ARG A N 5405 C CA . ARG A 692 ? 0.1894 0.3259 0.2528 -0.0151 0.0031 -0.0149 727 ARG A CA 5406 C C . ARG A 692 ? 0.1857 0.3378 0.2521 -0.0219 0.0000 -0.0167 727 ARG A C 5407 O O . ARG A 692 ? 0.1850 0.3350 0.2455 -0.0248 -0.0034 -0.0165 727 ARG A O 5408 C CB . ARG A 692 ? 0.2068 0.3229 0.2585 -0.0186 0.0046 -0.0159 727 ARG A CB 5409 C CG . ARG A 692 ? 0.2208 0.3226 0.2688 -0.0122 0.0063 -0.0137 727 ARG A CG 5410 C CD . ARG A 692 ? 0.2296 0.3137 0.2676 -0.0155 0.0081 -0.0147 727 ARG A CD 5411 N NE . ARG A 692 ? 0.2558 0.3351 0.2875 -0.0184 0.0052 -0.0146 727 ARG A NE 5412 C CZ . ARG A 692 ? 0.2548 0.3202 0.2786 -0.0199 0.0059 -0.0149 727 ARG A CZ 5413 N NH1 . ARG A 692 ? 0.2371 0.2917 0.2576 -0.0191 0.0089 -0.0149 727 ARG A NH1 5414 N NH2 . ARG A 692 ? 0.2312 0.2943 0.2503 -0.0222 0.0037 -0.0153 727 ARG A NH2 5415 N N . ASN A 693 ? 0.1794 0.3483 0.2550 -0.0245 0.0012 -0.0186 728 ASN A N 5416 C CA . ASN A 693 ? 0.1769 0.3612 0.2553 -0.0329 -0.0011 -0.0212 728 ASN A CA 5417 C C . ASN A 693 ? 0.1794 0.3508 0.2475 -0.0433 0.0003 -0.0252 728 ASN A C 5418 O O . ASN A 693 ? 0.1944 0.3670 0.2577 -0.0484 -0.0028 -0.0266 728 ASN A O 5419 C CB . ASN A 693 ? 0.1838 0.3821 0.2653 -0.0298 -0.0075 -0.0182 728 ASN A CB 5420 C CG . ASN A 693 ? 0.1979 0.4200 0.2874 -0.0361 -0.0101 -0.0203 728 ASN A CG 5421 O OD1 . ASN A 693 ? 0.1996 0.4271 0.2919 -0.0440 -0.0067 -0.0245 728 ASN A OD1 5422 N ND2 . ASN A 693 ? 0.1922 0.4294 0.2851 -0.0333 -0.0162 -0.0173 728 ASN A ND2 5423 N N . GLY A 694 ? 0.1764 0.3345 0.2405 -0.0459 0.0055 -0.0269 729 GLY A N 5424 C CA . GLY A 694 ? 0.1818 0.3248 0.2362 -0.0543 0.0077 -0.0300 729 GLY A CA 5425 C C . GLY A 694 ? 0.1989 0.3216 0.2436 -0.0501 0.0074 -0.0282 729 GLY A C 5426 O O . GLY A 694 ? 0.1834 0.3058 0.2281 -0.0431 0.0044 -0.0252 729 GLY A O 5427 N N . VAL A 695 ? 0.1959 0.3021 0.2328 -0.0546 0.0106 -0.0298 730 VAL A N 5428 C CA . VAL A 695 ? 0.2077 0.2953 0.2356 -0.0518 0.0105 -0.0286 730 VAL A CA 5429 C C . VAL A 695 ? 0.2100 0.2854 0.2302 -0.0594 0.0122 -0.0317 730 VAL A C 5430 O O . VAL A 695 ? 0.2311 0.3069 0.2515 -0.0664 0.0149 -0.0339 730 VAL A O 5431 C CB . VAL A 695 ? 0.1910 0.2677 0.2170 -0.0462 0.0131 -0.0260 730 VAL A CB 5432 C CG1 . VAL A 695 ? 0.2133 0.2980 0.2453 -0.0380 0.0117 -0.0233 730 VAL A CG1 5433 C CG2 . VAL A 695 ? 0.2072 0.2806 0.2326 -0.0508 0.0176 -0.0270 730 VAL A CG2 5434 N N . ASN A 696 ? 0.2019 0.2663 0.2156 -0.0577 0.0110 -0.0317 731 ASN A N 5435 C CA . ASN A 696 ? 0.2191 0.2676 0.2250 -0.0622 0.0131 -0.0339 731 ASN A CA 5436 C C . ASN A 696 ? 0.2302 0.2642 0.2319 -0.0566 0.0146 -0.0308 731 ASN A C 5437 O O . ASN A 696 ? 0.2264 0.2604 0.2285 -0.0499 0.0128 -0.0283 731 ASN A O 5438 C CB . ASN A 696 ? 0.2247 0.2718 0.2264 -0.0640 0.0111 -0.0367 731 ASN A CB 5439 C CG . ASN A 696 ? 0.2413 0.2704 0.2352 -0.0669 0.0137 -0.0390 731 ASN A CG 5440 O OD1 . ASN A 696 ? 0.2355 0.2540 0.2255 -0.0617 0.0139 -0.0375 731 ASN A OD1 5441 N ND2 . ASN A 696 ? 0.2502 0.2754 0.2419 -0.0750 0.0160 -0.0424 731 ASN A ND2 5442 N N . VAL A 697 ? 0.2155 0.2376 0.2130 -0.0598 0.0178 -0.0308 732 VAL A N 5443 C CA . VAL A 697 ? 0.2145 0.2240 0.2080 -0.0553 0.0191 -0.0275 732 VAL A CA 5444 C C . VAL A 697 ? 0.2353 0.2289 0.2219 -0.0568 0.0203 -0.0284 732 VAL A C 5445 O O . VAL A 697 ? 0.2642 0.2525 0.2482 -0.0633 0.0223 -0.0309 732 VAL A O 5446 C CB . VAL A 697 ? 0.2092 0.2186 0.2033 -0.0574 0.0220 -0.0259 732 VAL A CB 5447 C CG1 . VAL A 697 ? 0.2183 0.2160 0.2075 -0.0531 0.0228 -0.0223 732 VAL A CG1 5448 C CG2 . VAL A 697 ? 0.2086 0.2343 0.2104 -0.0559 0.0216 -0.0258 732 VAL A CG2 5449 N N . ILE A 698 ? 0.2161 0.2023 0.2001 -0.0508 0.0193 -0.0264 733 ILE A N 5450 C CA . ILE A 698 ? 0.2308 0.2017 0.2092 -0.0501 0.0207 -0.0260 733 ILE A CA 5451 C C . ILE A 698 ? 0.2355 0.2005 0.2122 -0.0453 0.0208 -0.0214 733 ILE A C 5452 O O . ILE A 698 ? 0.2233 0.1934 0.2021 -0.0403 0.0189 -0.0196 733 ILE A O 5453 C CB . ILE A 698 ? 0.2474 0.2158 0.2245 -0.0473 0.0196 -0.0283 733 ILE A CB 5454 C CG1 . ILE A 698 ? 0.2680 0.2444 0.2461 -0.0523 0.0190 -0.0331 733 ILE A CG1 5455 C CG2 . ILE A 698 ? 0.2658 0.2181 0.2380 -0.0462 0.0217 -0.0282 733 ILE A CG2 5456 C CD1 . ILE A 698 ? 0.3024 0.2771 0.2783 -0.0503 0.0183 -0.0359 733 ILE A CD1 5457 N N . SER A 699 ? 0.2338 0.1880 0.2063 -0.0473 0.0229 -0.0194 734 SER A N 5458 C CA . SER A 699 ? 0.2249 0.1738 0.1948 -0.0437 0.0227 -0.0147 734 SER A CA 5459 C C . SER A 699 ? 0.2334 0.1677 0.1985 -0.0415 0.0233 -0.0125 734 SER A C 5460 O O . SER A 699 ? 0.2464 0.1715 0.2091 -0.0444 0.0251 -0.0144 734 SER A O 5461 C CB . SER A 699 ? 0.2291 0.1799 0.1978 -0.0480 0.0246 -0.0130 734 SER A CB 5462 O OG . SER A 699 ? 0.2441 0.2088 0.2182 -0.0488 0.0243 -0.0148 734 SER A OG 5463 N N . GLY A 700 ? 0.2297 0.1616 0.1935 -0.0363 0.0219 -0.0083 735 GLY A N 5464 C CA . GLY A 700 ? 0.2421 0.1612 0.2020 -0.0332 0.0222 -0.0054 735 GLY A CA 5465 C C . GLY A 700 ? 0.2422 0.1623 0.2014 -0.0277 0.0198 -0.0005 735 GLY A C 5466 O O . GLY A 700 ? 0.2579 0.1879 0.2189 -0.0270 0.0183 0.0000 735 GLY A O 5467 N N . PRO A 701 ? 0.2543 0.1642 0.2108 -0.0239 0.0196 0.0030 736 PRO A N 5468 C CA . PRO A 701 ? 0.2557 0.1671 0.2115 -0.0187 0.0169 0.0081 736 PRO A CA 5469 C C . PRO A 701 ? 0.2587 0.1769 0.2198 -0.0128 0.0150 0.0068 736 PRO A C 5470 O O . PRO A 701 ? 0.2735 0.1906 0.2375 -0.0115 0.0162 0.0028 736 PRO A O 5471 C CB . PRO A 701 ? 0.2791 0.1759 0.2304 -0.0169 0.0178 0.0126 736 PRO A CB 5472 C CG . PRO A 701 ? 0.2821 0.1700 0.2342 -0.0179 0.0206 0.0081 736 PRO A CG 5473 C CD . PRO A 701 ? 0.2657 0.1611 0.2193 -0.0247 0.0220 0.0027 736 PRO A CD 5474 N N . ILE A 702 ? 0.2465 0.1715 0.2082 -0.0096 0.0122 0.0103 737 ILE A N 5475 C CA . ILE A 702 ? 0.2340 0.1658 0.2005 -0.0041 0.0102 0.0101 737 ILE A CA 5476 C C . ILE A 702 ? 0.2475 0.1791 0.2128 0.0000 0.0076 0.0161 737 ILE A C 5477 O O . ILE A 702 ? 0.2589 0.1913 0.2198 -0.0023 0.0064 0.0196 737 ILE A O 5478 C CB . ILE A 702 ? 0.2139 0.1580 0.1833 -0.0058 0.0091 0.0074 737 ILE A CB 5479 C CG1 . ILE A 702 ? 0.2092 0.1551 0.1813 -0.0076 0.0109 0.0019 737 ILE A CG1 5480 C CG2 . ILE A 702 ? 0.2101 0.1626 0.1828 -0.0017 0.0065 0.0091 737 ILE A CG2 5481 C CD1 . ILE A 702 ? 0.2195 0.1747 0.1932 -0.0101 0.0102 -0.0002 737 ILE A CD1 5482 N N . PHE A 703 ? 0.2282 0.1600 0.1976 0.0064 0.0068 0.0172 738 PHE A N 5483 C CA . PHE A 703 ? 0.2408 0.1749 0.2107 0.0115 0.0038 0.0231 738 PHE A CA 5484 C C . PHE A 703 ? 0.2466 0.1944 0.2231 0.0149 0.0019 0.0219 738 PHE A C 5485 O O . PHE A 703 ? 0.2369 0.1854 0.2187 0.0189 0.0034 0.0190 738 PHE A O 5486 C CB . PHE A 703 ? 0.2647 0.1861 0.2342 0.0170 0.0049 0.0264 738 PHE A CB 5487 C CG . PHE A 703 ? 0.2789 0.1852 0.2416 0.0128 0.0075 0.0272 738 PHE A CG 5488 C CD1 . PHE A 703 ? 0.2776 0.1759 0.2399 0.0095 0.0114 0.0215 738 PHE A CD1 5489 C CD2 . PHE A 703 ? 0.2969 0.1975 0.2530 0.0115 0.0061 0.0337 738 PHE A CD2 5490 C CE1 . PHE A 703 ? 0.2975 0.1827 0.2537 0.0045 0.0140 0.0219 738 PHE A CE1 5491 C CE2 . PHE A 703 ? 0.2953 0.1822 0.2448 0.0066 0.0089 0.0345 738 PHE A CE2 5492 C CZ . PHE A 703 ? 0.2991 0.1782 0.2490 0.0030 0.0129 0.0284 738 PHE A CZ 5493 N N . ASP A 704 ? 0.2429 0.2014 0.2188 0.0127 -0.0010 0.0237 739 ASP A N 5494 C CA . ASP A 704 ? 0.2351 0.2074 0.2170 0.0149 -0.0031 0.0230 739 ASP A CA 5495 C C . ASP A 704 ? 0.2421 0.2229 0.2229 0.0154 -0.0074 0.0282 739 ASP A C 5496 O O . ASP A 704 ? 0.2301 0.2203 0.2101 0.0111 -0.0091 0.0272 739 ASP A O 5497 C CB . ASP A 704 ? 0.2192 0.1975 0.2021 0.0100 -0.0019 0.0177 739 ASP A CB 5498 C CG . ASP A 704 ? 0.2099 0.2008 0.1991 0.0119 -0.0030 0.0165 739 ASP A CG 5499 O OD1 . ASP A 704 ? 0.2063 0.2009 0.2007 0.0177 -0.0036 0.0182 739 ASP A OD1 5500 O OD2 . ASP A 704 ? 0.1911 0.1879 0.1801 0.0075 -0.0030 0.0138 739 ASP A OD2 5501 N N . TYR A 705 ? 0.2522 0.2298 0.2329 0.0207 -0.0092 0.0338 740 TYR A N 5502 C CA . TYR A 705 ? 0.2602 0.2465 0.2394 0.0215 -0.0139 0.0398 740 TYR A CA 5503 C C . TYR A 705 ? 0.2615 0.2653 0.2478 0.0229 -0.0167 0.0392 740 TYR A C 5504 O O . TYR A 705 ? 0.2468 0.2606 0.2309 0.0199 -0.0204 0.0417 740 TYR A O 5505 C CB . TYR A 705 ? 0.2789 0.2573 0.2567 0.0278 -0.0154 0.0468 740 TYR A CB 5506 C CG . TYR A 705 ? 0.2953 0.2596 0.2634 0.0238 -0.0140 0.0491 740 TYR A CG 5507 C CD1 . TYR A 705 ? 0.2969 0.2462 0.2630 0.0229 -0.0095 0.0462 740 TYR A CD1 5508 C CD2 . TYR A 705 ? 0.3191 0.2859 0.2793 0.0198 -0.0171 0.0538 740 TYR A CD2 5509 C CE1 . TYR A 705 ? 0.3139 0.2514 0.2712 0.0181 -0.0079 0.0481 740 TYR A CE1 5510 C CE2 . TYR A 705 ? 0.3195 0.2744 0.2706 0.0154 -0.0153 0.0558 740 TYR A CE2 5511 C CZ . TYR A 705 ? 0.3286 0.2691 0.2786 0.0146 -0.0107 0.0530 740 TYR A CZ 5512 O OH . TYR A 705 ? 0.3476 0.2774 0.2888 0.0094 -0.0088 0.0549 740 TYR A OH 5513 N N . ASN A 706 ? 0.2685 0.2764 0.2628 0.0265 -0.0147 0.0357 741 ASN A N 5514 C CA . ASN A 706 ? 0.2585 0.2839 0.2601 0.0271 -0.0168 0.0349 741 ASN A CA 5515 C C . ASN A 706 ? 0.2437 0.2736 0.2449 0.0201 -0.0149 0.0289 741 ASN A C 5516 O O . ASN A 706 ? 0.2303 0.2730 0.2374 0.0197 -0.0154 0.0272 741 ASN A O 5517 C CB . ASN A 706 ? 0.2576 0.2874 0.2689 0.0359 -0.0158 0.0353 741 ASN A CB 5518 C CG . ASN A 706 ? 0.2772 0.2979 0.2903 0.0372 -0.0104 0.0296 741 ASN A CG 5519 O OD1 . ASN A 706 ? 0.2485 0.2583 0.2557 0.0323 -0.0078 0.0261 741 ASN A OD1 5520 N ND2 . ASN A 706 ? 0.2967 0.3229 0.3182 0.0438 -0.0088 0.0283 741 ASN A ND2 5521 N N . TYR A 707 ? 0.2265 0.2462 0.2208 0.0145 -0.0128 0.0261 742 TYR A N 5522 C CA . TYR A 707 ? 0.2193 0.2411 0.2118 0.0080 -0.0113 0.0213 742 TYR A CA 5523 C C . TYR A 707 ? 0.2168 0.2457 0.2158 0.0087 -0.0095 0.0177 742 TYR A C 5524 O O . TYR A 707 ? 0.2026 0.2394 0.2021 0.0042 -0.0101 0.0160 742 TYR A O 5525 C CB . TYR A 707 ? 0.2231 0.2509 0.2107 0.0020 -0.0141 0.0222 742 TYR A CB 5526 C CG . TYR A 707 ? 0.2343 0.2761 0.2252 0.0028 -0.0183 0.0256 742 TYR A CG 5527 C CD1 . TYR A 707 ? 0.2531 0.3074 0.2491 0.0006 -0.0190 0.0237 742 TYR A CD1 5528 C CD2 . TYR A 707 ? 0.2735 0.3168 0.2621 0.0054 -0.0218 0.0312 742 TYR A CD2 5529 C CE1 . TYR A 707 ? 0.2695 0.3387 0.2691 0.0007 -0.0230 0.0266 742 TYR A CE1 5530 C CE2 . TYR A 707 ? 0.2923 0.3505 0.2842 0.0062 -0.0262 0.0346 742 TYR A CE2 5531 C CZ . TYR A 707 ? 0.2957 0.3675 0.2936 0.0037 -0.0269 0.0321 742 TYR A CZ 5532 O OH . TYR A 707 ? 0.3102 0.3986 0.3121 0.0039 -0.0314 0.0353 742 TYR A OH 5533 N N . ASP A 708 ? 0.2157 0.2413 0.2190 0.0140 -0.0070 0.0165 743 ASP A N 5534 C CA . ASP A 708 ? 0.2068 0.2390 0.2155 0.0146 -0.0047 0.0128 743 ASP A CA 5535 C C . ASP A 708 ? 0.2035 0.2270 0.2089 0.0117 -0.0013 0.0084 743 ASP A C 5536 O O . ASP A 708 ? 0.1930 0.2205 0.2012 0.0116 0.0009 0.0053 743 ASP A O 5537 C CB . ASP A 708 ? 0.2104 0.2481 0.2270 0.0224 -0.0039 0.0136 743 ASP A CB 5538 C CG . ASP A 708 ? 0.2176 0.2419 0.2333 0.0277 -0.0014 0.0132 743 ASP A CG 5539 O OD1 . ASP A 708 ? 0.2153 0.2268 0.2244 0.0250 -0.0006 0.0129 743 ASP A OD1 5540 O OD2 . ASP A 708 ? 0.2388 0.2653 0.2606 0.0345 0.0000 0.0130 743 ASP A OD2 5541 N N . GLY A 709 ? 0.1924 0.2054 0.1917 0.0089 -0.0009 0.0082 744 GLY A N 5542 C CA . GLY A 709 ? 0.1987 0.2047 0.1953 0.0063 0.0017 0.0045 744 GLY A CA 5543 C C . GLY A 709 ? 0.2035 0.2025 0.2011 0.0098 0.0044 0.0022 744 GLY A C 5544 O O . GLY A 709 ? 0.2085 0.2038 0.2041 0.0074 0.0064 -0.0010 744 GLY A O 5545 N N . LEU A 710 ? 0.1937 0.1908 0.1941 0.0154 0.0045 0.0041 745 LEU A N 5546 C CA . LEU A 710 ? 0.2129 0.2025 0.2146 0.0194 0.0075 0.0016 745 LEU A CA 5547 C C . LEU A 710 ? 0.2212 0.1987 0.2200 0.0218 0.0075 0.0044 745 LEU A C 5548 O O . LEU A 710 ? 0.2250 0.2034 0.2236 0.0236 0.0048 0.0094 745 LEU A O 5549 C CB . LEU A 710 ? 0.2297 0.2274 0.2383 0.0252 0.0086 0.0009 745 LEU A CB 5550 C CG . LEU A 710 ? 0.2268 0.2380 0.2387 0.0227 0.0088 -0.0012 745 LEU A CG 5551 C CD1 . LEU A 710 ? 0.2404 0.2611 0.2598 0.0286 0.0103 -0.0018 745 LEU A CD1 5552 C CD2 . LEU A 710 ? 0.2173 0.2260 0.2254 0.0180 0.0112 -0.0057 745 LEU A CD2 5553 N N . ARG A 711 ? 0.2249 0.1910 0.2212 0.0216 0.0105 0.0013 746 ARG A N 5554 C CA . ARG A 711 ? 0.2593 0.2116 0.2525 0.0236 0.0113 0.0036 746 ARG A CA 5555 C C . ARG A 711 ? 0.2467 0.1987 0.2437 0.0315 0.0100 0.0085 746 ARG A C 5556 O O . ARG A 711 ? 0.2310 0.1874 0.2338 0.0372 0.0113 0.0071 746 ARG A O 5557 C CB . ARG A 711 ? 0.2994 0.2410 0.2907 0.0228 0.0155 -0.0017 746 ARG A CB 5558 C CG . ARG A 711 ? 0.3701 0.2954 0.3587 0.0258 0.0174 -0.0002 746 ARG A CG 5559 C CD . ARG A 711 ? 0.3980 0.3138 0.3860 0.0263 0.0219 -0.0065 746 ARG A CD 5560 N NE . ARG A 711 ? 0.3884 0.3104 0.3822 0.0325 0.0237 -0.0093 746 ARG A NE 5561 C CZ . ARG A 711 ? 0.4076 0.3253 0.4056 0.0411 0.0250 -0.0076 746 ARG A CZ 5562 N NH1 . ARG A 711 ? 0.4247 0.3301 0.4212 0.0452 0.0245 -0.0024 746 ARG A NH1 5563 N NH2 . ARG A 711 ? 0.4061 0.3322 0.4099 0.0459 0.0271 -0.0112 746 ARG A NH2 5564 N N . ASP A 712 ? 0.2608 0.2076 0.2544 0.0319 0.0077 0.0143 747 ASP A N 5565 C CA . ASP A 712 ? 0.2688 0.2150 0.2653 0.0396 0.0058 0.0202 747 ASP A CA 5566 C C . ASP A 712 ? 0.2987 0.2295 0.2954 0.0451 0.0094 0.0193 747 ASP A C 5567 O O . ASP A 712 ? 0.3079 0.2247 0.2991 0.0411 0.0124 0.0163 747 ASP A O 5568 C CB . ASP A 712 ? 0.2783 0.2217 0.2692 0.0377 0.0023 0.0270 747 ASP A CB 5569 C CG . ASP A 712 ? 0.2747 0.2333 0.2657 0.0340 -0.0016 0.0289 747 ASP A CG 5570 O OD1 . ASP A 712 ? 0.2613 0.2329 0.2572 0.0330 -0.0019 0.0255 747 ASP A OD1 5571 O OD2 . ASP A 712 ? 0.2822 0.2393 0.2676 0.0316 -0.0042 0.0338 747 ASP A OD2 5572 N N . THR A 713 ? 0.3268 0.2604 0.3301 0.0543 0.0091 0.0217 748 THR A N 5573 C CA . THR A 713 ? 0.3474 0.2645 0.3506 0.0613 0.0119 0.0230 748 THR A CA 5574 C C . THR A 713 ? 0.3708 0.2776 0.3681 0.0622 0.0091 0.0315 748 THR A C 5575 O O . THR A 713 ? 0.3379 0.2531 0.3325 0.0585 0.0047 0.0363 748 THR A O 5576 C CB . THR A 713 ? 0.3650 0.2901 0.3782 0.0720 0.0125 0.0235 748 THR A CB 5577 O OG1 . THR A 713 ? 0.3700 0.3108 0.3878 0.0755 0.0070 0.0305 748 THR A OG1 5578 C CG2 . THR A 713 ? 0.3602 0.2955 0.3785 0.0709 0.0158 0.0152 748 THR A CG2 5579 N N . GLU A 714 ? 0.4050 0.2931 0.4001 0.0671 0.0117 0.0334 749 GLU A N 5580 C CA . GLU A 714 ? 0.4436 0.3194 0.4319 0.0676 0.0095 0.0419 749 GLU A CA 5581 C C . GLU A 714 ? 0.4381 0.3278 0.4303 0.0737 0.0035 0.0507 749 GLU A C 5582 O O . GLU A 714 ? 0.4146 0.3053 0.4003 0.0696 -0.0002 0.0569 749 GLU A O 5583 C CB . GLU A 714 ? 0.5196 0.3714 0.5051 0.0727 0.0138 0.0425 749 GLU A CB 5584 C CG . GLU A 714 ? 0.5638 0.3971 0.5380 0.0656 0.0146 0.0460 749 GLU A CG 5585 C CD . GLU A 714 ? 0.6191 0.4275 0.5901 0.0714 0.0182 0.0485 749 GLU A CD 5586 O OE1 . GLU A 714 ? 0.6558 0.4550 0.6296 0.0741 0.0233 0.0413 749 GLU A OE1 5587 O OE2 . GLU A 714 ? 0.6925 0.4902 0.6577 0.0731 0.0162 0.0576 749 GLU A OE2 5588 N N . ASP A 715 ? 0.4552 0.3572 0.4579 0.0829 0.0026 0.0508 750 ASP A N 5589 C CA . ASP A 715 ? 0.4882 0.4063 0.4960 0.0890 -0.0033 0.0589 750 ASP A CA 5590 C C . ASP A 715 ? 0.4618 0.3999 0.4686 0.0810 -0.0078 0.0590 750 ASP A C 5591 O O . ASP A 715 ? 0.4581 0.4066 0.4647 0.0825 -0.0134 0.0664 750 ASP A O 5592 C CB . ASP A 715 ? 0.5514 0.4792 0.5720 0.1010 -0.0027 0.0586 750 ASP A CB 5593 C CG . ASP A 715 ? 0.6308 0.5413 0.6527 0.1126 -0.0013 0.0644 750 ASP A CG 5594 O OD1 . ASP A 715 ? 0.6916 0.5777 0.7047 0.1108 0.0019 0.0648 750 ASP A OD1 5595 O OD2 . ASP A 715 ? 0.7412 0.6623 0.7731 0.1238 -0.0034 0.0686 750 ASP A OD2 5596 N N . GLU A 716 ? 0.4119 0.3550 0.4177 0.0725 -0.0055 0.0510 751 GLU A N 5597 C CA . GLU A 716 ? 0.3976 0.3568 0.4015 0.0644 -0.0090 0.0504 751 GLU A CA 5598 C C . GLU A 716 ? 0.3899 0.3417 0.3825 0.0558 -0.0105 0.0531 751 GLU A C 5599 O O . GLU A 716 ? 0.3716 0.3353 0.3618 0.0501 -0.0137 0.0537 751 GLU A O 5600 C CB . GLU A 716 ? 0.3902 0.3580 0.3980 0.0597 -0.0061 0.0416 751 GLU A CB 5601 C CG . GLU A 716 ? 0.4113 0.3936 0.4306 0.0668 -0.0059 0.0399 751 GLU A CG 5602 C CD . GLU A 716 ? 0.4023 0.3893 0.4248 0.0633 -0.0018 0.0312 751 GLU A CD 5603 O OE1 . GLU A 716 ? 0.3642 0.3396 0.3809 0.0578 0.0015 0.0262 751 GLU A OE1 5604 O OE2 . GLU A 716 ? 0.4363 0.4394 0.4673 0.0663 -0.0021 0.0297 751 GLU A OE2 5605 N N . ILE A 717 ? 0.3980 0.3300 0.3834 0.0547 -0.0078 0.0544 752 ILE A N 5606 C CA . ILE A 717 ? 0.4031 0.3281 0.3778 0.0464 -0.0083 0.0566 752 ILE A CA 5607 C C . ILE A 717 ? 0.4282 0.3561 0.3986 0.0488 -0.0135 0.0664 752 ILE A C 5608 O O . ILE A 717 ? 0.4368 0.3574 0.4082 0.0566 -0.0146 0.0728 752 ILE A O 5609 C CB . ILE A 717 ? 0.4334 0.3377 0.4022 0.0430 -0.0032 0.0538 752 ILE A CB 5610 C CG1 . ILE A 717 ? 0.4339 0.3404 0.4057 0.0381 0.0006 0.0439 752 ILE A CG1 5611 C CG2 . ILE A 717 ? 0.4479 0.3442 0.4059 0.0358 -0.0037 0.0580 752 ILE A CG2 5612 C CD1 . ILE A 717 ? 0.4650 0.3537 0.4332 0.0353 0.0057 0.0396 752 ILE A CD1 5613 N N . LYS A 718 ? 0.4447 0.3833 0.4101 0.0420 -0.0166 0.0676 753 LYS A N 5614 C CA . LYS A 718 ? 0.4528 0.3990 0.4145 0.0437 -0.0223 0.0764 753 LYS A CA 5615 C C . LYS A 718 ? 0.4583 0.3948 0.4071 0.0373 -0.0227 0.0812 753 LYS A C 5616 O O . LYS A 718 ? 0.4717 0.4148 0.4158 0.0376 -0.0275 0.0884 753 LYS A O 5617 C CB . LYS A 718 ? 0.4519 0.4203 0.4176 0.0412 -0.0264 0.0747 753 LYS A CB 5618 C CG . LYS A 718 ? 0.4433 0.4243 0.4219 0.0474 -0.0266 0.0713 753 LYS A CG 5619 C CD . LYS A 718 ? 0.4694 0.4497 0.4546 0.0593 -0.0286 0.0779 753 LYS A CD 5620 C CE . LYS A 718 ? 0.4721 0.4687 0.4706 0.0650 -0.0289 0.0745 753 LYS A CE 5621 N NZ . LYS A 718 ? 0.4907 0.4843 0.4970 0.0776 -0.0291 0.0794 753 LYS A NZ 5622 N N . GLN A 719 ? 0.4395 0.3618 0.3825 0.0313 -0.0178 0.0774 754 GLN A N 5623 C CA . GLN A 719 ? 0.4584 0.3720 0.3893 0.0248 -0.0175 0.0817 754 GLN A CA 5624 C C . GLN A 719 ? 0.4428 0.3361 0.3697 0.0222 -0.0119 0.0801 754 GLN A C 5625 O O . GLN A 719 ? 0.3821 0.2722 0.3136 0.0203 -0.0077 0.0721 754 GLN A O 5626 C CB . GLN A 719 ? 0.4625 0.3876 0.3889 0.0155 -0.0177 0.0774 754 GLN A CB 5627 C CG . GLN A 719 ? 0.5246 0.4439 0.4382 0.0086 -0.0174 0.0818 754 GLN A CG 5628 C CD . GLN A 719 ? 0.5568 0.4861 0.4668 -0.0001 -0.0164 0.0758 754 GLN A CD 5629 O OE1 . GLN A 719 ? 0.6012 0.5438 0.5171 -0.0004 -0.0177 0.0707 754 GLN A OE1 5630 N NE2 . GLN A 719 ? 0.5677 0.4904 0.4679 -0.0075 -0.0135 0.0763 754 GLN A NE2 5631 N N . TYR A 720 ? 0.4343 0.3143 0.3522 0.0219 -0.0121 0.0879 755 TYR A N 5632 C CA . TYR A 720 ? 0.4595 0.3192 0.3720 0.0185 -0.0069 0.0875 755 TYR A CA 5633 C C . TYR A 720 ? 0.4604 0.3158 0.3602 0.0098 -0.0064 0.0919 755 TYR A C 5634 O O . TYR A 720 ? 0.4534 0.3191 0.3481 0.0086 -0.0106 0.0971 755 TYR A O 5635 C CB . TYR A 720 ? 0.4927 0.3360 0.4064 0.0277 -0.0068 0.0937 755 TYR A CB 5636 C CG . TYR A 720 ? 0.4818 0.3278 0.4079 0.0361 -0.0060 0.0883 755 TYR A CG 5637 C CD1 . TYR A 720 ? 0.4925 0.3549 0.4271 0.0442 -0.0106 0.0901 755 TYR A CD1 5638 C CD2 . TYR A 720 ? 0.4973 0.3303 0.4261 0.0354 -0.0004 0.0813 755 TYR A CD2 5639 C CE1 . TYR A 720 ? 0.4958 0.3619 0.4417 0.0515 -0.0093 0.0849 755 TYR A CE1 5640 C CE2 . TYR A 720 ? 0.5283 0.3640 0.4675 0.0426 0.0007 0.0758 755 TYR A CE2 5641 C CZ . TYR A 720 ? 0.5228 0.3753 0.4707 0.0508 -0.0034 0.0777 755 TYR A CZ 5642 O OH . TYR A 720 ? 0.5098 0.3658 0.4680 0.0577 -0.0016 0.0722 755 TYR A OH 5643 N N . VAL A 721 ? 0.4612 0.3027 0.3561 0.0030 -0.0012 0.0893 756 VAL A N 5644 C CA . VAL A 721 ? 0.4840 0.3187 0.3663 -0.0051 0.0002 0.0942 756 VAL A CA 5645 C C . VAL A 721 ? 0.5231 0.3469 0.3983 0.0004 -0.0031 0.1066 756 VAL A C 5646 O O . VAL A 721 ? 0.5283 0.3382 0.4066 0.0079 -0.0027 0.1097 756 VAL A O 5647 C CB . VAL A 721 ? 0.4853 0.3067 0.3648 -0.0132 0.0068 0.0891 756 VAL A CB 5648 C CG1 . VAL A 721 ? 0.5066 0.3218 0.3733 -0.0223 0.0088 0.0942 756 VAL A CG1 5649 C CG2 . VAL A 721 ? 0.4740 0.3077 0.3614 -0.0177 0.0094 0.0775 756 VAL A CG2 5650 N N . GLU A 722 ? 0.5558 0.3865 0.4217 -0.0026 -0.0064 0.1135 757 GLU A N 5651 C CA . GLU A 722 ? 0.6334 0.4557 0.4909 0.0021 -0.0104 0.1266 757 GLU A CA 5652 C C . GLU A 722 ? 0.6076 0.4050 0.4633 0.0070 -0.0080 0.1323 757 GLU A C 5653 O O . GLU A 722 ? 0.6251 0.4069 0.4754 0.0000 -0.0023 0.1302 757 GLU A O 5654 C CB . GLU A 722 ? 0.7017 0.5256 0.5445 -0.0073 -0.0106 0.1319 757 GLU A CB 5655 C CG . GLU A 722 ? 0.7554 0.6004 0.5955 -0.0076 -0.0165 0.1343 757 GLU A CG 5656 C CD . GLU A 722 ? 0.8180 0.6627 0.6543 0.0007 -0.0233 0.1472 757 GLU A CD 5657 O OE1 . GLU A 722 ? 0.8676 0.7268 0.7127 0.0084 -0.0288 0.1476 757 GLU A OE1 5658 O OE2 . GLU A 722 ? 0.8943 0.7246 0.7189 -0.0006 -0.0233 0.1571 757 GLU A OE2 5659 N N . GLY A 723 ? 0.6199 0.4140 0.4805 0.0191 -0.0120 0.1391 758 GLY A N 5660 C CA . GLY A 723 ? 0.6399 0.4088 0.4977 0.0252 -0.0101 0.1461 758 GLY A CA 5661 C C . GLY A 723 ? 0.6335 0.3866 0.4981 0.0262 -0.0038 0.1375 758 GLY A C 5662 O O . GLY A 723 ? 0.6490 0.3785 0.5101 0.0298 -0.0012 0.1422 758 GLY A O 5663 N N . SER A 724 ? 0.5829 0.3483 0.4566 0.0229 -0.0014 0.1250 759 SER A N 5664 C CA . SER A 724 ? 0.5794 0.3323 0.4583 0.0213 0.0047 0.1155 759 SER A CA 5665 C C . SER A 724 ? 0.5506 0.3158 0.4438 0.0296 0.0037 0.1081 759 SER A C 5666 O O . SER A 724 ? 0.5543 0.3388 0.4535 0.0352 -0.0013 0.1096 759 SER A O 5667 C CB . SER A 724 ? 0.5738 0.3305 0.4494 0.0076 0.0091 0.1069 759 SER A CB 5668 O OG . SER A 724 ? 0.5263 0.3073 0.4093 0.0058 0.0072 0.0995 759 SER A OG 5669 N N . SER A 725 ? 0.5705 0.3249 0.4684 0.0294 0.0088 0.0998 760 SER A N 5670 C CA . SER A 725 ? 0.5717 0.3386 0.4821 0.0347 0.0091 0.0908 760 SER A CA 5671 C C . SER A 725 ? 0.5346 0.3125 0.4471 0.0244 0.0119 0.0797 760 SER A C 5672 O O . SER A 725 ? 0.5242 0.3056 0.4445 0.0260 0.0142 0.0710 760 SER A O 5673 C CB . SER A 725 ? 0.6357 0.3840 0.5504 0.0429 0.0128 0.0887 760 SER A CB 5674 O OG . SER A 725 ? 0.6961 0.4249 0.6050 0.0347 0.0191 0.0833 760 SER A OG 5675 N N . ILE A 726 ? 0.5101 0.2943 0.4158 0.0144 0.0118 0.0801 761 ILE A N 5676 C CA . ILE A 726 ? 0.4708 0.2667 0.3791 0.0055 0.0141 0.0704 761 ILE A CA 5677 C C . ILE A 726 ? 0.4355 0.2553 0.3506 0.0085 0.0096 0.0686 761 ILE A C 5678 O O . ILE A 726 ? 0.4289 0.2583 0.3400 0.0074 0.0060 0.0739 761 ILE A O 5679 C CB . ILE A 726 ? 0.4887 0.2818 0.3875 -0.0063 0.0165 0.0711 761 ILE A CB 5680 C CG1 . ILE A 726 ? 0.5217 0.2904 0.4118 -0.0100 0.0204 0.0752 761 ILE A CG1 5681 C CG2 . ILE A 726 ? 0.4805 0.2856 0.3836 -0.0142 0.0191 0.0609 761 ILE A CG2 5682 C CD1 . ILE A 726 ? 0.5200 0.2870 0.4000 -0.0211 0.0223 0.0781 761 ILE A CD1 5683 N N . PRO A 727 ? 0.4141 0.2433 0.3388 0.0120 0.0099 0.0612 762 PRO A N 5684 C CA . PRO A 727 ? 0.3826 0.2332 0.3135 0.0144 0.0059 0.0597 762 PRO A CA 5685 C C . PRO A 727 ? 0.3588 0.2213 0.2873 0.0052 0.0062 0.0555 762 PRO A C 5686 O O . PRO A 727 ? 0.3642 0.2221 0.2906 -0.0019 0.0101 0.0506 762 PRO A O 5687 C CB . PRO A 727 ? 0.3811 0.2352 0.3217 0.0193 0.0074 0.0525 762 PRO A CB 5688 C CG . PRO A 727 ? 0.3871 0.2279 0.3255 0.0135 0.0128 0.0465 762 PRO A CG 5689 C CD . PRO A 727 ? 0.4185 0.2405 0.3477 0.0113 0.0143 0.0528 762 PRO A CD 5690 N N . VAL A 728 ? 0.3375 0.2157 0.2667 0.0055 0.0023 0.0572 763 VAL A N 5691 C CA . VAL A 728 ? 0.3263 0.2156 0.2534 -0.0020 0.0027 0.0532 763 VAL A CA 5692 C C . VAL A 728 ? 0.3097 0.2114 0.2454 -0.0014 0.0028 0.0455 763 VAL A C 5693 O O . VAL A 728 ? 0.3082 0.2194 0.2494 0.0039 -0.0003 0.0461 763 VAL A O 5694 C CB . VAL A 728 ? 0.3328 0.2310 0.2541 -0.0031 -0.0012 0.0589 763 VAL A CB 5695 C CG1 . VAL A 728 ? 0.3371 0.2450 0.2559 -0.0109 0.0001 0.0540 763 VAL A CG1 5696 C CG2 . VAL A 728 ? 0.3582 0.2442 0.2701 -0.0035 -0.0016 0.0676 763 VAL A CG2 5697 N N . PRO A 729 ? 0.2930 0.1954 0.2300 -0.0070 0.0062 0.0388 764 PRO A N 5698 C CA . PRO A 729 ? 0.2753 0.1893 0.2195 -0.0065 0.0060 0.0325 764 PRO A CA 5699 C C . PRO A 729 ? 0.2624 0.1900 0.2065 -0.0074 0.0030 0.0328 764 PRO A C 5700 O O . PRO A 729 ? 0.2497 0.1789 0.1875 -0.0114 0.0024 0.0353 764 PRO A O 5701 C CB . PRO A 729 ? 0.2625 0.1746 0.2067 -0.0127 0.0098 0.0267 764 PRO A CB 5702 C CG . PRO A 729 ? 0.2789 0.1760 0.2186 -0.0145 0.0124 0.0288 764 PRO A CG 5703 C CD . PRO A 729 ? 0.2923 0.1856 0.2253 -0.0136 0.0103 0.0365 764 PRO A CD 5704 N N . THR A 730 ? 0.2477 0.1847 0.1984 -0.0043 0.0014 0.0301 765 THR A N 5705 C CA . THR A 730 ? 0.2320 0.1810 0.1830 -0.0063 -0.0006 0.0288 765 THR A CA 5706 C C . THR A 730 ? 0.2232 0.1747 0.1742 -0.0116 0.0020 0.0230 765 THR A C 5707 O O . THR A 730 ? 0.2187 0.1762 0.1671 -0.0148 0.0015 0.0220 765 THR A O 5708 C CB . THR A 730 ? 0.2247 0.1831 0.1824 -0.0016 -0.0032 0.0283 765 THR A CB 5709 O OG1 . THR A 730 ? 0.2174 0.1748 0.1812 0.0002 -0.0010 0.0237 765 THR A OG1 5710 C CG2 . THR A 730 ? 0.2462 0.2052 0.2047 0.0040 -0.0064 0.0345 765 THR A CG2 5711 N N . HIS A 731 ? 0.2160 0.1630 0.1699 -0.0123 0.0049 0.0192 766 HIS A N 5712 C CA . HIS A 731 ? 0.2086 0.1591 0.1641 -0.0161 0.0072 0.0142 766 HIS A CA 5713 C C . HIS A 731 ? 0.2150 0.1586 0.1706 -0.0184 0.0102 0.0121 766 HIS A C 5714 O O . HIS A 731 ? 0.2260 0.1617 0.1814 -0.0166 0.0107 0.0134 766 HIS A O 5715 C CB . HIS A 731 ? 0.1963 0.1539 0.1579 -0.0140 0.0064 0.0106 766 HIS A CB 5716 C CG . HIS A 731 ? 0.2055 0.1705 0.1677 -0.0126 0.0037 0.0118 766 HIS A CG 5717 N ND1 . HIS A 731 ? 0.1990 0.1660 0.1625 -0.0087 0.0011 0.0151 766 HIS A ND1 5718 C CD2 . HIS A 731 ? 0.2014 0.1723 0.1629 -0.0149 0.0032 0.0101 766 HIS A CD2 5719 C CE1 . HIS A 731 ? 0.2003 0.1753 0.1641 -0.0093 -0.0009 0.0153 766 HIS A CE1 5720 N NE2 . HIS A 731 ? 0.1991 0.1757 0.1613 -0.0132 0.0003 0.0122 766 HIS A NE2 5721 N N . TYR A 732 ? 0.2023 0.1495 0.1588 -0.0223 0.0123 0.0085 767 TYR A N 5722 C CA . TYR A 732 ? 0.2215 0.1656 0.1795 -0.0254 0.0149 0.0055 767 TYR A CA 5723 C C . TYR A 732 ? 0.2146 0.1670 0.1782 -0.0253 0.0150 0.0010 767 TYR A C 5724 O O . TYR A 732 ? 0.2183 0.1776 0.1831 -0.0253 0.0146 0.0000 767 TYR A O 5725 C CB . TYR A 732 ? 0.2334 0.1752 0.1871 -0.0308 0.0175 0.0063 767 TYR A CB 5726 C CG . TYR A 732 ? 0.2368 0.1676 0.1844 -0.0316 0.0179 0.0109 767 TYR A CG 5727 C CD1 . TYR A 732 ? 0.2635 0.1848 0.2107 -0.0327 0.0195 0.0106 767 TYR A CD1 5728 C CD2 . TYR A 732 ? 0.2538 0.1832 0.1955 -0.0313 0.0166 0.0159 767 TYR A CD2 5729 C CE1 . TYR A 732 ? 0.2751 0.1843 0.2164 -0.0330 0.0200 0.0154 767 TYR A CE1 5730 C CE2 . TYR A 732 ? 0.2706 0.1895 0.2063 -0.0316 0.0167 0.0211 767 TYR A CE2 5731 C CZ . TYR A 732 ? 0.2750 0.1830 0.2106 -0.0322 0.0185 0.0211 767 TYR A CZ 5732 O OH . TYR A 732 ? 0.2899 0.1855 0.2192 -0.0322 0.0188 0.0267 767 TYR A OH 5733 N N . TYR A 733 ? 0.2203 0.1716 0.1869 -0.0251 0.0155 -0.0017 768 TYR A N 5734 C CA . TYR A 733 ? 0.2102 0.1697 0.1815 -0.0250 0.0151 -0.0052 768 TYR A CA 5735 C C . TYR A 733 ? 0.2180 0.1802 0.1909 -0.0294 0.0170 -0.0081 768 TYR A C 5736 O O . TYR A 733 ? 0.2153 0.1717 0.1858 -0.0331 0.0188 -0.0081 768 TYR A O 5737 C CB . TYR A 733 ? 0.2009 0.1602 0.1745 -0.0218 0.0140 -0.0066 768 TYR A CB 5738 C CG . TYR A 733 ? 0.2156 0.1683 0.1884 -0.0232 0.0155 -0.0088 768 TYR A CG 5739 C CD1 . TYR A 733 ? 0.2202 0.1763 0.1946 -0.0266 0.0164 -0.0127 768 TYR A CD1 5740 C CD2 . TYR A 733 ? 0.2260 0.1689 0.1964 -0.0210 0.0161 -0.0071 768 TYR A CD2 5741 C CE1 . TYR A 733 ? 0.2195 0.1689 0.1924 -0.0289 0.0180 -0.0154 768 TYR A CE1 5742 C CE2 . TYR A 733 ? 0.2455 0.1803 0.2146 -0.0224 0.0180 -0.0096 768 TYR A CE2 5743 C CZ . TYR A 733 ? 0.2291 0.1670 0.1991 -0.0269 0.0191 -0.0141 768 TYR A CZ 5744 O OH . TYR A 733 ? 0.2573 0.1871 0.2254 -0.0293 0.0212 -0.0175 768 TYR A OH 5745 N N . SER A 734 ? 0.2116 0.1828 0.1887 -0.0292 0.0164 -0.0102 769 SER A N 5746 C CA . SER A 734 ? 0.2253 0.2020 0.2055 -0.0326 0.0172 -0.0133 769 SER A CA 5747 C C . SER A 734 ? 0.2189 0.2036 0.2030 -0.0302 0.0152 -0.0148 769 SER A C 5748 O O . SER A 734 ? 0.2114 0.1990 0.1966 -0.0266 0.0140 -0.0134 769 SER A O 5749 C CB . SER A 734 ? 0.2408 0.2229 0.2226 -0.0357 0.0191 -0.0135 769 SER A CB 5750 O OG . SER A 734 ? 0.3049 0.2797 0.2823 -0.0390 0.0212 -0.0121 769 SER A OG 5751 N N . ILE A 735 ? 0.1953 0.1831 0.1808 -0.0327 0.0150 -0.0175 770 ILE A N 5752 C CA . ILE A 735 ? 0.1875 0.1838 0.1759 -0.0313 0.0129 -0.0187 770 ILE A CA 5753 C C . ILE A 735 ? 0.1975 0.2034 0.1898 -0.0349 0.0130 -0.0206 770 ILE A C 5754 O O . ILE A 735 ? 0.2146 0.2194 0.2061 -0.0400 0.0142 -0.0231 770 ILE A O 5755 C CB . ILE A 735 ? 0.1966 0.1894 0.1826 -0.0315 0.0124 -0.0208 770 ILE A CB 5756 C CG1 . ILE A 735 ? 0.2045 0.1893 0.1878 -0.0276 0.0125 -0.0190 770 ILE A CG1 5757 C CG2 . ILE A 735 ? 0.1956 0.1981 0.1835 -0.0311 0.0102 -0.0219 770 ILE A CG2 5758 C CD1 . ILE A 735 ? 0.2257 0.2050 0.2066 -0.0277 0.0133 -0.0215 770 ILE A CD1 5759 N N . ILE A 736 ? 0.1886 0.2039 0.1854 -0.0323 0.0117 -0.0194 771 ILE A N 5760 C CA . ILE A 736 ? 0.2084 0.2352 0.2106 -0.0345 0.0117 -0.0206 771 ILE A CA 5761 C C . ILE A 736 ? 0.2040 0.2408 0.2091 -0.0328 0.0085 -0.0205 771 ILE A C 5762 O O . ILE A 736 ? 0.2000 0.2388 0.2064 -0.0277 0.0070 -0.0180 771 ILE A O 5763 C CB . ILE A 736 ? 0.2173 0.2469 0.2227 -0.0322 0.0134 -0.0191 771 ILE A CB 5764 C CG1 . ILE A 736 ? 0.2375 0.2564 0.2381 -0.0341 0.0162 -0.0185 771 ILE A CG1 5765 C CG2 . ILE A 736 ? 0.2127 0.2558 0.2250 -0.0343 0.0139 -0.0204 771 ILE A CG2 5766 C CD1 . ILE A 736 ? 0.2613 0.2819 0.2633 -0.0328 0.0185 -0.0177 771 ILE A CD1 5767 N N . THR A 737 ? 0.1899 0.2328 0.1954 -0.0375 0.0076 -0.0233 772 THR A N 5768 C CA . THR A 737 ? 0.2035 0.2558 0.2100 -0.0369 0.0042 -0.0233 772 THR A CA 5769 C C . THR A 737 ? 0.2053 0.2737 0.2186 -0.0393 0.0027 -0.0240 772 THR A C 5770 O O . THR A 737 ? 0.1890 0.2600 0.2044 -0.0442 0.0047 -0.0263 772 THR A O 5771 C CB . THR A 737 ? 0.2197 0.2668 0.2202 -0.0409 0.0040 -0.0265 772 THR A CB 5772 O OG1 . THR A 737 ? 0.2204 0.2532 0.2158 -0.0390 0.0059 -0.0263 772 THR A OG1 5773 C CG2 . THR A 737 ? 0.2306 0.2867 0.2304 -0.0398 0.0004 -0.0259 772 THR A CG2 5774 N N . SER A 738 ? 0.1816 0.2609 0.1983 -0.0355 -0.0006 -0.0216 773 SER A N 5775 C CA . SER A 738 ? 0.1904 0.2874 0.2141 -0.0369 -0.0029 -0.0217 773 SER A CA 5776 C C . SER A 738 ? 0.2017 0.3073 0.2245 -0.0346 -0.0076 -0.0194 773 SER A C 5777 O O . SER A 738 ? 0.1868 0.2840 0.2030 -0.0330 -0.0084 -0.0184 773 SER A O 5778 C CB . SER A 738 ? 0.1935 0.2967 0.2253 -0.0321 -0.0016 -0.0194 773 SER A CB 5779 O OG . SER A 738 ? 0.2036 0.3017 0.2354 -0.0240 -0.0023 -0.0153 773 SER A OG 5780 N N . CYS A 739 ? 0.1872 0.3105 0.2166 -0.0344 -0.0107 -0.0183 774 CYS A N 5781 C CA . CYS A 739 ? 0.1895 0.3225 0.2179 -0.0323 -0.0157 -0.0153 774 CYS A CA 5782 C C . CYS A 739 ? 0.1881 0.3197 0.2193 -0.0226 -0.0170 -0.0091 774 CYS A C 5783 O O . CYS A 739 ? 0.1958 0.3323 0.2351 -0.0177 -0.0161 -0.0071 774 CYS A O 5784 C CB . CYS A 739 ? 0.2064 0.3606 0.2411 -0.0362 -0.0191 -0.0163 774 CYS A CB 5785 S SG . CYS A 739 ? 0.2216 0.3878 0.2514 -0.0379 -0.0254 -0.0146 774 CYS A SG 5786 N N . LEU A 740 ? 0.1906 0.3166 0.2154 -0.0200 -0.0191 -0.0059 775 LEU A N 5787 C CA . LEU A 740 ? 0.2021 0.3257 0.2288 -0.0113 -0.0204 0.0003 775 LEU A CA 5788 C C . LEU A 740 ? 0.1994 0.3409 0.2353 -0.0068 -0.0241 0.0041 775 LEU A C 5789 O O . LEU A 740 ? 0.2164 0.3573 0.2585 0.0005 -0.0233 0.0075 775 LEU A O 5790 C CB . LEU A 740 ? 0.2265 0.3422 0.2442 -0.0105 -0.0220 0.0032 775 LEU A CB 5791 C CG . LEU A 740 ? 0.2498 0.3587 0.2675 -0.0026 -0.0226 0.0096 775 LEU A CG 5792 C CD1 . LEU A 740 ? 0.2660 0.3602 0.2846 0.0003 -0.0180 0.0088 775 LEU A CD1 5793 C CD2 . LEU A 740 ? 0.2904 0.3949 0.2988 -0.0036 -0.0246 0.0124 775 LEU A CD2 5794 N N . ASP A 741 ? 0.1926 0.3502 0.2294 -0.0113 -0.0281 0.0033 776 ASP A N 5795 C CA . ASP A 741 ? 0.1948 0.3730 0.2418 -0.0082 -0.0318 0.0060 776 ASP A CA 5796 C C . ASP A 741 ? 0.1837 0.3682 0.2393 -0.0112 -0.0283 0.0012 776 ASP A C 5797 O O . ASP A 741 ? 0.1728 0.3648 0.2282 -0.0199 -0.0281 -0.0039 776 ASP A O 5798 C CB . ASP A 741 ? 0.2077 0.4021 0.2518 -0.0134 -0.0375 0.0062 776 ASP A CB 5799 C CG . ASP A 741 ? 0.2088 0.4275 0.2641 -0.0109 -0.0419 0.0090 776 ASP A CG 5800 O OD1 . ASP A 741 ? 0.1992 0.4227 0.2654 -0.0039 -0.0406 0.0112 776 ASP A OD1 5801 O OD2 . ASP A 741 ? 0.2040 0.4379 0.2572 -0.0161 -0.0469 0.0088 776 ASP A OD2 5802 N N . PHE A 742 ? 0.1875 0.3683 0.2500 -0.0042 -0.0252 0.0029 777 PHE A N 5803 C CA . PHE A 742 ? 0.1871 0.3735 0.2578 -0.0060 -0.0212 -0.0009 777 PHE A CA 5804 C C . PHE A 742 ? 0.1920 0.4040 0.2735 -0.0084 -0.0239 -0.0018 777 PHE A C 5805 O O . PHE A 742 ? 0.1976 0.4161 0.2856 -0.0118 -0.0204 -0.0056 777 PHE A O 5806 C CB . PHE A 742 ? 0.1947 0.3720 0.2700 0.0026 -0.0171 0.0009 777 PHE A CB 5807 C CG . PHE A 742 ? 0.2033 0.3870 0.2850 0.0134 -0.0201 0.0074 777 PHE A CG 5808 C CD1 . PHE A 742 ? 0.2126 0.4172 0.3072 0.0179 -0.0218 0.0090 777 PHE A CD1 5809 C CD2 . PHE A 742 ? 0.2164 0.3848 0.2914 0.0193 -0.0210 0.0121 777 PHE A CD2 5810 C CE1 . PHE A 742 ? 0.2220 0.4318 0.3227 0.0288 -0.0246 0.0154 777 PHE A CE1 5811 C CE2 . PHE A 742 ? 0.2235 0.3958 0.3036 0.0293 -0.0236 0.0185 777 PHE A CE2 5812 C CZ . PHE A 742 ? 0.2472 0.4397 0.3403 0.0346 -0.0255 0.0203 777 PHE A CZ 5813 N N . THR A 743 ? 0.1828 0.4103 0.2664 -0.0065 -0.0301 0.0020 778 THR A N 5814 C CA . THR A 743 ? 0.1887 0.4429 0.2821 -0.0102 -0.0336 0.0010 778 THR A CA 5815 C C . THR A 743 ? 0.1976 0.4552 0.2853 -0.0240 -0.0334 -0.0057 778 THR A C 5816 O O . THR A 743 ? 0.2093 0.4878 0.3045 -0.0295 -0.0353 -0.0081 778 THR A O 5817 C CB . THR A 743 ? 0.1869 0.4588 0.2845 -0.0041 -0.0409 0.0077 778 THR A CB 5818 O OG1 . THR A 743 ? 0.1842 0.4519 0.2696 -0.0091 -0.0450 0.0083 778 THR A OG1 5819 C CG2 . THR A 743 ? 0.1840 0.4501 0.2864 0.0098 -0.0410 0.0148 778 THR A CG2 5820 N N . GLN A 744 ? 0.2012 0.4386 0.2760 -0.0295 -0.0313 -0.0089 779 GLN A N 5821 C CA . GLN A 744 ? 0.2063 0.4414 0.2745 -0.0420 -0.0299 -0.0158 779 GLN A CA 5822 C C . GLN A 744 ? 0.2063 0.4231 0.2716 -0.0454 -0.0229 -0.0201 779 GLN A C 5823 O O . GLN A 744 ? 0.2094 0.4076 0.2708 -0.0395 -0.0197 -0.0182 779 GLN A O 5824 C CB . GLN A 744 ? 0.2213 0.4480 0.2767 -0.0457 -0.0325 -0.0164 779 GLN A CB 5825 C CG . GLN A 744 ? 0.2451 0.4906 0.3014 -0.0442 -0.0397 -0.0124 779 GLN A CG 5826 C CD . GLN A 744 ? 0.2749 0.5148 0.3179 -0.0504 -0.0419 -0.0146 779 GLN A CD 5827 O OE1 . GLN A 744 ? 0.2655 0.4847 0.2989 -0.0515 -0.0383 -0.0169 779 GLN A OE1 5828 N NE2 . GLN A 744 ? 0.2900 0.5495 0.3325 -0.0545 -0.0478 -0.0142 779 GLN A NE2 5829 N N . PRO A 745 ? 0.2030 0.4247 0.2698 -0.0553 -0.0204 -0.0257 780 PRO A N 5830 C CA . PRO A 745 ? 0.2124 0.4160 0.2752 -0.0589 -0.0141 -0.0290 780 PRO A CA 5831 C C . PRO A 745 ? 0.2174 0.3980 0.2669 -0.0615 -0.0125 -0.0310 780 PRO A C 5832 O O . PRO A 745 ? 0.2164 0.3976 0.2597 -0.0641 -0.0157 -0.0320 780 PRO A O 5833 C CB . PRO A 745 ? 0.2199 0.4357 0.2869 -0.0699 -0.0125 -0.0341 780 PRO A CB 5834 C CG . PRO A 745 ? 0.2381 0.4720 0.3059 -0.0749 -0.0181 -0.0353 780 PRO A CG 5835 C CD . PRO A 745 ? 0.2271 0.4707 0.2988 -0.0641 -0.0234 -0.0289 780 PRO A CD 5836 N N . ALA A 746 ? 0.2252 0.3867 0.2706 -0.0605 -0.0075 -0.0316 781 ALA A N 5837 C CA . ALA A 746 ? 0.2230 0.3630 0.2571 -0.0612 -0.0059 -0.0328 781 ALA A CA 5838 C C . ALA A 746 ? 0.2583 0.3952 0.2850 -0.0712 -0.0060 -0.0384 781 ALA A C 5839 O O . ALA A 746 ? 0.2430 0.3699 0.2615 -0.0710 -0.0067 -0.0394 781 ALA A O 5840 C CB . ALA A 746 ? 0.2332 0.3558 0.2648 -0.0594 -0.0009 -0.0325 781 ALA A CB 5841 N N . ASP A 747 ? 0.2761 0.4221 0.3058 -0.0801 -0.0051 -0.0424 782 ASP A N 5842 C CA . ASP A 747 ? 0.3201 0.4617 0.3425 -0.0906 -0.0045 -0.0484 782 ASP A CA 5843 C C . ASP A 747 ? 0.3393 0.4979 0.3611 -0.0943 -0.0098 -0.0502 782 ASP A C 5844 O O . ASP A 747 ? 0.3902 0.5457 0.4053 -0.1035 -0.0093 -0.0559 782 ASP A O 5845 C CB . ASP A 747 ? 0.3699 0.5110 0.3941 -0.1000 -0.0006 -0.0523 782 ASP A CB 5846 C CG . ASP A 747 ? 0.3880 0.5550 0.4228 -0.1043 -0.0028 -0.0526 782 ASP A CG 5847 O OD1 . ASP A 747 ? 0.3919 0.5766 0.4350 -0.0971 -0.0068 -0.0485 782 ASP A OD1 5848 O OD2 . ASP A 747 ? 0.4878 0.6573 0.5227 -0.1149 -0.0005 -0.0571 782 ASP A OD2 5849 N N . LYS A 748 ? 0.3355 0.5112 0.3637 -0.0875 -0.0146 -0.0453 783 LYS A N 5850 C CA . LYS A 748 ? 0.3598 0.5532 0.3872 -0.0904 -0.0204 -0.0457 783 LYS A CA 5851 C C . LYS A 748 ? 0.3352 0.5312 0.3624 -0.0797 -0.0244 -0.0391 783 LYS A C 5852 O O . LYS A 748 ? 0.3507 0.5666 0.3842 -0.0763 -0.0296 -0.0350 783 LYS A O 5853 C CB . LYS A 748 ? 0.3990 0.6182 0.4369 -0.0953 -0.0232 -0.0463 783 LYS A CB 5854 C CG . LYS A 748 ? 0.4504 0.6689 0.4878 -0.1080 -0.0196 -0.0532 783 LYS A CG 5855 C CD . LYS A 748 ? 0.5069 0.7542 0.5556 -0.1131 -0.0228 -0.0537 783 LYS A CD 5856 C CE . LYS A 748 ? 0.5630 0.8108 0.6093 -0.1282 -0.0198 -0.0613 783 LYS A CE 5857 N NZ . LYS A 748 ? 0.5936 0.8246 0.6400 -0.1304 -0.0127 -0.0627 783 LYS A NZ 5858 N N . CYS A 749 ? 0.3083 0.4842 0.3284 -0.0745 -0.0219 -0.0377 784 CYS A N 5859 C CA . CYS A 749 ? 0.2819 0.4561 0.3008 -0.0648 -0.0245 -0.0314 784 CYS A CA 5860 C C . CYS A 749 ? 0.3113 0.4860 0.3203 -0.0682 -0.0272 -0.0329 784 CYS A C 5861 O O . CYS A 749 ? 0.3252 0.4861 0.3254 -0.0733 -0.0240 -0.0382 784 CYS A O 5862 C CB . CYS A 749 ? 0.2645 0.4175 0.2811 -0.0583 -0.0200 -0.0294 784 CYS A CB 5863 S SG . CYS A 749 ? 0.2881 0.4367 0.3030 -0.0473 -0.0224 -0.0217 784 CYS A SG 5864 N N . ASP A 750 ? 0.3100 0.5003 0.3202 -0.0648 -0.0329 -0.0280 785 ASP A N 5865 C CA . ASP A 750 ? 0.3396 0.5329 0.3397 -0.0680 -0.0361 -0.0287 785 ASP A CA 5866 C C . ASP A 750 ? 0.3277 0.5060 0.3205 -0.0619 -0.0348 -0.0252 785 ASP A C 5867 O O . ASP A 750 ? 0.3557 0.5312 0.3383 -0.0657 -0.0351 -0.0277 785 ASP A O 5868 C CB . ASP A 750 ? 0.3562 0.5736 0.3602 -0.0666 -0.0434 -0.0236 785 ASP A CB 5869 C CG . ASP A 750 ? 0.3932 0.6302 0.4025 -0.0750 -0.0460 -0.0278 785 ASP A CG 5870 O OD1 . ASP A 750 ? 0.4116 0.6431 0.4175 -0.0846 -0.0425 -0.0359 785 ASP A OD1 5871 O OD2 . ASP A 750 ? 0.4298 0.6883 0.4468 -0.0720 -0.0517 -0.0227 785 ASP A OD2 5872 N N . GLY A 751 ? 0.2721 0.4422 0.2698 -0.0527 -0.0334 -0.0195 786 GLY A N 5873 C CA . GLY A 751 ? 0.2738 0.4350 0.2663 -0.0464 -0.0337 -0.0143 786 GLY A CA 5874 C C . GLY A 751 ? 0.2420 0.3830 0.2337 -0.0424 -0.0283 -0.0146 786 GLY A C 5875 O O . GLY A 751 ? 0.2208 0.3519 0.2118 -0.0462 -0.0241 -0.0201 786 GLY A O 5876 N N . PRO A 752 ? 0.2591 0.3939 0.2507 -0.0349 -0.0287 -0.0082 787 PRO A N 5877 C CA . PRO A 752 ? 0.2297 0.3470 0.2208 -0.0313 -0.0241 -0.0081 787 PRO A CA 5878 C C . PRO A 752 ? 0.2229 0.3353 0.2213 -0.0304 -0.0208 -0.0103 787 PRO A C 5879 O O . PRO A 752 ? 0.1951 0.3182 0.2012 -0.0298 -0.0223 -0.0096 787 PRO A O 5880 C CB . PRO A 752 ? 0.2526 0.3678 0.2438 -0.0238 -0.0260 -0.0003 787 PRO A CB 5881 C CG . PRO A 752 ? 0.2679 0.3955 0.2550 -0.0249 -0.0309 0.0029 787 PRO A CG 5882 C CD . PRO A 752 ? 0.2549 0.3980 0.2455 -0.0301 -0.0334 -0.0007 787 PRO A CD 5883 N N . LEU A 753 ? 0.2082 0.3056 0.2040 -0.0306 -0.0165 -0.0128 788 LEU A N 5884 C CA . LEU A 753 ? 0.2125 0.3027 0.2127 -0.0304 -0.0130 -0.0148 788 LEU A CA 5885 C C . LEU A 753 ? 0.2115 0.2944 0.2146 -0.0235 -0.0118 -0.0104 788 LEU A C 5886 O O . LEU A 753 ? 0.2200 0.2993 0.2204 -0.0196 -0.0128 -0.0065 788 LEU A O 5887 C CB . LEU A 753 ? 0.2295 0.3075 0.2242 -0.0349 -0.0092 -0.0201 788 LEU A CB 5888 C CG . LEU A 753 ? 0.2327 0.3149 0.2235 -0.0424 -0.0095 -0.0257 788 LEU A CG 5889 C CD1 . LEU A 753 ? 0.2464 0.3142 0.2318 -0.0452 -0.0053 -0.0304 788 LEU A CD1 5890 C CD2 . LEU A 753 ? 0.2349 0.3282 0.2314 -0.0466 -0.0105 -0.0276 788 LEU A CD2 5891 N N . SER A 754 ? 0.2099 0.2906 0.2183 -0.0226 -0.0094 -0.0112 789 SER A N 5892 C CA . SER A 754 ? 0.2056 0.2782 0.2160 -0.0172 -0.0074 -0.0084 789 SER A CA 5893 C C . SER A 754 ? 0.1959 0.2577 0.2044 -0.0199 -0.0035 -0.0117 789 SER A C 5894 O O . SER A 754 ? 0.1900 0.2541 0.1999 -0.0244 -0.0022 -0.0150 789 SER A O 5895 C CB . SER A 754 ? 0.2218 0.3040 0.2407 -0.0132 -0.0081 -0.0062 789 SER A CB 5896 O OG . SER A 754 ? 0.2241 0.2976 0.2445 -0.0088 -0.0053 -0.0048 789 SER A OG 5897 N N . VAL A 755 ? 0.1802 0.2304 0.1852 -0.0174 -0.0018 -0.0105 790 VAL A N 5898 C CA . VAL A 755 ? 0.1918 0.2320 0.1943 -0.0196 0.0012 -0.0128 790 VAL A CA 5899 C C . VAL A 755 ? 0.1917 0.2247 0.1945 -0.0159 0.0029 -0.0107 790 VAL A C 5900 O O . VAL A 755 ? 0.2057 0.2372 0.2081 -0.0122 0.0019 -0.0079 790 VAL A O 5901 C CB . VAL A 755 ? 0.2041 0.2372 0.2006 -0.0219 0.0017 -0.0147 790 VAL A CB 5902 C CG1 . VAL A 755 ? 0.2230 0.2522 0.2164 -0.0187 0.0009 -0.0120 790 VAL A CG1 5903 C CG2 . VAL A 755 ? 0.1971 0.2208 0.1917 -0.0240 0.0045 -0.0167 790 VAL A CG2 5904 N N . SER A 756 ? 0.1956 0.2243 0.1985 -0.0175 0.0055 -0.0122 791 SER A N 5905 C CA . SER A 756 ? 0.2167 0.2371 0.2176 -0.0156 0.0073 -0.0111 791 SER A CA 5906 C C . SER A 756 ? 0.2208 0.2341 0.2181 -0.0189 0.0090 -0.0126 791 SER A C 5907 O O . SER A 756 ? 0.2186 0.2335 0.2164 -0.0225 0.0100 -0.0145 791 SER A O 5908 C CB . SER A 756 ? 0.2329 0.2564 0.2379 -0.0133 0.0088 -0.0107 791 SER A CB 5909 O OG . SER A 756 ? 0.2799 0.3091 0.2882 -0.0162 0.0103 -0.0127 791 SER A OG 5910 N N . SER A 757 ? 0.1928 0.1986 0.1864 -0.0177 0.0094 -0.0114 792 SER A N 5911 C CA . SER A 757 ? 0.1994 0.1983 0.1895 -0.0197 0.0105 -0.0118 792 SER A CA 5912 C C . SER A 757 ? 0.1866 0.1805 0.1741 -0.0186 0.0113 -0.0103 792 SER A C 5913 O O . SER A 757 ? 0.1733 0.1676 0.1611 -0.0165 0.0109 -0.0093 792 SER A O 5914 C CB . SER A 757 ? 0.2250 0.2209 0.2129 -0.0194 0.0095 -0.0121 792 SER A CB 5915 O OG . SER A 757 ? 0.2443 0.2452 0.2335 -0.0207 0.0086 -0.0139 792 SER A OG 5916 N N . PHE A 758 ? 0.1857 0.1743 0.1702 -0.0203 0.0123 -0.0099 793 PHE A N 5917 C CA A PHE A 758 ? 0.1867 0.1713 0.1678 -0.0203 0.0129 -0.0083 793 PHE A CA 5918 C CA B PHE A 758 ? 0.1919 0.1765 0.1730 -0.0199 0.0126 -0.0082 793 PHE A CA 5919 C C . PHE A 758 ? 0.1877 0.1665 0.1654 -0.0203 0.0122 -0.0067 793 PHE A C 5920 O O . PHE A 758 ? 0.1863 0.1623 0.1640 -0.0213 0.0126 -0.0071 793 PHE A O 5921 C CB A PHE A 758 ? 0.1949 0.1804 0.1755 -0.0227 0.0153 -0.0090 793 PHE A CB 5922 C CB B PHE A 758 ? 0.2085 0.1941 0.1890 -0.0214 0.0147 -0.0087 793 PHE A CB 5923 C CG A PHE A 758 ? 0.1967 0.1888 0.1819 -0.0220 0.0164 -0.0107 793 PHE A CG 5924 C CG B PHE A 758 ? 0.2159 0.2009 0.1957 -0.0248 0.0167 -0.0092 793 PHE A CG 5925 C CD1 A PHE A 758 ? 0.1865 0.1793 0.1720 -0.0197 0.0168 -0.0108 793 PHE A CD1 5926 C CD1 B PHE A 758 ? 0.2266 0.2054 0.2020 -0.0266 0.0169 -0.0074 793 PHE A CD1 5927 C CD2 A PHE A 758 ? 0.1993 0.1972 0.1886 -0.0235 0.0170 -0.0122 793 PHE A CD2 5928 C CD2 B PHE A 758 ? 0.2274 0.2186 0.2114 -0.0261 0.0183 -0.0111 793 PHE A CD2 5929 C CE1 A PHE A 758 ? 0.1835 0.1818 0.1737 -0.0178 0.0180 -0.0121 793 PHE A CE1 5930 C CE1 B PHE A 758 ? 0.2324 0.2093 0.2064 -0.0304 0.0190 -0.0076 793 PHE A CE1 5931 C CE2 A PHE A 758 ? 0.2055 0.2113 0.2002 -0.0220 0.0177 -0.0133 793 PHE A CE2 5932 C CE2 B PHE A 758 ? 0.2183 0.2096 0.2016 -0.0302 0.0204 -0.0117 793 PHE A CE2 5933 C CZ A PHE A 758 ? 0.2000 0.2056 0.1953 -0.0186 0.0183 -0.0131 793 PHE A CZ 5934 C CZ B PHE A 758 ? 0.2239 0.2074 0.2018 -0.0327 0.0210 -0.0099 793 PHE A CZ 5935 N N . ILE A 759 ? 0.1856 0.1627 0.1607 -0.0193 0.0112 -0.0047 794 ILE A N 5936 C CA . ILE A 759 ? 0.1861 0.1588 0.1582 -0.0187 0.0104 -0.0023 794 ILE A CA 5937 C C . ILE A 759 ? 0.2064 0.1783 0.1742 -0.0203 0.0105 -0.0007 794 ILE A C 5938 O O . ILE A 759 ? 0.1961 0.1703 0.1628 -0.0199 0.0094 -0.0003 794 ILE A O 5939 C CB . ILE A 759 ? 0.1922 0.1664 0.1659 -0.0157 0.0084 -0.0014 794 ILE A CB 5940 C CG1 . ILE A 759 ? 0.1863 0.1617 0.1633 -0.0145 0.0086 -0.0036 794 ILE A CG1 5941 C CG2 . ILE A 759 ? 0.1985 0.1692 0.1701 -0.0142 0.0073 0.0016 794 ILE A CG2 5942 C CD1 . ILE A 759 ? 0.1705 0.1497 0.1495 -0.0122 0.0073 -0.0035 794 ILE A CD1 5943 N N . LEU A 760 ? 0.2182 0.1869 0.1830 -0.0228 0.0122 0.0000 795 LEU A N 5944 C CA . LEU A 760 ? 0.2412 0.2098 0.2009 -0.0250 0.0128 0.0011 795 LEU A CA 5945 C C . LEU A 760 ? 0.2357 0.2013 0.1908 -0.0244 0.0107 0.0052 795 LEU A C 5946 O O . LEU A 760 ? 0.2271 0.1877 0.1815 -0.0235 0.0103 0.0077 795 LEU A O 5947 C CB . LEU A 760 ? 0.2804 0.2479 0.2384 -0.0286 0.0159 0.0004 795 LEU A CB 5948 C CG . LEU A 760 ? 0.3557 0.3280 0.3190 -0.0291 0.0181 -0.0032 795 LEU A CG 5949 C CD1 . LEU A 760 ? 0.3783 0.3518 0.3403 -0.0331 0.0215 -0.0042 795 LEU A CD1 5950 C CD2 . LEU A 760 ? 0.3845 0.3613 0.3508 -0.0269 0.0178 -0.0055 795 LEU A CD2 5951 N N . PRO A 761 ? 0.2371 0.2056 0.1888 -0.0250 0.0092 0.0061 796 PRO A N 5952 C CA . PRO A 761 ? 0.2405 0.2081 0.1877 -0.0246 0.0066 0.0105 796 PRO A CA 5953 C C . PRO A 761 ? 0.2416 0.2042 0.1826 -0.0272 0.0080 0.0134 796 PRO A C 5954 O O . PRO A 761 ? 0.2509 0.2139 0.1884 -0.0310 0.0108 0.0115 796 PRO A O 5955 C CB . PRO A 761 ? 0.2682 0.2411 0.2125 -0.0263 0.0052 0.0096 796 PRO A CB 5956 C CG . PRO A 761 ? 0.2924 0.2676 0.2414 -0.0259 0.0064 0.0052 796 PRO A CG 5957 C CD . PRO A 761 ? 0.2654 0.2380 0.2172 -0.0260 0.0096 0.0030 796 PRO A CD 5958 N N . HIS A 762 ? 0.2365 0.1942 0.1763 -0.0251 0.0065 0.0178 797 HIS A N 5959 C CA . HIS A 762 ? 0.2479 0.1992 0.1808 -0.0276 0.0076 0.0218 797 HIS A CA 5960 C C . HIS A 762 ? 0.2541 0.2085 0.1800 -0.0286 0.0048 0.0259 797 HIS A C 5961 O O . HIS A 762 ? 0.2653 0.2186 0.1900 -0.0252 0.0014 0.0312 797 HIS A O 5962 C CB . HIS A 762 ? 0.2479 0.1907 0.1824 -0.0247 0.0075 0.0248 797 HIS A CB 5963 C CG . HIS A 762 ? 0.2626 0.1970 0.1896 -0.0275 0.0087 0.0294 797 HIS A CG 5964 N ND1 . HIS A 762 ? 0.2743 0.1996 0.1992 -0.0243 0.0074 0.0349 797 HIS A ND1 5965 C CD2 . HIS A 762 ? 0.2625 0.1960 0.1832 -0.0333 0.0114 0.0296 797 HIS A CD2 5966 C CE1 . HIS A 762 ? 0.2856 0.2040 0.2027 -0.0284 0.0090 0.0388 797 HIS A CE1 5967 N NE2 . HIS A 762 ? 0.2885 0.2122 0.2029 -0.0341 0.0115 0.0355 797 HIS A NE2 5968 N N . ARG A 763 ? 0.2701 0.2287 0.1914 -0.0330 0.0063 0.0235 798 ARG A N 5969 C CA . ARG A 763 ? 0.2751 0.2380 0.1889 -0.0350 0.0037 0.0262 798 ARG A CA 5970 C C . ARG A 763 ? 0.2852 0.2447 0.1891 -0.0398 0.0057 0.0291 798 ARG A C 5971 O O . ARG A 763 ? 0.2808 0.2376 0.1841 -0.0431 0.0102 0.0262 798 ARG A O 5972 C CB . ARG A 763 ? 0.2934 0.2635 0.2081 -0.0368 0.0038 0.0209 798 ARG A CB 5973 C CG . ARG A 763 ? 0.2949 0.2691 0.2176 -0.0326 0.0009 0.0198 798 ARG A CG 5974 C CD . ARG A 763 ? 0.3444 0.3240 0.2676 -0.0347 0.0010 0.0150 798 ARG A CD 5975 N NE . ARG A 763 ? 0.3710 0.3547 0.2857 -0.0390 -0.0005 0.0154 798 ARG A NE 5976 C CZ . ARG A 763 ? 0.3818 0.3693 0.2950 -0.0421 -0.0004 0.0110 798 ARG A CZ 5977 N NH1 . ARG A 763 ? 0.3829 0.3700 0.3025 -0.0409 0.0010 0.0066 798 ARG A NH1 5978 N NH2 . ARG A 763 ? 0.4143 0.4055 0.3186 -0.0468 -0.0017 0.0111 798 ARG A NH2 5979 N N . PRO A 764 ? 0.2903 0.2511 0.1864 -0.0405 0.0022 0.0348 799 PRO A N 5980 C CA . PRO A 764 ? 0.3051 0.2628 0.1902 -0.0453 0.0037 0.0387 799 PRO A CA 5981 C C . PRO A 764 ? 0.3135 0.2767 0.1919 -0.0515 0.0067 0.0338 799 PRO A C 5982 O O . PRO A 764 ? 0.3182 0.2802 0.1866 -0.0564 0.0084 0.0361 799 PRO A O 5983 C CB . PRO A 764 ? 0.3177 0.2765 0.1978 -0.0428 -0.0020 0.0468 799 PRO A CB 5984 C CG . PRO A 764 ? 0.3051 0.2732 0.1911 -0.0399 -0.0059 0.0445 799 PRO A CG 5985 C CD . PRO A 764 ? 0.2933 0.2593 0.1907 -0.0365 -0.0035 0.0389 799 PRO A CD 5986 N N . ASP A 765 ? 0.2898 0.2585 0.1730 -0.0514 0.0074 0.0270 800 ASP A N 5987 C CA . ASP A 765 ? 0.3108 0.2832 0.1888 -0.0565 0.0112 0.0209 800 ASP A CA 5988 C C . ASP A 765 ? 0.2812 0.2545 0.1689 -0.0545 0.0143 0.0135 800 ASP A C 5989 O O . ASP A 765 ? 0.2696 0.2420 0.1667 -0.0497 0.0124 0.0136 800 ASP A O 5990 C CB . ASP A 765 ? 0.3324 0.3111 0.2027 -0.0592 0.0076 0.0214 800 ASP A CB 5991 C CG . ASP A 765 ? 0.3554 0.3383 0.2329 -0.0554 0.0031 0.0207 800 ASP A CG 5992 O OD1 . ASP A 765 ? 0.3412 0.3244 0.2254 -0.0544 0.0050 0.0146 800 ASP A OD1 5993 O OD2 . ASP A 765 ? 0.4193 0.4052 0.2962 -0.0532 -0.0023 0.0267 800 ASP A OD2 5994 N N . ASN A 766 ? 0.2711 0.2461 0.1561 -0.0578 0.0190 0.0074 801 ASN A N 5995 C CA . ASN A 766 ? 0.2604 0.2362 0.1536 -0.0556 0.0218 0.0006 801 ASN A CA 5996 C C . ASN A 766 ? 0.2534 0.2313 0.1427 -0.0576 0.0216 -0.0039 801 ASN A C 5997 O O . ASN A 766 ? 0.2506 0.2280 0.1414 -0.0580 0.0260 -0.0104 801 ASN A O 5998 C CB . ASN A 766 ? 0.2616 0.2371 0.1572 -0.0567 0.0280 -0.0030 801 ASN A CB 5999 C CG . ASN A 766 ? 0.2549 0.2283 0.1573 -0.0546 0.0282 0.0000 801 ASN A CG 6000 O OD1 . ASN A 766 ? 0.2462 0.2188 0.1573 -0.0504 0.0263 0.0000 801 ASN A OD1 6001 N ND2 . ASN A 766 ? 0.2642 0.2364 0.1616 -0.0583 0.0307 0.0026 801 ASN A ND2 6002 N N . ASP A 767 ? 0.2690 0.2494 0.1538 -0.0587 0.0164 -0.0007 802 ASP A N 6003 C CA . ASP A 767 ? 0.2719 0.2546 0.1523 -0.0618 0.0156 -0.0050 802 ASP A CA 6004 C C . ASP A 767 ? 0.2623 0.2429 0.1516 -0.0587 0.0167 -0.0098 802 ASP A C 6005 O O . ASP A 767 ? 0.2623 0.2414 0.1486 -0.0613 0.0190 -0.0156 802 ASP A O 6006 C CB . ASP A 767 ? 0.2805 0.2686 0.1560 -0.0635 0.0092 -0.0002 802 ASP A CB 6007 C CG . ASP A 767 ? 0.3115 0.3019 0.1760 -0.0671 0.0077 0.0048 802 ASP A CG 6008 O OD1 . ASP A 767 ? 0.3078 0.2955 0.1670 -0.0695 0.0122 0.0038 802 ASP A OD1 6009 O OD2 . ASP A 767 ? 0.3541 0.3497 0.2154 -0.0674 0.0018 0.0102 802 ASP A OD2 6010 N N . GLU A 768 ? 0.2615 0.2409 0.1609 -0.0534 0.0154 -0.0075 803 GLU A N 6011 C CA . GLU A 768 ? 0.2661 0.2432 0.1736 -0.0503 0.0165 -0.0112 803 GLU A CA 6012 C C . GLU A 768 ? 0.2776 0.2511 0.1862 -0.0501 0.0225 -0.0172 803 GLU A C 6013 O O . GLU A 768 ? 0.2765 0.2469 0.1873 -0.0494 0.0239 -0.0213 803 GLU A O 6014 C CB . GLU A 768 ? 0.2694 0.2465 0.1866 -0.0451 0.0145 -0.0077 803 GLU A CB 6015 C CG . GLU A 768 ? 0.2705 0.2461 0.1950 -0.0421 0.0147 -0.0102 803 GLU A CG 6016 C CD . GLU A 768 ? 0.2664 0.2427 0.1993 -0.0376 0.0127 -0.0071 803 GLU A CD 6017 O OE1 . GLU A 768 ? 0.2430 0.2202 0.1763 -0.0364 0.0110 -0.0031 803 GLU A OE1 6018 O OE2 . GLU A 768 ? 0.2528 0.2280 0.1911 -0.0353 0.0131 -0.0089 803 GLU A OE2 6019 N N . SER A 769 ? 0.2625 0.2363 0.1694 -0.0508 0.0261 -0.0176 804 SER A N 6020 C CA . SER A 769 ? 0.2608 0.2332 0.1704 -0.0496 0.0321 -0.0228 804 SER A CA 6021 C C . SER A 769 ? 0.2772 0.2492 0.1769 -0.0545 0.0360 -0.0273 804 SER A C 6022 O O . SER A 769 ? 0.2690 0.2435 0.1623 -0.0579 0.0375 -0.0260 804 SER A O 6023 C CB . SER A 769 ? 0.2532 0.2280 0.1683 -0.0477 0.0339 -0.0206 804 SER A CB 6024 O OG . SER A 769 ? 0.2362 0.2109 0.1602 -0.0435 0.0306 -0.0175 804 SER A OG 6025 N N . CYS A 770 ? 0.2691 0.2372 0.1668 -0.0551 0.0380 -0.0328 805 CYS A N 6026 C CA . CYS A 770 ? 0.3038 0.2707 0.1906 -0.0604 0.0418 -0.0380 805 CYS A CA 6027 C C . CYS A 770 ? 0.2945 0.2629 0.1815 -0.0599 0.0486 -0.0416 805 CYS A C 6028 O O . CYS A 770 ? 0.2967 0.2664 0.1737 -0.0650 0.0518 -0.0445 805 CYS A O 6029 C CB . CYS A 770 ? 0.3272 0.2877 0.2118 -0.0613 0.0430 -0.0438 805 CYS A CB 6030 S SG . CYS A 770 ? 0.3703 0.3312 0.2531 -0.0641 0.0355 -0.0405 805 CYS A SG 6031 N N . ALA A 771 ? 0.2893 0.2589 0.1874 -0.0544 0.0508 -0.0414 806 ALA A N 6032 C CA . ALA A 771 ? 0.2898 0.2631 0.1900 -0.0537 0.0574 -0.0448 806 ALA A CA 6033 C C . ALA A 771 ? 0.2918 0.2713 0.1925 -0.0556 0.0571 -0.0398 806 ALA A C 6034 O O . ALA A 771 ? 0.3137 0.2980 0.2186 -0.0549 0.0623 -0.0420 806 ALA A O 6035 C CB . ALA A 771 ? 0.2926 0.2650 0.2049 -0.0466 0.0606 -0.0480 806 ALA A CB 6036 N N . SER A 772 ? 0.2886 0.2682 0.1846 -0.0584 0.0515 -0.0334 807 SER A N 6037 C CA . SER A 772 ? 0.2894 0.2722 0.1864 -0.0598 0.0506 -0.0279 807 SER A CA 6038 C C . SER A 772 ? 0.3187 0.3050 0.2074 -0.0653 0.0556 -0.0287 807 SER A C 6039 O O . SER A 772 ? 0.3342 0.3231 0.2251 -0.0667 0.0566 -0.0252 807 SER A O 6040 C CB . SER A 772 ? 0.2762 0.2568 0.1703 -0.0604 0.0436 -0.0206 807 SER A CB 6041 O OG . SER A 772 ? 0.2790 0.2591 0.1608 -0.0651 0.0413 -0.0188 807 SER A OG 6042 N N . SER A 773 ? 0.3477 0.3341 0.2268 -0.0691 0.0591 -0.0333 808 SER A N 6043 C CA . SER A 773 ? 0.3937 0.3844 0.2657 -0.0743 0.0651 -0.0351 808 SER A CA 6044 C C . SER A 773 ? 0.4055 0.4016 0.2879 -0.0713 0.0721 -0.0401 808 SER A C 6045 O O . SER A 773 ? 0.4326 0.4340 0.3122 -0.0752 0.0771 -0.0407 808 SER A O 6046 C CB . SER A 773 ? 0.4282 0.4181 0.2861 -0.0796 0.0673 -0.0392 808 SER A CB 6047 O OG . SER A 773 ? 0.4421 0.4302 0.2896 -0.0834 0.0607 -0.0334 808 SER A OG 6048 N N . GLU A 774 ? 0.3916 0.3871 0.2861 -0.0645 0.0723 -0.0434 809 GLU A N 6049 C CA . GLU A 774 ? 0.3895 0.3913 0.2955 -0.0604 0.0782 -0.0477 809 GLU A CA 6050 C C . GLU A 774 ? 0.3787 0.3857 0.2943 -0.0595 0.0762 -0.0427 809 GLU A C 6051 O O . GLU A 774 ? 0.3598 0.3634 0.2729 -0.0614 0.0705 -0.0362 809 GLU A O 6052 C CB . GLU A 774 ? 0.4273 0.4257 0.3416 -0.0532 0.0789 -0.0526 809 GLU A CB 6053 C CG . GLU A 774 ? 0.5233 0.5148 0.4278 -0.0547 0.0813 -0.0583 809 GLU A CG 6054 C CD . GLU A 774 ? 0.6061 0.5916 0.5180 -0.0478 0.0819 -0.0625 809 GLU A CD 6055 O OE1 . GLU A 774 ? 0.7039 0.6930 0.6289 -0.0411 0.0835 -0.0631 809 GLU A OE1 6056 O OE2 . GLU A 774 ? 0.7985 0.7755 0.7027 -0.0493 0.0808 -0.0651 809 GLU A OE2 6057 N N . ASP A 775 ? 0.3525 0.3681 0.2790 -0.0568 0.0810 -0.0459 810 ASP A N 6058 C CA . ASP A 775 ? 0.3584 0.3802 0.2949 -0.0562 0.0795 -0.0423 810 ASP A CA 6059 C C . ASP A 775 ? 0.3248 0.3416 0.2678 -0.0512 0.0724 -0.0388 810 ASP A C 6060 O O . ASP A 775 ? 0.3161 0.3286 0.2617 -0.0459 0.0709 -0.0410 810 ASP A O 6061 C CB . ASP A 775 ? 0.3842 0.4180 0.3332 -0.0528 0.0855 -0.0471 810 ASP A CB 6062 C CG . ASP A 775 ? 0.4188 0.4609 0.3775 -0.0540 0.0844 -0.0440 810 ASP A CG 6063 O OD1 . ASP A 775 ? 0.4817 0.5275 0.4359 -0.0611 0.0867 -0.0421 810 ASP A OD1 6064 O OD2 . ASP A 775 ? 0.4502 0.4951 0.4202 -0.0483 0.0811 -0.0434 810 ASP A OD2 6065 N N . GLU A 776 ? 0.3278 0.3446 0.2728 -0.0533 0.0686 -0.0337 811 GLU A N 6066 C CA . GLU A 776 ? 0.3124 0.3246 0.2623 -0.0495 0.0621 -0.0302 811 GLU A CA 6067 C C . GLU A 776 ? 0.2997 0.3162 0.2621 -0.0422 0.0616 -0.0329 811 GLU A C 6068 O O . GLU A 776 ? 0.2587 0.2699 0.2231 -0.0382 0.0568 -0.0312 811 GLU A O 6069 C CB . GLU A 776 ? 0.3136 0.3257 0.2640 -0.0533 0.0595 -0.0253 811 GLU A CB 6070 C CG . GLU A 776 ? 0.3455 0.3494 0.2834 -0.0585 0.0574 -0.0205 811 GLU A CG 6071 C CD . GLU A 776 ? 0.3877 0.3942 0.3180 -0.0656 0.0623 -0.0201 811 GLU A CD 6072 O OE1 . GLU A 776 ? 0.3808 0.3963 0.3155 -0.0667 0.0681 -0.0243 811 GLU A OE1 6073 O OE2 . GLU A 776 ? 0.4526 0.4523 0.3724 -0.0698 0.0605 -0.0152 811 GLU A OE2 6074 N N . SER A 777 ? 0.2944 0.3207 0.2650 -0.0403 0.0666 -0.0367 812 SER A N 6075 C CA . SER A 777 ? 0.3071 0.3379 0.2893 -0.0325 0.0666 -0.0391 812 SER A CA 6076 C C . SER A 777 ? 0.3231 0.3451 0.3024 -0.0276 0.0665 -0.0414 812 SER A C 6077 O O . SER A 777 ? 0.3431 0.3655 0.3305 -0.0209 0.0652 -0.0419 812 SER A O 6078 C CB . SER A 777 ? 0.3200 0.3645 0.3116 -0.0311 0.0727 -0.0429 812 SER A CB 6079 O OG . SER A 777 ? 0.3298 0.3741 0.3154 -0.0328 0.0790 -0.0474 812 SER A OG 6080 N N . LYS A 778 ? 0.3252 0.3393 0.2928 -0.0311 0.0677 -0.0428 813 LYS A N 6081 C CA . LYS A 778 ? 0.3396 0.3442 0.3028 -0.0282 0.0678 -0.0456 813 LYS A CA 6082 C C . LYS A 778 ? 0.3213 0.3164 0.2781 -0.0295 0.0614 -0.0419 813 LYS A C 6083 O O . LYS A 778 ? 0.3091 0.2963 0.2623 -0.0279 0.0611 -0.0440 813 LYS A O 6084 C CB . LYS A 778 ? 0.3836 0.3863 0.3372 -0.0319 0.0737 -0.0507 813 LYS A CB 6085 C CG . LYS A 778 ? 0.4388 0.4516 0.3979 -0.0311 0.0811 -0.0551 813 LYS A CG 6086 C CD . LYS A 778 ? 0.4912 0.5072 0.4634 -0.0220 0.0834 -0.0580 813 LYS A CD 6087 C CE . LYS A 778 ? 0.5624 0.5872 0.5392 -0.0202 0.0919 -0.0640 813 LYS A CE 6088 N NZ . LYS A 778 ? 0.6027 0.6320 0.5938 -0.0102 0.0935 -0.0657 813 LYS A NZ 6089 N N . TRP A 779 ? 0.2862 0.2818 0.2414 -0.0326 0.0567 -0.0367 814 TRP A N 6090 C CA . TRP A 779 ? 0.2691 0.2575 0.2185 -0.0339 0.0510 -0.0332 814 TRP A CA 6091 C C . TRP A 779 ? 0.2663 0.2553 0.2195 -0.0335 0.0456 -0.0280 814 TRP A C 6092 O O . TRP A 779 ? 0.2671 0.2512 0.2191 -0.0323 0.0413 -0.0258 814 TRP A O 6093 C CB . TRP A 779 ? 0.2814 0.2661 0.2179 -0.0399 0.0511 -0.0331 814 TRP A CB 6094 C CG . TRP A 779 ? 0.2791 0.2674 0.2108 -0.0449 0.0517 -0.0301 814 TRP A CG 6095 C CD1 . TRP A 779 ? 0.2763 0.2693 0.2055 -0.0482 0.0573 -0.0325 814 TRP A CD1 6096 C CD2 . TRP A 779 ? 0.2640 0.2504 0.1921 -0.0475 0.0471 -0.0241 814 TRP A CD2 6097 N NE1 . TRP A 779 ? 0.2806 0.2744 0.2044 -0.0531 0.0562 -0.0280 814 TRP A NE1 6098 C CE2 . TRP A 779 ? 0.2771 0.2662 0.2003 -0.0524 0.0499 -0.0227 814 TRP A CE2 6099 C CE3 . TRP A 779 ? 0.2593 0.2419 0.1882 -0.0459 0.0410 -0.0198 814 TRP A CE3 6100 C CZ2 . TRP A 779 ? 0.2838 0.2702 0.2023 -0.0555 0.0468 -0.0166 814 TRP A CZ2 6101 C CZ3 . TRP A 779 ? 0.2732 0.2542 0.1981 -0.0484 0.0381 -0.0143 814 TRP A CZ3 6102 C CH2 . TRP A 779 ? 0.2735 0.2555 0.1930 -0.0530 0.0409 -0.0126 814 TRP A CH2 6103 N N . VAL A 780 ? 0.2553 0.2498 0.2125 -0.0349 0.0461 -0.0262 815 VAL A N 6104 C CA . VAL A 780 ? 0.2492 0.2425 0.2081 -0.0353 0.0414 -0.0217 815 VAL A CA 6105 C C . VAL A 780 ? 0.2620 0.2558 0.2290 -0.0301 0.0383 -0.0213 815 VAL A C 6106 O O . VAL A 780 ? 0.2255 0.2152 0.1914 -0.0294 0.0340 -0.0185 815 VAL A O 6107 C CB . VAL A 780 ? 0.2519 0.2495 0.2121 -0.0391 0.0430 -0.0202 815 VAL A CB 6108 C CG1 . VAL A 780 ? 0.2458 0.2415 0.2090 -0.0388 0.0388 -0.0168 815 VAL A CG1 6109 C CG2 . VAL A 780 ? 0.2376 0.2324 0.1875 -0.0448 0.0448 -0.0186 815 VAL A CG2 6110 N N . GLU A 781 ? 0.2720 0.2716 0.2472 -0.0264 0.0405 -0.0238 816 GLU A N 6111 C CA . GLU A 781 ? 0.3036 0.3040 0.2858 -0.0215 0.0374 -0.0229 816 GLU A CA 6112 C C . GLU A 781 ? 0.2818 0.2744 0.2606 -0.0193 0.0350 -0.0224 816 GLU A C 6113 O O . GLU A 781 ? 0.2624 0.2534 0.2428 -0.0178 0.0311 -0.0199 816 GLU A O 6114 C CB . GLU A 781 ? 0.3496 0.3581 0.3414 -0.0171 0.0398 -0.0250 816 GLU A CB 6115 C CG . GLU A 781 ? 0.3915 0.4088 0.3906 -0.0175 0.0379 -0.0235 816 GLU A CG 6116 C CD . GLU A 781 ? 0.4290 0.4557 0.4385 -0.0122 0.0388 -0.0246 816 GLU A CD 6117 O OE1 . GLU A 781 ? 0.4158 0.4470 0.4285 -0.0104 0.0432 -0.0274 816 GLU A OE1 6118 O OE2 . GLU A 781 ? 0.4387 0.4688 0.4531 -0.0097 0.0350 -0.0226 816 GLU A OE2 6119 N N . GLU A 782 ? 0.2780 0.2657 0.2515 -0.0197 0.0376 -0.0250 817 GLU A N 6120 C CA . GLU A 782 ? 0.2855 0.2652 0.2545 -0.0192 0.0357 -0.0250 817 GLU A CA 6121 C C . GLU A 782 ? 0.2615 0.2390 0.2256 -0.0224 0.0312 -0.0215 817 GLU A C 6122 O O . GLU A 782 ? 0.2291 0.2038 0.1938 -0.0211 0.0280 -0.0198 817 GLU A O 6123 C CB . GLU A 782 ? 0.3244 0.2995 0.2873 -0.0206 0.0398 -0.0292 817 GLU A CB 6124 C CG . GLU A 782 ? 0.3905 0.3573 0.3466 -0.0224 0.0383 -0.0299 817 GLU A CG 6125 C CD . GLU A 782 ? 0.4342 0.3962 0.3830 -0.0250 0.0427 -0.0350 817 GLU A CD 6126 O OE1 . GLU A 782 ? 0.5094 0.4736 0.4597 -0.0236 0.0477 -0.0385 817 GLU A OE1 6127 O OE2 . GLU A 782 ? 0.4872 0.4437 0.4287 -0.0286 0.0415 -0.0359 817 GLU A OE2 6128 N N . LEU A 783 ? 0.2264 0.2055 0.1862 -0.0262 0.0311 -0.0201 818 LEU A N 6129 C CA . LEU A 783 ? 0.2270 0.2043 0.1828 -0.0283 0.0270 -0.0165 818 LEU A CA 6130 C C . LEU A 783 ? 0.2121 0.1912 0.1742 -0.0257 0.0241 -0.0140 818 LEU A C 6131 O O . LEU A 783 ? 0.2330 0.2105 0.1952 -0.0248 0.0207 -0.0121 818 LEU A O 6132 C CB . LEU A 783 ? 0.2208 0.1988 0.1708 -0.0323 0.0276 -0.0148 818 LEU A CB 6133 C CG . LEU A 783 ? 0.2216 0.1978 0.1684 -0.0333 0.0235 -0.0103 818 LEU A CG 6134 C CD1 . LEU A 783 ? 0.2275 0.2022 0.1695 -0.0342 0.0208 -0.0097 818 LEU A CD1 6135 C CD2 . LEU A 783 ? 0.2343 0.2100 0.1760 -0.0367 0.0245 -0.0078 818 LEU A CD2 6136 N N . MET A 784 ? 0.2217 0.2049 0.1893 -0.0248 0.0254 -0.0144 819 MET A N 6137 C CA . MET A 784 ? 0.2270 0.2121 0.1996 -0.0232 0.0230 -0.0128 819 MET A CA 6138 C C . MET A 784 ? 0.2054 0.1905 0.1817 -0.0196 0.0211 -0.0128 819 MET A C 6139 O O . MET A 784 ? 0.2024 0.1868 0.1794 -0.0189 0.0182 -0.0110 819 MET A O 6140 C CB . MET A 784 ? 0.2540 0.2446 0.2314 -0.0240 0.0248 -0.0137 819 MET A CB 6141 C CG . MET A 784 ? 0.3007 0.2899 0.2737 -0.0284 0.0262 -0.0126 819 MET A CG 6142 S SD . MET A 784 ? 0.3619 0.3585 0.3405 -0.0307 0.0291 -0.0143 819 MET A SD 6143 C CE . MET A 784 ? 0.3837 0.3837 0.3690 -0.0284 0.0258 -0.0141 819 MET A CE 6144 N N . LYS A 785 ? 0.2009 0.1861 0.1793 -0.0173 0.0229 -0.0146 820 LYS A N 6145 C CA . LYS A 785 ? 0.2098 0.1935 0.1908 -0.0139 0.0213 -0.0140 820 LYS A CA 6146 C C . LYS A 785 ? 0.2052 0.1836 0.1813 -0.0153 0.0191 -0.0127 820 LYS A C 6147 O O . LYS A 785 ? 0.1782 0.1565 0.1559 -0.0140 0.0167 -0.0110 820 LYS A O 6148 C CB . LYS A 785 ? 0.2341 0.2170 0.2178 -0.0106 0.0241 -0.0160 820 LYS A CB 6149 C CG . LYS A 785 ? 0.2484 0.2395 0.2394 -0.0083 0.0257 -0.0167 820 LYS A CG 6150 C CD . LYS A 785 ? 0.2991 0.2900 0.2934 -0.0042 0.0291 -0.0189 820 LYS A CD 6151 C CE . LYS A 785 ? 0.3370 0.3388 0.3397 -0.0019 0.0305 -0.0195 820 LYS A CE 6152 N NZ . LYS A 785 ? 0.3950 0.3964 0.4017 0.0032 0.0341 -0.0216 820 LYS A NZ 6153 N N . MET A 786 ? 0.2023 0.1776 0.1726 -0.0183 0.0197 -0.0136 821 MET A N 6154 C CA A MET A 786 ? 0.2050 0.1775 0.1712 -0.0202 0.0175 -0.0125 821 MET A CA 6155 C CA B MET A 786 ? 0.2010 0.1735 0.1671 -0.0203 0.0175 -0.0125 821 MET A CA 6156 C C . MET A 786 ? 0.1954 0.1708 0.1628 -0.0203 0.0143 -0.0097 821 MET A C 6157 O O . MET A 786 ? 0.1947 0.1701 0.1617 -0.0206 0.0122 -0.0085 821 MET A O 6158 C CB A MET A 786 ? 0.2279 0.1983 0.1873 -0.0239 0.0185 -0.0140 821 MET A CB 6159 C CB B MET A 786 ? 0.2177 0.1881 0.1769 -0.0240 0.0185 -0.0139 821 MET A CB 6160 C CG A MET A 786 ? 0.2550 0.2230 0.2101 -0.0265 0.0168 -0.0140 821 MET A CG 6161 C CG B MET A 786 ? 0.2343 0.2041 0.1890 -0.0269 0.0159 -0.0129 821 MET A CG 6162 S SD A MET A 786 ? 0.2588 0.2208 0.2150 -0.0253 0.0179 -0.0156 821 MET A SD 6163 S SD B MET A 786 ? 0.2339 0.1993 0.1886 -0.0273 0.0156 -0.0140 821 MET A SD 6164 C CE A MET A 786 ? 0.2631 0.2247 0.2132 -0.0308 0.0157 -0.0157 821 MET A CE 6165 C CE B MET A 786 ? 0.2520 0.2108 0.2066 -0.0254 0.0202 -0.0178 821 MET A CE 6166 N N . HIS A 787 ? 0.1797 0.1575 0.1486 -0.0202 0.0144 -0.0089 822 HIS A N 6167 C CA . HIS A 787 ? 0.1819 0.1610 0.1517 -0.0200 0.0122 -0.0067 822 HIS A CA 6168 C C . HIS A 787 ? 0.1904 0.1718 0.1652 -0.0181 0.0118 -0.0068 822 HIS A C 6169 O O . HIS A 787 ? 0.1941 0.1757 0.1696 -0.0180 0.0110 -0.0059 822 HIS A O 6170 C CB . HIS A 787 ? 0.1841 0.1620 0.1502 -0.0220 0.0125 -0.0055 822 HIS A CB 6171 C CG . HIS A 787 ? 0.1862 0.1632 0.1467 -0.0240 0.0117 -0.0047 822 HIS A CG 6172 N ND1 . HIS A 787 ? 0.1871 0.1653 0.1466 -0.0237 0.0088 -0.0025 822 HIS A ND1 6173 C CD2 . HIS A 787 ? 0.2039 0.1799 0.1596 -0.0265 0.0134 -0.0062 822 HIS A CD2 6174 C CE1 . HIS A 787 ? 0.1889 0.1674 0.1431 -0.0263 0.0082 -0.0024 822 HIS A CE1 6175 N NE2 . HIS A 787 ? 0.2070 0.1836 0.1583 -0.0282 0.0111 -0.0048 822 HIS A NE2 6176 N N . THR A 788 ? 0.1862 0.1692 0.1641 -0.0164 0.0124 -0.0078 823 THR A N 6177 C CA . THR A 788 ? 0.1789 0.1652 0.1607 -0.0148 0.0113 -0.0075 823 THR A CA 6178 C C . THR A 788 ? 0.1662 0.1525 0.1474 -0.0147 0.0093 -0.0064 823 THR A C 6179 O O . THR A 788 ? 0.1735 0.1582 0.1523 -0.0152 0.0086 -0.0055 823 THR A O 6180 C CB . THR A 788 ? 0.1851 0.1726 0.1695 -0.0124 0.0116 -0.0076 823 THR A CB 6181 O OG1 . THR A 788 ? 0.1808 0.1733 0.1689 -0.0112 0.0103 -0.0072 823 THR A OG1 6182 C CG2 . THR A 788 ? 0.1834 0.1668 0.1653 -0.0121 0.0109 -0.0066 823 THR A CG2 6183 N N . ALA A 789 ? 0.1733 0.1624 0.1566 -0.0143 0.0087 -0.0067 824 ALA A N 6184 C CA . ALA A 789 ? 0.1702 0.1596 0.1531 -0.0140 0.0075 -0.0063 824 ALA A CA 6185 C C . ALA A 789 ? 0.1613 0.1544 0.1460 -0.0136 0.0069 -0.0071 824 ALA A C 6186 O O . ALA A 789 ? 0.1610 0.1569 0.1475 -0.0139 0.0071 -0.0079 824 ALA A O 6187 C CB . ALA A 789 ? 0.1803 0.1668 0.1620 -0.0145 0.0079 -0.0064 824 ALA A CB 6188 N N . ARG A 790 ? 0.1689 0.1631 0.1529 -0.0132 0.0063 -0.0070 825 ARG A N 6189 C CA . ARG A 790 ? 0.1642 0.1620 0.1485 -0.0134 0.0060 -0.0082 825 ARG A CA 6190 C C . ARG A 790 ? 0.1746 0.1704 0.1587 -0.0143 0.0070 -0.0106 825 ARG A C 6191 O O . ARG A 790 ? 0.1835 0.1751 0.1672 -0.0137 0.0077 -0.0105 825 ARG A O 6192 C CB . ARG A 790 ? 0.1633 0.1631 0.1465 -0.0130 0.0056 -0.0075 825 ARG A CB 6193 C CG . ARG A 790 ? 0.1715 0.1714 0.1539 -0.0129 0.0050 -0.0050 825 ARG A CG 6194 C CD . ARG A 790 ? 0.1743 0.1770 0.1555 -0.0134 0.0050 -0.0043 825 ARG A CD 6195 N NE . ARG A 790 ? 0.1759 0.1792 0.1583 -0.0129 0.0058 -0.0056 825 ARG A NE 6196 C CZ . ARG A 790 ? 0.1676 0.1747 0.1502 -0.0127 0.0067 -0.0066 825 ARG A CZ 6197 N NH1 . ARG A 790 ? 0.1803 0.1910 0.1610 -0.0138 0.0069 -0.0066 825 ARG A NH1 6198 N NH2 . ARG A 790 ? 0.1787 0.1860 0.1633 -0.0111 0.0075 -0.0076 825 ARG A NH2 6199 N N . VAL A 791 ? 0.1810 0.1796 0.1652 -0.0158 0.0069 -0.0127 826 VAL A N 6200 C CA . VAL A 791 ? 0.1834 0.1786 0.1666 -0.0171 0.0083 -0.0157 826 VAL A CA 6201 C C . VAL A 791 ? 0.1934 0.1860 0.1757 -0.0150 0.0093 -0.0162 826 VAL A C 6202 O O . VAL A 791 ? 0.1770 0.1637 0.1590 -0.0141 0.0106 -0.0170 826 VAL A O 6203 C CB . VAL A 791 ? 0.1810 0.1806 0.1636 -0.0200 0.0080 -0.0185 826 VAL A CB 6204 C CG1 . VAL A 791 ? 0.1823 0.1767 0.1629 -0.0217 0.0100 -0.0223 826 VAL A CG1 6205 C CG2 . VAL A 791 ? 0.1897 0.1928 0.1745 -0.0219 0.0073 -0.0182 826 VAL A CG2 6206 N N . ARG A 792 ? 0.1821 0.1793 0.1642 -0.0139 0.0087 -0.0153 827 ARG A N 6207 C CA A ARG A 792 ? 0.1957 0.1929 0.1782 -0.0118 0.0098 -0.0158 827 ARG A CA 6208 C CA B ARG A 792 ? 0.1919 0.1891 0.1744 -0.0118 0.0098 -0.0158 827 ARG A CA 6209 C C . ARG A 792 ? 0.1828 0.1765 0.1670 -0.0093 0.0098 -0.0136 827 ARG A C 6210 O O . ARG A 792 ? 0.2044 0.1964 0.1898 -0.0068 0.0111 -0.0144 827 ARG A O 6211 C CB A ARG A 792 ? 0.2102 0.2138 0.1922 -0.0119 0.0093 -0.0146 827 ARG A CB 6212 C CB B ARG A 792 ? 0.2015 0.2052 0.1833 -0.0121 0.0093 -0.0147 827 ARG A CB 6213 C CG A ARG A 792 ? 0.2336 0.2415 0.2130 -0.0137 0.0097 -0.0168 827 ARG A CG 6214 C CG B ARG A 792 ? 0.2136 0.2201 0.1958 -0.0107 0.0110 -0.0163 827 ARG A CG 6215 C CD A ARG A 792 ? 0.2457 0.2525 0.2244 -0.0132 0.0122 -0.0211 827 ARG A CD 6216 C CD B ARG A 792 ? 0.2429 0.2495 0.2229 -0.0117 0.0128 -0.0207 827 ARG A CD 6217 N NE A ARG A 792 ? 0.2629 0.2722 0.2434 -0.0108 0.0139 -0.0211 827 ARG A NE 6218 N NE B ARG A 792 ? 0.2588 0.2681 0.2396 -0.0098 0.0153 -0.0229 827 ARG A NE 6219 C CZ A ARG A 792 ? 0.2841 0.2907 0.2662 -0.0080 0.0163 -0.0238 827 ARG A CZ 6220 C CZ B ARG A 792 ? 0.2952 0.3002 0.2781 -0.0067 0.0175 -0.0251 827 ARG A CZ 6221 N NH1 A ARG A 792 ? 0.2996 0.2988 0.2810 -0.0077 0.0176 -0.0267 827 ARG A NH1 6222 N NH1 B ARG A 792 ? 0.2938 0.2906 0.2772 -0.0058 0.0173 -0.0251 827 ARG A NH1 6223 N NH2 A ARG A 792 ? 0.2658 0.2770 0.2508 -0.0055 0.0177 -0.0235 827 ARG A NH2 6224 N NH2 B ARG A 792 ? 0.3127 0.3213 0.2971 -0.0043 0.0200 -0.0272 827 ARG A NH2 6225 N N . ASP A 793 ? 0.1861 0.1791 0.1704 -0.0099 0.0085 -0.0109 828 ASP A N 6226 C CA . ASP A 793 ? 0.1906 0.1814 0.1757 -0.0084 0.0080 -0.0086 828 ASP A CA 6227 C C . ASP A 793 ? 0.1910 0.1750 0.1754 -0.0074 0.0089 -0.0090 828 ASP A C 6228 O O . ASP A 793 ? 0.2004 0.1825 0.1858 -0.0047 0.0090 -0.0076 828 ASP A O 6229 C CB . ASP A 793 ? 0.1847 0.1754 0.1687 -0.0100 0.0068 -0.0066 828 ASP A CB 6230 C CG . ASP A 793 ? 0.2017 0.1967 0.1856 -0.0109 0.0061 -0.0057 828 ASP A CG 6231 O OD1 . ASP A 793 ? 0.1920 0.1910 0.1770 -0.0103 0.0061 -0.0055 828 ASP A OD1 6232 O OD2 . ASP A 793 ? 0.1939 0.1880 0.1768 -0.0122 0.0058 -0.0052 828 ASP A OD2 6233 N N . ILE A 794 ? 0.1861 0.1667 0.1691 -0.0098 0.0097 -0.0105 829 ILE A N 6234 C CA . ILE A 794 ? 0.1914 0.1642 0.1731 -0.0102 0.0110 -0.0110 829 ILE A CA 6235 C C . ILE A 794 ? 0.2003 0.1693 0.1822 -0.0081 0.0127 -0.0135 829 ILE A C 6236 O O . ILE A 794 ? 0.1988 0.1606 0.1802 -0.0059 0.0136 -0.0126 829 ILE A O 6237 C CB . ILE A 794 ? 0.2022 0.1739 0.1827 -0.0143 0.0116 -0.0125 829 ILE A CB 6238 C CG1 . ILE A 794 ? 0.2039 0.1784 0.1843 -0.0154 0.0107 -0.0102 829 ILE A CG1 6239 C CG2 . ILE A 794 ? 0.1966 0.1592 0.1749 -0.0158 0.0135 -0.0134 829 ILE A CG2 6240 C CD1 . ILE A 794 ? 0.2179 0.1956 0.1991 -0.0187 0.0112 -0.0118 829 ILE A CD1 6241 N N . GLU A 795 ? 0.2027 0.1762 0.1850 -0.0087 0.0133 -0.0167 830 GLU A N 6242 C CA . GLU A 795 ? 0.2077 0.1781 0.1900 -0.0068 0.0155 -0.0199 830 GLU A CA 6243 C C . GLU A 795 ? 0.2044 0.1748 0.1895 -0.0013 0.0158 -0.0179 830 GLU A C 6244 O O . GLU A 795 ? 0.2202 0.1832 0.2056 0.0016 0.0177 -0.0188 830 GLU A O 6245 C CB . GLU A 795 ? 0.2075 0.1846 0.1888 -0.0087 0.0160 -0.0234 830 GLU A CB 6246 C CG . GLU A 795 ? 0.2247 0.2024 0.2036 -0.0137 0.0157 -0.0258 830 GLU A CG 6247 C CD . GLU A 795 ? 0.2501 0.2342 0.2270 -0.0159 0.0160 -0.0294 830 GLU A CD 6248 O OE1 . GLU A 795 ? 0.2706 0.2605 0.2480 -0.0140 0.0160 -0.0287 830 GLU A OE1 6249 O OE2 . GLU A 795 ? 0.2491 0.2327 0.2234 -0.0200 0.0164 -0.0328 830 GLU A OE2 6250 N N . HIS A 796 ? 0.1949 0.1735 0.1823 -0.0001 0.0140 -0.0151 831 HIS A N 6251 C CA . HIS A 796 ? 0.2160 0.1975 0.2071 0.0045 0.0137 -0.0129 831 HIS A CA 6252 C C . HIS A 796 ? 0.2010 0.1754 0.1920 0.0070 0.0129 -0.0094 831 HIS A C 6253 O O . HIS A 796 ? 0.2121 0.1844 0.2057 0.0121 0.0135 -0.0083 831 HIS A O 6254 C CB . HIS A 796 ? 0.2415 0.2327 0.2344 0.0038 0.0115 -0.0102 831 HIS A CB 6255 C CG . HIS A 796 ? 0.2618 0.2606 0.2547 0.0015 0.0120 -0.0121 831 HIS A CG 6256 N ND1 . HIS A 796 ? 0.3055 0.3070 0.2991 0.0025 0.0145 -0.0156 831 HIS A ND1 6257 C CD2 . HIS A 796 ? 0.2734 0.2774 0.2653 -0.0016 0.0105 -0.0106 831 HIS A CD2 6258 C CE1 . HIS A 796 ? 0.3236 0.3320 0.3162 -0.0002 0.0143 -0.0158 831 HIS A CE1 6259 N NE2 . HIS A 796 ? 0.2923 0.3017 0.2840 -0.0027 0.0118 -0.0126 831 HIS A NE2 6260 N N . LEU A 797 ? 0.2010 0.1723 0.1889 0.0037 0.0114 -0.0073 832 LEU A N 6261 C CA . LEU A 797 ? 0.2077 0.1731 0.1942 0.0051 0.0103 -0.0033 832 LEU A CA 6262 C C . LEU A 797 ? 0.2184 0.1714 0.2024 0.0058 0.0124 -0.0039 832 LEU A C 6263 O O . LEU A 797 ? 0.2298 0.1769 0.2125 0.0079 0.0117 0.0000 832 LEU A O 6264 C CB . LEU A 797 ? 0.2039 0.1707 0.1874 0.0009 0.0087 -0.0013 832 LEU A CB 6265 C CG . LEU A 797 ? 0.2037 0.1800 0.1886 0.0007 0.0063 0.0006 832 LEU A CG 6266 C CD1 . LEU A 797 ? 0.2148 0.1920 0.1967 -0.0037 0.0057 0.0005 832 LEU A CD1 6267 C CD2 . LEU A 797 ? 0.2198 0.1975 0.2054 0.0040 0.0042 0.0049 832 LEU A CD2 6268 N N . THR A 798 ? 0.2134 0.1622 0.1962 0.0035 0.0149 -0.0086 833 THR A N 6269 C CA . THR A 798 ? 0.2365 0.1722 0.2161 0.0025 0.0174 -0.0100 833 THR A CA 6270 C C . THR A 798 ? 0.2470 0.1771 0.2275 0.0054 0.0205 -0.0143 833 THR A C 6271 O O . THR A 798 ? 0.2626 0.1797 0.2406 0.0059 0.0227 -0.0150 833 THR A O 6272 C CB . THR A 798 ? 0.2394 0.1734 0.2157 -0.0045 0.0181 -0.0127 833 THR A CB 6273 O OG1 . THR A 798 ? 0.2412 0.1830 0.2186 -0.0070 0.0184 -0.0172 833 THR A OG1 6274 C CG2 . THR A 798 ? 0.2481 0.1857 0.2232 -0.0075 0.0161 -0.0090 833 THR A CG2 6275 N N . GLY A 799 ? 0.2371 0.1762 0.2206 0.0071 0.0209 -0.0175 834 GLY A N 6276 C CA . GLY A 799 ? 0.2524 0.1869 0.2358 0.0088 0.0245 -0.0230 834 GLY A CA 6277 C C . GLY A 799 ? 0.2504 0.1791 0.2290 0.0022 0.0265 -0.0284 834 GLY A C 6278 O O . GLY A 799 ? 0.2631 0.1832 0.2398 0.0026 0.0300 -0.0332 834 GLY A O 6279 N N . LEU A 800 ? 0.2404 0.1741 0.2172 -0.0037 0.0245 -0.0279 835 LEU A N 6280 C CA . LEU A 800 ? 0.2502 0.1824 0.2233 -0.0105 0.0255 -0.0327 835 LEU A CA 6281 C C . LEU A 800 ? 0.2631 0.2085 0.2366 -0.0129 0.0243 -0.0353 835 LEU A C 6282 O O . LEU A 800 ? 0.2576 0.2129 0.2338 -0.0107 0.0221 -0.0321 835 LEU A O 6283 C CB . LEU A 800 ? 0.2513 0.1813 0.2227 -0.0156 0.0242 -0.0303 835 LEU A CB 6284 C CG . LEU A 800 ? 0.2644 0.1810 0.2340 -0.0145 0.0254 -0.0270 835 LEU A CG 6285 C CD1 . LEU A 800 ? 0.2668 0.1851 0.2352 -0.0197 0.0240 -0.0243 835 LEU A CD1 6286 C CD2 . LEU A 800 ? 0.2962 0.1981 0.2622 -0.0156 0.0292 -0.0312 835 LEU A CD2 6287 N N . ASP A 801 ? 0.2697 0.2149 0.2398 -0.0179 0.0257 -0.0408 836 ASP A N 6288 C CA . ASP A 801 ? 0.2652 0.2225 0.2344 -0.0207 0.0243 -0.0430 836 ASP A CA 6289 C C . ASP A 801 ? 0.2578 0.2180 0.2248 -0.0279 0.0230 -0.0449 836 ASP A C 6290 O O . ASP A 801 ? 0.2853 0.2381 0.2489 -0.0322 0.0251 -0.0494 836 ASP A O 6291 C CB . ASP A 801 ? 0.2704 0.2271 0.2373 -0.0197 0.0274 -0.0485 836 ASP A CB 6292 C CG . ASP A 801 ? 0.2926 0.2626 0.2580 -0.0219 0.0259 -0.0497 836 ASP A CG 6293 O OD1 . ASP A 801 ? 0.2954 0.2735 0.2637 -0.0189 0.0240 -0.0454 836 ASP A OD1 6294 O OD2 . ASP A 801 ? 0.3324 0.3047 0.2933 -0.0269 0.0266 -0.0548 836 ASP A OD2 6295 N N . PHE A 802 ? 0.2349 0.2059 0.2040 -0.0291 0.0196 -0.0414 837 PHE A N 6296 C CA . PHE A 802 ? 0.2388 0.2151 0.2078 -0.0347 0.0178 -0.0418 837 PHE A CA 6297 C C . PHE A 802 ? 0.2421 0.2295 0.2091 -0.0382 0.0161 -0.0446 837 PHE A C 6298 O O . PHE A 802 ? 0.2499 0.2411 0.2150 -0.0363 0.0163 -0.0456 837 PHE A O 6299 C CB . PHE A 802 ? 0.2280 0.2088 0.2011 -0.0330 0.0155 -0.0362 837 PHE A CB 6300 C CG . PHE A 802 ? 0.2272 0.1984 0.2012 -0.0304 0.0167 -0.0332 837 PHE A CG 6301 C CD1 . PHE A 802 ? 0.2403 0.2041 0.2131 -0.0342 0.0183 -0.0339 837 PHE A CD1 6302 C CD2 . PHE A 802 ? 0.2286 0.1983 0.2041 -0.0248 0.0163 -0.0294 837 PHE A CD2 6303 C CE1 . PHE A 802 ? 0.2396 0.1944 0.2122 -0.0320 0.0193 -0.0305 837 PHE A CE1 6304 C CE2 . PHE A 802 ? 0.2308 0.1925 0.2066 -0.0226 0.0170 -0.0264 837 PHE A CE2 6305 C CZ . PHE A 802 ? 0.2356 0.1895 0.2096 -0.0260 0.0185 -0.0267 837 PHE A CZ 6306 N N . TYR A 803 ? 0.2420 0.2357 0.2093 -0.0436 0.0145 -0.0457 838 TYR A N 6307 C CA . TYR A 803 ? 0.2420 0.2486 0.2078 -0.0471 0.0118 -0.0472 838 TYR A CA 6308 C C . TYR A 803 ? 0.2685 0.2739 0.2283 -0.0498 0.0136 -0.0531 838 TYR A C 6309 O O . TYR A 803 ? 0.2538 0.2678 0.2113 -0.0494 0.0120 -0.0529 838 TYR A O 6310 C CB . TYR A 803 ? 0.2283 0.2451 0.1970 -0.0428 0.0085 -0.0415 838 TYR A CB 6311 C CG . TYR A 803 ? 0.2336 0.2522 0.2080 -0.0402 0.0070 -0.0364 838 TYR A CG 6312 C CD1 . TYR A 803 ? 0.2549 0.2801 0.2325 -0.0437 0.0056 -0.0364 838 TYR A CD1 6313 C CD2 . TYR A 803 ? 0.2447 0.2590 0.2211 -0.0347 0.0073 -0.0321 838 TYR A CD2 6314 C CE1 . TYR A 803 ? 0.2402 0.2671 0.2229 -0.0412 0.0050 -0.0324 838 TYR A CE1 6315 C CE2 . TYR A 803 ? 0.2435 0.2589 0.2242 -0.0327 0.0064 -0.0283 838 TYR A CE2 6316 C CZ . TYR A 803 ? 0.2391 0.2606 0.2229 -0.0357 0.0055 -0.0285 838 TYR A CZ 6317 O OH . TYR A 803 ? 0.2395 0.2622 0.2275 -0.0335 0.0053 -0.0252 838 TYR A OH 6318 N N . ARG A 804 ? 0.2845 0.2783 0.2411 -0.0527 0.0173 -0.0585 839 ARG A N 6319 C CA . ARG A 804 ? 0.3097 0.3001 0.2601 -0.0550 0.0201 -0.0652 839 ARG A CA 6320 C C . ARG A 804 ? 0.3353 0.3340 0.2812 -0.0635 0.0187 -0.0704 839 ARG A C 6321 O O . ARG A 804 ? 0.3403 0.3404 0.2803 -0.0658 0.0201 -0.0755 839 ARG A O 6322 C CB . ARG A 804 ? 0.3353 0.3079 0.2843 -0.0534 0.0250 -0.0686 839 ARG A CB 6323 C CG . ARG A 804 ? 0.3289 0.2967 0.2818 -0.0445 0.0259 -0.0638 839 ARG A CG 6324 C CD . ARG A 804 ? 0.3638 0.3147 0.3159 -0.0416 0.0304 -0.0663 839 ARG A CD 6325 N NE . ARG A 804 ? 0.3734 0.3189 0.3206 -0.0422 0.0344 -0.0736 839 ARG A NE 6326 C CZ . ARG A 804 ? 0.3653 0.3119 0.3130 -0.0366 0.0366 -0.0746 839 ARG A CZ 6327 N NH1 . ARG A 804 ? 0.3646 0.3180 0.3174 -0.0302 0.0349 -0.0686 839 ARG A NH1 6328 N NH2 . ARG A 804 ? 0.3955 0.3361 0.3383 -0.0376 0.0411 -0.0824 839 ARG A NH2 6329 N N . LYS A 805 ? 0.3211 0.3266 0.2698 -0.0682 0.0159 -0.0691 840 LYS A N 6330 C CA . LYS A 805 ? 0.3723 0.3879 0.3174 -0.0770 0.0140 -0.0739 840 LYS A CA 6331 C C . LYS A 805 ? 0.3428 0.3765 0.2933 -0.0775 0.0085 -0.0685 840 LYS A C 6332 O O . LYS A 805 ? 0.3394 0.3761 0.2947 -0.0801 0.0075 -0.0671 840 LYS A O 6333 C CB . LYS A 805 ? 0.4091 0.4140 0.3519 -0.0844 0.0172 -0.0799 840 LYS A CB 6334 C CG . LYS A 805 ? 0.4874 0.4734 0.4241 -0.0844 0.0230 -0.0862 840 LYS A CG 6335 C CD . LYS A 805 ? 0.5700 0.5591 0.4986 -0.0891 0.0241 -0.0937 840 LYS A CD 6336 C CE . LYS A 805 ? 0.6293 0.6007 0.5532 -0.0856 0.0302 -0.0990 840 LYS A CE 6337 N NZ . LYS A 805 ? 0.6616 0.6128 0.5848 -0.0872 0.0347 -0.1019 840 LYS A NZ 6338 N N . THR A 806 ? 0.3426 0.3881 0.2924 -0.0745 0.0051 -0.0651 841 THR A N 6339 C CA . THR A 806 ? 0.3316 0.3941 0.2865 -0.0736 -0.0002 -0.0593 841 THR A CA 6340 C C . THR A 806 ? 0.3427 0.4193 0.2921 -0.0775 -0.0037 -0.0607 841 THR A C 6341 O O . THR A 806 ? 0.3594 0.4322 0.3008 -0.0810 -0.0015 -0.0664 841 THR A O 6342 C CB . THR A 806 ? 0.3139 0.3761 0.2740 -0.0645 -0.0014 -0.0513 841 THR A CB 6343 O OG1 . THR A 806 ? 0.2921 0.3551 0.2474 -0.0613 -0.0017 -0.0498 841 THR A OG1 6344 C CG2 . THR A 806 ? 0.3101 0.3571 0.2737 -0.0603 0.0022 -0.0501 841 THR A CG2 6345 N N . SER A 807 ? 0.3289 0.4217 0.2824 -0.0765 -0.0090 -0.0552 842 SER A N 6346 C CA . SER A 807 ? 0.3469 0.4549 0.2955 -0.0791 -0.0135 -0.0544 842 SER A CA 6347 C C . SER A 807 ? 0.3222 0.4311 0.2693 -0.0717 -0.0149 -0.0475 842 SER A C 6348 O O . SER A 807 ? 0.3453 0.4669 0.2889 -0.0724 -0.0192 -0.0444 842 SER A O 6349 C CB . SER A 807 ? 0.3545 0.4811 0.3093 -0.0816 -0.0189 -0.0516 842 SER A CB 6350 O OG . SER A 807 ? 0.3668 0.4958 0.3309 -0.0736 -0.0206 -0.0437 842 SER A OG 6351 N N . ARG A 808 ? 0.2850 0.3805 0.2343 -0.0653 -0.0116 -0.0450 843 ARG A N 6352 C CA . ARG A 808 ? 0.2919 0.3868 0.2406 -0.0587 -0.0125 -0.0383 843 ARG A CA 6353 C C . ARG A 808 ? 0.2773 0.3642 0.2182 -0.0593 -0.0085 -0.0421 843 ARG A C 6354 O O . ARG A 808 ? 0.2681 0.3456 0.2065 -0.0621 -0.0041 -0.0492 843 ARG A O 6355 C CB . ARG A 808 ? 0.3056 0.3924 0.2624 -0.0517 -0.0114 -0.0332 843 ARG A CB 6356 C CG . ARG A 808 ? 0.3224 0.4151 0.2877 -0.0509 -0.0137 -0.0308 843 ARG A CG 6357 C CD . ARG A 808 ? 0.3559 0.4662 0.3229 -0.0522 -0.0193 -0.0276 843 ARG A CD 6358 N NE . ARG A 808 ? 0.3865 0.5019 0.3522 -0.0470 -0.0226 -0.0201 843 ARG A NE 6359 C CZ . ARG A 808 ? 0.4129 0.5431 0.3775 -0.0475 -0.0278 -0.0163 843 ARG A CZ 6360 N NH1 . ARG A 808 ? 0.4861 0.6299 0.4511 -0.0534 -0.0307 -0.0196 843 ARG A NH1 6361 N NH2 . ARG A 808 ? 0.4439 0.5756 0.4067 -0.0424 -0.0303 -0.0089 843 ARG A NH2 6362 N N . SER A 809 ? 0.2827 0.3734 0.2197 -0.0567 -0.0098 -0.0374 844 SER A N 6363 C CA . SER A 809 ? 0.2922 0.3765 0.2229 -0.0565 -0.0056 -0.0401 844 SER A CA 6364 C C . SER A 809 ? 0.2771 0.3478 0.2130 -0.0513 -0.0014 -0.0401 844 SER A C 6365 O O . SER A 809 ? 0.2718 0.3390 0.2151 -0.0471 -0.0024 -0.0357 844 SER A O 6366 C CB . SER A 809 ? 0.3235 0.4151 0.2489 -0.0552 -0.0080 -0.0340 844 SER A CB 6367 O OG . SER A 809 ? 0.3341 0.4212 0.2650 -0.0489 -0.0086 -0.0266 844 SER A OG 6368 N N . TYR A 810 ? 0.2582 0.3220 0.1906 -0.0514 0.0034 -0.0451 845 TYR A N 6369 C CA . TYR A 810 ? 0.2631 0.3157 0.2009 -0.0463 0.0071 -0.0449 845 TYR A CA 6370 C C . TYR A 810 ? 0.2632 0.3165 0.2044 -0.0413 0.0056 -0.0370 845 TYR A C 6371 O O . TYR A 810 ? 0.2531 0.3000 0.2006 -0.0374 0.0061 -0.0344 845 TYR A O 6372 C CB . TYR A 810 ? 0.2754 0.3213 0.2099 -0.0465 0.0127 -0.0519 845 TYR A CB 6373 C CG . TYR A 810 ? 0.2723 0.3077 0.2129 -0.0410 0.0161 -0.0517 845 TYR A CG 6374 C CD1 . TYR A 810 ? 0.2912 0.3185 0.2373 -0.0394 0.0159 -0.0511 845 TYR A CD1 6375 C CD2 . TYR A 810 ? 0.2745 0.3087 0.2151 -0.0377 0.0196 -0.0521 845 TYR A CD2 6376 C CE1 . TYR A 810 ? 0.2791 0.2975 0.2302 -0.0343 0.0184 -0.0503 845 TYR A CE1 6377 C CE2 . TYR A 810 ? 0.2848 0.3111 0.2315 -0.0324 0.0221 -0.0516 845 TYR A CE2 6378 C CZ . TYR A 810 ? 0.2881 0.3063 0.2397 -0.0307 0.0213 -0.0505 845 TYR A CZ 6379 O OH . TYR A 810 ? 0.3200 0.3311 0.2771 -0.0255 0.0233 -0.0494 845 TYR A OH 6380 N N . SER A 811 ? 0.2697 0.3307 0.2064 -0.0420 0.0037 -0.0330 846 SER A N 6381 C CA A SER A 811 ? 0.2668 0.3272 0.2060 -0.0381 0.0024 -0.0254 846 SER A CA 6382 C CA B SER A 811 ? 0.2684 0.3287 0.2075 -0.0381 0.0024 -0.0255 846 SER A CA 6383 C C . SER A 811 ? 0.2623 0.3222 0.2075 -0.0354 -0.0013 -0.0200 846 SER A C 6384 O O . SER A 811 ? 0.2263 0.2806 0.1761 -0.0317 -0.0009 -0.0164 846 SER A O 6385 C CB A SER A 811 ? 0.2794 0.3471 0.2114 -0.0400 0.0012 -0.0217 846 SER A CB 6386 C CB B SER A 811 ? 0.2831 0.3507 0.2151 -0.0400 0.0014 -0.0219 846 SER A CB 6387 O OG A SER A 811 ? 0.2805 0.3569 0.2086 -0.0428 -0.0030 -0.0197 846 SER A OG 6388 O OG B SER A 811 ? 0.2875 0.3547 0.2154 -0.0414 0.0060 -0.0262 846 SER A OG 6389 N N . GLU A 812 ? 0.2562 0.3227 0.2017 -0.0374 -0.0047 -0.0200 847 GLU A N 6390 C CA . GLU A 812 ? 0.2604 0.3277 0.2125 -0.0346 -0.0078 -0.0158 847 GLU A CA 6391 C C . GLU A 812 ? 0.2374 0.2958 0.1959 -0.0328 -0.0052 -0.0186 847 GLU A C 6392 O O . GLU A 812 ? 0.2256 0.2801 0.1891 -0.0291 -0.0055 -0.0148 847 GLU A O 6393 C CB . GLU A 812 ? 0.3106 0.3889 0.2627 -0.0375 -0.0117 -0.0162 847 GLU A CB 6394 C CG . GLU A 812 ? 0.3466 0.4347 0.2933 -0.0380 -0.0157 -0.0110 847 GLU A CG 6395 C CD . GLU A 812 ? 0.4214 0.5230 0.3666 -0.0421 -0.0198 -0.0122 847 GLU A CD 6396 O OE1 . GLU A 812 ? 0.3953 0.4990 0.3415 -0.0466 -0.0190 -0.0189 847 GLU A OE1 6397 O OE2 . GLU A 812 ? 0.4607 0.5711 0.4034 -0.0410 -0.0241 -0.0061 847 GLU A OE2 6398 N N . ILE A 813 ? 0.2245 0.2791 0.1819 -0.0358 -0.0023 -0.0252 848 ILE A N 6399 C CA . ILE A 813 ? 0.2100 0.2549 0.1720 -0.0343 0.0003 -0.0275 848 ILE A CA 6400 C C . ILE A 813 ? 0.1942 0.2317 0.1579 -0.0300 0.0025 -0.0250 848 ILE A C 6401 O O . ILE A 813 ? 0.1941 0.2263 0.1624 -0.0274 0.0029 -0.0231 848 ILE A O 6402 C CB . ILE A 813 ? 0.2264 0.2669 0.1857 -0.0383 0.0033 -0.0349 848 ILE A CB 6403 C CG1 . ILE A 813 ? 0.2276 0.2751 0.1864 -0.0435 0.0010 -0.0376 848 ILE A CG1 6404 C CG2 . ILE A 813 ? 0.2360 0.2645 0.1985 -0.0361 0.0066 -0.0366 848 ILE A CG2 6405 C CD1 . ILE A 813 ? 0.2336 0.2848 0.1989 -0.0428 -0.0013 -0.0342 848 ILE A CD1 6406 N N . LEU A 814 ? 0.1932 0.2315 0.1533 -0.0296 0.0039 -0.0250 849 LEU A N 6407 C CA . LEU A 814 ? 0.2039 0.2372 0.1662 -0.0260 0.0056 -0.0224 849 LEU A CA 6408 C C . LEU A 814 ? 0.1946 0.2280 0.1597 -0.0236 0.0031 -0.0160 849 LEU A C 6409 O O . LEU A 814 ? 0.2164 0.2443 0.1851 -0.0212 0.0039 -0.0145 849 LEU A O 6410 C CB . LEU A 814 ? 0.2092 0.2451 0.1676 -0.0266 0.0079 -0.0237 849 LEU A CB 6411 C CG . LEU A 814 ? 0.2157 0.2490 0.1724 -0.0275 0.0117 -0.0307 849 LEU A CG 6412 C CD1 . LEU A 814 ? 0.2265 0.2638 0.1798 -0.0278 0.0144 -0.0319 849 LEU A CD1 6413 C CD2 . LEU A 814 ? 0.2177 0.2422 0.1793 -0.0245 0.0138 -0.0325 849 LEU A CD2 6414 N N . THR A 815 ? 0.2156 0.2548 0.1787 -0.0243 0.0002 -0.0124 850 THR A N 6415 C CA . THR A 815 ? 0.2027 0.2409 0.1683 -0.0216 -0.0019 -0.0066 850 THR A CA 6416 C C . THR A 815 ? 0.2023 0.2374 0.1737 -0.0199 -0.0022 -0.0072 850 THR A C 6417 O O . THR A 815 ? 0.2116 0.2411 0.1858 -0.0176 -0.0015 -0.0052 850 THR A O 6418 C CB . THR A 815 ? 0.2379 0.2832 0.2004 -0.0220 -0.0053 -0.0025 850 THR A CB 6419 O OG1 . THR A 815 ? 0.2276 0.2761 0.1836 -0.0243 -0.0048 -0.0020 850 THR A OG1 6420 C CG2 . THR A 815 ? 0.2648 0.3073 0.2299 -0.0184 -0.0071 0.0034 850 THR A CG2 6421 N N . LEU A 816 ? 0.1800 0.2188 0.1527 -0.0218 -0.0028 -0.0104 851 LEU A N 6422 C CA . LEU A 816 ? 0.1864 0.2230 0.1643 -0.0212 -0.0025 -0.0114 851 LEU A CA 6423 C C . LEU A 816 ? 0.1877 0.2151 0.1668 -0.0201 0.0003 -0.0128 851 LEU A C 6424 O O . LEU A 816 ? 0.1960 0.2200 0.1784 -0.0182 0.0006 -0.0111 851 LEU A O 6425 C CB . LEU A 816 ? 0.1946 0.2362 0.1728 -0.0250 -0.0029 -0.0155 851 LEU A CB 6426 C CG . LEU A 816 ? 0.1970 0.2386 0.1802 -0.0256 -0.0025 -0.0167 851 LEU A CG 6427 C CD1 . LEU A 816 ? 0.1998 0.2482 0.1879 -0.0229 -0.0049 -0.0127 851 LEU A CD1 6428 C CD2 . LEU A 816 ? 0.2129 0.2575 0.1949 -0.0309 -0.0021 -0.0218 851 LEU A CD2 6429 N N . LYS A 817 ? 0.1914 0.2152 0.1681 -0.0211 0.0024 -0.0159 852 LYS A N 6430 C CA . LYS A 817 ? 0.1939 0.2099 0.1719 -0.0197 0.0047 -0.0168 852 LYS A CA 6431 C C . LYS A 817 ? 0.1848 0.1984 0.1638 -0.0171 0.0047 -0.0132 852 LYS A C 6432 O O . LYS A 817 ? 0.1913 0.1999 0.1720 -0.0158 0.0056 -0.0128 852 LYS A O 6433 C CB . LYS A 817 ? 0.2083 0.2214 0.1841 -0.0205 0.0071 -0.0210 852 LYS A CB 6434 C CG . LYS A 817 ? 0.2249 0.2373 0.1993 -0.0238 0.0079 -0.0256 852 LYS A CG 6435 C CD . LYS A 817 ? 0.2533 0.2606 0.2254 -0.0237 0.0110 -0.0299 852 LYS A CD 6436 C CE . LYS A 817 ? 0.2926 0.2950 0.2631 -0.0271 0.0125 -0.0347 852 LYS A CE 6437 N NZ . LYS A 817 ? 0.3203 0.3161 0.2885 -0.0261 0.0161 -0.0391 852 LYS A NZ 6438 N N . THR A 818 ? 0.1893 0.2062 0.1666 -0.0168 0.0036 -0.0105 853 THR A N 6439 C CA . THR A 818 ? 0.1952 0.2094 0.1730 -0.0153 0.0036 -0.0072 853 THR A CA 6440 C C . THR A 818 ? 0.1900 0.2024 0.1693 -0.0140 0.0023 -0.0041 853 THR A C 6441 O O . THR A 818 ? 0.1839 0.1924 0.1630 -0.0134 0.0026 -0.0020 853 THR A O 6442 C CB . THR A 818 ? 0.1990 0.2162 0.1736 -0.0162 0.0038 -0.0056 853 THR A CB 6443 O OG1 . THR A 818 ? 0.2124 0.2335 0.1844 -0.0169 0.0020 -0.0035 853 THR A OG1 6444 C CG2 . THR A 818 ? 0.2014 0.2207 0.1751 -0.0169 0.0059 -0.0090 853 THR A CG2 6445 N N . TYR A 819 ? 0.1807 0.1961 0.1616 -0.0137 0.0011 -0.0041 854 TYR A N 6446 C CA . TYR A 819 ? 0.1839 0.1982 0.1673 -0.0116 0.0003 -0.0017 854 TYR A CA 6447 C C . TYR A 819 ? 0.1674 0.1760 0.1525 -0.0110 0.0020 -0.0026 854 TYR A C 6448 O O . TYR A 819 ? 0.1755 0.1825 0.1611 -0.0122 0.0031 -0.0051 854 TYR A O 6449 C CB . TYR A 819 ? 0.1938 0.2150 0.1800 -0.0115 -0.0011 -0.0022 854 TYR A CB 6450 C CG . TYR A 819 ? 0.1985 0.2200 0.1884 -0.0084 -0.0015 0.0000 854 TYR A CG 6451 C CD1 . TYR A 819 ? 0.2334 0.2546 0.2230 -0.0055 -0.0029 0.0041 854 TYR A CD1 6452 C CD2 . TYR A 819 ? 0.2046 0.2259 0.1983 -0.0083 -0.0001 -0.0020 854 TYR A CD2 6453 C CE1 . TYR A 819 ? 0.2358 0.2563 0.2293 -0.0017 -0.0028 0.0059 854 TYR A CE1 6454 C CE2 . TYR A 819 ? 0.2009 0.2231 0.1986 -0.0051 0.0001 -0.0006 854 TYR A CE2 6455 C CZ . TYR A 819 ? 0.2472 0.2687 0.2451 -0.0014 -0.0011 0.0032 854 TYR A CZ 6456 O OH . TYR A 819 ? 0.2670 0.2885 0.2692 0.0026 -0.0003 0.0044 854 TYR A OH 6457 N N . LEU A 820 ? 0.1630 0.1674 0.1483 -0.0094 0.0023 -0.0004 855 LEU A N 6458 C CA . LEU A 820 ? 0.1675 0.1673 0.1539 -0.0091 0.0039 -0.0015 855 LEU A CA 6459 C C . LEU A 820 ? 0.1744 0.1746 0.1637 -0.0065 0.0041 -0.0006 855 LEU A C 6460 O O . LEU A 820 ? 0.2012 0.1998 0.1901 -0.0044 0.0035 0.0018 855 LEU A O 6461 C CB . LEU A 820 ? 0.1683 0.1624 0.1518 -0.0100 0.0046 -0.0007 855 LEU A CB 6462 C CG . LEU A 820 ? 0.1761 0.1657 0.1591 -0.0105 0.0061 -0.0020 855 LEU A CG 6463 C CD1 . LEU A 820 ? 0.1740 0.1649 0.1571 -0.0119 0.0063 -0.0037 855 LEU A CD1 6464 C CD2 . LEU A 820 ? 0.1893 0.1741 0.1692 -0.0120 0.0064 -0.0011 855 LEU A CD2 6465 N N . HIS A 821 ? 0.1939 0.1960 0.1860 -0.0065 0.0052 -0.0026 856 HIS A N 6466 C CA . HIS A 821 ? 0.2218 0.2246 0.2174 -0.0036 0.0063 -0.0024 856 HIS A CA 6467 C C . HIS A 821 ? 0.2258 0.2203 0.2188 -0.0034 0.0085 -0.0029 856 HIS A C 6468 O O . HIS A 821 ? 0.2323 0.2246 0.2236 -0.0057 0.0099 -0.0049 856 HIS A O 6469 C CB . HIS A 821 ? 0.2356 0.2448 0.2352 -0.0045 0.0073 -0.0047 856 HIS A CB 6470 C CG . HIS A 821 ? 0.2836 0.2977 0.2887 -0.0009 0.0079 -0.0043 856 HIS A CG 6471 N ND1 . HIS A 821 ? 0.3921 0.4166 0.4023 0.0001 0.0062 -0.0036 856 HIS A ND1 6472 C CD2 . HIS A 821 ? 0.3811 0.3916 0.3877 0.0021 0.0102 -0.0045 856 HIS A CD2 6473 C CE1 . HIS A 821 ? 0.3791 0.4072 0.3946 0.0043 0.0073 -0.0031 856 HIS A CE1 6474 N NE2 . HIS A 821 ? 0.3426 0.3616 0.3559 0.0057 0.0100 -0.0039 856 HIS A NE2 6475 N N . THR A 822 ? 0.2254 0.2148 0.2176 -0.0008 0.0088 -0.0011 857 THR A N 6476 C CA . THR A 822 ? 0.2591 0.2393 0.2473 -0.0019 0.0108 -0.0021 857 THR A CA 6477 C C . THR A 822 ? 0.3012 0.2789 0.2911 0.0000 0.0139 -0.0045 857 THR A C 6478 O O . THR A 822 ? 0.3156 0.2871 0.3014 -0.0023 0.0159 -0.0067 857 THR A O 6479 C CB . THR A 822 ? 0.2826 0.2559 0.2678 -0.0013 0.0103 0.0004 857 THR A CB 6480 O OG1 . THR A 822 ? 0.3146 0.2877 0.3029 0.0034 0.0101 0.0027 857 THR A OG1 6481 C CG2 . THR A 822 ? 0.2989 0.2750 0.2819 -0.0038 0.0080 0.0023 857 THR A CG2 6482 N N . TYR A 823 ? 0.3005 0.2838 0.2961 0.0039 0.0143 -0.0043 858 TYR A N 6483 C CA . TYR A 823 ? 0.3212 0.3035 0.3196 0.0066 0.0179 -0.0068 858 TYR A CA 6484 C C . TYR A 823 ? 0.3818 0.3529 0.3775 0.0091 0.0200 -0.0069 858 TYR A C 6485 O O . TYR A 823 ? 0.4160 0.3826 0.4109 0.0097 0.0237 -0.0102 858 TYR A O 6486 C CB . TYR A 823 ? 0.2986 0.2821 0.2950 0.0026 0.0202 -0.0104 858 TYR A CB 6487 C CG . TYR A 823 ? 0.2988 0.2913 0.2975 0.0001 0.0187 -0.0104 858 TYR A CG 6488 C CD1 . TYR A 823 ? 0.3021 0.3042 0.3075 0.0018 0.0193 -0.0109 858 TYR A CD1 6489 C CD2 . TYR A 823 ? 0.2953 0.2867 0.2898 -0.0039 0.0167 -0.0098 858 TYR A CD2 6490 C CE1 . TYR A 823 ? 0.3198 0.3292 0.3267 -0.0014 0.0181 -0.0112 858 TYR A CE1 6491 C CE2 . TYR A 823 ? 0.2838 0.2814 0.2800 -0.0063 0.0157 -0.0099 858 TYR A CE2 6492 C CZ . TYR A 823 ? 0.3124 0.3184 0.3143 -0.0055 0.0164 -0.0108 858 TYR A CZ 6493 O OH . TYR A 823 ? 0.3275 0.3385 0.3303 -0.0089 0.0157 -0.0113 858 TYR A OH 6494 N N . GLU A 824 ? 0.3986 0.3649 0.3927 0.0105 0.0179 -0.0033 859 GLU A N 6495 C CA . GLU A 824 ? 0.4668 0.4207 0.4580 0.0127 0.0198 -0.0026 859 GLU A CA 6496 C C . GLU A 824 ? 0.5552 0.5099 0.5518 0.0201 0.0191 0.0010 859 GLU A C 6497 O O . GLU A 824 ? 0.6345 0.5991 0.6351 0.0218 0.0157 0.0043 859 GLU A O 6498 C CB . GLU A 824 ? 0.4400 0.3871 0.4245 0.0081 0.0181 -0.0008 859 GLU A CB 6499 C CG . GLU A 824 ? 0.4342 0.3797 0.4135 0.0016 0.0188 -0.0042 859 GLU A CG 6500 C CD . GLU A 824 ? 0.4585 0.3926 0.4330 0.0000 0.0224 -0.0077 859 GLU A CD 6501 O OE1 . GLU A 824 ? 0.4378 0.3607 0.4095 0.0009 0.0237 -0.0067 859 GLU A OE1 6502 O OE2 . GLU A 824 ? 0.5077 0.4433 0.4803 -0.0029 0.0241 -0.0116 859 GLU A OE2 6504 C C1 . NAG B . ? 0.2084 0.1898 0.1909 0.0012 0.0074 0.0000 901 NAG A C1 6505 C C2 . NAG B . ? 0.2198 0.1945 0.2001 0.0020 0.0080 0.0016 901 NAG A C2 6506 C C3 . NAG B . ? 0.2185 0.1932 0.2008 0.0068 0.0087 0.0041 901 NAG A C3 6507 C C4 . NAG B . ? 0.2416 0.2157 0.2253 0.0097 0.0110 0.0027 901 NAG A C4 6508 C C5 . NAG B . ? 0.2339 0.2146 0.2194 0.0078 0.0104 0.0004 901 NAG A C5 6509 C C6 . NAG B . ? 0.2590 0.2383 0.2450 0.0101 0.0133 -0.0013 901 NAG A C6 6510 C C7 . NAG B . ? 0.2371 0.2082 0.2138 -0.0033 0.0067 0.0027 901 NAG A C7 6511 C C8 . NAG B . ? 0.2398 0.2130 0.2163 -0.0049 0.0055 0.0046 901 NAG A C8 6512 N N2 . NAG B . ? 0.2104 0.1862 0.1898 -0.0002 0.0064 0.0031 901 NAG A N2 6513 O O3 . NAG B . ? 0.2281 0.1948 0.2077 0.0079 0.0098 0.0059 901 NAG A O3 6514 O O4 . NAG B . ? 0.2703 0.2486 0.2581 0.0144 0.0111 0.0057 901 NAG A O4 6515 O O5 . NAG B . ? 0.2133 0.1927 0.1959 0.0033 0.0095 -0.0015 901 NAG A O5 6516 O O6 . NAG B . ? 0.2852 0.2542 0.2661 0.0094 0.0157 -0.0034 901 NAG A O6 6517 O O7 . NAG B . ? 0.2678 0.2332 0.2420 -0.0050 0.0079 0.0008 901 NAG A O7 6518 C C1 . NAG C . ? 0.3589 0.3306 0.3464 0.0186 0.0144 0.0062 902 NAG A C1 6519 C C2 . NAG C . ? 0.4146 0.3946 0.4084 0.0238 0.0145 0.0091 902 NAG A C2 6520 C C3 . NAG C . ? 0.4528 0.4253 0.4468 0.0295 0.0185 0.0105 902 NAG A C3 6521 C C4 . NAG C . ? 0.4685 0.4288 0.4574 0.0302 0.0199 0.0119 902 NAG A C4 6522 C C5 . NAG C . ? 0.4579 0.4115 0.4405 0.0235 0.0192 0.0083 902 NAG A C5 6523 C C6 . NAG C . ? 0.4814 0.4242 0.4589 0.0225 0.0200 0.0096 902 NAG A C6 6524 C C7 . NAG C . ? 0.4967 0.4941 0.4964 0.0201 0.0118 0.0068 902 NAG A C7 6525 C C8 . NAG C . ? 0.5291 0.5317 0.5313 0.0195 0.0131 0.0044 902 NAG A C8 6526 N N2 . NAG C . ? 0.4762 0.4639 0.4733 0.0229 0.0145 0.0070 902 NAG A N2 6527 O O3 . NAG C . ? 0.5210 0.5031 0.5221 0.0348 0.0182 0.0142 902 NAG A O3 6528 O O4 . NAG C . ? 0.5802 0.5314 0.5680 0.0349 0.0249 0.0115 902 NAG A O4 6529 O O5 . NAG C . ? 0.3728 0.3355 0.3567 0.0192 0.0152 0.0079 902 NAG A O5 6530 O O6 . NAG C . ? 0.4996 0.4476 0.4796 0.0246 0.0175 0.0144 902 NAG A O6 6531 O O7 . NAG C . ? 0.5487 0.5499 0.5482 0.0179 0.0087 0.0082 902 NAG A O7 6532 C C1 . BMA D . ? 0.7648 0.7057 0.7503 0.0389 0.0274 0.0147 903 BMA A C1 6533 C C2 . BMA D . ? 0.8289 0.7540 0.8074 0.0379 0.0325 0.0107 903 BMA A C2 6534 C C3 . BMA D . ? 0.9518 0.8632 0.9267 0.0419 0.0362 0.0135 903 BMA A C3 6535 C C4 . BMA D . ? 0.9595 0.8760 0.9410 0.0507 0.0369 0.0199 903 BMA A C4 6536 C C5 . BMA D . ? 0.9154 0.8506 0.9048 0.0512 0.0312 0.0235 903 BMA A C5 6537 C C6 . BMA D . ? 0.9371 0.8798 0.9343 0.0601 0.0323 0.0292 903 BMA A C6 6538 O O2 . BMA D . ? 0.7453 0.6721 0.7260 0.0408 0.0358 0.0084 903 BMA A O2 6539 O O3 . BMA D . ? 1.0116 0.9081 0.9801 0.0418 0.0419 0.0096 903 BMA A O3 6540 O O4 . BMA D . ? 0.9103 0.8154 0.8879 0.0529 0.0385 0.0236 903 BMA A O4 6541 O O5 . BMA D . ? 0.8724 0.8177 0.8639 0.0467 0.0288 0.0195 903 BMA A O5 6542 O O6 . BMA D . ? 0.9646 0.9187 0.9658 0.0610 0.0271 0.0346 903 BMA A O6 6543 ZN ZN . ZN E . ? 0.2907 0.2079 0.1999 -0.0575 0.0636 -0.0042 904 ZN A ZN 6544 ZN ZN . ZN F . ? 0.2805 0.2831 0.2353 -0.0480 0.0441 0.0434 905 ZN A ZN 6545 C C18 . 5JK G . ? 0.2760 0.3587 0.2982 -0.0332 0.0099 -0.0061 906 5JK A C18 6546 C C13 . 5JK G . ? 0.2841 0.3548 0.3014 -0.0305 0.0132 -0.0072 906 5JK A C13 6547 C C12 . 5JK G . ? 0.2599 0.3228 0.2739 -0.0257 0.0121 -0.0068 906 5JK A C12 6548 C C11 . 5JK G . ? 0.2521 0.3203 0.2714 -0.0199 0.0111 -0.0049 906 5JK A C11 6549 C C9 . 5JK G . ? 0.2602 0.3325 0.2842 -0.0170 0.0142 -0.0045 906 5JK A C9 6550 C C10 . 5JK G . ? 0.2465 0.3238 0.2760 -0.0111 0.0137 -0.0024 906 5JK A C10 6551 C C19 . 5JK G . ? 0.2387 0.3284 0.2748 -0.0112 0.0107 0.0000 906 5JK A C19 6552 C C1 . 5JK G . ? 0.2376 0.3045 0.2619 -0.0076 0.0130 -0.0025 906 5JK A C1 6553 C C2 . 5JK G . ? 0.2560 0.3230 0.2834 -0.0014 0.0141 -0.0012 906 5JK A C2 6554 C C3 . 5JK G . ? 0.2769 0.3431 0.3051 0.0002 0.0183 -0.0023 906 5JK A C3 6555 O O1 . 5JK G . ? 0.2834 0.3471 0.3130 0.0059 0.0202 -0.0016 906 5JK A O1 6556 C C4 . 5JK G . ? 0.2737 0.3508 0.3081 -0.0019 0.0196 -0.0017 906 5JK A C4 6557 C C5 . 5JK G . ? 0.2621 0.3426 0.2955 -0.0083 0.0175 -0.0023 906 5JK A C5 6558 C C6 . 5JK G . ? 0.2667 0.3523 0.3024 -0.0118 0.0198 -0.0030 906 5JK A C6 6559 C C7 . 5JK G . ? 0.2704 0.3528 0.3014 -0.0185 0.0195 -0.0046 906 5JK A C7 6560 O O2 . 5JK G . ? 0.2417 0.3126 0.2658 -0.0178 0.0219 -0.0061 906 5JK A O2 6561 C C8 . 5JK G . ? 0.2613 0.3418 0.2891 -0.0215 0.0156 -0.0048 906 5JK A C8 6562 C C14 . 5JK G . ? 0.2837 0.3576 0.3052 -0.0276 0.0163 -0.0067 906 5JK A C14 6563 C C15 . 5JK G . ? 0.3085 0.3879 0.3320 -0.0333 0.0181 -0.0074 906 5JK A C15 6564 C C16 . 5JK G . ? 0.3167 0.3875 0.3329 -0.0387 0.0179 -0.0092 906 5JK A C16 6565 C C17 . 5JK G . ? 0.3156 0.3788 0.3271 -0.0359 0.0157 -0.0092 906 5JK A C17 6566 C C20 . 5JK G . ? 0.3581 0.4167 0.3641 -0.0413 0.0146 -0.0107 906 5JK A C20 6567 C C21 . 5JK G . ? 0.3666 0.4194 0.3688 -0.0384 0.0124 -0.0105 906 5JK A C21 6568 C C22 . 5JK G . ? 0.3740 0.4225 0.3738 -0.0450 0.0181 -0.0123 906 5JK A C22 6569 C C23 . 5JK G . ? 0.3997 0.4443 0.3942 -0.0515 0.0181 -0.0143 906 5JK A C23 6570 C C24 . 5JK G . ? 0.4163 0.4521 0.4059 -0.0556 0.0224 -0.0156 906 5JK A C24 6571 C C25 . 5JK G . ? 0.4788 0.5051 0.4607 -0.0608 0.0237 -0.0178 906 5JK A C25 6572 C C27 . 5JK G . ? 0.4870 0.5014 0.4634 -0.0625 0.0286 -0.0183 906 5JK A C27 6573 C C26 . 5JK G . ? 0.5048 0.5390 0.4871 -0.0681 0.0216 -0.0195 906 5JK A C26 6574 CA CA . CA H . ? 0.2297 0.2033 0.2098 -0.0105 0.0180 0.0188 907 CA A CA 6575 I I . IOD I . ? 0.3020 0.3231 0.2245 -0.0308 0.0483 -0.0003 908 IOD A I 6576 I I . IOD J . ? 0.5782 0.5355 0.3160 0.0057 0.0606 0.0238 909 IOD A I 6577 I I . IOD K . ? 0.6157 0.5328 0.2582 0.0424 0.0326 0.0490 910 IOD A I 6578 I I . IOD L . ? 0.3841 0.5874 0.4190 -0.0470 0.0600 -0.0206 911 IOD A I 6579 I I . IOD M . ? 0.6441 0.4407 0.3927 -0.1199 0.1148 -0.0398 912 IOD A I 6580 I I . IOD N . ? 0.9291 0.4483 0.6970 -0.2236 0.1609 0.0109 913 IOD A I 6581 I I . IOD O . ? 0.7945 0.4888 0.4805 -0.2222 0.0321 -0.0605 914 IOD A I 6582 I I . IOD P . ? 0.3203 0.4623 0.3027 -0.0288 -0.0135 -0.0304 915 IOD A I 6583 I I . IOD Q . ? 0.3370 0.4905 0.3538 -0.0847 0.0180 -0.0133 916 IOD A I 6584 I I . IOD R . ? 0.6855 0.5752 0.3419 -0.0969 -0.0245 -0.0880 917 IOD A I # 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 ALA 1 36 ? ? ? A . n A 1 2 GLU 2 37 ? ? ? A . n A 1 3 TRP 3 38 ? ? ? A . n A 1 4 ASP 4 39 ? ? ? A . n A 1 5 GLU 5 40 ? ? ? A . n A 1 6 GLY 6 41 ? ? ? A . n A 1 7 PRO 7 42 ? ? ? A . n A 1 8 PRO 8 43 ? ? ? A . n A 1 9 THR 9 44 ? ? ? A . n A 1 10 VAL 10 45 ? ? ? A . n A 1 11 LEU 11 46 ? ? ? A . n A 1 12 SER 12 47 ? ? ? A . n A 1 13 ASP 13 48 ? ? ? A . n A 1 14 SER 14 49 ? ? ? A . n A 1 15 PRO 15 50 ? ? ? A . n A 1 16 TRP 16 51 ? ? ? A . n A 1 17 THR 17 52 ? ? ? A . n A 1 18 ASN 18 53 ? ? ? A . n A 1 19 THR 19 54 ? ? ? A . n A 1 20 SER 20 55 ? ? ? A . n A 1 21 GLY 21 56 56 GLY GLY A . n A 1 22 SER 22 57 57 SER SER A . n A 1 23 CYS 23 58 58 CYS CYS A . n A 1 24 LYS 24 59 59 LYS LYS A . n A 1 25 GLY 25 60 60 GLY GLY A . n A 1 26 ARG 26 61 61 ARG ARG A . n A 1 27 CYS 27 62 62 CYS CYS A . n A 1 28 PHE 28 63 63 PHE PHE A . n A 1 29 GLU 29 64 64 GLU GLU A . n A 1 30 LEU 30 65 65 LEU LEU A . n A 1 31 GLN 31 66 66 GLN GLN A . n A 1 32 GLU 32 67 67 GLU GLU A . n A 1 33 VAL 33 68 68 VAL VAL A . n A 1 34 GLY 34 69 69 GLY GLY A . n A 1 35 PRO 35 70 70 PRO PRO A . n A 1 36 PRO 36 71 71 PRO PRO A . n A 1 37 ASP 37 72 72 ASP ASP A . n A 1 38 CYS 38 73 73 CYS CYS A . n A 1 39 ARG 39 74 74 ARG ARG A . n A 1 40 CYS 40 75 75 CYS CYS A . n A 1 41 ASP 41 76 76 ASP ASP A . n A 1 42 ASN 42 77 77 ASN ASN A . n A 1 43 LEU 43 78 78 LEU LEU A . n A 1 44 CYS 44 79 79 CYS CYS A . n A 1 45 LYS 45 80 80 LYS LYS A . n A 1 46 SER 46 81 81 SER SER A . n A 1 47 TYR 47 82 82 TYR TYR A . n A 1 48 SER 48 83 83 SER SER A . n A 1 49 SER 49 84 84 SER SER A . n A 1 50 CYS 50 85 85 CYS CYS A . n A 1 51 CYS 51 86 86 CYS CYS A . n A 1 52 HIS 52 87 87 HIS HIS A . n A 1 53 ASP 53 88 88 ASP ASP A . n A 1 54 PHE 54 89 89 PHE PHE A . n A 1 55 ASP 55 90 90 ASP ASP A . n A 1 56 GLU 56 91 91 GLU GLU A . n A 1 57 LEU 57 92 92 LEU LEU A . n A 1 58 CYS 58 93 93 CYS CYS A . n A 1 59 LEU 59 94 94 LEU LEU A . n A 1 60 LYS 60 95 95 LYS LYS A . n A 1 61 THR 61 96 96 THR THR A . n A 1 62 ALA 62 97 97 ALA ALA A . n A 1 63 ARG 63 98 98 ARG ARG A . n A 1 64 GLY 64 99 99 GLY GLY A . n A 1 65 TRP 65 100 100 TRP TRP A . n A 1 66 GLU 66 101 101 GLU GLU A . n A 1 67 CYS 67 102 102 CYS CYS A . n A 1 68 THR 68 103 103 THR THR A . n A 1 69 LYS 69 104 104 LYS LYS A . n A 1 70 ASP 70 105 105 ASP ASP A . n A 1 71 ARG 71 106 106 ARG ARG A . n A 1 72 CYS 72 107 107 CYS CYS A . n A 1 73 GLY 73 108 108 GLY GLY A . n A 1 74 GLU 74 109 109 GLU GLU A . n A 1 75 VAL 75 110 110 VAL VAL A . n A 1 76 ARG 76 111 111 ARG ARG A . n A 1 77 ASN 77 112 112 ASN ASN A . n A 1 78 GLU 78 113 113 GLU GLU A . n A 1 79 GLU 79 114 114 GLU GLU A . n A 1 80 ASN 80 115 115 ASN ASN A . n A 1 81 ALA 81 116 116 ALA ALA A . n A 1 82 CYS 82 117 117 CYS CYS A . n A 1 83 HIS 83 118 118 HIS HIS A . n A 1 84 CYS 84 119 119 CYS CYS A . n A 1 85 SER 85 120 120 SER SER A . n A 1 86 GLU 86 121 121 GLU GLU A . n A 1 87 ASP 87 122 122 ASP ASP A . n A 1 88 CYS 88 123 123 CYS CYS A . n A 1 89 LEU 89 124 124 LEU LEU A . n A 1 90 SER 90 125 125 SER SER A . n A 1 91 ARG 91 126 126 ARG ARG A . n A 1 92 GLY 92 127 127 GLY GLY A . n A 1 93 ASP 93 128 128 ASP ASP A . n A 1 94 CYS 94 129 129 CYS CYS A . n A 1 95 CYS 95 130 130 CYS CYS A . n A 1 96 THR 96 131 131 THR THR A . n A 1 97 ASN 97 132 132 ASN ASN A . n A 1 98 TYR 98 133 133 TYR TYR A . n A 1 99 GLN 99 134 134 GLN GLN A . n A 1 100 VAL 100 135 135 VAL VAL A . n A 1 101 VAL 101 136 136 VAL VAL A . n A 1 102 CYS 102 137 137 CYS CYS A . n A 1 103 LYS 103 138 138 LYS LYS A . n A 1 104 GLY 104 139 139 GLY GLY A . n A 1 105 GLU 105 140 140 GLU GLU A . n A 1 106 SER 106 141 141 SER SER A . n A 1 107 HIS 107 142 142 HIS HIS A . n A 1 108 TRP 108 143 143 TRP TRP A . n A 1 109 VAL 109 144 144 VAL VAL A . n A 1 110 ASP 110 145 145 ASP ASP A . n A 1 111 ASP 111 146 146 ASP ASP A . n A 1 112 ASP 112 147 147 ASP ASP A . n A 1 113 CYS 113 148 148 CYS CYS A . n A 1 114 GLU 114 149 149 GLU GLU A . n A 1 115 GLU 115 150 150 GLU GLU A . n A 1 116 ILE 116 151 151 ILE ILE A . n A 1 117 LYS 117 152 152 LYS LYS A . n A 1 118 VAL 118 153 153 VAL VAL A . n A 1 119 PRO 119 154 154 PRO PRO A . n A 1 120 GLU 120 155 155 GLU GLU A . n A 1 121 CYS 121 156 156 CYS CYS A . n A 1 122 PRO 122 157 157 PRO PRO A . n A 1 123 ALA 123 158 158 ALA ALA A . n A 1 124 GLY 124 159 159 GLY GLY A . n A 1 125 PHE 125 160 160 PHE PHE A . n A 1 126 VAL 126 161 161 VAL VAL A . n A 1 127 ARG 127 162 162 ARG ARG A . n A 1 128 PRO 128 163 163 PRO PRO A . n A 1 129 PRO 129 164 164 PRO PRO A . n A 1 130 LEU 130 165 165 LEU LEU A . n A 1 131 ILE 131 166 166 ILE ILE A . n A 1 132 ILE 132 167 167 ILE ILE A . n A 1 133 PHE 133 168 168 PHE PHE A . n A 1 134 SER 134 169 169 SER SER A . n A 1 135 VAL 135 170 170 VAL VAL A . n A 1 136 ASP 136 171 171 ASP ASP A . n A 1 137 GLY 137 172 172 GLY GLY A . n A 1 138 PHE 138 173 173 PHE PHE A . n A 1 139 ARG 139 174 174 ARG ARG A . n A 1 140 ALA 140 175 175 ALA ALA A . n A 1 141 SER 141 176 176 SER SER A . n A 1 142 TYR 142 177 177 TYR TYR A . n A 1 143 MET 143 178 178 MET MET A . n A 1 144 LYS 144 179 179 LYS LYS A . n A 1 145 LYS 145 180 180 LYS LYS A . n A 1 146 GLY 146 181 181 GLY GLY A . n A 1 147 SER 147 182 182 SER SER A . n A 1 148 LYS 148 183 183 LYS LYS A . n A 1 149 VAL 149 184 184 VAL VAL A . n A 1 150 MET 150 185 185 MET MET A . n A 1 151 PRO 151 186 186 PRO PRO A . n A 1 152 ASN 152 187 187 ASN ASN A . n A 1 153 ILE 153 188 188 ILE ILE A . n A 1 154 GLU 154 189 189 GLU GLU A . n A 1 155 LYS 155 190 190 LYS LYS A . n A 1 156 LEU 156 191 191 LEU LEU A . n A 1 157 ARG 157 192 192 ARG ARG A . n A 1 158 SER 158 193 193 SER SER A . n A 1 159 CYS 159 194 194 CYS CYS A . n A 1 160 GLY 160 195 195 GLY GLY A . n A 1 161 THR 161 196 196 THR THR A . n A 1 162 HIS 162 197 197 HIS HIS A . n A 1 163 ALA 163 198 198 ALA ALA A . n A 1 164 PRO 164 199 199 PRO PRO A . n A 1 165 TYR 165 200 200 TYR TYR A . n A 1 166 MET 166 201 201 MET MET A . n A 1 167 ARG 167 202 202 ARG ARG A . n A 1 168 PRO 168 203 203 PRO PRO A . n A 1 169 VAL 169 204 204 VAL VAL A . n A 1 170 TYR 170 205 205 TYR TYR A . n A 1 171 PRO 171 206 206 PRO PRO A . n A 1 172 THR 172 207 207 THR THR A . n A 1 173 LYS 173 208 208 LYS LYS A . n A 1 174 TPO 174 209 209 TPO TPO A . n A 1 175 PHE 175 210 210 PHE PHE A . n A 1 176 PRO 176 211 211 PRO PRO A . n A 1 177 ASN 177 212 212 ASN ASN A . n A 1 178 LEU 178 213 213 LEU LEU A . n A 1 179 TYR 179 214 214 TYR TYR A . n A 1 180 THR 180 215 215 THR THR A . n A 1 181 LEU 181 216 216 LEU LEU A . n A 1 182 ALA 182 217 217 ALA ALA A . n A 1 183 THR 183 218 218 THR THR A . n A 1 184 GLY 184 219 219 GLY GLY A . n A 1 185 LEU 185 220 220 LEU LEU A . n A 1 186 TYR 186 221 221 TYR TYR A . n A 1 187 PRO 187 222 222 PRO PRO A . n A 1 188 GLU 188 223 223 GLU GLU A . n A 1 189 SER 189 224 224 SER SER A . n A 1 190 HIS 190 225 225 HIS HIS A . n A 1 191 GLY 191 226 226 GLY GLY A . n A 1 192 ILE 192 227 227 ILE ILE A . n A 1 193 VAL 193 228 228 VAL VAL A . n A 1 194 GLY 194 229 229 GLY GLY A . n A 1 195 ASN 195 230 230 ASN ASN A . n A 1 196 SER 196 231 231 SER SER A . n A 1 197 MET 197 232 232 MET MET A . n A 1 198 TYR 198 233 233 TYR TYR A . n A 1 199 ASP 199 234 234 ASP ASP A . n A 1 200 PRO 200 235 235 PRO PRO A . n A 1 201 VAL 201 236 236 VAL VAL A . n A 1 202 PHE 202 237 237 PHE PHE A . n A 1 203 ASP 203 238 238 ASP ASP A . n A 1 204 ALA 204 239 239 ALA ALA A . n A 1 205 SER 205 240 240 SER SER A . n A 1 206 PHE 206 241 241 PHE PHE A . n A 1 207 HIS 207 242 242 HIS HIS A . n A 1 208 LEU 208 243 243 LEU LEU A . n A 1 209 ARG 209 244 244 ARG ARG A . n A 1 210 GLY 210 245 245 GLY GLY A . n A 1 211 ARG 211 246 246 ARG ARG A . n A 1 212 GLU 212 247 247 GLU GLU A . n A 1 213 LYS 213 248 248 LYS LYS A . n A 1 214 PHE 214 249 249 PHE PHE A . n A 1 215 ASN 215 250 250 ASN ASN A . n A 1 216 HIS 216 251 251 HIS HIS A . n A 1 217 ARG 217 252 252 ARG ARG A . n A 1 218 TRP 218 253 253 TRP TRP A . n A 1 219 TRP 219 254 254 TRP TRP A . n A 1 220 GLY 220 255 255 GLY GLY A . n A 1 221 GLY 221 256 256 GLY GLY A . n A 1 222 GLN 222 257 257 GLN GLN A . n A 1 223 PRO 223 258 258 PRO PRO A . n A 1 224 LEU 224 259 259 LEU LEU A . n A 1 225 TRP 225 260 260 TRP TRP A . n A 1 226 ILE 226 261 261 ILE ILE A . n A 1 227 THR 227 262 262 THR THR A . n A 1 228 ALA 228 263 263 ALA ALA A . n A 1 229 THR 229 264 264 THR THR A . n A 1 230 LYS 230 265 265 LYS LYS A . n A 1 231 GLN 231 266 266 GLN GLN A . n A 1 232 GLY 232 267 267 GLY GLY A . n A 1 233 VAL 233 268 268 VAL VAL A . n A 1 234 ARG 234 269 269 ARG ARG A . n A 1 235 ALA 235 270 270 ALA ALA A . n A 1 236 GLY 236 271 271 GLY GLY A . n A 1 237 THR 237 272 272 THR THR A . n A 1 238 PHE 238 273 273 PHE PHE A . n A 1 239 PHE 239 274 274 PHE PHE A . n A 1 240 TRP 240 275 275 TRP TRP A . n A 1 241 SER 241 276 276 SER SER A . n A 1 242 VAL 242 277 277 VAL VAL A . n A 1 243 SER 243 278 278 SER SER A . n A 1 244 ILE 244 279 279 ILE ILE A . n A 1 245 PRO 245 280 280 PRO PRO A . n A 1 246 HIS 246 281 281 HIS HIS A . n A 1 247 GLU 247 282 282 GLU GLU A . n A 1 248 ARG 248 283 283 ARG ARG A . n A 1 249 ARG 249 284 284 ARG ARG A . n A 1 250 ILE 250 285 285 ILE ILE A . n A 1 251 LEU 251 286 286 LEU LEU A . n A 1 252 THR 252 287 287 THR THR A . n A 1 253 ILE 253 288 288 ILE ILE A . n A 1 254 LEU 254 289 289 LEU LEU A . n A 1 255 GLN 255 290 290 GLN GLN A . n A 1 256 TRP 256 291 291 TRP TRP A . n A 1 257 LEU 257 292 292 LEU LEU A . n A 1 258 SER 258 293 293 SER SER A . n A 1 259 LEU 259 294 294 LEU LEU A . n A 1 260 PRO 260 295 295 PRO PRO A . n A 1 261 ASP 261 296 296 ASP ASP A . n A 1 262 ASN 262 297 297 ASN ASN A . n A 1 263 GLU 263 298 298 GLU GLU A . n A 1 264 ARG 264 299 299 ARG ARG A . n A 1 265 PRO 265 300 300 PRO PRO A . n A 1 266 SER 266 301 301 SER SER A . n A 1 267 VAL 267 302 302 VAL VAL A . n A 1 268 TYR 268 303 303 TYR TYR A . n A 1 269 ALA 269 304 304 ALA ALA A . n A 1 270 PHE 270 305 305 PHE PHE A . n A 1 271 TYR 271 306 306 TYR TYR A . n A 1 272 SER 272 307 307 SER SER A . n A 1 273 GLU 273 308 308 GLU GLU A . n A 1 274 GLN 274 309 309 GLN GLN A . n A 1 275 PRO 275 310 310 PRO PRO A . n A 1 276 ASP 276 311 311 ASP ASP A . n A 1 277 PHE 277 312 312 PHE PHE A . n A 1 278 SER 278 313 313 SER SER A . n A 1 279 GLY 279 314 314 GLY GLY A . n A 1 280 HIS 280 315 315 HIS HIS A . n A 1 281 LYS 281 316 316 LYS LYS A . n A 1 282 TYR 282 317 317 TYR TYR A . n A 1 283 GLY 283 318 318 GLY GLY A . n A 1 284 PRO 284 319 319 PRO PRO A . n A 1 285 PHE 285 320 320 PHE PHE A . n A 1 286 GLY 286 321 321 GLY GLY A . n A 1 287 PRO 287 322 322 PRO PRO A . n A 1 288 GLU 288 323 323 GLU GLU A . n A 1 289 MET 289 324 324 MET MET A . n A 1 290 THR 290 325 325 THR THR A . n A 1 291 ASN 291 326 326 ASN ASN A . n A 1 292 PRO 292 327 327 PRO PRO A . n A 1 293 LEU 293 328 328 LEU LEU A . n A 1 294 ARG 294 329 329 ARG ARG A . n A 1 295 GLU 295 330 330 GLU GLU A . n A 1 296 ILE 296 331 331 ILE ILE A . n A 1 297 ASP 297 332 332 ASP ASP A . n A 1 298 LYS 298 333 333 LYS LYS A . n A 1 299 THR 299 334 334 THR THR A . n A 1 300 VAL 300 335 335 VAL VAL A . n A 1 301 GLY 301 336 336 GLY GLY A . n A 1 302 GLN 302 337 337 GLN GLN A . n A 1 303 LEU 303 338 338 LEU LEU A . n A 1 304 MET 304 339 339 MET MET A . n A 1 305 ASP 305 340 340 ASP ASP A . n A 1 306 GLY 306 341 341 GLY GLY A . n A 1 307 LEU 307 342 342 LEU LEU A . n A 1 308 LYS 308 343 343 LYS LYS A . n A 1 309 GLN 309 344 344 GLN GLN A . n A 1 310 LEU 310 345 345 LEU LEU A . n A 1 311 ARG 311 346 346 ARG ARG A . n A 1 312 LEU 312 347 347 LEU LEU A . n A 1 313 HIS 313 348 348 HIS HIS A . n A 1 314 ARG 314 349 349 ARG ARG A . n A 1 315 CYS 315 350 350 CYS CYS A . n A 1 316 VAL 316 351 351 VAL VAL A . n A 1 317 ASN 317 352 352 ASN ASN A . n A 1 318 VAL 318 353 353 VAL VAL A . n A 1 319 ILE 319 354 354 ILE ILE A . n A 1 320 PHE 320 355 355 PHE PHE A . n A 1 321 VAL 321 356 356 VAL VAL A . n A 1 322 GLY 322 357 357 GLY GLY A . n A 1 323 ASP 323 358 358 ASP ASP A . n A 1 324 HIS 324 359 359 HIS HIS A . n A 1 325 GLY 325 360 360 GLY GLY A . n A 1 326 MET 326 361 361 MET MET A . n A 1 327 GLU 327 362 362 GLU GLU A . n A 1 328 ASP 328 363 363 ASP ASP A . n A 1 329 VAL 329 364 364 VAL VAL A . n A 1 330 THR 330 365 365 THR THR A . n A 1 331 CYS 331 366 366 CYS CYS A . n A 1 332 ASP 332 367 367 ASP ASP A . n A 1 333 ARG 333 368 368 ARG ARG A . n A 1 334 THR 334 369 369 THR THR A . n A 1 335 GLU 335 370 370 GLU GLU A . n A 1 336 PHE 336 371 371 PHE PHE A . n A 1 337 LEU 337 372 372 LEU LEU A . n A 1 338 SER 338 373 373 SER SER A . n A 1 339 ASN 339 374 374 ASN ASN A . n A 1 340 TYR 340 375 375 TYR TYR A . n A 1 341 LEU 341 376 376 LEU LEU A . n A 1 342 THR 342 377 377 THR THR A . n A 1 343 ASN 343 378 378 ASN ASN A . n A 1 344 VAL 344 379 379 VAL VAL A . n A 1 345 ASP 345 380 380 ASP ASP A . n A 1 346 ASP 346 381 381 ASP ASP A . n A 1 347 ILE 347 382 382 ILE ILE A . n A 1 348 THR 348 383 383 THR THR A . n A 1 349 LEU 349 384 384 LEU LEU A . n A 1 350 VAL 350 385 385 VAL VAL A . n A 1 351 PRO 351 386 386 PRO PRO A . n A 1 352 GLY 352 387 387 GLY GLY A . n A 1 353 THR 353 388 388 THR THR A . n A 1 354 LEU 354 389 389 LEU LEU A . n A 1 355 GLY 355 390 390 GLY GLY A . n A 1 356 ARG 356 391 391 ARG ARG A . n A 1 357 ILE 357 392 392 ILE ILE A . n A 1 358 ARG 358 393 393 ARG ARG A . n A 1 359 ALA 359 394 394 ALA ALA A . n A 1 360 LYS 360 395 395 LYS LYS A . n A 1 361 SER 361 396 396 SER SER A . n A 1 362 ILE 362 397 397 ILE ILE A . n A 1 363 ASN 363 398 398 ASN ASN A . n A 1 364 ASN 364 399 399 ASN ASN A . n A 1 365 SER 365 400 400 SER SER A . n A 1 366 LYS 366 401 401 LYS LYS A . n A 1 367 TYR 367 402 402 TYR TYR A . n A 1 368 ASP 368 403 403 ASP ASP A . n A 1 369 PRO 369 404 404 PRO PRO A . n A 1 370 LYS 370 405 405 LYS LYS A . n A 1 371 THR 371 406 406 THR THR A . n A 1 372 ILE 372 407 407 ILE ILE A . n A 1 373 ILE 373 408 408 ILE ILE A . n A 1 374 ALA 374 409 409 ALA ALA A . n A 1 375 ALA 375 410 410 ALA ALA A . n A 1 376 LEU 376 411 411 LEU LEU A . n A 1 377 THR 377 412 412 THR THR A . n A 1 378 CYS 378 413 413 CYS CYS A . n A 1 379 LYS 379 414 414 LYS LYS A . n A 1 380 LYS 380 415 415 LYS LYS A . n A 1 381 PRO 381 416 416 PRO PRO A . n A 1 382 ASP 382 417 417 ASP ASP A . n A 1 383 GLN 383 418 418 GLN GLN A . n A 1 384 HIS 384 419 419 HIS HIS A . n A 1 385 PHE 385 420 420 PHE PHE A . n A 1 386 LYS 386 421 421 LYS LYS A . n A 1 387 PRO 387 422 422 PRO PRO A . n A 1 388 TYR 388 423 423 TYR TYR A . n A 1 389 MET 389 424 424 MET MET A . n A 1 390 LYS 390 425 425 LYS LYS A . n A 1 391 GLN 391 426 426 GLN GLN A . n A 1 392 HIS 392 427 427 HIS HIS A . n A 1 393 LEU 393 428 428 LEU LEU A . n A 1 394 PRO 394 429 429 PRO PRO A . n A 1 395 LYS 395 430 430 LYS LYS A . n A 1 396 ARG 396 431 431 ARG ARG A . n A 1 397 LEU 397 432 432 LEU LEU A . n A 1 398 HIS 398 433 433 HIS HIS A . n A 1 399 TYR 399 434 434 TYR TYR A . n A 1 400 ALA 400 435 435 ALA ALA A . n A 1 401 ASN 401 436 436 ASN ASN A . n A 1 402 ASN 402 437 437 ASN ASN A . n A 1 403 ARG 403 438 438 ARG ARG A . n A 1 404 ARG 404 439 439 ARG ARG A . n A 1 405 ILE 405 440 440 ILE ILE A . n A 1 406 GLU 406 441 441 GLU GLU A . n A 1 407 ASP 407 442 442 ASP ASP A . n A 1 408 ILE 408 443 443 ILE ILE A . n A 1 409 HIS 409 444 444 HIS HIS A . n A 1 410 LEU 410 445 445 LEU LEU A . n A 1 411 LEU 411 446 446 LEU LEU A . n A 1 412 VAL 412 447 447 VAL VAL A . n A 1 413 ASP 413 448 448 ASP ASP A . n A 1 414 ARG 414 449 449 ARG ARG A . n A 1 415 ARG 415 450 450 ARG ARG A . n A 1 416 TRP 416 451 451 TRP TRP A . n A 1 417 HIS 417 452 452 HIS HIS A . n A 1 418 VAL 418 453 453 VAL VAL A . n A 1 419 ALA 419 454 454 ALA ALA A . n A 1 420 ARG 420 455 455 ARG ARG A . n A 1 421 LYS 421 456 456 LYS LYS A . n A 1 422 PRO 422 457 457 PRO PRO A . n A 1 423 LEU 423 458 458 LEU LEU A . n A 1 424 ASP 424 459 459 ASP ASP A . n A 1 425 VAL 425 460 ? ? ? A . n A 1 426 TYR 426 461 ? ? ? A . n A 1 427 LYS 427 462 ? ? ? A . n A 1 428 LYS 428 463 ? ? ? A . n A 1 429 PRO 429 464 ? ? ? A . n A 1 430 SER 430 465 ? ? ? A . n A 1 431 GLY 431 466 ? ? ? A . n A 1 432 LYS 432 467 467 LYS LYS A . n A 1 433 CYS 433 468 468 CYS CYS A . n A 1 434 PHE 434 469 469 PHE PHE A . n A 1 435 PHE 435 470 470 PHE PHE A . n A 1 436 GLN 436 471 471 GLN GLN A . n A 1 437 GLY 437 472 472 GLY GLY A . n A 1 438 ASP 438 473 473 ASP ASP A . n A 1 439 HIS 439 474 474 HIS HIS A . n A 1 440 GLY 440 475 475 GLY GLY A . n A 1 441 PHE 441 476 476 PHE PHE A . n A 1 442 ASP 442 477 477 ASP ASP A . n A 1 443 ASN 443 478 478 ASN ASN A . n A 1 444 LYS 444 479 479 LYS LYS A . n A 1 445 VAL 445 480 480 VAL VAL A . n A 1 446 ASN 446 481 481 ASN ASN A . n A 1 447 SER 447 482 482 SER SER A . n A 1 448 MET 448 483 483 MET MET A . n A 1 449 GLN 449 484 484 GLN GLN A . n A 1 450 THR 450 485 485 THR THR A . n A 1 451 VAL 451 486 486 VAL VAL A . n A 1 452 PHE 452 487 487 PHE PHE A . n A 1 453 VAL 453 488 488 VAL VAL A . n A 1 454 GLY 454 489 489 GLY GLY A . n A 1 455 TYR 455 490 490 TYR TYR A . n A 1 456 GLY 456 491 491 GLY GLY A . n A 1 457 PRO 457 492 492 PRO PRO A . n A 1 458 THR 458 493 493 THR THR A . n A 1 459 PHE 459 494 494 PHE PHE A . n A 1 460 LYS 460 495 495 LYS LYS A . n A 1 461 TYR 461 496 496 TYR TYR A . n A 1 462 ARG 462 497 497 ARG ARG A . n A 1 463 THR 463 498 498 THR THR A . n A 1 464 LYS 464 499 499 LYS LYS A . n A 1 465 VAL 465 500 500 VAL VAL A . n A 1 466 PRO 466 501 501 PRO PRO A . n A 1 467 PRO 467 502 502 PRO PRO A . n A 1 468 PHE 468 503 503 PHE PHE A . n A 1 469 GLU 469 504 504 GLU GLU A . n A 1 470 ASN 470 505 505 ASN ASN A . n A 1 471 ILE 471 506 506 ILE ILE A . n A 1 472 GLU 472 507 507 GLU GLU A . n A 1 473 LEU 473 508 508 LEU LEU A . n A 1 474 TYR 474 509 509 TYR TYR A . n A 1 475 ASN 475 510 510 ASN ASN A . n A 1 476 VAL 476 511 511 VAL VAL A . n A 1 477 MET 477 512 512 MET MET A . n A 1 478 CYS 478 513 513 CYS CYS A . n A 1 479 ASP 479 514 514 ASP ASP A . n A 1 480 LEU 480 515 515 LEU LEU A . n A 1 481 LEU 481 516 516 LEU LEU A . n A 1 482 GLY 482 517 517 GLY GLY A . n A 1 483 LEU 483 518 518 LEU LEU A . n A 1 484 LYS 484 519 519 LYS LYS A . n A 1 485 PRO 485 520 520 PRO PRO A . n A 1 486 ALA 486 521 521 ALA ALA A . n A 1 487 PRO 487 522 522 PRO PRO A . n A 1 488 ASN 488 523 523 ASN ASN A . n A 1 489 ASN 489 524 524 ASN ASN A . n A 1 490 GLY 490 525 525 GLY GLY A . n A 1 491 THR 491 526 526 THR THR A . n A 1 492 HIS 492 527 527 HIS HIS A . n A 1 493 GLY 493 528 528 GLY GLY A . n A 1 494 SER 494 529 529 SER SER A . n A 1 495 LEU 495 530 530 LEU LEU A . n A 1 496 ASN 496 531 531 ASN ASN A . n A 1 497 HIS 497 532 532 HIS HIS A . n A 1 498 LEU 498 533 533 LEU LEU A . n A 1 499 LEU 499 534 534 LEU LEU A . n A 1 500 ARG 500 535 535 ARG ARG A . n A 1 501 THR 501 536 536 THR THR A . n A 1 502 ASN 502 537 537 ASN ASN A . n A 1 503 THR 503 538 538 THR THR A . n A 1 504 PHE 504 539 539 PHE PHE A . n A 1 505 ARG 505 540 540 ARG ARG A . n A 1 506 PRO 506 541 541 PRO PRO A . n A 1 507 THR 507 542 542 THR THR A . n A 1 508 MET 508 543 543 MET MET A . n A 1 509 PRO 509 544 544 PRO PRO A . n A 1 510 ASP 510 545 545 ASP ASP A . n A 1 511 GLU 511 546 546 GLU GLU A . n A 1 512 VAL 512 547 547 VAL VAL A . n A 1 513 SER 513 548 548 SER SER A . n A 1 514 ARG 514 549 549 ARG ARG A . n A 1 515 PRO 515 550 550 PRO PRO A . n A 1 516 ASN 516 551 551 ASN ASN A . n A 1 517 TYR 517 552 552 TYR TYR A . n A 1 518 PRO 518 553 553 PRO PRO A . n A 1 519 GLY 519 554 554 GLY GLY A . n A 1 520 ILE 520 555 555 ILE ILE A . n A 1 521 MET 521 556 556 MET MET A . n A 1 522 TYR 522 557 557 TYR TYR A . n A 1 523 LEU 523 558 558 LEU LEU A . n A 1 524 GLN 524 559 559 GLN GLN A . n A 1 525 SER 525 560 560 SER SER A . n A 1 526 GLU 526 561 561 GLU GLU A . n A 1 527 PHE 527 562 562 PHE PHE A . n A 1 528 ASP 528 563 563 ASP ASP A . n A 1 529 LEU 529 564 564 LEU LEU A . n A 1 530 GLY 530 565 565 GLY GLY A . n A 1 531 CYS 531 566 566 CYS CYS A . n A 1 532 THR 532 567 567 THR THR A . n A 1 533 CYS 533 568 568 CYS CYS A . n A 1 534 ASP 534 569 ? ? ? A . n A 1 535 ASP 535 570 ? ? ? A . n A 1 536 LYS 536 571 571 LYS LYS A . n A 1 537 VAL 537 572 572 VAL VAL A . n A 1 538 GLU 538 573 573 GLU GLU A . n A 1 539 PRO 539 574 574 PRO PRO A . n A 1 540 LYS 540 575 575 LYS LYS A . n A 1 541 ASN 541 576 576 ASN ASN A . n A 1 542 LYS 542 577 577 LYS LYS A . n A 1 543 LEU 543 578 578 LEU LEU A . n A 1 544 GLU 544 579 579 GLU GLU A . n A 1 545 GLU 545 580 580 GLU GLU A . n A 1 546 PHE 546 581 581 PHE PHE A . n A 1 547 ASN 547 582 582 ASN ASN A . n A 1 548 LYS 548 583 583 LYS LYS A . n A 1 549 ARG 549 584 584 ARG ARG A . n A 1 550 LEU 550 585 585 LEU LEU A . n A 1 551 HIS 551 586 586 HIS HIS A . n A 1 552 THR 552 587 587 THR THR A . n A 1 553 LYS 553 588 588 LYS LYS A . n A 1 554 GLY 554 589 589 GLY GLY A . n A 1 555 SER 555 590 590 SER SER A . n A 1 556 THR 556 591 591 THR THR A . n A 1 557 LYS 557 592 592 LYS LYS A . n A 1 558 GLU 558 593 593 GLU GLU A . n A 1 559 ARG 559 594 594 ARG ARG A . n A 1 560 HIS 560 595 595 HIS HIS A . n A 1 561 LEU 561 596 596 LEU LEU A . n A 1 562 LEU 562 597 597 LEU LEU A . n A 1 563 TYR 563 598 598 TYR TYR A . n A 1 564 GLY 564 599 599 GLY GLY A . n A 1 565 ARG 565 600 600 ARG ARG A . n A 1 566 PRO 566 601 601 PRO PRO A . n A 1 567 ALA 567 602 602 ALA ALA A . n A 1 568 VAL 568 603 603 VAL VAL A . n A 1 569 LEU 569 604 604 LEU LEU A . n A 1 570 TYR 570 605 605 TYR TYR A . n A 1 571 ARG 571 606 606 ARG ARG A . n A 1 572 THR 572 607 607 THR THR A . n A 1 573 SER 573 608 608 SER SER A . n A 1 574 TYR 574 609 609 TYR TYR A . n A 1 575 ASP 575 610 610 ASP ASP A . n A 1 576 ILE 576 611 611 ILE ILE A . n A 1 577 LEU 577 612 612 LEU LEU A . n A 1 578 TYR 578 613 613 TYR TYR A . n A 1 579 HIS 579 614 614 HIS HIS A . n A 1 580 THR 580 615 615 THR THR A . n A 1 581 ASP 581 616 616 ASP ASP A . n A 1 582 PHE 582 617 617 PHE PHE A . n A 1 583 GLU 583 618 618 GLU GLU A . n A 1 584 SER 584 619 619 SER SER A . n A 1 585 GLY 585 620 620 GLY GLY A . n A 1 586 TYR 586 621 621 TYR TYR A . n A 1 587 SER 587 622 622 SER SER A . n A 1 588 GLU 588 623 623 GLU GLU A . n A 1 589 ILE 589 624 624 ILE ILE A . n A 1 590 PHE 590 625 625 PHE PHE A . n A 1 591 LEU 591 626 626 LEU LEU A . n A 1 592 MET 592 627 627 MET MET A . n A 1 593 PRO 593 628 628 PRO PRO A . n A 1 594 LEU 594 629 629 LEU LEU A . n A 1 595 TRP 595 630 630 TRP TRP A . n A 1 596 THR 596 631 631 THR THR A . n A 1 597 SER 597 632 632 SER SER A . n A 1 598 TYR 598 633 633 TYR TYR A . n A 1 599 THR 599 634 634 THR THR A . n A 1 600 ILE 600 635 635 ILE ILE A . n A 1 601 SER 601 636 636 SER SER A . n A 1 602 LYS 602 637 637 LYS LYS A . n A 1 603 GLN 603 638 638 GLN GLN A . n A 1 604 ALA 604 639 639 ALA ALA A . n A 1 605 GLU 605 640 640 GLU GLU A . n A 1 606 VAL 606 641 641 VAL VAL A . n A 1 607 SER 607 642 642 SER SER A . n A 1 608 SER 608 643 643 SER SER A . n A 1 609 ILE 609 644 644 ILE ILE A . n A 1 610 PRO 610 645 645 PRO PRO A . n A 1 611 GLU 611 646 646 GLU GLU A . n A 1 612 HIS 612 647 647 HIS HIS A . n A 1 613 LEU 613 648 648 LEU LEU A . n A 1 614 THR 614 649 649 THR THR A . n A 1 615 ASN 615 650 650 ASN ASN A . n A 1 616 CYS 616 651 651 CYS CYS A . n A 1 617 VAL 617 652 652 VAL VAL A . n A 1 618 ARG 618 653 653 ARG ARG A . n A 1 619 PRO 619 654 654 PRO PRO A . n A 1 620 ASP 620 655 655 ASP ASP A . n A 1 621 VAL 621 656 656 VAL VAL A . n A 1 622 ARG 622 657 657 ARG ARG A . n A 1 623 VAL 623 658 658 VAL VAL A . n A 1 624 SER 624 659 659 SER SER A . n A 1 625 PRO 625 660 660 PRO PRO A . n A 1 626 GLY 626 661 661 GLY GLY A . n A 1 627 PHE 627 662 662 PHE PHE A . n A 1 628 SER 628 663 663 SER SER A . n A 1 629 GLN 629 664 664 GLN GLN A . n A 1 630 ASN 630 665 665 ASN ASN A . n A 1 631 CYS 631 666 666 CYS CYS A . n A 1 632 LEU 632 667 667 LEU LEU A . n A 1 633 ALA 633 668 668 ALA ALA A . n A 1 634 TYR 634 669 669 TYR TYR A . n A 1 635 LYS 635 670 670 LYS LYS A . n A 1 636 ASN 636 671 671 ASN ASN A . n A 1 637 ASP 637 672 672 ASP ASP A . n A 1 638 LYS 638 673 673 LYS LYS A . n A 1 639 GLN 639 674 674 GLN GLN A . n A 1 640 MET 640 675 675 MET MET A . n A 1 641 SER 641 676 676 SER SER A . n A 1 642 TYR 642 677 677 TYR TYR A . n A 1 643 GLY 643 678 678 GLY GLY A . n A 1 644 PHE 644 679 679 PHE PHE A . n A 1 645 LEU 645 680 680 LEU LEU A . n A 1 646 PHE 646 681 681 PHE PHE A . n A 1 647 PRO 647 682 682 PRO PRO A . n A 1 648 PRO 648 683 683 PRO PRO A . n A 1 649 TYR 649 684 684 TYR TYR A . n A 1 650 LEU 650 685 685 LEU LEU A . n A 1 651 SER 651 686 686 SER SER A . n A 1 652 SER 652 687 687 SER SER A . n A 1 653 SER 653 688 688 SER SER A . n A 1 654 PRO 654 689 689 PRO PRO A . n A 1 655 GLU 655 690 690 GLU GLU A . n A 1 656 ALA 656 691 691 ALA ALA A . n A 1 657 LYS 657 692 692 LYS LYS A . n A 1 658 TYR 658 693 693 TYR TYR A . n A 1 659 ASP 659 694 694 ASP ASP A . n A 1 660 ALA 660 695 695 ALA ALA A . n A 1 661 PHE 661 696 696 PHE PHE A . n A 1 662 LEU 662 697 697 LEU LEU A . n A 1 663 VAL 663 698 698 VAL VAL A . n A 1 664 THR 664 699 699 THR THR A . n A 1 665 ASN 665 700 700 ASN ASN A . n A 1 666 MET 666 701 701 MET MET A . n A 1 667 VAL 667 702 702 VAL VAL A . n A 1 668 PRO 668 703 703 PRO PRO A . n A 1 669 MET 669 704 704 MET MET A . n A 1 670 TYR 670 705 705 TYR TYR A . n A 1 671 PRO 671 706 706 PRO PRO A . n A 1 672 ALA 672 707 707 ALA ALA A . n A 1 673 PHE 673 708 708 PHE PHE A . n A 1 674 LYS 674 709 709 LYS LYS A . n A 1 675 ARG 675 710 710 ARG ARG A . n A 1 676 VAL 676 711 711 VAL VAL A . n A 1 677 TRP 677 712 712 TRP TRP A . n A 1 678 ALA 678 713 713 ALA ALA A . n A 1 679 TYR 679 714 714 TYR TYR A . n A 1 680 PHE 680 715 715 PHE PHE A . n A 1 681 GLN 681 716 716 GLN GLN A . n A 1 682 ARG 682 717 717 ARG ARG A . n A 1 683 VAL 683 718 718 VAL VAL A . n A 1 684 LEU 684 719 719 LEU LEU A . n A 1 685 VAL 685 720 720 VAL VAL A . n A 1 686 LYS 686 721 721 LYS LYS A . n A 1 687 LYS 687 722 722 LYS LYS A . n A 1 688 TYR 688 723 723 TYR TYR A . n A 1 689 ALA 689 724 724 ALA ALA A . n A 1 690 SER 690 725 725 SER SER A . n A 1 691 GLU 691 726 726 GLU GLU A . n A 1 692 ARG 692 727 727 ARG ARG A . n A 1 693 ASN 693 728 728 ASN ASN A . n A 1 694 GLY 694 729 729 GLY GLY A . n A 1 695 VAL 695 730 730 VAL VAL A . n A 1 696 ASN 696 731 731 ASN ASN A . n A 1 697 VAL 697 732 732 VAL VAL A . n A 1 698 ILE 698 733 733 ILE ILE A . n A 1 699 SER 699 734 734 SER SER A . n A 1 700 GLY 700 735 735 GLY GLY A . n A 1 701 PRO 701 736 736 PRO PRO A . n A 1 702 ILE 702 737 737 ILE ILE A . n A 1 703 PHE 703 738 738 PHE PHE A . n A 1 704 ASP 704 739 739 ASP ASP A . n A 1 705 TYR 705 740 740 TYR TYR A . n A 1 706 ASN 706 741 741 ASN ASN A . n A 1 707 TYR 707 742 742 TYR TYR A . n A 1 708 ASP 708 743 743 ASP ASP A . n A 1 709 GLY 709 744 744 GLY GLY A . n A 1 710 LEU 710 745 745 LEU LEU A . n A 1 711 ARG 711 746 746 ARG ARG A . n A 1 712 ASP 712 747 747 ASP ASP A . n A 1 713 THR 713 748 748 THR THR A . n A 1 714 GLU 714 749 749 GLU GLU A . n A 1 715 ASP 715 750 750 ASP ASP A . n A 1 716 GLU 716 751 751 GLU GLU A . n A 1 717 ILE 717 752 752 ILE ILE A . n A 1 718 LYS 718 753 753 LYS LYS A . n A 1 719 GLN 719 754 754 GLN GLN A . n A 1 720 TYR 720 755 755 TYR TYR A . n A 1 721 VAL 721 756 756 VAL VAL A . n A 1 722 GLU 722 757 757 GLU GLU A . n A 1 723 GLY 723 758 758 GLY GLY A . n A 1 724 SER 724 759 759 SER SER A . n A 1 725 SER 725 760 760 SER SER A . n A 1 726 ILE 726 761 761 ILE ILE A . n A 1 727 PRO 727 762 762 PRO PRO A . n A 1 728 VAL 728 763 763 VAL VAL A . n A 1 729 PRO 729 764 764 PRO PRO A . n A 1 730 THR 730 765 765 THR THR A . n A 1 731 HIS 731 766 766 HIS HIS A . n A 1 732 TYR 732 767 767 TYR TYR A . n A 1 733 TYR 733 768 768 TYR TYR A . n A 1 734 SER 734 769 769 SER SER A . n A 1 735 ILE 735 770 770 ILE ILE A . n A 1 736 ILE 736 771 771 ILE ILE A . n A 1 737 THR 737 772 772 THR THR A . n A 1 738 SER 738 773 773 SER SER A . n A 1 739 CYS 739 774 774 CYS CYS A . n A 1 740 LEU 740 775 775 LEU LEU A . n A 1 741 ASP 741 776 776 ASP ASP A . n A 1 742 PHE 742 777 777 PHE PHE A . n A 1 743 THR 743 778 778 THR THR A . n A 1 744 GLN 744 779 779 GLN GLN A . n A 1 745 PRO 745 780 780 PRO PRO A . n A 1 746 ALA 746 781 781 ALA ALA A . n A 1 747 ASP 747 782 782 ASP ASP A . n A 1 748 LYS 748 783 783 LYS LYS A . n A 1 749 CYS 749 784 784 CYS CYS A . n A 1 750 ASP 750 785 785 ASP ASP A . n A 1 751 GLY 751 786 786 GLY GLY A . n A 1 752 PRO 752 787 787 PRO PRO A . n A 1 753 LEU 753 788 788 LEU LEU A . n A 1 754 SER 754 789 789 SER SER A . n A 1 755 VAL 755 790 790 VAL VAL A . n A 1 756 SER 756 791 791 SER SER A . n A 1 757 SER 757 792 792 SER SER A . n A 1 758 PHE 758 793 793 PHE PHE A . n A 1 759 ILE 759 794 794 ILE ILE A . n A 1 760 LEU 760 795 795 LEU LEU A . n A 1 761 PRO 761 796 796 PRO PRO A . n A 1 762 HIS 762 797 797 HIS HIS A . n A 1 763 ARG 763 798 798 ARG ARG A . n A 1 764 PRO 764 799 799 PRO PRO A . n A 1 765 ASP 765 800 800 ASP ASP A . n A 1 766 ASN 766 801 801 ASN ASN A . n A 1 767 ASP 767 802 802 ASP ASP A . n A 1 768 GLU 768 803 803 GLU GLU A . n A 1 769 SER 769 804 804 SER SER A . n A 1 770 CYS 770 805 805 CYS CYS A . n A 1 771 ALA 771 806 806 ALA ALA A . n A 1 772 SER 772 807 807 SER SER A . n A 1 773 SER 773 808 808 SER SER A . n A 1 774 GLU 774 809 809 GLU GLU A . n A 1 775 ASP 775 810 810 ASP ASP A . n A 1 776 GLU 776 811 811 GLU GLU A . n A 1 777 SER 777 812 812 SER SER A . n A 1 778 LYS 778 813 813 LYS LYS A . n A 1 779 TRP 779 814 814 TRP TRP A . n A 1 780 VAL 780 815 815 VAL VAL A . n A 1 781 GLU 781 816 816 GLU GLU A . n A 1 782 GLU 782 817 817 GLU GLU A . n A 1 783 LEU 783 818 818 LEU LEU A . n A 1 784 MET 784 819 819 MET MET A . n A 1 785 LYS 785 820 820 LYS LYS A . n A 1 786 MET 786 821 821 MET MET A . n A 1 787 HIS 787 822 822 HIS HIS A . n A 1 788 THR 788 823 823 THR THR A . n A 1 789 ALA 789 824 824 ALA ALA A . n A 1 790 ARG 790 825 825 ARG ARG A . n A 1 791 VAL 791 826 826 VAL VAL A . n A 1 792 ARG 792 827 827 ARG ARG A . n A 1 793 ASP 793 828 828 ASP ASP A . n A 1 794 ILE 794 829 829 ILE ILE A . n A 1 795 GLU 795 830 830 GLU GLU A . n A 1 796 HIS 796 831 831 HIS HIS A . n A 1 797 LEU 797 832 832 LEU LEU A . n A 1 798 THR 798 833 833 THR THR A . n A 1 799 GLY 799 834 834 GLY GLY A . n A 1 800 LEU 800 835 835 LEU LEU A . n A 1 801 ASP 801 836 836 ASP ASP A . n A 1 802 PHE 802 837 837 PHE PHE A . n A 1 803 TYR 803 838 838 TYR TYR A . n A 1 804 ARG 804 839 839 ARG ARG A . n A 1 805 LYS 805 840 840 LYS LYS A . n A 1 806 THR 806 841 841 THR THR A . n A 1 807 SER 807 842 842 SER SER A . n A 1 808 ARG 808 843 843 ARG ARG A . n A 1 809 SER 809 844 844 SER SER A . n A 1 810 TYR 810 845 845 TYR TYR A . n A 1 811 SER 811 846 846 SER SER A . n A 1 812 GLU 812 847 847 GLU GLU A . n A 1 813 ILE 813 848 848 ILE ILE A . n A 1 814 LEU 814 849 849 LEU LEU A . n A 1 815 THR 815 850 850 THR THR A . n A 1 816 LEU 816 851 851 LEU LEU A . n A 1 817 LYS 817 852 852 LYS LYS A . n A 1 818 THR 818 853 853 THR THR A . n A 1 819 TYR 819 854 854 TYR TYR A . n A 1 820 LEU 820 855 855 LEU LEU A . n A 1 821 HIS 821 856 856 HIS HIS A . n A 1 822 THR 822 857 857 THR THR A . n A 1 823 TYR 823 858 858 TYR TYR A . n A 1 824 GLU 824 859 859 GLU GLU A . n A 1 825 SER 825 860 860 SER SER A . n A 1 826 GLU 826 861 ? ? ? A . n A 1 827 ILE 827 862 ? ? ? 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 NAG 1 901 1860 NAG NAG A . C 2 NAG 2 902 1861 NAG NAG A . D 3 BMA 3 903 1862 BMA BMA A . E 4 ZN 1 904 1867 ZN ZN A . F 4 ZN 1 905 1868 ZN ZN A . G 5 5JK 1 906 1870 5JK 7OS A . H 6 CA 1 907 1871 CA CA A . I 7 IOD 1 908 1880 IOD IOD A . J 7 IOD 1 909 1881 IOD IOD A . K 7 IOD 1 910 1882 IOD IOD A . L 7 IOD 1 911 1883 IOD IOD A . M 7 IOD 1 912 1884 IOD IOD A . N 7 IOD 1 913 1890 IOD IOD A . O 7 IOD 1 914 1891 IOD IOD A . P 7 IOD 1 915 1892 IOD IOD A . Q 7 IOD 1 916 1893 IOD IOD A . R 7 IOD 1 917 1894 IOD IOD A . S 8 SCN 1 918 1896 SCN SCN A . T 8 SCN 1 919 1897 SCN SCN A . U 8 SCN 1 920 1898 SCN SCN A . V 8 SCN 1 921 1899 SCN SCN A . W 8 SCN 1 922 1900 SCN SCN A . X 8 SCN 1 923 1901 SCN SCN A . Y 8 SCN 1 924 1902 SCN SCN A . Z 8 SCN 1 925 1903 SCN SCN A . AA 8 SCN 1 926 1904 SCN SCN A . BA 8 SCN 1 927 1905 SCN SCN A . CA 9 NA 1 928 1906 NA NA A . DA 9 NA 1 929 1907 NA NA A . EA 10 GOL 1 930 1908 GOL GOL A . FA 10 GOL 1 931 1 GOL GOL A . GA 10 GOL 1 932 2 GOL GOL A . HA 10 GOL 1 933 3 GOL GOL A . IA 10 GOL 1 934 4 GOL GOL A . JA 10 GOL 1 935 5 GOL GOL A . KA 10 GOL 1 936 6 GOL GOL A . LA 8 SCN 1 937 1 SCN SCN A . MA 11 HOH 1 1001 215 HOH HOH A . MA 11 HOH 2 1002 469 HOH HOH A . MA 11 HOH 3 1003 376 HOH HOH A . MA 11 HOH 4 1004 587 HOH HOH A . MA 11 HOH 5 1005 617 HOH HOH A . MA 11 HOH 6 1006 171 HOH HOH A . MA 11 HOH 7 1007 430 HOH HOH A . MA 11 HOH 8 1008 151 HOH HOH A . MA 11 HOH 9 1009 170 HOH HOH A . MA 11 HOH 10 1010 132 HOH HOH A . MA 11 HOH 11 1011 582 HOH HOH A . MA 11 HOH 12 1012 45 HOH HOH A . MA 11 HOH 13 1013 438 HOH HOH A . MA 11 HOH 14 1014 425 HOH HOH A . MA 11 HOH 15 1015 208 HOH HOH A . MA 11 HOH 16 1016 612 HOH HOH A . MA 11 HOH 17 1017 165 HOH HOH A . MA 11 HOH 18 1018 156 HOH HOH A . MA 11 HOH 19 1019 509 HOH HOH A . MA 11 HOH 20 1020 248 HOH HOH A . MA 11 HOH 21 1021 81 HOH HOH A . MA 11 HOH 22 1022 484 HOH HOH A . MA 11 HOH 23 1023 124 HOH HOH A . MA 11 HOH 24 1024 193 HOH HOH A . MA 11 HOH 25 1025 458 HOH HOH A . MA 11 HOH 26 1026 88 HOH HOH A . MA 11 HOH 27 1027 125 HOH HOH A . MA 11 HOH 28 1028 294 HOH HOH A . MA 11 HOH 29 1029 272 HOH HOH A . MA 11 HOH 30 1030 145 HOH HOH A . MA 11 HOH 31 1031 168 HOH HOH A . MA 11 HOH 32 1032 448 HOH HOH A . MA 11 HOH 33 1033 402 HOH HOH A . MA 11 HOH 34 1034 74 HOH HOH A . MA 11 HOH 35 1035 416 HOH HOH A . MA 11 HOH 36 1036 398 HOH HOH A . MA 11 HOH 37 1037 57 HOH HOH A . MA 11 HOH 38 1038 285 HOH HOH A . MA 11 HOH 39 1039 185 HOH HOH A . MA 11 HOH 40 1040 13 HOH HOH A . MA 11 HOH 41 1041 545 HOH HOH A . MA 11 HOH 42 1042 78 HOH HOH A . MA 11 HOH 43 1043 372 HOH HOH A . MA 11 HOH 44 1044 497 HOH HOH A . MA 11 HOH 45 1045 593 HOH HOH A . MA 11 HOH 46 1046 273 HOH HOH A . MA 11 HOH 47 1047 391 HOH HOH A . MA 11 HOH 48 1048 43 HOH HOH A . MA 11 HOH 49 1049 451 HOH HOH A . MA 11 HOH 50 1050 144 HOH HOH A . MA 11 HOH 51 1051 240 HOH HOH A . MA 11 HOH 52 1052 91 HOH HOH A . MA 11 HOH 53 1053 316 HOH HOH A . MA 11 HOH 54 1054 79 HOH HOH A . MA 11 HOH 55 1055 180 HOH HOH A . MA 11 HOH 56 1056 141 HOH HOH A . MA 11 HOH 57 1057 71 HOH HOH A . MA 11 HOH 58 1058 44 HOH HOH A . MA 11 HOH 59 1059 249 HOH HOH A . MA 11 HOH 60 1060 163 HOH HOH A . MA 11 HOH 61 1061 253 HOH HOH A . MA 11 HOH 62 1062 414 HOH HOH A . MA 11 HOH 63 1063 299 HOH HOH A . MA 11 HOH 64 1064 85 HOH HOH A . MA 11 HOH 65 1065 73 HOH HOH A . MA 11 HOH 66 1066 202 HOH HOH A . MA 11 HOH 67 1067 116 HOH HOH A . MA 11 HOH 68 1068 25 HOH HOH A . MA 11 HOH 69 1069 419 HOH HOH A . MA 11 HOH 70 1070 417 HOH HOH A . MA 11 HOH 71 1071 555 HOH HOH A . MA 11 HOH 72 1072 162 HOH HOH A . MA 11 HOH 73 1073 297 HOH HOH A . MA 11 HOH 74 1074 491 HOH HOH A . MA 11 HOH 75 1075 437 HOH HOH A . MA 11 HOH 76 1076 264 HOH HOH A . MA 11 HOH 77 1077 70 HOH HOH A . MA 11 HOH 78 1078 177 HOH HOH A . MA 11 HOH 79 1079 443 HOH HOH A . MA 11 HOH 80 1080 131 HOH HOH A . MA 11 HOH 81 1081 120 HOH HOH A . MA 11 HOH 82 1082 600 HOH HOH A . MA 11 HOH 83 1083 399 HOH HOH A . MA 11 HOH 84 1084 216 HOH HOH A . MA 11 HOH 85 1085 121 HOH HOH A . MA 11 HOH 86 1086 260 HOH HOH A . MA 11 HOH 87 1087 571 HOH HOH A . MA 11 HOH 88 1088 234 HOH HOH A . MA 11 HOH 89 1089 30 HOH HOH A . MA 11 HOH 90 1090 390 HOH HOH A . MA 11 HOH 91 1091 241 HOH HOH A . MA 11 HOH 92 1092 160 HOH HOH A . MA 11 HOH 93 1093 36 HOH HOH A . MA 11 HOH 94 1094 48 HOH HOH A . MA 11 HOH 95 1095 246 HOH HOH A . MA 11 HOH 96 1096 266 HOH HOH A . MA 11 HOH 97 1097 616 HOH HOH A . MA 11 HOH 98 1098 608 HOH HOH A . MA 11 HOH 99 1099 601 HOH HOH A . MA 11 HOH 100 1100 432 HOH HOH A . MA 11 HOH 101 1101 210 HOH HOH A . MA 11 HOH 102 1102 578 HOH HOH A . MA 11 HOH 103 1103 35 HOH HOH A . MA 11 HOH 104 1104 128 HOH HOH A . MA 11 HOH 105 1105 420 HOH HOH A . MA 11 HOH 106 1106 222 HOH HOH A . MA 11 HOH 107 1107 167 HOH HOH A . MA 11 HOH 108 1108 2 HOH HOH A . MA 11 HOH 109 1109 54 HOH HOH A . MA 11 HOH 110 1110 498 HOH HOH A . MA 11 HOH 111 1111 481 HOH HOH A . MA 11 HOH 112 1112 383 HOH HOH A . MA 11 HOH 113 1113 67 HOH HOH A . MA 11 HOH 114 1114 450 HOH HOH A . MA 11 HOH 115 1115 581 HOH HOH A . MA 11 HOH 116 1116 56 HOH HOH A . MA 11 HOH 117 1117 147 HOH HOH A . MA 11 HOH 118 1118 370 HOH HOH A . MA 11 HOH 119 1119 395 HOH HOH A . MA 11 HOH 120 1120 394 HOH HOH A . MA 11 HOH 121 1121 477 HOH HOH A . MA 11 HOH 122 1122 304 HOH HOH A . MA 11 HOH 123 1123 327 HOH HOH A . MA 11 HOH 124 1124 133 HOH HOH A . MA 11 HOH 125 1125 490 HOH HOH A . MA 11 HOH 126 1126 602 HOH HOH A . MA 11 HOH 127 1127 113 HOH HOH A . MA 11 HOH 128 1128 22 HOH HOH A . MA 11 HOH 129 1129 75 HOH HOH A . MA 11 HOH 130 1130 86 HOH HOH A . MA 11 HOH 131 1131 358 HOH HOH A . MA 11 HOH 132 1132 28 HOH HOH A . MA 11 HOH 133 1133 325 HOH HOH A . MA 11 HOH 134 1134 126 HOH HOH A . MA 11 HOH 135 1135 377 HOH HOH A . MA 11 HOH 136 1136 192 HOH HOH A . MA 11 HOH 137 1137 308 HOH HOH A . MA 11 HOH 138 1138 284 HOH HOH A . MA 11 HOH 139 1139 66 HOH HOH A . MA 11 HOH 140 1140 382 HOH HOH A . MA 11 HOH 141 1141 368 HOH HOH A . MA 11 HOH 142 1142 413 HOH HOH A . MA 11 HOH 143 1143 404 HOH HOH A . MA 11 HOH 144 1144 142 HOH HOH A . MA 11 HOH 145 1145 118 HOH HOH A . MA 11 HOH 146 1146 609 HOH HOH A . MA 11 HOH 147 1147 11 HOH HOH A . MA 11 HOH 148 1148 257 HOH HOH A . MA 11 HOH 149 1149 92 HOH HOH A . MA 11 HOH 150 1150 10 HOH HOH A . MA 11 HOH 151 1151 173 HOH HOH A . MA 11 HOH 152 1152 301 HOH HOH A . MA 11 HOH 153 1153 82 HOH HOH A . MA 11 HOH 154 1154 14 HOH HOH A . MA 11 HOH 155 1155 548 HOH HOH A . MA 11 HOH 156 1156 283 HOH HOH A . MA 11 HOH 157 1157 183 HOH HOH A . MA 11 HOH 158 1158 295 HOH HOH A . MA 11 HOH 159 1159 42 HOH HOH A . MA 11 HOH 160 1160 211 HOH HOH A . MA 11 HOH 161 1161 526 HOH HOH A . MA 11 HOH 162 1162 409 HOH HOH A . MA 11 HOH 163 1163 302 HOH HOH A . MA 11 HOH 164 1164 137 HOH HOH A . MA 11 HOH 165 1165 17 HOH HOH A . MA 11 HOH 166 1166 117 HOH HOH A . MA 11 HOH 167 1167 411 HOH HOH A . MA 11 HOH 168 1168 225 HOH HOH A . MA 11 HOH 169 1169 328 HOH HOH A . MA 11 HOH 170 1170 396 HOH HOH A . MA 11 HOH 171 1171 265 HOH HOH A . MA 11 HOH 172 1172 119 HOH HOH A . MA 11 HOH 173 1173 212 HOH HOH A . MA 11 HOH 174 1174 584 HOH HOH A . MA 11 HOH 175 1175 76 HOH HOH A . MA 11 HOH 176 1176 279 HOH HOH A . MA 11 HOH 177 1177 1 HOH HOH A . MA 11 HOH 178 1178 41 HOH HOH A . MA 11 HOH 179 1179 314 HOH HOH A . MA 11 HOH 180 1180 98 HOH HOH A . MA 11 HOH 181 1181 65 HOH HOH A . MA 11 HOH 182 1182 26 HOH HOH A . MA 11 HOH 183 1183 52 HOH HOH A . MA 11 HOH 184 1184 140 HOH HOH A . MA 11 HOH 185 1185 271 HOH HOH A . MA 11 HOH 186 1186 379 HOH HOH A . MA 11 HOH 187 1187 61 HOH HOH A . MA 11 HOH 188 1188 112 HOH HOH A . MA 11 HOH 189 1189 103 HOH HOH A . MA 11 HOH 190 1190 401 HOH HOH A . MA 11 HOH 191 1191 233 HOH HOH A . MA 11 HOH 192 1192 499 HOH HOH A . MA 11 HOH 193 1193 412 HOH HOH A . MA 11 HOH 194 1194 259 HOH HOH A . MA 11 HOH 195 1195 369 HOH HOH A . MA 11 HOH 196 1196 64 HOH HOH A . MA 11 HOH 197 1197 161 HOH HOH A . MA 11 HOH 198 1198 153 HOH HOH A . MA 11 HOH 199 1199 7 HOH HOH A . MA 11 HOH 200 1200 181 HOH HOH A . MA 11 HOH 201 1201 247 HOH HOH A . MA 11 HOH 202 1202 166 HOH HOH A . MA 11 HOH 203 1203 33 HOH HOH A . MA 11 HOH 204 1204 38 HOH HOH A . MA 11 HOH 205 1205 18 HOH HOH A . MA 11 HOH 206 1206 80 HOH HOH A . MA 11 HOH 207 1207 258 HOH HOH A . MA 11 HOH 208 1208 15 HOH HOH A . MA 11 HOH 209 1209 55 HOH HOH A . MA 11 HOH 210 1210 397 HOH HOH A . MA 11 HOH 211 1211 341 HOH HOH A . MA 11 HOH 212 1212 200 HOH HOH A . MA 11 HOH 213 1213 6 HOH HOH A . MA 11 HOH 214 1214 599 HOH HOH A . MA 11 HOH 215 1215 96 HOH HOH A . MA 11 HOH 216 1216 596 HOH HOH A . MA 11 HOH 217 1217 313 HOH HOH A . MA 11 HOH 218 1218 53 HOH HOH A . MA 11 HOH 219 1219 320 HOH HOH A . MA 11 HOH 220 1220 157 HOH HOH A . MA 11 HOH 221 1221 37 HOH HOH A . MA 11 HOH 222 1222 143 HOH HOH A . MA 11 HOH 223 1223 139 HOH HOH A . MA 11 HOH 224 1224 27 HOH HOH A . MA 11 HOH 225 1225 114 HOH HOH A . MA 11 HOH 226 1226 371 HOH HOH A . MA 11 HOH 227 1227 100 HOH HOH A . MA 11 HOH 228 1228 315 HOH HOH A . MA 11 HOH 229 1229 204 HOH HOH A . MA 11 HOH 230 1230 84 HOH HOH A . MA 11 HOH 231 1231 23 HOH HOH A . MA 11 HOH 232 1232 288 HOH HOH A . MA 11 HOH 233 1233 178 HOH HOH A . MA 11 HOH 234 1234 174 HOH HOH A . MA 11 HOH 235 1235 237 HOH HOH A . MA 11 HOH 236 1236 378 HOH HOH A . MA 11 HOH 237 1237 449 HOH HOH A . MA 11 HOH 238 1238 330 HOH HOH A . MA 11 HOH 239 1239 290 HOH HOH A . MA 11 HOH 240 1240 380 HOH HOH A . MA 11 HOH 241 1241 130 HOH HOH A . MA 11 HOH 242 1242 21 HOH HOH A . MA 11 HOH 243 1243 217 HOH HOH A . MA 11 HOH 244 1244 150 HOH HOH A . MA 11 HOH 245 1245 152 HOH HOH A . MA 11 HOH 246 1246 252 HOH HOH A . MA 11 HOH 247 1247 109 HOH HOH A . MA 11 HOH 248 1248 51 HOH HOH A . MA 11 HOH 249 1249 190 HOH HOH A . MA 11 HOH 250 1250 58 HOH HOH A . MA 11 HOH 251 1251 251 HOH HOH A . MA 11 HOH 252 1252 410 HOH HOH A . MA 11 HOH 253 1253 20 HOH HOH A . MA 11 HOH 254 1254 528 HOH HOH A . MA 11 HOH 255 1255 172 HOH HOH A . MA 11 HOH 256 1256 606 HOH HOH A . MA 11 HOH 257 1257 428 HOH HOH A . MA 11 HOH 258 1258 72 HOH HOH A . MA 11 HOH 259 1259 529 HOH HOH A . MA 11 HOH 260 1260 99 HOH HOH A . MA 11 HOH 261 1261 186 HOH HOH A . MA 11 HOH 262 1262 385 HOH HOH A . MA 11 HOH 263 1263 367 HOH HOH A . MA 11 HOH 264 1264 366 HOH HOH A . MA 11 HOH 265 1265 176 HOH HOH A . MA 11 HOH 266 1266 29 HOH HOH A . MA 11 HOH 267 1267 40 HOH HOH A . MA 11 HOH 268 1268 373 HOH HOH A . MA 11 HOH 269 1269 460 HOH HOH A . MA 11 HOH 270 1270 154 HOH HOH A . MA 11 HOH 271 1271 381 HOH HOH A . MA 11 HOH 272 1272 291 HOH HOH A . MA 11 HOH 273 1273 562 HOH HOH A . MA 11 HOH 274 1274 514 HOH HOH A . MA 11 HOH 275 1275 134 HOH HOH A . MA 11 HOH 276 1276 4 HOH HOH A . MA 11 HOH 277 1277 277 HOH HOH A . MA 11 HOH 278 1278 256 HOH HOH A . MA 11 HOH 279 1279 611 HOH HOH A . MA 11 HOH 280 1280 270 HOH HOH A . MA 11 HOH 281 1281 60 HOH HOH A . MA 11 HOH 282 1282 199 HOH HOH A . MA 11 HOH 283 1283 47 HOH HOH A . MA 11 HOH 284 1284 434 HOH HOH A . MA 11 HOH 285 1285 19 HOH HOH A . MA 11 HOH 286 1286 87 HOH HOH A . MA 11 HOH 287 1287 403 HOH HOH A . MA 11 HOH 288 1288 422 HOH HOH A . MA 11 HOH 289 1289 311 HOH HOH A . MA 11 HOH 290 1290 108 HOH HOH A . MA 11 HOH 291 1291 221 HOH HOH A . MA 11 HOH 292 1292 329 HOH HOH A . MA 11 HOH 293 1293 123 HOH HOH A . MA 11 HOH 294 1294 148 HOH HOH A . MA 11 HOH 295 1295 106 HOH HOH A . MA 11 HOH 296 1296 104 HOH HOH A . MA 11 HOH 297 1297 188 HOH HOH A . MA 11 HOH 298 1298 175 HOH HOH A . MA 11 HOH 299 1299 34 HOH HOH A . MA 11 HOH 300 1300 146 HOH HOH A . MA 11 HOH 301 1301 326 HOH HOH A . MA 11 HOH 302 1302 393 HOH HOH A . MA 11 HOH 303 1303 557 HOH HOH A . MA 11 HOH 304 1304 387 HOH HOH A . MA 11 HOH 305 1305 452 HOH HOH A . MA 11 HOH 306 1306 3 HOH HOH A . MA 11 HOH 307 1307 613 HOH HOH A . MA 11 HOH 308 1308 213 HOH HOH A . MA 11 HOH 309 1309 59 HOH HOH A . MA 11 HOH 310 1310 101 HOH HOH A . MA 11 HOH 311 1311 209 HOH HOH A . MA 11 HOH 312 1312 107 HOH HOH A . MA 11 HOH 313 1313 235 HOH HOH A . MA 11 HOH 314 1314 115 HOH HOH A . MA 11 HOH 315 1315 431 HOH HOH A . MA 11 HOH 316 1316 189 HOH HOH A . MA 11 HOH 317 1317 49 HOH HOH A . MA 11 HOH 318 1318 195 HOH HOH A . MA 11 HOH 319 1319 473 HOH HOH A . MA 11 HOH 320 1320 127 HOH HOH A . MA 11 HOH 321 1321 39 HOH HOH A . MA 11 HOH 322 1322 400 HOH HOH A . MA 11 HOH 323 1323 110 HOH HOH A . MA 11 HOH 324 1324 468 HOH HOH A . MA 11 HOH 325 1325 223 HOH HOH A . MA 11 HOH 326 1326 242 HOH HOH A . MA 11 HOH 327 1327 218 HOH HOH A . MA 11 HOH 328 1328 254 HOH HOH A . MA 11 HOH 329 1329 442 HOH HOH A . MA 11 HOH 330 1330 550 HOH HOH A . MA 11 HOH 331 1331 89 HOH HOH A . MA 11 HOH 332 1332 194 HOH HOH A . MA 11 HOH 333 1333 228 HOH HOH A . MA 11 HOH 334 1334 207 HOH HOH A . MA 11 HOH 335 1335 268 HOH HOH A . MA 11 HOH 336 1336 232 HOH HOH A . MA 11 HOH 337 1337 446 HOH HOH A . MA 11 HOH 338 1338 441 HOH HOH A . MA 11 HOH 339 1339 589 HOH HOH A . MA 11 HOH 340 1340 90 HOH HOH A . MA 11 HOH 341 1341 182 HOH HOH A . MA 11 HOH 342 1342 406 HOH HOH A . MA 11 HOH 343 1343 129 HOH HOH A . MA 11 HOH 344 1344 336 HOH HOH A . MA 11 HOH 345 1345 286 HOH HOH A . MA 11 HOH 346 1346 407 HOH HOH A . MA 11 HOH 347 1347 319 HOH HOH A . MA 11 HOH 348 1348 342 HOH HOH A . MA 11 HOH 349 1349 50 HOH HOH A . MA 11 HOH 350 1350 312 HOH HOH A . MA 11 HOH 351 1351 184 HOH HOH A . MA 11 HOH 352 1352 16 HOH HOH A . MA 11 HOH 353 1353 485 HOH HOH A . MA 11 HOH 354 1354 179 HOH HOH A . MA 11 HOH 355 1355 474 HOH HOH A . MA 11 HOH 356 1356 346 HOH HOH A . MA 11 HOH 357 1357 374 HOH HOH A . MA 11 HOH 358 1358 415 HOH HOH A . MA 11 HOH 359 1359 158 HOH HOH A . MA 11 HOH 360 1360 386 HOH HOH A . MA 11 HOH 361 1361 9 HOH HOH A . MA 11 HOH 362 1362 122 HOH HOH A . MA 11 HOH 363 1363 365 HOH HOH A . MA 11 HOH 364 1364 454 HOH HOH A . MA 11 HOH 365 1365 478 HOH HOH A . MA 11 HOH 366 1366 219 HOH HOH A . MA 11 HOH 367 1367 570 HOH HOH A . MA 11 HOH 368 1368 472 HOH HOH A . MA 11 HOH 369 1369 97 HOH HOH A . MA 11 HOH 370 1370 32 HOH HOH A . MA 11 HOH 371 1371 603 HOH HOH A . MA 11 HOH 372 1372 155 HOH HOH A . MA 11 HOH 373 1373 281 HOH HOH A . MA 11 HOH 374 1374 580 HOH HOH A . MA 11 HOH 375 1375 243 HOH HOH A . MA 11 HOH 376 1376 280 HOH HOH A . MA 11 HOH 377 1377 536 HOH HOH A . MA 11 HOH 378 1378 69 HOH HOH A . MA 11 HOH 379 1379 94 HOH HOH A . MA 11 HOH 380 1380 63 HOH HOH A . MA 11 HOH 381 1381 196 HOH HOH A . MA 11 HOH 382 1382 551 HOH HOH A . MA 11 HOH 383 1383 306 HOH HOH A . MA 11 HOH 384 1384 334 HOH HOH A . MA 11 HOH 385 1385 83 HOH HOH A . MA 11 HOH 386 1386 164 HOH HOH A . MA 11 HOH 387 1387 588 HOH HOH A . MA 11 HOH 388 1388 335 HOH HOH A . MA 11 HOH 389 1389 480 HOH HOH A . MA 11 HOH 390 1390 24 HOH HOH A . MA 11 HOH 391 1391 392 HOH HOH A . MA 11 HOH 392 1392 549 HOH HOH A . MA 11 HOH 393 1393 421 HOH HOH A . MA 11 HOH 394 1394 93 HOH HOH A . MA 11 HOH 395 1395 198 HOH HOH A . MA 11 HOH 396 1396 305 HOH HOH A . MA 11 HOH 397 1397 287 HOH HOH A . MA 11 HOH 398 1398 344 HOH HOH A . MA 11 HOH 399 1399 435 HOH HOH A . MA 11 HOH 400 1400 201 HOH HOH A . MA 11 HOH 401 1401 62 HOH HOH A . MA 11 HOH 402 1402 95 HOH HOH A . MA 11 HOH 403 1403 559 HOH HOH A . MA 11 HOH 404 1404 263 HOH HOH A . MA 11 HOH 405 1405 149 HOH HOH A . MA 11 HOH 406 1406 206 HOH HOH A . MA 11 HOH 407 1407 423 HOH HOH A . MA 11 HOH 408 1408 384 HOH HOH A . MA 11 HOH 409 1409 405 HOH HOH A . MA 11 HOH 410 1410 592 HOH HOH A . MA 11 HOH 411 1411 607 HOH HOH A . MA 11 HOH 412 1412 352 HOH HOH A . MA 11 HOH 413 1413 447 HOH HOH A . MA 11 HOH 414 1414 250 HOH HOH A . MA 11 HOH 415 1415 362 HOH HOH A . MA 11 HOH 416 1416 453 HOH HOH A . MA 11 HOH 417 1417 340 HOH HOH A . MA 11 HOH 418 1418 267 HOH HOH A . MA 11 HOH 419 1419 553 HOH HOH A . MA 11 HOH 420 1420 439 HOH HOH A . MA 11 HOH 421 1421 427 HOH HOH A . MA 11 HOH 422 1422 546 HOH HOH A . MA 11 HOH 423 1423 590 HOH HOH A . MA 11 HOH 424 1424 512 HOH HOH A . MA 11 HOH 425 1425 220 HOH HOH A . MA 11 HOH 426 1426 245 HOH HOH A . MA 11 HOH 427 1427 318 HOH HOH A . MA 11 HOH 428 1428 12 HOH HOH A . MA 11 HOH 429 1429 566 HOH HOH A . MA 11 HOH 430 1430 236 HOH HOH A . MA 11 HOH 431 1431 389 HOH HOH A . MA 11 HOH 432 1432 552 HOH HOH A . MA 11 HOH 433 1433 338 HOH HOH A . MA 11 HOH 434 1434 521 HOH HOH A . MA 11 HOH 435 1435 461 HOH HOH A . MA 11 HOH 436 1436 135 HOH HOH A . MA 11 HOH 437 1437 489 HOH HOH A . MA 11 HOH 438 1438 77 HOH HOH A . MA 11 HOH 439 1439 594 HOH HOH A . MA 11 HOH 440 1440 463 HOH HOH A . MA 11 HOH 441 1441 440 HOH HOH A . MA 11 HOH 442 1442 445 HOH HOH A . MA 11 HOH 443 1443 111 HOH HOH A . MA 11 HOH 444 1444 323 HOH HOH A . MA 11 HOH 445 1445 214 HOH HOH A . MA 11 HOH 446 1446 275 HOH HOH A . MA 11 HOH 447 1447 510 HOH HOH A . MA 11 HOH 448 1448 534 HOH HOH A . MA 11 HOH 449 1449 466 HOH HOH A . MA 11 HOH 450 1450 5 HOH HOH A . MA 11 HOH 451 1451 500 HOH HOH A . MA 11 HOH 452 1452 525 HOH HOH A . MA 11 HOH 453 1453 354 HOH HOH A . MA 11 HOH 454 1454 597 HOH HOH A . MA 11 HOH 455 1455 274 HOH HOH A . MA 11 HOH 456 1456 187 HOH HOH A . MA 11 HOH 457 1457 586 HOH HOH A . MA 11 HOH 458 1458 506 HOH HOH A . MA 11 HOH 459 1459 102 HOH HOH A . MA 11 HOH 460 1460 278 HOH HOH A . MA 11 HOH 461 1461 519 HOH HOH A . MA 11 HOH 462 1462 501 HOH HOH A . MA 11 HOH 463 1463 464 HOH HOH A . MA 11 HOH 464 1464 560 HOH HOH A . MA 11 HOH 465 1465 614 HOH HOH A . MA 11 HOH 466 1466 293 HOH HOH A . MA 11 HOH 467 1467 518 HOH HOH A . MA 11 HOH 468 1468 105 HOH HOH A . MA 11 HOH 469 1469 197 HOH HOH A . MA 11 HOH 470 1470 363 HOH HOH A . MA 11 HOH 471 1471 357 HOH HOH A . MA 11 HOH 472 1472 569 HOH HOH A . MA 11 HOH 473 1473 339 HOH HOH A . MA 11 HOH 474 1474 517 HOH HOH A . MA 11 HOH 475 1475 244 HOH HOH A . MA 11 HOH 476 1476 604 HOH HOH A . MA 11 HOH 477 1477 205 HOH HOH A . MA 11 HOH 478 1478 444 HOH HOH A . MA 11 HOH 479 1479 224 HOH HOH A . MA 11 HOH 480 1480 349 HOH HOH A . MA 11 HOH 481 1481 493 HOH HOH A . MA 11 HOH 482 1482 523 HOH HOH A . MA 11 HOH 483 1483 475 HOH HOH A . MA 11 HOH 484 1484 610 HOH HOH A . MA 11 HOH 485 1485 576 HOH HOH A . MA 11 HOH 486 1486 351 HOH HOH A . MA 11 HOH 487 1487 436 HOH HOH A . MA 11 HOH 488 1488 317 HOH HOH A . MA 11 HOH 489 1489 136 HOH HOH A . MA 11 HOH 490 1490 513 HOH HOH A . MA 11 HOH 491 1491 563 HOH HOH A . MA 11 HOH 492 1492 345 HOH HOH A . MA 11 HOH 493 1493 138 HOH HOH A . MA 11 HOH 494 1494 605 HOH HOH A . MA 11 HOH 495 1495 350 HOH HOH A . MA 11 HOH 496 1496 269 HOH HOH A . MA 11 HOH 497 1497 337 HOH HOH A . MA 11 HOH 498 1498 429 HOH HOH A . MA 11 HOH 499 1499 303 HOH HOH A . MA 11 HOH 500 1500 255 HOH HOH A . MA 11 HOH 501 1501 556 HOH HOH A . MA 11 HOH 502 1502 355 HOH HOH A . MA 11 HOH 503 1503 364 HOH HOH A . MA 11 HOH 504 1504 591 HOH HOH A . MA 11 HOH 505 1505 333 HOH HOH A . MA 11 HOH 506 1506 595 HOH HOH A . MA 11 HOH 507 1507 324 HOH HOH A . MA 11 HOH 508 1508 558 HOH HOH A . MA 11 HOH 509 1509 226 HOH HOH A . MA 11 HOH 510 1510 508 HOH HOH A . MA 11 HOH 511 1511 359 HOH HOH A . MA 11 HOH 512 1512 492 HOH HOH A . MA 11 HOH 513 1513 348 HOH HOH A . MA 11 HOH 514 1514 539 HOH HOH A . MA 11 HOH 515 1515 356 HOH HOH A . MA 11 HOH 516 1516 169 HOH HOH A . MA 11 HOH 517 1517 361 HOH HOH A . MA 11 HOH 518 1518 522 HOH HOH A . MA 11 HOH 519 1519 418 HOH HOH A . MA 11 HOH 520 1520 598 HOH HOH A . MA 11 HOH 521 1521 615 HOH HOH A . MA 11 HOH 522 1522 507 HOH HOH A . MA 11 HOH 523 1523 456 HOH HOH A . MA 11 HOH 524 1524 331 HOH HOH A . MA 11 HOH 525 1525 585 HOH HOH A . MA 11 HOH 526 1526 347 HOH HOH A . # _pdbx_struct_mod_residue.id 1 _pdbx_struct_mod_residue.label_asym_id A _pdbx_struct_mod_residue.label_comp_id TPO _pdbx_struct_mod_residue.label_seq_id 174 _pdbx_struct_mod_residue.auth_asym_id A _pdbx_struct_mod_residue.auth_comp_id TPO _pdbx_struct_mod_residue.auth_seq_id 209 _pdbx_struct_mod_residue.PDB_ins_code ? _pdbx_struct_mod_residue.parent_comp_id THR _pdbx_struct_mod_residue.details 'modified residue' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details monomeric _pdbx_struct_assembly.oligomeric_count 1 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA,EA,FA,GA,HA,IA,JA,KA,LA,MA # 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)' 6710 ? 1 MORE -98 ? 1 'SSA (A^2)' 32980 ? # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 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 OD1 ? A ASP 136 ? A ASP 171 ? 1_555 ZN ? F ZN . ? A ZN 905 ? 1_555 OG1 ? A TPO 174 ? A TPO 209 ? 1_555 128.2 ? 2 OD1 ? A ASP 136 ? A ASP 171 ? 1_555 ZN ? F ZN . ? A ZN 905 ? 1_555 O1P ? A TPO 174 ? A TPO 209 ? 1_555 89.8 ? 3 OG1 ? A TPO 174 ? A TPO 209 ? 1_555 ZN ? F ZN . ? A ZN 905 ? 1_555 O1P ? A TPO 174 ? A TPO 209 ? 1_555 63.1 ? 4 OD1 ? A ASP 136 ? A ASP 171 ? 1_555 ZN ? F ZN . ? A ZN 905 ? 1_555 OD2 ? A ASP 323 ? A ASP 358 ? 1_555 101.4 ? 5 OG1 ? A TPO 174 ? A TPO 209 ? 1_555 ZN ? F ZN . ? A ZN 905 ? 1_555 OD2 ? A ASP 323 ? A ASP 358 ? 1_555 98.0 ? 6 O1P ? A TPO 174 ? A TPO 209 ? 1_555 ZN ? F ZN . ? A ZN 905 ? 1_555 OD2 ? A ASP 323 ? A ASP 358 ? 1_555 161.0 ? 7 OD1 ? A ASP 136 ? A ASP 171 ? 1_555 ZN ? F ZN . ? A ZN 905 ? 1_555 NE2 ? A HIS 324 ? A HIS 359 ? 1_555 108.3 ? 8 OG1 ? A TPO 174 ? A TPO 209 ? 1_555 ZN ? F ZN . ? A ZN 905 ? 1_555 NE2 ? A HIS 324 ? A HIS 359 ? 1_555 116.6 ? 9 O1P ? A TPO 174 ? A TPO 209 ? 1_555 ZN ? F ZN . ? A ZN 905 ? 1_555 NE2 ? A HIS 324 ? A HIS 359 ? 1_555 94.7 ? 10 OD2 ? A ASP 323 ? A ASP 358 ? 1_555 ZN ? F ZN . ? A ZN 905 ? 1_555 NE2 ? A HIS 324 ? A HIS 359 ? 1_555 96.2 ? 11 O1P ? A TPO 174 ? A TPO 209 ? 1_555 ZN ? E ZN . ? A ZN 904 ? 1_555 OD1 ? A ASP 276 ? A ASP 311 ? 1_555 87.3 ? 12 O1P ? A TPO 174 ? A TPO 209 ? 1_555 ZN ? E ZN . ? A ZN 904 ? 1_555 OD2 ? A ASP 276 ? A ASP 311 ? 1_555 74.0 ? 13 OD1 ? A ASP 276 ? A ASP 311 ? 1_555 ZN ? E ZN . ? A ZN 904 ? 1_555 OD2 ? A ASP 276 ? A ASP 311 ? 1_555 53.1 ? 14 O1P ? A TPO 174 ? A TPO 209 ? 1_555 ZN ? E ZN . ? A ZN 904 ? 1_555 NE2 ? A HIS 280 ? A HIS 315 ? 1_555 165.3 ? 15 OD1 ? A ASP 276 ? A ASP 311 ? 1_555 ZN ? E ZN . ? A ZN 904 ? 1_555 NE2 ? A HIS 280 ? A HIS 315 ? 1_555 95.3 ? 16 OD2 ? A ASP 276 ? A ASP 311 ? 1_555 ZN ? E ZN . ? A ZN 904 ? 1_555 NE2 ? A HIS 280 ? A HIS 315 ? 1_555 96.0 ? 17 O1P ? A TPO 174 ? A TPO 209 ? 1_555 ZN ? E ZN . ? A ZN 904 ? 1_555 NE2 ? A HIS 439 ? A HIS 474 ? 1_555 91.1 ? 18 OD1 ? A ASP 276 ? A ASP 311 ? 1_555 ZN ? E ZN . ? A ZN 904 ? 1_555 NE2 ? A HIS 439 ? A HIS 474 ? 1_555 84.0 ? 19 OD2 ? A ASP 276 ? A ASP 311 ? 1_555 ZN ? E ZN . ? A ZN 904 ? 1_555 NE2 ? A HIS 439 ? A HIS 474 ? 1_555 134.4 ? 20 NE2 ? A HIS 280 ? A HIS 315 ? 1_555 ZN ? E ZN . ? A ZN 904 ? 1_555 NE2 ? A HIS 439 ? A HIS 474 ? 1_555 103.5 ? 21 O1P ? A TPO 174 ? A TPO 209 ? 1_555 ZN ? E ZN . ? A ZN 904 ? 1_555 O ? MA HOH . ? A HOH 1236 ? 1_555 74.8 ? 22 OD1 ? A ASP 276 ? A ASP 311 ? 1_555 ZN ? E ZN . ? A ZN 904 ? 1_555 O ? MA HOH . ? A HOH 1236 ? 1_555 147.4 ? 23 OD2 ? A ASP 276 ? A ASP 311 ? 1_555 ZN ? E ZN . ? A ZN 904 ? 1_555 O ? MA HOH . ? A HOH 1236 ? 1_555 95.3 ? 24 NE2 ? A HIS 280 ? A HIS 315 ? 1_555 ZN ? E ZN . ? A ZN 904 ? 1_555 O ? MA HOH . ? A HOH 1236 ? 1_555 95.9 ? 25 NE2 ? A HIS 439 ? A HIS 474 ? 1_555 ZN ? E ZN . ? A ZN 904 ? 1_555 O ? MA HOH . ? A HOH 1236 ? 1_555 122.6 ? 26 O ? A TYR 634 ? A TYR 669 ? 1_555 NA ? CA NA . ? A NA 928 ? 1_555 O ? A ASP 637 ? A ASP 672 ? 1_555 80.0 ? 27 O ? A TYR 634 ? A TYR 669 ? 1_555 NA ? CA NA . ? A NA 928 ? 1_555 O ? A MET 640 ? A MET 675 ? 1_555 106.7 ? 28 O ? A ASP 637 ? A ASP 672 ? 1_555 NA ? CA NA . ? A NA 928 ? 1_555 O ? A MET 640 ? A MET 675 ? 1_555 91.3 ? 29 O ? A TYR 634 ? A TYR 669 ? 1_555 NA ? CA NA . ? A NA 928 ? 1_555 O2 ? FA GOL . ? A GOL 931 ? 1_555 78.9 ? 30 O ? A ASP 637 ? A ASP 672 ? 1_555 NA ? CA NA . ? A NA 928 ? 1_555 O2 ? FA GOL . ? A GOL 931 ? 1_555 154.8 ? 31 O ? A MET 640 ? A MET 675 ? 1_555 NA ? CA NA . ? A NA 928 ? 1_555 O2 ? FA GOL . ? A GOL 931 ? 1_555 81.9 ? 32 O ? A TYR 634 ? A TYR 669 ? 1_555 NA ? CA NA . ? A NA 928 ? 1_555 O ? MA HOH . ? A HOH 1357 ? 1_555 80.1 ? 33 O ? A ASP 637 ? A ASP 672 ? 1_555 NA ? CA NA . ? A NA 928 ? 1_555 O ? MA HOH . ? A HOH 1357 ? 1_555 89.4 ? 34 O ? A MET 640 ? A MET 675 ? 1_555 NA ? CA NA . ? A NA 928 ? 1_555 O ? MA HOH . ? A HOH 1357 ? 1_555 173.2 ? 35 O2 ? FA GOL . ? A GOL 931 ? 1_555 NA ? CA NA . ? A NA 928 ? 1_555 O ? MA HOH . ? A HOH 1357 ? 1_555 100.2 ? 36 O ? A TYR 634 ? A TYR 669 ? 1_555 NA ? CA NA . ? A NA 928 ? 1_555 O ? MA HOH . ? A HOH 1414 ? 1_555 178.6 ? 37 O ? A ASP 637 ? A ASP 672 ? 1_555 NA ? CA NA . ? A NA 928 ? 1_555 O ? MA HOH . ? A HOH 1414 ? 1_555 100.4 ? 38 O ? A MET 640 ? A MET 675 ? 1_555 NA ? CA NA . ? A NA 928 ? 1_555 O ? MA HOH . ? A HOH 1414 ? 1_555 74.6 ? 39 O2 ? FA GOL . ? A GOL 931 ? 1_555 NA ? CA NA . ? A NA 928 ? 1_555 O ? MA HOH . ? A HOH 1414 ? 1_555 101.1 ? 40 O ? MA HOH . ? A HOH 1357 ? 1_555 NA ? CA NA . ? A NA 928 ? 1_555 O ? MA HOH . ? A HOH 1414 ? 1_555 98.6 ? 41 OD1 ? A ASP 704 ? A ASP 739 ? 1_555 CA ? H CA . ? A CA 907 ? 1_555 OD1 ? A ASN 706 ? A ASN 741 ? 1_555 82.7 ? 42 OD1 ? A ASP 704 ? A ASP 739 ? 1_555 CA ? H CA . ? A CA 907 ? 1_555 OD1 ? A ASP 708 ? A ASP 743 ? 1_555 79.3 ? 43 OD1 ? A ASN 706 ? A ASN 741 ? 1_555 CA ? H CA . ? A CA 907 ? 1_555 OD1 ? A ASP 708 ? A ASP 743 ? 1_555 84.5 ? 44 OD1 ? A ASP 704 ? A ASP 739 ? 1_555 CA ? H CA . ? A CA 907 ? 1_555 O ? A LEU 710 ? A LEU 745 ? 1_555 90.7 ? 45 OD1 ? A ASN 706 ? A ASN 741 ? 1_555 CA ? H CA . ? A CA 907 ? 1_555 O ? A LEU 710 ? A LEU 745 ? 1_555 167.9 ? 46 OD1 ? A ASP 708 ? A ASP 743 ? 1_555 CA ? H CA . ? A CA 907 ? 1_555 O ? A LEU 710 ? A LEU 745 ? 1_555 84.3 ? 47 OD1 ? A ASP 704 ? A ASP 739 ? 1_555 CA ? H CA . ? A CA 907 ? 1_555 OD1 ? A ASP 712 ? A ASP 747 ? 1_555 100.7 ? 48 OD1 ? A ASN 706 ? A ASN 741 ? 1_555 CA ? H CA . ? A CA 907 ? 1_555 OD1 ? A ASP 712 ? A ASP 747 ? 1_555 87.2 ? 49 OD1 ? A ASP 708 ? A ASP 743 ? 1_555 CA ? H CA . ? A CA 907 ? 1_555 OD1 ? A ASP 712 ? A ASP 747 ? 1_555 171.6 ? 50 O ? A LEU 710 ? A LEU 745 ? 1_555 CA ? H CA . ? A CA 907 ? 1_555 OD1 ? A ASP 712 ? A ASP 747 ? 1_555 104.1 ? 51 OD1 ? A ASP 704 ? A ASP 739 ? 1_555 CA ? H CA . ? A CA 907 ? 1_555 O ? MA HOH . ? A HOH 1318 ? 1_555 165.9 ? 52 OD1 ? A ASN 706 ? A ASN 741 ? 1_555 CA ? H CA . ? A CA 907 ? 1_555 O ? MA HOH . ? A HOH 1318 ? 1_555 89.7 ? 53 OD1 ? A ASP 708 ? A ASP 743 ? 1_555 CA ? H CA . ? A CA 907 ? 1_555 O ? MA HOH . ? A HOH 1318 ? 1_555 88.2 ? 54 O ? A LEU 710 ? A LEU 745 ? 1_555 CA ? H CA . ? A CA 907 ? 1_555 O ? MA HOH . ? A HOH 1318 ? 1_555 94.5 ? 55 OD1 ? A ASP 712 ? A ASP 747 ? 1_555 CA ? H CA . ? A CA 907 ? 1_555 O ? MA HOH . ? A HOH 1318 ? 1_555 90.7 ? 56 O ? A ASN 766 ? A ASN 801 ? 1_555 NA ? DA NA . ? A NA 929 ? 1_555 O ? A SER 769 ? A SER 804 ? 1_555 79.0 ? 57 O ? A ASN 766 ? A ASN 801 ? 1_555 NA ? DA NA . ? A NA 929 ? 1_555 OG ? A SER 772 ? A SER 807 ? 1_555 94.2 ? 58 O ? A SER 769 ? A SER 804 ? 1_555 NA ? DA NA . ? A NA 929 ? 1_555 OG ? A SER 772 ? A SER 807 ? 1_555 85.6 ? 59 O ? A ASN 766 ? A ASN 801 ? 1_555 NA ? DA NA . ? A NA 929 ? 1_555 O ? MA HOH . ? A HOH 1361 ? 1_555 99.7 ? 60 O ? A SER 769 ? A SER 804 ? 1_555 NA ? DA NA . ? A NA 929 ? 1_555 O ? MA HOH . ? A HOH 1361 ? 1_555 91.1 ? 61 OG ? A SER 772 ? A SER 807 ? 1_555 NA ? DA NA . ? A NA 929 ? 1_555 O ? MA HOH . ? A HOH 1361 ? 1_555 164.9 ? 62 O ? A ASN 766 ? A ASN 801 ? 1_555 NA ? DA NA . ? A NA 929 ? 1_555 O ? MA HOH . ? A HOH 1400 ? 1_555 84.9 ? 63 O ? A SER 769 ? A SER 804 ? 1_555 NA ? DA NA . ? A NA 929 ? 1_555 O ? MA HOH . ? A HOH 1400 ? 1_555 163.7 ? 64 OG ? A SER 772 ? A SER 807 ? 1_555 NA ? DA NA . ? A NA 929 ? 1_555 O ? MA HOH . ? A HOH 1400 ? 1_555 93.1 ? 65 O ? MA HOH . ? A HOH 1361 ? 1_555 NA ? DA NA . ? A NA 929 ? 1_555 O ? MA HOH . ? A HOH 1400 ? 1_555 94.2 ? 66 O ? A ASN 766 ? A ASN 801 ? 1_555 NA ? DA NA . ? A NA 929 ? 1_555 O ? MA HOH . ? A HOH 1438 ? 1_555 177.1 ? 67 O ? A SER 769 ? A SER 804 ? 1_555 NA ? DA NA . ? A NA 929 ? 1_555 O ? MA HOH . ? A HOH 1438 ? 1_555 103.9 ? 68 OG ? A SER 772 ? A SER 807 ? 1_555 NA ? DA NA . ? A NA 929 ? 1_555 O ? MA HOH . ? A HOH 1438 ? 1_555 86.0 ? 69 O ? MA HOH . ? A HOH 1361 ? 1_555 NA ? DA NA . ? A NA 929 ? 1_555 O ? MA HOH . ? A HOH 1438 ? 1_555 80.4 ? 70 O ? MA HOH . ? A HOH 1400 ? 1_555 NA ? DA NA . ? A NA 929 ? 1_555 O ? MA HOH . ? A HOH 1438 ? 1_555 92.2 ? # 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 2016-04-13 2 'Structure model' 1 1 2016-04-27 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # _pdbx_audit_revision_group.ordinal 1 _pdbx_audit_revision_group.revision_ordinal 2 _pdbx_audit_revision_group.data_content_type 'Structure model' _pdbx_audit_revision_group.group 'Database references' # _diffrn_reflns.diffrn_id 1 _diffrn_reflns.pdbx_d_res_high 1.600 _diffrn_reflns.pdbx_d_res_low 44.020 _diffrn_reflns.pdbx_number_obs 105202 _diffrn_reflns.pdbx_Rmerge_I_obs 0.065 _diffrn_reflns.pdbx_Rsym_value ? _diffrn_reflns.pdbx_chi_squared ? _diffrn_reflns.pdbx_redundancy 2.00 _diffrn_reflns.pdbx_rejects ? _diffrn_reflns.pdbx_percent_possible_obs 92.10 _diffrn_reflns.pdbx_observed_criterion ? _diffrn_reflns.number 205646 _diffrn_reflns.limit_h_max ? _diffrn_reflns.limit_h_min ? _diffrn_reflns.limit_k_max ? _diffrn_reflns.limit_k_min ? _diffrn_reflns.limit_l_max ? _diffrn_reflns.limit_l_min ? # loop_ _pdbx_diffrn_reflns_shell.diffrn_id _pdbx_diffrn_reflns_shell.d_res_high _pdbx_diffrn_reflns_shell.d_res_low _pdbx_diffrn_reflns_shell.number_obs _pdbx_diffrn_reflns_shell.rejects _pdbx_diffrn_reflns_shell.Rmerge_I_obs _pdbx_diffrn_reflns_shell.Rsym_value _pdbx_diffrn_reflns_shell.chi_squared _pdbx_diffrn_reflns_shell.redundancy _pdbx_diffrn_reflns_shell.percent_possible_obs 1 1.60 1.63 ? ? 0.868 ? ? 1.90 ? 1 8.76 44.02 ? ? 0.029 ? ? 2.10 ? # loop_ _pdbx_refine_tls.id _pdbx_refine_tls.pdbx_refine_id _pdbx_refine_tls.details _pdbx_refine_tls.method _pdbx_refine_tls.origin_x _pdbx_refine_tls.origin_y _pdbx_refine_tls.origin_z _pdbx_refine_tls.T[1][1] _pdbx_refine_tls.T[1][1]_esd _pdbx_refine_tls.T[1][2] _pdbx_refine_tls.T[1][2]_esd _pdbx_refine_tls.T[1][3] _pdbx_refine_tls.T[1][3]_esd _pdbx_refine_tls.T[2][2] _pdbx_refine_tls.T[2][2]_esd _pdbx_refine_tls.T[2][3] _pdbx_refine_tls.T[2][3]_esd _pdbx_refine_tls.T[3][3] _pdbx_refine_tls.T[3][3]_esd _pdbx_refine_tls.L[1][1] _pdbx_refine_tls.L[1][1]_esd _pdbx_refine_tls.L[1][2] _pdbx_refine_tls.L[1][2]_esd _pdbx_refine_tls.L[1][3] _pdbx_refine_tls.L[1][3]_esd _pdbx_refine_tls.L[2][2] _pdbx_refine_tls.L[2][2]_esd _pdbx_refine_tls.L[2][3] _pdbx_refine_tls.L[2][3]_esd _pdbx_refine_tls.L[3][3] _pdbx_refine_tls.L[3][3]_esd _pdbx_refine_tls.S[1][1] _pdbx_refine_tls.S[1][1]_esd _pdbx_refine_tls.S[1][2] _pdbx_refine_tls.S[1][2]_esd _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[1][3]_esd _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[2][1]_esd _pdbx_refine_tls.S[2][2] _pdbx_refine_tls.S[2][2]_esd _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[2][3]_esd _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][1]_esd _pdbx_refine_tls.S[3][2] _pdbx_refine_tls.S[3][2]_esd _pdbx_refine_tls.S[3][3] _pdbx_refine_tls.S[3][3]_esd 1 'X-RAY DIFFRACTION' ? refined 16.7855 0.5337 28.9868 0.0443 ? -0.0206 ? 0.0245 ? 0.0322 ? -0.0056 ? 0.0176 ? 0.4971 ? 0.1672 ? -0.3065 ? 0.5398 ? -0.1901 ? 0.8375 ? 0.0702 ? 0.0006 ? 0.0638 ? 0.0108 ? 0.0014 ? -0.0148 ? -0.1352 ? 0.0681 ? -0.0716 ? 2 'X-RAY DIFFRACTION' ? refined -6.4851 -31.7823 41.8265 0.1079 ? -0.0565 ? 0.0295 ? 0.0301 ? -0.0124 ? 0.0660 ? 0.8588 ? 0.2684 ? -0.1952 ? 0.5802 ? 0.0143 ? 1.1392 ? -0.0254 ? -0.0012 ? -0.1980 ? 0.0746 ? -0.0426 ? 0.0348 ? 0.3015 ? -0.1497 ? 0.0680 ? # loop_ _pdbx_refine_tls_group.id _pdbx_refine_tls_group.pdbx_refine_id _pdbx_refine_tls_group.refine_tls_id _pdbx_refine_tls_group.beg_label_asym_id _pdbx_refine_tls_group.beg_label_seq_id _pdbx_refine_tls_group.beg_auth_asym_id _pdbx_refine_tls_group.beg_auth_seq_id _pdbx_refine_tls_group.end_label_asym_id _pdbx_refine_tls_group.end_label_seq_id _pdbx_refine_tls_group.end_auth_asym_id _pdbx_refine_tls_group.end_auth_seq_id _pdbx_refine_tls_group.selection _pdbx_refine_tls_group.selection_details 1 'X-RAY DIFFRACTION' 1 ? ? A 56 ? ? A 560 ? ? 2 'X-RAY DIFFRACTION' 1 ? ? A 1860 ? ? A 1870 ? ? 3 'X-RAY DIFFRACTION' 1 ? ? A 1880 ? ? A 1884 ? ? 4 'X-RAY DIFFRACTION' 2 ? ? A 541 ? ? A 859 ? ? 5 'X-RAY DIFFRACTION' 2 ? ? A 1871 ? ? A 1871 ? ? 6 'X-RAY DIFFRACTION' 2 ? ? A 1890 ? ? A 1894 ? ? # loop_ _software.citation_id _software.classification _software.compiler_name _software.compiler_version _software.contact_author _software.contact_author_email _software.date _software.description _software.dependencies _software.hardware _software.language _software.location _software.mods _software.name _software.os _software.os_version _software.type _software.version _software.pdbx_ordinal ? refinement ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0129 1 ? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.15 2 ? 'data scaling' ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? . 3 ? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS ? ? ? . 4 ? phasing ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? . 5 ? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot ? ? ? . 6 # _pdbx_validate_rmsd_angle.id 1 _pdbx_validate_rmsd_angle.PDB_model_num 1 _pdbx_validate_rmsd_angle.auth_atom_id_1 NE _pdbx_validate_rmsd_angle.auth_asym_id_1 A _pdbx_validate_rmsd_angle.auth_comp_id_1 ARG _pdbx_validate_rmsd_angle.auth_seq_id_1 746 _pdbx_validate_rmsd_angle.PDB_ins_code_1 ? _pdbx_validate_rmsd_angle.label_alt_id_1 ? _pdbx_validate_rmsd_angle.auth_atom_id_2 CZ _pdbx_validate_rmsd_angle.auth_asym_id_2 A _pdbx_validate_rmsd_angle.auth_comp_id_2 ARG _pdbx_validate_rmsd_angle.auth_seq_id_2 746 _pdbx_validate_rmsd_angle.PDB_ins_code_2 ? _pdbx_validate_rmsd_angle.label_alt_id_2 ? _pdbx_validate_rmsd_angle.auth_atom_id_3 NH1 _pdbx_validate_rmsd_angle.auth_asym_id_3 A _pdbx_validate_rmsd_angle.auth_comp_id_3 ARG _pdbx_validate_rmsd_angle.auth_seq_id_3 746 _pdbx_validate_rmsd_angle.PDB_ins_code_3 ? _pdbx_validate_rmsd_angle.label_alt_id_3 ? _pdbx_validate_rmsd_angle.angle_value 123.41 _pdbx_validate_rmsd_angle.angle_target_value 120.30 _pdbx_validate_rmsd_angle.angle_deviation 3.11 _pdbx_validate_rmsd_angle.angle_standard_deviation 0.50 _pdbx_validate_rmsd_angle.linker_flag N # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 ASN A 77 ? ? -39.17 -39.80 2 1 LEU A 94 ? ? -100.58 53.38 3 1 ASP A 128 ? ? -147.04 28.68 4 1 ARG A 368 ? ? -104.14 67.41 5 1 ASN A 378 ? ? -108.49 53.87 6 1 ALA A 435 ? ? -153.36 -35.22 7 1 ARG A 450 ? ? 87.33 -1.95 8 1 ASP A 477 ? ? -29.23 125.85 9 1 THR A 485 ? ? -127.38 -165.67 10 1 ILE A 555 ? ? -67.38 98.30 11 1 SER A 676 ? ? -115.27 -158.27 12 1 GLU A 757 ? ? -26.92 120.05 13 1 TRP A 814 ? ? -148.84 -26.30 # loop_ _pdbx_unobs_or_zero_occ_atoms.id _pdbx_unobs_or_zero_occ_atoms.PDB_model_num _pdbx_unobs_or_zero_occ_atoms.polymer_flag _pdbx_unobs_or_zero_occ_atoms.occupancy_flag _pdbx_unobs_or_zero_occ_atoms.auth_asym_id _pdbx_unobs_or_zero_occ_atoms.auth_comp_id _pdbx_unobs_or_zero_occ_atoms.auth_seq_id _pdbx_unobs_or_zero_occ_atoms.PDB_ins_code _pdbx_unobs_or_zero_occ_atoms.auth_atom_id _pdbx_unobs_or_zero_occ_atoms.label_alt_id _pdbx_unobs_or_zero_occ_atoms.label_asym_id _pdbx_unobs_or_zero_occ_atoms.label_comp_id _pdbx_unobs_or_zero_occ_atoms.label_seq_id _pdbx_unobs_or_zero_occ_atoms.label_atom_id 1 1 Y 1 A SER 860 ? CA ? A SER 825 CA 2 1 Y 1 A SER 860 ? C ? A SER 825 C 3 1 Y 1 A SER 860 ? O ? A SER 825 O 4 1 Y 1 A SER 860 ? CB ? A SER 825 CB 5 1 Y 1 A SER 860 ? OG ? A SER 825 OG # 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 ALA 36 ? A ALA 1 2 1 Y 1 A GLU 37 ? A GLU 2 3 1 Y 1 A TRP 38 ? A TRP 3 4 1 Y 1 A ASP 39 ? A ASP 4 5 1 Y 1 A GLU 40 ? A GLU 5 6 1 Y 1 A GLY 41 ? A GLY 6 7 1 Y 1 A PRO 42 ? A PRO 7 8 1 Y 1 A PRO 43 ? A PRO 8 9 1 Y 1 A THR 44 ? A THR 9 10 1 Y 1 A VAL 45 ? A VAL 10 11 1 Y 1 A LEU 46 ? A LEU 11 12 1 Y 1 A SER 47 ? A SER 12 13 1 Y 1 A ASP 48 ? A ASP 13 14 1 Y 1 A SER 49 ? A SER 14 15 1 Y 1 A PRO 50 ? A PRO 15 16 1 Y 1 A TRP 51 ? A TRP 16 17 1 Y 1 A THR 52 ? A THR 17 18 1 Y 1 A ASN 53 ? A ASN 18 19 1 Y 1 A THR 54 ? A THR 19 20 1 Y 1 A SER 55 ? A SER 20 21 1 Y 1 A VAL 460 ? A VAL 425 22 1 Y 1 A TYR 461 ? A TYR 426 23 1 Y 1 A LYS 462 ? A LYS 427 24 1 Y 1 A LYS 463 ? A LYS 428 25 1 Y 1 A PRO 464 ? A PRO 429 26 1 Y 1 A SER 465 ? A SER 430 27 1 Y 1 A GLY 466 ? A GLY 431 28 1 Y 1 A ASP 569 ? A ASP 534 29 1 Y 1 A ASP 570 ? A ASP 535 30 1 Y 1 A GLU 861 ? A GLU 826 31 1 Y 1 A ILE 862 ? A ILE 827 # loop_ _pdbx_audit_support.funding_organization _pdbx_audit_support.country _pdbx_audit_support.grant_number _pdbx_audit_support.ordinal NWO Netherlands 700.10.354 1 NWO Netherlands 723.013.003 2 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 BETA-D-MANNOSE BMA 4 'ZINC ION' ZN 5 7alpha-hydroxycholesterol 5JK 6 'CALCIUM ION' CA 7 'IODIDE ION' IOD 8 'THIOCYANATE ION' SCN 9 'SODIUM ION' NA 10 GLYCEROL GOL 11 water HOH #