data_3A79 # _entry.id 3A79 # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.284 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 3A79 RCSB RCSB028899 WWPDB D_1000028899 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 3A7B 'TLR2-pnLTA complex' unspecified PDB 3A7C 'TLR2-PE-DTPA complex' unspecified # _pdbx_database_status.entry_id 3A79 _pdbx_database_status.deposit_site PDBJ _pdbx_database_status.process_site PDBJ _pdbx_database_status.recvd_initial_deposition_date 2009-09-20 _pdbx_database_status.status_code REL _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? _pdbx_database_status.pdb_format_compatible Y # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Kang, J.Y.' 1 'Jin, M.S.' 2 'Lee, J.-O.' 3 # _citation.id primary _citation.title 'Recognition of lipopeptide patterns by Toll-like receptor 2-Toll-like receptor 6 heterodimer' _citation.journal_abbrev Immunity _citation.journal_volume 31 _citation.page_first 873 _citation.page_last 884 _citation.year 2009 _citation.journal_id_ASTM IUNIEH _citation.country US _citation.journal_id_ISSN 1074-7613 _citation.journal_id_CSD 2048 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 19931471 _citation.pdbx_database_id_DOI 10.1016/j.immuni.2009.09.018 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Kang, J.Y.' 1 primary 'Nan, X.' 2 primary 'Jin, M.S.' 3 primary 'Youn, S.-J.' 4 primary 'Ryu, Y.H.' 5 primary 'Mah, S.' 6 primary 'Han, S.H.' 7 primary 'Lee, H.' 8 primary 'Paik, S.-G.' 9 primary 'Lee, J.-O.' 10 # _cell.entry_id 3A79 _cell.length_a 168.901 _cell.length_b 168.901 _cell.length_c 231.353 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 120.00 _cell.Z_PDB 12 _cell.pdbx_unique_axis ? _cell.length_a_esd ? _cell.length_b_esd ? _cell.length_c_esd ? _cell.angle_alpha_esd ? _cell.angle_beta_esd ? _cell.angle_gamma_esd ? # _symmetry.entry_id 3A79 _symmetry.space_group_name_H-M 'P 61 2 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 178 _symmetry.space_group_name_Hall ? # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer man 'Toll-like receptor 2, Variable lymphocyte receptor B' 65535.309 1 ? ? 'extracellular domain, UNP residues 1-506(mouse), UNP residues 133-200(Inshore hagfish)' ? 2 polymer man 'Toll-like receptor 6, Variable lymphocyte receptor B' 63785.551 1 ? ? 'extracellular domain, UNP residues 1-482(mouse), UNP residues 157-232(Inshore hagfish)' ? 3 polymer syn Pam2CSK4 724.955 1 ? ? ? ? 4 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 16 ? ? ? ? 5 non-polymer man BETA-D-MANNOSE 180.156 3 ? ? ? ? 6 non-polymer man '2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE' 221.208 1 ? ? ? ? 7 non-polymer syn '(2S)-propane-1,2-diyl dihexadecanoate' 552.912 1 ? ? ? ? # loop_ _entity_name_com.entity_id _entity_name_com.name 1 'TLR2, VLRB.61' 2 'TLR6, VLRB.59' # loop_ _entity_poly.entity_id _entity_poly.type _entity_poly.nstd_linkage _entity_poly.nstd_monomer _entity_poly.pdbx_seq_one_letter_code _entity_poly.pdbx_seq_one_letter_code_can _entity_poly.pdbx_strand_id _entity_poly.pdbx_target_identifier 1 'polypeptide(L)' no no ;MLRALWLFWILVAITVLFSKRCSAQESLSCDASGVCDGRSRSFTSIPSGLTAAMKSLDLSFNKITYIGHGDLRACANLQV LILKSSRINTIEGDAFYSLGSLEHLDLSDNHLSSLSSSWFGPLSSLKYLNLMGNPYQTLGVTSLFPNLTNLQTLRIGNVE TFSEIRRIDFAGLTSLNELEIKALSLRNYQSQSLKSIRDIHHLTLHLSESAFLLEIFADILSSVRYLELRDTNLARFQFS PLPVDEVSSPMKKLAFRGSVLTDESFNELLKLLRYILELSEVEFDDCTLNGLGDFNPSESDVVSELGKVETVTIRRLHIP QFYLFYDLSTVYSLLEKVKRITVENSKVFLVPCSFSQHLKSLEFLDLSENLMVEEYLKNSACKGAWPSLQTLVLSQNHLR SMQKTGEILLTLKNLTSLDISRNTFHPMPDSCQWPEKMRFLNLSSTGIRVVKTCIPQTLEVLDVSNNNLDSFSLFLPRLQ ELYISRNKLKTLPDASLFPVLLVMKIASNQLKSVPDGIFDRLTSLQKIWLHTNPWDCSCPRIDYLSRWLNKNSQKEQGSA KCSGSGKPVRSIICPTLVPR ; ;MLRALWLFWILVAITVLFSKRCSAQESLSCDASGVCDGRSRSFTSIPSGLTAAMKSLDLSFNKITYIGHGDLRACANLQV LILKSSRINTIEGDAFYSLGSLEHLDLSDNHLSSLSSSWFGPLSSLKYLNLMGNPYQTLGVTSLFPNLTNLQTLRIGNVE TFSEIRRIDFAGLTSLNELEIKALSLRNYQSQSLKSIRDIHHLTLHLSESAFLLEIFADILSSVRYLELRDTNLARFQFS PLPVDEVSSPMKKLAFRGSVLTDESFNELLKLLRYILELSEVEFDDCTLNGLGDFNPSESDVVSELGKVETVTIRRLHIP QFYLFYDLSTVYSLLEKVKRITVENSKVFLVPCSFSQHLKSLEFLDLSENLMVEEYLKNSACKGAWPSLQTLVLSQNHLR SMQKTGEILLTLKNLTSLDISRNTFHPMPDSCQWPEKMRFLNLSSTGIRVVKTCIPQTLEVLDVSNNNLDSFSLFLPRLQ ELYISRNKLKTLPDASLFPVLLVMKIASNQLKSVPDGIFDRLTSLQKIWLHTNPWDCSCPRIDYLSRWLNKNSQKEQGSA KCSGSGKPVRSIICPTLVPR ; A ? 2 'polypeptide(L)' no no ;MSQDRKPIVGSFHFVCALALIVGSMTPFSNELESMVDYSNRNLTHVPKDLPPRTKALSLSQNSISELRMPDISFLSELRV LRLSHNRIRSLDFHVFLFNQDLEYLDVSHNRLQNISCCPMASLRHLDLSFNDFDVLPVCKEFGNLTKLTFLGLSAAKFRQ LDLLPVAHLHLSCILLDLVSYHIKGGETESLQIPNTTVLHLVFHPNSLFSVQVNMSVNALGHLQLSNIKLNDENCQRLMT FLSELTRGPTLLNVTLQHIETTWKCSVKLFQFFWPRPVEYLNIYNLTITERIDREEFTYSETALKSLMIEHVKNQVFLFS KEALYSVFAEMNIKMLSISDTPFIHMVCPPSPSSFTFLNFTQNVFTDSVFQGCSTLKRLQTLILQRNGLKNFFKVALMTK NMSSLETLDVSLNSLNSHAYDRTCAWAESILVLNLSSNMLTGSVFRCLPPKVKVLDLHNNRIMSIPKDVTHLQALQELNV ASNQLKSVPDGVFDRLTSLQYIWLHDNPWDCTCPGIRYLSEWINKHSGVVRNSAGSVAPDSAKCSGSGKPVRSIICPTLV PR ; ;MSQDRKPIVGSFHFVCALALIVGSMTPFSNELESMVDYSNRNLTHVPKDLPPRTKALSLSQNSISELRMPDISFLSELRV LRLSHNRIRSLDFHVFLFNQDLEYLDVSHNRLQNISCCPMASLRHLDLSFNDFDVLPVCKEFGNLTKLTFLGLSAAKFRQ LDLLPVAHLHLSCILLDLVSYHIKGGETESLQIPNTTVLHLVFHPNSLFSVQVNMSVNALGHLQLSNIKLNDENCQRLMT FLSELTRGPTLLNVTLQHIETTWKCSVKLFQFFWPRPVEYLNIYNLTITERIDREEFTYSETALKSLMIEHVKNQVFLFS KEALYSVFAEMNIKMLSISDTPFIHMVCPPSPSSFTFLNFTQNVFTDSVFQGCSTLKRLQTLILQRNGLKNFFKVALMTK NMSSLETLDVSLNSLNSHAYDRTCAWAESILVLNLSSNMLTGSVFRCLPPKVKVLDLHNNRIMSIPKDVTHLQALQELNV ASNQLKSVPDGVFDRLTSLQYIWLHDNPWDCTCPGIRYLSEWINKHSGVVRNSAGSVAPDSAKCSGSGKPVRSIICPTLV PR ; B ? 3 'polypeptide(L)' no no CSKKKK CSKKKK C ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 MET n 1 2 LEU n 1 3 ARG n 1 4 ALA n 1 5 LEU n 1 6 TRP n 1 7 LEU n 1 8 PHE n 1 9 TRP n 1 10 ILE n 1 11 LEU n 1 12 VAL n 1 13 ALA n 1 14 ILE n 1 15 THR n 1 16 VAL n 1 17 LEU n 1 18 PHE n 1 19 SER n 1 20 LYS n 1 21 ARG n 1 22 CYS n 1 23 SER n 1 24 ALA n 1 25 GLN n 1 26 GLU n 1 27 SER n 1 28 LEU n 1 29 SER n 1 30 CYS n 1 31 ASP n 1 32 ALA n 1 33 SER n 1 34 GLY n 1 35 VAL n 1 36 CYS n 1 37 ASP n 1 38 GLY n 1 39 ARG n 1 40 SER n 1 41 ARG n 1 42 SER n 1 43 PHE n 1 44 THR n 1 45 SER n 1 46 ILE n 1 47 PRO n 1 48 SER n 1 49 GLY n 1 50 LEU n 1 51 THR n 1 52 ALA n 1 53 ALA n 1 54 MET n 1 55 LYS n 1 56 SER n 1 57 LEU n 1 58 ASP n 1 59 LEU n 1 60 SER n 1 61 PHE n 1 62 ASN n 1 63 LYS n 1 64 ILE n 1 65 THR n 1 66 TYR n 1 67 ILE n 1 68 GLY n 1 69 HIS n 1 70 GLY n 1 71 ASP n 1 72 LEU n 1 73 ARG n 1 74 ALA n 1 75 CYS n 1 76 ALA n 1 77 ASN n 1 78 LEU n 1 79 GLN n 1 80 VAL n 1 81 LEU n 1 82 ILE n 1 83 LEU n 1 84 LYS n 1 85 SER n 1 86 SER n 1 87 ARG n 1 88 ILE n 1 89 ASN n 1 90 THR n 1 91 ILE n 1 92 GLU n 1 93 GLY n 1 94 ASP n 1 95 ALA n 1 96 PHE n 1 97 TYR n 1 98 SER n 1 99 LEU n 1 100 GLY n 1 101 SER n 1 102 LEU n 1 103 GLU n 1 104 HIS n 1 105 LEU n 1 106 ASP n 1 107 LEU n 1 108 SER n 1 109 ASP n 1 110 ASN n 1 111 HIS n 1 112 LEU n 1 113 SER n 1 114 SER n 1 115 LEU n 1 116 SER n 1 117 SER n 1 118 SER n 1 119 TRP n 1 120 PHE n 1 121 GLY n 1 122 PRO n 1 123 LEU n 1 124 SER n 1 125 SER n 1 126 LEU n 1 127 LYS n 1 128 TYR n 1 129 LEU n 1 130 ASN n 1 131 LEU n 1 132 MET n 1 133 GLY n 1 134 ASN n 1 135 PRO n 1 136 TYR n 1 137 GLN n 1 138 THR n 1 139 LEU n 1 140 GLY n 1 141 VAL n 1 142 THR n 1 143 SER n 1 144 LEU n 1 145 PHE n 1 146 PRO n 1 147 ASN n 1 148 LEU n 1 149 THR n 1 150 ASN n 1 151 LEU n 1 152 GLN n 1 153 THR n 1 154 LEU n 1 155 ARG n 1 156 ILE n 1 157 GLY n 1 158 ASN n 1 159 VAL n 1 160 GLU n 1 161 THR n 1 162 PHE n 1 163 SER n 1 164 GLU n 1 165 ILE n 1 166 ARG n 1 167 ARG n 1 168 ILE n 1 169 ASP n 1 170 PHE n 1 171 ALA n 1 172 GLY n 1 173 LEU n 1 174 THR n 1 175 SER n 1 176 LEU n 1 177 ASN n 1 178 GLU n 1 179 LEU n 1 180 GLU n 1 181 ILE n 1 182 LYS n 1 183 ALA n 1 184 LEU n 1 185 SER n 1 186 LEU n 1 187 ARG n 1 188 ASN n 1 189 TYR n 1 190 GLN n 1 191 SER n 1 192 GLN n 1 193 SER n 1 194 LEU n 1 195 LYS n 1 196 SER n 1 197 ILE n 1 198 ARG n 1 199 ASP n 1 200 ILE n 1 201 HIS n 1 202 HIS n 1 203 LEU n 1 204 THR n 1 205 LEU n 1 206 HIS n 1 207 LEU n 1 208 SER n 1 209 GLU n 1 210 SER n 1 211 ALA n 1 212 PHE n 1 213 LEU n 1 214 LEU n 1 215 GLU n 1 216 ILE n 1 217 PHE n 1 218 ALA n 1 219 ASP n 1 220 ILE n 1 221 LEU n 1 222 SER n 1 223 SER n 1 224 VAL n 1 225 ARG n 1 226 TYR n 1 227 LEU n 1 228 GLU n 1 229 LEU n 1 230 ARG n 1 231 ASP n 1 232 THR n 1 233 ASN n 1 234 LEU n 1 235 ALA n 1 236 ARG n 1 237 PHE n 1 238 GLN n 1 239 PHE n 1 240 SER n 1 241 PRO n 1 242 LEU n 1 243 PRO n 1 244 VAL n 1 245 ASP n 1 246 GLU n 1 247 VAL n 1 248 SER n 1 249 SER n 1 250 PRO n 1 251 MET n 1 252 LYS n 1 253 LYS n 1 254 LEU n 1 255 ALA n 1 256 PHE n 1 257 ARG n 1 258 GLY n 1 259 SER n 1 260 VAL n 1 261 LEU n 1 262 THR n 1 263 ASP n 1 264 GLU n 1 265 SER n 1 266 PHE n 1 267 ASN n 1 268 GLU n 1 269 LEU n 1 270 LEU n 1 271 LYS n 1 272 LEU n 1 273 LEU n 1 274 ARG n 1 275 TYR n 1 276 ILE n 1 277 LEU n 1 278 GLU n 1 279 LEU n 1 280 SER n 1 281 GLU n 1 282 VAL n 1 283 GLU n 1 284 PHE n 1 285 ASP n 1 286 ASP n 1 287 CYS n 1 288 THR n 1 289 LEU n 1 290 ASN n 1 291 GLY n 1 292 LEU n 1 293 GLY n 1 294 ASP n 1 295 PHE n 1 296 ASN n 1 297 PRO n 1 298 SER n 1 299 GLU n 1 300 SER n 1 301 ASP n 1 302 VAL n 1 303 VAL n 1 304 SER n 1 305 GLU n 1 306 LEU n 1 307 GLY n 1 308 LYS n 1 309 VAL n 1 310 GLU n 1 311 THR n 1 312 VAL n 1 313 THR n 1 314 ILE n 1 315 ARG n 1 316 ARG n 1 317 LEU n 1 318 HIS n 1 319 ILE n 1 320 PRO n 1 321 GLN n 1 322 PHE n 1 323 TYR n 1 324 LEU n 1 325 PHE n 1 326 TYR n 1 327 ASP n 1 328 LEU n 1 329 SER n 1 330 THR n 1 331 VAL n 1 332 TYR n 1 333 SER n 1 334 LEU n 1 335 LEU n 1 336 GLU n 1 337 LYS n 1 338 VAL n 1 339 LYS n 1 340 ARG n 1 341 ILE n 1 342 THR n 1 343 VAL n 1 344 GLU n 1 345 ASN n 1 346 SER n 1 347 LYS n 1 348 VAL n 1 349 PHE n 1 350 LEU n 1 351 VAL n 1 352 PRO n 1 353 CYS n 1 354 SER n 1 355 PHE n 1 356 SER n 1 357 GLN n 1 358 HIS n 1 359 LEU n 1 360 LYS n 1 361 SER n 1 362 LEU n 1 363 GLU n 1 364 PHE n 1 365 LEU n 1 366 ASP n 1 367 LEU n 1 368 SER n 1 369 GLU n 1 370 ASN n 1 371 LEU n 1 372 MET n 1 373 VAL n 1 374 GLU n 1 375 GLU n 1 376 TYR n 1 377 LEU n 1 378 LYS n 1 379 ASN n 1 380 SER n 1 381 ALA n 1 382 CYS n 1 383 LYS n 1 384 GLY n 1 385 ALA n 1 386 TRP n 1 387 PRO n 1 388 SER n 1 389 LEU n 1 390 GLN n 1 391 THR n 1 392 LEU n 1 393 VAL n 1 394 LEU n 1 395 SER n 1 396 GLN n 1 397 ASN n 1 398 HIS n 1 399 LEU n 1 400 ARG n 1 401 SER n 1 402 MET n 1 403 GLN n 1 404 LYS n 1 405 THR n 1 406 GLY n 1 407 GLU n 1 408 ILE n 1 409 LEU n 1 410 LEU n 1 411 THR n 1 412 LEU n 1 413 LYS n 1 414 ASN n 1 415 LEU n 1 416 THR n 1 417 SER n 1 418 LEU n 1 419 ASP n 1 420 ILE n 1 421 SER n 1 422 ARG n 1 423 ASN n 1 424 THR n 1 425 PHE n 1 426 HIS n 1 427 PRO n 1 428 MET n 1 429 PRO n 1 430 ASP n 1 431 SER n 1 432 CYS n 1 433 GLN n 1 434 TRP n 1 435 PRO n 1 436 GLU n 1 437 LYS n 1 438 MET n 1 439 ARG n 1 440 PHE n 1 441 LEU n 1 442 ASN n 1 443 LEU n 1 444 SER n 1 445 SER n 1 446 THR n 1 447 GLY n 1 448 ILE n 1 449 ARG n 1 450 VAL n 1 451 VAL n 1 452 LYS n 1 453 THR n 1 454 CYS n 1 455 ILE n 1 456 PRO n 1 457 GLN n 1 458 THR n 1 459 LEU n 1 460 GLU n 1 461 VAL n 1 462 LEU n 1 463 ASP n 1 464 VAL n 1 465 SER n 1 466 ASN n 1 467 ASN n 1 468 ASN n 1 469 LEU n 1 470 ASP n 1 471 SER n 1 472 PHE n 1 473 SER n 1 474 LEU n 1 475 PHE n 1 476 LEU n 1 477 PRO n 1 478 ARG n 1 479 LEU n 1 480 GLN n 1 481 GLU n 1 482 LEU n 1 483 TYR n 1 484 ILE n 1 485 SER n 1 486 ARG n 1 487 ASN n 1 488 LYS n 1 489 LEU n 1 490 LYS n 1 491 THR n 1 492 LEU n 1 493 PRO n 1 494 ASP n 1 495 ALA n 1 496 SER n 1 497 LEU n 1 498 PHE n 1 499 PRO n 1 500 VAL n 1 501 LEU n 1 502 LEU n 1 503 VAL n 1 504 MET n 1 505 LYS n 1 506 ILE n 1 507 ALA n 1 508 SER n 1 509 ASN n 1 510 GLN n 1 511 LEU n 1 512 LYS n 1 513 SER n 1 514 VAL n 1 515 PRO n 1 516 ASP n 1 517 GLY n 1 518 ILE n 1 519 PHE n 1 520 ASP n 1 521 ARG n 1 522 LEU n 1 523 THR n 1 524 SER n 1 525 LEU n 1 526 GLN n 1 527 LYS n 1 528 ILE n 1 529 TRP n 1 530 LEU n 1 531 HIS n 1 532 THR n 1 533 ASN n 1 534 PRO n 1 535 TRP n 1 536 ASP n 1 537 CYS n 1 538 SER n 1 539 CYS n 1 540 PRO n 1 541 ARG n 1 542 ILE n 1 543 ASP n 1 544 TYR n 1 545 LEU n 1 546 SER n 1 547 ARG n 1 548 TRP n 1 549 LEU n 1 550 ASN n 1 551 LYS n 1 552 ASN n 1 553 SER n 1 554 GLN n 1 555 LYS n 1 556 GLU n 1 557 GLN n 1 558 GLY n 1 559 SER n 1 560 ALA n 1 561 LYS n 1 562 CYS n 1 563 SER n 1 564 GLY n 1 565 SER n 1 566 GLY n 1 567 LYS n 1 568 PRO n 1 569 VAL n 1 570 ARG n 1 571 SER n 1 572 ILE n 1 573 ILE n 1 574 CYS n 1 575 PRO n 1 576 THR n 1 577 LEU n 1 578 VAL n 1 579 PRO n 1 580 ARG n 2 1 MET n 2 2 SER n 2 3 GLN n 2 4 ASP n 2 5 ARG n 2 6 LYS n 2 7 PRO n 2 8 ILE n 2 9 VAL n 2 10 GLY n 2 11 SER n 2 12 PHE n 2 13 HIS n 2 14 PHE n 2 15 VAL n 2 16 CYS n 2 17 ALA n 2 18 LEU n 2 19 ALA n 2 20 LEU n 2 21 ILE n 2 22 VAL n 2 23 GLY n 2 24 SER n 2 25 MET n 2 26 THR n 2 27 PRO n 2 28 PHE n 2 29 SER n 2 30 ASN n 2 31 GLU n 2 32 LEU n 2 33 GLU n 2 34 SER n 2 35 MET n 2 36 VAL n 2 37 ASP n 2 38 TYR n 2 39 SER n 2 40 ASN n 2 41 ARG n 2 42 ASN n 2 43 LEU n 2 44 THR n 2 45 HIS n 2 46 VAL n 2 47 PRO n 2 48 LYS n 2 49 ASP n 2 50 LEU n 2 51 PRO n 2 52 PRO n 2 53 ARG n 2 54 THR n 2 55 LYS n 2 56 ALA n 2 57 LEU n 2 58 SER n 2 59 LEU n 2 60 SER n 2 61 GLN n 2 62 ASN n 2 63 SER n 2 64 ILE n 2 65 SER n 2 66 GLU n 2 67 LEU n 2 68 ARG n 2 69 MET n 2 70 PRO n 2 71 ASP n 2 72 ILE n 2 73 SER n 2 74 PHE n 2 75 LEU n 2 76 SER n 2 77 GLU n 2 78 LEU n 2 79 ARG n 2 80 VAL n 2 81 LEU n 2 82 ARG n 2 83 LEU n 2 84 SER n 2 85 HIS n 2 86 ASN n 2 87 ARG n 2 88 ILE n 2 89 ARG n 2 90 SER n 2 91 LEU n 2 92 ASP n 2 93 PHE n 2 94 HIS n 2 95 VAL n 2 96 PHE n 2 97 LEU n 2 98 PHE n 2 99 ASN n 2 100 GLN n 2 101 ASP n 2 102 LEU n 2 103 GLU n 2 104 TYR n 2 105 LEU n 2 106 ASP n 2 107 VAL n 2 108 SER n 2 109 HIS n 2 110 ASN n 2 111 ARG n 2 112 LEU n 2 113 GLN n 2 114 ASN n 2 115 ILE n 2 116 SER n 2 117 CYS n 2 118 CYS n 2 119 PRO n 2 120 MET n 2 121 ALA n 2 122 SER n 2 123 LEU n 2 124 ARG n 2 125 HIS n 2 126 LEU n 2 127 ASP n 2 128 LEU n 2 129 SER n 2 130 PHE n 2 131 ASN n 2 132 ASP n 2 133 PHE n 2 134 ASP n 2 135 VAL n 2 136 LEU n 2 137 PRO n 2 138 VAL n 2 139 CYS n 2 140 LYS n 2 141 GLU n 2 142 PHE n 2 143 GLY n 2 144 ASN n 2 145 LEU n 2 146 THR n 2 147 LYS n 2 148 LEU n 2 149 THR n 2 150 PHE n 2 151 LEU n 2 152 GLY n 2 153 LEU n 2 154 SER n 2 155 ALA n 2 156 ALA n 2 157 LYS n 2 158 PHE n 2 159 ARG n 2 160 GLN n 2 161 LEU n 2 162 ASP n 2 163 LEU n 2 164 LEU n 2 165 PRO n 2 166 VAL n 2 167 ALA n 2 168 HIS n 2 169 LEU n 2 170 HIS n 2 171 LEU n 2 172 SER n 2 173 CYS n 2 174 ILE n 2 175 LEU n 2 176 LEU n 2 177 ASP n 2 178 LEU n 2 179 VAL n 2 180 SER n 2 181 TYR n 2 182 HIS n 2 183 ILE n 2 184 LYS n 2 185 GLY n 2 186 GLY n 2 187 GLU n 2 188 THR n 2 189 GLU n 2 190 SER n 2 191 LEU n 2 192 GLN n 2 193 ILE n 2 194 PRO n 2 195 ASN n 2 196 THR n 2 197 THR n 2 198 VAL n 2 199 LEU n 2 200 HIS n 2 201 LEU n 2 202 VAL n 2 203 PHE n 2 204 HIS n 2 205 PRO n 2 206 ASN n 2 207 SER n 2 208 LEU n 2 209 PHE n 2 210 SER n 2 211 VAL n 2 212 GLN n 2 213 VAL n 2 214 ASN n 2 215 MET n 2 216 SER n 2 217 VAL n 2 218 ASN n 2 219 ALA n 2 220 LEU n 2 221 GLY n 2 222 HIS n 2 223 LEU n 2 224 GLN n 2 225 LEU n 2 226 SER n 2 227 ASN n 2 228 ILE n 2 229 LYS n 2 230 LEU n 2 231 ASN n 2 232 ASP n 2 233 GLU n 2 234 ASN n 2 235 CYS n 2 236 GLN n 2 237 ARG n 2 238 LEU n 2 239 MET n 2 240 THR n 2 241 PHE n 2 242 LEU n 2 243 SER n 2 244 GLU n 2 245 LEU n 2 246 THR n 2 247 ARG n 2 248 GLY n 2 249 PRO n 2 250 THR n 2 251 LEU n 2 252 LEU n 2 253 ASN n 2 254 VAL n 2 255 THR n 2 256 LEU n 2 257 GLN n 2 258 HIS n 2 259 ILE n 2 260 GLU n 2 261 THR n 2 262 THR n 2 263 TRP n 2 264 LYS n 2 265 CYS n 2 266 SER n 2 267 VAL n 2 268 LYS n 2 269 LEU n 2 270 PHE n 2 271 GLN n 2 272 PHE n 2 273 PHE n 2 274 TRP n 2 275 PRO n 2 276 ARG n 2 277 PRO n 2 278 VAL n 2 279 GLU n 2 280 TYR n 2 281 LEU n 2 282 ASN n 2 283 ILE n 2 284 TYR n 2 285 ASN n 2 286 LEU n 2 287 THR n 2 288 ILE n 2 289 THR n 2 290 GLU n 2 291 ARG n 2 292 ILE n 2 293 ASP n 2 294 ARG n 2 295 GLU n 2 296 GLU n 2 297 PHE n 2 298 THR n 2 299 TYR n 2 300 SER n 2 301 GLU n 2 302 THR n 2 303 ALA n 2 304 LEU n 2 305 LYS n 2 306 SER n 2 307 LEU n 2 308 MET n 2 309 ILE n 2 310 GLU n 2 311 HIS n 2 312 VAL n 2 313 LYS n 2 314 ASN n 2 315 GLN n 2 316 VAL n 2 317 PHE n 2 318 LEU n 2 319 PHE n 2 320 SER n 2 321 LYS n 2 322 GLU n 2 323 ALA n 2 324 LEU n 2 325 TYR n 2 326 SER n 2 327 VAL n 2 328 PHE n 2 329 ALA n 2 330 GLU n 2 331 MET n 2 332 ASN n 2 333 ILE n 2 334 LYS n 2 335 MET n 2 336 LEU n 2 337 SER n 2 338 ILE n 2 339 SER n 2 340 ASP n 2 341 THR n 2 342 PRO n 2 343 PHE n 2 344 ILE n 2 345 HIS n 2 346 MET n 2 347 VAL n 2 348 CYS n 2 349 PRO n 2 350 PRO n 2 351 SER n 2 352 PRO n 2 353 SER n 2 354 SER n 2 355 PHE n 2 356 THR n 2 357 PHE n 2 358 LEU n 2 359 ASN n 2 360 PHE n 2 361 THR n 2 362 GLN n 2 363 ASN n 2 364 VAL n 2 365 PHE n 2 366 THR n 2 367 ASP n 2 368 SER n 2 369 VAL n 2 370 PHE n 2 371 GLN n 2 372 GLY n 2 373 CYS n 2 374 SER n 2 375 THR n 2 376 LEU n 2 377 LYS n 2 378 ARG n 2 379 LEU n 2 380 GLN n 2 381 THR n 2 382 LEU n 2 383 ILE n 2 384 LEU n 2 385 GLN n 2 386 ARG n 2 387 ASN n 2 388 GLY n 2 389 LEU n 2 390 LYS n 2 391 ASN n 2 392 PHE n 2 393 PHE n 2 394 LYS n 2 395 VAL n 2 396 ALA n 2 397 LEU n 2 398 MET n 2 399 THR n 2 400 LYS n 2 401 ASN n 2 402 MET n 2 403 SER n 2 404 SER n 2 405 LEU n 2 406 GLU n 2 407 THR n 2 408 LEU n 2 409 ASP n 2 410 VAL n 2 411 SER n 2 412 LEU n 2 413 ASN n 2 414 SER n 2 415 LEU n 2 416 ASN n 2 417 SER n 2 418 HIS n 2 419 ALA n 2 420 TYR n 2 421 ASP n 2 422 ARG n 2 423 THR n 2 424 CYS n 2 425 ALA n 2 426 TRP n 2 427 ALA n 2 428 GLU n 2 429 SER n 2 430 ILE n 2 431 LEU n 2 432 VAL n 2 433 LEU n 2 434 ASN n 2 435 LEU n 2 436 SER n 2 437 SER n 2 438 ASN n 2 439 MET n 2 440 LEU n 2 441 THR n 2 442 GLY n 2 443 SER n 2 444 VAL n 2 445 PHE n 2 446 ARG n 2 447 CYS n 2 448 LEU n 2 449 PRO n 2 450 PRO n 2 451 LYS n 2 452 VAL n 2 453 LYS n 2 454 VAL n 2 455 LEU n 2 456 ASP n 2 457 LEU n 2 458 HIS n 2 459 ASN n 2 460 ASN n 2 461 ARG n 2 462 ILE n 2 463 MET n 2 464 SER n 2 465 ILE n 2 466 PRO n 2 467 LYS n 2 468 ASP n 2 469 VAL n 2 470 THR n 2 471 HIS n 2 472 LEU n 2 473 GLN n 2 474 ALA n 2 475 LEU n 2 476 GLN n 2 477 GLU n 2 478 LEU n 2 479 ASN n 2 480 VAL n 2 481 ALA n 2 482 SER n 2 483 ASN n 2 484 GLN n 2 485 LEU n 2 486 LYS n 2 487 SER n 2 488 VAL n 2 489 PRO n 2 490 ASP n 2 491 GLY n 2 492 VAL n 2 493 PHE n 2 494 ASP n 2 495 ARG n 2 496 LEU n 2 497 THR n 2 498 SER n 2 499 LEU n 2 500 GLN n 2 501 TYR n 2 502 ILE n 2 503 TRP n 2 504 LEU n 2 505 HIS n 2 506 ASP n 2 507 ASN n 2 508 PRO n 2 509 TRP n 2 510 ASP n 2 511 CYS n 2 512 THR n 2 513 CYS n 2 514 PRO n 2 515 GLY n 2 516 ILE n 2 517 ARG n 2 518 TYR n 2 519 LEU n 2 520 SER n 2 521 GLU n 2 522 TRP n 2 523 ILE n 2 524 ASN n 2 525 LYS n 2 526 HIS n 2 527 SER n 2 528 GLY n 2 529 VAL n 2 530 VAL n 2 531 ARG n 2 532 ASN n 2 533 SER n 2 534 ALA n 2 535 GLY n 2 536 SER n 2 537 VAL n 2 538 ALA n 2 539 PRO n 2 540 ASP n 2 541 SER n 2 542 ALA n 2 543 LYS n 2 544 CYS n 2 545 SER n 2 546 GLY n 2 547 SER n 2 548 GLY n 2 549 LYS n 2 550 PRO n 2 551 VAL n 2 552 ARG n 2 553 SER n 2 554 ILE n 2 555 ILE n 2 556 CYS n 2 557 PRO n 2 558 THR n 2 559 LEU n 2 560 VAL n 2 561 PRO n 2 562 ARG n 3 1 CYS n 3 2 SER n 3 3 LYS n 3 4 LYS n 3 5 LYS n 3 6 LYS n # loop_ _entity_src_gen.entity_id _entity_src_gen.pdbx_src_id _entity_src_gen.pdbx_alt_source_flag _entity_src_gen.pdbx_seq_type _entity_src_gen.pdbx_beg_seq_num _entity_src_gen.pdbx_end_seq_num _entity_src_gen.gene_src_common_name _entity_src_gen.gene_src_genus _entity_src_gen.pdbx_gene_src_gene _entity_src_gen.gene_src_species _entity_src_gen.gene_src_strain _entity_src_gen.gene_src_tissue _entity_src_gen.gene_src_tissue_fraction _entity_src_gen.gene_src_details _entity_src_gen.pdbx_gene_src_fragment _entity_src_gen.pdbx_gene_src_scientific_name _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id _entity_src_gen.pdbx_gene_src_variant _entity_src_gen.pdbx_gene_src_cell_line _entity_src_gen.pdbx_gene_src_atcc _entity_src_gen.pdbx_gene_src_organ _entity_src_gen.pdbx_gene_src_organelle _entity_src_gen.pdbx_gene_src_cell _entity_src_gen.pdbx_gene_src_cellular_location _entity_src_gen.host_org_common_name _entity_src_gen.pdbx_host_org_scientific_name _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id _entity_src_gen.host_org_genus _entity_src_gen.pdbx_host_org_gene _entity_src_gen.pdbx_host_org_organ _entity_src_gen.host_org_species _entity_src_gen.pdbx_host_org_tissue _entity_src_gen.pdbx_host_org_tissue_fraction _entity_src_gen.pdbx_host_org_strain _entity_src_gen.pdbx_host_org_variant _entity_src_gen.pdbx_host_org_cell_line _entity_src_gen.pdbx_host_org_atcc _entity_src_gen.pdbx_host_org_culture_collection _entity_src_gen.pdbx_host_org_cell _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 1 1 sample ? 1 506 'mouse, Inshore hagfish' ? Tlr2 ? ? ? ? ? ? 'Mus musculus' 10090 ? ? ? ? ? ? ? ? 'TRICHOPLUSIA NI' 7111 ? ? ? ? ? ? Hi-5 ? ? ? ? ? ? ? PLASMID ? ? ? PVL1393 ? ? 1 2 sample ? 509 576 'mouse, Inshore hagfish' ? Tlr2 ? ? ? ? ? ? 'Eptatretus burgeri' 7764 ? ? ? ? ? ? ? ? 'TRICHOPLUSIA NI' 7111 ? ? ? ? ? ? Hi-5 ? ? ? ? ? ? ? PLASMID ? ? ? PVL1393 ? ? 2 1 sample ? 1 482 'mouse, Inshore hagfish' ? Tlr6 ? ? ? ? ? ? 'Mus musculus' 10090 ? ? ? ? ? ? ? ? 'TRICHOPLUSIA NI' 7111 ? ? ? ? ? ? Hi-5 ? ? ? ? ? ? ? PLASMID ? ? ? PVL1393 ? ? 2 2 sample ? 483 558 'mouse, Inshore hagfish' ? Tlr6 ? ? ? ? ? ? 'Eptatretus burgeri' 7764 ? ? ? ? ? ? ? ? 'TRICHOPLUSIA NI' 7111 ? ? ? ? ? ? Hi-5 ? ? ? ? ? ? ? PLASMID ? ? ? PVL1393 ? ? # _pdbx_entity_src_syn.entity_id 3 _pdbx_entity_src_syn.pdbx_src_id 1 _pdbx_entity_src_syn.pdbx_alt_source_flag sample _pdbx_entity_src_syn.pdbx_beg_seq_num ? _pdbx_entity_src_syn.pdbx_end_seq_num ? _pdbx_entity_src_syn.organism_scientific 'synthetic construct' _pdbx_entity_src_syn.organism_common_name ? _pdbx_entity_src_syn.ncbi_taxonomy_id 32630 _pdbx_entity_src_syn.details 'synthetic peptide' # loop_ _struct_ref.id _struct_ref.db_name _struct_ref.db_code _struct_ref.pdbx_db_accession _struct_ref.entity_id _struct_ref.pdbx_seq_one_letter_code _struct_ref.pdbx_align_begin _struct_ref.pdbx_db_isoform 1 UNP TLR2_MOUSE Q9QUN7 1 ;MLRALWLFWILVAITVLFSKRCSAQESLSCDASGVCDGRSRSFTSIPSGLTAAMKSLDLSFNKITYIGHGDLRACANLQV LILKSSRINTIEGDAFYSLGSLEHLDLSDNHLSSLSSSWFGPLSSLKYLNLMGNPYQTLGVTSLFPNLTNLQTLRIGNVE TFSEIRRIDFAGLTSLNELEIKALSLRNYQSQSLKSIRDIHHLTLHLSESAFLLEIFADILSSVRYLELRDTNLARFQFS PLPVDEVSSPMKKLAFRGSVLTDESFNELLKLLRYILELSEVEFDDCTLNGLGDFNPSESDVVSELGKVETVTIRRLHIP QFYLFYDLSTVYSLLEKVKRITVENSKVFLVPCSFSQHLKSLEFLDLSENLMVEEYLKNSACKGAWPSLQTLVLSQNHLR SMQKTGEILLTLKNLTSLDISRNTFHPMPDSCQWPEKMRFLNLSSTGIRVVKTCIPQTLEVLDVSNNNLDSFSLFLPRLQ ELYISRNKLKTLPDASLFPVLLVMKI ; 1 ? 2 UNP Q4G1L2_EPTBU Q4G1L2 1 ASNQLKSVPDGIFDRLTSLQKIWLHTNPWDCSCPRIDYLSRWLNKNSQKEQGSAKCSGSGKPVRSIICPT 133 ? 3 UNP TLR6_MOUSE Q9EPW9 2 ;MSQDRKPIVGSFHFVCALALIVGSMTPFSNELESMVDYSNRNLTHVPKDLPPRTKALSLSQNSISELRMPDISFLSELRV LRLSHNRIRSLDFHVFLFNQDLEYLDVSHNRLQNISCCPMASLRHLDLSFNDFDVLPVCKEFGNLTKLTFLGLSAAKFRQ LDLLPVAHLHLSCILLDLVSYHIKGGETESLQIPNTTVLHLVFHPNSLFSVQVNMSVNALGHLQLSNIKLNDENCQRLMT FLSELTRGPTLLNVTLQHIETTWKCSVKLFQFFWPRPVEYLNIYNLTITERIDREEFTYSETALKSLMIEHVKNQVFLFS KEALYSVFAEMNIKMLSISDTPFIHMVCPPSPSSFTFLNFTQNVFTDSVFQGCSTLKRLQTLILQRNGLKNFFKVALMTK NMSSLETLDVSLNSLNSHAYDRTCAWAESILVLNLSSNMLTGSVFRCLPPKVKVLDLHNNRIMSIPKDVTHLQALQELNV AS ; 1 ? 4 UNP Q4G1L3_EPTBU Q4G1L3 2 NQLKSVPDGVFDRLTSLQYIWLHDNPWDCTCPGIRYLSEWINKHSGVVRNSAGSVAPDSAKCSGSGKPVRSIICPT 157 ? 5 PDB 3A79 3A79 3 CSKKKK 1 ? # loop_ _struct_ref_seq.align_id _struct_ref_seq.ref_id _struct_ref_seq.pdbx_PDB_id_code _struct_ref_seq.pdbx_strand_id _struct_ref_seq.seq_align_beg _struct_ref_seq.pdbx_seq_align_beg_ins_code _struct_ref_seq.seq_align_end _struct_ref_seq.pdbx_seq_align_end_ins_code _struct_ref_seq.pdbx_db_accession _struct_ref_seq.db_align_beg _struct_ref_seq.pdbx_db_align_beg_ins_code _struct_ref_seq.db_align_end _struct_ref_seq.pdbx_db_align_end_ins_code _struct_ref_seq.pdbx_auth_seq_align_beg _struct_ref_seq.pdbx_auth_seq_align_end 1 1 3A79 A 1 ? 506 ? Q9QUN7 1 ? 506 ? 1 506 2 2 3A79 A 509 ? 576 ? Q4G1L2 133 ? 200 ? 509 576 3 3 3A79 B 1 ? 482 ? Q9EPW9 1 ? 482 ? 1 482 4 4 3A79 B 483 ? 558 ? Q4G1L3 157 ? 232 ? 483 558 5 5 3A79 C 1 ? 6 ? 3A79 1 ? 6 ? 11 16 # 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 2 3A79 ALA A 507 ? UNP Q4G1L2 ? ? LINKER 507 1 2 3A79 SER A 508 ? UNP Q4G1L2 ? ? LINKER 508 2 2 3A79 LEU A 577 ? UNP Q4G1L2 ? ? 'EXPRESSION TAG' 577 3 2 3A79 VAL A 578 ? UNP Q4G1L2 ? ? 'EXPRESSION TAG' 578 4 2 3A79 PRO A 579 ? UNP Q4G1L2 ? ? 'EXPRESSION TAG' 579 5 2 3A79 ARG A 580 ? UNP Q4G1L2 ? ? 'EXPRESSION TAG' 580 6 4 3A79 LEU B 559 ? UNP Q4G1L3 ? ? 'EXPRESSION TAG' 559 7 4 3A79 VAL B 560 ? UNP Q4G1L3 ? ? 'EXPRESSION TAG' 560 8 4 3A79 PRO B 561 ? UNP Q4G1L3 ? ? 'EXPRESSION TAG' 561 9 4 3A79 ARG B 562 ? UNP Q4G1L3 ? ? 'EXPRESSION TAG' 562 10 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 BMA D-saccharide . BETA-D-MANNOSE ? 'C6 H12 O6' 180.156 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 NDG D-saccharide . '2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE' ? '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 PXS non-polymer . '(2S)-propane-1,2-diyl dihexadecanoate' ? 'C35 H68 O4' 552.912 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.crystals_number 1 _exptl.entry_id 3A79 _exptl.method 'X-RAY DIFFRACTION' # _exptl_crystal.id 1 _exptl_crystal.pdbx_mosaicity ? _exptl_crystal.pdbx_mosaicity_esd ? _exptl_crystal.density_Matthews 3.66 _exptl_crystal.density_diffrn ? _exptl_crystal.density_meas ? _exptl_crystal.density_meas_temp ? _exptl_crystal.density_percent_sol 66.39 _exptl_crystal.size_max ? _exptl_crystal.size_mid ? _exptl_crystal.size_min ? _exptl_crystal.size_rad ? _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, SITTING DROP' _exptl_crystal_grow.pH 5.5 _exptl_crystal_grow.temp 293 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pdbx_details '2.0M ammonium sulfate, 0.1M MES pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K' _exptl_crystal_grow.pdbx_pH_range ? # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type 'MARMOSAIC 225 mm CCD' _diffrn_detector.pdbx_collection_date 2008-09-24 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.monochromator 'Silicon 111' _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.87260 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'ESRF BEAMLINE ID23-2' _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 0.87260 _diffrn_source.pdbx_synchrotron_site ESRF _diffrn_source.pdbx_synchrotron_beamline ID23-2 # _reflns.entry_id 3A79 _reflns.B_iso_Wilson_estimate 56.990 _reflns.observed_criterion_sigma_I -3.000 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_high 2.9 _reflns.d_resolution_low 50 _reflns.number_all 43746 _reflns.number_obs 43573 _reflns.percent_possible_obs 99.67 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rsym_value 0.106 _reflns.pdbx_netI_over_sigmaI 8.2700 _reflns.pdbx_redundancy 3.4 _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # _reflns_shell.d_res_high 2.9 _reflns_shell.d_res_low 3.0 _reflns_shell.percent_possible_obs ? _reflns_shell.percent_possible_all 98.4 _reflns_shell.Rmerge_I_obs ? _reflns_shell.meanI_over_sigI_obs 2.330 _reflns_shell.pdbx_Rsym_value 0.52500 _reflns_shell.pdbx_redundancy 3.55 _reflns_shell.number_unique_all 3448 _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 # _refine.entry_id 3A79 _refine.ls_d_res_high 2.900 _refine.ls_d_res_low 34.11 _refine.pdbx_ls_sigma_F 0.0 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.ls_percent_reflns_obs 99.670 _refine.ls_number_reflns_obs 43573 _refine.ls_number_reflns_all ? _refine.pdbx_ls_cross_valid_method ? _refine.pdbx_R_Free_selection_details ? _refine.details ? _refine.ls_R_factor_all ? _refine.ls_R_factor_obs 0.215 _refine.ls_R_factor_R_work 0.208 _refine.ls_wR_factor_R_work ? _refine.ls_R_factor_R_free 0.280 _refine.ls_wR_factor_R_free ? _refine.ls_percent_reflns_R_free 10.160 _refine.ls_number_reflns_R_free 4429 _refine.ls_R_factor_R_free_error ? _refine.B_iso_mean 88.661 _refine.solvent_model_param_bsol 31.282 _refine.solvent_model_param_ksol 0.278 _refine.pdbx_isotropic_thermal_model ? _refine.aniso_B[1][1] -1.214 _refine.aniso_B[2][2] -1.214 _refine.aniso_B[3][3] -28.384 _refine.aniso_B[1][2] 0.000 _refine.aniso_B[1][3] -0.000 _refine.aniso_B[2][3] 0.000 _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML 2.750 _refine.overall_SU_B ? _refine.solvent_model_details 'FLAT BULK SOLVENT MODEL' _refine.pdbx_solvent_vdw_probe_radii 1.110 _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii 0.900 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.pdbx_starting_model 'PDB ENTRIES 2Z81, 2Z7X, 2O6R' _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_stereochemistry_target_values ML _refine.pdbx_stereochem_target_val_spec_case ? _refine.overall_FOM_work_R_set 0.799 _refine.B_iso_max 445.89 _refine.B_iso_min 24.01 _refine.occupancy_max 1.00 _refine.occupancy_min 1.00 _refine.pdbx_ls_sigma_I ? _refine.ls_redundancy_reflns_obs ? _refine.ls_R_factor_R_free_error_details ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.overall_FOM_free_R_set ? _refine.pdbx_overall_phase_error ? _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 8596 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 310 _refine_hist.number_atoms_solvent 0 _refine_hist.number_atoms_total 8906 _refine_hist.d_res_high 2.900 _refine_hist.d_res_low 34.11 # loop_ _refine_ls_restr.type _refine_ls_restr.number _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function f_bond_d 9122 0.008 ? ? 'X-RAY DIFFRACTION' ? f_angle_d 12385 1.251 ? ? 'X-RAY DIFFRACTION' ? f_chiral_restr 1479 0.076 ? ? 'X-RAY DIFFRACTION' ? f_plane_restr 1526 0.004 ? ? 'X-RAY DIFFRACTION' ? f_dihedral_angle_d 3482 22.858 ? ? 'X-RAY DIFFRACTION' ? # loop_ _refine_ls_shell.d_res_high _refine_ls_shell.d_res_low _refine_ls_shell.pdbx_total_number_of_bins_used _refine_ls_shell.percent_reflns_obs _refine_ls_shell.number_reflns_R_work _refine_ls_shell.R_factor_all _refine_ls_shell.R_factor_R_work _refine_ls_shell.R_factor_R_free _refine_ls_shell.percent_reflns_R_free _refine_ls_shell.number_reflns_R_free _refine_ls_shell.R_factor_R_free_error _refine_ls_shell.number_reflns_all _refine_ls_shell.number_reflns_obs _refine_ls_shell.redundancy_reflns_obs _refine_ls_shell.pdbx_refine_id 2.900 2.933 30 100.000 1280 . 0.340 0.412 . 132 . 1412 1280 . 'X-RAY DIFFRACTION' 2.933 2.967 30 100.000 1285 . 0.301 0.398 . 151 . 1436 1285 . 'X-RAY DIFFRACTION' 2.967 3.004 30 100.000 1281 . 0.304 0.354 . 144 . 1425 1281 . 'X-RAY DIFFRACTION' 3.004 3.042 30 100.000 1278 . 0.284 0.377 . 142 . 1420 1278 . 'X-RAY DIFFRACTION' 3.042 3.082 30 100.000 1280 . 0.270 0.333 . 159 . 1439 1280 . 'X-RAY DIFFRACTION' 3.082 3.124 30 100.000 1277 . 0.249 0.316 . 154 . 1431 1277 . 'X-RAY DIFFRACTION' 3.124 3.168 30 100.000 1259 . 0.246 0.337 . 149 . 1408 1259 . 'X-RAY DIFFRACTION' 3.168 3.216 30 100.000 1290 . 0.243 0.331 . 146 . 1436 1290 . 'X-RAY DIFFRACTION' 3.216 3.266 30 100.000 1294 . 0.229 0.317 . 142 . 1436 1294 . 'X-RAY DIFFRACTION' 3.266 3.319 30 100.000 1280 . 0.228 0.319 . 144 . 1424 1280 . 'X-RAY DIFFRACTION' 3.319 3.377 30 100.000 1301 . 0.220 0.319 . 145 . 1446 1301 . 'X-RAY DIFFRACTION' 3.377 3.438 30 100.000 1288 . 0.211 0.285 . 150 . 1438 1288 . 'X-RAY DIFFRACTION' 3.438 3.504 30 100.000 1306 . 0.198 0.298 . 122 . 1428 1306 . 'X-RAY DIFFRACTION' 3.504 3.575 30 100.000 1306 . 0.196 0.284 . 146 . 1452 1306 . 'X-RAY DIFFRACTION' 3.575 3.653 30 100.000 1290 . 0.185 0.252 . 143 . 1433 1290 . 'X-RAY DIFFRACTION' 3.653 3.738 30 100.000 1304 . 0.166 0.254 . 138 . 1442 1304 . 'X-RAY DIFFRACTION' 3.738 3.831 30 100.000 1281 . 0.172 0.238 . 159 . 1440 1281 . 'X-RAY DIFFRACTION' 3.831 3.935 30 100.000 1300 . 0.169 0.234 . 147 . 1447 1300 . 'X-RAY DIFFRACTION' 3.935 4.050 30 100.000 1279 . 0.170 0.248 . 162 . 1441 1279 . 'X-RAY DIFFRACTION' 4.050 4.181 30 99.000 1296 . 0.165 0.222 . 145 . 1441 1296 . 'X-RAY DIFFRACTION' 4.181 4.330 30 100.000 1310 . 0.152 0.248 . 145 . 1455 1310 . 'X-RAY DIFFRACTION' 4.330 4.503 30 99.000 1299 . 0.145 0.198 . 143 . 1442 1299 . 'X-RAY DIFFRACTION' 4.503 4.707 30 100.000 1320 . 0.143 0.210 . 147 . 1467 1320 . 'X-RAY DIFFRACTION' 4.707 4.955 30 100.000 1304 . 0.135 0.206 . 155 . 1459 1304 . 'X-RAY DIFFRACTION' 4.955 5.264 30 100.000 1338 . 0.161 0.241 . 143 . 1481 1338 . 'X-RAY DIFFRACTION' 5.264 5.669 30 100.000 1327 . 0.171 0.248 . 149 . 1476 1327 . 'X-RAY DIFFRACTION' 5.669 6.236 30 100.000 1336 . 0.198 0.297 . 159 . 1495 1336 . 'X-RAY DIFFRACTION' 6.236 7.132 30 100.000 1356 . 0.204 0.253 . 144 . 1500 1356 . 'X-RAY DIFFRACTION' 7.132 8.958 30 100.000 1365 . 0.214 0.306 . 167 . 1532 1365 . 'X-RAY DIFFRACTION' 8.958 34.111 30 97.000 1434 . 0.245 0.276 . 157 . 1591 1434 . 'X-RAY DIFFRACTION' # _struct.entry_id 3A79 _struct.title 'Crystal structure of TLR2-TLR6-Pam2CSK4 complex' _struct.pdbx_descriptor 'Toll-like receptor 2, Variable lymphocyte receptor B, Toll-like receptor 6, Variable lymphocyte receptor B, Pam2CSK4' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 3A79 _struct_keywords.pdbx_keywords 'IMMUNE SYSTEM' _struct_keywords.text ;Toll-like Receptor, diacyl lipopeptide, innate immunity, Leucine Rich Repeat, Cell membrane, Cytoplasmic vesicle, Disulfide bond, Glycoprotein, Immune response, Inflammatory response, LEUCINE-RICH REPEAT, Membrane, Receptor, Transmembrane, Phosphoprotein, IMMUNE SYSTEM ; # 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 3 ? D N N 4 ? E N N 4 ? F N N 4 ? G N N 4 ? H N N 4 ? I N N 4 ? J N N 4 ? K N N 4 ? L N N 4 ? M N N 4 ? N N N 5 ? O N N 4 ? P N N 4 ? Q N N 5 ? R N N 4 ? S N N 4 ? T N N 5 ? U N N 6 ? V N N 4 ? W N N 4 ? X N N 7 ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 GLU A 209 ? ALA A 211 ? GLU A 209 ALA A 211 5 ? 3 HELX_P HELX_P2 2 PHE A 212 ? ILE A 220 ? PHE A 212 ILE A 220 1 ? 9 HELX_P HELX_P3 3 ASP A 263 ? LEU A 270 ? ASP A 263 LEU A 270 1 ? 8 HELX_P HELX_P4 4 LYS A 271 ? TYR A 275 ? LYS A 271 TYR A 275 5 ? 5 HELX_P HELX_P5 5 SER A 298 ? GLU A 305 ? SER A 298 GLU A 305 1 ? 8 HELX_P HELX_P6 6 GLN A 321 ? PHE A 325 ? GLN A 321 PHE A 325 5 ? 5 HELX_P HELX_P7 7 LEU A 328 ? TYR A 332 ? LEU A 328 TYR A 332 5 ? 5 HELX_P HELX_P8 8 PRO A 352 ? LEU A 359 ? PRO A 352 LEU A 359 1 ? 8 HELX_P HELX_P9 9 VAL A 373 ? ALA A 381 ? VAL A 373 ALA A 381 1 ? 9 HELX_P HELX_P10 10 SER A 401 ? LEU A 409 ? SER A 401 LEU A 409 1 ? 9 HELX_P HELX_P11 11 LEU A 410 ? LEU A 412 ? LEU A 410 LEU A 412 5 ? 3 HELX_P HELX_P12 12 ILE A 542 ? ASN A 552 ? ILE A 542 ASN A 552 1 ? 11 HELX_P HELX_P13 13 ARG B 68 ? ILE B 72 ? ARG B 68 ILE B 72 5 ? 5 HELX_P HELX_P14 14 CYS B 139 ? LEU B 145 ? CYS B 139 LEU B 145 5 ? 7 HELX_P HELX_P15 15 LEU B 163 ? ALA B 167 ? LEU B 163 ALA B 167 5 ? 5 HELX_P HELX_P16 16 ASN B 234 ? ARG B 247 ? ASN B 234 ARG B 247 1 ? 14 HELX_P HELX_P17 17 THR B 262 ? TRP B 274 ? THR B 262 TRP B 274 1 ? 13 HELX_P HELX_P18 18 SER B 320 ? GLU B 330 ? SER B 320 GLU B 330 1 ? 11 HELX_P HELX_P19 19 PHE B 393 ? MET B 398 ? PHE B 393 MET B 398 1 ? 6 HELX_P HELX_P20 20 THR B 441 ? ARG B 446 ? THR B 441 ARG B 446 5 ? 6 HELX_P HELX_P21 21 THR B 512 ? HIS B 526 ? THR B 512 HIS B 526 1 ? 15 # _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 30 SG ? ? ? 1_555 A CYS 36 SG ? ? A CYS 30 A CYS 36 1_555 ? ? ? ? ? ? ? 2.034 ? disulf2 disulf ? ? A CYS 353 SG ? ? ? 1_555 A CYS 382 SG ? ? A CYS 353 A CYS 382 1_555 ? ? ? ? ? ? ? 2.047 ? disulf3 disulf ? ? A CYS 432 SG ? ? ? 1_555 A CYS 454 SG ? ? A CYS 432 A CYS 454 1_555 ? ? ? ? ? ? ? 2.045 ? disulf4 disulf ? ? A CYS 537 SG ? ? ? 1_555 A CYS 562 SG ? ? A CYS 537 A CYS 562 1_555 ? ? ? ? ? ? ? 2.030 ? disulf5 disulf ? ? A CYS 539 SG ? ? ? 1_555 A CYS 574 SG ? ? A CYS 539 A CYS 574 1_555 ? ? ? ? ? ? ? 2.032 ? disulf6 disulf ? ? B CYS 117 SG ? ? ? 1_555 B CYS 139 SG ? ? B CYS 117 B CYS 139 1_555 ? ? ? ? ? ? ? 2.043 ? disulf7 disulf ? ? B CYS 235 SG ? ? ? 1_555 B CYS 265 SG ? ? B CYS 235 B CYS 265 1_555 ? ? ? ? ? ? ? 2.058 ? disulf8 disulf ? ? B CYS 348 SG ? ? ? 1_555 B CYS 373 SG ? ? B CYS 348 B CYS 373 1_555 ? ? ? ? ? ? ? 2.033 ? disulf9 disulf ? ? B CYS 424 SG ? ? ? 1_555 B CYS 447 SG ? ? B CYS 424 B CYS 447 1_555 ? ? ? ? ? ? ? 2.042 ? disulf10 disulf ? ? B CYS 511 SG ? ? ? 1_555 B CYS 544 SG ? ? B CYS 511 B CYS 544 1_555 ? ? ? ? ? ? ? 2.032 ? disulf11 disulf ? ? B CYS 513 SG ? ? ? 1_555 B CYS 556 SG ? ? B CYS 513 B CYS 556 1_555 ? ? ? ? ? ? ? 2.033 ? covale1 covale ? ? A ASN 147 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 147 A NAG 811 1_555 ? ? ? ? ? ? ? 1.448 ? covale2 covale ? ? A ASN 414 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 414 A NAG 821 1_555 ? ? ? ? ? ? ? 1.444 ? covale3 covale ? ? A ASN 442 ND2 ? ? ? 1_555 F NAG . C1 ? ? A ASN 442 A NAG 831 1_555 ? ? ? ? ? ? ? 1.449 ? covale4 covale ? ? B ASN 144 ND2 ? ? ? 1_555 H NAG . C1 ? ? B ASN 144 B NAG 911 1_555 ? ? ? ? ? ? ? 1.460 ? covale5 covale ? ? B ASN 195 ND2 ? ? ? 1_555 W NAG . C1 ? ? B ASN 195 B NAG 981 1_555 ? ? ? ? ? ? ? 1.466 ? covale6 covale ? ? B ASN 214 ND2 ? ? ? 1_555 I NAG . C1 ? ? B ASN 214 B NAG 921 1_555 ? ? ? ? ? ? ? 1.456 ? covale7 covale ? ? B ASN 253 ND2 ? ? ? 1_555 J NAG . C1 ? ? B ASN 253 B NAG 931 1_555 ? ? ? ? ? ? ? 1.450 ? covale8 covale ? ? B ASN 285 ND2 ? ? ? 1_555 L NAG . C1 ? ? B ASN 285 B NAG 941 1_555 ? ? ? ? ? ? ? 1.446 ? covale9 covale ? ? B ASN 359 ND2 ? ? ? 1_555 O NAG . C1 ? ? B ASN 359 B NAG 951 1_555 ? ? ? ? ? ? ? 1.447 ? covale10 covale ? ? B ASN 401 ND2 ? ? ? 1_555 R NAG . C1 ? ? B ASN 401 B NAG 961 1_555 ? ? ? ? ? ? ? 1.452 ? covale11 covale ? ? B ASN 434 ND2 ? ? ? 1_555 U NDG . C1 ? ? B ASN 434 B NDG 971 1_555 ? ? ? ? ? ? ? 1.445 ? covale12 covale ? ? F NAG . O4 ? ? ? 1_555 G NAG . C1 ? ? A NAG 831 A NAG 832 1_555 ? ? ? ? ? ? ? 1.437 ? covale13 covale ? ? J NAG . O4 ? ? ? 1_555 K NAG . C1 ? ? B NAG 931 B NAG 932 1_555 ? ? ? ? ? ? ? 1.457 ? covale14 covale ? ? L NAG . O4 ? ? ? 1_555 M NAG . C1 ? ? B NAG 941 B NAG 942 1_555 ? ? ? ? ? ? ? 1.435 ? covale15 covale ? ? O NAG . O4 ? ? ? 1_555 P NAG . C1 ? ? B NAG 951 B NAG 952 1_555 ? ? ? ? ? ? ? 1.447 ? covale16 covale ? ? R NAG . O4 ? ? ? 1_555 S NAG . C1 ? ? B NAG 961 B NAG 962 1_555 ? ? ? ? ? ? ? 1.448 ? covale17 covale ? ? M NAG . O4 ? ? ? 1_555 N BMA . C1 ? ? B NAG 942 B BMA 943 1_555 ? ? ? ? ? ? ? 1.436 ? covale18 covale ? ? P NAG . O4 ? ? ? 1_555 Q BMA . C1 ? ? B NAG 952 B BMA 953 1_555 ? ? ? ? ? ? ? 1.441 ? covale19 covale ? ? S NAG . O4 ? ? ? 1_555 T BMA . C1 ? ? B NAG 962 B BMA 963 1_555 ? ? ? ? ? ? ? 1.450 ? covale20 covale ? ? U NDG . O4 ? ? ? 1_555 V NAG . C1 ? ? B NDG 971 B NAG 972 1_555 ? ? ? ? ? ? ? 1.450 ? covale21 covale ? ? C CYS 1 SG ? ? ? 1_555 X PXS . C20 ? ? C CYS 11 C PXS 581 1_555 ? ? ? ? ? ? ? 1.784 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 19 ? B ? 2 ? C ? 2 ? D ? 2 ? E ? 2 ? F ? 19 ? G ? 2 ? H ? 2 ? I ? 2 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? parallel A 2 3 ? parallel A 3 4 ? parallel A 4 5 ? parallel A 5 6 ? parallel A 6 7 ? parallel A 7 8 ? parallel A 8 9 ? parallel A 9 10 ? parallel A 10 11 ? parallel A 11 12 ? parallel A 12 13 ? parallel A 13 14 ? parallel A 14 15 ? parallel A 15 16 ? parallel A 16 17 ? parallel A 17 18 ? parallel A 18 19 ? parallel B 1 2 ? parallel C 1 2 ? parallel D 1 2 ? parallel E 1 2 ? parallel F 1 2 ? parallel F 2 3 ? parallel F 3 4 ? parallel F 4 5 ? parallel F 5 6 ? parallel F 6 7 ? parallel F 7 8 ? parallel F 8 9 ? parallel F 9 10 ? parallel F 10 11 ? parallel F 11 12 ? parallel F 12 13 ? parallel F 13 14 ? parallel F 14 15 ? parallel F 15 16 ? parallel F 16 17 ? parallel F 17 18 ? parallel F 18 19 ? parallel G 1 2 ? parallel H 1 2 ? parallel I 1 2 ? parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 VAL A 35 ? ASP A 37 ? VAL A 35 ASP A 37 A 2 SER A 56 ? ASP A 58 ? SER A 56 ASP A 58 A 3 VAL A 80 ? ILE A 82 ? VAL A 80 ILE A 82 A 4 HIS A 104 ? ASP A 106 ? HIS A 104 ASP A 106 A 5 TYR A 128 ? ASN A 130 ? TYR A 128 ASN A 130 A 6 THR A 153 ? ASN A 158 ? THR A 153 ASN A 158 A 7 SER A 175 ? ALA A 183 ? SER A 175 ALA A 183 A 8 ASP A 199 ? HIS A 206 ? ASP A 199 HIS A 206 A 9 TYR A 226 ? ARG A 230 ? TYR A 226 ARG A 230 A 10 LYS A 253 ? PHE A 256 ? LYS A 253 PHE A 256 A 11 GLU A 281 ? PHE A 284 ? GLU A 281 PHE A 284 A 12 THR A 311 ? ARG A 315 ? THR A 311 ARG A 315 A 13 ARG A 340 ? GLU A 344 ? ARG A 340 GLU A 344 A 14 PHE A 364 ? ASP A 366 ? PHE A 364 ASP A 366 A 15 THR A 391 ? VAL A 393 ? THR A 391 VAL A 393 A 16 SER A 417 ? ASP A 419 ? SER A 417 ASP A 419 A 17 PHE A 440 ? ASN A 442 ? PHE A 440 ASN A 442 A 18 VAL A 461 ? ASP A 463 ? VAL A 461 ASP A 463 A 19 GLU A 481 ? TYR A 483 ? GLU A 481 TYR A 483 B 1 TYR A 66 ? ILE A 67 ? TYR A 66 ILE A 67 B 2 THR A 90 ? ILE A 91 ? THR A 90 ILE A 91 C 1 GLU A 164 ? ILE A 165 ? GLU A 164 ILE A 165 C 2 ASN A 188 ? TYR A 189 ? ASN A 188 TYR A 189 D 1 VAL A 260 ? THR A 262 ? VAL A 260 THR A 262 D 2 THR A 288 ? ASN A 290 ? THR A 288 ASN A 290 E 1 VAL A 503 ? LYS A 505 ? VAL A 503 LYS A 505 E 2 LYS A 527 ? TRP A 529 ? LYS A 527 TRP A 529 F 1 MET B 35 ? ASP B 37 ? MET B 35 ASP B 37 F 2 ALA B 56 ? SER B 58 ? ALA B 56 SER B 58 F 3 VAL B 80 ? ARG B 82 ? VAL B 80 ARG B 82 F 4 TYR B 104 ? ASP B 106 ? TYR B 104 ASP B 106 F 5 HIS B 125 ? ASP B 127 ? HIS B 125 ASP B 127 F 6 PHE B 150 ? SER B 154 ? PHE B 150 SER B 154 F 7 LEU B 171 ? LEU B 178 ? LEU B 171 LEU B 178 F 8 THR B 196 ? PHE B 203 ? THR B 196 PHE B 203 F 9 LEU B 220 ? LYS B 229 ? LEU B 220 LYS B 229 F 10 LEU B 252 ? THR B 261 ? LEU B 252 THR B 261 F 11 VAL B 278 ? ILE B 288 ? VAL B 278 ILE B 288 F 12 SER B 306 ? ASN B 314 ? SER B 306 ASN B 314 F 13 MET B 335 ? SER B 339 ? MET B 335 SER B 339 F 14 PHE B 357 ? ASN B 359 ? PHE B 357 ASN B 359 F 15 THR B 381 ? ILE B 383 ? THR B 381 ILE B 383 F 16 THR B 407 ? ASP B 409 ? THR B 407 ASP B 409 F 17 VAL B 432 ? ASN B 434 ? VAL B 432 ASN B 434 F 18 VAL B 454 ? ASP B 456 ? VAL B 454 ASP B 456 F 19 GLU B 477 ? ASN B 479 ? GLU B 477 ASN B 479 G 1 SER B 90 ? LEU B 91 ? SER B 90 LEU B 91 G 2 ASN B 114 ? ILE B 115 ? ASN B 114 ILE B 115 H 1 SER B 190 ? ILE B 193 ? SER B 190 ILE B 193 H 2 ASN B 214 ? VAL B 217 ? ASN B 214 VAL B 217 I 1 ILE B 502 ? TRP B 503 ? ILE B 502 TRP B 503 I 2 VAL B 530 ? ARG B 531 ? VAL B 530 ARG B 531 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 N CYS A 36 ? N CYS A 36 O ASP A 58 ? O ASP A 58 A 2 3 N LEU A 57 ? N LEU A 57 O ILE A 82 ? O ILE A 82 A 3 4 N LEU A 81 ? N LEU A 81 O HIS A 104 ? O HIS A 104 A 4 5 N LEU A 105 ? N LEU A 105 O TYR A 128 ? O TYR A 128 A 5 6 N LEU A 129 ? N LEU A 129 O THR A 153 ? O THR A 153 A 6 7 N ILE A 156 ? N ILE A 156 O LYS A 182 ? O LYS A 182 A 7 8 N LEU A 179 ? N LEU A 179 O THR A 204 ? O THR A 204 A 8 9 N LEU A 205 ? N LEU A 205 O ARG A 230 ? O ARG A 230 A 9 10 N LEU A 229 ? N LEU A 229 O ALA A 255 ? O ALA A 255 A 10 11 N PHE A 256 ? N PHE A 256 O GLU A 283 ? O GLU A 283 A 11 12 N VAL A 282 ? N VAL A 282 O THR A 313 ? O THR A 313 A 12 13 N ILE A 314 ? N ILE A 314 O THR A 342 ? O THR A 342 A 13 14 N VAL A 343 ? N VAL A 343 O ASP A 366 ? O ASP A 366 A 14 15 N LEU A 365 ? N LEU A 365 O VAL A 393 ? O VAL A 393 A 15 16 N LEU A 392 ? N LEU A 392 O SER A 417 ? O SER A 417 A 16 17 N LEU A 418 ? N LEU A 418 O PHE A 440 ? O PHE A 440 A 17 18 N LEU A 441 ? N LEU A 441 O VAL A 461 ? O VAL A 461 A 18 19 N LEU A 462 ? N LEU A 462 O TYR A 483 ? O TYR A 483 B 1 2 N ILE A 67 ? N ILE A 67 O THR A 90 ? O THR A 90 C 1 2 N ILE A 165 ? N ILE A 165 O ASN A 188 ? O ASN A 188 D 1 2 N LEU A 261 ? N LEU A 261 O THR A 288 ? O THR A 288 E 1 2 N MET A 504 ? N MET A 504 O TRP A 529 ? O TRP A 529 F 1 2 N VAL B 36 ? N VAL B 36 O ALA B 56 ? O ALA B 56 F 2 3 N LEU B 57 ? N LEU B 57 O VAL B 80 ? O VAL B 80 F 3 4 N LEU B 81 ? N LEU B 81 O TYR B 104 ? O TYR B 104 F 4 5 N LEU B 105 ? N LEU B 105 O HIS B 125 ? O HIS B 125 F 5 6 N LEU B 126 ? N LEU B 126 O PHE B 150 ? O PHE B 150 F 6 7 N LEU B 153 ? N LEU B 153 O LEU B 175 ? O LEU B 175 F 7 8 N LEU B 178 ? N LEU B 178 O VAL B 202 ? O VAL B 202 F 8 9 N LEU B 201 ? N LEU B 201 O GLN B 224 ? O GLN B 224 F 9 10 N GLY B 221 ? N GLY B 221 O ASN B 253 ? O ASN B 253 F 10 11 N VAL B 254 ? N VAL B 254 O ASN B 282 ? O ASN B 282 F 11 12 N LEU B 281 ? N LEU B 281 O SER B 306 ? O SER B 306 F 12 13 N ILE B 309 ? N ILE B 309 O SER B 337 ? O SER B 337 F 13 14 N LEU B 336 ? N LEU B 336 O PHE B 357 ? O PHE B 357 F 14 15 N LEU B 358 ? N LEU B 358 O THR B 381 ? O THR B 381 F 15 16 N LEU B 382 ? N LEU B 382 O THR B 407 ? O THR B 407 F 16 17 N LEU B 408 ? N LEU B 408 O VAL B 432 ? O VAL B 432 F 17 18 N LEU B 433 ? N LEU B 433 O VAL B 454 ? O VAL B 454 F 18 19 N LEU B 455 ? N LEU B 455 O ASN B 479 ? O ASN B 479 G 1 2 N LEU B 91 ? N LEU B 91 O ASN B 114 ? O ASN B 114 H 1 2 N ILE B 193 ? N ILE B 193 O SER B 216 ? O SER B 216 I 1 2 N ILE B 502 ? N ILE B 502 O ARG B 531 ? O ARG B 531 # 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 ? ? ? ? 16 'BINDING SITE FOR RESIDUE PXS C 581' AC2 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG A 811' AC3 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 821' AC4 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 831' AC5 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 832' AC6 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG B 911' AC7 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG B 921' AC8 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG B 931' AC9 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG B 932' BC1 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG B 941' BC2 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG B 942' BC3 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE BMA B 943' BC4 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG B 951' BC5 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG B 952' BC6 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE BMA B 953' BC7 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG B 961' BC8 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG B 962' BC9 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE BMA B 963' CC1 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NDG B 971' CC2 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG B 972' CC3 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG B 981' # 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 16 THR A 262 ? THR A 262 . ? 1_555 ? 2 AC1 16 PHE A 266 ? PHE A 266 . ? 1_555 ? 3 AC1 16 LEU A 269 ? LEU A 269 . ? 1_555 ? 4 AC1 16 PHE A 284 ? PHE A 284 . ? 1_555 ? 5 AC1 16 ILE A 319 ? ILE A 319 . ? 1_555 ? 6 AC1 16 PHE A 325 ? PHE A 325 . ? 1_555 ? 7 AC1 16 TYR A 326 ? TYR A 326 . ? 1_555 ? 8 AC1 16 SER A 346 ? SER A 346 . ? 1_555 ? 9 AC1 16 LYS A 347 ? LYS A 347 . ? 1_555 ? 10 AC1 16 VAL A 348 ? VAL A 348 . ? 1_555 ? 11 AC1 16 PHE A 349 ? PHE A 349 . ? 1_555 ? 12 AC1 16 LEU A 350 ? LEU A 350 . ? 1_555 ? 13 AC1 16 VAL A 351 ? VAL A 351 . ? 1_555 ? 14 AC1 16 PRO A 352 ? PRO A 352 . ? 1_555 ? 15 AC1 16 PHE A 355 ? PHE A 355 . ? 1_555 ? 16 AC1 16 CYS C 1 ? CYS C 11 . ? 1_555 ? 17 AC2 1 ASN A 147 ? ASN A 147 . ? 1_555 ? 18 AC3 3 SER A 388 ? SER A 388 . ? 1_555 ? 19 AC3 3 LYS A 413 ? LYS A 413 . ? 1_555 ? 20 AC3 3 ASN A 414 ? ASN A 414 . ? 1_555 ? 21 AC4 5 SER A 421 ? SER A 421 . ? 1_555 ? 22 AC4 5 PHE A 440 ? PHE A 440 . ? 1_555 ? 23 AC4 5 ASN A 442 ? ASN A 442 . ? 1_555 ? 24 AC4 5 ASP A 463 ? ASP A 463 . ? 1_555 ? 25 AC4 5 NAG G . ? NAG A 832 . ? 1_555 ? 26 AC5 3 ARG A 422 ? ARG A 422 . ? 1_555 ? 27 AC5 3 ARG A 486 ? ARG A 486 . ? 1_555 ? 28 AC5 3 NAG F . ? NAG A 831 . ? 1_555 ? 29 AC6 4 CYS B 118 ? CYS B 118 . ? 1_555 ? 30 AC6 4 ALA B 121 ? ALA B 121 . ? 1_555 ? 31 AC6 4 ASN B 144 ? ASN B 144 . ? 1_555 ? 32 AC6 4 GLN B 160 ? GLN B 160 . ? 11_655 ? 33 AC7 3 GLN B 160 ? GLN B 160 . ? 1_555 ? 34 AC7 3 ASN B 214 ? ASN B 214 . ? 1_555 ? 35 AC7 3 SER B 216 ? SER B 216 . ? 1_555 ? 36 AC8 4 ASN B 253 ? ASN B 253 . ? 1_555 ? 37 AC8 4 GLU B 279 ? GLU B 279 . ? 1_555 ? 38 AC8 4 TYR B 280 ? TYR B 280 . ? 1_555 ? 39 AC8 4 NAG K . ? NAG B 932 . ? 1_555 ? 40 AC9 1 NAG J . ? NAG B 931 . ? 1_555 ? 41 BC1 3 HIS B 258 ? HIS B 258 . ? 1_555 ? 42 BC1 3 ASN B 285 ? ASN B 285 . ? 1_555 ? 43 BC1 3 NAG M . ? NAG B 942 . ? 1_555 ? 44 BC2 3 ASN B 206 ? ASN B 206 . ? 1_555 ? 45 BC2 3 NAG L . ? NAG B 941 . ? 1_555 ? 46 BC2 3 BMA N . ? BMA B 943 . ? 1_555 ? 47 BC3 2 ASN B 206 ? ASN B 206 . ? 1_555 ? 48 BC3 2 NAG M . ? NAG B 942 . ? 1_555 ? 49 BC4 6 GLU B 310 ? GLU B 310 . ? 1_555 ? 50 BC4 6 SER B 339 ? SER B 339 . ? 1_555 ? 51 BC4 6 PHE B 357 ? PHE B 357 . ? 1_555 ? 52 BC4 6 ASN B 359 ? ASN B 359 . ? 1_555 ? 53 BC4 6 ILE B 383 ? ILE B 383 . ? 1_555 ? 54 BC4 6 NAG P . ? NAG B 952 . ? 1_555 ? 55 BC5 5 GLU B 310 ? GLU B 310 . ? 1_555 ? 56 BC5 5 GLN B 362 ? GLN B 362 . ? 1_555 ? 57 BC5 5 ARG B 386 ? ARG B 386 . ? 1_555 ? 58 BC5 5 NAG O . ? NAG B 951 . ? 1_555 ? 59 BC5 5 BMA Q . ? BMA B 953 . ? 1_555 ? 60 BC6 1 NAG P . ? NAG B 952 . ? 1_555 ? 61 BC7 4 SER B 374 ? SER B 374 . ? 1_555 ? 62 BC7 4 LYS B 377 ? LYS B 377 . ? 1_555 ? 63 BC7 4 ASN B 401 ? ASN B 401 . ? 1_555 ? 64 BC7 4 NAG S . ? NAG B 962 . ? 1_555 ? 65 BC8 2 NAG R . ? NAG B 961 . ? 1_555 ? 66 BC8 2 BMA T . ? BMA B 963 . ? 1_555 ? 67 BC9 1 NAG S . ? NAG B 962 . ? 1_555 ? 68 CC1 6 SER B 411 ? SER B 411 . ? 1_555 ? 69 CC1 6 LEU B 412 ? LEU B 412 . ? 1_555 ? 70 CC1 6 ASN B 434 ? ASN B 434 . ? 1_555 ? 71 CC1 6 SER B 436 ? SER B 436 . ? 1_555 ? 72 CC1 6 ASP B 456 ? ASP B 456 . ? 1_555 ? 73 CC1 6 NAG V . ? NAG B 972 . ? 1_555 ? 74 CC2 2 HIS B 458 ? HIS B 458 . ? 1_555 ? 75 CC2 2 NDG U . ? NDG B 971 . ? 1_555 ? 76 CC3 2 ASN B 195 ? ASN B 195 . ? 1_555 ? 77 CC3 2 ASN B 218 ? ASN B 218 . ? 1_555 ? # _atom_sites.entry_id 3A79 _atom_sites.fract_transf_matrix[1][1] 0.005921 _atom_sites.fract_transf_matrix[1][2] 0.003418 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.006837 _atom_sites.fract_transf_matrix[2][3] 0.000000 _atom_sites.fract_transf_matrix[3][1] 0.000000 _atom_sites.fract_transf_matrix[3][2] 0.000000 _atom_sites.fract_transf_matrix[3][3] 0.004322 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O S # 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 . GLU A 1 26 ? 9.500 -2.927 -4.496 1.00 140.42 ? 26 GLU A N 1 ATOM 2 C CA . GLU A 1 26 ? 8.332 -2.391 -5.197 1.00 147.01 ? 26 GLU A CA 1 ATOM 3 C C . GLU A 1 26 ? 7.822 -3.357 -6.270 1.00 153.39 ? 26 GLU A C 1 ATOM 4 O O . GLU A 1 26 ? 6.981 -2.998 -7.101 1.00 153.22 ? 26 GLU A O 1 ATOM 5 C CB . GLU A 1 26 ? 8.642 -1.015 -5.809 1.00 142.84 ? 26 GLU A CB 1 ATOM 6 C CG . GLU A 1 26 ? 9.812 -0.981 -6.797 1.00 135.30 ? 26 GLU A CG 1 ATOM 7 C CD . GLU A 1 26 ? 9.427 -1.408 -8.211 1.00 128.98 ? 26 GLU A CD 1 ATOM 8 O OE1 . GLU A 1 26 ? 8.221 -1.463 -8.528 1.00 126.66 ? 26 GLU A OE1 1 ATOM 9 O OE2 . GLU A 1 26 ? 10.337 -1.683 -9.015 1.00 125.67 ? 26 GLU A OE2 1 ATOM 10 N N . SER A 1 27 ? 8.320 -4.592 -6.225 1.00 150.45 ? 27 SER A N 1 ATOM 11 C CA . SER A 1 27 ? 8.066 -5.570 -7.278 1.00 141.22 ? 27 SER A CA 1 ATOM 12 C C . SER A 1 27 ? 7.522 -6.897 -6.756 1.00 134.74 ? 27 SER A C 1 ATOM 13 O O . SER A 1 27 ? 8.080 -7.491 -5.833 1.00 131.85 ? 27 SER A O 1 ATOM 14 C CB . SER A 1 27 ? 9.363 -5.839 -8.043 1.00 136.46 ? 27 SER A CB 1 ATOM 15 O OG . SER A 1 27 ? 10.363 -6.356 -7.174 1.00 125.93 ? 27 SER A OG 1 ATOM 16 N N . LEU A 1 28 ? 6.435 -7.367 -7.358 1.00 131.26 ? 28 LEU A N 1 ATOM 17 C CA . LEU A 1 28 ? 5.987 -8.738 -7.138 1.00 126.71 ? 28 LEU A CA 1 ATOM 18 C C . LEU A 1 28 ? 6.471 -9.575 -8.322 1.00 124.27 ? 28 LEU A C 1 ATOM 19 O O . LEU A 1 28 ? 6.417 -9.128 -9.471 1.00 125.95 ? 28 LEU A O 1 ATOM 20 C CB . LEU A 1 28 ? 4.457 -8.805 -7.018 1.00 118.27 ? 28 LEU A CB 1 ATOM 21 C CG . LEU A 1 28 ? 3.761 -9.978 -6.305 1.00 95.72 ? 28 LEU A CG 1 ATOM 22 C CD1 . LEU A 1 28 ? 2.256 -9.814 -6.385 1.00 84.72 ? 28 LEU A CD1 1 ATOM 23 C CD2 . LEU A 1 28 ? 4.154 -11.326 -6.876 1.00 88.68 ? 28 LEU A CD2 1 ATOM 24 N N . SER A 1 29 ? 6.950 -10.783 -8.041 1.00 117.30 ? 29 SER A N 1 ATOM 25 C CA . SER A 1 29 ? 7.445 -11.674 -9.089 1.00 111.73 ? 29 SER A CA 1 ATOM 26 C C . SER A 1 29 ? 6.408 -12.729 -9.496 1.00 113.60 ? 29 SER A C 1 ATOM 27 O O . SER A 1 29 ? 5.270 -12.395 -9.836 1.00 116.68 ? 29 SER A O 1 ATOM 28 C CB . SER A 1 29 ? 8.708 -12.381 -8.618 1.00 89.99 ? 29 SER A CB 1 ATOM 29 O OG . SER A 1 29 ? 8.349 -13.504 -7.846 1.00 75.46 ? 29 SER A OG 1 ATOM 30 N N . CYS A 1 30 ? 6.835 -13.993 -9.476 1.00 103.60 ? 30 CYS A N 1 ATOM 31 C CA . CYS A 1 30 ? 5.987 -15.158 -9.731 1.00 107.94 ? 30 CYS A CA 1 ATOM 32 C C . CYS A 1 30 ? 6.739 -16.216 -10.550 1.00 126.02 ? 30 CYS A C 1 ATOM 33 O O . CYS A 1 30 ? 7.893 -16.010 -10.926 1.00 132.17 ? 30 CYS A O 1 ATOM 34 C CB . CYS A 1 30 ? 4.663 -14.778 -10.410 1.00 95.65 ? 30 CYS A CB 1 ATOM 35 S SG . CYS A 1 30 ? 3.263 -15.795 -9.871 1.00 231.48 ? 30 CYS A SG 1 ATOM 36 N N . ASP A 1 31 ? 6.090 -17.355 -10.799 1.00 129.45 ? 31 ASP A N 1 ATOM 37 C CA . ASP A 1 31 ? 6.658 -18.411 -11.642 1.00 120.56 ? 31 ASP A CA 1 ATOM 38 C C . ASP A 1 31 ? 5.578 -19.131 -12.468 1.00 122.15 ? 31 ASP A C 1 ATOM 39 O O . ASP A 1 31 ? 4.391 -18.802 -12.375 1.00 118.28 ? 31 ASP A O 1 ATOM 40 C CB . ASP A 1 31 ? 7.534 -19.391 -10.831 1.00 109.20 ? 31 ASP A CB 1 ATOM 41 C CG . ASP A 1 31 ? 6.725 -20.429 -10.049 1.00 106.85 ? 31 ASP A CG 1 ATOM 42 O OD1 . ASP A 1 31 ? 7.241 -20.917 -9.017 1.00 98.10 ? 31 ASP A OD1 1 ATOM 43 O OD2 . ASP A 1 31 ? 5.596 -20.776 -10.461 1.00 108.64 ? 31 ASP A OD2 1 ATOM 44 N N . ALA A 1 32 ? 6.001 -20.103 -13.275 1.00 125.48 ? 32 ALA A N 1 ATOM 45 C CA . ALA A 1 32 ? 5.120 -20.766 -14.241 1.00 117.00 ? 32 ALA A CA 1 ATOM 46 C C . ALA A 1 32 ? 3.946 -21.507 -13.593 1.00 111.65 ? 32 ALA A C 1 ATOM 47 O O . ALA A 1 32 ? 2.792 -21.331 -14.008 1.00 97.94 ? 32 ALA A O 1 ATOM 48 C CB . ALA A 1 32 ? 5.927 -21.708 -15.142 1.00 110.73 ? 32 ALA A CB 1 ATOM 49 N N . SER A 1 33 ? 4.252 -22.332 -12.588 1.00 110.85 ? 33 SER A N 1 ATOM 50 C CA . SER A 1 33 ? 3.241 -23.073 -11.828 1.00 102.57 ? 33 SER A CA 1 ATOM 51 C C . SER A 1 33 ? 2.102 -22.169 -11.370 1.00 102.29 ? 33 SER A C 1 ATOM 52 O O . SER A 1 33 ? 0.920 -22.464 -11.584 1.00 98.25 ? 33 SER A O 1 ATOM 53 C CB . SER A 1 33 ? 3.877 -23.746 -10.609 1.00 90.65 ? 33 SER A CB 1 ATOM 54 O OG . SER A 1 33 ? 4.209 -25.093 -10.879 1.00 91.92 ? 33 SER A OG 1 ATOM 55 N N . GLY A 1 34 ? 2.473 -21.063 -10.737 1.00 96.51 ? 34 GLY A N 1 ATOM 56 C CA . GLY A 1 34 ? 1.507 -20.113 -10.228 1.00 93.95 ? 34 GLY A CA 1 ATOM 57 C C . GLY A 1 34 ? 1.929 -19.697 -8.841 1.00 92.20 ? 34 GLY A C 1 ATOM 58 O O . GLY A 1 34 ? 1.105 -19.250 -8.045 1.00 93.96 ? 34 GLY A O 1 ATOM 59 N N . VAL A 1 35 ? 3.223 -19.845 -8.561 1.00 83.40 ? 35 VAL A N 1 ATOM 60 C CA . VAL A 1 35 ? 3.769 -19.576 -7.232 1.00 81.45 ? 35 VAL A CA 1 ATOM 61 C C . VAL A 1 35 ? 4.410 -18.186 -7.128 1.00 76.99 ? 35 VAL A C 1 ATOM 62 O O . VAL A 1 35 ? 5.628 -18.028 -7.211 1.00 70.98 ? 35 VAL A O 1 ATOM 63 C CB . VAL A 1 35 ? 4.773 -20.682 -6.781 1.00 70.51 ? 35 VAL A CB 1 ATOM 64 C CG1 . VAL A 1 35 ? 5.299 -20.400 -5.360 1.00 59.16 ? 35 VAL A CG1 1 ATOM 65 C CG2 . VAL A 1 35 ? 4.137 -22.080 -6.881 1.00 51.79 ? 35 VAL A CG2 1 ATOM 66 N N . CYS A 1 36 ? 3.568 -17.179 -6.941 1.00 86.20 ? 36 CYS A N 1 ATOM 67 C CA . CYS A 1 36 ? 4.023 -15.801 -6.823 1.00 84.54 ? 36 CYS A CA 1 ATOM 68 C C . CYS A 1 36 ? 4.758 -15.562 -5.500 1.00 84.76 ? 36 CYS A C 1 ATOM 69 O O . CYS A 1 36 ? 4.329 -16.035 -4.456 1.00 88.36 ? 36 CYS A O 1 ATOM 70 C CB . CYS A 1 36 ? 2.831 -14.849 -6.956 1.00 70.55 ? 36 CYS A CB 1 ATOM 71 S SG . CYS A 1 36 ? 2.197 -14.567 -8.649 1.00 170.76 ? 36 CYS A SG 1 ATOM 72 N N . ASP A 1 37 ? 5.866 -14.829 -5.552 1.00 88.74 ? 37 ASP A N 1 ATOM 73 C CA . ASP A 1 37 ? 6.640 -14.505 -4.351 1.00 84.24 ? 37 ASP A CA 1 ATOM 74 C C . ASP A 1 37 ? 6.809 -12.990 -4.150 1.00 92.11 ? 37 ASP A C 1 ATOM 75 O O . ASP A 1 37 ? 7.650 -12.358 -4.785 1.00 103.42 ? 37 ASP A O 1 ATOM 76 C CB . ASP A 1 37 ? 8.013 -15.192 -4.399 1.00 81.72 ? 37 ASP A CB 1 ATOM 77 C CG . ASP A 1 37 ? 8.995 -14.623 -3.377 1.00 95.52 ? 37 ASP A CG 1 ATOM 78 O OD1 . ASP A 1 37 ? 8.543 -14.105 -2.332 1.00 99.08 ? 37 ASP A OD1 1 ATOM 79 O OD2 . ASP A 1 37 ? 10.224 -14.695 -3.618 1.00 99.29 ? 37 ASP A OD2 1 ATOM 80 N N . GLY A 1 38 ? 6.015 -12.407 -3.260 1.00 85.95 ? 38 GLY A N 1 ATOM 81 C CA . GLY A 1 38 ? 6.160 -10.997 -2.951 1.00 88.26 ? 38 GLY A CA 1 ATOM 82 C C . GLY A 1 38 ? 6.683 -10.758 -1.547 1.00 94.03 ? 38 GLY A C 1 ATOM 83 O O . GLY A 1 38 ? 6.103 -9.975 -0.792 1.00 92.30 ? 38 GLY A O 1 ATOM 84 N N . ARG A 1 39 ? 7.786 -11.420 -1.200 1.00 100.09 ? 39 ARG A N 1 ATOM 85 C CA . ARG A 1 39 ? 8.318 -11.381 0.163 1.00 98.87 ? 39 ARG A CA 1 ATOM 86 C C . ARG A 1 39 ? 8.675 -9.963 0.625 1.00 102.94 ? 39 ARG A C 1 ATOM 87 O O . ARG A 1 39 ? 7.810 -9.093 0.668 1.00 122.66 ? 39 ARG A O 1 ATOM 88 C CB . ARG A 1 39 ? 9.517 -12.319 0.315 1.00 103.69 ? 39 ARG A CB 1 ATOM 89 C CG . ARG A 1 39 ? 9.498 -13.155 1.597 1.00 104.68 ? 39 ARG A CG 1 ATOM 90 C CD . ARG A 1 39 ? 8.843 -14.522 1.369 1.00 102.77 ? 39 ARG A CD 1 ATOM 91 N NE . ARG A 1 39 ? 9.811 -15.611 1.199 1.00 94.26 ? 39 ARG A NE 1 ATOM 92 C CZ . ARG A 1 39 ? 10.572 -15.794 0.119 1.00 90.12 ? 39 ARG A CZ 1 ATOM 93 N NH1 . ARG A 1 39 ? 10.511 -14.950 -0.901 1.00 99.35 ? 39 ARG A NH1 1 ATOM 94 N NH2 . ARG A 1 39 ? 11.411 -16.817 0.061 1.00 79.86 ? 39 ARG A NH2 1 ATOM 95 N N . SER A 1 40 ? 9.937 -9.717 0.960 1.00 84.44 ? 40 SER A N 1 ATOM 96 C CA . SER A 1 40 ? 10.262 -8.508 1.717 1.00 87.35 ? 40 SER A CA 1 ATOM 97 C C . SER A 1 40 ? 10.306 -7.178 0.963 1.00 103.16 ? 40 SER A C 1 ATOM 98 O O . SER A 1 40 ? 10.906 -6.218 1.455 1.00 110.46 ? 40 SER A O 1 ATOM 99 C CB . SER A 1 40 ? 11.537 -8.692 2.543 1.00 86.92 ? 40 SER A CB 1 ATOM 100 O OG . SER A 1 40 ? 11.227 -9.008 3.893 1.00 78.30 ? 40 SER A OG 1 ATOM 101 N N . ARG A 1 41 ? 9.669 -7.108 -0.205 1.00 108.76 ? 41 ARG A N 1 ATOM 102 C CA . ARG A 1 41 ? 9.444 -5.819 -0.866 1.00 117.33 ? 41 ARG A CA 1 ATOM 103 C C . ARG A 1 41 ? 8.585 -4.961 0.053 1.00 117.53 ? 41 ARG A C 1 ATOM 104 O O . ARG A 1 41 ? 7.457 -5.336 0.369 1.00 125.51 ? 41 ARG A O 1 ATOM 105 C CB . ARG A 1 41 ? 8.717 -5.997 -2.199 1.00 122.53 ? 41 ARG A CB 1 ATOM 106 C CG . ARG A 1 41 ? 9.527 -6.661 -3.294 1.00 129.56 ? 41 ARG A CG 1 ATOM 107 C CD . ARG A 1 41 ? 9.725 -8.139 -3.017 1.00 132.55 ? 41 ARG A CD 1 ATOM 108 N NE . ARG A 1 41 ? 9.917 -8.901 -4.247 1.00 133.64 ? 41 ARG A NE 1 ATOM 109 C CZ . ARG A 1 41 ? 10.446 -10.118 -4.294 1.00 127.56 ? 41 ARG A CZ 1 ATOM 110 N NH1 . ARG A 1 41 ? 10.851 -10.713 -3.177 1.00 121.94 ? 41 ARG A NH1 1 ATOM 111 N NH2 . ARG A 1 41 ? 10.577 -10.734 -5.462 1.00 123.53 ? 41 ARG A NH2 1 ATOM 112 N N . SER A 1 42 ? 9.100 -3.815 0.485 1.00 105.44 ? 42 SER A N 1 ATOM 113 C CA . SER A 1 42 ? 8.423 -3.078 1.542 1.00 101.92 ? 42 SER A CA 1 ATOM 114 C C . SER A 1 42 ? 7.075 -2.527 1.080 1.00 100.04 ? 42 SER A C 1 ATOM 115 O O . SER A 1 42 ? 6.979 -1.402 0.572 1.00 96.59 ? 42 SER A O 1 ATOM 116 C CB . SER A 1 42 ? 9.319 -1.981 2.119 1.00 105.56 ? 42 SER A CB 1 ATOM 117 O OG . SER A 1 42 ? 9.074 -1.810 3.510 1.00 106.80 ? 42 SER A OG 1 ATOM 118 N N . PHE A 1 43 ? 6.037 -3.343 1.259 1.00 96.93 ? 43 PHE A N 1 ATOM 119 C CA . PHE A 1 43 ? 4.677 -2.973 0.884 1.00 95.12 ? 43 PHE A CA 1 ATOM 120 C C . PHE A 1 43 ? 3.923 -2.325 2.038 1.00 102.05 ? 43 PHE A C 1 ATOM 121 O O . PHE A 1 43 ? 4.215 -2.575 3.208 1.00 111.78 ? 43 PHE A O 1 ATOM 122 C CB . PHE A 1 43 ? 3.885 -4.192 0.417 1.00 80.02 ? 43 PHE A CB 1 ATOM 123 C CG . PHE A 1 43 ? 4.386 -4.796 -0.854 1.00 85.07 ? 43 PHE A CG 1 ATOM 124 C CD1 . PHE A 1 43 ? 4.179 -6.137 -1.124 1.00 89.22 ? 43 PHE A CD1 1 ATOM 125 C CD2 . PHE A 1 43 ? 5.066 -4.035 -1.778 1.00 90.15 ? 43 PHE A CD2 1 ATOM 126 C CE1 . PHE A 1 43 ? 4.637 -6.705 -2.294 1.00 86.39 ? 43 PHE A CE1 1 ATOM 127 C CE2 . PHE A 1 43 ? 5.527 -4.602 -2.950 1.00 89.94 ? 43 PHE A CE2 1 ATOM 128 C CZ . PHE A 1 43 ? 5.309 -5.939 -3.206 1.00 84.10 ? 43 PHE A CZ 1 ATOM 129 N N . THR A 1 44 ? 2.942 -1.501 1.693 1.00 93.93 ? 44 THR A N 1 ATOM 130 C CA . THR A 1 44 ? 2.067 -0.882 2.672 1.00 90.46 ? 44 THR A CA 1 ATOM 131 C C . THR A 1 44 ? 0.641 -1.329 2.369 1.00 100.00 ? 44 THR A C 1 ATOM 132 O O . THR A 1 44 ? -0.296 -1.026 3.109 1.00 112.03 ? 44 THR A O 1 ATOM 133 C CB . THR A 1 44 ? 2.173 0.660 2.622 1.00 91.90 ? 44 THR A CB 1 ATOM 134 O OG1 . THR A 1 44 ? 1.918 1.132 1.287 1.00 78.83 ? 44 THR A OG1 1 ATOM 135 C CG2 . THR A 1 44 ? 3.566 1.114 3.068 1.00 89.16 ? 44 THR A CG2 1 ATOM 136 N N . SER A 1 45 ? 0.495 -2.061 1.268 1.00 90.07 ? 45 SER A N 1 ATOM 137 C CA . SER A 1 45 ? -0.798 -2.566 0.838 1.00 87.56 ? 45 SER A CA 1 ATOM 138 C C . SER A 1 45 ? -0.611 -3.856 0.060 1.00 89.76 ? 45 SER A C 1 ATOM 139 O O . SER A 1 45 ? 0.459 -4.099 -0.494 1.00 87.02 ? 45 SER A O 1 ATOM 140 C CB . SER A 1 45 ? -1.507 -1.540 -0.050 1.00 91.98 ? 45 SER A CB 1 ATOM 141 O OG . SER A 1 45 ? -0.983 -1.525 -1.373 1.00 86.61 ? 45 SER A OG 1 ATOM 142 N N . ILE A 1 46 ? -1.652 -4.681 0.020 1.00 92.76 ? 46 ILE A N 1 ATOM 143 C CA . ILE A 1 46 ? -1.616 -5.890 -0.790 1.00 98.11 ? 46 ILE A CA 1 ATOM 144 C C . ILE A 1 46 ? -1.343 -5.454 -2.224 1.00 102.25 ? 46 ILE A C 1 ATOM 145 O O . ILE A 1 46 ? -2.062 -4.613 -2.761 1.00 112.57 ? 46 ILE A O 1 ATOM 146 C CB . ILE A 1 46 ? -2.958 -6.687 -0.720 1.00 83.09 ? 46 ILE A CB 1 ATOM 147 C CG1 . ILE A 1 46 ? -3.276 -7.130 0.714 1.00 75.43 ? 46 ILE A CG1 1 ATOM 148 C CG2 . ILE A 1 46 ? -2.932 -7.893 -1.653 1.00 75.47 ? 46 ILE A CG2 1 ATOM 149 C CD1 . ILE A 1 46 ? -2.519 -8.350 1.188 1.00 47.76 ? 46 ILE A CD1 1 ATOM 150 N N . PRO A 1 47 ? -0.279 -5.995 -2.836 1.00 96.78 ? 47 PRO A N 1 ATOM 151 C CA . PRO A 1 47 ? 0.058 -5.752 -4.239 1.00 95.17 ? 47 PRO A CA 1 ATOM 152 C C . PRO A 1 47 ? -1.153 -5.639 -5.149 1.00 96.83 ? 47 PRO A C 1 ATOM 153 O O . PRO A 1 47 ? -1.953 -6.569 -5.242 1.00 87.95 ? 47 PRO A O 1 ATOM 154 C CB . PRO A 1 47 ? 0.871 -6.990 -4.596 1.00 88.87 ? 47 PRO A CB 1 ATOM 155 C CG . PRO A 1 47 ? 1.642 -7.247 -3.349 1.00 92.80 ? 47 PRO A CG 1 ATOM 156 C CD . PRO A 1 47 ? 0.752 -6.820 -2.185 1.00 96.33 ? 47 PRO A CD 1 ATOM 157 N N . SER A 1 48 ? -1.268 -4.491 -5.812 1.00 110.67 ? 48 SER A N 1 ATOM 158 C CA . SER A 1 48 ? -2.336 -4.244 -6.774 1.00 112.58 ? 48 SER A CA 1 ATOM 159 C C . SER A 1 48 ? -2.261 -5.258 -7.912 1.00 100.62 ? 48 SER A C 1 ATOM 160 O O . SER A 1 48 ? -1.202 -5.830 -8.183 1.00 94.90 ? 48 SER A O 1 ATOM 161 C CB . SER A 1 48 ? -2.246 -2.815 -7.326 1.00 108.92 ? 48 SER A CB 1 ATOM 162 O OG . SER A 1 48 ? -2.193 -1.859 -6.279 1.00 99.06 ? 48 SER A OG 1 ATOM 163 N N . GLY A 1 49 ? -3.393 -5.485 -8.566 1.00 92.19 ? 49 GLY A N 1 ATOM 164 C CA . GLY A 1 49 ? -3.433 -6.407 -9.684 1.00 99.06 ? 49 GLY A CA 1 ATOM 165 C C . GLY A 1 49 ? -2.929 -7.799 -9.352 1.00 97.75 ? 49 GLY A C 1 ATOM 166 O O . GLY A 1 49 ? -1.726 -8.092 -9.431 1.00 77.13 ? 49 GLY A O 1 ATOM 167 N N . LEU A 1 50 ? -3.871 -8.657 -8.976 1.00 104.22 ? 50 LEU A N 1 ATOM 168 C CA . LEU A 1 50 ? -3.588 -10.055 -8.701 1.00 90.86 ? 50 LEU A CA 1 ATOM 169 C C . LEU A 1 50 ? -4.394 -10.909 -9.680 1.00 97.79 ? 50 LEU A C 1 ATOM 170 O O . LEU A 1 50 ? -5.509 -10.550 -10.058 1.00 90.46 ? 50 LEU A O 1 ATOM 171 C CB . LEU A 1 50 ? -3.932 -10.389 -7.250 1.00 67.10 ? 50 LEU A CB 1 ATOM 172 C CG . LEU A 1 50 ? -3.195 -9.599 -6.166 1.00 75.92 ? 50 LEU A CG 1 ATOM 173 C CD1 . LEU A 1 50 ? -3.613 -10.054 -4.763 1.00 79.50 ? 50 LEU A CD1 1 ATOM 174 C CD2 . LEU A 1 50 ? -1.694 -9.735 -6.324 1.00 81.10 ? 50 LEU A CD2 1 ATOM 175 N N . THR A 1 51 ? -3.825 -12.035 -10.095 1.00 104.02 ? 51 THR A N 1 ATOM 176 C CA . THR A 1 51 ? -4.386 -12.813 -11.193 1.00 105.59 ? 51 THR A CA 1 ATOM 177 C C . THR A 1 51 ? -5.017 -14.108 -10.727 1.00 93.18 ? 51 THR A C 1 ATOM 178 O O . THR A 1 51 ? -4.604 -14.674 -9.714 1.00 99.91 ? 51 THR A O 1 ATOM 179 C CB . THR A 1 51 ? -3.295 -13.172 -12.204 1.00 115.60 ? 51 THR A CB 1 ATOM 180 O OG1 . THR A 1 51 ? -2.457 -12.029 -12.427 1.00 119.70 ? 51 THR A OG1 1 ATOM 181 C CG2 . THR A 1 51 ? -3.914 -13.629 -13.520 1.00 115.97 ? 51 THR A CG2 1 ATOM 182 N N . ALA A 1 52 ? -6.004 -14.590 -11.480 1.00 78.63 ? 52 ALA A N 1 ATOM 183 C CA . ALA A 1 52 ? -6.619 -15.888 -11.187 1.00 88.14 ? 52 ALA A CA 1 ATOM 184 C C . ALA A 1 52 ? -5.707 -17.060 -11.610 1.00 92.13 ? 52 ALA A C 1 ATOM 185 O O . ALA A 1 52 ? -6.119 -18.234 -11.643 1.00 72.22 ? 52 ALA A O 1 ATOM 186 C CB . ALA A 1 52 ? -8.014 -15.998 -11.818 1.00 72.39 ? 52 ALA A CB 1 ATOM 187 N N . ALA A 1 53 ? -4.459 -16.715 -11.920 1.00 98.35 ? 53 ALA A N 1 ATOM 188 C CA . ALA A 1 53 ? -3.427 -17.693 -12.232 1.00 98.28 ? 53 ALA A CA 1 ATOM 189 C C . ALA A 1 53 ? -2.630 -18.015 -10.977 1.00 103.52 ? 53 ALA A C 1 ATOM 190 O O . ALA A 1 53 ? -2.059 -19.101 -10.852 1.00 100.71 ? 53 ALA A O 1 ATOM 191 C CB . ALA A 1 53 ? -2.502 -17.151 -13.306 1.00 96.36 ? 53 ALA A CB 1 ATOM 192 N N . MET A 1 54 ? -2.584 -17.051 -10.060 1.00 106.85 ? 54 MET A N 1 ATOM 193 C CA . MET A 1 54 ? -1.857 -17.202 -8.806 1.00 92.24 ? 54 MET A CA 1 ATOM 194 C C . MET A 1 54 ? -2.448 -18.353 -7.998 1.00 89.35 ? 54 MET A C 1 ATOM 195 O O . MET A 1 54 ? -3.656 -18.401 -7.757 1.00 93.61 ? 54 MET A O 1 ATOM 196 C CB . MET A 1 54 ? -1.903 -15.900 -8.005 1.00 72.58 ? 54 MET A CB 1 ATOM 197 C CG . MET A 1 54 ? -1.382 -14.681 -8.756 1.00 66.98 ? 54 MET A CG 1 ATOM 198 S SD . MET A 1 54 ? -1.463 -13.150 -7.807 1.00 130.70 ? 54 MET A SD 1 ATOM 199 C CE . MET A 1 54 ? -0.140 -12.196 -8.548 1.00 71.38 ? 54 MET A CE 1 ATOM 200 N N . LYS A 1 55 ? -1.588 -19.287 -7.606 1.00 77.88 ? 55 LYS A N 1 ATOM 201 C CA . LYS A 1 55 ? -1.993 -20.430 -6.807 1.00 73.91 ? 55 LYS A CA 1 ATOM 202 C C . LYS A 1 55 ? -1.428 -20.289 -5.382 1.00 79.66 ? 55 LYS A C 1 ATOM 203 O O . LYS A 1 55 ? -2.007 -20.775 -4.409 1.00 78.79 ? 55 LYS A O 1 ATOM 204 C CB . LYS A 1 55 ? -1.494 -21.718 -7.463 1.00 66.65 ? 55 LYS A CB 1 ATOM 205 C CG . LYS A 1 55 ? -2.192 -22.085 -8.756 1.00 81.97 ? 55 LYS A CG 1 ATOM 206 C CD . LYS A 1 55 ? -3.496 -22.844 -8.516 1.00 99.97 ? 55 LYS A CD 1 ATOM 207 C CE . LYS A 1 55 ? -3.980 -23.580 -9.785 1.00 107.89 ? 55 LYS A CE 1 ATOM 208 N NZ . LYS A 1 55 ? -4.834 -22.758 -10.705 1.00 108.65 ? 55 LYS A NZ 1 ATOM 209 N N . SER A 1 56 ? -0.298 -19.603 -5.268 1.00 73.03 ? 56 SER A N 1 ATOM 210 C CA . SER A 1 56 ? 0.369 -19.436 -3.992 1.00 64.99 ? 56 SER A CA 1 ATOM 211 C C . SER A 1 56 ? 0.949 -18.035 -3.886 1.00 70.43 ? 56 SER A C 1 ATOM 212 O O . SER A 1 56 ? 1.939 -17.720 -4.527 1.00 79.69 ? 56 SER A O 1 ATOM 213 C CB . SER A 1 56 ? 1.481 -20.482 -3.836 1.00 59.41 ? 56 SER A CB 1 ATOM 214 O OG . SER A 1 56 ? 2.261 -20.261 -2.664 1.00 57.46 ? 56 SER A OG 1 ATOM 215 N N . LEU A 1 57 ? 0.325 -17.196 -3.072 1.00 75.09 ? 57 LEU A N 1 ATOM 216 C CA . LEU A 1 57 ? 0.831 -15.852 -2.814 1.00 75.67 ? 57 LEU A CA 1 ATOM 217 C C . LEU A 1 57 ? 1.588 -15.805 -1.487 1.00 74.66 ? 57 LEU A C 1 ATOM 218 O O . LEU A 1 57 ? 1.097 -16.304 -0.481 1.00 77.75 ? 57 LEU A O 1 ATOM 219 C CB . LEU A 1 57 ? -0.330 -14.852 -2.794 1.00 70.46 ? 57 LEU A CB 1 ATOM 220 C CG . LEU A 1 57 ? 0.011 -13.371 -2.682 1.00 69.03 ? 57 LEU A CG 1 ATOM 221 C CD1 . LEU A 1 57 ? 1.259 -13.050 -3.479 1.00 72.95 ? 57 LEU A CD1 1 ATOM 222 C CD2 . LEU A 1 57 ? -1.157 -12.552 -3.174 1.00 75.88 ? 57 LEU A CD2 1 ATOM 223 N N . ASP A 1 58 ? 2.783 -15.216 -1.492 1.00 78.59 ? 58 ASP A N 1 ATOM 224 C CA . ASP A 1 58 ? 3.551 -15.006 -0.266 1.00 81.79 ? 58 ASP A CA 1 ATOM 225 C C . ASP A 1 58 ? 3.949 -13.543 -0.109 1.00 90.82 ? 58 ASP A C 1 ATOM 226 O O . ASP A 1 58 ? 4.895 -13.087 -0.744 1.00 101.73 ? 58 ASP A O 1 ATOM 227 C CB . ASP A 1 58 ? 4.803 -15.886 -0.231 1.00 74.29 ? 58 ASP A CB 1 ATOM 228 C CG . ASP A 1 58 ? 5.574 -15.756 1.084 1.00 77.12 ? 58 ASP A CG 1 ATOM 229 O OD1 . ASP A 1 58 ? 6.471 -16.594 1.336 1.00 74.62 ? 58 ASP A OD1 1 ATOM 230 O OD2 . ASP A 1 58 ? 5.280 -14.821 1.868 1.00 68.41 ? 58 ASP A OD2 1 ATOM 231 N N . LEU A 1 59 ? 3.229 -12.818 0.746 1.00 85.32 ? 59 LEU A N 1 ATOM 232 C CA . LEU A 1 59 ? 3.506 -11.407 1.000 1.00 72.22 ? 59 LEU A CA 1 ATOM 233 C C . LEU A 1 59 ? 3.978 -11.208 2.431 1.00 67.43 ? 59 LEU A C 1 ATOM 234 O O . LEU A 1 59 ? 3.453 -10.361 3.147 1.00 82.79 ? 59 LEU A O 1 ATOM 235 C CB . LEU A 1 59 ? 2.256 -10.550 0.753 1.00 57.24 ? 59 LEU A CB 1 ATOM 236 C CG . LEU A 1 59 ? 1.485 -10.864 -0.525 1.00 56.19 ? 59 LEU A CG 1 ATOM 237 C CD1 . LEU A 1 59 ? 0.157 -10.133 -0.560 1.00 49.63 ? 59 LEU A CD1 1 ATOM 238 C CD2 . LEU A 1 59 ? 2.331 -10.522 -1.741 1.00 66.98 ? 59 LEU A CD2 1 ATOM 239 N N . SER A 1 60 ? 4.970 -11.981 2.847 1.00 54.92 ? 60 SER A N 1 ATOM 240 C CA . SER A 1 60 ? 5.458 -11.896 4.220 1.00 68.75 ? 60 SER A CA 1 ATOM 241 C C . SER A 1 60 ? 6.454 -10.760 4.498 1.00 75.88 ? 60 SER A C 1 ATOM 242 O O . SER A 1 60 ? 7.228 -10.362 3.629 1.00 84.02 ? 60 SER A O 1 ATOM 243 C CB . SER A 1 60 ? 6.066 -13.233 4.645 1.00 71.12 ? 60 SER A CB 1 ATOM 244 O OG . SER A 1 60 ? 5.070 -14.228 4.729 1.00 75.09 ? 60 SER A OG 1 ATOM 245 N N . PHE A 1 61 ? 6.415 -10.249 5.726 1.00 76.87 ? 61 PHE A N 1 ATOM 246 C CA . PHE A 1 61 ? 7.407 -9.298 6.238 1.00 78.56 ? 61 PHE A CA 1 ATOM 247 C C . PHE A 1 61 ? 7.295 -7.917 5.619 1.00 77.13 ? 61 PHE A C 1 ATOM 248 O O . PHE A 1 61 ? 8.299 -7.323 5.249 1.00 84.66 ? 61 PHE A O 1 ATOM 249 C CB . PHE A 1 61 ? 8.839 -9.839 6.072 1.00 71.63 ? 61 PHE A CB 1 ATOM 250 C CG . PHE A 1 61 ? 8.997 -11.276 6.486 1.00 68.23 ? 61 PHE A CG 1 ATOM 251 C CD1 . PHE A 1 61 ? 9.053 -12.281 5.536 1.00 69.12 ? 61 PHE A CD1 1 ATOM 252 C CD2 . PHE A 1 61 ? 9.074 -11.625 7.825 1.00 80.88 ? 61 PHE A CD2 1 ATOM 253 C CE1 . PHE A 1 61 ? 9.187 -13.612 5.911 1.00 75.06 ? 61 PHE A CE1 1 ATOM 254 C CE2 . PHE A 1 61 ? 9.206 -12.957 8.210 1.00 82.15 ? 61 PHE A CE2 1 ATOM 255 C CZ . PHE A 1 61 ? 9.262 -13.949 7.248 1.00 78.69 ? 61 PHE A CZ 1 ATOM 256 N N . ASN A 1 62 ? 6.075 -7.409 5.504 1.00 72.98 ? 62 ASN A N 1 ATOM 257 C CA . ASN A 1 62 ? 5.867 -6.058 4.996 1.00 81.64 ? 62 ASN A CA 1 ATOM 258 C C . ASN A 1 62 ? 5.057 -5.247 5.986 1.00 97.73 ? 62 ASN A C 1 ATOM 259 O O . ASN A 1 62 ? 4.767 -5.701 7.092 1.00 102.91 ? 62 ASN A O 1 ATOM 260 C CB . ASN A 1 62 ? 5.146 -6.056 3.645 1.00 77.12 ? 62 ASN A CB 1 ATOM 261 C CG . ASN A 1 62 ? 5.400 -7.309 2.843 1.00 82.32 ? 62 ASN A CG 1 ATOM 262 O OD1 . ASN A 1 62 ? 5.271 -8.416 3.355 1.00 85.36 ? 62 ASN A OD1 1 ATOM 263 N ND2 . ASN A 1 62 ? 5.741 -7.145 1.572 1.00 83.20 ? 62 ASN A ND2 1 ATOM 264 N N . LYS A 1 63 ? 4.685 -4.043 5.579 1.00 102.62 ? 63 LYS A N 1 ATOM 265 C CA . LYS A 1 63 ? 3.820 -3.223 6.401 1.00 111.02 ? 63 LYS A CA 1 ATOM 266 C C . LYS A 1 63 ? 2.417 -3.200 5.810 1.00 119.44 ? 63 LYS A C 1 ATOM 267 O O . LYS A 1 63 ? 1.848 -2.130 5.584 1.00 133.24 ? 63 LYS A O 1 ATOM 268 C CB . LYS A 1 63 ? 4.391 -1.809 6.546 1.00 120.67 ? 63 LYS A CB 1 ATOM 269 C CG . LYS A 1 63 ? 5.675 -1.749 7.372 1.00 126.71 ? 63 LYS A CG 1 ATOM 270 C CD . LYS A 1 63 ? 6.220 -0.327 7.525 1.00 132.93 ? 63 LYS A CD 1 ATOM 271 C CE . LYS A 1 63 ? 5.152 0.696 7.939 1.00 128.72 ? 63 LYS A CE 1 ATOM 272 N NZ . LYS A 1 63 ? 4.624 1.491 6.784 1.00 122.78 ? 63 LYS A NZ 1 ATOM 273 N N . ILE A 1 64 ? 1.866 -4.384 5.547 1.00 110.26 ? 64 ILE A N 1 ATOM 274 C CA . ILE A 1 64 ? 0.484 -4.481 5.089 1.00 100.49 ? 64 ILE A CA 1 ATOM 275 C C . ILE A 1 64 ? -0.415 -4.299 6.294 1.00 99.53 ? 64 ILE A C 1 ATOM 276 O O . ILE A 1 64 ? -1.158 -5.195 6.680 1.00 98.37 ? 64 ILE A O 1 ATOM 277 C CB . ILE A 1 64 ? 0.160 -5.829 4.439 1.00 88.85 ? 64 ILE A CB 1 ATOM 278 C CG1 . ILE A 1 64 ? 1.317 -6.308 3.563 1.00 88.67 ? 64 ILE A CG1 1 ATOM 279 C CG2 . ILE A 1 64 ? -1.119 -5.713 3.621 1.00 75.22 ? 64 ILE A CG2 1 ATOM 280 C CD1 . ILE A 1 64 ? 1.188 -5.894 2.131 1.00 92.67 ? 64 ILE A CD1 1 ATOM 281 N N . THR A 1 65 ? -0.315 -3.127 6.897 1.00 100.85 ? 65 THR A N 1 ATOM 282 C CA . THR A 1 65 ? -1.099 -2.776 8.061 1.00 89.70 ? 65 THR A CA 1 ATOM 283 C C . THR A 1 65 ? -2.584 -3.057 7.841 1.00 80.96 ? 65 THR A C 1 ATOM 284 O O . THR A 1 65 ? -3.271 -3.503 8.758 1.00 76.38 ? 65 THR A O 1 ATOM 285 C CB . THR A 1 65 ? -0.908 -1.292 8.384 1.00 88.51 ? 65 THR A CB 1 ATOM 286 O OG1 . THR A 1 65 ? -1.808 -0.906 9.425 1.00 92.74 ? 65 THR A OG1 1 ATOM 287 C CG2 . THR A 1 65 ? -1.170 -0.438 7.135 1.00 79.16 ? 65 THR A CG2 1 ATOM 288 N N . TYR A 1 66 ? -3.076 -2.807 6.628 1.00 74.33 ? 66 TYR A N 1 ATOM 289 C CA . TYR A 1 66 ? -4.507 -2.934 6.347 1.00 69.79 ? 66 TYR A CA 1 ATOM 290 C C . TYR A 1 66 ? -4.835 -3.805 5.142 1.00 70.58 ? 66 TYR A C 1 ATOM 291 O O . TYR A 1 66 ? -4.327 -3.583 4.039 1.00 76.17 ? 66 TYR A O 1 ATOM 292 C CB . TYR A 1 66 ? -5.120 -1.556 6.133 1.00 67.26 ? 66 TYR A CB 1 ATOM 293 C CG . TYR A 1 66 ? -6.618 -1.562 5.935 1.00 69.90 ? 66 TYR A CG 1 ATOM 294 C CD1 . TYR A 1 66 ? -7.479 -1.759 7.004 1.00 80.42 ? 66 TYR A CD1 1 ATOM 295 C CD2 . TYR A 1 66 ? -7.173 -1.345 4.687 1.00 71.67 ? 66 TYR A CD2 1 ATOM 296 C CE1 . TYR A 1 66 ? -8.853 -1.751 6.829 1.00 80.28 ? 66 TYR A CE1 1 ATOM 297 C CE2 . TYR A 1 66 ? -8.542 -1.339 4.501 1.00 74.51 ? 66 TYR A CE2 1 ATOM 298 C CZ . TYR A 1 66 ? -9.376 -1.540 5.576 1.00 80.15 ? 66 TYR A CZ 1 ATOM 299 O OH . TYR A 1 66 ? -10.737 -1.537 5.393 1.00 79.28 ? 66 TYR A OH 1 ATOM 300 N N . ILE A 1 67 ? -5.692 -4.796 5.360 1.00 59.54 ? 67 ILE A N 1 ATOM 301 C CA . ILE A 1 67 ? -6.272 -5.554 4.260 1.00 63.05 ? 67 ILE A CA 1 ATOM 302 C C . ILE A 1 67 ? -7.740 -5.140 4.099 1.00 70.34 ? 67 ILE A C 1 ATOM 303 O O . ILE A 1 67 ? -8.512 -5.147 5.065 1.00 74.17 ? 67 ILE A O 1 ATOM 304 C CB . ILE A 1 67 ? -6.146 -7.072 4.468 1.00 54.85 ? 67 ILE A CB 1 ATOM 305 C CG1 . ILE A 1 67 ? -4.683 -7.507 4.381 1.00 52.20 ? 67 ILE A CG1 1 ATOM 306 C CG2 . ILE A 1 67 ? -6.958 -7.815 3.428 1.00 48.44 ? 67 ILE A CG2 1 ATOM 307 C CD1 . ILE A 1 67 ? -4.390 -8.798 5.108 1.00 46.74 ? 67 ILE A CD1 1 ATOM 308 N N . GLY A 1 68 ? -8.111 -4.759 2.879 1.00 62.04 ? 68 GLY A N 1 ATOM 309 C CA . GLY A 1 68 ? -9.412 -4.169 2.622 1.00 63.75 ? 68 GLY A CA 1 ATOM 310 C C . GLY A 1 68 ? -10.425 -5.119 2.021 1.00 62.03 ? 68 GLY A C 1 ATOM 311 O O . GLY A 1 68 ? -10.173 -6.323 1.908 1.00 64.97 ? 68 GLY A O 1 ATOM 312 N N . HIS A 1 69 ? -11.575 -4.579 1.631 1.00 53.23 ? 69 HIS A N 1 ATOM 313 C CA . HIS A 1 69 ? -12.669 -5.411 1.144 1.00 60.02 ? 69 HIS A CA 1 ATOM 314 C C . HIS A 1 69 ? -12.324 -6.124 -0.158 1.00 78.37 ? 69 HIS A C 1 ATOM 315 O O . HIS A 1 69 ? -12.533 -7.338 -0.277 1.00 83.19 ? 69 HIS A O 1 ATOM 316 C CB . HIS A 1 69 ? -13.936 -4.580 0.970 1.00 67.23 ? 69 HIS A CB 1 ATOM 317 C CG . HIS A 1 69 ? -14.635 -4.264 2.255 1.00 74.65 ? 69 HIS A CG 1 ATOM 318 N ND1 . HIS A 1 69 ? -14.440 -3.084 2.937 1.00 81.42 ? 69 HIS A ND1 1 ATOM 319 C CD2 . HIS A 1 69 ? -15.537 -4.970 2.975 1.00 78.18 ? 69 HIS A CD2 1 ATOM 320 C CE1 . HIS A 1 69 ? -15.187 -3.079 4.027 1.00 82.95 ? 69 HIS A CE1 1 ATOM 321 N NE2 . HIS A 1 69 ? -15.856 -4.215 4.077 1.00 84.35 ? 69 HIS A NE2 1 ATOM 322 N N . GLY A 1 70 ? -11.787 -5.365 -1.118 1.00 81.96 ? 70 GLY A N 1 ATOM 323 C CA . GLY A 1 70 ? -11.446 -5.880 -2.435 1.00 76.72 ? 70 GLY A CA 1 ATOM 324 C C . GLY A 1 70 ? -10.015 -6.369 -2.661 1.00 77.40 ? 70 GLY A C 1 ATOM 325 O O . GLY A 1 70 ? -9.719 -6.921 -3.717 1.00 77.51 ? 70 GLY A O 1 ATOM 326 N N . ASP A 1 71 ? -9.133 -6.194 -1.681 1.00 74.90 ? 71 ASP A N 1 ATOM 327 C CA . ASP A 1 71 ? -7.715 -6.541 -1.839 1.00 79.79 ? 71 ASP A CA 1 ATOM 328 C C . ASP A 1 71 ? -7.426 -7.927 -2.431 1.00 78.99 ? 71 ASP A C 1 ATOM 329 O O . ASP A 1 71 ? -6.424 -8.103 -3.118 1.00 76.98 ? 71 ASP A O 1 ATOM 330 C CB . ASP A 1 71 ? -6.958 -6.391 -0.512 1.00 83.90 ? 71 ASP A CB 1 ATOM 331 C CG . ASP A 1 71 ? -6.763 -4.940 -0.107 1.00 91.36 ? 71 ASP A CG 1 ATOM 332 O OD1 . ASP A 1 71 ? -5.824 -4.658 0.674 1.00 91.63 ? 71 ASP A OD1 1 ATOM 333 O OD2 . ASP A 1 71 ? -7.548 -4.082 -0.570 1.00 90.54 ? 71 ASP A OD2 1 ATOM 334 N N . LEU A 1 72 ? -8.275 -8.912 -2.155 1.00 72.55 ? 72 LEU A N 1 ATOM 335 C CA . LEU A 1 72 ? -8.000 -10.271 -2.617 1.00 66.11 ? 72 LEU A CA 1 ATOM 336 C C . LEU A 1 72 ? -9.181 -10.927 -3.334 1.00 82.12 ? 72 LEU A C 1 ATOM 337 O O . LEU A 1 72 ? -9.485 -12.093 -3.087 1.00 94.47 ? 72 LEU A O 1 ATOM 338 C CB . LEU A 1 72 ? -7.552 -11.164 -1.452 1.00 64.79 ? 72 LEU A CB 1 ATOM 339 C CG . LEU A 1 72 ? -6.328 -10.784 -0.606 1.00 72.54 ? 72 LEU A CG 1 ATOM 340 C CD1 . LEU A 1 72 ? -6.344 -11.544 0.681 1.00 60.26 ? 72 LEU A CD1 1 ATOM 341 C CD2 . LEU A 1 72 ? -5.032 -11.054 -1.334 1.00 85.64 ? 72 LEU A CD2 1 ATOM 342 N N . ARG A 1 73 ? -9.843 -10.190 -4.222 1.00 81.40 ? 73 ARG A N 1 ATOM 343 C CA . ARG A 1 73 ? -10.958 -10.746 -4.984 1.00 79.53 ? 73 ARG A CA 1 ATOM 344 C C . ARG A 1 73 ? -10.442 -11.398 -6.258 1.00 88.60 ? 73 ARG A C 1 ATOM 345 O O . ARG A 1 73 ? -10.990 -12.400 -6.733 1.00 86.57 ? 73 ARG A O 1 ATOM 346 C CB . ARG A 1 73 ? -11.963 -9.654 -5.341 1.00 74.30 ? 73 ARG A CB 1 ATOM 347 C CG . ARG A 1 73 ? -12.792 -9.173 -4.181 1.00 85.13 ? 73 ARG A CG 1 ATOM 348 C CD . ARG A 1 73 ? -13.975 -10.091 -3.917 1.00 101.22 ? 73 ARG A CD 1 ATOM 349 N NE . ARG A 1 73 ? -14.345 -10.064 -2.504 1.00 112.26 ? 73 ARG A NE 1 ATOM 350 C CZ . ARG A 1 73 ? -15.043 -9.091 -1.929 1.00 122.25 ? 73 ARG A CZ 1 ATOM 351 N NH1 . ARG A 1 73 ? -15.463 -8.052 -2.644 1.00 129.00 ? 73 ARG A NH1 1 ATOM 352 N NH2 . ARG A 1 73 ? -15.321 -9.158 -0.635 1.00 121.09 ? 73 ARG A NH2 1 ATOM 353 N N . ALA A 1 74 ? -9.379 -10.817 -6.804 1.00 85.71 ? 74 ALA A N 1 ATOM 354 C CA . ALA A 1 74 ? -8.818 -11.285 -8.058 1.00 79.57 ? 74 ALA A CA 1 ATOM 355 C C . ALA A 1 74 ? -8.297 -12.738 -7.986 1.00 87.79 ? 74 ALA A C 1 ATOM 356 O O . ALA A 1 74 ? -8.706 -13.589 -8.790 1.00 81.86 ? 74 ALA A O 1 ATOM 357 C CB . ALA A 1 74 ? -7.739 -10.329 -8.532 1.00 62.56 ? 74 ALA A CB 1 ATOM 358 N N . CYS A 1 75 ? -7.428 -13.023 -7.011 1.00 83.05 ? 75 CYS A N 1 ATOM 359 C CA . CYS A 1 75 ? -6.795 -14.346 -6.877 1.00 85.41 ? 75 CYS A CA 1 ATOM 360 C C . CYS A 1 75 ? -7.679 -15.429 -6.242 1.00 80.84 ? 75 CYS A C 1 ATOM 361 O O . CYS A 1 75 ? -7.300 -16.058 -5.262 1.00 70.82 ? 75 CYS A O 1 ATOM 362 C CB . CYS A 1 75 ? -5.483 -14.234 -6.100 1.00 84.04 ? 75 CYS A CB 1 ATOM 363 S SG . CYS A 1 75 ? -5.616 -13.331 -4.548 1.00 97.63 ? 75 CYS A SG 1 ATOM 364 N N . ALA A 1 76 ? -8.839 -15.659 -6.841 1.00 74.74 ? 76 ALA A N 1 ATOM 365 C CA . ALA A 1 76 ? -9.823 -16.596 -6.323 1.00 62.69 ? 76 ALA A CA 1 ATOM 366 C C . ALA A 1 76 ? -9.433 -18.071 -6.473 1.00 75.77 ? 76 ALA A C 1 ATOM 367 O O . ALA A 1 76 ? -10.186 -18.964 -6.061 1.00 81.73 ? 76 ALA A O 1 ATOM 368 C CB . ALA A 1 76 ? -11.168 -16.336 -6.988 1.00 48.60 ? 76 ALA A CB 1 ATOM 369 N N . ASN A 1 77 ? -8.278 -18.335 -7.075 1.00 80.68 ? 77 ASN A N 1 ATOM 370 C CA . ASN A 1 77 ? -7.845 -19.716 -7.277 1.00 93.39 ? 77 ASN A CA 1 ATOM 371 C C . ASN A 1 77 ? -6.680 -20.060 -6.379 1.00 94.54 ? 77 ASN A C 1 ATOM 372 O O . ASN A 1 77 ? -6.045 -21.109 -6.526 1.00 92.70 ? 77 ASN A O 1 ATOM 373 C CB . ASN A 1 77 ? -7.475 -19.968 -8.735 1.00 106.83 ? 77 ASN A CB 1 ATOM 374 C CG . ASN A 1 77 ? -8.616 -20.565 -9.525 1.00 115.51 ? 77 ASN A CG 1 ATOM 375 O OD1 . ASN A 1 77 ? -9.446 -21.298 -8.978 1.00 113.03 ? 77 ASN A OD1 1 ATOM 376 N ND2 . ASN A 1 77 ? -8.664 -20.260 -10.821 1.00 117.97 ? 77 ASN A ND2 1 ATOM 377 N N . LEU A 1 78 ? -6.428 -19.153 -5.439 1.00 85.22 ? 78 LEU A N 1 ATOM 378 C CA . LEU A 1 78 ? -5.279 -19.207 -4.552 1.00 62.07 ? 78 LEU A CA 1 ATOM 379 C C . LEU A 1 78 ? -5.445 -20.377 -3.594 1.00 61.54 ? 78 LEU A C 1 ATOM 380 O O . LEU A 1 78 ? -6.499 -20.535 -2.986 1.00 79.08 ? 78 LEU A O 1 ATOM 381 C CB . LEU A 1 78 ? -5.198 -17.886 -3.799 1.00 34.68 ? 78 LEU A CB 1 ATOM 382 C CG . LEU A 1 78 ? -3.866 -17.441 -3.223 1.00 67.35 ? 78 LEU A CG 1 ATOM 383 C CD1 . LEU A 1 78 ? -2.895 -17.064 -4.316 1.00 63.06 ? 78 LEU A CD1 1 ATOM 384 C CD2 . LEU A 1 78 ? -4.077 -16.272 -2.270 1.00 75.93 ? 78 LEU A CD2 1 ATOM 385 N N . GLN A 1 79 ? -4.420 -21.216 -3.486 1.00 54.50 ? 79 GLN A N 1 ATOM 386 C CA . GLN A 1 79 ? -4.436 -22.341 -2.556 1.00 58.49 ? 79 GLN A CA 1 ATOM 387 C C . GLN A 1 79 ? -3.679 -21.998 -1.264 1.00 64.39 ? 79 GLN A C 1 ATOM 388 O O . GLN A 1 79 ? -3.891 -22.615 -0.214 1.00 51.66 ? 79 GLN A O 1 ATOM 389 C CB . GLN A 1 79 ? -3.770 -23.550 -3.200 1.00 64.66 ? 79 GLN A CB 1 ATOM 390 C CG . GLN A 1 79 ? -4.644 -24.360 -4.122 1.00 84.06 ? 79 GLN A CG 1 ATOM 391 C CD . GLN A 1 79 ? -3.834 -25.345 -4.954 1.00 96.65 ? 79 GLN A CD 1 ATOM 392 O OE1 . GLN A 1 79 ? -4.392 -26.131 -5.716 1.00 103.22 ? 79 GLN A OE1 1 ATOM 393 N NE2 . GLN A 1 79 ? -2.509 -25.303 -4.810 1.00 94.30 ? 79 GLN A NE2 1 ATOM 394 N N . VAL A 1 80 ? -2.789 -21.015 -1.361 1.00 65.00 ? 80 VAL A N 1 ATOM 395 C CA . VAL A 1 80 ? -1.880 -20.677 -0.280 1.00 57.58 ? 80 VAL A CA 1 ATOM 396 C C . VAL A 1 80 ? -1.637 -19.184 -0.165 1.00 71.67 ? 80 VAL A C 1 ATOM 397 O O . VAL A 1 80 ? -1.098 -18.565 -1.078 1.00 81.20 ? 80 VAL A O 1 ATOM 398 C CB . VAL A 1 80 ? -0.516 -21.279 -0.524 1.00 46.77 ? 80 VAL A CB 1 ATOM 399 C CG1 . VAL A 1 80 ? 0.437 -20.830 0.572 1.00 45.09 ? 80 VAL A CG1 1 ATOM 400 C CG2 . VAL A 1 80 ? -0.621 -22.779 -0.617 1.00 33.52 ? 80 VAL A CG2 1 ATOM 401 N N . LEU A 1 81 ? -2.010 -18.611 0.970 1.00 65.17 ? 81 LEU A N 1 ATOM 402 C CA . LEU A 1 81 ? -1.764 -17.205 1.219 1.00 57.08 ? 81 LEU A CA 1 ATOM 403 C C . LEU A 1 81 ? -0.889 -17.076 2.460 1.00 59.01 ? 81 LEU A C 1 ATOM 404 O O . LEU A 1 81 ? -1.325 -17.350 3.567 1.00 55.39 ? 81 LEU A O 1 ATOM 405 C CB . LEU A 1 81 ? -3.089 -16.466 1.382 1.00 56.44 ? 81 LEU A CB 1 ATOM 406 C CG . LEU A 1 81 ? -3.032 -15.014 1.848 1.00 60.39 ? 81 LEU A CG 1 ATOM 407 C CD1 . LEU A 1 81 ? -1.890 -14.293 1.176 1.00 61.61 ? 81 LEU A CD1 1 ATOM 408 C CD2 . LEU A 1 81 ? -4.354 -14.325 1.577 1.00 58.63 ? 81 LEU A CD2 1 ATOM 409 N N . ILE A 1 82 ? 0.363 -16.684 2.261 1.00 67.45 ? 82 ILE A N 1 ATOM 410 C CA . ILE A 1 82 ? 1.323 -16.582 3.351 1.00 70.70 ? 82 ILE A CA 1 ATOM 411 C C . ILE A 1 82 ? 1.544 -15.111 3.729 1.00 75.73 ? 82 ILE A C 1 ATOM 412 O O . ILE A 1 82 ? 2.165 -14.353 2.988 1.00 81.65 ? 82 ILE A O 1 ATOM 413 C CB . ILE A 1 82 ? 2.666 -17.245 2.972 1.00 80.93 ? 82 ILE A CB 1 ATOM 414 C CG1 . ILE A 1 82 ? 2.543 -18.772 2.945 1.00 76.12 ? 82 ILE A CG1 1 ATOM 415 C CG2 . ILE A 1 82 ? 3.745 -16.853 3.949 1.00 103.61 ? 82 ILE A CG2 1 ATOM 416 C CD1 . ILE A 1 82 ? 3.743 -19.448 2.315 1.00 30.02 ? 82 ILE A CD1 1 ATOM 417 N N . LEU A 1 83 ? 1.031 -14.718 4.891 1.00 71.38 ? 83 LEU A N 1 ATOM 418 C CA . LEU A 1 83 ? 1.060 -13.328 5.331 1.00 64.51 ? 83 LEU A CA 1 ATOM 419 C C . LEU A 1 83 ? 1.813 -13.163 6.648 1.00 79.14 ? 83 LEU A C 1 ATOM 420 O O . LEU A 1 83 ? 1.633 -12.167 7.360 1.00 71.56 ? 83 LEU A O 1 ATOM 421 C CB . LEU A 1 83 ? -0.366 -12.808 5.476 1.00 41.78 ? 83 LEU A CB 1 ATOM 422 C CG . LEU A 1 83 ? -0.978 -12.440 4.132 1.00 60.39 ? 83 LEU A CG 1 ATOM 423 C CD1 . LEU A 1 83 ? -2.474 -12.262 4.249 1.00 66.78 ? 83 LEU A CD1 1 ATOM 424 C CD2 . LEU A 1 83 ? -0.333 -11.176 3.603 1.00 65.67 ? 83 LEU A CD2 1 ATOM 425 N N . LYS A 1 84 ? 2.657 -14.150 6.953 1.00 90.54 ? 84 LYS A N 1 ATOM 426 C CA . LYS A 1 84 ? 3.406 -14.210 8.210 1.00 90.98 ? 84 LYS A CA 1 ATOM 427 C C . LYS A 1 84 ? 4.203 -12.938 8.487 1.00 93.59 ? 84 LYS A C 1 ATOM 428 O O . LYS A 1 84 ? 4.851 -12.389 7.600 1.00 99.25 ? 84 LYS A O 1 ATOM 429 C CB . LYS A 1 84 ? 4.355 -15.422 8.221 1.00 85.52 ? 84 LYS A CB 1 ATOM 430 C CG . LYS A 1 84 ? 5.151 -15.583 9.523 1.00 90.73 ? 84 LYS A CG 1 ATOM 431 C CD . LYS A 1 84 ? 6.470 -16.357 9.347 1.00 95.32 ? 84 LYS A CD 1 ATOM 432 C CE . LYS A 1 84 ? 6.256 -17.839 9.019 1.00 100.61 ? 84 LYS A CE 1 ATOM 433 N NZ . LYS A 1 84 ? 5.569 -18.613 10.105 1.00 96.26 ? 84 LYS A NZ 1 ATOM 434 N N . SER A 1 85 ? 4.138 -12.477 9.729 1.00 90.08 ? 85 SER A N 1 ATOM 435 C CA . SER A 1 85 ? 5.008 -11.420 10.233 1.00 87.92 ? 85 SER A CA 1 ATOM 436 C C . SER A 1 85 ? 5.037 -10.148 9.398 1.00 84.64 ? 85 SER A C 1 ATOM 437 O O . SER A 1 85 ? 6.060 -9.466 9.341 1.00 91.52 ? 85 SER A O 1 ATOM 438 C CB . SER A 1 85 ? 6.435 -11.946 10.425 1.00 96.87 ? 85 SER A CB 1 ATOM 439 O OG . SER A 1 85 ? 7.125 -11.213 11.428 1.00 101.39 ? 85 SER A OG 1 ATOM 440 N N . SER A 1 86 ? 3.926 -9.820 8.749 1.00 81.81 ? 86 SER A N 1 ATOM 441 C CA . SER A 1 86 ? 3.796 -8.493 8.164 1.00 83.07 ? 86 SER A CA 1 ATOM 442 C C . SER A 1 86 ? 3.404 -7.553 9.286 1.00 96.07 ? 86 SER A C 1 ATOM 443 O O . SER A 1 86 ? 3.821 -7.737 10.434 1.00 111.71 ? 86 SER A O 1 ATOM 444 C CB . SER A 1 86 ? 2.760 -8.464 7.052 1.00 77.77 ? 86 SER A CB 1 ATOM 445 O OG . SER A 1 86 ? 3.278 -9.067 5.884 1.00 75.26 ? 86 SER A OG 1 ATOM 446 N N . ARG A 1 87 ? 2.598 -6.548 8.988 1.00 79.66 ? 87 ARG A N 1 ATOM 447 C CA . ARG A 1 87 ? 2.279 -5.607 10.042 1.00 90.91 ? 87 ARG A CA 1 ATOM 448 C C . ARG A 1 87 ? 0.790 -5.557 10.272 1.00 85.71 ? 87 ARG A C 1 ATOM 449 O O . ARG A 1 87 ? 0.267 -4.590 10.832 1.00 88.69 ? 87 ARG A O 1 ATOM 450 C CB . ARG A 1 87 ? 2.816 -4.229 9.683 1.00 106.92 ? 87 ARG A CB 1 ATOM 451 C CG . ARG A 1 87 ? 4.330 -4.150 9.677 1.00 107.37 ? 87 ARG A CG 1 ATOM 452 C CD . ARG A 1 87 ? 4.863 -3.973 11.080 1.00 113.48 ? 87 ARG A CD 1 ATOM 453 N NE . ARG A 1 87 ? 6.314 -3.818 11.089 1.00 122.17 ? 87 ARG A NE 1 ATOM 454 C CZ . ARG A 1 87 ? 6.957 -2.704 10.748 1.00 119.16 ? 87 ARG A CZ 1 ATOM 455 N NH1 . ARG A 1 87 ? 6.284 -1.626 10.359 1.00 102.10 ? 87 ARG A NH1 1 ATOM 456 N NH2 . ARG A 1 87 ? 8.282 -2.673 10.796 1.00 127.17 ? 87 ARG A NH2 1 ATOM 457 N N . ILE A 1 88 ? 0.115 -6.616 9.844 1.00 76.64 ? 88 ILE A N 1 ATOM 458 C CA . ILE A 1 88 ? -1.339 -6.597 9.755 1.00 76.43 ? 88 ILE A CA 1 ATOM 459 C C . ILE A 1 88 ? -2.013 -6.341 11.096 1.00 69.19 ? 88 ILE A C 1 ATOM 460 O O . ILE A 1 88 ? -1.884 -7.149 12.019 1.00 65.90 ? 88 ILE A O 1 ATOM 461 C CB . ILE A 1 88 ? -1.899 -7.897 9.154 1.00 59.29 ? 88 ILE A CB 1 ATOM 462 C CG1 . ILE A 1 88 ? -1.250 -8.177 7.796 1.00 64.66 ? 88 ILE A CG1 1 ATOM 463 C CG2 . ILE A 1 88 ? -3.403 -7.789 9.014 1.00 49.01 ? 88 ILE A CG2 1 ATOM 464 C CD1 . ILE A 1 88 ? -1.619 -9.521 7.168 1.00 61.54 ? 88 ILE A CD1 1 ATOM 465 N N . ASN A 1 89 ? -2.740 -5.226 11.198 1.00 47.98 ? 89 ASN A N 1 ATOM 466 C CA . ASN A 1 89 ? -3.468 -4.946 12.425 1.00 64.48 ? 89 ASN A CA 1 ATOM 467 C C . ASN A 1 89 ? -4.988 -4.863 12.265 1.00 61.89 ? 89 ASN A C 1 ATOM 468 O O . ASN A 1 89 ? -5.720 -4.901 13.239 1.00 69.16 ? 89 ASN A O 1 ATOM 469 C CB . ASN A 1 89 ? -2.892 -3.721 13.155 1.00 79.32 ? 89 ASN A CB 1 ATOM 470 C CG . ASN A 1 89 ? -3.419 -2.414 12.615 1.00 82.02 ? 89 ASN A CG 1 ATOM 471 O OD1 . ASN A 1 89 ? -4.039 -2.375 11.558 1.00 87.44 ? 89 ASN A OD1 1 ATOM 472 N ND2 . ASN A 1 89 ? -3.173 -1.331 13.344 1.00 81.12 ? 89 ASN A ND2 1 ATOM 473 N N . THR A 1 90 ? -5.472 -4.770 11.040 1.00 57.76 ? 90 THR A N 1 ATOM 474 C CA . THR A 1 90 ? -6.916 -4.826 10.846 1.00 68.63 ? 90 THR A CA 1 ATOM 475 C C . THR A 1 90 ? -7.307 -5.369 9.468 1.00 74.35 ? 90 THR A C 1 ATOM 476 O O . THR A 1 90 ? -6.840 -4.888 8.437 1.00 83.60 ? 90 THR A O 1 ATOM 477 C CB . THR A 1 90 ? -7.622 -3.467 11.205 1.00 64.44 ? 90 THR A CB 1 ATOM 478 O OG1 . THR A 1 90 ? -8.604 -3.139 10.215 1.00 64.18 ? 90 THR A OG1 1 ATOM 479 C CG2 . THR A 1 90 ? -6.630 -2.328 11.305 1.00 52.32 ? 90 THR A CG2 1 ATOM 480 N N . ILE A 1 91 ? -8.151 -6.396 9.471 1.00 70.07 ? 91 ILE A N 1 ATOM 481 C CA . ILE A 1 91 ? -8.580 -7.063 8.245 1.00 55.14 ? 91 ILE A CA 1 ATOM 482 C C . ILE A 1 91 ? -10.079 -6.982 8.138 1.00 57.30 ? 91 ILE A C 1 ATOM 483 O O . ILE A 1 91 ? -10.781 -7.554 8.966 1.00 67.96 ? 91 ILE A O 1 ATOM 484 C CB . ILE A 1 91 ? -8.254 -8.565 8.273 1.00 46.32 ? 91 ILE A CB 1 ATOM 485 C CG1 . ILE A 1 91 ? -6.744 -8.801 8.303 1.00 41.78 ? 91 ILE A CG1 1 ATOM 486 C CG2 . ILE A 1 91 ? -8.895 -9.265 7.088 1.00 48.74 ? 91 ILE A CG2 1 ATOM 487 C CD1 . ILE A 1 91 ? -6.369 -10.204 8.669 1.00 38.44 ? 91 ILE A CD1 1 ATOM 488 N N . GLU A 1 92 ? -10.579 -6.287 7.125 1.00 59.04 ? 92 GLU A N 1 ATOM 489 C CA . GLU A 1 92 ? -12.020 -6.208 6.933 1.00 66.05 ? 92 GLU A CA 1 ATOM 490 C C . GLU A 1 92 ? -12.641 -7.594 6.998 1.00 62.54 ? 92 GLU A C 1 ATOM 491 O O . GLU A 1 92 ? -12.018 -8.567 6.599 1.00 51.31 ? 92 GLU A O 1 ATOM 492 C CB . GLU A 1 92 ? -12.348 -5.524 5.610 1.00 74.02 ? 92 GLU A CB 1 ATOM 493 C CG . GLU A 1 92 ? -12.268 -4.017 5.688 1.00 77.42 ? 92 GLU A CG 1 ATOM 494 C CD . GLU A 1 92 ? -13.156 -3.456 6.777 1.00 85.01 ? 92 GLU A CD 1 ATOM 495 O OE1 . GLU A 1 92 ? -13.982 -4.217 7.338 1.00 96.21 ? 92 GLU A OE1 1 ATOM 496 O OE2 . GLU A 1 92 ? -13.024 -2.253 7.071 1.00 75.44 ? 92 GLU A OE2 1 ATOM 497 N N . GLY A 1 93 ? -13.863 -7.680 7.511 1.00 65.23 ? 93 GLY A N 1 ATOM 498 C CA . GLY A 1 93 ? -14.478 -8.968 7.780 1.00 57.16 ? 93 GLY A CA 1 ATOM 499 C C . GLY A 1 93 ? -14.544 -9.915 6.601 1.00 62.40 ? 93 GLY A C 1 ATOM 500 O O . GLY A 1 93 ? -14.326 -11.119 6.762 1.00 55.97 ? 93 GLY A O 1 ATOM 501 N N . ASP A 1 94 ? -14.846 -9.371 5.418 1.00 68.00 ? 94 ASP A N 1 ATOM 502 C CA . ASP A 1 94 ? -15.039 -10.166 4.191 1.00 67.73 ? 94 ASP A CA 1 ATOM 503 C C . ASP A 1 94 ? -13.822 -10.202 3.259 1.00 58.85 ? 94 ASP A C 1 ATOM 504 O O . ASP A 1 94 ? -13.932 -10.535 2.083 1.00 59.40 ? 94 ASP A O 1 ATOM 505 C CB . ASP A 1 94 ? -16.264 -9.681 3.411 1.00 62.09 ? 94 ASP A CB 1 ATOM 506 C CG . ASP A 1 94 ? -16.191 -8.209 3.065 1.00 72.45 ? 94 ASP A CG 1 ATOM 507 O OD1 . ASP A 1 94 ? -15.506 -7.456 3.790 1.00 80.06 ? 94 ASP A OD1 1 ATOM 508 O OD2 . ASP A 1 94 ? -16.836 -7.801 2.079 1.00 76.77 ? 94 ASP A OD2 1 ATOM 509 N N . ALA A 1 95 ? -12.666 -9.867 3.807 1.00 48.74 ? 95 ALA A N 1 ATOM 510 C CA . ALA A 1 95 ? -11.435 -9.846 3.061 1.00 54.13 ? 95 ALA A CA 1 ATOM 511 C C . ALA A 1 95 ? -11.223 -11.149 2.324 1.00 57.23 ? 95 ALA A C 1 ATOM 512 O O . ALA A 1 95 ? -10.659 -11.160 1.236 1.00 75.81 ? 95 ALA A O 1 ATOM 513 C CB . ALA A 1 95 ? -10.267 -9.582 3.999 1.00 63.69 ? 95 ALA A CB 1 ATOM 514 N N . PHE A 1 96 ? -11.668 -12.253 2.906 1.00 49.76 ? 96 PHE A N 1 ATOM 515 C CA . PHE A 1 96 ? -11.291 -13.555 2.363 1.00 61.90 ? 96 PHE A CA 1 ATOM 516 C C . PHE A 1 96 ? -12.420 -14.309 1.656 1.00 62.45 ? 96 PHE A C 1 ATOM 517 O O . PHE A 1 96 ? -12.219 -15.445 1.227 1.00 55.67 ? 96 PHE A O 1 ATOM 518 C CB . PHE A 1 96 ? -10.679 -14.452 3.446 1.00 63.73 ? 96 PHE A CB 1 ATOM 519 C CG . PHE A 1 96 ? -9.506 -13.844 4.175 1.00 67.07 ? 96 PHE A CG 1 ATOM 520 C CD1 . PHE A 1 96 ? -8.380 -13.424 3.494 1.00 71.71 ? 96 PHE A CD1 1 ATOM 521 C CD2 . PHE A 1 96 ? -9.512 -13.738 5.554 1.00 68.64 ? 96 PHE A CD2 1 ATOM 522 C CE1 . PHE A 1 96 ? -7.291 -12.889 4.176 1.00 66.22 ? 96 PHE A CE1 1 ATOM 523 C CE2 . PHE A 1 96 ? -8.423 -13.201 6.234 1.00 67.06 ? 96 PHE A CE2 1 ATOM 524 C CZ . PHE A 1 96 ? -7.315 -12.780 5.540 1.00 60.86 ? 96 PHE A CZ 1 ATOM 525 N N . TYR A 1 97 ? -13.584 -13.674 1.524 1.00 61.37 ? 97 TYR A N 1 ATOM 526 C CA . TYR A 1 97 ? -14.784 -14.312 0.966 1.00 66.72 ? 97 TYR A CA 1 ATOM 527 C C . TYR A 1 97 ? -14.633 -14.993 -0.415 1.00 69.04 ? 97 TYR A C 1 ATOM 528 O O . TYR A 1 97 ? -15.319 -15.967 -0.721 1.00 59.77 ? 97 TYR A O 1 ATOM 529 C CB . TYR A 1 97 ? -15.938 -13.302 0.906 1.00 69.90 ? 97 TYR A CB 1 ATOM 530 C CG . TYR A 1 97 ? -16.710 -13.141 2.193 1.00 86.51 ? 97 TYR A CG 1 ATOM 531 C CD1 . TYR A 1 97 ? -16.137 -13.464 3.414 1.00 95.04 ? 97 TYR A CD1 1 ATOM 532 C CD2 . TYR A 1 97 ? -18.009 -12.634 2.192 1.00 97.26 ? 97 TYR A CD2 1 ATOM 533 C CE1 . TYR A 1 97 ? -16.839 -13.306 4.605 1.00 103.41 ? 97 TYR A CE1 1 ATOM 534 C CE2 . TYR A 1 97 ? -18.723 -12.469 3.377 1.00 102.80 ? 97 TYR A CE2 1 ATOM 535 C CZ . TYR A 1 97 ? -18.128 -12.806 4.582 1.00 109.13 ? 97 TYR A CZ 1 ATOM 536 O OH . TYR A 1 97 ? -18.815 -12.645 5.767 1.00 112.51 ? 97 TYR A OH 1 ATOM 537 N N . SER A 1 98 ? -13.764 -14.479 -1.268 1.00 78.30 ? 98 SER A N 1 ATOM 538 C CA . SER A 1 98 ? -13.717 -15.015 -2.619 1.00 75.11 ? 98 SER A CA 1 ATOM 539 C C . SER A 1 98 ? -12.621 -16.062 -2.774 1.00 65.87 ? 98 SER A C 1 ATOM 540 O O . SER A 1 98 ? -12.429 -16.590 -3.858 1.00 56.78 ? 98 SER A O 1 ATOM 541 C CB . SER A 1 98 ? -13.582 -13.895 -3.656 1.00 73.29 ? 98 SER A CB 1 ATOM 542 O OG . SER A 1 98 ? -12.426 -13.117 -3.420 1.00 81.02 ? 98 SER A OG 1 ATOM 543 N N . LEU A 1 99 ? -11.941 -16.387 -1.676 1.00 66.93 ? 99 LEU A N 1 ATOM 544 C CA . LEU A 1 99 ? -10.815 -17.325 -1.689 1.00 75.74 ? 99 LEU A CA 1 ATOM 545 C C . LEU A 1 99 ? -11.200 -18.806 -1.515 1.00 72.39 ? 99 LEU A C 1 ATOM 546 O O . LEU A 1 99 ? -10.405 -19.603 -1.021 1.00 83.66 ? 99 LEU A O 1 ATOM 547 C CB . LEU A 1 99 ? -9.820 -16.940 -0.593 1.00 77.85 ? 99 LEU A CB 1 ATOM 548 C CG . LEU A 1 99 ? -9.041 -15.643 -0.776 1.00 73.37 ? 99 LEU A CG 1 ATOM 549 C CD1 . LEU A 1 99 ? -8.598 -15.103 0.563 1.00 76.90 ? 99 LEU A CD1 1 ATOM 550 C CD2 . LEU A 1 99 ? -7.852 -15.898 -1.646 1.00 72.81 ? 99 LEU A CD2 1 ATOM 551 N N . GLY A 1 100 ? -12.406 -19.166 -1.933 1.00 52.72 ? 100 GLY A N 1 ATOM 552 C CA . GLY A 1 100 ? -12.976 -20.474 -1.667 1.00 46.99 ? 100 GLY A CA 1 ATOM 553 C C . GLY A 1 100 ? -12.209 -21.745 -1.992 1.00 58.81 ? 100 GLY A C 1 ATOM 554 O O . GLY A 1 100 ? -12.746 -22.833 -1.799 1.00 73.41 ? 100 GLY A O 1 ATOM 555 N N . SER A 1 101 ? -10.976 -21.632 -2.477 1.00 43.46 ? 101 SER A N 1 ATOM 556 C CA . SER A 1 101 ? -10.176 -22.808 -2.823 1.00 43.21 ? 101 SER A CA 1 ATOM 557 C C . SER A 1 101 ? -8.954 -22.840 -1.934 1.00 61.34 ? 101 SER A C 1 ATOM 558 O O . SER A 1 101 ? -8.122 -23.754 -2.016 1.00 65.90 ? 101 SER A O 1 ATOM 559 C CB . SER A 1 101 ? -9.702 -22.755 -4.286 1.00 55.38 ? 101 SER A CB 1 ATOM 560 O OG . SER A 1 101 ? -10.738 -23.040 -5.214 1.00 70.18 ? 101 SER A OG 1 ATOM 561 N N . LEU A 1 102 ? -8.851 -21.816 -1.094 1.00 67.07 ? 102 LEU A N 1 ATOM 562 C CA . LEU A 1 102 ? -7.669 -21.581 -0.282 1.00 67.05 ? 102 LEU A CA 1 ATOM 563 C C . LEU A 1 102 ? -7.561 -22.642 0.791 1.00 59.48 ? 102 LEU A C 1 ATOM 564 O O . LEU A 1 102 ? -8.514 -22.881 1.525 1.00 58.19 ? 102 LEU A O 1 ATOM 565 C CB . LEU A 1 102 ? -7.762 -20.196 0.351 1.00 68.81 ? 102 LEU A CB 1 ATOM 566 C CG . LEU A 1 102 ? -6.651 -19.754 1.291 1.00 61.96 ? 102 LEU A CG 1 ATOM 567 C CD1 . LEU A 1 102 ? -5.359 -19.528 0.515 1.00 50.65 ? 102 LEU A CD1 1 ATOM 568 C CD2 . LEU A 1 102 ? -7.119 -18.491 1.981 1.00 63.51 ? 102 LEU A CD2 1 ATOM 569 N N . GLU A 1 103 ? -6.411 -23.296 0.877 1.00 57.12 ? 103 GLU A N 1 ATOM 570 C CA . GLU A 1 103 ? -6.256 -24.334 1.884 1.00 64.05 ? 103 GLU A CA 1 ATOM 571 C C . GLU A 1 103 ? -5.185 -24.053 2.956 1.00 69.26 ? 103 GLU A C 1 ATOM 572 O O . GLU A 1 103 ? -5.251 -24.600 4.054 1.00 69.60 ? 103 GLU A O 1 ATOM 573 C CB . GLU A 1 103 ? -6.110 -25.726 1.246 1.00 66.25 ? 103 GLU A CB 1 ATOM 574 C CG . GLU A 1 103 ? -5.458 -25.787 -0.127 1.00 69.45 ? 103 GLU A CG 1 ATOM 575 C CD . GLU A 1 103 ? -5.642 -27.156 -0.802 1.00 82.98 ? 103 GLU A CD 1 ATOM 576 O OE1 . GLU A 1 103 ? -5.654 -28.178 -0.083 1.00 88.88 ? 103 GLU A OE1 1 ATOM 577 O OE2 . GLU A 1 103 ? -5.776 -27.218 -2.048 1.00 86.29 ? 103 GLU A OE2 1 ATOM 578 N N . HIS A 1 104 ? -4.227 -23.182 2.641 1.00 68.39 ? 104 HIS A N 1 ATOM 579 C CA . HIS A 1 104 ? -3.166 -22.795 3.575 1.00 60.55 ? 104 HIS A CA 1 ATOM 580 C C . HIS A 1 104 ? -3.229 -21.291 3.868 1.00 64.01 ? 104 HIS A C 1 ATOM 581 O O . HIS A 1 104 ? -2.996 -20.477 2.983 1.00 75.18 ? 104 HIS A O 1 ATOM 582 C CB . HIS A 1 104 ? -1.802 -23.160 2.978 1.00 56.92 ? 104 HIS A CB 1 ATOM 583 C CG . HIS A 1 104 ? -0.648 -22.988 3.920 1.00 65.76 ? 104 HIS A CG 1 ATOM 584 N ND1 . HIS A 1 104 ? 0.142 -24.041 4.328 1.00 72.41 ? 104 HIS A ND1 1 ATOM 585 C CD2 . HIS A 1 104 ? -0.138 -21.883 4.517 1.00 58.86 ? 104 HIS A CD2 1 ATOM 586 C CE1 . HIS A 1 104 ? 1.083 -23.596 5.144 1.00 63.07 ? 104 HIS A CE1 1 ATOM 587 N NE2 . HIS A 1 104 ? 0.938 -22.290 5.271 1.00 61.17 ? 104 HIS A NE2 1 ATOM 588 N N . LEU A 1 105 ? -3.552 -20.921 5.102 1.00 59.10 ? 105 LEU A N 1 ATOM 589 C CA . LEU A 1 105 ? -3.618 -19.506 5.487 1.00 53.82 ? 105 LEU A CA 1 ATOM 590 C C . LEU A 1 105 ? -2.757 -19.240 6.714 1.00 58.38 ? 105 LEU A C 1 ATOM 591 O O . LEU A 1 105 ? -2.981 -19.806 7.782 1.00 60.98 ? 105 LEU A O 1 ATOM 592 C CB . LEU A 1 105 ? -5.062 -19.049 5.749 1.00 47.07 ? 105 LEU A CB 1 ATOM 593 C CG . LEU A 1 105 ? -5.198 -17.669 6.392 1.00 43.47 ? 105 LEU A CG 1 ATOM 594 C CD1 . LEU A 1 105 ? -4.699 -16.615 5.463 1.00 48.73 ? 105 LEU A CD1 1 ATOM 595 C CD2 . LEU A 1 105 ? -6.627 -17.365 6.755 1.00 51.16 ? 105 LEU A CD2 1 ATOM 596 N N . ASP A 1 106 ? -1.775 -18.363 6.553 1.00 57.40 ? 106 ASP A N 1 ATOM 597 C CA . ASP A 1 106 ? -0.793 -18.117 7.594 1.00 55.37 ? 106 ASP A CA 1 ATOM 598 C C . ASP A 1 106 ? -0.775 -16.643 7.993 1.00 55.79 ? 106 ASP A C 1 ATOM 599 O O . ASP A 1 106 ? -0.196 -15.821 7.289 1.00 49.93 ? 106 ASP A O 1 ATOM 600 C CB . ASP A 1 106 ? 0.578 -18.571 7.107 1.00 53.38 ? 106 ASP A CB 1 ATOM 601 C CG . ASP A 1 106 ? 1.664 -18.377 8.133 1.00 69.35 ? 106 ASP A CG 1 ATOM 602 O OD1 . ASP A 1 106 ? 1.375 -17.918 9.265 1.00 73.55 ? 106 ASP A OD1 1 ATOM 603 O OD2 . ASP A 1 106 ? 2.823 -18.687 7.791 1.00 74.39 ? 106 ASP A OD2 1 ATOM 604 N N . LEU A 1 107 ? -1.412 -16.326 9.124 1.00 55.34 ? 107 LEU A N 1 ATOM 605 C CA . LEU A 1 107 ? -1.481 -14.957 9.628 1.00 57.87 ? 107 LEU A CA 1 ATOM 606 C C . LEU A 1 107 ? -0.616 -14.770 10.862 1.00 59.45 ? 107 LEU A C 1 ATOM 607 O O . LEU A 1 107 ? -0.735 -13.764 11.561 1.00 57.23 ? 107 LEU A O 1 ATOM 608 C CB . LEU A 1 107 ? -2.915 -14.563 9.975 1.00 48.22 ? 107 LEU A CB 1 ATOM 609 C CG . LEU A 1 107 ? -3.956 -14.541 8.865 1.00 51.47 ? 107 LEU A CG 1 ATOM 610 C CD1 . LEU A 1 107 ? -5.271 -14.121 9.449 1.00 51.90 ? 107 LEU A CD1 1 ATOM 611 C CD2 . LEU A 1 107 ? -3.556 -13.601 7.771 1.00 63.16 ? 107 LEU A CD2 1 ATOM 612 N N . SER A 1 108 ? 0.251 -15.736 11.138 1.00 57.58 ? 108 SER A N 1 ATOM 613 C CA . SER A 1 108 ? 1.103 -15.642 12.324 1.00 64.19 ? 108 SER A CA 1 ATOM 614 C C . SER A 1 108 ? 1.934 -14.351 12.399 1.00 62.35 ? 108 SER A C 1 ATOM 615 O O . SER A 1 108 ? 2.320 -13.785 11.380 1.00 62.57 ? 108 SER A O 1 ATOM 616 C CB . SER A 1 108 ? 2.014 -16.872 12.441 1.00 59.39 ? 108 SER A CB 1 ATOM 617 O OG . SER A 1 108 ? 3.005 -16.898 11.428 1.00 52.11 ? 108 SER A OG 1 ATOM 618 N N . ASP A 1 109 ? 2.184 -13.900 13.626 1.00 68.96 ? 109 ASP A N 1 ATOM 619 C CA . ASP A 1 109 ? 3.151 -12.836 13.937 1.00 73.64 ? 109 ASP A CA 1 ATOM 620 C C . ASP A 1 109 ? 2.745 -11.441 13.492 1.00 72.60 ? 109 ASP A C 1 ATOM 621 O O . ASP A 1 109 ? 3.582 -10.657 13.057 1.00 79.80 ? 109 ASP A O 1 ATOM 622 C CB . ASP A 1 109 ? 4.550 -13.175 13.409 1.00 73.20 ? 109 ASP A CB 1 ATOM 623 C CG . ASP A 1 109 ? 5.151 -14.398 14.091 1.00 84.89 ? 109 ASP A CG 1 ATOM 624 O OD1 . ASP A 1 109 ? 4.855 -14.633 15.296 1.00 77.10 ? 109 ASP A OD1 1 ATOM 625 O OD2 . ASP A 1 109 ? 5.913 -15.126 13.411 1.00 86.16 ? 109 ASP A OD2 1 ATOM 626 N N . ASN A 1 110 ? 1.463 -11.133 13.617 1.00 63.56 ? 110 ASN A N 1 ATOM 627 C CA . ASN A 1 110 ? 0.973 -9.819 13.258 1.00 69.88 ? 110 ASN A CA 1 ATOM 628 C C . ASN A 1 110 ? 0.392 -9.148 14.483 1.00 79.31 ? 110 ASN A C 1 ATOM 629 O O . ASN A 1 110 ? 0.489 -9.695 15.575 1.00 86.12 ? 110 ASN A O 1 ATOM 630 C CB . ASN A 1 110 ? -0.060 -9.926 12.138 1.00 68.37 ? 110 ASN A CB 1 ATOM 631 C CG . ASN A 1 110 ? 0.547 -10.416 10.843 1.00 59.37 ? 110 ASN A CG 1 ATOM 632 O OD1 . ASN A 1 110 ? 0.797 -11.605 10.678 1.00 62.60 ? 110 ASN A OD1 1 ATOM 633 N ND2 . ASN A 1 110 ? 0.788 -9.502 9.917 1.00 52.71 ? 110 ASN A ND2 1 ATOM 634 N N . HIS A 1 111 ? -0.204 -7.971 14.310 1.00 81.13 ? 111 HIS A N 1 ATOM 635 C CA . HIS A 1 111 ? -0.771 -7.232 15.435 1.00 74.57 ? 111 HIS A CA 1 ATOM 636 C C . HIS A 1 111 ? -2.273 -7.340 15.462 1.00 72.29 ? 111 HIS A C 1 ATOM 637 O O . HIS A 1 111 ? -2.958 -6.353 15.732 1.00 73.74 ? 111 HIS A O 1 ATOM 638 C CB . HIS A 1 111 ? -0.392 -5.752 15.384 1.00 76.02 ? 111 HIS A CB 1 ATOM 639 C CG . HIS A 1 111 ? 1.060 -5.507 15.127 1.00 79.25 ? 111 HIS A CG 1 ATOM 640 N ND1 . HIS A 1 111 ? 1.508 -4.505 14.293 1.00 92.00 ? 111 HIS A ND1 1 ATOM 641 C CD2 . HIS A 1 111 ? 2.166 -6.141 15.583 1.00 67.51 ? 111 HIS A CD2 1 ATOM 642 C CE1 . HIS A 1 111 ? 2.828 -4.529 14.252 1.00 87.88 ? 111 HIS A CE1 1 ATOM 643 N NE2 . HIS A 1 111 ? 3.251 -5.511 15.026 1.00 75.55 ? 111 HIS A NE2 1 ATOM 644 N N . LEU A 1 112 ? -2.782 -8.533 15.169 1.00 67.14 ? 112 LEU A N 1 ATOM 645 C CA . LEU A 1 112 ? -4.215 -8.796 15.256 1.00 74.34 ? 112 LEU A CA 1 ATOM 646 C C . LEU A 1 112 ? -4.696 -8.772 16.718 1.00 75.73 ? 112 LEU A C 1 ATOM 647 O O . LEU A 1 112 ? -4.600 -9.763 17.441 1.00 65.76 ? 112 LEU A O 1 ATOM 648 C CB . LEU A 1 112 ? -4.552 -10.120 14.564 1.00 69.20 ? 112 LEU A CB 1 ATOM 649 C CG . LEU A 1 112 ? -4.965 -10.088 13.083 1.00 60.83 ? 112 LEU A CG 1 ATOM 650 C CD1 . LEU A 1 112 ? -4.658 -8.755 12.396 1.00 55.08 ? 112 LEU A CD1 1 ATOM 651 C CD2 . LEU A 1 112 ? -4.375 -11.272 12.321 1.00 42.49 ? 112 LEU A CD2 1 ATOM 652 N N . SER A 1 113 ? -5.209 -7.623 17.145 1.00 81.26 ? 113 SER A N 1 ATOM 653 C CA . SER A 1 113 ? -5.532 -7.402 18.550 1.00 77.26 ? 113 SER A CA 1 ATOM 654 C C . SER A 1 113 ? -6.685 -8.288 18.968 1.00 69.76 ? 113 SER A C 1 ATOM 655 O O . SER A 1 113 ? -6.930 -8.503 20.146 1.00 71.47 ? 113 SER A O 1 ATOM 656 C CB . SER A 1 113 ? -5.890 -5.934 18.787 1.00 87.86 ? 113 SER A CB 1 ATOM 657 O OG . SER A 1 113 ? -4.909 -5.063 18.240 1.00 92.87 ? 113 SER A OG 1 ATOM 658 N N . SER A 1 114 ? -7.395 -8.803 17.981 1.00 78.32 ? 114 SER A N 1 ATOM 659 C CA . SER A 1 114 ? -8.531 -9.666 18.240 1.00 84.26 ? 114 SER A CA 1 ATOM 660 C C . SER A 1 114 ? -9.003 -10.245 16.913 1.00 80.01 ? 114 SER A C 1 ATOM 661 O O . SER A 1 114 ? -8.676 -9.718 15.856 1.00 81.30 ? 114 SER A O 1 ATOM 662 C CB . SER A 1 114 ? -9.646 -8.876 18.907 1.00 81.00 ? 114 SER A CB 1 ATOM 663 O OG . SER A 1 114 ? -10.097 -7.872 18.029 1.00 75.01 ? 114 SER A OG 1 ATOM 664 N N . LEU A 1 115 ? -9.770 -11.326 16.975 1.00 70.88 ? 115 LEU A N 1 ATOM 665 C CA . LEU A 1 115 ? -10.085 -12.113 15.788 1.00 64.33 ? 115 LEU A CA 1 ATOM 666 C C . LEU A 1 115 ? -11.560 -12.008 15.420 1.00 70.10 ? 115 LEU A C 1 ATOM 667 O O . LEU A 1 115 ? -12.407 -11.774 16.278 1.00 74.95 ? 115 LEU A O 1 ATOM 668 C CB . LEU A 1 115 ? -9.688 -13.579 16.013 1.00 52.36 ? 115 LEU A CB 1 ATOM 669 C CG . LEU A 1 115 ? -8.319 -13.768 16.671 1.00 47.65 ? 115 LEU A CG 1 ATOM 670 C CD1 . LEU A 1 115 ? -7.941 -15.226 16.821 1.00 46.60 ? 115 LEU A CD1 1 ATOM 671 C CD2 . LEU A 1 115 ? -7.270 -13.047 15.867 1.00 56.05 ? 115 LEU A CD2 1 ATOM 672 N N . SER A 1 116 ? -11.865 -12.178 14.139 1.00 64.27 ? 116 SER A N 1 ATOM 673 C CA . SER A 1 116 ? -13.238 -12.055 13.678 1.00 62.14 ? 116 SER A CA 1 ATOM 674 C C . SER A 1 116 ? -13.778 -13.396 13.168 1.00 67.47 ? 116 SER A C 1 ATOM 675 O O . SER A 1 116 ? -13.090 -14.125 12.457 1.00 67.89 ? 116 SER A O 1 ATOM 676 C CB . SER A 1 116 ? -13.325 -10.992 12.593 1.00 56.46 ? 116 SER A CB 1 ATOM 677 O OG . SER A 1 116 ? -14.676 -10.685 12.303 1.00 65.28 ? 116 SER A OG 1 ATOM 678 N N . SER A 1 117 ? -15.008 -13.726 13.544 1.00 65.78 ? 117 SER A N 1 ATOM 679 C CA . SER A 1 117 ? -15.600 -14.997 13.147 1.00 67.90 ? 117 SER A CA 1 ATOM 680 C C . SER A 1 117 ? -15.843 -15.043 11.642 1.00 82.49 ? 117 SER A C 1 ATOM 681 O O . SER A 1 117 ? -16.045 -16.117 11.065 1.00 87.85 ? 117 SER A O 1 ATOM 682 C CB . SER A 1 117 ? -16.911 -15.214 13.892 1.00 67.21 ? 117 SER A CB 1 ATOM 683 O OG . SER A 1 117 ? -17.718 -14.053 13.819 1.00 72.45 ? 117 SER A OG 1 ATOM 684 N N . SER A 1 118 ? -15.799 -13.865 11.019 1.00 78.48 ? 118 SER A N 1 ATOM 685 C CA . SER A 1 118 ? -16.140 -13.683 9.608 1.00 66.23 ? 118 SER A CA 1 ATOM 686 C C . SER A 1 118 ? -15.025 -14.048 8.630 1.00 65.67 ? 118 SER A C 1 ATOM 687 O O . SER A 1 118 ? -15.285 -14.369 7.469 1.00 73.95 ? 118 SER A O 1 ATOM 688 C CB . SER A 1 118 ? -16.549 -12.229 9.360 1.00 66.39 ? 118 SER A CB 1 ATOM 689 O OG . SER A 1 118 ? -17.749 -11.909 10.036 1.00 68.64 ? 118 SER A OG 1 ATOM 690 N N . TRP A 1 119 ? -13.784 -13.975 9.090 1.00 61.28 ? 119 TRP A N 1 ATOM 691 C CA . TRP A 1 119 ? -12.647 -14.223 8.217 1.00 57.65 ? 119 TRP A CA 1 ATOM 692 C C . TRP A 1 119 ? -12.596 -15.635 7.663 1.00 56.80 ? 119 TRP A C 1 ATOM 693 O O . TRP A 1 119 ? -12.113 -15.859 6.558 1.00 58.11 ? 119 TRP A O 1 ATOM 694 C CB . TRP A 1 119 ? -11.344 -13.978 8.961 1.00 49.93 ? 119 TRP A CB 1 ATOM 695 C CG . TRP A 1 119 ? -11.118 -12.582 9.387 1.00 53.53 ? 119 TRP A CG 1 ATOM 696 C CD1 . TRP A 1 119 ? -11.661 -11.451 8.852 1.00 49.28 ? 119 TRP A CD1 1 ATOM 697 C CD2 . TRP A 1 119 ? -10.240 -12.156 10.427 1.00 61.04 ? 119 TRP A CD2 1 ATOM 698 N NE1 . TRP A 1 119 ? -11.180 -10.345 9.509 1.00 51.58 ? 119 TRP A NE1 1 ATOM 699 C CE2 . TRP A 1 119 ? -10.310 -10.753 10.482 1.00 52.94 ? 119 TRP A CE2 1 ATOM 700 C CE3 . TRP A 1 119 ? -9.414 -12.830 11.331 1.00 59.57 ? 119 TRP A CE3 1 ATOM 701 C CZ2 . TRP A 1 119 ? -9.585 -10.017 11.398 1.00 59.03 ? 119 TRP A CZ2 1 ATOM 702 C CZ3 . TRP A 1 119 ? -8.695 -12.095 12.237 1.00 63.02 ? 119 TRP A CZ3 1 ATOM 703 C CH2 . TRP A 1 119 ? -8.781 -10.704 12.265 1.00 64.70 ? 119 TRP A CH2 1 ATOM 704 N N . PHE A 1 120 ? -13.074 -16.590 8.443 1.00 57.38 ? 120 PHE A N 1 ATOM 705 C CA . PHE A 1 120 ? -12.812 -17.987 8.154 1.00 63.35 ? 120 PHE A CA 1 ATOM 706 C C . PHE A 1 120 ? -14.020 -18.756 7.617 1.00 73.66 ? 120 PHE A C 1 ATOM 707 O O . PHE A 1 120 ? -13.881 -19.884 7.138 1.00 69.25 ? 120 PHE A O 1 ATOM 708 C CB . PHE A 1 120 ? -12.260 -18.647 9.409 1.00 63.83 ? 120 PHE A CB 1 ATOM 709 C CG . PHE A 1 120 ? -11.132 -17.889 10.023 1.00 70.79 ? 120 PHE A CG 1 ATOM 710 C CD1 . PHE A 1 120 ? -10.018 -17.568 9.275 1.00 67.03 ? 120 PHE A CD1 1 ATOM 711 C CD2 . PHE A 1 120 ? -11.182 -17.485 11.344 1.00 78.10 ? 120 PHE A CD2 1 ATOM 712 C CE1 . PHE A 1 120 ? -8.972 -16.862 9.840 1.00 71.29 ? 120 PHE A CE1 1 ATOM 713 C CE2 . PHE A 1 120 ? -10.131 -16.783 11.913 1.00 65.07 ? 120 PHE A CE2 1 ATOM 714 C CZ . PHE A 1 120 ? -9.029 -16.472 11.160 1.00 62.88 ? 120 PHE A CZ 1 ATOM 715 N N . GLY A 1 121 ? -15.191 -18.129 7.681 1.00 76.98 ? 121 GLY A N 1 ATOM 716 C CA . GLY A 1 121 ? -16.444 -18.768 7.316 1.00 80.82 ? 121 GLY A CA 1 ATOM 717 C C . GLY A 1 121 ? -16.518 -19.325 5.913 1.00 81.12 ? 121 GLY A C 1 ATOM 718 O O . GLY A 1 121 ? -16.923 -20.477 5.729 1.00 83.35 ? 121 GLY A O 1 ATOM 719 N N . PRO A 1 122 ? -16.142 -18.502 4.920 1.00 81.58 ? 122 PRO A N 1 ATOM 720 C CA . PRO A 1 122 ? -16.140 -18.805 3.484 1.00 73.89 ? 122 PRO A CA 1 ATOM 721 C C . PRO A 1 122 ? -15.012 -19.724 3.055 1.00 68.44 ? 122 PRO A C 1 ATOM 722 O O . PRO A 1 122 ? -15.057 -20.193 1.914 1.00 75.68 ? 122 PRO A O 1 ATOM 723 C CB . PRO A 1 122 ? -15.894 -17.435 2.852 1.00 68.12 ? 122 PRO A CB 1 ATOM 724 C CG . PRO A 1 122 ? -15.111 -16.721 3.881 1.00 83.09 ? 122 PRO A CG 1 ATOM 725 C CD . PRO A 1 122 ? -15.834 -17.083 5.146 1.00 85.51 ? 122 PRO A CD 1 ATOM 726 N N . LEU A 1 123 ? -14.024 -19.965 3.919 1.00 42.38 ? 123 LEU A N 1 ATOM 727 C CA . LEU A 1 123 ? -12.886 -20.809 3.541 1.00 59.78 ? 123 LEU A CA 1 ATOM 728 C C . LEU A 1 123 ? -13.097 -22.312 3.769 1.00 68.46 ? 123 LEU A C 1 ATOM 729 O O . LEU A 1 123 ? -12.219 -22.978 4.314 1.00 74.36 ? 123 LEU A O 1 ATOM 730 C CB . LEU A 1 123 ? -11.621 -20.386 4.286 1.00 62.63 ? 123 LEU A CB 1 ATOM 731 C CG . LEU A 1 123 ? -11.354 -18.903 4.486 1.00 56.43 ? 123 LEU A CG 1 ATOM 732 C CD1 . LEU A 1 123 ? -10.006 -18.757 5.137 1.00 54.37 ? 123 LEU A CD1 1 ATOM 733 C CD2 . LEU A 1 123 ? -11.394 -18.183 3.172 1.00 52.14 ? 123 LEU A CD2 1 ATOM 734 N N . SER A 1 124 ? -14.247 -22.837 3.350 1.00 67.90 ? 124 SER A N 1 ATOM 735 C CA . SER A 1 124 ? -14.544 -24.272 3.437 1.00 61.12 ? 124 SER A CA 1 ATOM 736 C C . SER A 1 124 ? -13.455 -25.211 2.856 1.00 61.51 ? 124 SER A C 1 ATOM 737 O O . SER A 1 124 ? -13.521 -26.427 3.017 1.00 64.75 ? 124 SER A O 1 ATOM 738 C CB . SER A 1 124 ? -15.912 -24.576 2.804 1.00 59.96 ? 124 SER A CB 1 ATOM 739 O OG . SER A 1 124 ? -15.891 -24.460 1.386 1.00 58.63 ? 124 SER A OG 1 ATOM 740 N N . SER A 1 125 ? -12.444 -24.656 2.203 1.00 58.25 ? 125 SER A N 1 ATOM 741 C CA . SER A 1 125 ? -11.389 -25.488 1.641 1.00 55.12 ? 125 SER A CA 1 ATOM 742 C C . SER A 1 125 ? -10.113 -25.523 2.488 1.00 62.06 ? 125 SER A C 1 ATOM 743 O O . SER A 1 125 ? -9.144 -26.210 2.143 1.00 61.19 ? 125 SER A O 1 ATOM 744 C CB . SER A 1 125 ? -11.061 -25.007 0.237 1.00 53.02 ? 125 SER A CB 1 ATOM 745 O OG . SER A 1 125 ? -12.050 -25.442 -0.667 1.00 62.36 ? 125 SER A OG 1 ATOM 746 N N . LEU A 1 126 ? -10.135 -24.793 3.601 1.00 53.35 ? 126 LEU A N 1 ATOM 747 C CA . LEU A 1 126 ? -8.950 -24.538 4.408 1.00 50.19 ? 126 LEU A CA 1 ATOM 748 C C . LEU A 1 126 ? -8.482 -25.797 5.128 1.00 57.82 ? 126 LEU A C 1 ATOM 749 O O . LEU A 1 126 ? -9.268 -26.465 5.788 1.00 63.36 ? 126 LEU A O 1 ATOM 750 C CB . LEU A 1 126 ? -9.251 -23.417 5.411 1.00 47.87 ? 126 LEU A CB 1 ATOM 751 C CG . LEU A 1 126 ? -8.120 -22.582 6.013 1.00 48.40 ? 126 LEU A CG 1 ATOM 752 C CD1 . LEU A 1 126 ? -7.350 -21.841 4.952 1.00 50.36 ? 126 LEU A CD1 1 ATOM 753 C CD2 . LEU A 1 126 ? -8.707 -21.594 6.972 1.00 59.81 ? 126 LEU A CD2 1 ATOM 754 N N . LYS A 1 127 ? -7.203 -26.124 4.980 1.00 60.07 ? 127 LYS A N 1 ATOM 755 C CA . LYS A 1 127 ? -6.605 -27.255 5.691 1.00 68.42 ? 127 LYS A CA 1 ATOM 756 C C . LYS A 1 127 ? -5.677 -26.788 6.825 1.00 67.37 ? 127 LYS A C 1 ATOM 757 O O . LYS A 1 127 ? -5.522 -27.461 7.845 1.00 67.60 ? 127 LYS A O 1 ATOM 758 C CB . LYS A 1 127 ? -5.823 -28.158 4.722 1.00 63.23 ? 127 LYS A CB 1 ATOM 759 C CG . LYS A 1 127 ? -6.676 -28.955 3.765 1.00 65.79 ? 127 LYS A CG 1 ATOM 760 C CD . LYS A 1 127 ? -5.863 -30.034 3.049 1.00 73.08 ? 127 LYS A CD 1 ATOM 761 C CE . LYS A 1 127 ? -6.651 -30.671 1.889 1.00 88.07 ? 127 LYS A CE 1 ATOM 762 N NZ . LYS A 1 127 ? -7.919 -31.361 2.307 1.00 89.18 ? 127 LYS A NZ 1 ATOM 763 N N . TYR A 1 128 ? -5.067 -25.625 6.631 1.00 59.20 ? 128 TYR A N 1 ATOM 764 C CA . TYR A 1 128 ? -4.028 -25.130 7.514 1.00 52.39 ? 128 TYR A CA 1 ATOM 765 C C . TYR A 1 128 ? -4.270 -23.664 7.847 1.00 59.46 ? 128 TYR A C 1 ATOM 766 O O . TYR A 1 128 ? -4.437 -22.847 6.950 1.00 70.29 ? 128 TYR A O 1 ATOM 767 C CB . TYR A 1 128 ? -2.676 -25.283 6.830 1.00 46.89 ? 128 TYR A CB 1 ATOM 768 C CG . TYR A 1 128 ? -1.552 -24.623 7.572 1.00 55.34 ? 128 TYR A CG 1 ATOM 769 C CD1 . TYR A 1 128 ? -0.620 -25.379 8.265 1.00 50.72 ? 128 TYR A CD1 1 ATOM 770 C CD2 . TYR A 1 128 ? -1.421 -23.232 7.583 1.00 65.37 ? 128 TYR A CD2 1 ATOM 771 C CE1 . TYR A 1 128 ? 0.418 -24.771 8.963 1.00 65.50 ? 128 TYR A CE1 1 ATOM 772 C CE2 . TYR A 1 128 ? -0.385 -22.609 8.279 1.00 69.91 ? 128 TYR A CE2 1 ATOM 773 C CZ . TYR A 1 128 ? 0.539 -23.384 8.969 1.00 66.21 ? 128 TYR A CZ 1 ATOM 774 O OH . TYR A 1 128 ? 1.579 -22.789 9.668 1.00 51.39 ? 128 TYR A OH 1 ATOM 775 N N . LEU A 1 129 ? -4.263 -23.333 9.135 1.00 56.15 ? 129 LEU A N 1 ATOM 776 C CA . LEU A 1 129 ? -4.546 -21.975 9.614 1.00 55.44 ? 129 LEU A CA 1 ATOM 777 C C . LEU A 1 129 ? -3.677 -21.655 10.817 1.00 60.71 ? 129 LEU A C 1 ATOM 778 O O . LEU A 1 129 ? -3.945 -22.120 11.925 1.00 66.28 ? 129 LEU A O 1 ATOM 779 C CB . LEU A 1 129 ? -6.020 -21.843 10.017 1.00 48.41 ? 129 LEU A CB 1 ATOM 780 C CG . LEU A 1 129 ? -6.460 -20.599 10.787 1.00 42.54 ? 129 LEU A CG 1 ATOM 781 C CD1 . LEU A 1 129 ? -6.334 -19.407 9.901 1.00 44.63 ? 129 LEU A CD1 1 ATOM 782 C CD2 . LEU A 1 129 ? -7.890 -20.740 11.271 1.00 40.60 ? 129 LEU A CD2 1 ATOM 783 N N . ASN A 1 130 ? -2.641 -20.859 10.599 1.00 59.55 ? 130 ASN A N 1 ATOM 784 C CA . ASN A 1 130 ? -1.731 -20.473 11.673 1.00 57.63 ? 130 ASN A CA 1 ATOM 785 C C . ASN A 1 130 ? -1.975 -19.031 12.158 1.00 61.81 ? 130 ASN A C 1 ATOM 786 O O . ASN A 1 130 ? -1.723 -18.051 11.446 1.00 59.26 ? 130 ASN A O 1 ATOM 787 C CB . ASN A 1 130 ? -0.287 -20.701 11.227 1.00 50.13 ? 130 ASN A CB 1 ATOM 788 C CG . ASN A 1 130 ? 0.728 -20.282 12.260 1.00 53.59 ? 130 ASN A CG 1 ATOM 789 O OD1 . ASN A 1 130 ? 0.379 -19.874 13.372 1.00 48.76 ? 130 ASN A OD1 1 ATOM 790 N ND2 . ASN A 1 130 ? 2.008 -20.379 11.893 1.00 53.96 ? 130 ASN A ND2 1 ATOM 791 N N . LEU A 1 131 ? -2.484 -18.925 13.381 1.00 57.49 ? 131 LEU A N 1 ATOM 792 C CA . LEU A 1 131 ? -2.855 -17.648 13.969 1.00 51.60 ? 131 LEU A CA 1 ATOM 793 C C . LEU A 1 131 ? -1.926 -17.177 15.104 1.00 60.98 ? 131 LEU A C 1 ATOM 794 O O . LEU A 1 131 ? -2.104 -16.073 15.619 1.00 48.56 ? 131 LEU A O 1 ATOM 795 C CB . LEU A 1 131 ? -4.288 -17.716 14.488 1.00 43.43 ? 131 LEU A CB 1 ATOM 796 C CG . LEU A 1 131 ? -5.423 -17.742 13.471 1.00 57.65 ? 131 LEU A CG 1 ATOM 797 C CD1 . LEU A 1 131 ? -6.754 -17.665 14.195 1.00 57.91 ? 131 LEU A CD1 1 ATOM 798 C CD2 . LEU A 1 131 ? -5.287 -16.585 12.492 1.00 64.30 ? 131 LEU A CD2 1 ATOM 799 N N . MET A 1 132 ? -0.946 -17.999 15.493 1.00 72.78 ? 132 MET A N 1 ATOM 800 C CA . MET A 1 132 ? -0.032 -17.643 16.591 1.00 73.00 ? 132 MET A CA 1 ATOM 801 C C . MET A 1 132 ? 0.672 -16.312 16.344 1.00 73.30 ? 132 MET A C 1 ATOM 802 O O . MET A 1 132 ? 0.868 -15.913 15.199 1.00 81.05 ? 132 MET A O 1 ATOM 803 C CB . MET A 1 132 ? 1.054 -18.699 16.773 1.00 57.91 ? 132 MET A CB 1 ATOM 804 C CG . MET A 1 132 ? 0.604 -20.032 17.261 1.00 53.34 ? 132 MET A CG 1 ATOM 805 S SD . MET A 1 132 ? 2.076 -21.050 17.488 1.00 55.52 ? 132 MET A SD 1 ATOM 806 C CE . MET A 1 132 ? 2.803 -20.977 15.856 1.00 63.40 ? 132 MET A CE 1 ATOM 807 N N . GLY A 1 133 ? 1.078 -15.636 17.411 1.00 57.12 ? 133 GLY A N 1 ATOM 808 C CA . GLY A 1 133 ? 1.944 -14.482 17.257 1.00 56.20 ? 133 GLY A CA 1 ATOM 809 C C . GLY A 1 133 ? 1.204 -13.168 17.285 1.00 68.82 ? 133 GLY A C 1 ATOM 810 O O . GLY A 1 133 ? 1.792 -12.119 17.052 1.00 78.11 ? 133 GLY A O 1 ATOM 811 N N . ASN A 1 134 ? -0.091 -13.229 17.570 1.00 75.72 ? 134 ASN A N 1 ATOM 812 C CA . ASN A 1 134 ? -0.932 -12.041 17.591 1.00 74.36 ? 134 ASN A CA 1 ATOM 813 C C . ASN A 1 134 ? -1.451 -11.766 19.001 1.00 74.61 ? 134 ASN A C 1 ATOM 814 O O . ASN A 1 134 ? -1.894 -12.675 19.694 1.00 79.46 ? 134 ASN A O 1 ATOM 815 C CB . ASN A 1 134 ? -2.100 -12.162 16.591 1.00 73.05 ? 134 ASN A CB 1 ATOM 816 C CG . ASN A 1 134 ? -1.651 -12.093 15.126 1.00 66.44 ? 134 ASN A CG 1 ATOM 817 O OD1 . ASN A 1 134 ? -1.186 -13.080 14.565 1.00 50.85 ? 134 ASN A OD1 1 ATOM 818 N ND2 . ASN A 1 134 ? -1.824 -10.931 14.499 1.00 71.00 ? 134 ASN A ND2 1 ATOM 819 N N . PRO A 1 135 ? -1.395 -10.497 19.417 1.00 70.76 ? 135 PRO A N 1 ATOM 820 C CA . PRO A 1 135 ? -1.695 -9.958 20.744 1.00 58.54 ? 135 PRO A CA 1 ATOM 821 C C . PRO A 1 135 ? -3.155 -10.076 21.160 1.00 68.08 ? 135 PRO A C 1 ATOM 822 O O . PRO A 1 135 ? -3.648 -9.217 21.898 1.00 73.63 ? 135 PRO A O 1 ATOM 823 C CB . PRO A 1 135 ? -1.366 -8.476 20.590 1.00 64.59 ? 135 PRO A CB 1 ATOM 824 C CG . PRO A 1 135 ? -0.492 -8.394 19.397 1.00 77.03 ? 135 PRO A CG 1 ATOM 825 C CD . PRO A 1 135 ? -0.977 -9.439 18.489 1.00 78.86 ? 135 PRO A CD 1 ATOM 826 N N . TYR A 1 136 ? -3.854 -11.102 20.702 1.00 59.80 ? 136 TYR A N 1 ATOM 827 C CA . TYR A 1 136 ? -5.224 -11.268 21.154 1.00 65.78 ? 136 TYR A CA 1 ATOM 828 C C . TYR A 1 136 ? -5.259 -11.945 22.520 1.00 62.92 ? 136 TYR A C 1 ATOM 829 O O . TYR A 1 136 ? -4.410 -12.761 22.824 1.00 59.92 ? 136 TYR A O 1 ATOM 830 C CB . TYR A 1 136 ? -6.052 -12.038 20.123 1.00 68.00 ? 136 TYR A CB 1 ATOM 831 C CG . TYR A 1 136 ? -5.422 -13.303 19.616 1.00 61.05 ? 136 TYR A CG 1 ATOM 832 C CD1 . TYR A 1 136 ? -5.598 -14.499 20.278 1.00 62.79 ? 136 TYR A CD1 1 ATOM 833 C CD2 . TYR A 1 136 ? -4.667 -13.305 18.463 1.00 70.19 ? 136 TYR A CD2 1 ATOM 834 C CE1 . TYR A 1 136 ? -5.034 -15.653 19.808 1.00 68.07 ? 136 TYR A CE1 1 ATOM 835 C CE2 . TYR A 1 136 ? -4.102 -14.458 17.986 1.00 67.88 ? 136 TYR A CE2 1 ATOM 836 C CZ . TYR A 1 136 ? -4.286 -15.627 18.663 1.00 69.26 ? 136 TYR A CZ 1 ATOM 837 O OH . TYR A 1 136 ? -3.720 -16.785 18.192 1.00 78.02 ? 136 TYR A OH 1 ATOM 838 N N . GLN A 1 137 ? -6.242 -11.603 23.341 1.00 71.00 ? 137 GLN A N 1 ATOM 839 C CA . GLN A 1 137 ? -6.319 -12.141 24.700 1.00 77.93 ? 137 GLN A CA 1 ATOM 840 C C . GLN A 1 137 ? -7.041 -13.480 24.752 1.00 77.51 ? 137 GLN A C 1 ATOM 841 O O . GLN A 1 137 ? -6.759 -14.311 25.616 1.00 73.96 ? 137 GLN A O 1 ATOM 842 C CB . GLN A 1 137 ? -7.015 -11.138 25.621 1.00 83.23 ? 137 GLN A CB 1 ATOM 843 C CG . GLN A 1 137 ? -7.267 -11.627 27.038 1.00 80.70 ? 137 GLN A CG 1 ATOM 844 C CD . GLN A 1 137 ? -7.708 -10.499 27.959 1.00 77.45 ? 137 GLN A CD 1 ATOM 845 O OE1 . GLN A 1 137 ? -8.591 -9.707 27.607 1.00 68.99 ? 137 GLN A OE1 1 ATOM 846 N NE2 . GLN A 1 137 ? -7.087 -10.412 29.140 1.00 64.02 ? 137 GLN A NE2 1 ATOM 847 N N . THR A 1 138 ? -7.989 -13.662 23.835 1.00 78.53 ? 138 THR A N 1 ATOM 848 C CA . THR A 1 138 ? -8.736 -14.909 23.689 1.00 73.48 ? 138 THR A CA 1 ATOM 849 C C . THR A 1 138 ? -9.030 -15.083 22.210 1.00 74.25 ? 138 THR A C 1 ATOM 850 O O . THR A 1 138 ? -8.563 -14.294 21.389 1.00 75.16 ? 138 THR A O 1 ATOM 851 C CB . THR A 1 138 ? -10.073 -14.878 24.460 1.00 72.36 ? 138 THR A CB 1 ATOM 852 O OG1 . THR A 1 138 ? -10.979 -13.980 23.815 1.00 73.01 ? 138 THR A OG1 1 ATOM 853 C CG2 . THR A 1 138 ? -9.866 -14.424 25.916 1.00 74.91 ? 138 THR A CG2 1 ATOM 854 N N . LEU A 1 139 ? -9.802 -16.104 21.853 1.00 70.44 ? 139 LEU A N 1 ATOM 855 C CA . LEU A 1 139 ? -10.205 -16.257 20.455 1.00 53.75 ? 139 LEU A CA 1 ATOM 856 C C . LEU A 1 139 ? -11.538 -15.565 20.178 1.00 55.60 ? 139 LEU A C 1 ATOM 857 O O . LEU A 1 139 ? -12.252 -15.933 19.259 1.00 69.11 ? 139 LEU A O 1 ATOM 858 C CB . LEU A 1 139 ? -10.274 -17.733 20.044 1.00 45.85 ? 139 LEU A CB 1 ATOM 859 C CG . LEU A 1 139 ? -8.988 -18.572 20.019 1.00 57.40 ? 139 LEU A CG 1 ATOM 860 C CD1 . LEU A 1 139 ? -9.336 -20.035 19.843 1.00 63.53 ? 139 LEU A CD1 1 ATOM 861 C CD2 . LEU A 1 139 ? -7.957 -18.127 18.959 1.00 47.07 ? 139 LEU A CD2 1 ATOM 862 N N . GLY A 1 140 ? -11.880 -14.563 20.974 1.00 57.92 ? 140 GLY A N 1 ATOM 863 C CA . GLY A 1 140 ? -13.133 -13.858 20.770 1.00 78.51 ? 140 GLY A CA 1 ATOM 864 C C . GLY A 1 140 ? -14.377 -14.615 21.213 1.00 81.61 ? 140 GLY A C 1 ATOM 865 O O . GLY A 1 140 ? -14.325 -15.805 21.543 1.00 76.28 ? 140 GLY A O 1 ATOM 866 N N . VAL A 1 141 ? -15.508 -13.917 21.189 1.00 75.32 ? 141 VAL A N 1 ATOM 867 C CA . VAL A 1 141 ? -16.743 -14.421 21.776 1.00 69.85 ? 141 VAL A CA 1 ATOM 868 C C . VAL A 1 141 ? -17.618 -15.277 20.863 1.00 70.11 ? 141 VAL A C 1 ATOM 869 O O . VAL A 1 141 ? -18.701 -15.678 21.274 1.00 81.77 ? 141 VAL A O 1 ATOM 870 C CB . VAL A 1 141 ? -17.600 -13.268 22.282 1.00 68.00 ? 141 VAL A CB 1 ATOM 871 C CG1 . VAL A 1 141 ? -16.722 -12.254 22.984 1.00 81.13 ? 141 VAL A CG1 1 ATOM 872 C CG2 . VAL A 1 141 ? -18.296 -12.617 21.127 1.00 57.41 ? 141 VAL A CG2 1 ATOM 873 N N . THR A 1 142 ? -17.172 -15.546 19.635 1.00 60.91 ? 142 THR A N 1 ATOM 874 C CA . THR A 1 142 ? -17.894 -16.455 18.737 1.00 58.35 ? 142 THR A CA 1 ATOM 875 C C . THR A 1 142 ? -16.924 -17.486 18.182 1.00 59.35 ? 142 THR A C 1 ATOM 876 O O . THR A 1 142 ? -15.790 -17.141 17.829 1.00 64.18 ? 142 THR A O 1 ATOM 877 C CB . THR A 1 142 ? -18.544 -15.734 17.526 1.00 77.93 ? 142 THR A CB 1 ATOM 878 O OG1 . THR A 1 142 ? -18.900 -14.383 17.859 1.00 77.67 ? 142 THR A OG1 1 ATOM 879 C CG2 . THR A 1 142 ? -19.774 -16.497 17.073 1.00 76.49 ? 142 THR A CG2 1 ATOM 880 N N . SER A 1 143 ? -17.362 -18.743 18.099 1.00 51.60 ? 143 SER A N 1 ATOM 881 C CA . SER A 1 143 ? -16.487 -19.820 17.638 1.00 61.90 ? 143 SER A CA 1 ATOM 882 C C . SER A 1 143 ? -15.898 -19.441 16.286 1.00 72.69 ? 143 SER A C 1 ATOM 883 O O . SER A 1 143 ? -16.606 -18.973 15.401 1.00 87.86 ? 143 SER A O 1 ATOM 884 C CB . SER A 1 143 ? -17.233 -21.164 17.530 1.00 65.46 ? 143 SER A CB 1 ATOM 885 O OG . SER A 1 143 ? -18.146 -21.372 18.598 1.00 72.25 ? 143 SER A OG 1 ATOM 886 N N . LEU A 1 144 ? -14.602 -19.637 16.112 1.00 70.07 ? 144 LEU A N 1 ATOM 887 C CA . LEU A 1 144 ? -13.993 -19.276 14.847 1.00 59.86 ? 144 LEU A CA 1 ATOM 888 C C . LEU A 1 144 ? -14.038 -20.399 13.823 1.00 63.77 ? 144 LEU A C 1 ATOM 889 O O . LEU A 1 144 ? -14.118 -20.139 12.617 1.00 71.81 ? 144 LEU A O 1 ATOM 890 C CB . LEU A 1 144 ? -12.554 -18.844 15.063 1.00 50.05 ? 144 LEU A CB 1 ATOM 891 C CG . LEU A 1 144 ? -12.421 -17.648 15.993 1.00 53.40 ? 144 LEU A CG 1 ATOM 892 C CD1 . LEU A 1 144 ? -10.938 -17.258 16.183 1.00 47.96 ? 144 LEU A CD1 1 ATOM 893 C CD2 . LEU A 1 144 ? -13.249 -16.492 15.467 1.00 33.14 ? 144 LEU A CD2 1 ATOM 894 N N . PHE A 1 145 ? -14.005 -21.643 14.294 1.00 57.68 ? 145 PHE A N 1 ATOM 895 C CA . PHE A 1 145 ? -13.716 -22.762 13.399 1.00 49.94 ? 145 PHE A CA 1 ATOM 896 C C . PHE A 1 145 ? -14.835 -23.773 13.091 1.00 57.97 ? 145 PHE A C 1 ATOM 897 O O . PHE A 1 145 ? -14.550 -24.839 12.544 1.00 57.63 ? 145 PHE A O 1 ATOM 898 C CB . PHE A 1 145 ? -12.492 -23.521 13.915 1.00 38.96 ? 145 PHE A CB 1 ATOM 899 C CG . PHE A 1 145 ? -11.476 -22.653 14.578 1.00 52.41 ? 145 PHE A CG 1 ATOM 900 C CD1 . PHE A 1 145 ? -10.847 -21.644 13.883 1.00 55.24 ? 145 PHE A CD1 1 ATOM 901 C CD2 . PHE A 1 145 ? -11.140 -22.853 15.903 1.00 74.53 ? 145 PHE A CD2 1 ATOM 902 C CE1 . PHE A 1 145 ? -9.905 -20.846 14.494 1.00 68.56 ? 145 PHE A CE1 1 ATOM 903 C CE2 . PHE A 1 145 ? -10.197 -22.058 16.523 1.00 79.34 ? 145 PHE A CE2 1 ATOM 904 C CZ . PHE A 1 145 ? -9.578 -21.054 15.818 1.00 79.49 ? 145 PHE A CZ 1 ATOM 905 N N . PRO A 1 146 ? -16.103 -23.448 13.403 1.00 65.58 ? 146 PRO A N 1 ATOM 906 C CA . PRO A 1 146 ? -17.104 -24.520 13.350 1.00 63.32 ? 146 PRO A CA 1 ATOM 907 C C . PRO A 1 146 ? -17.358 -25.036 11.936 1.00 76.61 ? 146 PRO A C 1 ATOM 908 O O . PRO A 1 146 ? -17.699 -26.212 11.783 1.00 75.82 ? 146 PRO A O 1 ATOM 909 C CB . PRO A 1 146 ? -18.380 -23.854 13.894 1.00 53.03 ? 146 PRO A CB 1 ATOM 910 C CG . PRO A 1 146 ? -17.983 -22.496 14.359 1.00 61.75 ? 146 PRO A CG 1 ATOM 911 C CD . PRO A 1 146 ? -16.728 -22.136 13.632 1.00 72.27 ? 146 PRO A CD 1 ATOM 912 N N . ASN A 1 147 ? -17.201 -24.172 10.933 1.00 83.44 ? 147 ASN A N 1 ATOM 913 C CA . ASN A 1 147 ? -17.526 -24.528 9.561 1.00 94.49 ? 147 ASN A CA 1 ATOM 914 C C . ASN A 1 147 ? -16.263 -24.768 8.751 1.00 82.66 ? 147 ASN A C 1 ATOM 915 O O . ASN A 1 147 ? -16.106 -24.225 7.665 1.00 93.46 ? 147 ASN A O 1 ATOM 916 C CB . ASN A 1 147 ? -18.344 -23.422 8.881 1.00 113.35 ? 147 ASN A CB 1 ATOM 917 C CG . ASN A 1 147 ? -19.121 -22.563 9.862 1.00 126.54 ? 147 ASN A CG 1 ATOM 918 O OD1 . ASN A 1 147 ? -18.933 -21.346 9.916 1.00 120.19 ? 147 ASN A OD1 1 ATOM 919 N ND2 . ASN A 1 147 ? -19.996 -23.191 10.643 1.00 150.96 ? 147 ASN A ND2 1 ATOM 920 N N . LEU A 1 148 ? -15.353 -25.567 9.283 1.00 65.59 ? 148 LEU A N 1 ATOM 921 C CA . LEU A 1 148 ? -14.094 -25.818 8.600 1.00 62.87 ? 148 LEU A CA 1 ATOM 922 C C . LEU A 1 148 ? -13.835 -27.304 8.528 1.00 67.59 ? 148 LEU A C 1 ATOM 923 O O . LEU A 1 148 ? -12.787 -27.783 8.962 1.00 68.29 ? 148 LEU A O 1 ATOM 924 C CB . LEU A 1 148 ? -12.932 -25.118 9.303 1.00 55.82 ? 148 LEU A CB 1 ATOM 925 C CG . LEU A 1 148 ? -12.796 -23.629 9.009 1.00 54.24 ? 148 LEU A CG 1 ATOM 926 C CD1 . LEU A 1 148 ? -13.978 -22.865 9.574 1.00 69.63 ? 148 LEU A CD1 1 ATOM 927 C CD2 . LEU A 1 148 ? -11.501 -23.115 9.592 1.00 43.55 ? 148 LEU A CD2 1 ATOM 928 N N . THR A 1 149 ? -14.807 -28.016 7.972 1.00 69.34 ? 149 THR A N 1 ATOM 929 C CA . THR A 1 149 ? -14.790 -29.472 7.873 1.00 68.31 ? 149 THR A CA 1 ATOM 930 C C . THR A 1 149 ? -13.515 -30.049 7.288 1.00 62.55 ? 149 THR A C 1 ATOM 931 O O . THR A 1 149 ? -13.305 -31.257 7.351 1.00 60.02 ? 149 THR A O 1 ATOM 932 C CB . THR A 1 149 ? -15.934 -29.965 6.990 1.00 71.39 ? 149 THR A CB 1 ATOM 933 O OG1 . THR A 1 149 ? -15.846 -29.318 5.708 1.00 66.16 ? 149 THR A OG1 1 ATOM 934 C CG2 . THR A 1 149 ? -17.275 -29.665 7.653 1.00 71.29 ? 149 THR A CG2 1 ATOM 935 N N . ASN A 1 150 ? -12.675 -29.200 6.709 1.00 57.71 ? 150 ASN A N 1 ATOM 936 C CA . ASN A 1 150 ? -11.459 -29.685 6.073 1.00 66.28 ? 150 ASN A CA 1 ATOM 937 C C . ASN A 1 150 ? -10.159 -29.371 6.810 1.00 70.29 ? 150 ASN A C 1 ATOM 938 O O . ASN A 1 150 ? -9.069 -29.648 6.296 1.00 63.53 ? 150 ASN A O 1 ATOM 939 C CB . ASN A 1 150 ? -11.383 -29.179 4.636 1.00 80.78 ? 150 ASN A CB 1 ATOM 940 C CG . ASN A 1 150 ? -12.005 -30.137 3.663 1.00 80.54 ? 150 ASN A CG 1 ATOM 941 O OD1 . ASN A 1 150 ? -11.301 -30.924 3.032 1.00 87.62 ? 150 ASN A OD1 1 ATOM 942 N ND2 . ASN A 1 150 ? -13.333 -30.111 3.561 1.00 66.63 ? 150 ASN A ND2 1 ATOM 943 N N . LEU A 1 151 ? -10.284 -28.819 8.017 1.00 73.38 ? 151 LEU A N 1 ATOM 944 C CA . LEU A 1 151 ? -9.140 -28.354 8.793 1.00 60.11 ? 151 LEU A CA 1 ATOM 945 C C . LEU A 1 151 ? -8.327 -29.522 9.351 1.00 66.02 ? 151 LEU A C 1 ATOM 946 O O . LEU A 1 151 ? -8.889 -30.488 9.864 1.00 69.91 ? 151 LEU A O 1 ATOM 947 C CB . LEU A 1 151 ? -9.607 -27.422 9.913 1.00 53.47 ? 151 LEU A CB 1 ATOM 948 C CG . LEU A 1 151 ? -8.497 -26.564 10.527 1.00 64.93 ? 151 LEU A CG 1 ATOM 949 C CD1 . LEU A 1 151 ? -7.945 -25.577 9.491 1.00 73.40 ? 151 LEU A CD1 1 ATOM 950 C CD2 . LEU A 1 151 ? -8.962 -25.840 11.794 1.00 52.36 ? 151 LEU A CD2 1 ATOM 951 N N . GLN A 1 152 ? -7.003 -29.435 9.228 1.00 65.37 ? 152 GLN A N 1 ATOM 952 C CA . GLN A 1 152 ? -6.100 -30.496 9.679 1.00 60.44 ? 152 GLN A CA 1 ATOM 953 C C . GLN A 1 152 ? -5.033 -29.949 10.615 1.00 59.38 ? 152 GLN A C 1 ATOM 954 O O . GLN A 1 152 ? -4.421 -30.698 11.370 1.00 59.60 ? 152 GLN A O 1 ATOM 955 C CB . GLN A 1 152 ? -5.398 -31.168 8.497 1.00 58.95 ? 152 GLN A CB 1 ATOM 956 C CG . GLN A 1 152 ? -6.249 -32.126 7.695 1.00 72.67 ? 152 GLN A CG 1 ATOM 957 C CD . GLN A 1 152 ? -5.728 -32.302 6.271 1.00 88.09 ? 152 GLN A CD 1 ATOM 958 O OE1 . GLN A 1 152 ? -4.522 -32.202 6.023 1.00 80.29 ? 152 GLN A OE1 1 ATOM 959 N NE2 . GLN A 1 152 ? -6.639 -32.552 5.326 1.00 96.43 ? 152 GLN A NE2 1 ATOM 960 N N . THR A 1 153 ? -4.806 -28.641 10.564 1.00 49.54 ? 153 THR A N 1 ATOM 961 C CA . THR A 1 153 ? -3.744 -28.042 11.354 1.00 38.57 ? 153 THR A CA 1 ATOM 962 C C . THR A 1 153 ? -4.082 -26.659 11.876 1.00 41.52 ? 153 THR A C 1 ATOM 963 O O . THR A 1 153 ? -4.116 -25.710 11.115 1.00 52.21 ? 153 THR A O 1 ATOM 964 C CB . THR A 1 153 ? -2.437 -28.002 10.550 1.00 43.22 ? 153 THR A CB 1 ATOM 965 O OG1 . THR A 1 153 ? -1.940 -29.339 10.408 1.00 46.23 ? 153 THR A OG1 1 ATOM 966 C CG2 . THR A 1 153 ? -1.378 -27.118 11.234 1.00 28.66 ? 153 THR A CG2 1 ATOM 967 N N . LEU A 1 154 ? -4.320 -26.555 13.183 1.00 58.46 ? 154 LEU A N 1 ATOM 968 C CA . LEU A 1 154 ? -4.583 -25.273 13.853 1.00 57.47 ? 154 LEU A CA 1 ATOM 969 C C . LEU A 1 154 ? -3.426 -24.837 14.770 1.00 52.37 ? 154 LEU A C 1 ATOM 970 O O . LEU A 1 154 ? -2.902 -25.627 15.541 1.00 53.73 ? 154 LEU A O 1 ATOM 971 C CB . LEU A 1 154 ? -5.887 -25.357 14.654 1.00 53.59 ? 154 LEU A CB 1 ATOM 972 C CG . LEU A 1 154 ? -6.418 -24.054 15.245 1.00 54.10 ? 154 LEU A CG 1 ATOM 973 C CD1 . LEU A 1 154 ? -6.458 -22.966 14.191 1.00 60.79 ? 154 LEU A CD1 1 ATOM 974 C CD2 . LEU A 1 154 ? -7.792 -24.265 15.824 1.00 53.65 ? 154 LEU A CD2 1 ATOM 975 N N . ARG A 1 155 ? -3.019 -23.580 14.671 1.00 55.23 ? 155 ARG A N 1 ATOM 976 C CA . ARG A 1 155 ? -2.006 -23.033 15.573 1.00 52.79 ? 155 ARG A CA 1 ATOM 977 C C . ARG A 1 155 ? -2.484 -21.694 16.109 1.00 58.06 ? 155 ARG A C 1 ATOM 978 O O . ARG A 1 155 ? -2.553 -20.720 15.376 1.00 72.55 ? 155 ARG A O 1 ATOM 979 C CB . ARG A 1 155 ? -0.655 -22.846 14.869 1.00 46.58 ? 155 ARG A CB 1 ATOM 980 C CG . ARG A 1 155 ? -0.075 -24.099 14.227 1.00 44.66 ? 155 ARG A CG 1 ATOM 981 C CD . ARG A 1 155 ? 1.394 -23.905 13.827 1.00 45.06 ? 155 ARG A CD 1 ATOM 982 N NE . ARG A 1 155 ? 1.888 -24.972 12.956 1.00 48.70 ? 155 ARG A NE 1 ATOM 983 C CZ . ARG A 1 155 ? 1.964 -26.249 13.320 1.00 51.39 ? 155 ARG A CZ 1 ATOM 984 N NH1 . ARG A 1 155 ? 1.571 -26.618 14.522 1.00 62.78 ? 155 ARG A NH1 1 ATOM 985 N NH2 . ARG A 1 155 ? 2.412 -27.164 12.485 1.00 45.56 ? 155 ARG A NH2 1 ATOM 986 N N . ILE A 1 156 ? -2.819 -21.644 17.388 1.00 55.32 ? 156 ILE A N 1 ATOM 987 C CA . ILE A 1 156 ? -3.261 -20.403 17.992 1.00 56.99 ? 156 ILE A CA 1 ATOM 988 C C . ILE A 1 156 ? -2.417 -20.096 19.217 1.00 59.82 ? 156 ILE A C 1 ATOM 989 O O . ILE A 1 156 ? -1.557 -20.879 19.596 1.00 56.82 ? 156 ILE A O 1 ATOM 990 C CB . ILE A 1 156 ? -4.700 -20.517 18.459 1.00 54.78 ? 156 ILE A CB 1 ATOM 991 C CG1 . ILE A 1 156 ? -4.758 -21.408 19.704 1.00 50.69 ? 156 ILE A CG1 1 ATOM 992 C CG2 . ILE A 1 156 ? -5.567 -21.052 17.348 1.00 45.96 ? 156 ILE A CG2 1 ATOM 993 C CD1 . ILE A 1 156 ? -6.130 -21.572 20.262 1.00 56.16 ? 156 ILE A CD1 1 ATOM 994 N N . GLY A 1 157 ? -2.682 -18.955 19.841 1.00 66.08 ? 157 GLY A N 1 ATOM 995 C CA . GLY A 1 157 ? -2.015 -18.585 21.072 1.00 67.41 ? 157 GLY A CA 1 ATOM 996 C C . GLY A 1 157 ? -0.832 -17.662 20.881 1.00 69.13 ? 157 GLY A C 1 ATOM 997 O O . GLY A 1 157 ? -0.432 -17.365 19.755 1.00 68.63 ? 157 GLY A O 1 ATOM 998 N N . ASN A 1 158 ? -0.280 -17.205 22.001 1.00 73.65 ? 158 ASN A N 1 ATOM 999 C CA . ASN A 1 158 ? 0.900 -16.348 22.008 1.00 78.89 ? 158 ASN A CA 1 ATOM 1000 C C . ASN A 1 158 ? 1.623 -16.404 23.340 1.00 77.34 ? 158 ASN A C 1 ATOM 1001 O O . ASN A 1 158 ? 1.123 -16.976 24.315 1.00 83.93 ? 158 ASN A O 1 ATOM 1002 C CB . ASN A 1 158 ? 0.527 -14.897 21.698 1.00 84.03 ? 158 ASN A CB 1 ATOM 1003 C CG . ASN A 1 158 ? -0.390 -14.290 22.745 1.00 84.15 ? 158 ASN A CG 1 ATOM 1004 O OD1 . ASN A 1 158 ? -0.311 -14.610 23.932 1.00 83.35 ? 158 ASN A OD1 1 ATOM 1005 N ND2 . ASN A 1 158 ? -1.264 -13.403 22.306 1.00 87.43 ? 158 ASN A ND2 1 ATOM 1006 N N . VAL A 1 159 ? 2.784 -15.768 23.387 1.00 69.06 ? 159 VAL A N 1 ATOM 1007 C CA . VAL A 1 159 ? 3.615 -15.805 24.578 1.00 62.15 ? 159 VAL A CA 1 ATOM 1008 C C . VAL A 1 159 ? 3.108 -14.951 25.749 1.00 74.33 ? 159 VAL A C 1 ATOM 1009 O O . VAL A 1 159 ? 3.101 -15.408 26.891 1.00 77.87 ? 159 VAL A O 1 ATOM 1010 C CB . VAL A 1 159 ? 5.054 -15.393 24.253 1.00 49.36 ? 159 VAL A CB 1 ATOM 1011 C CG1 . VAL A 1 159 ? 5.764 -14.981 25.502 1.00 47.75 ? 159 VAL A CG1 1 ATOM 1012 C CG2 . VAL A 1 159 ? 5.794 -16.520 23.567 1.00 38.40 ? 159 VAL A CG2 1 ATOM 1013 N N . GLU A 1 160 ? 2.671 -13.726 25.473 1.00 80.61 ? 160 GLU A N 1 ATOM 1014 C CA . GLU A 1 160 ? 2.460 -12.751 26.546 1.00 76.73 ? 160 GLU A CA 1 ATOM 1015 C C . GLU A 1 160 ? 1.030 -12.286 26.821 1.00 74.25 ? 160 GLU A C 1 ATOM 1016 O O . GLU A 1 160 ? 0.819 -11.536 27.762 1.00 85.24 ? 160 GLU A O 1 ATOM 1017 C CB . GLU A 1 160 ? 3.329 -11.524 26.287 1.00 83.08 ? 160 GLU A CB 1 ATOM 1018 C CG . GLU A 1 160 ? 4.692 -11.884 25.739 1.00 90.83 ? 160 GLU A CG 1 ATOM 1019 C CD . GLU A 1 160 ? 5.380 -10.726 25.048 1.00 95.38 ? 160 GLU A CD 1 ATOM 1020 O OE1 . GLU A 1 160 ? 6.589 -10.869 24.731 1.00 90.03 ? 160 GLU A OE1 1 ATOM 1021 O OE2 . GLU A 1 160 ? 4.713 -9.684 24.824 1.00 89.87 ? 160 GLU A OE2 1 ATOM 1022 N N . THR A 1 161 ? 0.050 -12.701 26.022 1.00 73.97 ? 161 THR A N 1 ATOM 1023 C CA . THR A 1 161 ? -1.309 -12.170 26.206 1.00 75.53 ? 161 THR A CA 1 ATOM 1024 C C . THR A 1 161 ? -2.463 -13.165 26.086 1.00 71.75 ? 161 THR A C 1 ATOM 1025 O O . THR A 1 161 ? -3.548 -12.921 26.611 1.00 69.54 ? 161 THR A O 1 ATOM 1026 C CB . THR A 1 161 ? -1.588 -10.941 25.306 1.00 68.42 ? 161 THR A CB 1 ATOM 1027 O OG1 . THR A 1 161 ? -0.828 -11.052 24.098 1.00 71.70 ? 161 THR A OG1 1 ATOM 1028 C CG2 . THR A 1 161 ? -1.189 -9.652 26.032 1.00 64.69 ? 161 THR A CG2 1 ATOM 1029 N N . PHE A 1 162 ? -2.244 -14.284 25.407 1.00 65.43 ? 162 PHE A N 1 ATOM 1030 C CA . PHE A 1 162 ? -3.301 -15.281 25.315 1.00 65.34 ? 162 PHE A CA 1 ATOM 1031 C C . PHE A 1 162 ? -3.537 -15.852 26.700 1.00 67.73 ? 162 PHE A C 1 ATOM 1032 O O . PHE A 1 162 ? -2.679 -16.558 27.240 1.00 75.31 ? 162 PHE A O 1 ATOM 1033 C CB . PHE A 1 162 ? -2.958 -16.382 24.303 1.00 61.67 ? 162 PHE A CB 1 ATOM 1034 C CG . PHE A 1 162 ? -4.091 -17.336 24.046 1.00 53.16 ? 162 PHE A CG 1 ATOM 1035 C CD1 . PHE A 1 162 ? -5.282 -16.886 23.477 1.00 63.03 ? 162 PHE A CD1 1 ATOM 1036 C CD2 . PHE A 1 162 ? -3.976 -18.674 24.377 1.00 39.28 ? 162 PHE A CD2 1 ATOM 1037 C CE1 . PHE A 1 162 ? -6.337 -17.761 23.237 1.00 61.61 ? 162 PHE A CE1 1 ATOM 1038 C CE2 . PHE A 1 162 ? -5.031 -19.555 24.147 1.00 50.95 ? 162 PHE A CE2 1 ATOM 1039 C CZ . PHE A 1 162 ? -6.207 -19.099 23.570 1.00 57.05 ? 162 PHE A CZ 1 ATOM 1040 N N . SER A 1 163 ? -4.698 -15.541 27.268 1.00 69.66 ? 163 SER A N 1 ATOM 1041 C CA . SER A 1 163 ? -4.941 -15.764 28.694 1.00 81.10 ? 163 SER A CA 1 ATOM 1042 C C . SER A 1 163 ? -6.146 -16.652 29.044 1.00 87.41 ? 163 SER A C 1 ATOM 1043 O O . SER A 1 163 ? -6.184 -17.242 30.129 1.00 81.98 ? 163 SER A O 1 ATOM 1044 C CB . SER A 1 163 ? -5.051 -14.421 29.425 1.00 79.51 ? 163 SER A CB 1 ATOM 1045 O OG . SER A 1 163 ? -6.236 -13.734 29.062 1.00 83.13 ? 163 SER A OG 1 ATOM 1046 N N . GLU A 1 164 ? -7.124 -16.748 28.145 1.00 81.41 ? 164 GLU A N 1 ATOM 1047 C CA . GLU A 1 164 ? -8.275 -17.616 28.395 1.00 80.65 ? 164 GLU A CA 1 ATOM 1048 C C . GLU A 1 164 ? -8.448 -18.707 27.349 1.00 84.69 ? 164 GLU A C 1 ATOM 1049 O O . GLU A 1 164 ? -8.020 -18.560 26.206 1.00 88.77 ? 164 GLU A O 1 ATOM 1050 C CB . GLU A 1 164 ? -9.564 -16.808 28.523 1.00 81.89 ? 164 GLU A CB 1 ATOM 1051 C CG . GLU A 1 164 ? -9.729 -16.172 29.879 1.00 103.99 ? 164 GLU A CG 1 ATOM 1052 C CD . GLU A 1 164 ? -11.176 -16.113 30.311 1.00 123.29 ? 164 GLU A CD 1 ATOM 1053 O OE1 . GLU A 1 164 ? -12.060 -16.244 29.436 1.00 120.80 ? 164 GLU A OE1 1 ATOM 1054 O OE2 . GLU A 1 164 ? -11.426 -15.944 31.526 1.00 134.57 ? 164 GLU A OE2 1 ATOM 1055 N N . ILE A 1 165 ? -9.062 -19.812 27.758 1.00 79.34 ? 165 ILE A N 1 ATOM 1056 C CA . ILE A 1 165 ? -9.428 -20.881 26.839 1.00 80.07 ? 165 ILE A CA 1 ATOM 1057 C C . ILE A 1 165 ? -10.834 -21.326 27.211 1.00 78.24 ? 165 ILE A C 1 ATOM 1058 O O . ILE A 1 165 ? -11.036 -21.922 28.268 1.00 66.66 ? 165 ILE A O 1 ATOM 1059 C CB . ILE A 1 165 ? -8.466 -22.100 26.918 1.00 71.60 ? 165 ILE A CB 1 ATOM 1060 C CG1 . ILE A 1 165 ? -7.094 -21.773 26.309 1.00 81.06 ? 165 ILE A CG1 1 ATOM 1061 C CG2 . ILE A 1 165 ? -9.075 -23.316 26.219 1.00 60.39 ? 165 ILE A CG2 1 ATOM 1062 C CD1 . ILE A 1 165 ? -6.054 -22.920 26.422 1.00 58.09 ? 165 ILE A CD1 1 ATOM 1063 N N . ARG A 1 166 ? -11.808 -21.026 26.355 1.00 70.54 ? 166 ARG A N 1 ATOM 1064 C CA . ARG A 1 166 ? -13.192 -21.336 26.677 1.00 64.80 ? 166 ARG A CA 1 ATOM 1065 C C . ARG A 1 166 ? -13.716 -22.538 25.915 1.00 69.40 ? 166 ARG A C 1 ATOM 1066 O O . ARG A 1 166 ? -13.094 -23.000 24.961 1.00 63.90 ? 166 ARG A O 1 ATOM 1067 C CB . ARG A 1 166 ? -14.083 -20.122 26.449 1.00 70.32 ? 166 ARG A CB 1 ATOM 1068 C CG . ARG A 1 166 ? -13.778 -18.979 27.384 1.00 85.36 ? 166 ARG A CG 1 ATOM 1069 C CD . ARG A 1 166 ? -12.717 -18.063 26.808 1.00 102.73 ? 166 ARG A CD 1 ATOM 1070 N NE . ARG A 1 166 ? -13.282 -16.810 26.307 1.00 113.72 ? 166 ARG A NE 1 ATOM 1071 C CZ . ARG A 1 166 ? -13.362 -16.475 25.024 1.00 114.76 ? 166 ARG A CZ 1 ATOM 1072 N NH1 . ARG A 1 166 ? -12.910 -17.302 24.085 1.00 105.25 ? 166 ARG A NH1 1 ATOM 1073 N NH2 . ARG A 1 166 ? -13.891 -15.305 24.686 1.00 119.45 ? 166 ARG A NH2 1 ATOM 1074 N N . ARG A 1 167 ? -14.868 -23.041 26.342 1.00 78.79 ? 167 ARG A N 1 ATOM 1075 C CA . ARG A 1 167 ? -15.427 -24.255 25.761 1.00 81.59 ? 167 ARG A CA 1 ATOM 1076 C C . ARG A 1 167 ? -15.923 -24.046 24.316 1.00 78.80 ? 167 ARG A C 1 ATOM 1077 O O . ARG A 1 167 ? -16.015 -25.001 23.540 1.00 77.66 ? 167 ARG A O 1 ATOM 1078 C CB . ARG A 1 167 ? -16.540 -24.793 26.664 1.00 82.22 ? 167 ARG A CB 1 ATOM 1079 C CG . ARG A 1 167 ? -16.639 -26.311 26.735 1.00 88.90 ? 167 ARG A CG 1 ATOM 1080 C CD . ARG A 1 167 ? -17.876 -26.739 27.529 1.00 103.12 ? 167 ARG A CD 1 ATOM 1081 N NE . ARG A 1 167 ? -18.151 -25.847 28.659 1.00 112.97 ? 167 ARG A NE 1 ATOM 1082 C CZ . ARG A 1 167 ? -17.964 -26.163 29.938 1.00 119.85 ? 167 ARG A CZ 1 ATOM 1083 N NH1 . ARG A 1 167 ? -17.505 -27.363 30.268 1.00 123.37 ? 167 ARG A NH1 1 ATOM 1084 N NH2 . ARG A 1 167 ? -18.243 -25.282 30.891 1.00 120.27 ? 167 ARG A NH2 1 ATOM 1085 N N . ILE A 1 168 ? -16.234 -22.801 23.956 1.00 73.86 ? 168 ILE A N 1 ATOM 1086 C CA . ILE A 1 168 ? -16.662 -22.495 22.594 1.00 80.61 ? 168 ILE A CA 1 ATOM 1087 C C . ILE A 1 168 ? -15.498 -22.584 21.614 1.00 91.02 ? 168 ILE A C 1 ATOM 1088 O O . ILE A 1 168 ? -15.669 -22.990 20.464 1.00 101.14 ? 168 ILE A O 1 ATOM 1089 C CB . ILE A 1 168 ? -17.263 -21.065 22.450 1.00 71.97 ? 168 ILE A CB 1 ATOM 1090 C CG1 . ILE A 1 168 ? -16.284 -20.004 22.953 1.00 67.76 ? 168 ILE A CG1 1 ATOM 1091 C CG2 . ILE A 1 168 ? -18.614 -20.944 23.128 1.00 39.20 ? 168 ILE A CG2 1 ATOM 1092 C CD1 . ILE A 1 168 ? -16.689 -18.594 22.571 1.00 61.96 ? 168 ILE A CD1 1 ATOM 1093 N N . ASP A 1 169 ? -14.314 -22.199 22.078 1.00 86.60 ? 169 ASP A N 1 ATOM 1094 C CA . ASP A 1 169 ? -13.166 -21.976 21.199 1.00 83.88 ? 169 ASP A CA 1 ATOM 1095 C C . ASP A 1 169 ? -12.900 -23.065 20.140 1.00 78.84 ? 169 ASP A C 1 ATOM 1096 O O . ASP A 1 169 ? -12.470 -22.741 19.034 1.00 88.80 ? 169 ASP A O 1 ATOM 1097 C CB . ASP A 1 169 ? -11.903 -21.635 22.016 1.00 89.50 ? 169 ASP A CB 1 ATOM 1098 C CG . ASP A 1 169 ? -12.045 -20.319 22.813 1.00 91.01 ? 169 ASP A CG 1 ATOM 1099 O OD1 . ASP A 1 169 ? -12.897 -19.479 22.441 1.00 97.27 ? 169 ASP A OD1 1 ATOM 1100 O OD2 . ASP A 1 169 ? -11.304 -20.123 23.808 1.00 74.11 ? 169 ASP A OD2 1 ATOM 1101 N N . PHE A 1 170 ? -13.182 -24.332 20.450 1.00 70.86 ? 170 PHE A N 1 ATOM 1102 C CA . PHE A 1 170 ? -12.933 -25.431 19.497 1.00 60.92 ? 170 PHE A CA 1 ATOM 1103 C C . PHE A 1 170 ? -14.180 -26.230 19.108 1.00 60.64 ? 170 PHE A C 1 ATOM 1104 O O . PHE A 1 170 ? -14.112 -27.441 18.852 1.00 57.67 ? 170 PHE A O 1 ATOM 1105 C CB . PHE A 1 170 ? -11.843 -26.368 20.020 1.00 56.59 ? 170 PHE A CB 1 ATOM 1106 C CG . PHE A 1 170 ? -10.593 -25.655 20.416 1.00 70.30 ? 170 PHE A CG 1 ATOM 1107 C CD1 . PHE A 1 170 ? -9.685 -25.247 19.466 1.00 79.22 ? 170 PHE A CD1 1 ATOM 1108 C CD2 . PHE A 1 170 ? -10.340 -25.358 21.737 1.00 74.58 ? 170 PHE A CD2 1 ATOM 1109 C CE1 . PHE A 1 170 ? -8.541 -24.572 19.832 1.00 78.01 ? 170 PHE A CE1 1 ATOM 1110 C CE2 . PHE A 1 170 ? -9.196 -24.688 22.102 1.00 70.22 ? 170 PHE A CE2 1 ATOM 1111 C CZ . PHE A 1 170 ? -8.302 -24.295 21.152 1.00 71.46 ? 170 PHE A CZ 1 ATOM 1112 N N . ALA A 1 171 ? -15.316 -25.543 19.053 1.00 60.48 ? 171 ALA A N 1 ATOM 1113 C CA . ALA A 1 171 ? -16.572 -26.181 18.698 1.00 64.41 ? 171 ALA A CA 1 ATOM 1114 C C . ALA A 1 171 ? -16.612 -26.407 17.204 1.00 80.51 ? 171 ALA A C 1 ATOM 1115 O O . ALA A 1 171 ? -16.175 -25.552 16.433 1.00 90.97 ? 171 ALA A O 1 ATOM 1116 C CB . ALA A 1 171 ? -17.739 -25.326 19.128 1.00 64.76 ? 171 ALA A CB 1 ATOM 1117 N N . GLY A 1 172 ? -17.132 -27.559 16.798 1.00 81.35 ? 172 GLY A N 1 ATOM 1118 C CA . GLY A 1 172 ? -17.240 -27.876 15.388 1.00 92.37 ? 172 GLY A CA 1 ATOM 1119 C C . GLY A 1 172 ? -16.000 -28.554 14.838 1.00 98.27 ? 172 GLY A C 1 ATOM 1120 O O . GLY A 1 172 ? -15.979 -28.958 13.674 1.00 107.36 ? 172 GLY A O 1 ATOM 1121 N N . LEU A 1 173 ? -14.964 -28.667 15.669 1.00 86.85 ? 173 LEU A N 1 ATOM 1122 C CA . LEU A 1 173 ? -13.765 -29.420 15.317 1.00 78.22 ? 173 LEU A CA 1 ATOM 1123 C C . LEU A 1 173 ? -13.886 -30.832 15.865 1.00 77.74 ? 173 LEU A C 1 ATOM 1124 O O . LEU A 1 173 ? -14.108 -31.015 17.060 1.00 90.19 ? 173 LEU A O 1 ATOM 1125 C CB . LEU A 1 173 ? -12.520 -28.760 15.901 1.00 78.16 ? 173 LEU A CB 1 ATOM 1126 C CG . LEU A 1 173 ? -12.172 -27.340 15.466 1.00 81.12 ? 173 LEU A CG 1 ATOM 1127 C CD1 . LEU A 1 173 ? -10.985 -26.839 16.263 1.00 82.02 ? 173 LEU A CD1 1 ATOM 1128 C CD2 . LEU A 1 173 ? -11.871 -27.290 13.982 1.00 81.70 ? 173 LEU A CD2 1 ATOM 1129 N N . THR A 1 174 ? -13.749 -31.828 14.998 1.00 72.47 ? 174 THR A N 1 ATOM 1130 C CA . THR A 1 174 ? -13.868 -33.218 15.430 1.00 77.14 ? 174 THR A CA 1 ATOM 1131 C C . THR A 1 174 ? -12.529 -33.953 15.336 1.00 78.52 ? 174 THR A C 1 ATOM 1132 O O . THR A 1 174 ? -12.227 -34.804 16.161 1.00 83.41 ? 174 THR A O 1 ATOM 1133 C CB . THR A 1 174 ? -15.010 -34.003 14.683 1.00 79.13 ? 174 THR A CB 1 ATOM 1134 O OG1 . THR A 1 174 ? -14.661 -34.231 13.312 1.00 76.63 ? 174 THR A OG1 1 ATOM 1135 C CG2 . THR A 1 174 ? -16.332 -33.250 14.751 1.00 75.44 ? 174 THR A CG2 1 ATOM 1136 N N . SER A 1 175 ? -11.722 -33.607 14.343 1.00 78.06 ? 175 SER A N 1 ATOM 1137 C CA . SER A 1 175 ? -10.424 -34.241 14.167 1.00 71.31 ? 175 SER A CA 1 ATOM 1138 C C . SER A 1 175 ? -9.399 -33.193 13.726 1.00 62.90 ? 175 SER A C 1 ATOM 1139 O O . SER A 1 175 ? -9.758 -32.220 13.073 1.00 71.39 ? 175 SER A O 1 ATOM 1140 C CB . SER A 1 175 ? -10.537 -35.379 13.146 1.00 71.00 ? 175 SER A CB 1 ATOM 1141 O OG . SER A 1 175 ? -9.276 -35.960 12.853 1.00 78.33 ? 175 SER A OG 1 ATOM 1142 N N . LEU A 1 176 ? -8.137 -33.380 14.107 1.00 47.41 ? 176 LEU A N 1 ATOM 1143 C CA . LEU A 1 176 ? -7.043 -32.504 13.686 1.00 47.63 ? 176 LEU A CA 1 ATOM 1144 C C . LEU A 1 176 ? -5.756 -33.299 13.692 1.00 55.69 ? 176 LEU A C 1 ATOM 1145 O O . LEU A 1 176 ? -5.587 -34.185 14.521 1.00 60.80 ? 176 LEU A O 1 ATOM 1146 C CB . LEU A 1 176 ? -6.897 -31.291 14.609 1.00 46.88 ? 176 LEU A CB 1 ATOM 1147 C CG . LEU A 1 176 ? -7.869 -30.125 14.394 1.00 55.86 ? 176 LEU A CG 1 ATOM 1148 C CD1 . LEU A 1 176 ? -7.787 -29.137 15.525 1.00 62.77 ? 176 LEU A CD1 1 ATOM 1149 C CD2 . LEU A 1 176 ? -7.618 -29.428 13.074 1.00 52.44 ? 176 LEU A CD2 1 ATOM 1150 N N . ASN A 1 177 ? -4.860 -32.998 12.757 1.00 52.95 ? 177 ASN A N 1 ATOM 1151 C CA . ASN A 1 177 ? -3.577 -33.679 12.676 1.00 48.92 ? 177 ASN A CA 1 ATOM 1152 C C . ASN A 1 177 ? -2.645 -33.049 13.673 1.00 55.36 ? 177 ASN A C 1 ATOM 1153 O O . ASN A 1 177 ? -1.975 -33.728 14.444 1.00 72.15 ? 177 ASN A O 1 ATOM 1154 C CB . ASN A 1 177 ? -2.948 -33.516 11.293 1.00 69.32 ? 177 ASN A CB 1 ATOM 1155 C CG . ASN A 1 177 ? -3.704 -34.249 10.203 1.00 74.85 ? 177 ASN A CG 1 ATOM 1156 O OD1 . ASN A 1 177 ? -3.215 -34.354 9.069 1.00 64.35 ? 177 ASN A OD1 1 ATOM 1157 N ND2 . ASN A 1 177 ? -4.900 -34.758 10.530 1.00 66.38 ? 177 ASN A ND2 1 ATOM 1158 N N . GLU A 1 178 ? -2.607 -31.726 13.636 1.00 48.90 ? 178 GLU A N 1 ATOM 1159 C CA . GLU A 1 178 ? -1.740 -30.949 14.489 1.00 45.72 ? 178 GLU A CA 1 ATOM 1160 C C . GLU A 1 178 ? -2.553 -29.831 15.104 1.00 51.00 ? 178 GLU A C 1 ATOM 1161 O O . GLU A 1 178 ? -3.134 -29.034 14.393 1.00 54.15 ? 178 GLU A O 1 ATOM 1162 C CB . GLU A 1 178 ? -0.594 -30.357 13.682 1.00 58.75 ? 178 GLU A CB 1 ATOM 1163 C CG . GLU A 1 178 ? 0.481 -31.341 13.276 1.00 81.12 ? 178 GLU A CG 1 ATOM 1164 C CD . GLU A 1 178 ? 1.860 -30.695 13.266 1.00 108.20 ? 178 GLU A CD 1 ATOM 1165 O OE1 . GLU A 1 178 ? 2.520 -30.719 12.202 1.00 112.11 ? 178 GLU A OE1 1 ATOM 1166 O OE2 . GLU A 1 178 ? 2.274 -30.150 14.322 1.00 113.38 ? 178 GLU A OE2 1 ATOM 1167 N N . LEU A 1 179 ? -2.628 -29.802 16.430 1.00 57.56 ? 179 LEU A N 1 ATOM 1168 C CA . LEU A 1 179 ? -3.184 -28.665 17.150 1.00 43.31 ? 179 LEU A CA 1 ATOM 1169 C C . LEU A 1 179 ? -2.026 -28.118 17.950 1.00 43.06 ? 179 LEU A C 1 ATOM 1170 O O . LEU A 1 179 ? -1.262 -28.887 18.526 1.00 47.80 ? 179 LEU A O 1 ATOM 1171 C CB . LEU A 1 179 ? -4.323 -29.097 18.068 1.00 42.30 ? 179 LEU A CB 1 ATOM 1172 C CG . LEU A 1 179 ? -4.961 -27.996 18.912 1.00 47.46 ? 179 LEU A CG 1 ATOM 1173 C CD1 . LEU A 1 179 ? -5.242 -26.772 18.083 1.00 40.16 ? 179 LEU A CD1 1 ATOM 1174 C CD2 . LEU A 1 179 ? -6.235 -28.498 19.565 1.00 56.76 ? 179 LEU A CD2 1 ATOM 1175 N N . GLU A 1 180 ? -1.851 -26.803 17.939 1.00 47.64 ? 180 GLU A N 1 ATOM 1176 C CA . GLU A 1 180 ? -0.773 -26.186 18.708 1.00 56.12 ? 180 GLU A CA 1 ATOM 1177 C C . GLU A 1 180 ? -1.262 -24.958 19.486 1.00 68.24 ? 180 GLU A C 1 ATOM 1178 O O . GLU A 1 180 ? -1.364 -23.861 18.944 1.00 77.47 ? 180 GLU A O 1 ATOM 1179 C CB . GLU A 1 180 ? 0.432 -25.830 17.826 1.00 36.92 ? 180 GLU A CB 1 ATOM 1180 C CG . GLU A 1 180 ? 1.527 -25.110 18.608 1.00 56.48 ? 180 GLU A CG 1 ATOM 1181 C CD . GLU A 1 180 ? 2.737 -24.749 17.770 1.00 63.94 ? 180 GLU A CD 1 ATOM 1182 O OE1 . GLU A 1 180 ? 2.734 -25.062 16.564 1.00 70.30 ? 180 GLU A OE1 1 ATOM 1183 O OE2 . GLU A 1 180 ? 3.695 -24.152 18.318 1.00 53.83 ? 180 GLU A OE2 1 ATOM 1184 N N . ILE A 1 181 ? -1.571 -25.161 20.762 1.00 58.96 ? 181 ILE A N 1 ATOM 1185 C CA . ILE A 1 181 ? -1.991 -24.074 21.632 1.00 50.62 ? 181 ILE A CA 1 ATOM 1186 C C . ILE A 1 181 ? -0.792 -23.464 22.359 1.00 53.08 ? 181 ILE A C 1 ATOM 1187 O O . ILE A 1 181 ? -0.159 -24.113 23.200 1.00 52.11 ? 181 ILE A O 1 ATOM 1188 C CB . ILE A 1 181 ? -3.039 -24.564 22.650 1.00 42.04 ? 181 ILE A CB 1 ATOM 1189 C CG1 . ILE A 1 181 ? -4.299 -25.020 21.908 1.00 39.60 ? 181 ILE A CG1 1 ATOM 1190 C CG2 . ILE A 1 181 ? -3.344 -23.468 23.670 1.00 34.21 ? 181 ILE A CG2 1 ATOM 1191 C CD1 . ILE A 1 181 ? -5.177 -25.941 22.686 1.00 38.70 ? 181 ILE A CD1 1 ATOM 1192 N N . LYS A 1 182 ? -0.458 -22.224 22.018 1.00 56.85 ? 182 LYS A N 1 ATOM 1193 C CA . LYS A 1 182 ? 0.600 -21.512 22.733 1.00 66.31 ? 182 LYS A CA 1 ATOM 1194 C C . LYS A 1 182 ? 0.020 -20.596 23.815 1.00 76.07 ? 182 LYS A C 1 ATOM 1195 O O . LYS A 1 182 ? -0.298 -19.438 23.555 1.00 79.52 ? 182 LYS A O 1 ATOM 1196 C CB . LYS A 1 182 ? 1.491 -20.728 21.772 1.00 58.31 ? 182 LYS A CB 1 ATOM 1197 C CG . LYS A 1 182 ? 2.387 -19.732 22.473 1.00 62.80 ? 182 LYS A CG 1 ATOM 1198 C CD . LYS A 1 182 ? 3.831 -19.852 22.021 1.00 68.12 ? 182 LYS A CD 1 ATOM 1199 C CE . LYS A 1 182 ? 4.029 -19.510 20.556 1.00 65.36 ? 182 LYS A CE 1 ATOM 1200 N NZ . LYS A 1 182 ? 5.480 -19.456 20.224 1.00 55.17 ? 182 LYS A NZ 1 ATOM 1201 N N . ALA A 1 183 ? -0.109 -21.124 25.031 1.00 71.91 ? 183 ALA A N 1 ATOM 1202 C CA . ALA A 1 183 ? -0.819 -20.423 26.088 1.00 71.60 ? 183 ALA A CA 1 ATOM 1203 C C . ALA A 1 183 ? 0.023 -20.210 27.353 1.00 76.08 ? 183 ALA A C 1 ATOM 1204 O O . ALA A 1 183 ? -0.436 -20.474 28.468 1.00 85.90 ? 183 ALA A O 1 ATOM 1205 C CB . ALA A 1 183 ? -2.120 -21.157 26.410 1.00 61.01 ? 183 ALA A CB 1 ATOM 1206 N N . LEU A 1 184 ? 1.245 -19.715 27.180 1.00 60.67 ? 184 LEU A N 1 ATOM 1207 C CA . LEU A 1 184 ? 2.143 -19.488 28.312 1.00 61.05 ? 184 LEU A CA 1 ATOM 1208 C C . LEU A 1 184 ? 1.512 -18.657 29.423 1.00 70.02 ? 184 LEU A C 1 ATOM 1209 O O . LEU A 1 184 ? 1.800 -18.864 30.595 1.00 84.06 ? 184 LEU A O 1 ATOM 1210 C CB . LEU A 1 184 ? 3.445 -18.835 27.849 1.00 56.29 ? 184 LEU A CB 1 ATOM 1211 C CG . LEU A 1 184 ? 4.214 -19.703 26.844 1.00 62.36 ? 184 LEU A CG 1 ATOM 1212 C CD1 . LEU A 1 184 ? 5.046 -18.855 25.898 1.00 58.00 ? 184 LEU A CD1 1 ATOM 1213 C CD2 . LEU A 1 184 ? 5.073 -20.771 27.538 1.00 50.16 ? 184 LEU A CD2 1 ATOM 1214 N N . SER A 1 185 ? 0.645 -17.723 29.057 1.00 68.15 ? 185 SER A N 1 ATOM 1215 C CA . SER A 1 185 ? 0.078 -16.804 30.030 1.00 55.52 ? 185 SER A CA 1 ATOM 1216 C C . SER A 1 185 ? -1.335 -17.193 30.395 1.00 56.91 ? 185 SER A C 1 ATOM 1217 O O . SER A 1 185 ? -2.102 -16.358 30.845 1.00 65.98 ? 185 SER A O 1 ATOM 1218 C CB . SER A 1 185 ? 0.080 -15.375 29.484 1.00 60.39 ? 185 SER A CB 1 ATOM 1219 O OG . SER A 1 185 ? 1.382 -14.964 29.108 1.00 63.62 ? 185 SER A OG 1 ATOM 1220 N N . LEU A 1 186 ? -1.676 -18.459 30.197 1.00 64.07 ? 186 LEU A N 1 ATOM 1221 C CA . LEU A 1 186 ? -3.018 -18.959 30.490 1.00 71.53 ? 186 LEU A CA 1 ATOM 1222 C C . LEU A 1 186 ? -3.457 -18.639 31.918 1.00 93.76 ? 186 LEU A C 1 ATOM 1223 O O . LEU A 1 186 ? -3.062 -19.328 32.863 1.00 102.28 ? 186 LEU A O 1 ATOM 1224 C CB . LEU A 1 186 ? -3.072 -20.469 30.253 1.00 69.62 ? 186 LEU A CB 1 ATOM 1225 C CG . LEU A 1 186 ? -4.400 -21.166 30.555 1.00 73.37 ? 186 LEU A CG 1 ATOM 1226 C CD1 . LEU A 1 186 ? -5.547 -20.377 29.971 1.00 69.14 ? 186 LEU A CD1 1 ATOM 1227 C CD2 . LEU A 1 186 ? -4.405 -22.596 30.024 1.00 74.77 ? 186 LEU A CD2 1 ATOM 1228 N N . ARG A 1 187 ? -4.274 -17.598 32.076 1.00 100.87 ? 187 ARG A N 1 ATOM 1229 C CA . ARG A 1 187 ? -4.746 -17.198 33.404 1.00 98.30 ? 187 ARG A CA 1 ATOM 1230 C C . ARG A 1 187 ? -5.967 -18.020 33.809 1.00 91.45 ? 187 ARG A C 1 ATOM 1231 O O . ARG A 1 187 ? -6.283 -18.143 34.991 1.00 94.47 ? 187 ARG A O 1 ATOM 1232 C CB . ARG A 1 187 ? -5.049 -15.688 33.471 1.00 96.63 ? 187 ARG A CB 1 ATOM 1233 C CG . ARG A 1 187 ? -3.832 -14.778 33.234 1.00 105.32 ? 187 ARG A CG 1 ATOM 1234 C CD . ARG A 1 187 ? -4.153 -13.274 33.359 1.00 120.56 ? 187 ARG A CD 1 ATOM 1235 N NE . ARG A 1 187 ? -4.063 -12.789 34.743 1.00 134.22 ? 187 ARG A NE 1 ATOM 1236 C CZ . ARG A 1 187 ? -3.877 -11.515 35.095 1.00 127.25 ? 187 ARG A CZ 1 ATOM 1237 N NH1 . ARG A 1 187 ? -3.749 -10.572 34.169 1.00 126.23 ? 187 ARG A NH1 1 ATOM 1238 N NH2 . ARG A 1 187 ? -3.811 -11.184 36.379 1.00 116.63 ? 187 ARG A NH2 1 ATOM 1239 N N . ASN A 1 188 ? -6.635 -18.603 32.821 1.00 87.15 ? 188 ASN A N 1 ATOM 1240 C CA . ASN A 1 188 ? -7.857 -19.355 33.076 1.00 92.85 ? 188 ASN A CA 1 ATOM 1241 C C . ASN A 1 188 ? -8.207 -20.300 31.930 1.00 85.18 ? 188 ASN A C 1 ATOM 1242 O O . ASN A 1 188 ? -8.211 -19.913 30.765 1.00 96.74 ? 188 ASN A O 1 ATOM 1243 C CB . ASN A 1 188 ? -9.019 -18.394 33.341 1.00 105.20 ? 188 ASN A CB 1 ATOM 1244 C CG . ASN A 1 188 ? -10.226 -19.086 33.926 1.00 113.03 ? 188 ASN A CG 1 ATOM 1245 O OD1 . ASN A 1 188 ? -10.642 -20.146 33.452 1.00 111.31 ? 188 ASN A OD1 1 ATOM 1246 N ND2 . ASN A 1 188 ? -10.800 -18.488 34.967 1.00 118.24 ? 188 ASN A ND2 1 ATOM 1247 N N . TYR A 1 189 ? -8.499 -21.545 32.274 1.00 70.62 ? 189 TYR A N 1 ATOM 1248 C CA . TYR A 1 189 ? -8.859 -22.557 31.299 1.00 63.18 ? 189 TYR A CA 1 ATOM 1249 C C . TYR A 1 189 ? -10.172 -23.182 31.732 1.00 69.74 ? 189 TYR A C 1 ATOM 1250 O O . TYR A 1 189 ? -10.214 -24.006 32.636 1.00 82.46 ? 189 TYR A O 1 ATOM 1251 C CB . TYR A 1 189 ? -7.754 -23.625 31.170 1.00 67.53 ? 189 TYR A CB 1 ATOM 1252 C CG . TYR A 1 189 ? -8.180 -24.903 30.459 1.00 76.10 ? 189 TYR A CG 1 ATOM 1253 C CD1 . TYR A 1 189 ? -7.791 -25.167 29.152 1.00 71.46 ? 189 TYR A CD1 1 ATOM 1254 C CD2 . TYR A 1 189 ? -8.973 -25.844 31.101 1.00 87.71 ? 189 TYR A CD2 1 ATOM 1255 C CE1 . TYR A 1 189 ? -8.191 -26.330 28.512 1.00 76.20 ? 189 TYR A CE1 1 ATOM 1256 C CE2 . TYR A 1 189 ? -9.376 -27.005 30.467 1.00 87.37 ? 189 TYR A CE2 1 ATOM 1257 C CZ . TYR A 1 189 ? -8.985 -27.248 29.178 1.00 77.20 ? 189 TYR A CZ 1 ATOM 1258 O OH . TYR A 1 189 ? -9.398 -28.412 28.568 1.00 62.92 ? 189 TYR A OH 1 ATOM 1259 N N . GLN A 1 190 ? -11.255 -22.761 31.098 1.00 75.84 ? 190 GLN A N 1 ATOM 1260 C CA . GLN A 1 190 ? -12.556 -23.348 31.349 1.00 75.39 ? 190 GLN A CA 1 ATOM 1261 C C . GLN A 1 190 ? -12.532 -24.871 31.231 1.00 82.70 ? 190 GLN A C 1 ATOM 1262 O O . GLN A 1 190 ? -11.904 -25.439 30.344 1.00 76.27 ? 190 GLN A O 1 ATOM 1263 C CB . GLN A 1 190 ? -13.580 -22.765 30.388 1.00 71.34 ? 190 GLN A CB 1 ATOM 1264 C CG . GLN A 1 190 ? -14.931 -23.426 30.468 1.00 86.30 ? 190 GLN A CG 1 ATOM 1265 C CD . GLN A 1 190 ? -15.998 -22.571 29.840 1.00 98.57 ? 190 GLN A CD 1 ATOM 1266 O OE1 . GLN A 1 190 ? -15.796 -21.375 29.632 1.00 106.70 ? 190 GLN A OE1 1 ATOM 1267 N NE2 . GLN A 1 190 ? -17.143 -23.173 29.535 1.00 96.36 ? 190 GLN A NE2 1 ATOM 1268 N N . SER A 1 191 ? -13.224 -25.529 32.145 1.00 100.74 ? 191 SER A N 1 ATOM 1269 C CA . SER A 1 191 ? -13.279 -26.979 32.155 1.00 105.35 ? 191 SER A CA 1 ATOM 1270 C C . SER A 1 191 ? -13.906 -27.529 30.874 1.00 91.31 ? 191 SER A C 1 ATOM 1271 O O . SER A 1 191 ? -14.944 -27.046 30.433 1.00 77.33 ? 191 SER A O 1 ATOM 1272 C CB . SER A 1 191 ? -14.037 -27.463 33.399 1.00 115.87 ? 191 SER A CB 1 ATOM 1273 O OG . SER A 1 191 ? -14.817 -26.417 33.970 1.00 116.52 ? 191 SER A OG 1 ATOM 1274 N N . GLN A 1 192 ? -13.239 -28.515 30.275 1.00 89.73 ? 192 GLN A N 1 ATOM 1275 C CA . GLN A 1 192 ? -13.774 -29.307 29.158 1.00 83.24 ? 192 GLN A CA 1 ATOM 1276 C C . GLN A 1 192 ? -13.651 -28.672 27.765 1.00 81.69 ? 192 GLN A C 1 ATOM 1277 O O . GLN A 1 192 ? -14.332 -29.077 26.824 1.00 73.20 ? 192 GLN A O 1 ATOM 1278 C CB . GLN A 1 192 ? -15.216 -29.737 29.433 1.00 78.23 ? 192 GLN A CB 1 ATOM 1279 C CG . GLN A 1 192 ? -15.372 -30.578 30.678 1.00 84.98 ? 192 GLN A CG 1 ATOM 1280 C CD . GLN A 1 192 ? -16.669 -31.358 30.690 1.00 91.89 ? 192 GLN A CD 1 ATOM 1281 O OE1 . GLN A 1 192 ? -17.218 -31.683 29.636 1.00 90.99 ? 192 GLN A OE1 1 ATOM 1282 N NE2 . GLN A 1 192 ? -17.163 -31.673 31.886 1.00 91.60 ? 192 GLN A NE2 1 ATOM 1283 N N . SER A 1 193 ? -12.767 -27.692 27.633 1.00 84.91 ? 193 SER A N 1 ATOM 1284 C CA . SER A 1 193 ? -12.519 -27.063 26.342 1.00 74.42 ? 193 SER A CA 1 ATOM 1285 C C . SER A 1 193 ? -12.012 -28.039 25.276 1.00 72.84 ? 193 SER A C 1 ATOM 1286 O O . SER A 1 193 ? -12.581 -28.096 24.192 1.00 87.63 ? 193 SER A O 1 ATOM 1287 C CB . SER A 1 193 ? -11.547 -25.903 26.506 1.00 74.70 ? 193 SER A CB 1 ATOM 1288 O OG . SER A 1 193 ? -12.027 -25.017 27.503 1.00 76.48 ? 193 SER A OG 1 ATOM 1289 N N . LEU A 1 194 ? -10.962 -28.807 25.576 1.00 61.66 ? 194 LEU A N 1 ATOM 1290 C CA . LEU A 1 194 ? -10.390 -29.755 24.608 1.00 54.88 ? 194 LEU A CA 1 ATOM 1291 C C . LEU A 1 194 ? -11.121 -31.096 24.489 1.00 73.66 ? 194 LEU A C 1 ATOM 1292 O O . LEU A 1 194 ? -10.719 -31.945 23.680 1.00 82.47 ? 194 LEU A O 1 ATOM 1293 C CB . LEU A 1 194 ? -8.924 -30.073 24.926 1.00 54.16 ? 194 LEU A CB 1 ATOM 1294 C CG . LEU A 1 194 ? -7.774 -29.099 24.698 1.00 56.69 ? 194 LEU A CG 1 ATOM 1295 C CD1 . LEU A 1 194 ? -7.824 -28.536 23.296 1.00 74.97 ? 194 LEU A CD1 1 ATOM 1296 C CD2 . LEU A 1 194 ? -7.851 -27.996 25.717 1.00 53.59 ? 194 LEU A CD2 1 ATOM 1297 N N . LYS A 1 195 ? -12.164 -31.313 25.289 1.00 76.79 ? 195 LYS A N 1 ATOM 1298 C CA . LYS A 1 195 ? -12.780 -32.646 25.346 1.00 81.72 ? 195 LYS A CA 1 ATOM 1299 C C . LYS A 1 195 ? -13.709 -32.985 24.169 1.00 87.89 ? 195 LYS A C 1 ATOM 1300 O O . LYS A 1 195 ? -13.872 -34.159 23.824 1.00 92.71 ? 195 LYS A O 1 ATOM 1301 C CB . LYS A 1 195 ? -13.499 -32.883 26.679 1.00 78.09 ? 195 LYS A CB 1 ATOM 1302 C CG . LYS A 1 195 ? -13.853 -34.348 26.919 1.00 84.10 ? 195 LYS A CG 1 ATOM 1303 C CD . LYS A 1 195 ? -14.948 -34.515 27.969 1.00 95.64 ? 195 LYS A CD 1 ATOM 1304 C CE . LYS A 1 195 ? -15.028 -35.956 28.480 1.00 94.78 ? 195 LYS A CE 1 ATOM 1305 N NZ . LYS A 1 195 ? -15.298 -36.939 27.394 1.00 90.01 ? 195 LYS A NZ 1 ATOM 1306 N N . SER A 1 196 ? -14.312 -31.966 23.557 1.00 81.83 ? 196 SER A N 1 ATOM 1307 C CA . SER A 1 196 ? -15.236 -32.184 22.443 1.00 85.64 ? 196 SER A CA 1 ATOM 1308 C C . SER A 1 196 ? -14.517 -32.732 21.209 1.00 87.53 ? 196 SER A C 1 ATOM 1309 O O . SER A 1 196 ? -15.087 -33.503 20.432 1.00 84.13 ? 196 SER A O 1 ATOM 1310 C CB . SER A 1 196 ? -15.985 -30.893 22.107 1.00 84.82 ? 196 SER A CB 1 ATOM 1311 O OG . SER A 1 196 ? -15.154 -29.759 22.302 1.00 88.55 ? 196 SER A OG 1 ATOM 1312 N N . ILE A 1 197 ? -13.258 -32.332 21.046 1.00 81.27 ? 197 ILE A N 1 ATOM 1313 C CA . ILE A 1 197 ? -12.428 -32.810 19.953 1.00 70.81 ? 197 ILE A CA 1 ATOM 1314 C C . ILE A 1 197 ? -12.159 -34.303 20.086 1.00 65.92 ? 197 ILE A C 1 ATOM 1315 O O . ILE A 1 197 ? -11.515 -34.738 21.030 1.00 70.76 ? 197 ILE A O 1 ATOM 1316 C CB . ILE A 1 197 ? -11.092 -32.052 19.889 1.00 62.19 ? 197 ILE A CB 1 ATOM 1317 C CG1 . ILE A 1 197 ? -11.336 -30.542 19.829 1.00 55.54 ? 197 ILE A CG1 1 ATOM 1318 C CG2 . ILE A 1 197 ? -10.282 -32.516 18.686 1.00 55.81 ? 197 ILE A CG2 1 ATOM 1319 C CD1 . ILE A 1 197 ? -10.059 -29.717 19.789 1.00 52.01 ? 197 ILE A CD1 1 ATOM 1320 N N . ARG A 1 198 ? -12.646 -35.074 19.120 1.00 67.69 ? 198 ARG A N 1 ATOM 1321 C CA . ARG A 1 198 ? -12.623 -36.533 19.181 1.00 80.99 ? 198 ARG A CA 1 ATOM 1322 C C . ARG A 1 198 ? -11.236 -37.162 18.980 1.00 74.83 ? 198 ARG A C 1 ATOM 1323 O O . ARG A 1 198 ? -10.899 -38.167 19.617 1.00 70.73 ? 198 ARG A O 1 ATOM 1324 C CB . ARG A 1 198 ? -13.629 -37.112 18.167 1.00 91.42 ? 198 ARG A CB 1 ATOM 1325 C CG . ARG A 1 198 ? -13.875 -38.612 18.306 1.00 112.16 ? 198 ARG A CG 1 ATOM 1326 C CD . ARG A 1 198 ? -15.168 -39.061 17.626 1.00 131.77 ? 198 ARG A CD 1 ATOM 1327 N NE . ARG A 1 198 ? -14.977 -39.502 16.243 1.00 145.72 ? 198 ARG A NE 1 ATOM 1328 C CZ . ARG A 1 198 ? -14.411 -40.657 15.894 1.00 150.25 ? 198 ARG A CZ 1 ATOM 1329 N NH1 . ARG A 1 198 ? -13.957 -41.486 16.826 1.00 148.91 ? 198 ARG A NH1 1 ATOM 1330 N NH2 . ARG A 1 198 ? -14.287 -40.980 14.613 1.00 149.01 ? 198 ARG A NH2 1 ATOM 1331 N N . ASP A 1 199 ? -10.442 -36.571 18.094 1.00 67.65 ? 199 ASP A N 1 ATOM 1332 C CA . ASP A 1 199 ? -9.154 -37.132 17.717 1.00 69.15 ? 199 ASP A CA 1 ATOM 1333 C C . ASP A 1 199 ? -8.161 -36.009 17.414 1.00 68.73 ? 199 ASP A C 1 ATOM 1334 O O . ASP A 1 199 ? -8.456 -35.124 16.615 1.00 69.74 ? 199 ASP A O 1 ATOM 1335 C CB . ASP A 1 199 ? -9.327 -38.036 16.491 1.00 81.59 ? 199 ASP A CB 1 ATOM 1336 C CG . ASP A 1 199 ? -8.086 -38.868 16.184 1.00 92.62 ? 199 ASP A CG 1 ATOM 1337 O OD1 . ASP A 1 199 ? -8.039 -39.487 15.095 1.00 85.13 ? 199 ASP A OD1 1 ATOM 1338 O OD2 . ASP A 1 199 ? -7.163 -38.908 17.030 1.00 93.89 ? 199 ASP A OD2 1 ATOM 1339 N N . ILE A 1 200 ? -6.997 -36.041 18.066 1.00 62.40 ? 200 ILE A N 1 ATOM 1340 C CA . ILE A 1 200 ? -5.912 -35.084 17.805 1.00 55.39 ? 200 ILE A CA 1 ATOM 1341 C C . ILE A 1 200 ? -4.588 -35.817 17.626 1.00 55.62 ? 200 ILE A C 1 ATOM 1342 O O . ILE A 1 200 ? -4.121 -36.466 18.545 1.00 58.37 ? 200 ILE A O 1 ATOM 1343 C CB . ILE A 1 200 ? -5.740 -34.092 18.954 1.00 54.31 ? 200 ILE A CB 1 ATOM 1344 C CG1 . ILE A 1 200 ? -6.993 -33.216 19.085 1.00 61.17 ? 200 ILE A CG1 1 ATOM 1345 C CG2 . ILE A 1 200 ? -4.484 -33.266 18.734 1.00 48.13 ? 200 ILE A CG2 1 ATOM 1346 C CD1 . ILE A 1 200 ? -7.033 -32.323 20.325 1.00 59.18 ? 200 ILE A CD1 1 ATOM 1347 N N . HIS A 1 201 ? -3.975 -35.727 16.452 1.00 54.81 ? 201 HIS A N 1 ATOM 1348 C CA . HIS A 1 201 ? -2.832 -36.591 16.180 1.00 51.46 ? 201 HIS A CA 1 ATOM 1349 C C . HIS A 1 201 ? -1.588 -36.142 16.902 1.00 60.96 ? 201 HIS A C 1 ATOM 1350 O O . HIS A 1 201 ? -0.763 -36.966 17.311 1.00 63.69 ? 201 HIS A O 1 ATOM 1351 C CB . HIS A 1 201 ? -2.578 -36.747 14.683 1.00 60.14 ? 201 HIS A CB 1 ATOM 1352 C CG . HIS A 1 201 ? -3.684 -37.455 13.963 1.00 80.77 ? 201 HIS A CG 1 ATOM 1353 N ND1 . HIS A 1 201 ? -3.926 -37.288 12.616 1.00 83.58 ? 201 HIS A ND1 1 ATOM 1354 C CD2 . HIS A 1 201 ? -4.632 -38.311 14.413 1.00 87.02 ? 201 HIS A CD2 1 ATOM 1355 C CE1 . HIS A 1 201 ? -4.969 -38.020 12.267 1.00 88.63 ? 201 HIS A CE1 1 ATOM 1356 N NE2 . HIS A 1 201 ? -5.415 -38.652 13.339 1.00 91.47 ? 201 HIS A NE2 1 ATOM 1357 N N . HIS A 1 202 ? -1.471 -34.832 17.082 1.00 58.71 ? 202 HIS A N 1 ATOM 1358 C CA . HIS A 1 202 ? -0.308 -34.261 17.736 1.00 50.49 ? 202 HIS A CA 1 ATOM 1359 C C . HIS A 1 202 ? -0.653 -32.874 18.268 1.00 53.48 ? 202 HIS A C 1 ATOM 1360 O O . HIS A 1 202 ? -0.785 -31.907 17.525 1.00 54.21 ? 202 HIS A O 1 ATOM 1361 C CB . HIS A 1 202 ? 0.889 -34.288 16.772 1.00 47.55 ? 202 HIS A CB 1 ATOM 1362 C CG . HIS A 1 202 ? 2.104 -33.552 17.244 1.00 51.79 ? 202 HIS A CG 1 ATOM 1363 N ND1 . HIS A 1 202 ? 3.060 -33.079 16.371 1.00 56.87 ? 202 HIS A ND1 1 ATOM 1364 C CD2 . HIS A 1 202 ? 2.525 -33.203 18.481 1.00 65.69 ? 202 HIS A CD2 1 ATOM 1365 C CE1 . HIS A 1 202 ? 4.019 -32.478 17.050 1.00 59.25 ? 202 HIS A CE1 1 ATOM 1366 N NE2 . HIS A 1 202 ? 3.717 -32.534 18.332 1.00 61.30 ? 202 HIS A NE2 1 ATOM 1367 N N . LEU A 1 203 ? -0.835 -32.816 19.581 1.00 57.61 ? 203 LEU A N 1 ATOM 1368 C CA . LEU A 1 203 ? -1.107 -31.582 20.297 1.00 48.15 ? 203 LEU A CA 1 ATOM 1369 C C . LEU A 1 203 ? 0.181 -31.068 20.917 1.00 56.53 ? 203 LEU A C 1 ATOM 1370 O O . LEU A 1 203 ? 0.823 -31.765 21.697 1.00 57.52 ? 203 LEU A O 1 ATOM 1371 C CB . LEU A 1 203 ? -2.129 -31.848 21.391 1.00 40.76 ? 203 LEU A CB 1 ATOM 1372 C CG . LEU A 1 203 ? -2.377 -30.731 22.392 1.00 52.70 ? 203 LEU A CG 1 ATOM 1373 C CD1 . LEU A 1 203 ? -2.992 -29.559 21.689 1.00 62.63 ? 203 LEU A CD1 1 ATOM 1374 C CD2 . LEU A 1 203 ? -3.280 -31.222 23.519 1.00 57.33 ? 203 LEU A CD2 1 ATOM 1375 N N . THR A 1 204 ? 0.563 -29.854 20.545 1.00 61.71 ? 204 THR A N 1 ATOM 1376 C CA . THR A 1 204 ? 1.702 -29.183 21.146 1.00 57.44 ? 204 THR A CA 1 ATOM 1377 C C . THR A 1 204 ? 1.169 -28.071 22.043 1.00 59.23 ? 204 THR A C 1 ATOM 1378 O O . THR A 1 204 ? 0.573 -27.114 21.557 1.00 61.27 ? 204 THR A O 1 ATOM 1379 C CB . THR A 1 204 ? 2.649 -28.613 20.067 1.00 52.00 ? 204 THR A CB 1 ATOM 1380 O OG1 . THR A 1 204 ? 3.148 -29.684 19.276 1.00 55.11 ? 204 THR A OG1 1 ATOM 1381 C CG2 . THR A 1 204 ? 3.836 -27.908 20.682 1.00 48.29 ? 204 THR A CG2 1 ATOM 1382 N N . LEU A 1 205 ? 1.368 -28.227 23.351 1.00 61.11 ? 205 LEU A N 1 ATOM 1383 C CA . LEU A 1 205 ? 0.990 -27.227 24.357 1.00 56.74 ? 205 LEU A CA 1 ATOM 1384 C C . LEU A 1 205 ? 2.194 -26.450 24.870 1.00 59.02 ? 205 LEU A C 1 ATOM 1385 O O . LEU A 1 205 ? 3.217 -27.042 25.189 1.00 62.87 ? 205 LEU A O 1 ATOM 1386 C CB . LEU A 1 205 ? 0.362 -27.921 25.559 1.00 55.88 ? 205 LEU A CB 1 ATOM 1387 C CG . LEU A 1 205 ? -1.141 -28.090 25.591 1.00 56.87 ? 205 LEU A CG 1 ATOM 1388 C CD1 . LEU A 1 205 ? -1.563 -28.585 26.960 1.00 54.55 ? 205 LEU A CD1 1 ATOM 1389 C CD2 . LEU A 1 205 ? -1.743 -26.745 25.291 1.00 59.21 ? 205 LEU A CD2 1 ATOM 1390 N N . HIS A 1 206 ? 2.075 -25.130 24.962 1.00 63.16 ? 206 HIS A N 1 ATOM 1391 C CA . HIS A 1 206 ? 3.065 -24.328 25.684 1.00 59.36 ? 206 HIS A CA 1 ATOM 1392 C C . HIS A 1 206 ? 2.424 -23.758 26.936 1.00 57.96 ? 206 HIS A C 1 ATOM 1393 O O . HIS A 1 206 ? 1.624 -22.829 26.852 1.00 52.65 ? 206 HIS A O 1 ATOM 1394 C CB . HIS A 1 206 ? 3.565 -23.149 24.854 1.00 65.63 ? 206 HIS A CB 1 ATOM 1395 C CG . HIS A 1 206 ? 3.990 -23.504 23.466 1.00 67.82 ? 206 HIS A CG 1 ATOM 1396 N ND1 . HIS A 1 206 ? 5.217 -23.146 22.955 1.00 61.13 ? 206 HIS A ND1 1 ATOM 1397 C CD2 . HIS A 1 206 ? 3.343 -24.160 22.476 1.00 70.18 ? 206 HIS A CD2 1 ATOM 1398 C CE1 . HIS A 1 206 ? 5.313 -23.578 21.712 1.00 56.54 ? 206 HIS A CE1 1 ATOM 1399 N NE2 . HIS A 1 206 ? 4.190 -24.197 21.396 1.00 61.66 ? 206 HIS A NE2 1 ATOM 1400 N N . LEU A 1 207 ? 2.765 -24.317 28.091 1.00 64.58 ? 207 LEU A N 1 ATOM 1401 C CA . LEU A 1 207 ? 2.353 -23.752 29.370 1.00 60.43 ? 207 LEU A CA 1 ATOM 1402 C C . LEU A 1 207 ? 3.615 -23.390 30.140 1.00 69.89 ? 207 LEU A C 1 ATOM 1403 O O . LEU A 1 207 ? 4.594 -24.144 30.104 1.00 64.35 ? 207 LEU A O 1 ATOM 1404 C CB . LEU A 1 207 ? 1.530 -24.763 30.165 1.00 48.52 ? 207 LEU A CB 1 ATOM 1405 C CG . LEU A 1 207 ? 0.255 -25.300 29.520 1.00 53.66 ? 207 LEU A CG 1 ATOM 1406 C CD1 . LEU A 1 207 ? -0.184 -26.551 30.257 1.00 57.32 ? 207 LEU A CD1 1 ATOM 1407 C CD2 . LEU A 1 207 ? -0.862 -24.250 29.501 1.00 43.00 ? 207 LEU A CD2 1 ATOM 1408 N N . SER A 1 208 ? 3.598 -22.245 30.828 1.00 69.48 ? 208 SER A N 1 ATOM 1409 C CA . SER A 1 208 ? 4.747 -21.797 31.626 1.00 60.82 ? 208 SER A CA 1 ATOM 1410 C C . SER A 1 208 ? 4.829 -22.455 33.002 1.00 65.62 ? 208 SER A C 1 ATOM 1411 O O . SER A 1 208 ? 5.886 -22.444 33.639 1.00 74.22 ? 208 SER A O 1 ATOM 1412 C CB . SER A 1 208 ? 4.757 -20.271 31.777 1.00 63.43 ? 208 SER A CB 1 ATOM 1413 O OG . SER A 1 208 ? 3.649 -19.802 32.525 1.00 65.74 ? 208 SER A OG 1 ATOM 1414 N N . GLU A 1 209 ? 3.714 -23.031 33.445 1.00 57.05 ? 209 GLU A N 1 ATOM 1415 C CA . GLU A 1 209 ? 3.623 -23.643 34.759 1.00 61.83 ? 209 GLU A CA 1 ATOM 1416 C C . GLU A 1 209 ? 2.468 -24.635 34.866 1.00 62.80 ? 209 GLU A C 1 ATOM 1417 O O . GLU A 1 209 ? 1.593 -24.661 34.011 1.00 73.80 ? 209 GLU A O 1 ATOM 1418 C CB . GLU A 1 209 ? 3.530 -22.558 35.829 1.00 80.34 ? 209 GLU A CB 1 ATOM 1419 C CG . GLU A 1 209 ? 2.886 -21.269 35.355 1.00 85.45 ? 209 GLU A CG 1 ATOM 1420 C CD . GLU A 1 209 ? 1.391 -21.269 35.561 1.00 94.80 ? 209 GLU A CD 1 ATOM 1421 O OE1 . GLU A 1 209 ? 0.727 -20.297 35.129 1.00 99.40 ? 209 GLU A OE1 1 ATOM 1422 O OE2 . GLU A 1 209 ? 0.888 -22.246 36.159 1.00 92.60 ? 209 GLU A OE2 1 ATOM 1423 N N . SER A 1 210 ? 2.463 -25.429 35.936 1.00 64.88 ? 210 SER A N 1 ATOM 1424 C CA . SER A 1 210 ? 1.651 -26.650 36.034 1.00 66.48 ? 210 SER A CA 1 ATOM 1425 C C . SER A 1 210 ? 0.167 -26.474 36.385 1.00 72.14 ? 210 SER A C 1 ATOM 1426 O O . SER A 1 210 ? -0.611 -27.443 36.333 1.00 63.58 ? 210 SER A O 1 ATOM 1427 C CB . SER A 1 210 ? 2.287 -27.597 37.054 1.00 77.71 ? 210 SER A CB 1 ATOM 1428 O OG . SER A 1 210 ? 2.261 -27.028 38.359 1.00 90.63 ? 210 SER A OG 1 ATOM 1429 N N . ALA A 1 211 ? -0.215 -25.248 36.738 1.00 75.16 ? 211 ALA A N 1 ATOM 1430 C CA . ALA A 1 211 ? -1.546 -24.956 37.283 1.00 74.05 ? 211 ALA A CA 1 ATOM 1431 C C . ALA A 1 211 ? -2.739 -25.554 36.524 1.00 83.96 ? 211 ALA A C 1 ATOM 1432 O O . ALA A 1 211 ? -3.795 -25.811 37.112 1.00 87.08 ? 211 ALA A O 1 ATOM 1433 C CB . ALA A 1 211 ? -1.733 -23.452 37.449 1.00 68.69 ? 211 ALA A CB 1 ATOM 1434 N N . PHE A 1 212 ? -2.596 -25.762 35.222 1.00 78.26 ? 212 PHE A N 1 ATOM 1435 C CA . PHE A 1 212 ? -3.735 -26.259 34.470 1.00 76.74 ? 212 PHE A CA 1 ATOM 1436 C C . PHE A 1 212 ? -3.457 -27.593 33.803 1.00 73.38 ? 212 PHE A C 1 ATOM 1437 O O . PHE A 1 212 ? -4.370 -28.202 33.244 1.00 61.46 ? 212 PHE A O 1 ATOM 1438 C CB . PHE A 1 212 ? -4.195 -25.237 33.435 1.00 78.08 ? 212 PHE A CB 1 ATOM 1439 C CG . PHE A 1 212 ? -5.020 -24.114 34.006 1.00 77.87 ? 212 PHE A CG 1 ATOM 1440 C CD1 . PHE A 1 212 ? -4.480 -22.843 34.155 1.00 71.70 ? 212 PHE A CD1 1 ATOM 1441 C CD2 . PHE A 1 212 ? -6.343 -24.322 34.374 1.00 78.69 ? 212 PHE A CD2 1 ATOM 1442 C CE1 . PHE A 1 212 ? -5.242 -21.804 34.664 1.00 67.88 ? 212 PHE A CE1 1 ATOM 1443 C CE2 . PHE A 1 212 ? -7.113 -23.282 34.888 1.00 72.02 ? 212 PHE A CE2 1 ATOM 1444 C CZ . PHE A 1 212 ? -6.561 -22.023 35.033 1.00 67.20 ? 212 PHE A CZ 1 ATOM 1445 N N . LEU A 1 213 ? -2.207 -28.050 33.869 1.00 68.91 ? 213 LEU A N 1 ATOM 1446 C CA . LEU A 1 213 ? -1.821 -29.295 33.205 1.00 56.73 ? 213 LEU A CA 1 ATOM 1447 C C . LEU A 1 213 ? -2.722 -30.473 33.593 1.00 63.79 ? 213 LEU A C 1 ATOM 1448 O O . LEU A 1 213 ? -3.213 -31.186 32.720 1.00 74.57 ? 213 LEU A O 1 ATOM 1449 C CB . LEU A 1 213 ? -0.336 -29.617 33.416 1.00 51.14 ? 213 LEU A CB 1 ATOM 1450 C CG . LEU A 1 213 ? 0.222 -30.948 32.880 1.00 54.80 ? 213 LEU A CG 1 ATOM 1451 C CD1 . LEU A 1 213 ? 0.187 -31.054 31.349 1.00 44.83 ? 213 LEU A CD1 1 ATOM 1452 C CD2 . LEU A 1 213 ? 1.630 -31.205 33.383 1.00 47.43 ? 213 LEU A CD2 1 ATOM 1453 N N . LEU A 1 214 ? -2.958 -30.675 34.884 1.00 64.97 ? 214 LEU A N 1 ATOM 1454 C CA . LEU A 1 214 ? -3.855 -31.749 35.315 1.00 70.30 ? 214 LEU A CA 1 ATOM 1455 C C . LEU A 1 214 ? -5.242 -31.644 34.701 1.00 65.83 ? 214 LEU A C 1 ATOM 1456 O O . LEU A 1 214 ? -5.787 -32.634 34.211 1.00 62.70 ? 214 LEU A O 1 ATOM 1457 C CB . LEU A 1 214 ? -3.983 -31.793 36.836 1.00 79.50 ? 214 LEU A CB 1 ATOM 1458 C CG . LEU A 1 214 ? -3.123 -32.850 37.518 1.00 84.32 ? 214 LEU A CG 1 ATOM 1459 C CD1 . LEU A 1 214 ? -3.354 -32.820 39.023 1.00 86.86 ? 214 LEU A CD1 1 ATOM 1460 C CD2 . LEU A 1 214 ? -3.411 -34.228 36.929 1.00 76.91 ? 214 LEU A CD2 1 ATOM 1461 N N . GLU A 1 215 ? -5.818 -30.446 34.749 1.00 66.41 ? 215 GLU A N 1 ATOM 1462 C CA . GLU A 1 215 ? -7.141 -30.211 34.170 1.00 72.86 ? 215 GLU A CA 1 ATOM 1463 C C . GLU A 1 215 ? -7.225 -30.489 32.644 1.00 80.49 ? 215 GLU A C 1 ATOM 1464 O O . GLU A 1 215 ? -8.190 -31.100 32.167 1.00 71.72 ? 215 GLU A O 1 ATOM 1465 C CB . GLU A 1 215 ? -7.626 -28.791 34.499 1.00 70.54 ? 215 GLU A CB 1 ATOM 1466 C CG . GLU A 1 215 ? -8.842 -28.747 35.396 1.00 81.04 ? 215 GLU A CG 1 ATOM 1467 C CD . GLU A 1 215 ? -9.746 -27.553 35.116 1.00 95.89 ? 215 GLU A CD 1 ATOM 1468 O OE1 . GLU A 1 215 ? -10.974 -27.754 34.960 1.00 94.50 ? 215 GLU A OE1 1 ATOM 1469 O OE2 . GLU A 1 215 ? -9.230 -26.414 35.053 1.00 101.52 ? 215 GLU A OE2 1 ATOM 1470 N N . ILE A 1 216 ? -6.214 -30.041 31.894 1.00 72.11 ? 216 ILE A N 1 ATOM 1471 C CA . ILE A 1 216 ? -6.179 -30.214 30.445 1.00 66.51 ? 216 ILE A CA 1 ATOM 1472 C C . ILE A 1 216 ? -5.879 -31.658 30.057 1.00 65.51 ? 216 ILE A C 1 ATOM 1473 O O . ILE A 1 216 ? -6.501 -32.206 29.155 1.00 76.50 ? 216 ILE A O 1 ATOM 1474 C CB . ILE A 1 216 ? -5.143 -29.282 29.772 1.00 68.54 ? 216 ILE A CB 1 ATOM 1475 C CG1 . ILE A 1 216 ? -5.387 -27.827 30.153 1.00 72.33 ? 216 ILE A CG1 1 ATOM 1476 C CG2 . ILE A 1 216 ? -5.204 -29.418 28.260 1.00 65.09 ? 216 ILE A CG2 1 ATOM 1477 C CD1 . ILE A 1 216 ? -4.292 -26.895 29.683 1.00 69.64 ? 216 ILE A CD1 1 ATOM 1478 N N . PHE A 1 217 ? -4.915 -32.264 30.737 1.00 65.76 ? 217 PHE A N 1 ATOM 1479 C CA . PHE A 1 217 ? -4.545 -33.656 30.498 1.00 64.62 ? 217 PHE A CA 1 ATOM 1480 C C . PHE A 1 217 ? -5.762 -34.579 30.592 1.00 66.04 ? 217 PHE A C 1 ATOM 1481 O O . PHE A 1 217 ? -5.829 -35.596 29.915 1.00 68.42 ? 217 PHE A O 1 ATOM 1482 C CB . PHE A 1 217 ? -3.454 -34.076 31.495 1.00 64.57 ? 217 PHE A CB 1 ATOM 1483 C CG . PHE A 1 217 ? -2.979 -35.494 31.335 1.00 68.16 ? 217 PHE A CG 1 ATOM 1484 C CD1 . PHE A 1 217 ? -2.093 -35.835 30.331 1.00 60.39 ? 217 PHE A CD1 1 ATOM 1485 C CD2 . PHE A 1 217 ? -3.393 -36.482 32.217 1.00 79.15 ? 217 PHE A CD2 1 ATOM 1486 C CE1 . PHE A 1 217 ? -1.643 -37.141 30.192 1.00 60.36 ? 217 PHE A CE1 1 ATOM 1487 C CE2 . PHE A 1 217 ? -2.945 -37.789 32.082 1.00 80.00 ? 217 PHE A CE2 1 ATOM 1488 C CZ . PHE A 1 217 ? -2.067 -38.116 31.066 1.00 71.09 ? 217 PHE A CZ 1 ATOM 1489 N N . ALA A 1 218 ? -6.730 -34.219 31.424 1.00 67.07 ? 218 ALA A N 1 ATOM 1490 C CA . ALA A 1 218 ? -7.910 -35.052 31.590 1.00 74.67 ? 218 ALA A CA 1 ATOM 1491 C C . ALA A 1 218 ? -8.812 -34.927 30.375 1.00 77.23 ? 218 ALA A C 1 ATOM 1492 O O . ALA A 1 218 ? -9.510 -35.871 29.999 1.00 89.83 ? 218 ALA A O 1 ATOM 1493 C CB . ALA A 1 218 ? -8.660 -34.662 32.849 1.00 77.10 ? 218 ALA A CB 1 ATOM 1494 N N . ASP A 1 219 ? -8.787 -33.751 29.763 1.00 70.06 ? 219 ASP A N 1 ATOM 1495 C CA . ASP A 1 219 ? -9.676 -33.436 28.653 1.00 70.14 ? 219 ASP A CA 1 ATOM 1496 C C . ASP A 1 219 ? -9.228 -34.052 27.337 1.00 68.79 ? 219 ASP A C 1 ATOM 1497 O O . ASP A 1 219 ? -10.017 -34.163 26.404 1.00 70.78 ? 219 ASP A O 1 ATOM 1498 C CB . ASP A 1 219 ? -9.808 -31.924 28.499 1.00 77.83 ? 219 ASP A CB 1 ATOM 1499 C CG . ASP A 1 219 ? -10.829 -31.330 29.451 1.00 84.67 ? 219 ASP A CG 1 ATOM 1500 O OD1 . ASP A 1 219 ? -11.629 -32.107 30.021 1.00 81.86 ? 219 ASP A OD1 1 ATOM 1501 O OD2 . ASP A 1 219 ? -10.834 -30.090 29.619 1.00 83.92 ? 219 ASP A OD2 1 ATOM 1502 N N . ILE A 1 220 ? -7.966 -34.469 27.276 1.00 72.15 ? 220 ILE A N 1 ATOM 1503 C CA . ILE A 1 220 ? -7.383 -35.017 26.055 1.00 65.31 ? 220 ILE A CA 1 ATOM 1504 C C . ILE A 1 220 ? -7.055 -36.506 26.169 1.00 60.40 ? 220 ILE A C 1 ATOM 1505 O O . ILE A 1 220 ? -6.314 -37.056 25.360 1.00 63.61 ? 220 ILE A O 1 ATOM 1506 C CB . ILE A 1 220 ? -6.089 -34.277 25.695 1.00 59.59 ? 220 ILE A CB 1 ATOM 1507 C CG1 . ILE A 1 220 ? -5.070 -34.453 26.822 1.00 54.42 ? 220 ILE A CG1 1 ATOM 1508 C CG2 . ILE A 1 220 ? -6.369 -32.797 25.388 1.00 50.35 ? 220 ILE A CG2 1 ATOM 1509 C CD1 . ILE A 1 220 ? -3.658 -34.184 26.409 1.00 66.87 ? 220 ILE A CD1 1 ATOM 1510 N N . LEU A 1 221 ? -7.606 -37.165 27.174 1.00 66.06 ? 221 LEU A N 1 ATOM 1511 C CA . LEU A 1 221 ? -7.245 -38.552 27.423 1.00 67.44 ? 221 LEU A CA 1 ATOM 1512 C C . LEU A 1 221 ? -7.683 -39.474 26.312 1.00 74.74 ? 221 LEU A C 1 ATOM 1513 O O . LEU A 1 221 ? -7.062 -40.509 26.089 1.00 73.31 ? 221 LEU A O 1 ATOM 1514 C CB . LEU A 1 221 ? -7.822 -39.042 28.741 1.00 64.55 ? 221 LEU A CB 1 ATOM 1515 C CG . LEU A 1 221 ? -6.938 -38.835 29.962 1.00 65.21 ? 221 LEU A CG 1 ATOM 1516 C CD1 . LEU A 1 221 ? -7.461 -39.710 31.083 1.00 68.54 ? 221 LEU A CD1 1 ATOM 1517 C CD2 . LEU A 1 221 ? -5.483 -39.170 29.617 1.00 51.28 ? 221 LEU A CD2 1 ATOM 1518 N N . SER A 1 222 ? -8.754 -39.102 25.617 1.00 77.46 ? 222 SER A N 1 ATOM 1519 C CA . SER A 1 222 ? -9.322 -39.985 24.602 1.00 80.56 ? 222 SER A CA 1 ATOM 1520 C C . SER A 1 222 ? -9.093 -39.482 23.188 1.00 73.22 ? 222 SER A C 1 ATOM 1521 O O . SER A 1 222 ? -9.466 -40.147 22.226 1.00 70.44 ? 222 SER A O 1 ATOM 1522 C CB . SER A 1 222 ? -10.819 -40.201 24.845 1.00 77.72 ? 222 SER A CB 1 ATOM 1523 O OG . SER A 1 222 ? -11.488 -38.962 24.932 1.00 75.34 ? 222 SER A OG 1 ATOM 1524 N N . SER A 1 223 ? -8.473 -38.313 23.068 1.00 70.70 ? 223 SER A N 1 ATOM 1525 C CA . SER A 1 223 ? -8.273 -37.690 21.764 1.00 68.31 ? 223 SER A CA 1 ATOM 1526 C C . SER A 1 223 ? -6.817 -37.658 21.292 1.00 71.39 ? 223 SER A C 1 ATOM 1527 O O . SER A 1 223 ? -6.509 -38.083 20.177 1.00 72.50 ? 223 SER A O 1 ATOM 1528 C CB . SER A 1 223 ? -8.872 -36.282 21.742 1.00 60.00 ? 223 SER A CB 1 ATOM 1529 O OG . SER A 1 223 ? -8.428 -35.521 22.844 1.00 69.72 ? 223 SER A OG 1 ATOM 1530 N N . VAL A 1 224 ? -5.927 -37.150 22.137 1.00 71.30 ? 224 VAL A N 1 ATOM 1531 C CA . VAL A 1 224 ? -4.524 -36.989 21.761 1.00 65.27 ? 224 VAL A CA 1 ATOM 1532 C C . VAL A 1 224 ? -3.743 -38.289 21.617 1.00 65.40 ? 224 VAL A C 1 ATOM 1533 O O . VAL A 1 224 ? -3.872 -39.210 22.420 1.00 77.64 ? 224 VAL A O 1 ATOM 1534 C CB . VAL A 1 224 ? -3.778 -36.102 22.745 1.00 61.80 ? 224 VAL A CB 1 ATOM 1535 C CG1 . VAL A 1 224 ? -2.296 -36.033 22.363 1.00 52.58 ? 224 VAL A CG1 1 ATOM 1536 C CG2 . VAL A 1 224 ? -4.424 -34.733 22.787 1.00 60.01 ? 224 VAL A CG2 1 ATOM 1537 N N . ARG A 1 225 ? -2.913 -38.321 20.585 1.00 62.56 ? 225 ARG A N 1 ATOM 1538 C CA . ARG A 1 225 ? -2.140 -39.490 20.213 1.00 67.29 ? 225 ARG A CA 1 ATOM 1539 C C . ARG A 1 225 ? -0.665 -39.188 20.456 1.00 62.94 ? 225 ARG A C 1 ATOM 1540 O O . ARG A 1 225 ? 0.174 -40.092 20.491 1.00 54.12 ? 225 ARG A O 1 ATOM 1541 C CB . ARG A 1 225 ? -2.360 -39.815 18.725 1.00 67.18 ? 225 ARG A CB 1 ATOM 1542 C CG . ARG A 1 225 ? -3.713 -40.426 18.362 1.00 61.36 ? 225 ARG A CG 1 ATOM 1543 C CD . ARG A 1 225 ? -3.879 -40.484 16.854 1.00 67.51 ? 225 ARG A CD 1 ATOM 1544 N NE . ARG A 1 225 ? -5.119 -41.136 16.446 1.00 80.25 ? 225 ARG A NE 1 ATOM 1545 C CZ . ARG A 1 225 ? -5.227 -42.441 16.220 1.00 82.38 ? 225 ARG A CZ 1 ATOM 1546 N NH1 . ARG A 1 225 ? -4.167 -43.224 16.373 1.00 90.07 ? 225 ARG A NH1 1 ATOM 1547 N NH2 . ARG A 1 225 ? -6.388 -42.965 15.852 1.00 69.42 ? 225 ARG A NH2 1 ATOM 1548 N N . TYR A 1 226 ? -0.356 -37.905 20.601 1.00 49.22 ? 226 TYR A N 1 ATOM 1549 C CA . TYR A 1 226 ? 1.003 -37.480 20.864 1.00 48.05 ? 226 TYR A CA 1 ATOM 1550 C C . TYR A 1 226 ? 0.936 -36.119 21.526 1.00 58.02 ? 226 TYR A C 1 ATOM 1551 O O . TYR A 1 226 ? 0.467 -35.153 20.930 1.00 56.53 ? 226 TYR A O 1 ATOM 1552 C CB . TYR A 1 226 ? 1.816 -37.456 19.570 1.00 43.19 ? 226 TYR A CB 1 ATOM 1553 C CG . TYR A 1 226 ? 3.173 -36.776 19.616 1.00 46.71 ? 226 TYR A CG 1 ATOM 1554 C CD1 . TYR A 1 226 ? 3.810 -36.384 18.443 1.00 48.51 ? 226 TYR A CD1 1 ATOM 1555 C CD2 . TYR A 1 226 ? 3.814 -36.519 20.812 1.00 48.63 ? 226 TYR A CD2 1 ATOM 1556 C CE1 . TYR A 1 226 ? 5.050 -35.768 18.471 1.00 55.20 ? 226 TYR A CE1 1 ATOM 1557 C CE2 . TYR A 1 226 ? 5.041 -35.893 20.847 1.00 47.88 ? 226 TYR A CE2 1 ATOM 1558 C CZ . TYR A 1 226 ? 5.658 -35.525 19.681 1.00 55.22 ? 226 TYR A CZ 1 ATOM 1559 O OH . TYR A 1 226 ? 6.887 -34.912 19.733 1.00 69.30 ? 226 TYR A OH 1 ATOM 1560 N N . LEU A 1 227 ? 1.381 -36.072 22.780 1.00 52.39 ? 227 LEU A N 1 ATOM 1561 C CA . LEU A 1 227 ? 1.374 -34.852 23.569 1.00 45.39 ? 227 LEU A CA 1 ATOM 1562 C C . LEU A 1 227 ? 2.782 -34.297 23.697 1.00 53.00 ? 227 LEU A C 1 ATOM 1563 O O . LEU A 1 227 ? 3.694 -34.985 24.130 1.00 51.24 ? 227 LEU A O 1 ATOM 1564 C CB . LEU A 1 227 ? 0.781 -35.126 24.946 1.00 43.12 ? 227 LEU A CB 1 ATOM 1565 C CG . LEU A 1 227 ? 0.709 -33.954 25.916 1.00 47.62 ? 227 LEU A CG 1 ATOM 1566 C CD1 . LEU A 1 227 ? 0.040 -32.750 25.277 1.00 42.17 ? 227 LEU A CD1 1 ATOM 1567 C CD2 . LEU A 1 227 ? -0.044 -34.394 27.154 1.00 47.20 ? 227 LEU A CD2 1 ATOM 1568 N N . GLU A 1 228 ? 2.957 -33.054 23.279 1.00 62.69 ? 228 GLU A N 1 ATOM 1569 C CA . GLU A 1 228 ? 4.232 -32.375 23.406 1.00 64.93 ? 228 GLU A CA 1 ATOM 1570 C C . GLU A 1 228 ? 3.998 -31.183 24.321 1.00 65.28 ? 228 GLU A C 1 ATOM 1571 O O . GLU A 1 228 ? 3.236 -30.278 23.994 1.00 64.15 ? 228 GLU A O 1 ATOM 1572 C CB . GLU A 1 228 ? 4.745 -31.925 22.030 1.00 65.26 ? 228 GLU A CB 1 ATOM 1573 C CG . GLU A 1 228 ? 6.156 -31.342 22.019 1.00 63.34 ? 228 GLU A CG 1 ATOM 1574 C CD . GLU A 1 228 ? 6.573 -30.815 20.652 1.00 69.06 ? 228 GLU A CD 1 ATOM 1575 O OE1 . GLU A 1 228 ? 7.300 -29.798 20.590 1.00 65.45 ? 228 GLU A OE1 1 ATOM 1576 O OE2 . GLU A 1 228 ? 6.171 -31.413 19.633 1.00 75.59 ? 228 GLU A OE2 1 ATOM 1577 N N . LEU A 1 229 ? 4.638 -31.199 25.483 1.00 66.31 ? 229 LEU A N 1 ATOM 1578 C CA . LEU A 1 229 ? 4.481 -30.132 26.461 1.00 55.29 ? 229 LEU A CA 1 ATOM 1579 C C . LEU A 1 229 ? 5.737 -29.271 26.464 1.00 49.59 ? 229 LEU A C 1 ATOM 1580 O O . LEU A 1 229 ? 6.849 -29.782 26.598 1.00 56.45 ? 229 LEU A O 1 ATOM 1581 C CB . LEU A 1 229 ? 4.210 -30.738 27.842 1.00 52.00 ? 229 LEU A CB 1 ATOM 1582 C CG . LEU A 1 229 ? 3.772 -29.832 28.987 1.00 53.88 ? 229 LEU A CG 1 ATOM 1583 C CD1 . LEU A 1 229 ? 2.487 -29.110 28.665 1.00 52.25 ? 229 LEU A CD1 1 ATOM 1584 C CD2 . LEU A 1 229 ? 3.607 -30.670 30.230 1.00 63.39 ? 229 LEU A CD2 1 ATOM 1585 N N . ARG A 1 230 ? 5.555 -27.964 26.319 1.00 46.29 ? 230 ARG A N 1 ATOM 1586 C CA . ARG A 1 230 ? 6.681 -27.050 26.097 1.00 63.50 ? 230 ARG A CA 1 ATOM 1587 C C . ARG A 1 230 ? 6.870 -25.917 27.126 1.00 73.81 ? 230 ARG A C 1 ATOM 1588 O O . ARG A 1 230 ? 5.919 -25.201 27.475 1.00 71.20 ? 230 ARG A O 1 ATOM 1589 C CB . ARG A 1 230 ? 6.564 -26.423 24.706 1.00 57.64 ? 230 ARG A CB 1 ATOM 1590 C CG . ARG A 1 230 ? 7.098 -27.262 23.583 1.00 51.36 ? 230 ARG A CG 1 ATOM 1591 C CD . ARG A 1 230 ? 6.851 -26.569 22.267 1.00 69.16 ? 230 ARG A CD 1 ATOM 1592 N NE . ARG A 1 230 ? 7.655 -27.155 21.212 1.00 74.75 ? 230 ARG A NE 1 ATOM 1593 C CZ . ARG A 1 230 ? 8.906 -26.799 20.987 1.00 87.64 ? 230 ARG A CZ 1 ATOM 1594 N NH1 . ARG A 1 230 ? 9.459 -25.860 21.747 1.00 81.32 ? 230 ARG A NH1 1 ATOM 1595 N NH2 . ARG A 1 230 ? 9.595 -27.378 20.014 1.00 99.69 ? 230 ARG A NH2 1 ATOM 1596 N N . ASP A 1 231 ? 8.115 -25.750 27.577 1.00 69.33 ? 231 ASP A N 1 ATOM 1597 C CA . ASP A 1 231 ? 8.521 -24.588 28.373 1.00 62.90 ? 231 ASP A CA 1 ATOM 1598 C C . ASP A 1 231 ? 7.848 -24.474 29.738 1.00 66.77 ? 231 ASP A C 1 ATOM 1599 O O . ASP A 1 231 ? 7.639 -23.369 30.248 1.00 55.54 ? 231 ASP A O 1 ATOM 1600 C CB . ASP A 1 231 ? 8.272 -23.307 27.591 1.00 66.80 ? 231 ASP A CB 1 ATOM 1601 C CG . ASP A 1 231 ? 9.135 -23.206 26.362 1.00 72.81 ? 231 ASP A CG 1 ATOM 1602 O OD1 . ASP A 1 231 ? 10.313 -23.626 26.420 1.00 55.18 ? 231 ASP A OD1 1 ATOM 1603 O OD2 . ASP A 1 231 ? 8.622 -22.698 25.341 1.00 89.09 ? 231 ASP A OD2 1 ATOM 1604 N N . THR A 1 232 ? 7.541 -25.616 30.339 1.00 69.80 ? 232 THR A N 1 ATOM 1605 C CA . THR A 1 232 ? 6.789 -25.638 31.583 1.00 66.60 ? 232 THR A CA 1 ATOM 1606 C C . THR A 1 232 ? 7.660 -25.722 32.847 1.00 72.76 ? 232 THR A C 1 ATOM 1607 O O . THR A 1 232 ? 8.582 -26.546 32.932 1.00 67.50 ? 232 THR A O 1 ATOM 1608 C CB . THR A 1 232 ? 5.822 -26.824 31.590 1.00 60.50 ? 232 THR A CB 1 ATOM 1609 O OG1 . THR A 1 232 ? 5.453 -27.156 30.238 1.00 54.46 ? 232 THR A OG1 1 ATOM 1610 C CG2 . THR A 1 232 ? 4.596 -26.500 32.440 1.00 48.17 ? 232 THR A CG2 1 ATOM 1611 N N . ASN A 1 233 ? 7.365 -24.867 33.827 1.00 66.96 ? 233 ASN A N 1 ATOM 1612 C CA . ASN A 1 233 ? 7.895 -25.070 35.165 1.00 63.60 ? 233 ASN A CA 1 ATOM 1613 C C . ASN A 1 233 ? 7.065 -26.126 35.897 1.00 66.86 ? 233 ASN A C 1 ATOM 1614 O O . ASN A 1 233 ? 5.930 -25.882 36.328 1.00 66.78 ? 233 ASN A O 1 ATOM 1615 C CB . ASN A 1 233 ? 7.954 -23.767 35.955 1.00 69.89 ? 233 ASN A CB 1 ATOM 1616 C CG . ASN A 1 233 ? 8.923 -23.842 37.138 1.00 73.56 ? 233 ASN A CG 1 ATOM 1617 O OD1 . ASN A 1 233 ? 9.115 -22.863 37.863 1.00 72.15 ? 233 ASN A OD1 1 ATOM 1618 N ND2 . ASN A 1 233 ? 9.540 -25.004 37.328 1.00 73.12 ? 233 ASN A ND2 1 ATOM 1619 N N . LEU A 1 234 ? 7.648 -27.313 36.008 1.00 66.15 ? 234 LEU A N 1 ATOM 1620 C CA . LEU A 1 234 ? 7.002 -28.456 36.635 1.00 68.80 ? 234 LEU A CA 1 ATOM 1621 C C . LEU A 1 234 ? 7.553 -28.647 38.057 1.00 69.91 ? 234 LEU A C 1 ATOM 1622 O O . LEU A 1 234 ? 7.231 -29.615 38.755 1.00 66.50 ? 234 LEU A O 1 ATOM 1623 C CB . LEU A 1 234 ? 7.203 -29.704 35.762 1.00 59.64 ? 234 LEU A CB 1 ATOM 1624 C CG . LEU A 1 234 ? 6.389 -29.656 34.461 1.00 53.62 ? 234 LEU A CG 1 ATOM 1625 C CD1 . LEU A 1 234 ? 6.877 -30.615 33.380 1.00 32.51 ? 234 LEU A CD1 1 ATOM 1626 C CD2 . LEU A 1 234 ? 4.945 -29.928 34.800 1.00 61.18 ? 234 LEU A CD2 1 ATOM 1627 N N . ALA A 1 235 ? 8.354 -27.677 38.485 1.00 67.46 ? 235 ALA A N 1 ATOM 1628 C CA . ALA A 1 235 ? 9.065 -27.740 39.754 1.00 74.35 ? 235 ALA A CA 1 ATOM 1629 C C . ALA A 1 235 ? 8.198 -28.228 40.903 1.00 79.23 ? 235 ALA A C 1 ATOM 1630 O O . ALA A 1 235 ? 8.600 -29.118 41.654 1.00 91.55 ? 235 ALA A O 1 ATOM 1631 C CB . ALA A 1 235 ? 9.683 -26.387 40.085 1.00 79.04 ? 235 ALA A CB 1 ATOM 1632 N N . ARG A 1 236 ? 7.017 -27.648 41.059 1.00 72.33 ? 236 ARG A N 1 ATOM 1633 C CA . ARG A 1 236 ? 6.162 -28.054 42.167 1.00 86.19 ? 236 ARG A CA 1 ATOM 1634 C C . ARG A 1 236 ? 4.856 -28.621 41.642 1.00 81.50 ? 236 ARG A C 1 ATOM 1635 O O . ARG A 1 236 ? 3.776 -28.187 42.031 1.00 82.73 ? 236 ARG A O 1 ATOM 1636 C CB . ARG A 1 236 ? 5.928 -26.895 43.160 1.00 98.81 ? 236 ARG A CB 1 ATOM 1637 C CG . ARG A 1 236 ? 6.911 -26.836 44.371 1.00 89.64 ? 236 ARG A CG 1 ATOM 1638 C CD . ARG A 1 236 ? 6.337 -27.502 45.630 1.00 93.20 ? 236 ARG A CD 1 ATOM 1639 N NE . ARG A 1 236 ? 4.952 -27.079 45.871 1.00 106.71 ? 236 ARG A NE 1 ATOM 1640 C CZ . ARG A 1 236 ? 4.553 -26.249 46.837 1.00 105.28 ? 236 ARG A CZ 1 ATOM 1641 N NH1 . ARG A 1 236 ? 5.436 -25.752 47.701 1.00 111.06 ? 236 ARG A NH1 1 ATOM 1642 N NH2 . ARG A 1 236 ? 3.262 -25.926 46.948 1.00 86.07 ? 236 ARG A NH2 1 ATOM 1643 N N . PHE A 1 237 ? 4.970 -29.600 40.751 1.00 80.71 ? 237 PHE A N 1 ATOM 1644 C CA . PHE A 1 237 ? 3.797 -30.241 40.167 1.00 81.29 ? 237 PHE A CA 1 ATOM 1645 C C . PHE A 1 237 ? 3.279 -31.363 41.051 1.00 78.66 ? 237 PHE A C 1 ATOM 1646 O O . PHE A 1 237 ? 4.000 -32.319 41.339 1.00 75.50 ? 237 PHE A O 1 ATOM 1647 C CB . PHE A 1 237 ? 4.102 -30.796 38.773 1.00 76.82 ? 237 PHE A CB 1 ATOM 1648 C CG . PHE A 1 237 ? 3.035 -31.722 38.248 1.00 78.16 ? 237 PHE A CG 1 ATOM 1649 C CD1 . PHE A 1 237 ? 1.876 -31.213 37.670 1.00 75.96 ? 237 PHE A CD1 1 ATOM 1650 C CD2 . PHE A 1 237 ? 3.183 -33.102 38.341 1.00 75.65 ? 237 PHE A CD2 1 ATOM 1651 C CE1 . PHE A 1 237 ? 0.883 -32.062 37.188 1.00 74.63 ? 237 PHE A CE1 1 ATOM 1652 C CE2 . PHE A 1 237 ? 2.192 -33.956 37.863 1.00 76.10 ? 237 PHE A CE2 1 ATOM 1653 C CZ . PHE A 1 237 ? 1.041 -33.433 37.285 1.00 73.57 ? 237 PHE A CZ 1 ATOM 1654 N N . GLN A 1 238 ? 2.021 -31.246 41.460 1.00 75.88 ? 238 GLN A N 1 ATOM 1655 C CA . GLN A 1 238 ? 1.391 -32.251 42.302 1.00 86.13 ? 238 GLN A CA 1 ATOM 1656 C C . GLN A 1 238 ? 0.336 -33.035 41.509 1.00 79.47 ? 238 GLN A C 1 ATOM 1657 O O . GLN A 1 238 ? -0.553 -32.452 40.882 1.00 75.63 ? 238 GLN A O 1 ATOM 1658 C CB . GLN A 1 238 ? 0.750 -31.593 43.541 1.00 95.96 ? 238 GLN A CB 1 ATOM 1659 C CG . GLN A 1 238 ? 1.056 -32.283 44.870 1.00 96.26 ? 238 GLN A CG 1 ATOM 1660 C CD . GLN A 1 238 ? 2.352 -31.777 45.476 1.00 109.87 ? 238 GLN A CD 1 ATOM 1661 O OE1 . GLN A 1 238 ? 3.262 -32.553 45.795 1.00 110.86 ? 238 GLN A OE1 1 ATOM 1662 N NE2 . GLN A 1 238 ? 2.451 -30.459 45.619 1.00 114.06 ? 238 GLN A NE2 1 ATOM 1663 N N . PHE A 1 239 ? 0.442 -34.359 41.539 1.00 77.90 ? 239 PHE A N 1 ATOM 1664 C CA . PHE A 1 239 ? -0.579 -35.215 40.960 1.00 79.85 ? 239 PHE A CA 1 ATOM 1665 C C . PHE A 1 239 ? -1.695 -35.455 41.969 1.00 83.83 ? 239 PHE A C 1 ATOM 1666 O O . PHE A 1 239 ? -1.520 -35.248 43.170 1.00 86.62 ? 239 PHE A O 1 ATOM 1667 C CB . PHE A 1 239 ? 0.023 -36.552 40.520 1.00 76.00 ? 239 PHE A CB 1 ATOM 1668 C CG . PHE A 1 239 ? -0.995 -37.545 40.022 1.00 72.16 ? 239 PHE A CG 1 ATOM 1669 C CD1 . PHE A 1 239 ? -1.339 -37.594 38.678 1.00 74.66 ? 239 PHE A CD1 1 ATOM 1670 C CD2 . PHE A 1 239 ? -1.607 -38.431 40.898 1.00 60.14 ? 239 PHE A CD2 1 ATOM 1671 C CE1 . PHE A 1 239 ? -2.270 -38.512 38.220 1.00 70.33 ? 239 PHE A CE1 1 ATOM 1672 C CE2 . PHE A 1 239 ? -2.539 -39.344 40.452 1.00 54.30 ? 239 PHE A CE2 1 ATOM 1673 C CZ . PHE A 1 239 ? -2.869 -39.389 39.112 1.00 69.79 ? 239 PHE A CZ 1 ATOM 1674 N N . SER A 1 240 ? -2.845 -35.885 41.464 1.00 79.82 ? 240 SER A N 1 ATOM 1675 C CA . SER A 1 240 ? -3.957 -36.322 42.293 1.00 76.28 ? 240 SER A CA 1 ATOM 1676 C C . SER A 1 240 ? -4.990 -36.914 41.350 1.00 71.08 ? 240 SER A C 1 ATOM 1677 O O . SER A 1 240 ? -5.167 -36.415 40.249 1.00 58.94 ? 240 SER A O 1 ATOM 1678 C CB . SER A 1 240 ? -4.535 -35.160 43.109 1.00 76.95 ? 240 SER A CB 1 ATOM 1679 O OG . SER A 1 240 ? -5.102 -34.165 42.278 1.00 82.73 ? 240 SER A OG 1 ATOM 1680 N N . PRO A 1 241 ? -5.670 -37.989 41.775 1.00 82.12 ? 241 PRO A N 1 ATOM 1681 C CA . PRO A 1 241 ? -6.581 -38.750 40.904 1.00 79.99 ? 241 PRO A CA 1 ATOM 1682 C C . PRO A 1 241 ? -7.556 -37.878 40.116 1.00 76.95 ? 241 PRO A C 1 ATOM 1683 O O . PRO A 1 241 ? -8.054 -36.868 40.602 1.00 70.45 ? 241 PRO A O 1 ATOM 1684 C CB . PRO A 1 241 ? -7.340 -39.640 41.886 1.00 83.35 ? 241 PRO A CB 1 ATOM 1685 C CG . PRO A 1 241 ? -6.410 -39.803 43.025 1.00 82.50 ? 241 PRO A CG 1 ATOM 1686 C CD . PRO A 1 241 ? -5.668 -38.506 43.153 1.00 77.82 ? 241 PRO A CD 1 ATOM 1687 N N . LEU A 1 242 ? -7.823 -38.284 38.885 1.00 93.35 ? 242 LEU A N 1 ATOM 1688 C CA . LEU A 1 242 ? -8.641 -37.487 37.986 1.00 101.32 ? 242 LEU A CA 1 ATOM 1689 C C . LEU A 1 242 ? -10.103 -37.863 38.123 1.00 121.31 ? 242 LEU A C 1 ATOM 1690 O O . LEU A 1 242 ? -10.427 -39.029 38.354 1.00 126.84 ? 242 LEU A O 1 ATOM 1691 C CB . LEU A 1 242 ? -8.186 -37.692 36.541 1.00 84.72 ? 242 LEU A CB 1 ATOM 1692 C CG . LEU A 1 242 ? -6.676 -37.571 36.361 1.00 75.88 ? 242 LEU A CG 1 ATOM 1693 C CD1 . LEU A 1 242 ? -6.286 -37.954 34.961 1.00 78.10 ? 242 LEU A CD1 1 ATOM 1694 C CD2 . LEU A 1 242 ? -6.221 -36.157 36.688 1.00 70.26 ? 242 LEU A CD2 1 ATOM 1695 N N . PRO A 1 243 ? -10.991 -36.868 37.993 1.00 130.22 ? 243 PRO A N 1 ATOM 1696 C CA . PRO A 1 243 ? -12.434 -37.120 37.949 1.00 138.38 ? 243 PRO A CA 1 ATOM 1697 C C . PRO A 1 243 ? -12.799 -38.135 36.859 1.00 146.07 ? 243 PRO A C 1 ATOM 1698 O O . PRO A 1 243 ? -13.612 -39.028 37.113 1.00 153.76 ? 243 PRO A O 1 ATOM 1699 C CB . PRO A 1 243 ? -13.010 -35.743 37.611 1.00 131.68 ? 243 PRO A CB 1 ATOM 1700 C CG . PRO A 1 243 ? -12.011 -34.779 38.155 1.00 125.96 ? 243 PRO A CG 1 ATOM 1701 C CD . PRO A 1 243 ? -10.674 -35.428 37.970 1.00 124.31 ? 243 PRO A CD 1 ATOM 1702 N N . VAL A 1 244 ? -12.185 -38.003 35.682 1.00 140.08 ? 244 VAL A N 1 ATOM 1703 C CA . VAL A 1 244 ? -12.524 -38.796 34.492 1.00 136.09 ? 244 VAL A CA 1 ATOM 1704 C C . VAL A 1 244 ? -12.860 -40.270 34.745 1.00 133.82 ? 244 VAL A C 1 ATOM 1705 O O . VAL A 1 244 ? -12.403 -40.873 35.723 1.00 130.51 ? 244 VAL A O 1 ATOM 1706 C CB . VAL A 1 244 ? -11.392 -38.754 33.434 1.00 128.55 ? 244 VAL A CB 1 ATOM 1707 C CG1 . VAL A 1 244 ? -11.161 -37.330 32.927 1.00 115.33 ? 244 VAL A CG1 1 ATOM 1708 C CG2 . VAL A 1 244 ? -10.117 -39.360 34.008 1.00 131.69 ? 244 VAL A CG2 1 ATOM 1709 N N . ASP A 1 245 ? -13.651 -40.838 33.833 1.00 128.64 ? 245 ASP A N 1 ATOM 1710 C CA . ASP A 1 245 ? -14.033 -42.248 33.878 1.00 125.14 ? 245 ASP A CA 1 ATOM 1711 C C . ASP A 1 245 ? -12.978 -43.111 33.191 1.00 115.13 ? 245 ASP A C 1 ATOM 1712 O O . ASP A 1 245 ? -12.128 -42.599 32.465 1.00 111.83 ? 245 ASP A O 1 ATOM 1713 C CB . ASP A 1 245 ? -15.392 -42.460 33.204 1.00 132.30 ? 245 ASP A CB 1 ATOM 1714 C CG . ASP A 1 245 ? -16.472 -41.534 33.744 1.00 142.06 ? 245 ASP A CG 1 ATOM 1715 O OD1 . ASP A 1 245 ? -16.140 -40.399 34.147 1.00 143.15 ? 245 ASP A OD1 1 ATOM 1716 O OD2 . ASP A 1 245 ? -17.656 -41.939 33.754 1.00 145.59 ? 245 ASP A OD2 1 ATOM 1717 N N . GLU A 1 246 ? -13.032 -44.419 33.427 1.00 116.93 ? 246 GLU A N 1 ATOM 1718 C CA . GLU A 1 246 ? -12.084 -45.351 32.823 1.00 121.74 ? 246 GLU A CA 1 ATOM 1719 C C . GLU A 1 246 ? -12.142 -45.282 31.303 1.00 122.30 ? 246 GLU A C 1 ATOM 1720 O O . GLU A 1 246 ? -12.859 -46.056 30.661 1.00 120.47 ? 246 GLU A O 1 ATOM 1721 C CB . GLU A 1 246 ? -12.381 -46.786 33.259 1.00 136.88 ? 246 GLU A CB 1 ATOM 1722 C CG . GLU A 1 246 ? -12.200 -47.069 34.739 1.00 150.62 ? 246 GLU A CG 1 ATOM 1723 C CD . GLU A 1 246 ? -12.922 -48.337 35.174 1.00 159.29 ? 246 GLU A CD 1 ATOM 1724 O OE1 . GLU A 1 246 ? -14.130 -48.467 34.866 1.00 157.84 ? 246 GLU A OE1 1 ATOM 1725 O OE2 . GLU A 1 246 ? -12.285 -49.197 35.826 1.00 162.37 ? 246 GLU A OE2 1 ATOM 1726 N N . VAL A 1 247 ? -11.384 -44.358 30.725 1.00 121.49 ? 247 VAL A N 1 ATOM 1727 C CA . VAL A 1 247 ? -11.305 -44.246 29.275 1.00 111.59 ? 247 VAL A CA 1 ATOM 1728 C C . VAL A 1 247 ? -9.924 -44.686 28.772 1.00 103.37 ? 247 VAL A C 1 ATOM 1729 O O . VAL A 1 247 ? -8.892 -44.209 29.260 1.00 107.64 ? 247 VAL A O 1 ATOM 1730 C CB . VAL A 1 247 ? -11.658 -42.815 28.807 1.00 106.08 ? 247 VAL A CB 1 ATOM 1731 C CG1 . VAL A 1 247 ? -11.125 -42.557 27.413 1.00 111.55 ? 247 VAL A CG1 1 ATOM 1732 C CG2 . VAL A 1 247 ? -13.170 -42.606 28.847 1.00 99.31 ? 247 VAL A CG2 1 ATOM 1733 N N . SER A 1 248 ? -9.915 -45.622 27.821 1.00 89.54 ? 248 SER A N 1 ATOM 1734 C CA . SER A 1 248 ? -8.675 -46.110 27.214 1.00 88.74 ? 248 SER A CA 1 ATOM 1735 C C . SER A 1 248 ? -8.023 -45.045 26.313 1.00 84.94 ? 248 SER A C 1 ATOM 1736 O O . SER A 1 248 ? -8.596 -44.642 25.298 1.00 86.89 ? 248 SER A O 1 ATOM 1737 C CB . SER A 1 248 ? -8.948 -47.395 26.421 1.00 85.35 ? 248 SER A CB 1 ATOM 1738 O OG . SER A 1 248 ? -7.752 -47.933 25.880 1.00 80.28 ? 248 SER A OG 1 ATOM 1739 N N . SER A 1 249 ? -6.828 -44.592 26.682 1.00 65.76 ? 249 SER A N 1 ATOM 1740 C CA . SER A 1 249 ? -6.189 -43.489 25.970 1.00 61.31 ? 249 SER A CA 1 ATOM 1741 C C . SER A 1 249 ? -5.403 -43.912 24.744 1.00 73.86 ? 249 SER A C 1 ATOM 1742 O O . SER A 1 249 ? -4.621 -44.855 24.795 1.00 85.35 ? 249 SER A O 1 ATOM 1743 C CB . SER A 1 249 ? -5.254 -42.697 26.878 1.00 63.54 ? 249 SER A CB 1 ATOM 1744 O OG . SER A 1 249 ? -4.388 -41.889 26.098 1.00 63.76 ? 249 SER A OG 1 ATOM 1745 N N . PRO A 1 250 ? -5.590 -43.170 23.648 1.00 73.03 ? 250 PRO A N 1 ATOM 1746 C CA . PRO A 1 250 ? -4.915 -43.251 22.352 1.00 63.15 ? 250 PRO A CA 1 ATOM 1747 C C . PRO A 1 250 ? -3.447 -42.818 22.416 1.00 69.97 ? 250 PRO A C 1 ATOM 1748 O O . PRO A 1 250 ? -2.680 -43.127 21.503 1.00 65.41 ? 250 PRO A O 1 ATOM 1749 C CB . PRO A 1 250 ? -5.673 -42.225 21.508 1.00 47.89 ? 250 PRO A CB 1 ATOM 1750 C CG . PRO A 1 250 ? -6.907 -41.904 22.267 1.00 54.64 ? 250 PRO A CG 1 ATOM 1751 C CD . PRO A 1 250 ? -6.574 -42.078 23.679 1.00 71.55 ? 250 PRO A CD 1 ATOM 1752 N N . MET A 1 251 ? -3.068 -42.099 23.469 1.00 67.20 ? 251 MET A N 1 ATOM 1753 C CA . MET A 1 251 ? -1.757 -41.471 23.520 1.00 60.35 ? 251 MET A CA 1 ATOM 1754 C C . MET A 1 251 ? -0.645 -42.501 23.449 1.00 63.99 ? 251 MET A C 1 ATOM 1755 O O . MET A 1 251 ? -0.634 -43.456 24.214 1.00 72.59 ? 251 MET A O 1 ATOM 1756 C CB . MET A 1 251 ? -1.634 -40.641 24.787 1.00 61.38 ? 251 MET A CB 1 ATOM 1757 C CG . MET A 1 251 ? -0.313 -39.940 24.942 1.00 59.27 ? 251 MET A CG 1 ATOM 1758 S SD . MET A 1 251 ? -0.477 -38.640 26.166 1.00 59.95 ? 251 MET A SD 1 ATOM 1759 C CE . MET A 1 251 ? -1.798 -37.657 25.465 1.00 115.95 ? 251 MET A CE 1 ATOM 1760 N N . LYS A 1 252 ? 0.283 -42.310 22.520 1.00 61.54 ? 252 LYS A N 1 ATOM 1761 C CA . LYS A 1 252 ? 1.384 -43.248 22.338 1.00 60.48 ? 252 LYS A CA 1 ATOM 1762 C C . LYS A 1 252 ? 2.735 -42.579 22.582 1.00 61.96 ? 252 LYS A C 1 ATOM 1763 O O . LYS A 1 252 ? 3.725 -43.255 22.836 1.00 64.37 ? 252 LYS A O 1 ATOM 1764 C CB . LYS A 1 252 ? 1.356 -43.855 20.932 1.00 52.25 ? 252 LYS A CB 1 ATOM 1765 C CG . LYS A 1 252 ? 0.046 -44.537 20.553 1.00 56.23 ? 252 LYS A CG 1 ATOM 1766 C CD . LYS A 1 252 ? -0.085 -45.938 21.124 1.00 61.90 ? 252 LYS A CD 1 ATOM 1767 C CE . LYS A 1 252 ? 0.509 -46.996 20.205 1.00 70.18 ? 252 LYS A CE 1 ATOM 1768 N NZ . LYS A 1 252 ? 1.027 -48.155 21.012 1.00 85.05 ? 252 LYS A NZ 1 ATOM 1769 N N . LYS A 1 253 ? 2.775 -41.253 22.491 1.00 58.73 ? 253 LYS A N 1 ATOM 1770 C CA . LYS A 1 253 ? 4.005 -40.504 22.730 1.00 57.58 ? 253 LYS A CA 1 ATOM 1771 C C . LYS A 1 253 ? 3.763 -39.363 23.712 1.00 68.99 ? 253 LYS A C 1 ATOM 1772 O O . LYS A 1 253 ? 2.719 -38.704 23.667 1.00 68.28 ? 253 LYS A O 1 ATOM 1773 C CB . LYS A 1 253 ? 4.568 -39.927 21.428 1.00 49.63 ? 253 LYS A CB 1 ATOM 1774 C CG . LYS A 1 253 ? 6.086 -39.745 21.410 1.00 47.44 ? 253 LYS A CG 1 ATOM 1775 C CD . LYS A 1 253 ? 6.526 -38.687 20.397 1.00 51.95 ? 253 LYS A CD 1 ATOM 1776 C CE . LYS A 1 253 ? 7.924 -38.961 19.826 1.00 61.24 ? 253 LYS A CE 1 ATOM 1777 N NZ . LYS A 1 253 ? 8.688 -37.708 19.528 1.00 67.69 ? 253 LYS A NZ 1 ATOM 1778 N N . LEU A 1 254 ? 4.741 -39.145 24.589 1.00 65.86 ? 254 LEU A N 1 ATOM 1779 C CA . LEU A 1 254 ? 4.743 -38.032 25.527 1.00 61.87 ? 254 LEU A CA 1 ATOM 1780 C C . LEU A 1 254 ? 6.118 -37.399 25.492 1.00 67.76 ? 254 LEU A C 1 ATOM 1781 O O . LEU A 1 254 ? 7.131 -38.088 25.595 1.00 72.40 ? 254 LEU A O 1 ATOM 1782 C CB . LEU A 1 254 ? 4.438 -38.519 26.940 1.00 60.07 ? 254 LEU A CB 1 ATOM 1783 C CG . LEU A 1 254 ? 4.313 -37.481 28.052 1.00 51.17 ? 254 LEU A CG 1 ATOM 1784 C CD1 . LEU A 1 254 ? 3.139 -36.598 27.778 1.00 40.26 ? 254 LEU A CD1 1 ATOM 1785 C CD2 . LEU A 1 254 ? 4.145 -38.189 29.390 1.00 51.63 ? 254 LEU A CD2 1 ATOM 1786 N N . ALA A 1 255 ? 6.155 -36.084 25.337 1.00 67.09 ? 255 ALA A N 1 ATOM 1787 C CA . ALA A 1 255 ? 7.422 -35.384 25.203 1.00 54.05 ? 255 ALA A CA 1 ATOM 1788 C C . ALA A 1 255 ? 7.430 -34.071 25.978 1.00 56.20 ? 255 ALA A C 1 ATOM 1789 O O . ALA A 1 255 ? 6.471 -33.298 25.943 1.00 47.14 ? 255 ALA A O 1 ATOM 1790 C CB . ALA A 1 255 ? 7.742 -35.150 23.743 1.00 35.23 ? 255 ALA A CB 1 ATOM 1791 N N . PHE A 1 256 ? 8.522 -33.837 26.695 1.00 60.79 ? 256 PHE A N 1 ATOM 1792 C CA . PHE A 1 256 ? 8.696 -32.607 27.445 1.00 62.36 ? 256 PHE A CA 1 ATOM 1793 C C . PHE A 1 256 ? 9.835 -31.844 26.791 1.00 64.90 ? 256 PHE A C 1 ATOM 1794 O O . PHE A 1 256 ? 10.947 -32.368 26.682 1.00 64.33 ? 256 PHE A O 1 ATOM 1795 C CB . PHE A 1 256 ? 9.012 -32.924 28.909 1.00 54.07 ? 256 PHE A CB 1 ATOM 1796 C CG . PHE A 1 256 ? 7.887 -33.611 29.636 1.00 52.74 ? 256 PHE A CG 1 ATOM 1797 C CD1 . PHE A 1 256 ? 7.792 -34.992 29.650 1.00 53.69 ? 256 PHE A CD1 1 ATOM 1798 C CD2 . PHE A 1 256 ? 6.919 -32.874 30.306 1.00 57.55 ? 256 PHE A CD2 1 ATOM 1799 C CE1 . PHE A 1 256 ? 6.749 -35.631 30.318 1.00 56.67 ? 256 PHE A CE1 1 ATOM 1800 C CE2 . PHE A 1 256 ? 5.876 -33.508 30.979 1.00 58.30 ? 256 PHE A CE2 1 ATOM 1801 C CZ . PHE A 1 256 ? 5.792 -34.889 30.982 1.00 55.28 ? 256 PHE A CZ 1 ATOM 1802 N N . ARG A 1 257 ? 9.569 -30.619 26.339 1.00 57.47 ? 257 ARG A N 1 ATOM 1803 C CA . ARG A 1 257 ? 10.592 -29.903 25.592 1.00 67.27 ? 257 ARG A CA 1 ATOM 1804 C C . ARG A 1 257 ? 11.525 -29.107 26.474 1.00 79.11 ? 257 ARG A C 1 ATOM 1805 O O . ARG A 1 257 ? 12.653 -29.549 26.728 1.00 89.12 ? 257 ARG A O 1 ATOM 1806 C CB . ARG A 1 257 ? 10.008 -29.020 24.503 1.00 78.26 ? 257 ARG A CB 1 ATOM 1807 C CG . ARG A 1 257 ? 9.709 -29.762 23.199 1.00 83.61 ? 257 ARG A CG 1 ATOM 1808 C CD . ARG A 1 257 ? 10.938 -30.236 22.411 1.00 78.57 ? 257 ARG A CD 1 ATOM 1809 N NE . ARG A 1 257 ? 10.499 -31.140 21.345 1.00 81.99 ? 257 ARG A NE 1 ATOM 1810 C CZ . ARG A 1 257 ? 10.253 -32.438 21.530 1.00 86.38 ? 257 ARG A CZ 1 ATOM 1811 N NH1 . ARG A 1 257 ? 10.441 -32.979 22.725 1.00 106.96 ? 257 ARG A NH1 1 ATOM 1812 N NH2 . ARG A 1 257 ? 9.826 -33.206 20.536 1.00 59.27 ? 257 ARG A NH2 1 ATOM 1813 N N . GLY A 1 258 ? 11.077 -27.939 26.932 1.00 62.55 ? 258 GLY A N 1 ATOM 1814 C CA . GLY A 1 258 ? 11.959 -27.066 27.702 1.00 58.09 ? 258 GLY A CA 1 ATOM 1815 C C . GLY A 1 258 ? 11.596 -26.931 29.167 1.00 67.46 ? 258 GLY A C 1 ATOM 1816 O O . GLY A 1 258 ? 11.583 -25.824 29.711 1.00 77.50 ? 258 GLY A O 1 ATOM 1817 N N . SER A 1 259 ? 11.316 -28.064 29.807 1.00 71.36 ? 259 SER A N 1 ATOM 1818 C CA . SER A 1 259 ? 10.753 -28.091 31.155 1.00 72.61 ? 259 SER A CA 1 ATOM 1819 C C . SER A 1 259 ? 11.800 -27.899 32.232 1.00 72.19 ? 259 SER A C 1 ATOM 1820 O O . SER A 1 259 ? 12.958 -28.285 32.063 1.00 73.15 ? 259 SER A O 1 ATOM 1821 C CB . SER A 1 259 ? 10.048 -29.426 31.402 1.00 65.03 ? 259 SER A CB 1 ATOM 1822 O OG . SER A 1 259 ? 9.220 -29.761 30.309 1.00 66.50 ? 259 SER A OG 1 ATOM 1823 N N . VAL A 1 260 ? 11.391 -27.305 33.347 1.00 63.33 ? 260 VAL A N 1 ATOM 1824 C CA . VAL A 1 260 ? 12.205 -27.401 34.547 1.00 65.74 ? 260 VAL A CA 1 ATOM 1825 C C . VAL A 1 260 ? 11.592 -28.420 35.500 1.00 63.09 ? 260 VAL A C 1 ATOM 1826 O O . VAL A 1 260 ? 10.424 -28.338 35.854 1.00 72.79 ? 260 VAL A O 1 ATOM 1827 C CB . VAL A 1 260 ? 12.419 -26.057 35.233 1.00 60.06 ? 260 VAL A CB 1 ATOM 1828 C CG1 . VAL A 1 260 ? 13.433 -26.216 36.344 1.00 63.58 ? 260 VAL A CG1 1 ATOM 1829 C CG2 . VAL A 1 260 ? 12.924 -25.058 34.236 1.00 53.69 ? 260 VAL A CG2 1 ATOM 1830 N N . LEU A 1 261 ? 12.389 -29.398 35.892 1.00 56.12 ? 261 LEU A N 1 ATOM 1831 C CA . LEU A 1 261 ? 11.890 -30.494 36.697 1.00 65.37 ? 261 LEU A CA 1 ATOM 1832 C C . LEU A 1 261 ? 12.682 -30.587 37.995 1.00 70.24 ? 261 LEU A C 1 ATOM 1833 O O . LEU A 1 261 ? 13.830 -30.157 38.071 1.00 67.55 ? 261 LEU A O 1 ATOM 1834 C CB . LEU A 1 261 ? 12.003 -31.799 35.904 1.00 65.59 ? 261 LEU A CB 1 ATOM 1835 C CG . LEU A 1 261 ? 11.305 -31.769 34.541 1.00 67.51 ? 261 LEU A CG 1 ATOM 1836 C CD1 . LEU A 1 261 ? 12.163 -32.369 33.442 1.00 56.55 ? 261 LEU A CD1 1 ATOM 1837 C CD2 . LEU A 1 261 ? 9.955 -32.461 34.616 1.00 76.62 ? 261 LEU A CD2 1 ATOM 1838 N N . THR A 1 262 ? 12.060 -31.131 39.028 1.00 72.65 ? 262 THR A N 1 ATOM 1839 C CA . THR A 1 262 ? 12.776 -31.414 40.259 1.00 72.08 ? 262 THR A CA 1 ATOM 1840 C C . THR A 1 262 ? 12.595 -32.888 40.538 1.00 74.06 ? 262 THR A C 1 ATOM 1841 O O . THR A 1 262 ? 11.732 -33.532 39.935 1.00 68.68 ? 262 THR A O 1 ATOM 1842 C CB . THR A 1 262 ? 12.253 -30.581 41.445 1.00 64.87 ? 262 THR A CB 1 ATOM 1843 O OG1 . THR A 1 262 ? 10.836 -30.746 41.564 1.00 49.94 ? 262 THR A OG1 1 ATOM 1844 C CG2 . THR A 1 262 ? 12.573 -29.105 41.248 1.00 63.44 ? 262 THR A CG2 1 ATOM 1845 N N . ASP A 1 263 ? 13.408 -33.428 41.437 1.00 70.93 ? 263 ASP A N 1 ATOM 1846 C CA . ASP A 1 263 ? 13.297 -34.835 41.775 1.00 60.89 ? 263 ASP A CA 1 ATOM 1847 C C . ASP A 1 263 ? 11.871 -35.192 42.183 1.00 56.73 ? 263 ASP A C 1 ATOM 1848 O O . ASP A 1 263 ? 11.425 -36.305 41.961 1.00 66.48 ? 263 ASP A O 1 ATOM 1849 C CB . ASP A 1 263 ? 14.304 -35.200 42.856 1.00 73.77 ? 263 ASP A CB 1 ATOM 1850 C CG . ASP A 1 263 ? 15.694 -35.399 42.300 1.00 80.78 ? 263 ASP A CG 1 ATOM 1851 O OD1 . ASP A 1 263 ? 16.684 -35.280 43.061 1.00 82.31 ? 263 ASP A OD1 1 ATOM 1852 O OD2 . ASP A 1 263 ? 15.785 -35.683 41.090 1.00 81.08 ? 263 ASP A OD2 1 ATOM 1853 N N . GLU A 1 264 ? 11.147 -34.233 42.748 1.00 60.37 ? 264 GLU A N 1 ATOM 1854 C CA . GLU A 1 264 ? 9.743 -34.430 43.113 1.00 73.28 ? 264 GLU A CA 1 ATOM 1855 C C . GLU A 1 264 ? 8.844 -34.611 41.904 1.00 74.27 ? 264 GLU A C 1 ATOM 1856 O O . GLU A 1 264 ? 7.880 -35.373 41.930 1.00 75.41 ? 264 GLU A O 1 ATOM 1857 C CB . GLU A 1 264 ? 9.232 -33.245 43.933 1.00 86.81 ? 264 GLU A CB 1 ATOM 1858 C CG . GLU A 1 264 ? 9.584 -33.349 45.385 1.00 104.73 ? 264 GLU A CG 1 ATOM 1859 C CD . GLU A 1 264 ? 9.243 -34.716 45.935 1.00 120.68 ? 264 GLU A CD 1 ATOM 1860 O OE1 . GLU A 1 264 ? 8.219 -35.294 45.487 1.00 115.59 ? 264 GLU A OE1 1 ATOM 1861 O OE2 . GLU A 1 264 ? 10.000 -35.209 46.805 1.00 129.68 ? 264 GLU A OE2 1 ATOM 1862 N N . SER A 1 265 ? 9.162 -33.885 40.845 1.00 74.81 ? 265 SER A N 1 ATOM 1863 C CA . SER A 1 265 ? 8.344 -33.881 39.655 1.00 73.56 ? 265 SER A CA 1 ATOM 1864 C C . SER A 1 265 ? 8.273 -35.275 39.063 1.00 81.28 ? 265 SER A C 1 ATOM 1865 O O . SER A 1 265 ? 7.233 -35.676 38.558 1.00 97.04 ? 265 SER A O 1 ATOM 1866 C CB . SER A 1 265 ? 8.924 -32.907 38.642 1.00 73.25 ? 265 SER A CB 1 ATOM 1867 O OG . SER A 1 265 ? 9.336 -31.718 39.283 1.00 66.71 ? 265 SER A OG 1 ATOM 1868 N N . PHE A 1 266 ? 9.382 -36.006 39.119 1.00 76.11 ? 266 PHE A N 1 ATOM 1869 C CA . PHE A 1 266 ? 9.430 -37.370 38.607 1.00 70.39 ? 266 PHE A CA 1 ATOM 1870 C C . PHE A 1 266 ? 8.393 -38.214 39.321 1.00 70.58 ? 266 PHE A C 1 ATOM 1871 O O . PHE A 1 266 ? 7.681 -39.023 38.716 1.00 64.69 ? 266 PHE A O 1 ATOM 1872 C CB . PHE A 1 266 ? 10.813 -37.986 38.845 1.00 69.56 ? 266 PHE A CB 1 ATOM 1873 C CG . PHE A 1 266 ? 10.944 -39.395 38.336 1.00 78.32 ? 266 PHE A CG 1 ATOM 1874 C CD1 . PHE A 1 266 ? 11.643 -39.662 37.169 1.00 84.95 ? 266 PHE A CD1 1 ATOM 1875 C CD2 . PHE A 1 266 ? 10.351 -40.453 39.013 1.00 76.49 ? 266 PHE A CD2 1 ATOM 1876 C CE1 . PHE A 1 266 ? 11.756 -40.958 36.690 1.00 82.07 ? 266 PHE A CE1 1 ATOM 1877 C CE2 . PHE A 1 266 ? 10.454 -41.747 38.536 1.00 74.96 ? 266 PHE A CE2 1 ATOM 1878 C CZ . PHE A 1 266 ? 11.160 -41.999 37.378 1.00 77.93 ? 266 PHE A CZ 1 ATOM 1879 N N . ASN A 1 267 ? 8.321 -38.019 40.628 1.00 70.99 ? 267 ASN A N 1 ATOM 1880 C CA . ASN A 1 267 ? 7.477 -38.840 41.472 1.00 74.02 ? 267 ASN A CA 1 ATOM 1881 C C . ASN A 1 267 ? 5.993 -38.677 41.135 1.00 73.55 ? 267 ASN A C 1 ATOM 1882 O O . ASN A 1 267 ? 5.220 -39.634 41.217 1.00 82.26 ? 267 ASN A O 1 ATOM 1883 C CB . ASN A 1 267 ? 7.780 -38.532 42.942 1.00 80.86 ? 267 ASN A CB 1 ATOM 1884 C CG . ASN A 1 267 ? 9.253 -38.760 43.294 1.00 83.42 ? 267 ASN A CG 1 ATOM 1885 O OD1 . ASN A 1 267 ? 9.913 -39.627 42.711 1.00 83.87 ? 267 ASN A OD1 1 ATOM 1886 N ND2 . ASN A 1 267 ? 9.769 -37.984 44.250 1.00 75.25 ? 267 ASN A ND2 1 ATOM 1887 N N . GLU A 1 268 ? 5.619 -37.467 40.728 1.00 64.22 ? 268 GLU A N 1 ATOM 1888 C CA . GLU A 1 268 ? 4.240 -37.136 40.388 1.00 68.00 ? 268 GLU A CA 1 ATOM 1889 C C . GLU A 1 268 ? 3.902 -37.436 38.928 1.00 74.36 ? 268 GLU A C 1 ATOM 1890 O O . GLU A 1 268 ? 2.942 -38.151 38.649 1.00 79.10 ? 268 GLU A O 1 ATOM 1891 C CB . GLU A 1 268 ? 3.974 -35.661 40.681 1.00 78.12 ? 268 GLU A CB 1 ATOM 1892 C CG . GLU A 1 268 ? 4.348 -35.224 42.091 1.00 89.83 ? 268 GLU A CG 1 ATOM 1893 C CD . GLU A 1 268 ? 3.355 -35.688 43.152 1.00 99.05 ? 268 GLU A CD 1 ATOM 1894 O OE1 . GLU A 1 268 ? 2.205 -36.039 42.797 1.00 95.31 ? 268 GLU A OE1 1 ATOM 1895 O OE2 . GLU A 1 268 ? 3.729 -35.693 44.347 1.00 106.95 ? 268 GLU A OE2 1 ATOM 1896 N N . LEU A 1 269 ? 4.683 -36.869 38.008 1.00 73.28 ? 269 LEU A N 1 ATOM 1897 C CA . LEU A 1 269 ? 4.544 -37.119 36.568 1.00 67.69 ? 269 LEU A CA 1 ATOM 1898 C C . LEU A 1 269 ? 4.421 -38.606 36.218 1.00 72.30 ? 269 LEU A C 1 ATOM 1899 O O . LEU A 1 269 ? 3.599 -38.988 35.381 1.00 71.76 ? 269 LEU A O 1 ATOM 1900 C CB . LEU A 1 269 ? 5.722 -36.507 35.805 1.00 64.32 ? 269 LEU A CB 1 ATOM 1901 C CG . LEU A 1 269 ? 5.809 -34.983 35.681 1.00 67.58 ? 269 LEU A CG 1 ATOM 1902 C CD1 . LEU A 1 269 ? 7.234 -34.527 35.350 1.00 59.39 ? 269 LEU A CD1 1 ATOM 1903 C CD2 . LEU A 1 269 ? 4.808 -34.463 34.651 1.00 63.75 ? 269 LEU A CD2 1 ATOM 1904 N N . LEU A 1 270 ? 5.239 -39.443 36.854 1.00 68.09 ? 270 LEU A N 1 ATOM 1905 C CA . LEU A 1 270 ? 5.175 -40.885 36.636 1.00 58.46 ? 270 LEU A CA 1 ATOM 1906 C C . LEU A 1 270 ? 3.775 -41.409 36.948 1.00 70.96 ? 270 LEU A C 1 ATOM 1907 O O . LEU A 1 270 ? 3.356 -42.419 36.397 1.00 80.42 ? 270 LEU A O 1 ATOM 1908 C CB . LEU A 1 270 ? 6.201 -41.593 37.517 1.00 54.45 ? 270 LEU A CB 1 ATOM 1909 C CG . LEU A 1 270 ? 6.808 -42.911 37.034 1.00 55.37 ? 270 LEU A CG 1 ATOM 1910 C CD1 . LEU A 1 270 ? 6.926 -43.922 38.181 1.00 55.79 ? 270 LEU A CD1 1 ATOM 1911 C CD2 . LEU A 1 270 ? 5.996 -43.489 35.908 1.00 52.28 ? 270 LEU A CD2 1 ATOM 1912 N N . LYS A 1 271 ? 3.066 -40.718 37.842 1.00 75.00 ? 271 LYS A N 1 ATOM 1913 C CA . LYS A 1 271 ? 1.674 -41.035 38.185 1.00 68.71 ? 271 LYS A CA 1 ATOM 1914 C C . LYS A 1 271 ? 0.671 -40.760 37.033 1.00 73.51 ? 271 LYS A C 1 ATOM 1915 O O . LYS A 1 271 ? -0.440 -41.298 37.018 1.00 66.65 ? 271 LYS A O 1 ATOM 1916 C CB . LYS A 1 271 ? 1.243 -40.262 39.441 1.00 65.77 ? 271 LYS A CB 1 ATOM 1917 C CG . LYS A 1 271 ? 1.839 -40.746 40.763 1.00 76.23 ? 271 LYS A CG 1 ATOM 1918 C CD . LYS A 1 271 ? 1.298 -39.921 41.943 1.00 80.90 ? 271 LYS A CD 1 ATOM 1919 C CE . LYS A 1 271 ? 1.906 -40.322 43.303 1.00 83.49 ? 271 LYS A CE 1 ATOM 1920 N NZ . LYS A 1 271 ? 1.012 -39.968 44.474 1.00 80.20 ? 271 LYS A NZ 1 ATOM 1921 N N . LEU A 1 272 ? 1.057 -39.919 36.078 1.00 66.54 ? 272 LEU A N 1 ATOM 1922 C CA . LEU A 1 272 ? 0.184 -39.612 34.953 1.00 69.63 ? 272 LEU A CA 1 ATOM 1923 C C . LEU A 1 272 ? 0.018 -40.807 34.021 1.00 70.06 ? 272 LEU A C 1 ATOM 1924 O O . LEU A 1 272 ? -1.026 -40.971 33.389 1.00 68.83 ? 272 LEU A O 1 ATOM 1925 C CB . LEU A 1 272 ? 0.714 -38.417 34.161 1.00 74.59 ? 272 LEU A CB 1 ATOM 1926 C CG . LEU A 1 272 ? 0.618 -37.026 34.788 1.00 71.36 ? 272 LEU A CG 1 ATOM 1927 C CD1 . LEU A 1 272 ? 1.316 -36.011 33.898 1.00 68.47 ? 272 LEU A CD1 1 ATOM 1928 C CD2 . LEU A 1 272 ? -0.825 -36.625 35.027 1.00 60.26 ? 272 LEU A CD2 1 ATOM 1929 N N . LEU A 1 273 ? 1.053 -41.634 33.930 1.00 69.18 ? 273 LEU A N 1 ATOM 1930 C CA . LEU A 1 273 ? 1.036 -42.772 33.020 1.00 62.45 ? 273 LEU A CA 1 ATOM 1931 C C . LEU A 1 273 ? -0.078 -43.749 33.351 1.00 69.58 ? 273 LEU A C 1 ATOM 1932 O O . LEU A 1 273 ? -0.435 -44.580 32.520 1.00 75.69 ? 273 LEU A O 1 ATOM 1933 C CB . LEU A 1 273 ? 2.372 -43.515 33.026 1.00 60.97 ? 273 LEU A CB 1 ATOM 1934 C CG . LEU A 1 273 ? 3.647 -42.779 32.634 1.00 61.00 ? 273 LEU A CG 1 ATOM 1935 C CD1 . LEU A 1 273 ? 4.628 -43.761 32.029 1.00 51.29 ? 273 LEU A CD1 1 ATOM 1936 C CD2 . LEU A 1 273 ? 3.339 -41.673 31.653 1.00 72.85 ? 273 LEU A CD2 1 ATOM 1937 N N . ARG A 1 274 ? -0.620 -43.665 34.563 1.00 66.58 ? 274 ARG A N 1 ATOM 1938 C CA . ARG A 1 274 ? -1.716 -44.550 34.949 1.00 71.14 ? 274 ARG A CA 1 ATOM 1939 C C . ARG A 1 274 ? -2.954 -44.328 34.081 1.00 68.01 ? 274 ARG A C 1 ATOM 1940 O O . ARG A 1 274 ? -3.828 -45.195 33.996 1.00 57.35 ? 274 ARG A O 1 ATOM 1941 C CB . ARG A 1 274 ? -2.088 -44.354 36.407 1.00 75.52 ? 274 ARG A CB 1 ATOM 1942 C CG . ARG A 1 274 ? -0.954 -44.540 37.363 1.00 82.47 ? 274 ARG A CG 1 ATOM 1943 C CD . ARG A 1 274 ? -1.437 -44.311 38.784 1.00 84.72 ? 274 ARG A CD 1 ATOM 1944 N NE . ARG A 1 274 ? -0.331 -44.324 39.727 1.00 88.93 ? 274 ARG A NE 1 ATOM 1945 C CZ . ARG A 1 274 ? -0.375 -43.771 40.930 1.00 82.67 ? 274 ARG A CZ 1 ATOM 1946 N NH1 . ARG A 1 274 ? -1.479 -43.158 41.338 1.00 78.40 ? 274 ARG A NH1 1 ATOM 1947 N NH2 . ARG A 1 274 ? 0.688 -43.831 41.716 1.00 72.75 ? 274 ARG A NH2 1 ATOM 1948 N N . TYR A 1 275 ? -3.021 -43.166 33.438 1.00 69.52 ? 275 TYR A N 1 ATOM 1949 C CA . TYR A 1 275 ? -4.166 -42.820 32.604 1.00 72.33 ? 275 TYR A CA 1 ATOM 1950 C C . TYR A 1 275 ? -3.932 -43.080 31.114 1.00 71.78 ? 275 TYR A C 1 ATOM 1951 O O . TYR A 1 275 ? -4.886 -43.232 30.346 1.00 70.28 ? 275 TYR A O 1 ATOM 1952 C CB . TYR A 1 275 ? -4.608 -41.382 32.874 1.00 70.65 ? 275 TYR A CB 1 ATOM 1953 C CG . TYR A 1 275 ? -5.203 -41.227 34.260 1.00 77.34 ? 275 TYR A CG 1 ATOM 1954 C CD1 . TYR A 1 275 ? -4.404 -40.878 35.347 1.00 78.05 ? 275 TYR A CD1 1 ATOM 1955 C CD2 . TYR A 1 275 ? -6.558 -41.457 34.487 1.00 71.58 ? 275 TYR A CD2 1 ATOM 1956 C CE1 . TYR A 1 275 ? -4.939 -40.745 36.618 1.00 73.23 ? 275 TYR A CE1 1 ATOM 1957 C CE2 . TYR A 1 275 ? -7.101 -41.324 35.746 1.00 81.76 ? 275 TYR A CE2 1 ATOM 1958 C CZ . TYR A 1 275 ? -6.286 -40.970 36.811 1.00 82.91 ? 275 TYR A CZ 1 ATOM 1959 O OH . TYR A 1 275 ? -6.825 -40.845 38.069 1.00 87.06 ? 275 TYR A OH 1 ATOM 1960 N N . ILE A 1 276 ? -2.661 -43.164 30.730 1.00 70.78 ? 276 ILE A N 1 ATOM 1961 C CA . ILE A 1 276 ? -2.266 -43.434 29.351 1.00 71.50 ? 276 ILE A CA 1 ATOM 1962 C C . ILE A 1 276 ? -1.550 -44.775 29.249 1.00 68.29 ? 276 ILE A C 1 ATOM 1963 O O . ILE A 1 276 ? -0.333 -44.833 29.034 1.00 56.44 ? 276 ILE A O 1 ATOM 1964 C CB . ILE A 1 276 ? -1.361 -42.309 28.786 1.00 47.98 ? 276 ILE A CB 1 ATOM 1965 C CG1 . ILE A 1 276 ? -0.258 -41.945 29.787 1.00 44.83 ? 276 ILE A CG1 1 ATOM 1966 C CG2 . ILE A 1 276 ? -2.199 -41.091 28.425 1.00 42.39 ? 276 ILE A CG2 1 ATOM 1967 C CD1 . ILE A 1 276 ? 0.589 -40.749 29.392 1.00 40.49 ? 276 ILE A CD1 1 ATOM 1968 N N . LEU A 1 277 ? -2.318 -45.850 29.397 1.00 64.46 ? 277 LEU A N 1 ATOM 1969 C CA . LEU A 1 277 ? -1.754 -47.195 29.469 1.00 60.32 ? 277 LEU A CA 1 ATOM 1970 C C . LEU A 1 277 ? -1.011 -47.624 28.209 1.00 75.14 ? 277 LEU A C 1 ATOM 1971 O O . LEU A 1 277 ? -0.058 -48.418 28.268 1.00 71.02 ? 277 LEU A O 1 ATOM 1972 C CB . LEU A 1 277 ? -2.852 -48.193 29.802 1.00 49.73 ? 277 LEU A CB 1 ATOM 1973 C CG . LEU A 1 277 ? -3.441 -47.967 31.199 1.00 60.40 ? 277 LEU A CG 1 ATOM 1974 C CD1 . LEU A 1 277 ? -4.658 -48.845 31.460 1.00 58.61 ? 277 LEU A CD1 1 ATOM 1975 C CD2 . LEU A 1 277 ? -2.385 -48.165 32.286 1.00 44.24 ? 277 LEU A CD2 1 ATOM 1976 N N . GLU A 1 278 ? -1.439 -47.075 27.073 1.00 74.62 ? 278 GLU A N 1 ATOM 1977 C CA . GLU A 1 278 ? -0.921 -47.498 25.783 1.00 58.01 ? 278 GLU A CA 1 ATOM 1978 C C . GLU A 1 278 ? 0.392 -46.820 25.425 1.00 63.98 ? 278 GLU A C 1 ATOM 1979 O O . GLU A 1 278 ? 1.065 -47.237 24.484 1.00 64.89 ? 278 GLU A O 1 ATOM 1980 C CB . GLU A 1 278 ? -1.958 -47.275 24.690 1.00 61.58 ? 278 GLU A CB 1 ATOM 1981 C CG . GLU A 1 278 ? -3.285 -47.974 24.937 1.00 75.51 ? 278 GLU A CG 1 ATOM 1982 C CD . GLU A 1 278 ? -3.124 -49.370 25.505 1.00 87.37 ? 278 GLU A CD 1 ATOM 1983 O OE1 . GLU A 1 278 ? -3.929 -49.744 26.387 1.00 90.51 ? 278 GLU A OE1 1 ATOM 1984 O OE2 . GLU A 1 278 ? -2.194 -50.090 25.080 1.00 87.17 ? 278 GLU A OE2 1 ATOM 1985 N N . LEU A 1 279 ? 0.758 -45.791 26.187 1.00 70.34 ? 279 LEU A N 1 ATOM 1986 C CA . LEU A 1 279 ? 1.994 -45.040 25.954 1.00 62.70 ? 279 LEU A CA 1 ATOM 1987 C C . LEU A 1 279 ? 3.165 -45.980 25.704 1.00 59.76 ? 279 LEU A C 1 ATOM 1988 O O . LEU A 1 279 ? 3.307 -46.989 26.387 1.00 60.13 ? 279 LEU A O 1 ATOM 1989 C CB . LEU A 1 279 ? 2.306 -44.135 27.148 1.00 66.02 ? 279 LEU A CB 1 ATOM 1990 C CG . LEU A 1 279 ? 3.002 -42.782 26.945 1.00 69.19 ? 279 LEU A CG 1 ATOM 1991 C CD1 . LEU A 1 279 ? 3.723 -42.379 28.225 1.00 67.73 ? 279 LEU A CD1 1 ATOM 1992 C CD2 . LEU A 1 279 ? 3.975 -42.797 25.791 1.00 68.41 ? 279 LEU A CD2 1 ATOM 1993 N N . SER A 1 280 ? 3.996 -45.631 24.724 1.00 68.25 ? 280 SER A N 1 ATOM 1994 C CA . SER A 1 280 ? 5.134 -46.449 24.327 1.00 67.03 ? 280 SER A CA 1 ATOM 1995 C C . SER A 1 280 ? 6.417 -45.643 24.121 1.00 65.81 ? 280 SER A C 1 ATOM 1996 O O . SER A 1 280 ? 7.446 -46.211 23.788 1.00 69.22 ? 280 SER A O 1 ATOM 1997 C CB . SER A 1 280 ? 4.815 -47.237 23.054 1.00 76.53 ? 280 SER A CB 1 ATOM 1998 O OG . SER A 1 280 ? 4.674 -46.386 21.922 1.00 76.30 ? 280 SER A OG 1 ATOM 1999 N N . GLU A 1 281 ? 6.365 -44.330 24.323 1.00 62.91 ? 281 GLU A N 1 ATOM 2000 C CA . GLU A 1 281 ? 7.569 -43.507 24.205 1.00 62.72 ? 281 GLU A CA 1 ATOM 2001 C C . GLU A 1 281 ? 7.509 -42.251 25.072 1.00 61.98 ? 281 GLU A C 1 ATOM 2002 O O . GLU A 1 281 ? 6.546 -41.491 24.994 1.00 57.56 ? 281 GLU A O 1 ATOM 2003 C CB . GLU A 1 281 ? 7.811 -43.129 22.738 1.00 72.58 ? 281 GLU A CB 1 ATOM 2004 C CG . GLU A 1 281 ? 8.989 -42.183 22.492 1.00 86.70 ? 281 GLU A CG 1 ATOM 2005 C CD . GLU A 1 281 ? 9.278 -41.959 21.006 1.00 93.20 ? 281 GLU A CD 1 ATOM 2006 O OE1 . GLU A 1 281 ? 8.428 -42.345 20.160 1.00 81.17 ? 281 GLU A OE1 1 ATOM 2007 O OE2 . GLU A 1 281 ? 10.358 -41.394 20.695 1.00 97.21 ? 281 GLU A OE2 1 ATOM 2008 N N . VAL A 1 282 ? 8.535 -42.048 25.904 1.00 64.54 ? 282 VAL A N 1 ATOM 2009 C CA . VAL A 1 282 ? 8.698 -40.794 26.653 1.00 63.31 ? 282 VAL A CA 1 ATOM 2010 C C . VAL A 1 282 ? 9.958 -40.066 26.204 1.00 51.91 ? 282 VAL A C 1 ATOM 2011 O O . VAL A 1 282 ? 11.004 -40.683 26.000 1.00 45.59 ? 282 VAL A O 1 ATOM 2012 C CB . VAL A 1 282 ? 8.800 -40.979 28.203 1.00 52.50 ? 282 VAL A CB 1 ATOM 2013 C CG1 . VAL A 1 282 ? 8.053 -39.868 28.895 1.00 56.60 ? 282 VAL A CG1 1 ATOM 2014 C CG2 . VAL A 1 282 ? 8.269 -42.323 28.665 1.00 43.37 ? 282 VAL A CG2 1 ATOM 2015 N N . GLU A 1 283 ? 9.859 -38.750 26.073 1.00 50.95 ? 283 GLU A N 1 ATOM 2016 C CA . GLU A 1 283 ? 10.997 -37.949 25.650 1.00 58.63 ? 283 GLU A CA 1 ATOM 2017 C C . GLU A 1 283 ? 11.128 -36.699 26.501 1.00 61.88 ? 283 GLU A C 1 ATOM 2018 O O . GLU A 1 283 ? 10.132 -36.093 26.897 1.00 65.97 ? 283 GLU A O 1 ATOM 2019 C CB . GLU A 1 283 ? 10.878 -37.575 24.165 1.00 77.18 ? 283 GLU A CB 1 ATOM 2020 C CG . GLU A 1 283 ? 11.999 -36.674 23.630 1.00 90.52 ? 283 GLU A CG 1 ATOM 2021 C CD . GLU A 1 283 ? 12.159 -36.738 22.109 1.00 93.93 ? 283 GLU A CD 1 ATOM 2022 O OE1 . GLU A 1 283 ? 11.172 -37.075 21.412 1.00 87.82 ? 283 GLU A OE1 1 ATOM 2023 O OE2 . GLU A 1 283 ? 13.279 -36.449 21.615 1.00 93.42 ? 283 GLU A OE2 1 ATOM 2024 N N . PHE A 1 284 ? 12.373 -36.337 26.790 1.00 58.27 ? 284 PHE A N 1 ATOM 2025 C CA . PHE A 1 284 ? 12.701 -35.109 27.493 1.00 53.95 ? 284 PHE A CA 1 ATOM 2026 C C . PHE A 1 284 ? 13.748 -34.413 26.665 1.00 58.53 ? 284 PHE A C 1 ATOM 2027 O O . PHE A 1 284 ? 14.830 -34.968 26.461 1.00 62.89 ? 284 PHE A O 1 ATOM 2028 C CB . PHE A 1 284 ? 13.266 -35.421 28.880 1.00 49.69 ? 284 PHE A CB 1 ATOM 2029 C CG . PHE A 1 284 ? 12.238 -35.943 29.845 1.00 54.63 ? 284 PHE A CG 1 ATOM 2030 C CD1 . PHE A 1 284 ? 11.507 -35.067 30.638 1.00 53.00 ? 284 PHE A CD1 1 ATOM 2031 C CD2 . PHE A 1 284 ? 11.984 -37.307 29.942 1.00 49.25 ? 284 PHE A CD2 1 ATOM 2032 C CE1 . PHE A 1 284 ? 10.547 -35.538 31.518 1.00 56.94 ? 284 PHE A CE1 1 ATOM 2033 C CE2 . PHE A 1 284 ? 11.021 -37.782 30.814 1.00 59.11 ? 284 PHE A CE2 1 ATOM 2034 C CZ . PHE A 1 284 ? 10.300 -36.891 31.608 1.00 59.75 ? 284 PHE A CZ 1 ATOM 2035 N N . ASP A 1 285 ? 13.436 -33.214 26.171 1.00 55.02 ? 285 ASP A N 1 ATOM 2036 C CA . ASP A 1 285 ? 14.417 -32.459 25.398 1.00 63.97 ? 285 ASP A CA 1 ATOM 2037 C C . ASP A 1 285 ? 15.247 -31.507 26.235 1.00 79.81 ? 285 ASP A C 1 ATOM 2038 O O . ASP A 1 285 ? 15.774 -31.891 27.288 1.00 106.32 ? 285 ASP A O 1 ATOM 2039 C CB . ASP A 1 285 ? 13.780 -31.727 24.232 1.00 82.58 ? 285 ASP A CB 1 ATOM 2040 C CG . ASP A 1 285 ? 13.965 -32.468 22.926 1.00 92.77 ? 285 ASP A CG 1 ATOM 2041 O OD1 . ASP A 1 285 ? 14.226 -33.692 22.993 1.00 77.05 ? 285 ASP A OD1 1 ATOM 2042 O OD2 . ASP A 1 285 ? 13.859 -31.825 21.849 1.00 106.37 ? 285 ASP A OD2 1 ATOM 2043 N N . ASP A 1 286 ? 15.384 -30.275 25.762 1.00 62.88 ? 286 ASP A N 1 ATOM 2044 C CA . ASP A 1 286 ? 16.224 -29.301 26.453 1.00 67.04 ? 286 ASP A CA 1 ATOM 2045 C C . ASP A 1 286 ? 15.648 -28.970 27.834 1.00 68.51 ? 286 ASP A C 1 ATOM 2046 O O . ASP A 1 286 ? 15.138 -27.873 28.061 1.00 72.22 ? 286 ASP A O 1 ATOM 2047 C CB . ASP A 1 286 ? 16.406 -28.036 25.611 1.00 70.03 ? 286 ASP A CB 1 ATOM 2048 C CG . ASP A 1 286 ? 17.190 -28.291 24.329 1.00 88.78 ? 286 ASP A CG 1 ATOM 2049 O OD1 . ASP A 1 286 ? 18.410 -28.006 24.324 1.00 104.06 ? 286 ASP A OD1 1 ATOM 2050 O OD2 . ASP A 1 286 ? 16.596 -28.776 23.332 1.00 82.78 ? 286 ASP A OD2 1 ATOM 2051 N N . CYS A 1 287 ? 15.739 -29.930 28.751 1.00 54.09 ? 287 CYS A N 1 ATOM 2052 C CA . CYS A 1 287 ? 15.079 -29.830 30.036 1.00 44.29 ? 287 CYS A CA 1 ATOM 2053 C C . CYS A 1 287 ? 16.108 -29.595 31.134 1.00 54.33 ? 287 CYS A C 1 ATOM 2054 O O . CYS A 1 287 ? 17.225 -30.090 31.054 1.00 61.88 ? 287 CYS A O 1 ATOM 2055 C CB . CYS A 1 287 ? 14.288 -31.105 30.317 1.00 38.35 ? 287 CYS A CB 1 ATOM 2056 S SG . CYS A 1 287 ? 12.649 -31.259 29.499 1.00 57.34 ? 287 CYS A SG 1 ATOM 2057 N N . THR A 1 288 ? 15.745 -28.819 32.147 1.00 46.61 ? 288 THR A N 1 ATOM 2058 C CA . THR A 1 288 ? 16.608 -28.678 33.308 1.00 56.15 ? 288 THR A CA 1 ATOM 2059 C C . THR A 1 288 ? 16.124 -29.554 34.478 1.00 54.95 ? 288 THR A C 1 ATOM 2060 O O . THR A 1 288 ? 14.959 -29.499 34.877 1.00 52.53 ? 288 THR A O 1 ATOM 2061 C CB . THR A 1 288 ? 16.749 -27.204 33.749 1.00 62.18 ? 288 THR A CB 1 ATOM 2062 O OG1 . THR A 1 288 ? 17.787 -26.566 32.994 1.00 63.83 ? 288 THR A OG1 1 ATOM 2063 C CG2 . THR A 1 288 ? 17.119 -27.133 35.207 1.00 59.54 ? 288 THR A CG2 1 ATOM 2064 N N . LEU A 1 289 ? 17.012 -30.389 35.007 1.00 46.36 ? 289 LEU A N 1 ATOM 2065 C CA . LEU A 1 289 ? 16.705 -31.118 36.234 1.00 49.16 ? 289 LEU A CA 1 ATOM 2066 C C . LEU A 1 289 ? 17.449 -30.518 37.430 1.00 51.66 ? 289 LEU A C 1 ATOM 2067 O O . LEU A 1 289 ? 18.627 -30.798 37.630 1.00 55.97 ? 289 LEU A O 1 ATOM 2068 C CB . LEU A 1 289 ? 17.024 -32.601 36.097 1.00 41.96 ? 289 LEU A CB 1 ATOM 2069 C CG . LEU A 1 289 ? 16.874 -33.406 37.385 1.00 45.29 ? 289 LEU A CG 1 ATOM 2070 C CD1 . LEU A 1 289 ? 15.469 -33.285 37.987 1.00 37.32 ? 289 LEU A CD1 1 ATOM 2071 C CD2 . LEU A 1 289 ? 17.237 -34.850 37.113 1.00 33.56 ? 289 LEU A CD2 1 ATOM 2072 N N . ASN A 1 290 ? 16.746 -29.663 38.178 1.00 50.72 ? 290 ASN A N 1 ATOM 2073 C CA . ASN A 1 290 ? 17.198 -29.095 39.449 1.00 57.64 ? 290 ASN A CA 1 ATOM 2074 C C . ASN A 1 290 ? 16.995 -30.143 40.546 1.00 66.14 ? 290 ASN A C 1 ATOM 2075 O O . ASN A 1 290 ? 16.050 -30.073 41.343 1.00 63.99 ? 290 ASN A O 1 ATOM 2076 C CB . ASN A 1 290 ? 16.397 -27.831 39.798 1.00 55.22 ? 290 ASN A CB 1 ATOM 2077 C CG . ASN A 1 290 ? 16.804 -26.608 38.975 1.00 52.02 ? 290 ASN A CG 1 ATOM 2078 O OD1 . ASN A 1 290 ? 17.977 -26.409 38.647 1.00 52.13 ? 290 ASN A OD1 1 ATOM 2079 N ND2 . ASN A 1 290 ? 15.827 -25.769 38.666 1.00 34.06 ? 290 ASN A ND2 1 ATOM 2080 N N . GLY A 1 291 ? 17.898 -31.114 40.565 1.00 60.92 ? 291 GLY A N 1 ATOM 2081 C CA . GLY A 1 291 ? 17.754 -32.313 41.359 1.00 60.73 ? 291 GLY A CA 1 ATOM 2082 C C . GLY A 1 291 ? 18.981 -33.177 41.149 1.00 60.90 ? 291 GLY A C 1 ATOM 2083 O O . GLY A 1 291 ? 19.963 -32.729 40.559 1.00 69.12 ? 291 GLY A O 1 ATOM 2084 N N . LEU A 1 292 ? 18.922 -34.415 41.624 1.00 52.91 ? 292 LEU A N 1 ATOM 2085 C CA . LEU A 1 292 ? 20.094 -35.272 41.647 1.00 61.01 ? 292 LEU A CA 1 ATOM 2086 C C . LEU A 1 292 ? 19.672 -36.716 41.523 1.00 62.55 ? 292 LEU A C 1 ATOM 2087 O O . LEU A 1 292 ? 20.422 -37.613 41.902 1.00 65.72 ? 292 LEU A O 1 ATOM 2088 C CB . LEU A 1 292 ? 20.879 -35.102 42.958 1.00 59.72 ? 292 LEU A CB 1 ATOM 2089 C CG . LEU A 1 292 ? 21.595 -33.796 43.312 1.00 57.58 ? 292 LEU A CG 1 ATOM 2090 C CD1 . LEU A 1 292 ? 22.218 -33.913 44.680 1.00 54.40 ? 292 LEU A CD1 1 ATOM 2091 C CD2 . LEU A 1 292 ? 22.660 -33.450 42.300 1.00 63.36 ? 292 LEU A CD2 1 ATOM 2092 N N . GLY A 1 293 ? 18.465 -36.941 41.019 1.00 57.31 ? 293 GLY A N 1 ATOM 2093 C CA . GLY A 1 293 ? 17.977 -38.292 40.805 1.00 63.11 ? 293 GLY A CA 1 ATOM 2094 C C . GLY A 1 293 ? 17.494 -38.992 42.064 1.00 71.52 ? 293 GLY A C 1 ATOM 2095 O O . GLY A 1 293 ? 17.402 -40.219 42.095 1.00 69.52 ? 293 GLY A O 1 ATOM 2096 N N . ASP A 1 294 ? 17.194 -38.211 43.101 1.00 74.47 ? 294 ASP A N 1 ATOM 2097 C CA . ASP A 1 294 ? 16.620 -38.741 44.337 1.00 82.99 ? 294 ASP A CA 1 ATOM 2098 C C . ASP A 1 294 ? 15.121 -39.040 44.162 1.00 85.85 ? 294 ASP A C 1 ATOM 2099 O O . ASP A 1 294 ? 14.261 -38.390 44.772 1.00 86.15 ? 294 ASP A O 1 ATOM 2100 C CB . ASP A 1 294 ? 16.846 -37.755 45.490 1.00 90.53 ? 294 ASP A CB 1 ATOM 2101 C CG . ASP A 1 294 ? 16.713 -38.408 46.867 1.00 94.45 ? 294 ASP A CG 1 ATOM 2102 O OD1 . ASP A 1 294 ? 16.475 -37.676 47.864 1.00 91.77 ? 294 ASP A OD1 1 ATOM 2103 O OD2 . ASP A 1 294 ? 16.853 -39.649 46.947 1.00 89.07 ? 294 ASP A OD2 1 ATOM 2104 N N . PHE A 1 295 ? 14.817 -40.033 43.330 1.00 79.12 ? 295 PHE A N 1 ATOM 2105 C CA . PHE A 1 295 ? 13.434 -40.353 42.989 1.00 77.37 ? 295 PHE A CA 1 ATOM 2106 C C . PHE A 1 295 ? 12.790 -41.315 43.990 1.00 78.48 ? 295 PHE A C 1 ATOM 2107 O O . PHE A 1 295 ? 13.378 -42.334 44.327 1.00 72.66 ? 295 PHE A O 1 ATOM 2108 C CB . PHE A 1 295 ? 13.355 -40.963 41.584 1.00 73.17 ? 295 PHE A CB 1 ATOM 2109 C CG . PHE A 1 295 ? 13.989 -40.121 40.509 1.00 77.68 ? 295 PHE A CG 1 ATOM 2110 C CD1 . PHE A 1 295 ? 14.788 -40.702 39.541 1.00 71.89 ? 295 PHE A CD1 1 ATOM 2111 C CD2 . PHE A 1 295 ? 13.783 -38.747 40.465 1.00 82.72 ? 295 PHE A CD2 1 ATOM 2112 C CE1 . PHE A 1 295 ? 15.366 -39.929 38.556 1.00 71.26 ? 295 PHE A CE1 1 ATOM 2113 C CE2 . PHE A 1 295 ? 14.363 -37.970 39.477 1.00 69.06 ? 295 PHE A CE2 1 ATOM 2114 C CZ . PHE A 1 295 ? 15.150 -38.561 38.527 1.00 64.71 ? 295 PHE A CZ 1 ATOM 2115 N N . ASN A 1 296 ? 11.583 -40.996 44.455 1.00 76.04 ? 296 ASN A N 1 ATOM 2116 C CA . ASN A 1 296 ? 10.805 -41.949 45.250 1.00 72.75 ? 296 ASN A CA 1 ATOM 2117 C C . ASN A 1 296 ? 9.424 -42.238 44.666 1.00 75.58 ? 296 ASN A C 1 ATOM 2118 O O . ASN A 1 296 ? 8.411 -41.686 45.102 1.00 70.17 ? 296 ASN A O 1 ATOM 2119 C CB . ASN A 1 296 ? 10.741 -41.533 46.715 1.00 70.74 ? 296 ASN A CB 1 ATOM 2120 C CG . ASN A 1 296 ? 12.124 -41.302 47.300 1.00 96.63 ? 296 ASN A CG 1 ATOM 2121 O OD1 . ASN A 1 296 ? 12.755 -42.218 47.847 1.00 90.95 ? 296 ASN A OD1 1 ATOM 2122 N ND2 . ASN A 1 296 ? 12.627 -40.082 47.144 1.00 114.20 ? 296 ASN A ND2 1 ATOM 2123 N N . PRO A 1 297 ? 9.397 -43.112 43.655 1.00 73.95 ? 297 PRO A N 1 ATOM 2124 C CA . PRO A 1 297 ? 8.215 -43.543 42.903 1.00 72.33 ? 297 PRO A CA 1 ATOM 2125 C C . PRO A 1 297 ? 7.262 -44.340 43.770 1.00 77.53 ? 297 PRO A C 1 ATOM 2126 O O . PRO A 1 297 ? 7.696 -45.300 44.383 1.00 83.77 ? 297 PRO A O 1 ATOM 2127 C CB . PRO A 1 297 ? 8.803 -44.478 41.844 1.00 61.16 ? 297 PRO A CB 1 ATOM 2128 C CG . PRO A 1 297 ? 10.243 -44.131 41.769 1.00 59.86 ? 297 PRO A CG 1 ATOM 2129 C CD . PRO A 1 297 ? 10.630 -43.725 43.139 1.00 66.93 ? 297 PRO A CD 1 ATOM 2130 N N . SER A 1 298 ? 5.992 -43.962 43.819 1.00 81.34 ? 298 SER A N 1 ATOM 2131 C CA . SER A 1 298 ? 4.994 -44.791 44.477 1.00 77.40 ? 298 SER A CA 1 ATOM 2132 C C . SER A 1 298 ? 5.191 -46.246 44.070 1.00 79.21 ? 298 SER A C 1 ATOM 2133 O O . SER A 1 298 ? 5.719 -46.526 42.997 1.00 74.65 ? 298 SER A O 1 ATOM 2134 C CB . SER A 1 298 ? 3.587 -44.330 44.111 1.00 87.23 ? 298 SER A CB 1 ATOM 2135 O OG . SER A 1 298 ? 3.456 -42.930 44.283 1.00 100.35 ? 298 SER A OG 1 ATOM 2136 N N . GLU A 1 299 ? 4.775 -47.173 44.927 1.00 89.72 ? 299 GLU A N 1 ATOM 2137 C CA . GLU A 1 299 ? 5.034 -48.592 44.696 1.00 97.41 ? 299 GLU A CA 1 ATOM 2138 C C . GLU A 1 299 ? 4.106 -49.203 43.655 1.00 94.62 ? 299 GLU A C 1 ATOM 2139 O O . GLU A 1 299 ? 4.480 -50.152 42.956 1.00 87.85 ? 299 GLU A O 1 ATOM 2140 C CB . GLU A 1 299 ? 4.975 -49.375 46.006 1.00 112.77 ? 299 GLU A CB 1 ATOM 2141 C CG . GLU A 1 299 ? 6.302 -49.413 46.756 1.00 125.64 ? 299 GLU A CG 1 ATOM 2142 C CD . GLU A 1 299 ? 7.312 -50.354 46.114 1.00 130.68 ? 299 GLU A CD 1 ATOM 2143 O OE1 . GLU A 1 299 ? 8.529 -50.060 46.189 1.00 131.24 ? 299 GLU A OE1 1 ATOM 2144 O OE2 . GLU A 1 299 ? 6.887 -51.384 45.536 1.00 127.83 ? 299 GLU A OE2 1 ATOM 2145 N N . SER A 1 300 ? 2.897 -48.659 43.559 1.00 93.19 ? 300 SER A N 1 ATOM 2146 C CA . SER A 1 300 ? 1.975 -49.057 42.506 1.00 90.02 ? 300 SER A CA 1 ATOM 2147 C C . SER A 1 300 ? 2.714 -48.939 41.186 1.00 98.20 ? 300 SER A C 1 ATOM 2148 O O . SER A 1 300 ? 2.747 -49.882 40.396 1.00 103.44 ? 300 SER A O 1 ATOM 2149 C CB . SER A 1 300 ? 0.751 -48.145 42.493 1.00 89.83 ? 300 SER A CB 1 ATOM 2150 O OG . SER A 1 300 ? 0.419 -47.707 43.805 1.00 99.54 ? 300 SER A OG 1 ATOM 2151 N N . ASP A 1 301 ? 3.334 -47.777 40.977 1.00 96.14 ? 301 ASP A N 1 ATOM 2152 C CA . ASP A 1 301 ? 4.011 -47.447 39.727 1.00 89.31 ? 301 ASP A CA 1 ATOM 2153 C C . ASP A 1 301 ? 5.224 -48.332 39.431 1.00 87.06 ? 301 ASP A C 1 ATOM 2154 O O . ASP A 1 301 ? 5.517 -48.611 38.276 1.00 98.61 ? 301 ASP A O 1 ATOM 2155 C CB . ASP A 1 301 ? 4.431 -45.970 39.710 1.00 92.93 ? 301 ASP A CB 1 ATOM 2156 C CG . ASP A 1 301 ? 3.300 -45.030 40.101 1.00 95.91 ? 301 ASP A CG 1 ATOM 2157 O OD1 . ASP A 1 301 ? 2.123 -45.427 39.965 1.00 91.98 ? 301 ASP A OD1 1 ATOM 2158 O OD2 . ASP A 1 301 ? 3.595 -43.894 40.545 1.00 96.42 ? 301 ASP A OD2 1 ATOM 2159 N N . VAL A 1 302 ? 5.935 -48.773 40.459 1.00 86.58 ? 302 VAL A N 1 ATOM 2160 C CA . VAL A 1 302 ? 7.150 -49.552 40.228 1.00 86.15 ? 302 VAL A CA 1 ATOM 2161 C C . VAL A 1 302 ? 6.845 -51.003 39.835 1.00 84.22 ? 302 VAL A C 1 ATOM 2162 O O . VAL A 1 302 ? 7.610 -51.633 39.106 1.00 83.90 ? 302 VAL A O 1 ATOM 2163 C CB . VAL A 1 302 ? 8.140 -49.458 41.425 1.00 70.93 ? 302 VAL A CB 1 ATOM 2164 C CG1 . VAL A 1 302 ? 9.321 -50.413 41.238 1.00 60.40 ? 302 VAL A CG1 1 ATOM 2165 C CG2 . VAL A 1 302 ? 8.640 -48.009 41.596 1.00 55.74 ? 302 VAL A CG2 1 ATOM 2166 N N . VAL A 1 303 ? 5.716 -51.523 40.302 1.00 85.83 ? 303 VAL A N 1 ATOM 2167 C CA . VAL A 1 303 ? 5.221 -52.816 39.828 1.00 90.87 ? 303 VAL A CA 1 ATOM 2168 C C . VAL A 1 303 ? 4.827 -52.780 38.336 1.00 85.26 ? 303 VAL A C 1 ATOM 2169 O O . VAL A 1 303 ? 4.978 -53.765 37.617 1.00 78.18 ? 303 VAL A O 1 ATOM 2170 C CB . VAL A 1 303 ? 4.008 -53.272 40.651 1.00 88.63 ? 303 VAL A CB 1 ATOM 2171 C CG1 . VAL A 1 303 ? 3.649 -54.717 40.321 1.00 86.69 ? 303 VAL A CG1 1 ATOM 2172 C CG2 . VAL A 1 303 ? 4.293 -53.101 42.131 1.00 79.08 ? 303 VAL A CG2 1 ATOM 2173 N N . SER A 1 304 ? 4.327 -51.634 37.886 1.00 81.98 ? 304 SER A N 1 ATOM 2174 C CA . SER A 1 304 ? 3.900 -51.440 36.504 1.00 82.47 ? 304 SER A CA 1 ATOM 2175 C C . SER A 1 304 ? 5.052 -51.488 35.511 1.00 86.66 ? 304 SER A C 1 ATOM 2176 O O . SER A 1 304 ? 4.846 -51.706 34.314 1.00 87.41 ? 304 SER A O 1 ATOM 2177 C CB . SER A 1 304 ? 3.202 -50.090 36.365 1.00 86.02 ? 304 SER A CB 1 ATOM 2178 O OG . SER A 1 304 ? 2.225 -49.921 37.375 1.00 93.06 ? 304 SER A OG 1 ATOM 2179 N N . GLU A 1 305 ? 6.260 -51.258 36.007 1.00 85.52 ? 305 GLU A N 1 ATOM 2180 C CA . GLU A 1 305 ? 7.444 -51.262 35.164 1.00 78.61 ? 305 GLU A CA 1 ATOM 2181 C C . GLU A 1 305 ? 7.265 -50.362 33.949 1.00 78.41 ? 305 GLU A C 1 ATOM 2182 O O . GLU A 1 305 ? 7.651 -50.729 32.840 1.00 89.39 ? 305 GLU A O 1 ATOM 2183 C CB . GLU A 1 305 ? 7.763 -52.686 34.708 1.00 72.48 ? 305 GLU A CB 1 ATOM 2184 C CG . GLU A 1 305 ? 7.786 -53.708 35.832 1.00 81.91 ? 305 GLU A CG 1 ATOM 2185 C CD . GLU A 1 305 ? 8.355 -55.048 35.397 1.00 88.12 ? 305 GLU A CD 1 ATOM 2186 O OE1 . GLU A 1 305 ? 9.451 -55.406 35.890 1.00 79.08 ? 305 GLU A OE1 1 ATOM 2187 O OE2 . GLU A 1 305 ? 7.713 -55.734 34.563 1.00 94.38 ? 305 GLU A OE2 1 ATOM 2188 N N . LEU A 1 306 ? 6.675 -49.188 34.159 1.00 72.41 ? 306 LEU A N 1 ATOM 2189 C CA . LEU A 1 306 ? 6.452 -48.232 33.067 1.00 75.62 ? 306 LEU A CA 1 ATOM 2190 C C . LEU A 1 306 ? 5.511 -48.702 31.954 1.00 73.78 ? 306 LEU A C 1 ATOM 2191 O O . LEU A 1 306 ? 5.647 -48.248 30.822 1.00 82.12 ? 306 LEU A O 1 ATOM 2192 C CB . LEU A 1 306 ? 7.776 -47.839 32.406 1.00 73.56 ? 306 LEU A CB 1 ATOM 2193 C CG . LEU A 1 306 ? 8.565 -46.610 32.839 1.00 61.91 ? 306 LEU A CG 1 ATOM 2194 C CD1 . LEU A 1 306 ? 9.390 -46.152 31.660 1.00 48.65 ? 306 LEU A CD1 1 ATOM 2195 C CD2 . LEU A 1 306 ? 7.632 -45.515 33.293 1.00 62.34 ? 306 LEU A CD2 1 ATOM 2196 N N . GLY A 1 307 ? 4.580 -49.602 32.262 1.00 68.26 ? 307 GLY A N 1 ATOM 2197 C CA . GLY A 1 307 ? 3.593 -50.067 31.297 1.00 65.88 ? 307 GLY A CA 1 ATOM 2198 C C . GLY A 1 307 ? 4.102 -50.556 29.943 1.00 71.46 ? 307 GLY A C 1 ATOM 2199 O O . GLY A 1 307 ? 4.967 -51.426 29.862 1.00 75.14 ? 307 GLY A O 1 ATOM 2200 N N . LYS A 1 308 ? 3.557 -49.997 28.868 1.00 75.74 ? 308 LYS A N 1 ATOM 2201 C CA . LYS A 1 308 ? 3.940 -50.413 27.524 1.00 70.96 ? 308 LYS A CA 1 ATOM 2202 C C . LYS A 1 308 ? 5.015 -49.508 26.913 1.00 67.13 ? 308 LYS A C 1 ATOM 2203 O O . LYS A 1 308 ? 5.284 -49.581 25.708 1.00 74.48 ? 308 LYS A O 1 ATOM 2204 C CB . LYS A 1 308 ? 2.703 -50.486 26.617 1.00 64.50 ? 308 LYS A CB 1 ATOM 2205 C CG . LYS A 1 308 ? 1.927 -51.787 26.730 1.00 62.79 ? 308 LYS A CG 1 ATOM 2206 C CD . LYS A 1 308 ? 0.448 -51.601 26.418 1.00 73.51 ? 308 LYS A CD 1 ATOM 2207 C CE . LYS A 1 308 ? -0.334 -52.905 26.620 1.00 80.37 ? 308 LYS A CE 1 ATOM 2208 N NZ . LYS A 1 308 ? -1.815 -52.699 26.725 1.00 77.73 ? 308 LYS A NZ 1 ATOM 2209 N N . VAL A 1 309 ? 5.619 -48.658 27.746 1.00 55.91 ? 309 VAL A N 1 ATOM 2210 C CA . VAL A 1 309 ? 6.693 -47.756 27.315 1.00 58.91 ? 309 VAL A CA 1 ATOM 2211 C C . VAL A 1 309 ? 7.977 -48.511 27.009 1.00 67.31 ? 309 VAL A C 1 ATOM 2212 O O . VAL A 1 309 ? 8.652 -49.016 27.910 1.00 73.62 ? 309 VAL A O 1 ATOM 2213 C CB . VAL A 1 309 ? 6.979 -46.639 28.345 1.00 54.56 ? 309 VAL A CB 1 ATOM 2214 C CG1 . VAL A 1 309 ? 8.351 -46.002 28.102 1.00 49.11 ? 309 VAL A CG1 1 ATOM 2215 C CG2 . VAL A 1 309 ? 5.908 -45.594 28.271 1.00 52.62 ? 309 VAL A CG2 1 ATOM 2216 N N . GLU A 1 310 ? 8.304 -48.578 25.725 1.00 65.68 ? 310 GLU A N 1 ATOM 2217 C CA . GLU A 1 310 ? 9.428 -49.366 25.255 1.00 69.42 ? 310 GLU A CA 1 ATOM 2218 C C . GLU A 1 310 ? 10.644 -48.479 25.111 1.00 58.80 ? 310 GLU A C 1 ATOM 2219 O O . GLU A 1 310 ? 11.769 -48.938 25.260 1.00 59.12 ? 310 GLU A O 1 ATOM 2220 C CB . GLU A 1 310 ? 9.101 -50.012 23.900 1.00 92.84 ? 310 GLU A CB 1 ATOM 2221 C CG . GLU A 1 310 ? 7.861 -50.920 23.881 1.00 113.15 ? 310 GLU A CG 1 ATOM 2222 C CD . GLU A 1 310 ? 8.074 -52.236 24.620 1.00 132.10 ? 310 GLU A CD 1 ATOM 2223 O OE1 . GLU A 1 310 ? 9.179 -52.444 25.163 1.00 142.57 ? 310 GLU A OE1 1 ATOM 2224 O OE2 . GLU A 1 310 ? 7.140 -53.066 24.664 1.00 132.02 ? 310 GLU A OE2 1 ATOM 2225 N N . THR A 1 311 ? 10.413 -47.200 24.826 1.00 54.22 ? 311 THR A N 1 ATOM 2226 C CA . THR A 1 311 ? 11.505 -46.286 24.478 1.00 56.56 ? 311 THR A CA 1 ATOM 2227 C C . THR A 1 311 ? 11.499 -45.034 25.331 1.00 56.67 ? 311 THR A C 1 ATOM 2228 O O . THR A 1 311 ? 10.460 -44.395 25.512 1.00 65.85 ? 311 THR A O 1 ATOM 2229 C CB . THR A 1 311 ? 11.458 -45.871 22.978 1.00 69.00 ? 311 THR A CB 1 ATOM 2230 O OG1 . THR A 1 311 ? 11.568 -47.036 22.150 1.00 76.68 ? 311 THR A OG1 1 ATOM 2231 C CG2 . THR A 1 311 ? 12.587 -44.906 22.631 1.00 54.89 ? 311 THR A CG2 1 ATOM 2232 N N . VAL A 1 312 ? 12.676 -44.695 25.847 1.00 44.57 ? 312 VAL A N 1 ATOM 2233 C CA . VAL A 1 312 ? 12.852 -43.539 26.713 1.00 52.11 ? 312 VAL A CA 1 ATOM 2234 C C . VAL A 1 312 ? 13.967 -42.694 26.135 1.00 50.69 ? 312 VAL A C 1 ATOM 2235 O O . VAL A 1 312 ? 15.072 -43.188 25.909 1.00 58.33 ? 312 VAL A O 1 ATOM 2236 C CB . VAL A 1 312 ? 13.254 -43.979 28.137 1.00 53.94 ? 312 VAL A CB 1 ATOM 2237 C CG1 . VAL A 1 312 ? 13.959 -42.845 28.874 1.00 46.12 ? 312 VAL A CG1 1 ATOM 2238 C CG2 . VAL A 1 312 ? 12.042 -44.484 28.907 1.00 52.38 ? 312 VAL A CG2 1 ATOM 2239 N N . THR A 1 313 ? 13.697 -41.423 25.884 1.00 40.66 ? 313 THR A N 1 ATOM 2240 C CA . THR A 1 313 ? 14.706 -40.601 25.226 1.00 54.52 ? 313 THR A CA 1 ATOM 2241 C C . THR A 1 313 ? 14.986 -39.287 25.937 1.00 60.92 ? 313 THR A C 1 ATOM 2242 O O . THR A 1 313 ? 14.093 -38.446 26.069 1.00 61.63 ? 313 THR A O 1 ATOM 2243 C CB . THR A 1 313 ? 14.335 -40.277 23.762 1.00 57.49 ? 313 THR A CB 1 ATOM 2244 O OG1 . THR A 1 313 ? 13.964 -41.477 23.068 1.00 65.16 ? 313 THR A OG1 1 ATOM 2245 C CG2 . THR A 1 313 ? 15.513 -39.623 23.064 1.00 41.06 ? 313 THR A CG2 1 ATOM 2246 N N . ILE A 1 314 ? 16.236 -39.104 26.360 1.00 53.69 ? 314 ILE A N 1 ATOM 2247 C CA . ILE A 1 314 ? 16.652 -37.886 27.040 1.00 53.19 ? 314 ILE A CA 1 ATOM 2248 C C . ILE A 1 314 ? 17.760 -37.174 26.258 1.00 53.98 ? 314 ILE A C 1 ATOM 2249 O O . ILE A 1 314 ? 18.835 -37.738 26.066 1.00 56.64 ? 314 ILE A O 1 ATOM 2250 C CB . ILE A 1 314 ? 17.074 -38.213 28.494 1.00 53.18 ? 314 ILE A CB 1 ATOM 2251 C CG1 . ILE A 1 314 ? 15.875 -38.809 29.234 1.00 40.89 ? 314 ILE A CG1 1 ATOM 2252 C CG2 . ILE A 1 314 ? 17.655 -36.969 29.238 1.00 25.37 ? 314 ILE A CG2 1 ATOM 2253 C CD1 . ILE A 1 314 ? 16.236 -39.874 30.216 1.00 48.41 ? 314 ILE A CD1 1 ATOM 2254 N N . ARG A 1 315 ? 17.478 -35.947 25.800 1.00 50.71 ? 315 ARG A N 1 ATOM 2255 C CA . ARG A 1 315 ? 18.439 -35.129 25.040 1.00 52.42 ? 315 ARG A CA 1 ATOM 2256 C C . ARG A 1 315 ? 18.726 -33.805 25.723 1.00 49.95 ? 315 ARG A C 1 ATOM 2257 O O . ARG A 1 315 ? 17.792 -33.088 26.057 1.00 60.11 ? 315 ARG A O 1 ATOM 2258 C CB . ARG A 1 315 ? 17.911 -34.808 23.634 1.00 54.74 ? 315 ARG A CB 1 ATOM 2259 C CG . ARG A 1 315 ? 17.589 -36.005 22.788 1.00 66.93 ? 315 ARG A CG 1 ATOM 2260 C CD . ARG A 1 315 ? 17.929 -35.773 21.328 1.00 71.98 ? 315 ARG A CD 1 ATOM 2261 N NE . ARG A 1 315 ? 18.297 -37.036 20.698 1.00 72.88 ? 315 ARG A NE 1 ATOM 2262 C CZ . ARG A 1 315 ? 17.418 -37.891 20.190 1.00 78.01 ? 315 ARG A CZ 1 ATOM 2263 N NH1 . ARG A 1 315 ? 16.117 -37.592 20.215 1.00 77.81 ? 315 ARG A NH1 1 ATOM 2264 N NH2 . ARG A 1 315 ? 17.843 -39.033 19.651 1.00 73.66 ? 315 ARG A NH2 1 ATOM 2265 N N . ARG A 1 316 ? 20.005 -33.462 25.893 1.00 49.67 ? 316 ARG A N 1 ATOM 2266 C CA . ARG A 1 316 ? 20.407 -32.173 26.490 1.00 54.08 ? 316 ARG A CA 1 ATOM 2267 C C . ARG A 1 316 ? 19.649 -31.867 27.789 1.00 63.90 ? 316 ARG A C 1 ATOM 2268 O O . ARG A 1 316 ? 19.002 -30.823 27.913 1.00 61.75 ? 316 ARG A O 1 ATOM 2269 C CB . ARG A 1 316 ? 20.211 -31.011 25.504 1.00 61.19 ? 316 ARG A CB 1 ATOM 2270 C CG . ARG A 1 316 ? 21.133 -31.019 24.284 1.00 80.17 ? 316 ARG A CG 1 ATOM 2271 C CD . ARG A 1 316 ? 20.719 -29.999 23.201 1.00 82.75 ? 316 ARG A CD 1 ATOM 2272 N NE . ARG A 1 316 ? 19.344 -30.191 22.728 1.00 91.79 ? 316 ARG A NE 1 ATOM 2273 C CZ . ARG A 1 316 ? 18.937 -31.180 21.926 1.00 86.95 ? 316 ARG A CZ 1 ATOM 2274 N NH1 . ARG A 1 316 ? 19.797 -32.103 21.497 1.00 85.90 ? 316 ARG A NH1 1 ATOM 2275 N NH2 . ARG A 1 316 ? 17.658 -31.255 21.563 1.00 70.16 ? 316 ARG A NH2 1 ATOM 2276 N N . LEU A 1 317 ? 19.720 -32.788 28.745 1.00 69.56 ? 317 LEU A N 1 ATOM 2277 C CA . LEU A 1 317 ? 19.168 -32.567 30.075 1.00 67.47 ? 317 LEU A CA 1 ATOM 2278 C C . LEU A 1 317 ? 20.218 -31.882 30.943 1.00 64.03 ? 317 LEU A C 1 ATOM 2279 O O . LEU A 1 317 ? 21.242 -32.485 31.257 1.00 63.09 ? 317 LEU A O 1 ATOM 2280 C CB . LEU A 1 317 ? 18.758 -33.898 30.705 1.00 64.88 ? 317 LEU A CB 1 ATOM 2281 C CG . LEU A 1 317 ? 18.372 -33.887 32.185 1.00 51.78 ? 317 LEU A CG 1 ATOM 2282 C CD1 . LEU A 1 317 ? 17.163 -32.991 32.419 1.00 29.38 ? 317 LEU A CD1 1 ATOM 2283 C CD2 . LEU A 1 317 ? 18.103 -35.312 32.655 1.00 49.57 ? 317 LEU A CD2 1 ATOM 2284 N N . HIS A 1 318 ? 19.968 -30.621 31.310 1.00 68.62 ? 318 HIS A N 1 ATOM 2285 C CA . HIS A 1 318 ? 20.907 -29.837 32.114 1.00 60.45 ? 318 HIS A CA 1 ATOM 2286 C C . HIS A 1 318 ? 20.668 -30.100 33.590 1.00 64.37 ? 318 HIS A C 1 ATOM 2287 O O . HIS A 1 318 ? 19.568 -29.904 34.104 1.00 64.00 ? 318 HIS A O 1 ATOM 2288 C CB . HIS A 1 318 ? 20.825 -28.336 31.798 1.00 67.12 ? 318 HIS A CB 1 ATOM 2289 C CG . HIS A 1 318 ? 21.810 -27.496 32.564 1.00 99.75 ? 318 HIS A CG 1 ATOM 2290 N ND1 . HIS A 1 318 ? 21.438 -26.664 33.603 1.00 103.61 ? 318 HIS A ND1 1 ATOM 2291 C CD2 . HIS A 1 318 ? 23.154 -27.357 32.441 1.00 103.08 ? 318 HIS A CD2 1 ATOM 2292 C CE1 . HIS A 1 318 ? 22.506 -26.052 34.083 1.00 90.84 ? 318 HIS A CE1 1 ATOM 2293 N NE2 . HIS A 1 318 ? 23.561 -26.452 33.395 1.00 90.83 ? 318 HIS A NE2 1 ATOM 2294 N N . ILE A 1 319 ? 21.716 -30.568 34.255 1.00 62.42 ? 319 ILE A N 1 ATOM 2295 C CA . ILE A 1 319 ? 21.659 -30.936 35.654 1.00 52.54 ? 319 ILE A CA 1 ATOM 2296 C C . ILE A 1 319 ? 22.775 -30.180 36.354 1.00 55.84 ? 319 ILE A C 1 ATOM 2297 O O . ILE A 1 319 ? 23.930 -30.605 36.315 1.00 49.59 ? 319 ILE A O 1 ATOM 2298 C CB . ILE A 1 319 ? 21.861 -32.442 35.799 1.00 47.27 ? 319 ILE A CB 1 ATOM 2299 C CG1 . ILE A 1 319 ? 20.781 -33.178 35.012 1.00 53.89 ? 319 ILE A CG1 1 ATOM 2300 C CG2 . ILE A 1 319 ? 21.820 -32.857 37.243 1.00 53.94 ? 319 ILE A CG2 1 ATOM 2301 C CD1 . ILE A 1 319 ? 21.091 -34.627 34.748 1.00 56.41 ? 319 ILE A CD1 1 ATOM 2302 N N . PRO A 1 320 ? 22.425 -29.047 36.991 1.00 50.78 ? 320 PRO A N 1 ATOM 2303 C CA . PRO A 1 320 ? 23.355 -28.086 37.593 1.00 45.00 ? 320 PRO A CA 1 ATOM 2304 C C . PRO A 1 320 ? 24.504 -28.724 38.358 1.00 55.89 ? 320 PRO A C 1 ATOM 2305 O O . PRO A 1 320 ? 25.654 -28.331 38.149 1.00 66.19 ? 320 PRO A O 1 ATOM 2306 C CB . PRO A 1 320 ? 22.462 -27.286 38.542 1.00 41.21 ? 320 PRO A CB 1 ATOM 2307 C CG . PRO A 1 320 ? 21.119 -27.333 37.927 1.00 49.30 ? 320 PRO A CG 1 ATOM 2308 C CD . PRO A 1 320 ? 21.019 -28.672 37.232 1.00 55.35 ? 320 PRO A CD 1 ATOM 2309 N N . GLN A 1 321 ? 24.213 -29.669 39.243 1.00 56.36 ? 321 GLN A N 1 ATOM 2310 C CA . GLN A 1 321 ? 25.285 -30.305 40.000 1.00 63.04 ? 321 GLN A CA 1 ATOM 2311 C C . GLN A 1 321 ? 25.418 -31.738 39.550 1.00 62.79 ? 321 GLN A C 1 ATOM 2312 O O . GLN A 1 321 ? 25.370 -32.659 40.359 1.00 57.66 ? 321 GLN A O 1 ATOM 2313 C CB . GLN A 1 321 ? 25.009 -30.260 41.497 1.00 76.88 ? 321 GLN A CB 1 ATOM 2314 C CG . GLN A 1 321 ? 25.225 -28.914 42.148 1.00 87.24 ? 321 GLN A CG 1 ATOM 2315 C CD . GLN A 1 321 ? 24.630 -28.865 43.540 1.00 97.76 ? 321 GLN A CD 1 ATOM 2316 O OE1 . GLN A 1 321 ? 23.481 -29.272 43.746 1.00 99.97 ? 321 GLN A OE1 1 ATOM 2317 N NE2 . GLN A 1 321 ? 25.407 -28.368 44.506 1.00 92.16 ? 321 GLN A NE2 1 ATOM 2318 N N . PHE A 1 322 ? 25.590 -31.914 38.246 1.00 64.43 ? 322 PHE A N 1 ATOM 2319 C CA . PHE A 1 322 ? 25.576 -33.228 37.632 1.00 49.22 ? 322 PHE A CA 1 ATOM 2320 C C . PHE A 1 322 ? 26.441 -34.243 38.392 1.00 59.42 ? 322 PHE A C 1 ATOM 2321 O O . PHE A 1 322 ? 26.068 -35.412 38.493 1.00 66.41 ? 322 PHE A O 1 ATOM 2322 C CB . PHE A 1 322 ? 26.006 -33.121 36.175 1.00 36.32 ? 322 PHE A CB 1 ATOM 2323 C CG . PHE A 1 322 ? 27.491 -33.084 35.984 1.00 49.27 ? 322 PHE A CG 1 ATOM 2324 C CD1 . PHE A 1 322 ? 28.205 -34.249 35.745 1.00 56.15 ? 322 PHE A CD1 1 ATOM 2325 C CD2 . PHE A 1 322 ? 28.178 -31.892 36.051 1.00 51.64 ? 322 PHE A CD2 1 ATOM 2326 C CE1 . PHE A 1 322 ? 29.579 -34.218 35.586 1.00 56.79 ? 322 PHE A CE1 1 ATOM 2327 C CE2 . PHE A 1 322 ? 29.554 -31.858 35.888 1.00 58.75 ? 322 PHE A CE2 1 ATOM 2328 C CZ . PHE A 1 322 ? 30.253 -33.017 35.659 1.00 54.78 ? 322 PHE A CZ 1 ATOM 2329 N N . TYR A 1 323 ? 27.572 -33.791 38.940 1.00 48.26 ? 323 TYR A N 1 ATOM 2330 C CA . TYR A 1 323 ? 28.551 -34.677 39.590 1.00 57.06 ? 323 TYR A CA 1 ATOM 2331 C C . TYR A 1 323 ? 28.061 -35.282 40.908 1.00 68.88 ? 323 TYR A C 1 ATOM 2332 O O . TYR A 1 323 ? 28.632 -36.253 41.406 1.00 76.16 ? 323 TYR A O 1 ATOM 2333 C CB . TYR A 1 323 ? 29.900 -33.958 39.799 1.00 59.23 ? 323 TYR A CB 1 ATOM 2334 C CG . TYR A 1 323 ? 29.847 -32.830 40.809 1.00 57.70 ? 323 TYR A CG 1 ATOM 2335 C CD1 . TYR A 1 323 ? 30.430 -32.959 42.059 1.00 70.50 ? 323 TYR A CD1 1 ATOM 2336 C CD2 . TYR A 1 323 ? 29.199 -31.644 40.516 1.00 47.03 ? 323 TYR A CD2 1 ATOM 2337 C CE1 . TYR A 1 323 ? 30.370 -31.927 42.989 1.00 69.36 ? 323 TYR A CE1 1 ATOM 2338 C CE2 . TYR A 1 323 ? 29.127 -30.624 41.427 1.00 51.90 ? 323 TYR A CE2 1 ATOM 2339 C CZ . TYR A 1 323 ? 29.713 -30.763 42.666 1.00 62.50 ? 323 TYR A CZ 1 ATOM 2340 O OH . TYR A 1 323 ? 29.639 -29.727 43.577 1.00 64.42 ? 323 TYR A OH 1 ATOM 2341 N N . LEU A 1 324 ? 26.997 -34.715 41.464 1.00 66.82 ? 324 LEU A N 1 ATOM 2342 C CA . LEU A 1 324 ? 26.475 -35.169 42.746 1.00 63.55 ? 324 LEU A CA 1 ATOM 2343 C C . LEU A 1 324 ? 25.317 -36.125 42.544 1.00 64.89 ? 324 LEU A C 1 ATOM 2344 O O . LEU A 1 324 ? 24.565 -36.412 43.462 1.00 70.47 ? 324 LEU A O 1 ATOM 2345 C CB . LEU A 1 324 ? 26.002 -33.975 43.571 1.00 57.71 ? 324 LEU A CB 1 ATOM 2346 C CG . LEU A 1 324 ? 27.040 -32.946 44.023 1.00 61.10 ? 324 LEU A CG 1 ATOM 2347 C CD1 . LEU A 1 324 ? 26.390 -31.909 44.914 1.00 35.70 ? 324 LEU A CD1 1 ATOM 2348 C CD2 . LEU A 1 324 ? 28.198 -33.621 44.740 1.00 48.10 ? 324 LEU A CD2 1 ATOM 2349 N N . PHE A 1 325 ? 25.167 -36.617 41.328 1.00 63.53 ? 325 PHE A N 1 ATOM 2350 C CA . PHE A 1 325 ? 23.984 -37.393 40.991 1.00 67.60 ? 325 PHE A CA 1 ATOM 2351 C C . PHE A 1 325 ? 23.942 -38.711 41.747 1.00 69.73 ? 325 PHE A C 1 ATOM 2352 O O . PHE A 1 325 ? 24.968 -39.363 41.937 1.00 75.04 ? 325 PHE A O 1 ATOM 2353 C CB . PHE A 1 325 ? 23.899 -37.628 39.478 1.00 54.39 ? 325 PHE A CB 1 ATOM 2354 C CG . PHE A 1 325 ? 22.500 -37.600 38.946 1.00 48.42 ? 325 PHE A CG 1 ATOM 2355 C CD1 . PHE A 1 325 ? 21.887 -36.389 38.640 1.00 43.20 ? 325 PHE A CD1 1 ATOM 2356 C CD2 . PHE A 1 325 ? 21.788 -38.774 38.768 1.00 55.55 ? 325 PHE A CD2 1 ATOM 2357 C CE1 . PHE A 1 325 ? 20.605 -36.348 38.163 1.00 43.97 ? 325 PHE A CE1 1 ATOM 2358 C CE2 . PHE A 1 325 ? 20.495 -38.740 38.288 1.00 62.22 ? 325 PHE A CE2 1 ATOM 2359 C CZ . PHE A 1 325 ? 19.903 -37.526 37.987 1.00 56.80 ? 325 PHE A CZ 1 ATOM 2360 N N . TYR A 1 326 ? 22.745 -39.094 42.173 1.00 68.36 ? 326 TYR A N 1 ATOM 2361 C CA . TYR A 1 326 ? 22.562 -40.308 42.953 1.00 71.24 ? 326 TYR A CA 1 ATOM 2362 C C . TYR A 1 326 ? 22.657 -41.607 42.144 1.00 74.50 ? 326 TYR A C 1 ATOM 2363 O O . TYR A 1 326 ? 22.757 -41.609 40.913 1.00 47.89 ? 326 TYR A O 1 ATOM 2364 C CB . TYR A 1 326 ? 21.237 -40.278 43.722 1.00 65.60 ? 326 TYR A CB 1 ATOM 2365 C CG . TYR A 1 326 ? 21.230 -39.369 44.936 1.00 73.69 ? 326 TYR A CG 1 ATOM 2366 C CD1 . TYR A 1 326 ? 20.650 -38.115 44.880 1.00 83.88 ? 326 TYR A CD1 1 ATOM 2367 C CD2 . TYR A 1 326 ? 21.795 -39.767 46.139 1.00 72.52 ? 326 TYR A CD2 1 ATOM 2368 C CE1 . TYR A 1 326 ? 20.638 -37.280 45.979 1.00 74.39 ? 326 TYR A CE1 1 ATOM 2369 C CE2 . TYR A 1 326 ? 21.782 -38.935 47.247 1.00 71.34 ? 326 TYR A CE2 1 ATOM 2370 C CZ . TYR A 1 326 ? 21.197 -37.693 47.155 1.00 69.90 ? 326 TYR A CZ 1 ATOM 2371 O OH . TYR A 1 326 ? 21.158 -36.840 48.232 1.00 78.39 ? 326 TYR A OH 1 ATOM 2372 N N . ASP A 1 327 ? 22.623 -42.704 42.897 1.00 85.60 ? 327 ASP A N 1 ATOM 2373 C CA . ASP A 1 327 ? 22.710 -44.081 42.426 1.00 73.21 ? 327 ASP A CA 1 ATOM 2374 C C . ASP A 1 327 ? 21.749 -44.369 41.289 1.00 71.97 ? 327 ASP A C 1 ATOM 2375 O O . ASP A 1 327 ? 21.999 -45.242 40.442 1.00 53.75 ? 327 ASP A O 1 ATOM 2376 C CB . ASP A 1 327 ? 22.331 -44.982 43.593 1.00 71.85 ? 327 ASP A CB 1 ATOM 2377 C CG . ASP A 1 327 ? 22.894 -46.347 43.461 1.00 91.42 ? 327 ASP A CG 1 ATOM 2378 O OD1 . ASP A 1 327 ? 23.343 -46.681 42.345 1.00 99.73 ? 327 ASP A OD1 1 ATOM 2379 O OD2 . ASP A 1 327 ? 22.900 -47.080 44.472 1.00 104.37 ? 327 ASP A OD2 1 ATOM 2380 N N . LEU A 1 328 ? 20.629 -43.646 41.313 1.00 75.94 ? 328 LEU A N 1 ATOM 2381 C CA . LEU A 1 328 ? 19.539 -43.840 40.375 1.00 61.02 ? 328 LEU A CA 1 ATOM 2382 C C . LEU A 1 328 ? 18.957 -45.234 40.550 1.00 68.84 ? 328 LEU A C 1 ATOM 2383 O O . LEU A 1 328 ? 18.460 -45.823 39.602 1.00 82.13 ? 328 LEU A O 1 ATOM 2384 C CB . LEU A 1 328 ? 20.039 -43.637 38.946 1.00 45.76 ? 328 LEU A CB 1 ATOM 2385 C CG . LEU A 1 328 ? 19.028 -43.190 37.903 1.00 47.69 ? 328 LEU A CG 1 ATOM 2386 C CD1 . LEU A 1 328 ? 18.168 -42.010 38.383 1.00 41.21 ? 328 LEU A CD1 1 ATOM 2387 C CD2 . LEU A 1 328 ? 19.771 -42.849 36.637 1.00 56.31 ? 328 LEU A CD2 1 ATOM 2388 N N . SER A 1 329 ? 19.007 -45.749 41.773 1.00 73.00 ? 329 SER A N 1 ATOM 2389 C CA . SER A 1 329 ? 18.618 -47.129 42.056 1.00 72.94 ? 329 SER A CA 1 ATOM 2390 C C . SER A 1 329 ? 17.160 -47.258 42.476 1.00 75.43 ? 329 SER A C 1 ATOM 2391 O O . SER A 1 329 ? 16.634 -48.365 42.624 1.00 75.55 ? 329 SER A O 1 ATOM 2392 C CB . SER A 1 329 ? 19.487 -47.689 43.170 1.00 65.20 ? 329 SER A CB 1 ATOM 2393 O OG . SER A 1 329 ? 19.025 -47.206 44.407 1.00 61.74 ? 329 SER A OG 1 ATOM 2394 N N . THR A 1 330 ? 16.516 -46.120 42.685 1.00 72.32 ? 330 THR A N 1 ATOM 2395 C CA . THR A 1 330 ? 15.107 -46.102 43.027 1.00 71.58 ? 330 THR A CA 1 ATOM 2396 C C . THR A 1 330 ? 14.242 -46.411 41.809 1.00 79.59 ? 330 THR A C 1 ATOM 2397 O O . THR A 1 330 ? 13.040 -46.625 41.936 1.00 92.88 ? 330 THR A O 1 ATOM 2398 C CB . THR A 1 330 ? 14.718 -44.748 43.610 1.00 65.97 ? 330 THR A CB 1 ATOM 2399 O OG1 . THR A 1 330 ? 15.387 -43.708 42.882 1.00 68.82 ? 330 THR A OG1 1 ATOM 2400 C CG2 . THR A 1 330 ? 15.144 -44.670 45.055 1.00 48.46 ? 330 THR A CG2 1 ATOM 2401 N N . VAL A 1 331 ? 14.862 -46.437 40.630 1.00 69.72 ? 331 VAL A N 1 ATOM 2402 C CA . VAL A 1 331 ? 14.162 -46.797 39.395 1.00 70.48 ? 331 VAL A CA 1 ATOM 2403 C C . VAL A 1 331 ? 14.724 -48.045 38.698 1.00 69.85 ? 331 VAL A C 1 ATOM 2404 O O . VAL A 1 331 ? 14.458 -48.250 37.512 1.00 78.11 ? 331 VAL A O 1 ATOM 2405 C CB . VAL A 1 331 ? 14.102 -45.614 38.355 1.00 58.04 ? 331 VAL A CB 1 ATOM 2406 C CG1 . VAL A 1 331 ? 13.336 -44.425 38.913 1.00 55.24 ? 331 VAL A CG1 1 ATOM 2407 C CG2 . VAL A 1 331 ? 15.499 -45.195 37.885 1.00 45.95 ? 331 VAL A CG2 1 ATOM 2408 N N . TYR A 1 332 ? 15.487 -48.875 39.412 1.00 66.76 ? 332 TYR A N 1 ATOM 2409 C CA . TYR A 1 332 ? 16.099 -50.051 38.786 1.00 69.36 ? 332 TYR A CA 1 ATOM 2410 C C . TYR A 1 332 ? 15.054 -51.080 38.415 1.00 76.03 ? 332 TYR A C 1 ATOM 2411 O O . TYR A 1 332 ? 15.230 -51.847 37.468 1.00 72.31 ? 332 TYR A O 1 ATOM 2412 C CB . TYR A 1 332 ? 17.107 -50.730 39.697 1.00 67.11 ? 332 TYR A CB 1 ATOM 2413 C CG . TYR A 1 332 ? 18.402 -50.000 39.866 1.00 69.05 ? 332 TYR A CG 1 ATOM 2414 C CD1 . TYR A 1 332 ? 18.714 -48.914 39.074 1.00 67.46 ? 332 TYR A CD1 1 ATOM 2415 C CD2 . TYR A 1 332 ? 19.337 -50.423 40.808 1.00 66.78 ? 332 TYR A CD2 1 ATOM 2416 C CE1 . TYR A 1 332 ? 19.916 -48.241 39.240 1.00 73.83 ? 332 TYR A CE1 1 ATOM 2417 C CE2 . TYR A 1 332 ? 20.542 -49.765 40.972 1.00 62.28 ? 332 TYR A CE2 1 ATOM 2418 C CZ . TYR A 1 332 ? 20.823 -48.669 40.192 1.00 64.21 ? 332 TYR A CZ 1 ATOM 2419 O OH . TYR A 1 332 ? 22.013 -48.007 40.349 1.00 59.07 ? 332 TYR A OH 1 ATOM 2420 N N . SER A 1 333 ? 13.971 -51.102 39.180 1.00 76.35 ? 333 SER A N 1 ATOM 2421 C CA . SER A 1 333 ? 12.893 -52.042 38.937 1.00 77.13 ? 333 SER A CA 1 ATOM 2422 C C . SER A 1 333 ? 11.934 -51.526 37.866 1.00 80.30 ? 333 SER A C 1 ATOM 2423 O O . SER A 1 333 ? 11.480 -52.276 37.014 1.00 81.09 ? 333 SER A O 1 ATOM 2424 C CB . SER A 1 333 ? 12.156 -52.320 40.242 1.00 75.01 ? 333 SER A CB 1 ATOM 2425 O OG . SER A 1 333 ? 13.074 -52.752 41.231 1.00 70.59 ? 333 SER A OG 1 ATOM 2426 N N . LEU A 1 334 ? 11.647 -50.232 37.923 1.00 86.14 ? 334 LEU A N 1 ATOM 2427 C CA . LEU A 1 334 ? 10.757 -49.548 36.991 1.00 79.85 ? 334 LEU A CA 1 ATOM 2428 C C . LEU A 1 334 ? 11.130 -49.769 35.529 1.00 86.70 ? 334 LEU A C 1 ATOM 2429 O O . LEU A 1 334 ? 10.269 -49.734 34.647 1.00 89.93 ? 334 LEU A O 1 ATOM 2430 C CB . LEU A 1 334 ? 10.821 -48.049 37.285 1.00 80.02 ? 334 LEU A CB 1 ATOM 2431 C CG . LEU A 1 334 ? 9.722 -47.109 36.817 1.00 76.79 ? 334 LEU A CG 1 ATOM 2432 C CD1 . LEU A 1 334 ? 8.428 -47.507 37.478 1.00 82.12 ? 334 LEU A CD1 1 ATOM 2433 C CD2 . LEU A 1 334 ? 10.100 -45.684 37.175 1.00 64.34 ? 334 LEU A CD2 1 ATOM 2434 N N . LEU A 1 335 ? 12.416 -49.988 35.274 1.00 86.86 ? 335 LEU A N 1 ATOM 2435 C CA . LEU A 1 335 ? 12.936 -49.985 33.906 1.00 82.31 ? 335 LEU A CA 1 ATOM 2436 C C . LEU A 1 335 ? 13.371 -51.358 33.366 1.00 82.66 ? 335 LEU A C 1 ATOM 2437 O O . LEU A 1 335 ? 14.068 -51.441 32.351 1.00 67.74 ? 335 LEU A O 1 ATOM 2438 C CB . LEU A 1 335 ? 14.101 -48.999 33.811 1.00 68.32 ? 335 LEU A CB 1 ATOM 2439 C CG . LEU A 1 335 ? 13.829 -47.624 34.414 1.00 64.80 ? 335 LEU A CG 1 ATOM 2440 C CD1 . LEU A 1 335 ? 15.089 -46.783 34.428 1.00 62.51 ? 335 LEU A CD1 1 ATOM 2441 C CD2 . LEU A 1 335 ? 12.732 -46.922 33.644 1.00 64.99 ? 335 LEU A CD2 1 ATOM 2442 N N . GLU A 1 336 ? 12.964 -52.430 34.039 1.00 92.61 ? 336 GLU A N 1 ATOM 2443 C CA . GLU A 1 336 ? 13.386 -53.777 33.654 1.00 92.63 ? 336 GLU A CA 1 ATOM 2444 C C . GLU A 1 336 ? 12.854 -54.170 32.284 1.00 85.27 ? 336 GLU A C 1 ATOM 2445 O O . GLU A 1 336 ? 13.394 -55.056 31.626 1.00 73.70 ? 336 GLU A O 1 ATOM 2446 C CB . GLU A 1 336 ? 12.955 -54.811 34.701 1.00 100.64 ? 336 GLU A CB 1 ATOM 2447 C CG . GLU A 1 336 ? 13.803 -54.809 35.964 1.00 110.42 ? 336 GLU A CG 1 ATOM 2448 C CD . GLU A 1 336 ? 13.624 -56.066 36.797 1.00 120.43 ? 336 GLU A CD 1 ATOM 2449 O OE1 . GLU A 1 336 ? 12.867 -56.965 36.366 1.00 124.57 ? 336 GLU A OE1 1 ATOM 2450 O OE2 . GLU A 1 336 ? 14.245 -56.152 37.881 1.00 117.47 ? 336 GLU A OE2 1 ATOM 2451 N N . LYS A 1 337 ? 11.803 -53.483 31.855 1.00 95.15 ? 337 LYS A N 1 ATOM 2452 C CA . LYS A 1 337 ? 11.082 -53.846 30.645 1.00 89.44 ? 337 LYS A CA 1 ATOM 2453 C C . LYS A 1 337 ? 11.451 -52.976 29.420 1.00 78.40 ? 337 LYS A C 1 ATOM 2454 O O . LYS A 1 337 ? 11.349 -53.441 28.290 1.00 77.46 ? 337 LYS A O 1 ATOM 2455 C CB . LYS A 1 337 ? 9.570 -53.873 30.935 1.00 96.93 ? 337 LYS A CB 1 ATOM 2456 C CG . LYS A 1 337 ? 8.662 -53.894 29.715 1.00 118.16 ? 337 LYS A CG 1 ATOM 2457 C CD . LYS A 1 337 ? 8.156 -52.494 29.330 1.00 120.06 ? 337 LYS A CD 1 ATOM 2458 C CE . LYS A 1 337 ? 7.621 -52.465 27.887 1.00 110.75 ? 337 LYS A CE 1 ATOM 2459 N NZ . LYS A 1 337 ? 6.700 -53.594 27.534 1.00 97.44 ? 337 LYS A NZ 1 ATOM 2460 N N . VAL A 1 338 ? 11.916 -51.744 29.635 1.00 67.19 ? 338 VAL A N 1 ATOM 2461 C CA . VAL A 1 338 ? 12.273 -50.853 28.510 1.00 65.74 ? 338 VAL A CA 1 ATOM 2462 C C . VAL A 1 338 ? 13.366 -51.390 27.555 1.00 68.56 ? 338 VAL A C 1 ATOM 2463 O O . VAL A 1 338 ? 14.309 -52.048 27.981 1.00 78.04 ? 338 VAL A O 1 ATOM 2464 C CB . VAL A 1 338 ? 12.546 -49.369 28.981 1.00 55.70 ? 338 VAL A CB 1 ATOM 2465 C CG1 . VAL A 1 338 ? 12.867 -49.320 30.441 1.00 59.54 ? 338 VAL A CG1 1 ATOM 2466 C CG2 . VAL A 1 338 ? 13.640 -48.694 28.163 1.00 57.04 ? 338 VAL A CG2 1 ATOM 2467 N N . LYS A 1 339 ? 13.221 -51.100 26.262 1.00 73.00 ? 339 LYS A N 1 ATOM 2468 C CA . LYS A 1 339 ? 14.068 -51.687 25.215 1.00 68.87 ? 339 LYS A CA 1 ATOM 2469 C C . LYS A 1 339 ? 15.024 -50.711 24.516 1.00 66.25 ? 339 LYS A C 1 ATOM 2470 O O . LYS A 1 339 ? 16.085 -51.123 24.052 1.00 66.96 ? 339 LYS A O 1 ATOM 2471 C CB . LYS A 1 339 ? 13.207 -52.377 24.151 1.00 59.72 ? 339 LYS A CB 1 ATOM 2472 C CG . LYS A 1 339 ? 12.328 -53.491 24.671 1.00 61.72 ? 339 LYS A CG 1 ATOM 2473 C CD . LYS A 1 339 ? 11.575 -54.195 23.545 1.00 64.67 ? 339 LYS A CD 1 ATOM 2474 C CE . LYS A 1 339 ? 11.148 -55.595 23.979 1.00 75.92 ? 339 LYS A CE 1 ATOM 2475 N NZ . LYS A 1 339 ? 12.204 -56.273 24.818 1.00 76.17 ? 339 LYS A NZ 1 ATOM 2476 N N . ARG A 1 340 ? 14.640 -49.439 24.399 1.00 60.96 ? 340 ARG A N 1 ATOM 2477 C CA . ARG A 1 340 ? 15.544 -48.419 23.852 1.00 57.59 ? 340 ARG A CA 1 ATOM 2478 C C . ARG A 1 340 ? 15.683 -47.213 24.791 1.00 56.73 ? 340 ARG A C 1 ATOM 2479 O O . ARG A 1 340 ? 14.690 -46.550 25.112 1.00 56.80 ? 340 ARG A O 1 ATOM 2480 C CB . ARG A 1 340 ? 15.109 -47.942 22.457 1.00 55.31 ? 340 ARG A CB 1 ATOM 2481 C CG . ARG A 1 340 ? 14.196 -48.891 21.673 1.00 75.62 ? 340 ARG A CG 1 ATOM 2482 C CD . ARG A 1 340 ? 14.576 -48.980 20.178 1.00 82.01 ? 340 ARG A CD 1 ATOM 2483 N NE . ARG A 1 340 ? 15.150 -47.735 19.666 1.00 88.51 ? 340 ARG A NE 1 ATOM 2484 C CZ . ARG A 1 340 ? 16.046 -47.667 18.682 1.00 83.47 ? 340 ARG A CZ 1 ATOM 2485 N NH1 . ARG A 1 340 ? 16.480 -48.782 18.094 1.00 71.21 ? 340 ARG A NH1 1 ATOM 2486 N NH2 . ARG A 1 340 ? 16.517 -46.480 18.292 1.00 76.59 ? 340 ARG A NH2 1 ATOM 2487 N N . ILE A 1 341 ? 16.915 -46.946 25.233 1.00 40.60 ? 341 ILE A N 1 ATOM 2488 C CA . ILE A 1 341 ? 17.216 -45.771 26.035 1.00 50.42 ? 341 ILE A CA 1 ATOM 2489 C C . ILE A 1 341 ? 18.200 -44.862 25.299 1.00 55.03 ? 341 ILE A C 1 ATOM 2490 O O . ILE A 1 341 ? 19.218 -45.326 24.773 1.00 42.78 ? 341 ILE A O 1 ATOM 2491 C CB . ILE A 1 341 ? 17.797 -46.151 27.432 1.00 53.23 ? 341 ILE A CB 1 ATOM 2492 C CG1 . ILE A 1 341 ? 16.747 -46.880 28.268 1.00 54.66 ? 341 ILE A CG1 1 ATOM 2493 C CG2 . ILE A 1 341 ? 18.321 -44.906 28.187 1.00 37.42 ? 341 ILE A CG2 1 ATOM 2494 C CD1 . ILE A 1 341 ? 17.219 -47.226 29.660 1.00 53.01 ? 341 ILE A CD1 1 ATOM 2495 N N . THR A 1 342 ? 17.881 -43.570 25.255 1.00 56.96 ? 342 THR A N 1 ATOM 2496 C CA . THR A 1 342 ? 18.802 -42.562 24.741 1.00 57.98 ? 342 THR A CA 1 ATOM 2497 C C . THR A 1 342 ? 19.033 -41.502 25.807 1.00 64.28 ? 342 THR A C 1 ATOM 2498 O O . THR A 1 342 ? 18.094 -40.926 26.357 1.00 67.75 ? 342 THR A O 1 ATOM 2499 C CB . THR A 1 342 ? 18.270 -41.851 23.470 1.00 68.43 ? 342 THR A CB 1 ATOM 2500 O OG1 . THR A 1 342 ? 18.142 -42.781 22.387 1.00 69.46 ? 342 THR A OG1 1 ATOM 2501 C CG2 . THR A 1 342 ? 19.218 -40.743 23.056 1.00 59.69 ? 342 THR A CG2 1 ATOM 2502 N N . VAL A 1 343 ? 20.296 -41.251 26.104 1.00 65.08 ? 343 VAL A N 1 ATOM 2503 C CA . VAL A 1 343 ? 20.656 -40.214 27.045 1.00 55.68 ? 343 VAL A CA 1 ATOM 2504 C C . VAL A 1 343 ? 21.853 -39.516 26.459 1.00 60.55 ? 343 VAL A C 1 ATOM 2505 O O . VAL A 1 343 ? 22.999 -39.912 26.674 1.00 61.31 ? 343 VAL A O 1 ATOM 2506 C CB . VAL A 1 343 ? 21.001 -40.793 28.400 1.00 50.20 ? 343 VAL A CB 1 ATOM 2507 C CG1 . VAL A 1 343 ? 20.750 -39.743 29.488 1.00 46.16 ? 343 VAL A CG1 1 ATOM 2508 C CG2 . VAL A 1 343 ? 20.172 -42.057 28.642 1.00 46.69 ? 343 VAL A CG2 1 ATOM 2509 N N . GLU A 1 344 ? 21.557 -38.482 25.687 1.00 67.49 ? 344 GLU A N 1 ATOM 2510 C CA . GLU A 1 344 ? 22.546 -37.800 24.875 1.00 71.82 ? 344 GLU A CA 1 ATOM 2511 C C . GLU A 1 344 ? 22.868 -36.408 25.420 1.00 63.32 ? 344 GLU A C 1 ATOM 2512 O O . GLU A 1 344 ? 21.970 -35.663 25.824 1.00 51.89 ? 344 GLU A O 1 ATOM 2513 C CB . GLU A 1 344 ? 22.035 -37.689 23.440 1.00 73.64 ? 344 GLU A CB 1 ATOM 2514 C CG . GLU A 1 344 ? 22.795 -36.688 22.597 1.00 81.42 ? 344 GLU A CG 1 ATOM 2515 C CD . GLU A 1 344 ? 21.931 -36.084 21.527 1.00 85.34 ? 344 GLU A CD 1 ATOM 2516 O OE1 . GLU A 1 344 ? 21.712 -34.847 21.568 1.00 86.53 ? 344 GLU A OE1 1 ATOM 2517 O OE2 . GLU A 1 344 ? 21.456 -36.853 20.663 1.00 85.73 ? 344 GLU A OE2 1 ATOM 2518 N N . ASN A 1 345 ? 24.155 -36.069 25.428 1.00 50.63 ? 345 ASN A N 1 ATOM 2519 C CA . ASN A 1 345 ? 24.593 -34.754 25.855 1.00 58.75 ? 345 ASN A CA 1 ATOM 2520 C C . ASN A 1 345 ? 23.956 -34.305 27.172 1.00 59.63 ? 345 ASN A C 1 ATOM 2521 O O . ASN A 1 345 ? 23.323 -33.253 27.233 1.00 64.16 ? 345 ASN A O 1 ATOM 2522 C CB . ASN A 1 345 ? 24.294 -33.741 24.754 1.00 62.88 ? 345 ASN A CB 1 ATOM 2523 C CG . ASN A 1 345 ? 25.085 -32.469 24.904 1.00 64.96 ? 345 ASN A CG 1 ATOM 2524 O OD1 . ASN A 1 345 ? 25.936 -32.343 25.782 1.00 68.78 ? 345 ASN A OD1 1 ATOM 2525 N ND2 . ASN A 1 345 ? 24.818 -31.516 24.033 1.00 71.22 ? 345 ASN A ND2 1 ATOM 2526 N N . SER A 1 346 ? 24.128 -35.111 28.215 1.00 54.51 ? 346 SER A N 1 ATOM 2527 C CA . SER A 1 346 ? 23.579 -34.817 29.535 1.00 56.00 ? 346 SER A CA 1 ATOM 2528 C C . SER A 1 346 ? 24.633 -35.004 30.618 1.00 65.70 ? 346 SER A C 1 ATOM 2529 O O . SER A 1 346 ? 24.335 -34.965 31.817 1.00 66.69 ? 346 SER A O 1 ATOM 2530 C CB . SER A 1 346 ? 22.379 -35.704 29.839 1.00 49.42 ? 346 SER A CB 1 ATOM 2531 O OG . SER A 1 346 ? 21.283 -35.357 29.025 1.00 60.52 ? 346 SER A OG 1 ATOM 2532 N N . LYS A 1 347 ? 25.869 -35.206 30.184 1.00 59.01 ? 347 LYS A N 1 ATOM 2533 C CA . LYS A 1 347 ? 26.988 -35.296 31.105 1.00 55.17 ? 347 LYS A CA 1 ATOM 2534 C C . LYS A 1 347 ? 27.015 -36.635 31.819 1.00 49.37 ? 347 LYS A C 1 ATOM 2535 O O . LYS A 1 347 ? 27.488 -36.724 32.942 1.00 45.94 ? 347 LYS A O 1 ATOM 2536 C CB . LYS A 1 347 ? 26.950 -34.153 32.133 1.00 54.24 ? 347 LYS A CB 1 ATOM 2537 C CG . LYS A 1 347 ? 26.978 -32.739 31.544 1.00 43.59 ? 347 LYS A CG 1 ATOM 2538 C CD . LYS A 1 347 ? 27.830 -31.818 32.409 1.00 53.93 ? 347 LYS A CD 1 ATOM 2539 C CE . LYS A 1 347 ? 27.663 -30.356 32.042 1.00 53.73 ? 347 LYS A CE 1 ATOM 2540 N NZ . LYS A 1 347 ? 28.513 -29.537 32.923 1.00 48.33 ? 347 LYS A NZ 1 ATOM 2541 N N . VAL A 1 348 ? 26.510 -37.677 31.170 1.00 49.72 ? 348 VAL A N 1 ATOM 2542 C CA . VAL A 1 348 ? 26.558 -39.015 31.752 1.00 55.46 ? 348 VAL A CA 1 ATOM 2543 C C . VAL A 1 348 ? 28.001 -39.464 31.908 1.00 54.81 ? 348 VAL A C 1 ATOM 2544 O O . VAL A 1 348 ? 28.761 -39.445 30.946 1.00 55.38 ? 348 VAL A O 1 ATOM 2545 C CB . VAL A 1 348 ? 25.802 -40.030 30.880 1.00 52.61 ? 348 VAL A CB 1 ATOM 2546 C CG1 . VAL A 1 348 ? 25.697 -41.390 31.578 1.00 40.73 ? 348 VAL A CG1 1 ATOM 2547 C CG2 . VAL A 1 348 ? 24.430 -39.486 30.532 1.00 54.88 ? 348 VAL A CG2 1 ATOM 2548 N N . PHE A 1 349 ? 28.387 -39.860 33.115 1.00 54.03 ? 349 PHE A N 1 ATOM 2549 C CA . PHE A 1 349 ? 29.765 -40.281 33.338 1.00 55.02 ? 349 PHE A CA 1 ATOM 2550 C C . PHE A 1 349 ? 29.865 -41.678 33.902 1.00 61.03 ? 349 PHE A C 1 ATOM 2551 O O . PHE A 1 349 ? 30.963 -42.189 34.073 1.00 64.14 ? 349 PHE A O 1 ATOM 2552 C CB . PHE A 1 349 ? 30.499 -39.317 34.262 1.00 54.17 ? 349 PHE A CB 1 ATOM 2553 C CG . PHE A 1 349 ? 29.913 -39.236 35.638 1.00 51.11 ? 349 PHE A CG 1 ATOM 2554 C CD1 . PHE A 1 349 ? 30.238 -40.182 36.604 1.00 54.35 ? 349 PHE A CD1 1 ATOM 2555 C CD2 . PHE A 1 349 ? 29.041 -38.210 35.971 1.00 51.79 ? 349 PHE A CD2 1 ATOM 2556 C CE1 . PHE A 1 349 ? 29.702 -40.112 37.887 1.00 52.86 ? 349 PHE A CE1 1 ATOM 2557 C CE2 . PHE A 1 349 ? 28.498 -38.128 37.245 1.00 65.67 ? 349 PHE A CE2 1 ATOM 2558 C CZ . PHE A 1 349 ? 28.831 -39.083 38.209 1.00 59.94 ? 349 PHE A CZ 1 ATOM 2559 N N . LEU A 1 350 ? 28.725 -42.293 34.199 1.00 66.36 ? 350 LEU A N 1 ATOM 2560 C CA . LEU A 1 350 ? 28.715 -43.680 34.652 1.00 61.98 ? 350 LEU A CA 1 ATOM 2561 C C . LEU A 1 350 ? 27.314 -44.253 34.715 1.00 62.61 ? 350 LEU A C 1 ATOM 2562 O O . LEU A 1 350 ? 26.437 -43.652 35.309 1.00 74.24 ? 350 LEU A O 1 ATOM 2563 C CB . LEU A 1 350 ? 29.343 -43.795 36.038 1.00 55.21 ? 350 LEU A CB 1 ATOM 2564 C CG . LEU A 1 350 ? 29.120 -45.166 36.674 1.00 52.72 ? 350 LEU A CG 1 ATOM 2565 C CD1 . LEU A 1 350 ? 30.146 -46.146 36.168 1.00 49.18 ? 350 LEU A CD1 1 ATOM 2566 C CD2 . LEU A 1 350 ? 29.157 -45.080 38.181 1.00 51.91 ? 350 LEU A CD2 1 ATOM 2567 N N . VAL A 1 351 ? 27.098 -45.413 34.107 1.00 61.90 ? 351 VAL A N 1 ATOM 2568 C CA . VAL A 1 351 ? 25.879 -46.175 34.378 1.00 67.71 ? 351 VAL A CA 1 ATOM 2569 C C . VAL A 1 351 ? 26.256 -47.266 35.362 1.00 65.26 ? 351 VAL A C 1 ATOM 2570 O O . VAL A 1 351 ? 26.877 -48.253 34.979 1.00 64.88 ? 351 VAL A O 1 ATOM 2571 C CB . VAL A 1 351 ? 25.254 -46.832 33.110 1.00 68.84 ? 351 VAL A CB 1 ATOM 2572 C CG1 . VAL A 1 351 ? 23.971 -47.568 33.477 1.00 62.98 ? 351 VAL A CG1 1 ATOM 2573 C CG2 . VAL A 1 351 ? 24.978 -45.797 32.014 1.00 66.13 ? 351 VAL A CG2 1 ATOM 2574 N N . PRO A 1 352 ? 25.899 -47.081 36.640 1.00 64.10 ? 352 PRO A N 1 ATOM 2575 C CA . PRO A 1 352 ? 26.242 -48.031 37.703 1.00 61.19 ? 352 PRO A CA 1 ATOM 2576 C C . PRO A 1 352 ? 25.915 -49.476 37.333 1.00 68.71 ? 352 PRO A C 1 ATOM 2577 O O . PRO A 1 352 ? 24.794 -49.774 36.928 1.00 66.29 ? 352 PRO A O 1 ATOM 2578 C CB . PRO A 1 352 ? 25.368 -47.573 38.869 1.00 49.10 ? 352 PRO A CB 1 ATOM 2579 C CG . PRO A 1 352 ? 25.222 -46.126 38.650 1.00 53.43 ? 352 PRO A CG 1 ATOM 2580 C CD . PRO A 1 352 ? 25.113 -45.950 37.158 1.00 58.77 ? 352 PRO A CD 1 ATOM 2581 N N . CYS A 1 353 ? 26.906 -50.351 37.486 1.00 72.33 ? 353 CYS A N 1 ATOM 2582 C CA . CYS A 1 353 ? 26.770 -51.774 37.215 1.00 65.53 ? 353 CYS A CA 1 ATOM 2583 C C . CYS A 1 353 ? 25.418 -52.374 37.611 1.00 67.39 ? 353 CYS A C 1 ATOM 2584 O O . CYS A 1 353 ? 24.804 -53.090 36.819 1.00 62.74 ? 353 CYS A O 1 ATOM 2585 C CB . CYS A 1 353 ? 27.888 -52.548 37.916 1.00 59.77 ? 353 CYS A CB 1 ATOM 2586 S SG . CYS A 1 353 ? 27.658 -54.339 37.842 1.00 100.19 ? 353 CYS A SG 1 ATOM 2587 N N . SER A 1 354 ? 24.960 -52.114 38.835 1.00 65.34 ? 354 SER A N 1 ATOM 2588 C CA . SER A 1 354 ? 23.680 -52.671 39.262 1.00 63.43 ? 354 SER A CA 1 ATOM 2589 C C . SER A 1 354 ? 22.553 -52.208 38.342 1.00 58.63 ? 354 SER A C 1 ATOM 2590 O O . SER A 1 354 ? 21.722 -53.012 37.936 1.00 62.68 ? 354 SER A O 1 ATOM 2591 C CB . SER A 1 354 ? 23.365 -52.348 40.723 1.00 71.19 ? 354 SER A CB 1 ATOM 2592 O OG . SER A 1 354 ? 22.217 -53.069 41.160 1.00 72.53 ? 354 SER A OG 1 ATOM 2593 N N . PHE A 1 355 ? 22.533 -50.921 38.002 1.00 53.13 ? 355 PHE A N 1 ATOM 2594 C CA . PHE A 1 355 ? 21.584 -50.411 37.013 1.00 53.11 ? 355 PHE A CA 1 ATOM 2595 C C . PHE A 1 355 ? 21.633 -51.230 35.721 1.00 59.38 ? 355 PHE A C 1 ATOM 2596 O O . PHE A 1 355 ? 20.613 -51.747 35.243 1.00 55.84 ? 355 PHE A O 1 ATOM 2597 C CB . PHE A 1 355 ? 21.878 -48.946 36.708 1.00 49.70 ? 355 PHE A CB 1 ATOM 2598 C CG . PHE A 1 355 ? 20.728 -48.212 36.061 1.00 57.80 ? 355 PHE A CG 1 ATOM 2599 C CD1 . PHE A 1 355 ? 19.485 -48.806 35.945 1.00 60.78 ? 355 PHE A CD1 1 ATOM 2600 C CD2 . PHE A 1 355 ? 20.886 -46.909 35.606 1.00 63.44 ? 355 PHE A CD2 1 ATOM 2601 C CE1 . PHE A 1 355 ? 18.436 -48.130 35.361 1.00 70.49 ? 355 PHE A CE1 1 ATOM 2602 C CE2 . PHE A 1 355 ? 19.835 -46.224 35.030 1.00 68.81 ? 355 PHE A CE2 1 ATOM 2603 C CZ . PHE A 1 355 ? 18.609 -46.833 34.906 1.00 71.57 ? 355 PHE A CZ 1 ATOM 2604 N N . SER A 1 356 ? 22.832 -51.338 35.164 1.00 57.53 ? 356 SER A N 1 ATOM 2605 C CA . SER A 1 356 ? 23.059 -52.130 33.972 1.00 59.58 ? 356 SER A CA 1 ATOM 2606 C C . SER A 1 356 ? 22.516 -53.546 34.077 1.00 63.65 ? 356 SER A C 1 ATOM 2607 O O . SER A 1 356 ? 21.986 -54.075 33.115 1.00 77.58 ? 356 SER A O 1 ATOM 2608 C CB . SER A 1 356 ? 24.545 -52.170 33.646 1.00 61.88 ? 356 SER A CB 1 ATOM 2609 O OG . SER A 1 356 ? 24.991 -50.897 33.233 1.00 66.59 ? 356 SER A OG 1 ATOM 2610 N N . GLN A 1 357 ? 22.648 -54.173 35.235 1.00 65.48 ? 357 GLN A N 1 ATOM 2611 C CA . GLN A 1 357 ? 22.185 -55.548 35.370 1.00 65.62 ? 357 GLN A CA 1 ATOM 2612 C C . GLN A 1 357 ? 20.682 -55.609 35.489 1.00 66.32 ? 357 GLN A C 1 ATOM 2613 O O . GLN A 1 357 ? 20.100 -56.686 35.424 1.00 73.79 ? 357 GLN A O 1 ATOM 2614 C CB . GLN A 1 357 ? 22.775 -56.203 36.604 1.00 60.45 ? 357 GLN A CB 1 ATOM 2615 C CG . GLN A 1 357 ? 24.257 -56.411 36.581 1.00 64.08 ? 357 GLN A CG 1 ATOM 2616 C CD . GLN A 1 357 ? 24.715 -57.094 37.842 1.00 68.86 ? 357 GLN A CD 1 ATOM 2617 O OE1 . GLN A 1 357 ? 24.840 -56.458 38.896 1.00 67.38 ? 357 GLN A OE1 1 ATOM 2618 N NE2 . GLN A 1 357 ? 24.936 -58.405 37.756 1.00 62.45 ? 357 GLN A NE2 1 ATOM 2619 N N . HIS A 1 358 ? 20.060 -54.456 35.702 1.00 62.63 ? 358 HIS A N 1 ATOM 2620 C CA . HIS A 1 358 ? 18.618 -54.396 35.889 1.00 69.72 ? 358 HIS A CA 1 ATOM 2621 C C . HIS A 1 358 ? 17.907 -54.020 34.600 1.00 76.76 ? 358 HIS A C 1 ATOM 2622 O O . HIS A 1 358 ? 16.704 -54.230 34.460 1.00 76.06 ? 358 HIS A O 1 ATOM 2623 C CB . HIS A 1 358 ? 18.253 -53.429 37.015 1.00 65.31 ? 358 HIS A CB 1 ATOM 2624 C CG . HIS A 1 358 ? 17.940 -54.111 38.309 1.00 76.98 ? 358 HIS A CG 1 ATOM 2625 N ND1 . HIS A 1 358 ? 18.880 -54.304 39.298 1.00 81.18 ? 358 HIS A ND1 1 ATOM 2626 C CD2 . HIS A 1 358 ? 16.793 -54.664 38.767 1.00 87.50 ? 358 HIS A CD2 1 ATOM 2627 C CE1 . HIS A 1 358 ? 18.324 -54.935 40.316 1.00 83.93 ? 358 HIS A CE1 1 ATOM 2628 N NE2 . HIS A 1 358 ? 17.060 -55.167 40.019 1.00 96.03 ? 358 HIS A NE2 1 ATOM 2629 N N . LEU A 1 359 ? 18.665 -53.454 33.669 1.00 74.44 ? 359 LEU A N 1 ATOM 2630 C CA . LEU A 1 359 ? 18.172 -53.162 32.337 1.00 68.10 ? 359 LEU A CA 1 ATOM 2631 C C . LEU A 1 359 ? 18.208 -54.447 31.516 1.00 80.27 ? 359 LEU A C 1 ATOM 2632 O O . LEU A 1 359 ? 18.923 -54.552 30.511 1.00 78.25 ? 359 LEU A O 1 ATOM 2633 C CB . LEU A 1 359 ? 19.030 -52.076 31.695 1.00 62.88 ? 359 LEU A CB 1 ATOM 2634 C CG . LEU A 1 359 ? 18.908 -50.714 32.376 1.00 59.24 ? 359 LEU A CG 1 ATOM 2635 C CD1 . LEU A 1 359 ? 20.060 -49.789 32.016 1.00 59.50 ? 359 LEU A CD1 1 ATOM 2636 C CD2 . LEU A 1 359 ? 17.578 -50.092 32.020 1.00 43.01 ? 359 LEU A CD2 1 ATOM 2637 N N . LYS A 1 360 ? 17.428 -55.425 31.968 1.00 89.03 ? 360 LYS A N 1 ATOM 2638 C CA . LYS A 1 360 ? 17.387 -56.751 31.360 1.00 90.24 ? 360 LYS A CA 1 ATOM 2639 C C . LYS A 1 360 ? 17.017 -56.669 29.890 1.00 86.44 ? 360 LYS A C 1 ATOM 2640 O O . LYS A 1 360 ? 17.726 -57.180 29.029 1.00 91.36 ? 360 LYS A O 1 ATOM 2641 C CB . LYS A 1 360 ? 16.364 -57.640 32.079 1.00 85.58 ? 360 LYS A CB 1 ATOM 2642 C CG . LYS A 1 360 ? 16.564 -57.788 33.577 1.00 80.86 ? 360 LYS A CG 1 ATOM 2643 C CD . LYS A 1 360 ? 17.501 -58.934 33.915 1.00 94.04 ? 360 LYS A CD 1 ATOM 2644 C CE . LYS A 1 360 ? 17.689 -59.060 35.425 1.00 105.25 ? 360 LYS A CE 1 ATOM 2645 N NZ . LYS A 1 360 ? 16.404 -58.861 36.165 1.00 104.73 ? 360 LYS A NZ 1 ATOM 2646 N N . SER A 1 361 ? 15.900 -56.009 29.617 1.00 80.66 ? 361 SER A N 1 ATOM 2647 C CA . SER A 1 361 ? 15.286 -56.056 28.303 1.00 81.87 ? 361 SER A CA 1 ATOM 2648 C C . SER A 1 361 ? 15.838 -55.006 27.349 1.00 86.03 ? 361 SER A C 1 ATOM 2649 O O . SER A 1 361 ? 15.255 -54.753 26.295 1.00 91.54 ? 361 SER A O 1 ATOM 2650 C CB . SER A 1 361 ? 13.775 -55.877 28.444 1.00 80.93 ? 361 SER A CB 1 ATOM 2651 O OG . SER A 1 361 ? 13.276 -56.677 29.499 1.00 85.62 ? 361 SER A OG 1 ATOM 2652 N N . LEU A 1 362 ? 16.962 -54.401 27.713 1.00 81.57 ? 362 LEU A N 1 ATOM 2653 C CA . LEU A 1 362 ? 17.487 -53.279 26.947 1.00 77.61 ? 362 LEU A CA 1 ATOM 2654 C C . LEU A 1 362 ? 18.248 -53.718 25.693 1.00 87.68 ? 362 LEU A C 1 ATOM 2655 O O . LEU A 1 362 ? 19.227 -54.460 25.781 1.00 101.64 ? 362 LEU A O 1 ATOM 2656 C CB . LEU A 1 362 ? 18.370 -52.408 27.833 1.00 63.88 ? 362 LEU A CB 1 ATOM 2657 C CG . LEU A 1 362 ? 18.659 -51.011 27.294 1.00 54.71 ? 362 LEU A CG 1 ATOM 2658 C CD1 . LEU A 1 362 ? 17.352 -50.283 27.019 1.00 47.16 ? 362 LEU A CD1 1 ATOM 2659 C CD2 . LEU A 1 362 ? 19.534 -50.233 28.278 1.00 48.78 ? 362 LEU A CD2 1 ATOM 2660 N N . GLU A 1 363 ? 17.792 -53.239 24.535 1.00 76.67 ? 363 GLU A N 1 ATOM 2661 C CA . GLU A 1 363 ? 18.330 -53.634 23.232 1.00 74.81 ? 363 GLU A CA 1 ATOM 2662 C C . GLU A 1 363 ? 19.149 -52.542 22.554 1.00 77.32 ? 363 GLU A C 1 ATOM 2663 O O . GLU A 1 363 ? 20.154 -52.817 21.903 1.00 78.32 ? 363 GLU A O 1 ATOM 2664 C CB . GLU A 1 363 ? 17.192 -54.047 22.304 1.00 78.81 ? 363 GLU A CB 1 ATOM 2665 C CG . GLU A 1 363 ? 16.753 -55.483 22.496 1.00 91.08 ? 363 GLU A CG 1 ATOM 2666 C CD . GLU A 1 363 ? 15.371 -55.762 21.955 1.00 93.38 ? 363 GLU A CD 1 ATOM 2667 O OE1 . GLU A 1 363 ? 14.959 -55.095 20.980 1.00 89.23 ? 363 GLU A OE1 1 ATOM 2668 O OE2 . GLU A 1 363 ? 14.701 -56.659 22.511 1.00 99.50 ? 363 GLU A OE2 1 ATOM 2669 N N . PHE A 1 364 ? 18.702 -51.302 22.696 1.00 73.80 ? 364 PHE A N 1 ATOM 2670 C CA . PHE A 1 364 ? 19.410 -50.159 22.141 1.00 60.70 ? 364 PHE A CA 1 ATOM 2671 C C . PHE A 1 364 ? 19.837 -49.211 23.269 1.00 75.67 ? 364 PHE A C 1 ATOM 2672 O O . PHE A 1 364 ? 19.042 -48.899 24.156 1.00 83.43 ? 364 PHE A O 1 ATOM 2673 C CB . PHE A 1 364 ? 18.489 -49.449 21.166 1.00 48.28 ? 364 PHE A CB 1 ATOM 2674 C CG . PHE A 1 364 ? 19.055 -48.195 20.587 1.00 52.33 ? 364 PHE A CG 1 ATOM 2675 C CD1 . PHE A 1 364 ? 19.830 -48.233 19.446 1.00 50.34 ? 364 PHE A CD1 1 ATOM 2676 C CD2 . PHE A 1 364 ? 18.788 -46.967 21.170 1.00 56.96 ? 364 PHE A CD2 1 ATOM 2677 C CE1 . PHE A 1 364 ? 20.334 -47.069 18.895 1.00 58.44 ? 364 PHE A CE1 1 ATOM 2678 C CE2 . PHE A 1 364 ? 19.300 -45.800 20.630 1.00 62.13 ? 364 PHE A CE2 1 ATOM 2679 C CZ . PHE A 1 364 ? 20.070 -45.852 19.489 1.00 62.79 ? 364 PHE A CZ 1 ATOM 2680 N N . LEU A 1 365 ? 21.096 -48.778 23.248 1.00 73.84 ? 365 LEU A N 1 ATOM 2681 C CA . LEU A 1 365 ? 21.594 -47.805 24.215 1.00 66.29 ? 365 LEU A CA 1 ATOM 2682 C C . LEU A 1 365 ? 22.474 -46.769 23.535 1.00 66.50 ? 365 LEU A C 1 ATOM 2683 O O . LEU A 1 365 ? 23.508 -47.096 22.956 1.00 66.61 ? 365 LEU A O 1 ATOM 2684 C CB . LEU A 1 365 ? 22.370 -48.486 25.345 1.00 66.59 ? 365 LEU A CB 1 ATOM 2685 C CG . LEU A 1 365 ? 23.023 -47.550 26.371 1.00 63.36 ? 365 LEU A CG 1 ATOM 2686 C CD1 . LEU A 1 365 ? 21.971 -46.677 27.017 1.00 63.29 ? 365 LEU A CD1 1 ATOM 2687 C CD2 . LEU A 1 365 ? 23.805 -48.321 27.426 1.00 62.09 ? 365 LEU A CD2 1 ATOM 2688 N N . ASP A 1 366 ? 22.060 -45.513 23.633 1.00 67.00 ? 366 ASP A N 1 ATOM 2689 C CA . ASP A 1 366 ? 22.739 -44.413 22.969 1.00 65.00 ? 366 ASP A CA 1 ATOM 2690 C C . ASP A 1 366 ? 23.228 -43.390 23.995 1.00 57.79 ? 366 ASP A C 1 ATOM 2691 O O . ASP A 1 366 ? 22.437 -42.614 24.520 1.00 61.42 ? 366 ASP A O 1 ATOM 2692 C CB . ASP A 1 366 ? 21.764 -43.763 21.983 1.00 75.67 ? 366 ASP A CB 1 ATOM 2693 C CG . ASP A 1 366 ? 22.417 -42.720 21.101 1.00 69.77 ? 366 ASP A CG 1 ATOM 2694 O OD1 . ASP A 1 366 ? 23.626 -42.458 21.272 1.00 67.16 ? 366 ASP A OD1 1 ATOM 2695 O OD2 . ASP A 1 366 ? 21.704 -42.161 20.237 1.00 61.36 ? 366 ASP A OD2 1 ATOM 2696 N N . LEU A 1 367 ? 24.532 -43.399 24.271 1.00 53.30 ? 367 LEU A N 1 ATOM 2697 C CA . LEU A 1 367 ? 25.150 -42.498 25.242 1.00 57.29 ? 367 LEU A CA 1 ATOM 2698 C C . LEU A 1 367 ? 26.081 -41.507 24.569 1.00 59.83 ? 367 LEU A C 1 ATOM 2699 O O . LEU A 1 367 ? 27.190 -41.264 25.039 1.00 57.53 ? 367 LEU A O 1 ATOM 2700 C CB . LEU A 1 367 ? 25.952 -43.298 26.259 1.00 61.00 ? 367 LEU A CB 1 ATOM 2701 C CG . LEU A 1 367 ? 25.138 -44.293 27.072 1.00 61.43 ? 367 LEU A CG 1 ATOM 2702 C CD1 . LEU A 1 367 ? 26.070 -45.181 27.878 1.00 66.86 ? 367 LEU A CD1 1 ATOM 2703 C CD2 . LEU A 1 367 ? 24.165 -43.533 27.960 1.00 56.56 ? 367 LEU A CD2 1 ATOM 2704 N N . SER A 1 368 ? 25.625 -40.932 23.465 1.00 63.08 ? 368 SER A N 1 ATOM 2705 C CA . SER A 1 368 ? 26.466 -40.051 22.673 1.00 62.38 ? 368 SER A CA 1 ATOM 2706 C C . SER A 1 368 ? 26.754 -38.741 23.392 1.00 64.45 ? 368 SER A C 1 ATOM 2707 O O . SER A 1 368 ? 25.905 -38.217 24.109 1.00 68.60 ? 368 SER A O 1 ATOM 2708 C CB . SER A 1 368 ? 25.800 -39.764 21.329 1.00 64.20 ? 368 SER A CB 1 ATOM 2709 O OG . SER A 1 368 ? 25.573 -40.952 20.592 1.00 71.36 ? 368 SER A OG 1 ATOM 2710 N N . GLU A 1 369 ? 27.958 -38.217 23.200 1.00 61.90 ? 369 GLU A N 1 ATOM 2711 C CA . GLU A 1 369 ? 28.277 -36.865 23.645 1.00 68.97 ? 369 GLU A CA 1 ATOM 2712 C C . GLU A 1 369 ? 28.319 -36.734 25.166 1.00 72.66 ? 369 GLU A C 1 ATOM 2713 O O . GLU A 1 369 ? 27.951 -35.700 25.727 1.00 84.00 ? 369 GLU A O 1 ATOM 2714 C CB . GLU A 1 369 ? 27.263 -35.883 23.061 1.00 81.55 ? 369 GLU A CB 1 ATOM 2715 C CG . GLU A 1 369 ? 27.818 -34.508 22.730 1.00 90.45 ? 369 GLU A CG 1 ATOM 2716 C CD . GLU A 1 369 ? 27.010 -33.801 21.649 1.00 96.38 ? 369 GLU A CD 1 ATOM 2717 O OE1 . GLU A 1 369 ? 27.123 -32.559 21.541 1.00 96.85 ? 369 GLU A OE1 1 ATOM 2718 O OE2 . GLU A 1 369 ? 26.266 -34.491 20.909 1.00 91.56 ? 369 GLU A OE2 1 ATOM 2719 N N . ASN A 1 370 ? 28.781 -37.777 25.838 1.00 59.28 ? 370 ASN A N 1 ATOM 2720 C CA . ASN A 1 370 ? 28.882 -37.716 27.281 1.00 59.75 ? 370 ASN A CA 1 ATOM 2721 C C . ASN A 1 370 ? 30.326 -37.801 27.799 1.00 63.16 ? 370 ASN A C 1 ATOM 2722 O O . ASN A 1 370 ? 31.261 -37.386 27.121 1.00 60.19 ? 370 ASN A O 1 ATOM 2723 C CB . ASN A 1 370 ? 27.975 -38.769 27.921 1.00 60.79 ? 370 ASN A CB 1 ATOM 2724 C CG . ASN A 1 370 ? 26.500 -38.475 27.710 1.00 64.30 ? 370 ASN A CG 1 ATOM 2725 O OD1 . ASN A 1 370 ? 25.796 -39.215 27.017 1.00 66.56 ? 370 ASN A OD1 1 ATOM 2726 N ND2 . ASN A 1 370 ? 26.026 -37.391 28.305 1.00 62.36 ? 370 ASN A ND2 1 ATOM 2727 N N . LEU A 1 371 ? 30.494 -38.320 29.011 1.00 59.66 ? 371 LEU A N 1 ATOM 2728 C CA . LEU A 1 371 ? 31.794 -38.359 29.659 1.00 48.28 ? 371 LEU A CA 1 ATOM 2729 C C . LEU A 1 371 ? 32.314 -39.777 29.918 1.00 57.76 ? 371 LEU A C 1 ATOM 2730 O O . LEU A 1 371 ? 33.234 -39.957 30.710 1.00 67.59 ? 371 LEU A O 1 ATOM 2731 C CB . LEU A 1 371 ? 31.731 -37.601 30.980 1.00 48.55 ? 371 LEU A CB 1 ATOM 2732 C CG . LEU A 1 371 ? 31.839 -36.078 30.976 1.00 50.16 ? 371 LEU A CG 1 ATOM 2733 C CD1 . LEU A 1 371 ? 31.409 -35.485 29.658 1.00 48.84 ? 371 LEU A CD1 1 ATOM 2734 C CD2 . LEU A 1 371 ? 31.018 -35.506 32.122 1.00 40.63 ? 371 LEU A CD2 1 ATOM 2735 N N . MET A 1 372 ? 31.740 -40.781 29.264 1.00 55.53 ? 372 MET A N 1 ATOM 2736 C CA . MET A 1 372 ? 32.222 -42.148 29.447 1.00 65.72 ? 372 MET A CA 1 ATOM 2737 C C . MET A 1 372 ? 33.682 -42.287 29.045 1.00 74.09 ? 372 MET A C 1 ATOM 2738 O O . MET A 1 372 ? 34.104 -41.834 27.984 1.00 86.72 ? 372 MET A O 1 ATOM 2739 C CB . MET A 1 372 ? 31.381 -43.161 28.669 1.00 63.90 ? 372 MET A CB 1 ATOM 2740 C CG . MET A 1 372 ? 29.906 -43.128 29.013 1.00 67.25 ? 372 MET A CG 1 ATOM 2741 S SD . MET A 1 372 ? 29.556 -43.581 30.716 1.00 127.58 ? 372 MET A SD 1 ATOM 2742 C CE . MET A 1 372 ? 29.906 -45.338 30.697 1.00 65.82 ? 372 MET A CE 1 ATOM 2743 N N . VAL A 1 373 ? 34.446 -42.910 29.927 1.00 76.09 ? 373 VAL A N 1 ATOM 2744 C CA . VAL A 1 373 ? 35.824 -43.276 29.664 1.00 76.12 ? 373 VAL A CA 1 ATOM 2745 C C . VAL A 1 373 ? 35.994 -44.740 30.090 1.00 69.87 ? 373 VAL A C 1 ATOM 2746 O O . VAL A 1 373 ? 35.284 -45.215 30.971 1.00 66.33 ? 373 VAL A O 1 ATOM 2747 C CB . VAL A 1 373 ? 36.803 -42.342 30.408 1.00 72.60 ? 373 VAL A CB 1 ATOM 2748 C CG1 . VAL A 1 373 ? 36.804 -40.980 29.754 1.00 77.19 ? 373 VAL A CG1 1 ATOM 2749 C CG2 . VAL A 1 373 ? 36.423 -42.214 31.880 1.00 70.01 ? 373 VAL A CG2 1 ATOM 2750 N N . GLU A 1 374 ? 36.906 -45.463 29.453 1.00 62.84 ? 374 GLU A N 1 ATOM 2751 C CA . GLU A 1 374 ? 37.039 -46.882 29.725 1.00 63.21 ? 374 GLU A CA 1 ATOM 2752 C C . GLU A 1 374 ? 36.895 -47.198 31.216 1.00 61.96 ? 374 GLU A C 1 ATOM 2753 O O . GLU A 1 374 ? 36.326 -48.230 31.585 1.00 54.97 ? 374 GLU A O 1 ATOM 2754 C CB . GLU A 1 374 ? 38.368 -47.414 29.191 1.00 78.73 ? 374 GLU A CB 1 ATOM 2755 C CG . GLU A 1 374 ? 38.534 -47.309 27.692 1.00 85.34 ? 374 GLU A CG 1 ATOM 2756 C CD . GLU A 1 374 ? 39.010 -45.943 27.265 1.00 89.36 ? 374 GLU A CD 1 ATOM 2757 O OE1 . GLU A 1 374 ? 39.173 -45.064 28.138 1.00 89.52 ? 374 GLU A OE1 1 ATOM 2758 O OE2 . GLU A 1 374 ? 39.227 -45.750 26.054 1.00 87.49 ? 374 GLU A OE2 1 ATOM 2759 N N . GLU A 1 375 ? 37.402 -46.305 32.065 1.00 66.66 ? 375 GLU A N 1 ATOM 2760 C CA . GLU A 1 375 ? 37.389 -46.516 33.517 1.00 77.28 ? 375 GLU A CA 1 ATOM 2761 C C . GLU A 1 375 ? 35.980 -46.682 34.079 1.00 68.63 ? 375 GLU A C 1 ATOM 2762 O O . GLU A 1 375 ? 35.729 -47.571 34.881 1.00 71.86 ? 375 GLU A O 1 ATOM 2763 C CB . GLU A 1 375 ? 38.148 -45.400 34.245 1.00 97.46 ? 375 GLU A CB 1 ATOM 2764 C CG . GLU A 1 375 ? 39.607 -45.251 33.805 1.00 115.47 ? 375 GLU A CG 1 ATOM 2765 C CD . GLU A 1 375 ? 39.752 -44.477 32.496 1.00 121.16 ? 375 GLU A CD 1 ATOM 2766 O OE1 . GLU A 1 375 ? 39.444 -43.267 32.501 1.00 127.73 ? 375 GLU A OE1 1 ATOM 2767 O OE2 . GLU A 1 375 ? 40.179 -45.066 31.473 1.00 112.26 ? 375 GLU A OE2 1 ATOM 2768 N N . TYR A 1 376 ? 35.060 -45.836 33.643 1.00 64.17 ? 376 TYR A N 1 ATOM 2769 C CA . TYR A 1 376 ? 33.662 -46.002 34.002 1.00 67.57 ? 376 TYR A CA 1 ATOM 2770 C C . TYR A 1 376 ? 32.990 -47.102 33.195 1.00 65.26 ? 376 TYR A C 1 ATOM 2771 O O . TYR A 1 376 ? 32.269 -47.934 33.739 1.00 69.73 ? 376 TYR A O 1 ATOM 2772 C CB . TYR A 1 376 ? 32.922 -44.691 33.802 1.00 71.66 ? 376 TYR A CB 1 ATOM 2773 C CG . TYR A 1 376 ? 33.468 -43.609 34.680 1.00 71.62 ? 376 TYR A CG 1 ATOM 2774 C CD1 . TYR A 1 376 ? 34.197 -42.566 34.144 1.00 73.25 ? 376 TYR A CD1 1 ATOM 2775 C CD2 . TYR A 1 376 ? 33.282 -43.647 36.059 1.00 63.99 ? 376 TYR A CD2 1 ATOM 2776 C CE1 . TYR A 1 376 ? 34.711 -41.574 34.955 1.00 77.53 ? 376 TYR A CE1 1 ATOM 2777 C CE2 . TYR A 1 376 ? 33.797 -42.662 36.878 1.00 61.08 ? 376 TYR A CE2 1 ATOM 2778 C CZ . TYR A 1 376 ? 34.511 -41.628 36.319 1.00 61.18 ? 376 TYR A CZ 1 ATOM 2779 O OH . TYR A 1 376 ? 35.033 -40.636 37.105 1.00 47.47 ? 376 TYR A OH 1 ATOM 2780 N N . LEU A 1 377 ? 33.222 -47.095 31.891 1.00 66.72 ? 377 LEU A N 1 ATOM 2781 C CA . LEU A 1 377 ? 32.633 -48.091 31.004 1.00 71.13 ? 377 LEU A CA 1 ATOM 2782 C C . LEU A 1 377 ? 32.902 -49.503 31.505 1.00 76.55 ? 377 LEU A C 1 ATOM 2783 O O . LEU A 1 377 ? 32.101 -50.410 31.274 1.00 67.65 ? 377 LEU A O 1 ATOM 2784 C CB . LEU A 1 377 ? 33.182 -47.932 29.589 1.00 69.30 ? 377 LEU A CB 1 ATOM 2785 C CG . LEU A 1 377 ? 32.487 -48.708 28.481 1.00 70.56 ? 377 LEU A CG 1 ATOM 2786 C CD1 . LEU A 1 377 ? 31.064 -48.203 28.344 1.00 59.67 ? 377 LEU A CD1 1 ATOM 2787 C CD2 . LEU A 1 377 ? 33.264 -48.561 27.177 1.00 71.45 ? 377 LEU A CD2 1 ATOM 2788 N N . LYS A 1 378 ? 34.028 -49.688 32.195 1.00 81.33 ? 378 LYS A N 1 ATOM 2789 C CA . LYS A 1 378 ? 34.371 -51.004 32.712 1.00 75.63 ? 378 LYS A CA 1 ATOM 2790 C C . LYS A 1 378 ? 33.413 -51.410 33.814 1.00 63.45 ? 378 LYS A C 1 ATOM 2791 O O . LYS A 1 378 ? 33.150 -52.588 34.014 1.00 56.84 ? 378 LYS A O 1 ATOM 2792 C CB . LYS A 1 378 ? 35.809 -51.065 33.210 1.00 80.78 ? 378 LYS A CB 1 ATOM 2793 C CG . LYS A 1 378 ? 36.268 -52.484 33.526 1.00 90.49 ? 378 LYS A CG 1 ATOM 2794 C CD . LYS A 1 378 ? 37.710 -52.515 33.998 1.00 98.14 ? 378 LYS A CD 1 ATOM 2795 C CE . LYS A 1 378 ? 38.371 -53.853 33.698 1.00 103.59 ? 378 LYS A CE 1 ATOM 2796 N NZ . LYS A 1 378 ? 39.847 -53.757 33.901 1.00 109.07 ? 378 LYS A NZ 1 ATOM 2797 N N . ASN A 1 379 ? 32.878 -50.435 34.532 1.00 63.36 ? 379 ASN A N 1 ATOM 2798 C CA . ASN A 1 379 ? 31.881 -50.758 35.537 1.00 73.50 ? 379 ASN A CA 1 ATOM 2799 C C . ASN A 1 379 ? 30.503 -50.854 34.923 1.00 79.35 ? 379 ASN A C 1 ATOM 2800 O O . ASN A 1 379 ? 29.714 -51.732 35.273 1.00 84.90 ? 379 ASN A O 1 ATOM 2801 C CB . ASN A 1 379 ? 31.856 -49.736 36.666 1.00 74.62 ? 379 ASN A CB 1 ATOM 2802 C CG . ASN A 1 379 ? 31.065 -50.226 37.855 1.00 74.46 ? 379 ASN A CG 1 ATOM 2803 O OD1 . ASN A 1 379 ? 30.017 -49.672 38.199 1.00 72.92 ? 379 ASN A OD1 1 ATOM 2804 N ND2 . ASN A 1 379 ? 31.551 -51.294 38.478 1.00 67.99 ? 379 ASN A ND2 1 ATOM 2805 N N . SER A 1 380 ? 30.214 -49.940 34.005 1.00 73.45 ? 380 SER A N 1 ATOM 2806 C CA . SER A 1 380 ? 28.894 -49.879 33.408 1.00 68.96 ? 380 SER A CA 1 ATOM 2807 C C . SER A 1 380 ? 28.597 -51.112 32.561 1.00 75.86 ? 380 SER A C 1 ATOM 2808 O O . SER A 1 380 ? 27.442 -51.503 32.421 1.00 81.10 ? 380 SER A O 1 ATOM 2809 C CB . SER A 1 380 ? 28.729 -48.590 32.619 1.00 62.01 ? 380 SER A CB 1 ATOM 2810 O OG . SER A 1 380 ? 28.873 -47.484 33.490 1.00 58.18 ? 380 SER A OG 1 ATOM 2811 N N . ALA A 1 381 ? 29.644 -51.725 32.011 1.00 77.78 ? 381 ALA A N 1 ATOM 2812 C CA . ALA A 1 381 ? 29.520 -53.018 31.333 1.00 69.88 ? 381 ALA A CA 1 ATOM 2813 C C . ALA A 1 381 ? 30.196 -54.109 32.164 1.00 73.72 ? 381 ALA A C 1 ATOM 2814 O O . ALA A 1 381 ? 31.247 -54.658 31.798 1.00 71.55 ? 381 ALA A O 1 ATOM 2815 C CB . ALA A 1 381 ? 30.106 -52.958 29.930 1.00 64.43 ? 381 ALA A CB 1 ATOM 2816 N N . CYS A 1 382 ? 29.584 -54.393 33.308 1.00 73.82 ? 382 CYS A N 1 ATOM 2817 C CA . CYS A 1 382 ? 30.061 -55.428 34.203 1.00 65.17 ? 382 CYS A CA 1 ATOM 2818 C C . CYS A 1 382 ? 29.657 -56.803 33.675 1.00 69.34 ? 382 CYS A C 1 ATOM 2819 O O . CYS A 1 382 ? 29.000 -56.892 32.649 1.00 69.98 ? 382 CYS A O 1 ATOM 2820 C CB . CYS A 1 382 ? 29.552 -55.178 35.624 1.00 47.52 ? 382 CYS A CB 1 ATOM 2821 S SG . CYS A 1 382 ? 27.802 -54.788 35.850 1.00 119.09 ? 382 CYS A SG 1 ATOM 2822 N N . LYS A 1 383 ? 30.040 -57.873 34.362 1.00 74.61 ? 383 LYS A N 1 ATOM 2823 C CA . LYS A 1 383 ? 29.834 -59.206 33.809 1.00 87.47 ? 383 LYS A CA 1 ATOM 2824 C C . LYS A 1 383 ? 28.383 -59.508 33.397 1.00 105.74 ? 383 LYS A C 1 ATOM 2825 O O . LYS A 1 383 ? 28.152 -60.229 32.423 1.00 115.17 ? 383 LYS A O 1 ATOM 2826 C CB . LYS A 1 383 ? 30.381 -60.307 34.730 1.00 84.27 ? 383 LYS A CB 1 ATOM 2827 C CG . LYS A 1 383 ? 30.423 -61.675 34.050 1.00 87.15 ? 383 LYS A CG 1 ATOM 2828 C CD . LYS A 1 383 ? 31.041 -62.755 34.916 1.00 98.62 ? 383 LYS A CD 1 ATOM 2829 C CE . LYS A 1 383 ? 31.104 -64.093 34.166 1.00 105.13 ? 383 LYS A CE 1 ATOM 2830 N NZ . LYS A 1 383 ? 31.991 -65.090 34.840 1.00 103.40 ? 383 LYS A NZ 1 ATOM 2831 N N . GLY A 1 384 ? 27.409 -58.961 34.119 1.00 100.04 ? 384 GLY A N 1 ATOM 2832 C CA . GLY A 1 384 ? 26.019 -59.282 33.831 1.00 94.90 ? 384 GLY A CA 1 ATOM 2833 C C . GLY A 1 384 ? 25.213 -58.157 33.209 1.00 87.31 ? 384 GLY A C 1 ATOM 2834 O O . GLY A 1 384 ? 23.979 -58.174 33.228 1.00 78.25 ? 384 GLY A O 1 ATOM 2835 N N . ALA A 1 385 ? 25.912 -57.178 32.651 1.00 83.36 ? 385 ALA A N 1 ATOM 2836 C CA . ALA A 1 385 ? 25.266 -55.966 32.170 1.00 76.92 ? 385 ALA A CA 1 ATOM 2837 C C . ALA A 1 385 ? 24.547 -56.160 30.838 1.00 86.26 ? 385 ALA A C 1 ATOM 2838 O O . ALA A 1 385 ? 24.905 -57.025 30.029 1.00 83.93 ? 385 ALA A O 1 ATOM 2839 C CB . ALA A 1 385 ? 26.278 -54.840 32.059 1.00 64.47 ? 385 ALA A CB 1 ATOM 2840 N N . TRP A 1 386 ? 23.510 -55.352 30.645 1.00 84.14 ? 386 TRP A N 1 ATOM 2841 C CA . TRP A 1 386 ? 22.854 -55.186 29.359 1.00 82.30 ? 386 TRP A CA 1 ATOM 2842 C C . TRP A 1 386 ? 22.683 -56.467 28.546 1.00 90.15 ? 386 TRP A C 1 ATOM 2843 O O . TRP A 1 386 ? 23.017 -56.500 27.359 1.00 102.07 ? 386 TRP A O 1 ATOM 2844 C CB . TRP A 1 386 ? 23.633 -54.158 28.555 1.00 74.22 ? 386 TRP A CB 1 ATOM 2845 C CG . TRP A 1 386 ? 23.677 -52.826 29.220 1.00 69.98 ? 386 TRP A CG 1 ATOM 2846 C CD1 . TRP A 1 386 ? 22.687 -52.247 29.961 1.00 63.11 ? 386 TRP A CD1 1 ATOM 2847 C CD2 . TRP A 1 386 ? 24.750 -51.886 29.180 1.00 66.80 ? 386 TRP A CD2 1 ATOM 2848 N NE1 . TRP A 1 386 ? 23.083 -51.009 30.394 1.00 63.63 ? 386 TRP A NE1 1 ATOM 2849 C CE2 . TRP A 1 386 ? 24.346 -50.760 29.925 1.00 65.97 ? 386 TRP A CE2 1 ATOM 2850 C CE3 . TRP A 1 386 ? 26.013 -51.886 28.585 1.00 57.85 ? 386 TRP A CE3 1 ATOM 2851 C CZ2 . TRP A 1 386 ? 25.158 -49.649 30.093 1.00 60.46 ? 386 TRP A CZ2 1 ATOM 2852 C CZ3 . TRP A 1 386 ? 26.816 -50.785 28.751 1.00 60.63 ? 386 TRP A CZ3 1 ATOM 2853 C CH2 . TRP A 1 386 ? 26.387 -49.679 29.503 1.00 60.11 ? 386 TRP A CH2 1 ATOM 2854 N N . PRO A 1 387 ? 22.122 -57.512 29.171 1.00 77.78 ? 387 PRO A N 1 ATOM 2855 C CA . PRO A 1 387 ? 22.084 -58.856 28.589 1.00 75.29 ? 387 PRO A CA 1 ATOM 2856 C C . PRO A 1 387 ? 21.478 -58.888 27.187 1.00 81.90 ? 387 PRO A C 1 ATOM 2857 O O . PRO A 1 387 ? 21.900 -59.694 26.364 1.00 89.06 ? 387 PRO A O 1 ATOM 2858 C CB . PRO A 1 387 ? 21.200 -59.639 29.563 1.00 64.20 ? 387 PRO A CB 1 ATOM 2859 C CG . PRO A 1 387 ? 21.169 -58.837 30.794 1.00 63.95 ? 387 PRO A CG 1 ATOM 2860 C CD . PRO A 1 387 ? 21.303 -57.421 30.385 1.00 71.25 ? 387 PRO A CD 1 ATOM 2861 N N . SER A 1 388 ? 20.507 -58.027 26.912 1.00 79.96 ? 388 SER A N 1 ATOM 2862 C CA . SER A 1 388 ? 19.842 -58.064 25.614 1.00 73.32 ? 388 SER A CA 1 ATOM 2863 C C . SER A 1 388 ? 20.346 -56.979 24.687 1.00 83.72 ? 388 SER A C 1 ATOM 2864 O O . SER A 1 388 ? 19.795 -56.784 23.612 1.00 97.72 ? 388 SER A O 1 ATOM 2865 C CB . SER A 1 388 ? 18.326 -57.930 25.768 1.00 61.07 ? 388 SER A CB 1 ATOM 2866 O OG . SER A 1 388 ? 17.839 -58.849 26.727 1.00 70.51 ? 388 SER A OG 1 ATOM 2867 N N . LEU A 1 389 ? 21.389 -56.268 25.094 1.00 81.47 ? 389 LEU A N 1 ATOM 2868 C CA . LEU A 1 389 ? 21.869 -55.158 24.285 1.00 79.07 ? 389 LEU A CA 1 ATOM 2869 C C . LEU A 1 389 ? 22.432 -55.625 22.955 1.00 79.33 ? 389 LEU A C 1 ATOM 2870 O O . LEU A 1 389 ? 23.318 -56.470 22.908 1.00 88.56 ? 389 LEU A O 1 ATOM 2871 C CB . LEU A 1 389 ? 22.928 -54.366 25.028 1.00 78.43 ? 389 LEU A CB 1 ATOM 2872 C CG . LEU A 1 389 ? 22.962 -52.922 24.564 1.00 71.44 ? 389 LEU A CG 1 ATOM 2873 C CD1 . LEU A 1 389 ? 21.639 -52.253 24.916 1.00 62.36 ? 389 LEU A CD1 1 ATOM 2874 C CD2 . LEU A 1 389 ? 24.119 -52.213 25.225 1.00 77.14 ? 389 LEU A CD2 1 ATOM 2875 N N . GLN A 1 390 ? 21.909 -55.064 21.874 1.00 78.71 ? 390 GLN A N 1 ATOM 2876 C CA . GLN A 1 390 ? 22.361 -55.406 20.535 1.00 74.11 ? 390 GLN A CA 1 ATOM 2877 C C . GLN A 1 390 ? 23.097 -54.241 19.907 1.00 72.89 ? 390 GLN A C 1 ATOM 2878 O O . GLN A 1 390 ? 24.002 -54.432 19.101 1.00 82.97 ? 390 GLN A O 1 ATOM 2879 C CB . GLN A 1 390 ? 21.178 -55.796 19.663 1.00 72.76 ? 390 GLN A CB 1 ATOM 2880 C CG . GLN A 1 390 ? 20.508 -57.075 20.110 1.00 79.82 ? 390 GLN A CG 1 ATOM 2881 C CD . GLN A 1 390 ? 19.129 -57.241 19.515 1.00 81.94 ? 390 GLN A CD 1 ATOM 2882 O OE1 . GLN A 1 390 ? 18.157 -57.449 20.243 1.00 88.78 ? 390 GLN A OE1 1 ATOM 2883 N NE2 . GLN A 1 390 ? 19.031 -57.143 18.187 1.00 69.67 ? 390 GLN A NE2 1 ATOM 2884 N N . THR A 1 391 ? 22.708 -53.032 20.291 1.00 60.05 ? 391 THR A N 1 ATOM 2885 C CA . THR A 1 391 ? 23.349 -51.837 19.774 1.00 61.01 ? 391 THR A CA 1 ATOM 2886 C C . THR A 1 391 ? 23.840 -50.935 20.895 1.00 71.56 ? 391 THR A C 1 ATOM 2887 O O . THR A 1 391 ? 23.061 -50.489 21.735 1.00 79.49 ? 391 THR A O 1 ATOM 2888 C CB . THR A 1 391 ? 22.386 -51.033 18.896 1.00 66.20 ? 391 THR A CB 1 ATOM 2889 O OG1 . THR A 1 391 ? 21.727 -51.918 17.978 1.00 73.24 ? 391 THR A OG1 1 ATOM 2890 C CG2 . THR A 1 391 ? 23.139 -49.941 18.134 1.00 53.49 ? 391 THR A CG2 1 ATOM 2891 N N . LEU A 1 392 ? 25.139 -50.668 20.904 1.00 67.09 ? 392 LEU A N 1 ATOM 2892 C CA . LEU A 1 392 ? 25.700 -49.709 21.832 1.00 55.59 ? 392 LEU A CA 1 ATOM 2893 C C . LEU A 1 392 ? 26.167 -48.503 21.040 1.00 57.34 ? 392 LEU A C 1 ATOM 2894 O O . LEU A 1 392 ? 26.796 -48.648 19.997 1.00 54.25 ? 392 LEU A O 1 ATOM 2895 C CB . LEU A 1 392 ? 26.869 -50.330 22.604 1.00 53.02 ? 392 LEU A CB 1 ATOM 2896 C CG . LEU A 1 392 ? 27.534 -49.466 23.691 1.00 61.60 ? 392 LEU A CG 1 ATOM 2897 C CD1 . LEU A 1 392 ? 26.531 -48.558 24.373 1.00 54.77 ? 392 LEU A CD1 1 ATOM 2898 C CD2 . LEU A 1 392 ? 28.251 -50.332 24.732 1.00 72.35 ? 392 LEU A CD2 1 ATOM 2899 N N . VAL A 1 393 ? 25.861 -47.307 21.521 1.00 54.43 ? 393 VAL A N 1 ATOM 2900 C CA . VAL A 1 393 ? 26.386 -46.121 20.870 1.00 58.94 ? 393 VAL A CA 1 ATOM 2901 C C . VAL A 1 393 ? 27.127 -45.254 21.865 1.00 67.32 ? 393 VAL A C 1 ATOM 2902 O O . VAL A 1 393 ? 26.516 -44.650 22.735 1.00 71.79 ? 393 VAL A O 1 ATOM 2903 C CB . VAL A 1 393 ? 25.281 -45.291 20.208 1.00 60.28 ? 393 VAL A CB 1 ATOM 2904 C CG1 . VAL A 1 393 ? 25.899 -44.196 19.372 1.00 58.78 ? 393 VAL A CG1 1 ATOM 2905 C CG2 . VAL A 1 393 ? 24.389 -46.174 19.349 1.00 48.15 ? 393 VAL A CG2 1 ATOM 2906 N N . LEU A 1 394 ? 28.448 -45.203 21.731 1.00 72.20 ? 394 LEU A N 1 ATOM 2907 C CA . LEU A 1 394 ? 29.284 -44.366 22.585 1.00 67.21 ? 394 LEU A CA 1 ATOM 2908 C C . LEU A 1 394 ? 30.037 -43.350 21.750 1.00 67.08 ? 394 LEU A C 1 ATOM 2909 O O . LEU A 1 394 ? 31.227 -43.126 21.972 1.00 69.40 ? 394 LEU A O 1 ATOM 2910 C CB . LEU A 1 394 ? 30.312 -45.208 23.329 1.00 62.71 ? 394 LEU A CB 1 ATOM 2911 C CG . LEU A 1 394 ? 29.842 -46.384 24.171 1.00 69.31 ? 394 LEU A CG 1 ATOM 2912 C CD1 . LEU A 1 394 ? 31.029 -47.263 24.501 1.00 63.74 ? 394 LEU A CD1 1 ATOM 2913 C CD2 . LEU A 1 394 ? 29.184 -45.866 25.439 1.00 85.19 ? 394 LEU A CD2 1 ATOM 2914 N N . SER A 1 395 ? 29.358 -42.753 20.777 1.00 54.82 ? 395 SER A N 1 ATOM 2915 C CA . SER A 1 395 ? 29.977 -41.717 19.977 1.00 51.88 ? 395 SER A CA 1 ATOM 2916 C C . SER A 1 395 ? 30.267 -40.503 20.833 1.00 53.25 ? 395 SER A C 1 ATOM 2917 O O . SER A 1 395 ? 29.581 -40.238 21.818 1.00 57.68 ? 395 SER A O 1 ATOM 2918 C CB . SER A 1 395 ? 29.067 -41.302 18.825 1.00 65.21 ? 395 SER A CB 1 ATOM 2919 O OG . SER A 1 395 ? 29.700 -40.342 17.990 1.00 74.74 ? 395 SER A OG 1 ATOM 2920 N N . GLN A 1 396 ? 31.298 -39.769 20.448 1.00 55.11 ? 396 GLN A N 1 ATOM 2921 C CA . GLN A 1 396 ? 31.604 -38.487 21.056 1.00 57.15 ? 396 GLN A CA 1 ATOM 2922 C C . GLN A 1 396 ? 31.677 -38.557 22.572 1.00 61.69 ? 396 GLN A C 1 ATOM 2923 O O . GLN A 1 396 ? 31.179 -37.679 23.266 1.00 69.02 ? 396 GLN A O 1 ATOM 2924 C CB . GLN A 1 396 ? 30.584 -37.444 20.626 1.00 63.51 ? 396 GLN A CB 1 ATOM 2925 C CG . GLN A 1 396 ? 31.091 -36.018 20.673 1.00 83.15 ? 396 GLN A CG 1 ATOM 2926 C CD . GLN A 1 396 ? 30.215 -35.088 19.853 1.00 99.38 ? 396 GLN A CD 1 ATOM 2927 O OE1 . GLN A 1 396 ? 29.375 -35.542 19.064 1.00 96.83 ? 396 GLN A OE1 1 ATOM 2928 N NE2 . GLN A 1 396 ? 30.405 -33.779 20.031 1.00 100.33 ? 396 GLN A NE2 1 ATOM 2929 N N . ASN A 1 397 ? 32.292 -39.612 23.082 1.00 61.51 ? 397 ASN A N 1 ATOM 2930 C CA . ASN A 1 397 ? 32.712 -39.622 24.469 1.00 72.43 ? 397 ASN A CA 1 ATOM 2931 C C . ASN A 1 397 ? 34.216 -39.389 24.528 1.00 81.50 ? 397 ASN A C 1 ATOM 2932 O O . ASN A 1 397 ? 34.777 -38.763 23.628 1.00 89.27 ? 397 ASN A O 1 ATOM 2933 C CB . ASN A 1 397 ? 32.264 -40.895 25.184 1.00 67.31 ? 397 ASN A CB 1 ATOM 2934 C CG . ASN A 1 397 ? 30.768 -40.909 25.433 1.00 65.34 ? 397 ASN A CG 1 ATOM 2935 O OD1 . ASN A 1 397 ? 29.970 -41.053 24.511 1.00 77.64 ? 397 ASN A OD1 1 ATOM 2936 N ND2 . ASN A 1 397 ? 30.382 -40.732 26.675 1.00 51.57 ? 397 ASN A ND2 1 ATOM 2937 N N . HIS A 1 398 ? 34.878 -39.855 25.576 1.00 75.25 ? 398 HIS A N 1 ATOM 2938 C CA . HIS A 1 398 ? 36.287 -39.524 25.714 1.00 81.19 ? 398 HIS A CA 1 ATOM 2939 C C . HIS A 1 398 ? 37.172 -40.754 25.740 1.00 84.61 ? 398 HIS A C 1 ATOM 2940 O O . HIS A 1 398 ? 38.197 -40.794 26.424 1.00 83.37 ? 398 HIS A O 1 ATOM 2941 C CB . HIS A 1 398 ? 36.514 -38.621 26.927 1.00 82.54 ? 398 HIS A CB 1 ATOM 2942 C CG . HIS A 1 398 ? 36.014 -37.225 26.725 1.00 85.50 ? 398 HIS A CG 1 ATOM 2943 N ND1 . HIS A 1 398 ? 36.633 -36.330 25.879 1.00 92.78 ? 398 HIS A ND1 1 ATOM 2944 C CD2 . HIS A 1 398 ? 34.941 -36.578 27.237 1.00 80.63 ? 398 HIS A CD2 1 ATOM 2945 C CE1 . HIS A 1 398 ? 35.969 -35.188 25.887 1.00 94.53 ? 398 HIS A CE1 1 ATOM 2946 N NE2 . HIS A 1 398 ? 34.937 -35.312 26.703 1.00 88.57 ? 398 HIS A NE2 1 ATOM 2947 N N . LEU A 1 399 ? 36.769 -41.755 24.968 1.00 81.20 ? 399 LEU A N 1 ATOM 2948 C CA . LEU A 1 399 ? 37.530 -42.986 24.870 1.00 86.60 ? 399 LEU A CA 1 ATOM 2949 C C . LEU A 1 399 ? 38.867 -42.734 24.174 1.00 98.50 ? 399 LEU A C 1 ATOM 2950 O O . LEU A 1 399 ? 38.949 -41.923 23.247 1.00 99.05 ? 399 LEU A O 1 ATOM 2951 C CB . LEU A 1 399 ? 36.720 -44.038 24.118 1.00 72.30 ? 399 LEU A CB 1 ATOM 2952 C CG . LEU A 1 399 ? 35.356 -44.348 24.732 1.00 61.87 ? 399 LEU A CG 1 ATOM 2953 C CD1 . LEU A 1 399 ? 34.547 -45.252 23.822 1.00 56.53 ? 399 LEU A CD1 1 ATOM 2954 C CD2 . LEU A 1 399 ? 35.526 -44.980 26.105 1.00 69.78 ? 399 LEU A CD2 1 ATOM 2955 N N . ARG A 1 400 ? 39.917 -43.417 24.631 1.00 96.58 ? 400 ARG A N 1 ATOM 2956 C CA . ARG A 1 400 ? 41.230 -43.279 24.007 1.00 84.68 ? 400 ARG A CA 1 ATOM 2957 C C . ARG A 1 400 ? 41.942 -44.599 23.638 1.00 86.27 ? 400 ARG A C 1 ATOM 2958 O O . ARG A 1 400 ? 42.989 -44.559 23.008 1.00 92.65 ? 400 ARG A O 1 ATOM 2959 C CB . ARG A 1 400 ? 42.143 -42.362 24.831 1.00 69.51 ? 400 ARG A CB 1 ATOM 2960 C CG . ARG A 1 400 ? 42.015 -40.860 24.519 1.00 82.84 ? 400 ARG A CG 1 ATOM 2961 C CD . ARG A 1 400 ? 43.389 -40.181 24.689 1.00 104.01 ? 400 ARG A CD 1 ATOM 2962 N NE . ARG A 1 400 ? 43.340 -38.784 25.140 1.00 105.70 ? 400 ARG A NE 1 ATOM 2963 C CZ . ARG A 1 400 ? 44.405 -38.100 25.563 1.00 86.09 ? 400 ARG A CZ 1 ATOM 2964 N NH1 . ARG A 1 400 ? 45.596 -38.687 25.589 1.00 81.39 ? 400 ARG A NH1 1 ATOM 2965 N NH2 . ARG A 1 400 ? 44.282 -36.835 25.958 1.00 64.95 ? 400 ARG A NH2 1 ATOM 2966 N N . SER A 1 401 ? 41.382 -45.754 24.004 1.00 83.68 ? 401 SER A N 1 ATOM 2967 C CA . SER A 1 401 ? 41.964 -47.046 23.593 1.00 81.82 ? 401 SER A CA 1 ATOM 2968 C C . SER A 1 401 ? 40.975 -48.111 23.131 1.00 78.77 ? 401 SER A C 1 ATOM 2969 O O . SER A 1 401 ? 40.287 -48.732 23.936 1.00 85.93 ? 401 SER A O 1 ATOM 2970 C CB . SER A 1 401 ? 42.843 -47.649 24.688 1.00 93.48 ? 401 SER A CB 1 ATOM 2971 O OG . SER A 1 401 ? 43.419 -48.873 24.246 1.00 98.35 ? 401 SER A OG 1 ATOM 2972 N N . MET A 1 402 ? 40.940 -48.340 21.829 1.00 76.30 ? 402 MET A N 1 ATOM 2973 C CA . MET A 1 402 ? 40.158 -49.426 21.258 1.00 85.74 ? 402 MET A CA 1 ATOM 2974 C C . MET A 1 402 ? 40.416 -50.803 21.858 1.00 78.63 ? 402 MET A C 1 ATOM 2975 O O . MET A 1 402 ? 39.505 -51.616 21.930 1.00 73.02 ? 402 MET A O 1 ATOM 2976 C CB . MET A 1 402 ? 40.404 -49.508 19.757 1.00 98.48 ? 402 MET A CB 1 ATOM 2977 C CG . MET A 1 402 ? 39.586 -48.545 18.955 1.00 102.86 ? 402 MET A CG 1 ATOM 2978 S SD . MET A 1 402 ? 40.331 -48.380 17.351 1.00 96.29 ? 402 MET A SD 1 ATOM 2979 C CE . MET A 1 402 ? 41.816 -47.471 17.769 1.00 445.89 ? 402 MET A CE 1 ATOM 2980 N N . GLN A 1 403 ? 41.648 -51.094 22.258 1.00 79.97 ? 403 GLN A N 1 ATOM 2981 C CA . GLN A 1 403 ? 41.899 -52.394 22.868 1.00 85.85 ? 403 GLN A CA 1 ATOM 2982 C C . GLN A 1 403 ? 41.212 -52.521 24.221 1.00 85.68 ? 403 GLN A C 1 ATOM 2983 O O . GLN A 1 403 ? 40.565 -53.532 24.506 1.00 82.20 ? 403 GLN A O 1 ATOM 2984 C CB . GLN A 1 403 ? 43.385 -52.687 23.026 1.00 90.45 ? 403 GLN A CB 1 ATOM 2985 C CG . GLN A 1 403 ? 43.622 -54.051 23.662 1.00 91.65 ? 403 GLN A CG 1 ATOM 2986 C CD . GLN A 1 403 ? 45.083 -54.408 23.753 1.00 98.70 ? 403 GLN A CD 1 ATOM 2987 O OE1 . GLN A 1 403 ? 45.932 -53.542 23.979 1.00 94.97 ? 403 GLN A OE1 1 ATOM 2988 N NE2 . GLN A 1 403 ? 45.391 -55.692 23.579 1.00 104.17 ? 403 GLN A NE2 1 ATOM 2989 N N . LYS A 1 404 ? 41.362 -51.499 25.057 1.00 86.79 ? 404 LYS A N 1 ATOM 2990 C CA . LYS A 1 404 ? 40.709 -51.503 26.358 1.00 87.68 ? 404 LYS A CA 1 ATOM 2991 C C . LYS A 1 404 ? 39.193 -51.560 26.190 1.00 83.95 ? 404 LYS A C 1 ATOM 2992 O O . LYS A 1 404 ? 38.518 -52.322 26.876 1.00 89.27 ? 404 LYS A O 1 ATOM 2993 C CB . LYS A 1 404 ? 41.146 -50.305 27.211 1.00 89.58 ? 404 LYS A CB 1 ATOM 2994 C CG . LYS A 1 404 ? 42.482 -50.520 27.935 1.00 96.53 ? 404 LYS A CG 1 ATOM 2995 C CD . LYS A 1 404 ? 42.843 -49.352 28.855 1.00 100.06 ? 404 LYS A CD 1 ATOM 2996 C CE . LYS A 1 404 ? 44.250 -49.501 29.423 1.00 100.89 ? 404 LYS A CE 1 ATOM 2997 N NZ . LYS A 1 404 ? 45.276 -49.691 28.349 1.00 103.33 ? 404 LYS A NZ 1 ATOM 2998 N N . THR A 1 405 ? 38.670 -50.778 25.251 1.00 77.30 ? 405 THR A N 1 ATOM 2999 C CA . THR A 1 405 ? 37.231 -50.724 24.996 1.00 76.28 ? 405 THR A CA 1 ATOM 3000 C C . THR A 1 405 ? 36.637 -52.078 24.588 1.00 75.02 ? 405 THR A C 1 ATOM 3001 O O . THR A 1 405 ? 35.734 -52.602 25.239 1.00 67.77 ? 405 THR A O 1 ATOM 3002 C CB . THR A 1 405 ? 36.898 -49.669 23.918 1.00 69.82 ? 405 THR A CB 1 ATOM 3003 O OG1 . THR A 1 405 ? 37.448 -48.408 24.308 1.00 73.43 ? 405 THR A OG1 1 ATOM 3004 C CG2 . THR A 1 405 ? 35.386 -49.523 23.745 1.00 55.40 ? 405 THR A CG2 1 ATOM 3005 N N . GLY A 1 406 ? 37.146 -52.639 23.502 1.00 78.46 ? 406 GLY A N 1 ATOM 3006 C CA . GLY A 1 406 ? 36.623 -53.888 22.991 1.00 77.13 ? 406 GLY A CA 1 ATOM 3007 C C . GLY A 1 406 ? 36.664 -55.001 24.013 1.00 74.53 ? 406 GLY A C 1 ATOM 3008 O O . GLY A 1 406 ? 35.825 -55.898 23.992 1.00 69.04 ? 406 GLY A O 1 ATOM 3009 N N . GLU A 1 407 ? 37.643 -54.941 24.909 1.00 79.55 ? 407 GLU A N 1 ATOM 3010 C CA . GLU A 1 407 ? 37.847 -56.006 25.884 1.00 91.39 ? 407 GLU A CA 1 ATOM 3011 C C . GLU A 1 407 ? 36.885 -55.873 27.055 1.00 86.96 ? 407 GLU A C 1 ATOM 3012 O O . GLU A 1 407 ? 36.442 -56.868 27.637 1.00 83.34 ? 407 GLU A O 1 ATOM 3013 C CB . GLU A 1 407 ? 39.288 -56.003 26.377 1.00 93.21 ? 407 GLU A CB 1 ATOM 3014 C CG . GLU A 1 407 ? 39.562 -57.007 27.473 1.00 100.75 ? 407 GLU A CG 1 ATOM 3015 C CD . GLU A 1 407 ? 41.032 -57.085 27.810 1.00 110.26 ? 407 GLU A CD 1 ATOM 3016 O OE1 . GLU A 1 407 ? 41.835 -57.323 26.879 1.00 111.75 ? 407 GLU A OE1 1 ATOM 3017 O OE2 . GLU A 1 407 ? 41.379 -56.902 29.001 1.00 103.37 ? 407 GLU A OE2 1 ATOM 3018 N N . ILE A 1 408 ? 36.568 -54.631 27.398 1.00 78.40 ? 408 ILE A N 1 ATOM 3019 C CA . ILE A 1 408 ? 35.585 -54.371 28.429 1.00 74.55 ? 408 ILE A CA 1 ATOM 3020 C C . ILE A 1 408 ? 34.250 -54.888 27.954 1.00 73.90 ? 408 ILE A C 1 ATOM 3021 O O . ILE A 1 408 ? 33.453 -55.405 28.731 1.00 79.98 ? 408 ILE A O 1 ATOM 3022 C CB . ILE A 1 408 ? 35.433 -52.877 28.701 1.00 70.67 ? 408 ILE A CB 1 ATOM 3023 C CG1 . ILE A 1 408 ? 36.690 -52.329 29.373 1.00 60.03 ? 408 ILE A CG1 1 ATOM 3024 C CG2 . ILE A 1 408 ? 34.206 -52.628 29.563 1.00 79.31 ? 408 ILE A CG2 1 ATOM 3025 C CD1 . ILE A 1 408 ? 36.925 -50.852 29.105 1.00 56.52 ? 408 ILE A CD1 1 ATOM 3026 N N . LEU A 1 409 ? 34.013 -54.753 26.660 1.00 72.65 ? 409 LEU A N 1 ATOM 3027 C CA . LEU A 1 409 ? 32.687 -54.998 26.123 1.00 74.88 ? 409 LEU A CA 1 ATOM 3028 C C . LEU A 1 409 ? 32.415 -56.479 25.926 1.00 74.35 ? 409 LEU A C 1 ATOM 3029 O O . LEU A 1 409 ? 31.321 -56.858 25.525 1.00 75.51 ? 409 LEU A O 1 ATOM 3030 C CB . LEU A 1 409 ? 32.491 -54.229 24.819 1.00 73.53 ? 409 LEU A CB 1 ATOM 3031 C CG . LEU A 1 409 ? 32.486 -52.710 24.983 1.00 67.52 ? 409 LEU A CG 1 ATOM 3032 C CD1 . LEU A 1 409 ? 32.823 -52.026 23.675 1.00 69.62 ? 409 LEU A CD1 1 ATOM 3033 C CD2 . LEU A 1 409 ? 31.147 -52.234 25.524 1.00 61.93 ? 409 LEU A CD2 1 ATOM 3034 N N . LEU A 1 410 ? 33.400 -57.318 26.224 1.00 74.35 ? 410 LEU A N 1 ATOM 3035 C CA . LEU A 1 410 ? 33.225 -58.756 26.048 1.00 81.21 ? 410 LEU A CA 1 ATOM 3036 C C . LEU A 1 410 ? 32.052 -59.266 26.881 1.00 84.13 ? 410 LEU A C 1 ATOM 3037 O O . LEU A 1 410 ? 31.438 -60.287 26.561 1.00 78.94 ? 410 LEU A O 1 ATOM 3038 C CB . LEU A 1 410 ? 34.510 -59.510 26.399 1.00 79.11 ? 410 LEU A CB 1 ATOM 3039 C CG . LEU A 1 410 ? 35.732 -59.167 25.550 1.00 78.22 ? 410 LEU A CG 1 ATOM 3040 C CD1 . LEU A 1 410 ? 36.748 -60.279 25.610 1.00 74.35 ? 410 LEU A CD1 1 ATOM 3041 C CD2 . LEU A 1 410 ? 35.311 -58.939 24.113 1.00 92.88 ? 410 LEU A CD2 1 ATOM 3042 N N . THR A 1 411 ? 31.753 -58.533 27.950 1.00 88.89 ? 411 THR A N 1 ATOM 3043 C CA . THR A 1 411 ? 30.633 -58.827 28.837 1.00 88.95 ? 411 THR A CA 1 ATOM 3044 C C . THR A 1 411 ? 29.296 -58.791 28.098 1.00 82.36 ? 411 THR A C 1 ATOM 3045 O O . THR A 1 411 ? 28.308 -59.378 28.533 1.00 87.17 ? 411 THR A O 1 ATOM 3046 C CB . THR A 1 411 ? 30.569 -57.787 29.953 1.00 85.82 ? 411 THR A CB 1 ATOM 3047 O OG1 . THR A 1 411 ? 30.863 -56.497 29.401 1.00 74.43 ? 411 THR A OG1 1 ATOM 3048 C CG2 . THR A 1 411 ? 31.573 -58.108 31.053 1.00 85.39 ? 411 THR A CG2 1 ATOM 3049 N N . LEU A 1 412 ? 29.266 -58.081 26.983 1.00 69.51 ? 412 LEU A N 1 ATOM 3050 C CA . LEU A 1 412 ? 28.043 -57.962 26.214 1.00 82.19 ? 412 LEU A CA 1 ATOM 3051 C C . LEU A 1 412 ? 27.984 -59.057 25.155 1.00 82.88 ? 412 LEU A C 1 ATOM 3052 O O . LEU A 1 412 ? 28.551 -58.927 24.066 1.00 81.60 ? 412 LEU A O 1 ATOM 3053 C CB . LEU A 1 412 ? 27.939 -56.568 25.586 1.00 87.37 ? 412 LEU A CB 1 ATOM 3054 C CG . LEU A 1 412 ? 28.240 -55.389 26.524 1.00 70.78 ? 412 LEU A CG 1 ATOM 3055 C CD1 . LEU A 1 412 ? 28.073 -54.071 25.780 1.00 64.60 ? 412 LEU A CD1 1 ATOM 3056 C CD2 . LEU A 1 412 ? 27.367 -55.436 27.775 1.00 56.69 ? 412 LEU A CD2 1 ATOM 3057 N N . LYS A 1 413 ? 27.284 -60.133 25.496 1.00 81.81 ? 413 LYS A N 1 ATOM 3058 C CA . LYS A 1 413 ? 27.205 -61.325 24.661 1.00 91.06 ? 413 LYS A CA 1 ATOM 3059 C C . LYS A 1 413 ? 26.310 -61.137 23.426 1.00 91.27 ? 413 LYS A C 1 ATOM 3060 O O . LYS A 1 413 ? 26.587 -61.656 22.336 1.00 80.21 ? 413 LYS A O 1 ATOM 3061 C CB . LYS A 1 413 ? 26.701 -62.494 25.513 1.00 102.95 ? 413 LYS A CB 1 ATOM 3062 C CG . LYS A 1 413 ? 27.602 -62.826 26.694 1.00 102.25 ? 413 LYS A CG 1 ATOM 3063 C CD . LYS A 1 413 ? 28.931 -63.390 26.214 1.00 108.64 ? 413 LYS A CD 1 ATOM 3064 C CE . LYS A 1 413 ? 30.067 -63.068 27.174 1.00 112.67 ? 413 LYS A CE 1 ATOM 3065 N NZ . LYS A 1 413 ? 31.369 -63.604 26.678 1.00 118.09 ? 413 LYS A NZ 1 ATOM 3066 N N . ASN A 1 414 ? 25.236 -60.381 23.605 1.00 95.30 ? 414 ASN A N 1 ATOM 3067 C CA . ASN A 1 414 ? 24.270 -60.168 22.543 1.00 88.59 ? 414 ASN A CA 1 ATOM 3068 C C . ASN A 1 414 ? 24.560 -58.926 21.704 1.00 87.89 ? 414 ASN A C 1 ATOM 3069 O O . ASN A 1 414 ? 23.749 -58.550 20.858 1.00 89.61 ? 414 ASN A O 1 ATOM 3070 C CB . ASN A 1 414 ? 22.865 -60.092 23.135 1.00 83.83 ? 414 ASN A CB 1 ATOM 3071 C CG . ASN A 1 414 ? 22.254 -61.456 23.358 1.00 92.24 ? 414 ASN A CG 1 ATOM 3072 O OD1 . ASN A 1 414 ? 22.064 -62.215 22.415 1.00 92.34 ? 414 ASN A OD1 1 ATOM 3073 N ND2 . ASN A 1 414 ? 21.932 -61.771 24.610 1.00 116.45 ? 414 ASN A ND2 1 ATOM 3074 N N . LEU A 1 415 ? 25.713 -58.296 21.934 1.00 86.11 ? 415 LEU A N 1 ATOM 3075 C CA . LEU A 1 415 ? 26.083 -57.086 21.194 1.00 83.38 ? 415 LEU A CA 1 ATOM 3076 C C . LEU A 1 415 ? 26.483 -57.415 19.758 1.00 78.53 ? 415 LEU A C 1 ATOM 3077 O O . LEU A 1 415 ? 27.387 -58.217 19.529 1.00 85.67 ? 415 LEU A O 1 ATOM 3078 C CB . LEU A 1 415 ? 27.212 -56.306 21.889 1.00 79.48 ? 415 LEU A CB 1 ATOM 3079 C CG . LEU A 1 415 ? 27.387 -54.870 21.369 1.00 76.55 ? 415 LEU A CG 1 ATOM 3080 C CD1 . LEU A 1 415 ? 26.466 -53.906 22.118 1.00 82.45 ? 415 LEU A CD1 1 ATOM 3081 C CD2 . LEU A 1 415 ? 28.823 -54.396 21.448 1.00 67.91 ? 415 LEU A CD2 1 ATOM 3082 N N . THR A 1 416 ? 25.817 -56.774 18.801 1.00 65.67 ? 416 THR A N 1 ATOM 3083 C CA . THR A 1 416 ? 25.986 -57.095 17.392 1.00 71.31 ? 416 THR A CA 1 ATOM 3084 C C . THR A 1 416 ? 26.332 -55.864 16.549 1.00 76.56 ? 416 THR A C 1 ATOM 3085 O O . THR A 1 416 ? 26.574 -55.961 15.347 1.00 81.29 ? 416 THR A O 1 ATOM 3086 C CB . THR A 1 416 ? 24.704 -57.765 16.832 1.00 83.22 ? 416 THR A CB 1 ATOM 3087 O OG1 . THR A 1 416 ? 23.697 -56.772 16.578 1.00 84.47 ? 416 THR A OG1 1 ATOM 3088 C CG2 . THR A 1 416 ? 24.170 -58.790 17.825 1.00 73.90 ? 416 THR A CG2 1 ATOM 3089 N N . SER A 1 417 ? 26.359 -54.704 17.191 1.00 76.96 ? 417 SER A N 1 ATOM 3090 C CA . SER A 1 417 ? 26.577 -53.444 16.491 1.00 68.63 ? 417 SER A CA 1 ATOM 3091 C C . SER A 1 417 ? 27.028 -52.342 17.451 1.00 67.42 ? 417 SER A C 1 ATOM 3092 O O . SER A 1 417 ? 26.265 -51.921 18.317 1.00 73.38 ? 417 SER A O 1 ATOM 3093 C CB . SER A 1 417 ? 25.288 -53.027 15.799 1.00 65.67 ? 417 SER A CB 1 ATOM 3094 O OG . SER A 1 417 ? 25.161 -51.626 15.838 1.00 71.35 ? 417 SER A OG 1 ATOM 3095 N N . LEU A 1 418 ? 28.268 -51.886 17.298 1.00 68.58 ? 418 LEU A N 1 ATOM 3096 C CA . LEU A 1 418 ? 28.856 -50.900 18.206 1.00 67.75 ? 418 LEU A CA 1 ATOM 3097 C C . LEU A 1 418 ? 29.307 -49.635 17.459 1.00 74.96 ? 418 LEU A C 1 ATOM 3098 O O . LEU A 1 418 ? 29.771 -49.705 16.318 1.00 73.34 ? 418 LEU A O 1 ATOM 3099 C CB . LEU A 1 418 ? 30.024 -51.512 18.982 1.00 59.59 ? 418 LEU A CB 1 ATOM 3100 C CG . LEU A 1 418 ? 30.861 -50.512 19.788 1.00 74.42 ? 418 LEU A CG 1 ATOM 3101 C CD1 . LEU A 1 418 ? 30.016 -49.908 20.886 1.00 81.04 ? 418 LEU A CD1 1 ATOM 3102 C CD2 . LEU A 1 418 ? 32.133 -51.132 20.378 1.00 70.81 ? 418 LEU A CD2 1 ATOM 3103 N N . ASP A 1 419 ? 29.145 -48.480 18.104 1.00 72.26 ? 419 ASP A N 1 ATOM 3104 C CA . ASP A 1 419 ? 29.509 -47.195 17.515 1.00 63.71 ? 419 ASP A CA 1 ATOM 3105 C C . ASP A 1 419 ? 30.343 -46.423 18.505 1.00 72.34 ? 419 ASP A C 1 ATOM 3106 O O . ASP A 1 419 ? 29.810 -45.848 19.452 1.00 76.52 ? 419 ASP A O 1 ATOM 3107 C CB . ASP A 1 419 ? 28.264 -46.371 17.155 1.00 64.01 ? 419 ASP A CB 1 ATOM 3108 C CG . ASP A 1 419 ? 28.610 -44.999 16.556 1.00 70.34 ? 419 ASP A CG 1 ATOM 3109 O OD1 . ASP A 1 419 ? 27.691 -44.279 16.083 1.00 64.57 ? 419 ASP A OD1 1 ATOM 3110 O OD2 . ASP A 1 419 ? 29.810 -44.642 16.557 1.00 70.98 ? 419 ASP A OD2 1 ATOM 3111 N N . ILE A 1 420 ? 31.652 -46.412 18.289 1.00 77.71 ? 420 ILE A N 1 ATOM 3112 C CA . ILE A 1 420 ? 32.559 -45.666 19.150 1.00 78.77 ? 420 ILE A CA 1 ATOM 3113 C C . ILE A 1 420 ? 33.180 -44.505 18.375 1.00 76.34 ? 420 ILE A C 1 ATOM 3114 O O . ILE A 1 420 ? 34.298 -44.077 18.670 1.00 78.69 ? 420 ILE A O 1 ATOM 3115 C CB . ILE A 1 420 ? 33.666 -46.577 19.731 1.00 81.96 ? 420 ILE A CB 1 ATOM 3116 C CG1 . ILE A 1 420 ? 34.682 -46.948 18.648 1.00 85.09 ? 420 ILE A CG1 1 ATOM 3117 C CG2 . ILE A 1 420 ? 33.056 -47.835 20.333 1.00 80.39 ? 420 ILE A CG2 1 ATOM 3118 C CD1 . ILE A 1 420 ? 35.683 -48.013 19.065 1.00 82.76 ? 420 ILE A CD1 1 ATOM 3119 N N . SER A 1 421 ? 32.435 -44.001 17.390 1.00 66.37 ? 421 SER A N 1 ATOM 3120 C CA . SER A 1 421 ? 32.885 -42.906 16.530 1.00 63.83 ? 421 SER A CA 1 ATOM 3121 C C . SER A 1 421 ? 33.086 -41.588 17.278 1.00 68.97 ? 421 SER A C 1 ATOM 3122 O O . SER A 1 421 ? 32.762 -41.472 18.458 1.00 71.26 ? 421 SER A O 1 ATOM 3123 C CB . SER A 1 421 ? 31.886 -42.685 15.398 1.00 64.67 ? 421 SER A CB 1 ATOM 3124 O OG . SER A 1 421 ? 30.669 -42.144 15.886 1.00 67.04 ? 421 SER A OG 1 ATOM 3125 N N . ARG A 1 422 ? 33.598 -40.592 16.566 1.00 68.00 ? 422 ARG A N 1 ATOM 3126 C CA . ARG A 1 422 ? 33.930 -39.288 17.146 1.00 69.77 ? 422 ARG A CA 1 ATOM 3127 C C . ARG A 1 422 ? 34.694 -39.369 18.490 1.00 70.97 ? 422 ARG A C 1 ATOM 3128 O O . ARG A 1 422 ? 34.537 -38.518 19.360 1.00 70.77 ? 422 ARG A O 1 ATOM 3129 C CB . ARG A 1 422 ? 32.697 -38.361 17.215 1.00 65.96 ? 422 ARG A CB 1 ATOM 3130 C CG . ARG A 1 422 ? 32.048 -38.069 15.857 1.00 78.82 ? 422 ARG A CG 1 ATOM 3131 C CD . ARG A 1 422 ? 31.224 -36.764 15.831 1.00 98.80 ? 422 ARG A CD 1 ATOM 3132 N NE . ARG A 1 422 ? 30.107 -36.836 14.872 1.00 109.46 ? 422 ARG A NE 1 ATOM 3133 C CZ . ARG A 1 422 ? 29.367 -35.801 14.458 1.00 92.14 ? 422 ARG A CZ 1 ATOM 3134 N NH1 . ARG A 1 422 ? 29.612 -34.566 14.902 1.00 80.75 ? 422 ARG A NH1 1 ATOM 3135 N NH2 . ARG A 1 422 ? 28.377 -36.004 13.591 1.00 69.59 ? 422 ARG A NH2 1 ATOM 3136 N N . ASN A 1 423 ? 35.536 -40.391 18.633 1.00 76.74 ? 423 ASN A N 1 ATOM 3137 C CA . ASN A 1 423 ? 36.423 -40.536 19.794 1.00 77.07 ? 423 ASN A CA 1 ATOM 3138 C C . ASN A 1 423 ? 37.898 -40.549 19.369 1.00 73.46 ? 423 ASN A C 1 ATOM 3139 O O . ASN A 1 423 ? 38.341 -41.497 18.725 1.00 79.86 ? 423 ASN A O 1 ATOM 3140 C CB . ASN A 1 423 ? 36.103 -41.831 20.564 1.00 79.61 ? 423 ASN A CB 1 ATOM 3141 C CG . ASN A 1 423 ? 34.791 -41.758 21.328 1.00 82.54 ? 423 ASN A CG 1 ATOM 3142 O OD1 . ASN A 1 423 ? 33.853 -41.091 20.907 1.00 93.36 ? 423 ASN A OD1 1 ATOM 3143 N ND2 . ASN A 1 423 ? 34.721 -42.451 22.451 1.00 77.75 ? 423 ASN A ND2 1 ATOM 3144 N N . THR A 1 424 ? 38.656 -39.520 19.745 1.00 61.39 ? 424 THR A N 1 ATOM 3145 C CA . THR A 1 424 ? 40.061 -39.357 19.314 1.00 61.64 ? 424 THR A CA 1 ATOM 3146 C C . THR A 1 424 ? 41.057 -40.468 19.718 1.00 57.98 ? 424 THR A C 1 ATOM 3147 O O . THR A 1 424 ? 41.997 -40.218 20.467 1.00 60.97 ? 424 THR A O 1 ATOM 3148 C CB . THR A 1 424 ? 40.607 -37.992 19.781 1.00 70.30 ? 424 THR A CB 1 ATOM 3149 O OG1 . THR A 1 424 ? 39.658 -37.388 20.679 1.00 84.49 ? 424 THR A OG1 1 ATOM 3150 C CG2 . THR A 1 424 ? 40.806 -37.068 18.596 1.00 68.66 ? 424 THR A CG2 1 ATOM 3151 N N . PHE A 1 425 ? 40.871 -41.674 19.180 1.00 58.47 ? 425 PHE A N 1 ATOM 3152 C CA . PHE A 1 425 ? 41.611 -42.874 19.597 1.00 63.99 ? 425 PHE A CA 1 ATOM 3153 C C . PHE A 1 425 ? 43.141 -42.854 19.427 1.00 76.05 ? 425 PHE A C 1 ATOM 3154 O O . PHE A 1 425 ? 43.666 -42.300 18.460 1.00 76.65 ? 425 PHE A O 1 ATOM 3155 C CB . PHE A 1 425 ? 41.055 -44.106 18.869 1.00 67.50 ? 425 PHE A CB 1 ATOM 3156 C CG . PHE A 1 425 ? 39.809 -44.671 19.488 1.00 79.69 ? 425 PHE A CG 1 ATOM 3157 C CD1 . PHE A 1 425 ? 38.597 -44.598 18.832 1.00 73.62 ? 425 PHE A CD1 1 ATOM 3158 C CD2 . PHE A 1 425 ? 39.849 -45.280 20.729 1.00 86.66 ? 425 PHE A CD2 1 ATOM 3159 C CE1 . PHE A 1 425 ? 37.444 -45.115 19.407 1.00 71.48 ? 425 PHE A CE1 1 ATOM 3160 C CE2 . PHE A 1 425 ? 38.697 -45.801 21.301 1.00 79.56 ? 425 PHE A CE2 1 ATOM 3161 C CZ . PHE A 1 425 ? 37.494 -45.714 20.637 1.00 67.16 ? 425 PHE A CZ 1 ATOM 3162 N N . HIS A 1 426 ? 43.845 -43.479 20.375 1.00 79.77 ? 426 HIS A N 1 ATOM 3163 C CA . HIS A 1 426 ? 45.251 -43.842 20.186 1.00 84.31 ? 426 HIS A CA 1 ATOM 3164 C C . HIS A 1 426 ? 45.314 -44.895 19.062 1.00 83.71 ? 426 HIS A C 1 ATOM 3165 O O . HIS A 1 426 ? 44.313 -45.539 18.752 1.00 75.15 ? 426 HIS A O 1 ATOM 3166 C CB . HIS A 1 426 ? 45.885 -44.425 21.475 1.00 101.54 ? 426 HIS A CB 1 ATOM 3167 C CG . HIS A 1 426 ? 45.925 -43.482 22.650 1.00 104.68 ? 426 HIS A CG 1 ATOM 3168 N ND1 . HIS A 1 426 ? 46.198 -42.134 22.529 1.00 111.76 ? 426 HIS A ND1 1 ATOM 3169 C CD2 . HIS A 1 426 ? 45.766 -43.711 23.977 1.00 92.82 ? 426 HIS A CD2 1 ATOM 3170 C CE1 . HIS A 1 426 ? 46.177 -41.569 23.725 1.00 97.43 ? 426 HIS A CE1 1 ATOM 3171 N NE2 . HIS A 1 426 ? 45.918 -42.505 24.621 1.00 92.86 ? 426 HIS A NE2 1 ATOM 3172 N N . PRO A 1 427 ? 46.497 -45.087 18.461 1.00 89.06 ? 427 PRO A N 1 ATOM 3173 C CA . PRO A 1 427 ? 46.680 -46.034 17.349 1.00 95.61 ? 427 PRO A CA 1 ATOM 3174 C C . PRO A 1 427 ? 46.335 -47.481 17.704 1.00 91.20 ? 427 PRO A C 1 ATOM 3175 O O . PRO A 1 427 ? 46.923 -48.029 18.632 1.00 92.05 ? 427 PRO A O 1 ATOM 3176 C CB . PRO A 1 427 ? 48.177 -45.934 17.051 1.00 100.90 ? 427 PRO A CB 1 ATOM 3177 C CG . PRO A 1 427 ? 48.593 -44.614 17.610 1.00 98.94 ? 427 PRO A CG 1 ATOM 3178 C CD . PRO A 1 427 ? 47.748 -44.395 18.810 1.00 90.55 ? 427 PRO A CD 1 ATOM 3179 N N . MET A 1 428 ? 45.415 -48.097 16.967 1.00 88.07 ? 428 MET A N 1 ATOM 3180 C CA . MET A 1 428 ? 45.015 -49.472 17.254 1.00 89.36 ? 428 MET A CA 1 ATOM 3181 C C . MET A 1 428 ? 46.162 -50.429 16.999 1.00 92.20 ? 428 MET A C 1 ATOM 3182 O O . MET A 1 428 ? 46.966 -50.206 16.098 1.00 89.94 ? 428 MET A O 1 ATOM 3183 C CB . MET A 1 428 ? 43.816 -49.874 16.405 1.00 86.83 ? 428 MET A CB 1 ATOM 3184 C CG . MET A 1 428 ? 44.032 -49.646 14.934 1.00 88.80 ? 428 MET A CG 1 ATOM 3185 S SD . MET A 1 428 ? 42.669 -50.276 13.947 1.00 128.00 ? 428 MET A SD 1 ATOM 3186 C CE . MET A 1 428 ? 41.543 -48.880 13.986 1.00 110.17 ? 428 MET A CE 1 ATOM 3187 N N . PRO A 1 429 ? 46.236 -51.505 17.795 1.00 100.70 ? 429 PRO A N 1 ATOM 3188 C CA . PRO A 1 429 ? 47.322 -52.484 17.769 1.00 106.44 ? 429 PRO A CA 1 ATOM 3189 C C . PRO A 1 429 ? 47.000 -53.632 16.823 1.00 111.23 ? 429 PRO A C 1 ATOM 3190 O O . PRO A 1 429 ? 46.020 -53.555 16.077 1.00 114.69 ? 429 PRO A O 1 ATOM 3191 C CB . PRO A 1 429 ? 47.343 -53.018 19.207 1.00 100.28 ? 429 PRO A CB 1 ATOM 3192 C CG . PRO A 1 429 ? 46.094 -52.474 19.874 1.00 101.54 ? 429 PRO A CG 1 ATOM 3193 C CD . PRO A 1 429 ? 45.240 -51.865 18.808 1.00 101.22 ? 429 PRO A CD 1 ATOM 3194 N N . ASP A 1 430 ? 47.811 -54.685 16.865 1.00 108.74 ? 430 ASP A N 1 ATOM 3195 C CA . ASP A 1 430 ? 47.579 -55.865 16.040 1.00 114.16 ? 430 ASP A CA 1 ATOM 3196 C C . ASP A 1 430 ? 46.532 -56.788 16.662 1.00 107.95 ? 430 ASP A C 1 ATOM 3197 O O . ASP A 1 430 ? 45.726 -57.393 15.952 1.00 94.42 ? 430 ASP A O 1 ATOM 3198 C CB . ASP A 1 430 ? 48.889 -56.630 15.817 1.00 126.29 ? 430 ASP A CB 1 ATOM 3199 C CG . ASP A 1 430 ? 49.736 -56.034 14.701 1.00 139.02 ? 430 ASP A CG 1 ATOM 3200 O OD1 . ASP A 1 430 ? 50.982 -56.121 14.793 1.00 140.28 ? 430 ASP A OD1 1 ATOM 3201 O OD2 . ASP A 1 430 ? 49.160 -55.485 13.732 1.00 142.84 ? 430 ASP A OD2 1 ATOM 3202 N N . SER A 1 431 ? 46.539 -56.875 17.991 1.00 116.16 ? 431 SER A N 1 ATOM 3203 C CA . SER A 1 431 ? 45.694 -57.830 18.710 1.00 109.91 ? 431 SER A CA 1 ATOM 3204 C C . SER A 1 431 ? 44.661 -57.177 19.648 1.00 104.72 ? 431 SER A C 1 ATOM 3205 O O . SER A 1 431 ? 45.024 -56.567 20.659 1.00 103.62 ? 431 SER A O 1 ATOM 3206 C CB . SER A 1 431 ? 46.575 -58.807 19.492 1.00 102.62 ? 431 SER A CB 1 ATOM 3207 O OG . SER A 1 431 ? 45.982 -60.092 19.535 1.00 103.63 ? 431 SER A OG 1 ATOM 3208 N N . CYS A 1 432 ? 43.380 -57.310 19.291 1.00 101.75 ? 432 CYS A N 1 ATOM 3209 C CA . CYS A 1 432 ? 42.258 -56.844 20.114 1.00 102.13 ? 432 CYS A CA 1 ATOM 3210 C C . CYS A 1 432 ? 41.221 -57.963 20.212 1.00 96.94 ? 432 CYS A C 1 ATOM 3211 O O . CYS A 1 432 ? 41.242 -58.891 19.413 1.00 79.91 ? 432 CYS A O 1 ATOM 3212 C CB . CYS A 1 432 ? 41.588 -55.596 19.506 1.00 96.01 ? 432 CYS A CB 1 ATOM 3213 S SG . CYS A 1 432 ? 42.675 -54.199 19.086 1.00 140.96 ? 432 CYS A SG 1 ATOM 3214 N N . GLN A 1 433 ? 40.322 -57.882 21.192 1.00 104.59 ? 433 GLN A N 1 ATOM 3215 C CA . GLN A 1 433 ? 39.161 -58.770 21.226 1.00 101.26 ? 433 GLN A CA 1 ATOM 3216 C C . GLN A 1 433 ? 37.904 -57.924 21.225 1.00 99.46 ? 433 GLN A C 1 ATOM 3217 O O . GLN A 1 433 ? 37.893 -56.831 21.789 1.00 105.23 ? 433 GLN A O 1 ATOM 3218 C CB . GLN A 1 433 ? 39.132 -59.639 22.480 1.00 100.75 ? 433 GLN A CB 1 ATOM 3219 C CG . GLN A 1 433 ? 40.468 -59.991 23.087 1.00 104.13 ? 433 GLN A CG 1 ATOM 3220 C CD . GLN A 1 433 ? 40.295 -60.853 24.322 1.00 109.66 ? 433 GLN A CD 1 ATOM 3221 O OE1 . GLN A 1 433 ? 39.912 -62.024 24.229 1.00 101.00 ? 433 GLN A OE1 1 ATOM 3222 N NE2 . GLN A 1 433 ? 40.559 -60.271 25.493 1.00 116.89 ? 433 GLN A NE2 1 ATOM 3223 N N . TRP A 1 434 ? 36.844 -58.433 20.604 1.00 89.15 ? 434 TRP A N 1 ATOM 3224 C CA . TRP A 1 434 ? 35.550 -57.758 20.615 1.00 83.54 ? 434 TRP A CA 1 ATOM 3225 C C . TRP A 1 434 ? 34.433 -58.776 20.760 1.00 86.09 ? 434 TRP A C 1 ATOM 3226 O O . TRP A 1 434 ? 34.676 -59.978 20.696 1.00 95.40 ? 434 TRP A O 1 ATOM 3227 C CB . TRP A 1 434 ? 35.342 -56.963 19.332 1.00 78.95 ? 434 TRP A CB 1 ATOM 3228 C CG . TRP A 1 434 ? 36.450 -56.026 19.008 1.00 85.15 ? 434 TRP A CG 1 ATOM 3229 C CD1 . TRP A 1 434 ? 37.635 -56.339 18.424 1.00 95.83 ? 434 TRP A CD1 1 ATOM 3230 C CD2 . TRP A 1 434 ? 36.474 -54.610 19.232 1.00 84.94 ? 434 TRP A CD2 1 ATOM 3231 N NE1 . TRP A 1 434 ? 38.403 -55.211 18.273 1.00 101.98 ? 434 TRP A NE1 1 ATOM 3232 C CE2 . TRP A 1 434 ? 37.712 -54.136 18.763 1.00 89.66 ? 434 TRP A CE2 1 ATOM 3233 C CE3 . TRP A 1 434 ? 35.573 -53.703 19.788 1.00 81.23 ? 434 TRP A CE3 1 ATOM 3234 C CZ2 . TRP A 1 434 ? 38.071 -52.794 18.830 1.00 78.08 ? 434 TRP A CZ2 1 ATOM 3235 C CZ3 . TRP A 1 434 ? 35.932 -52.373 19.853 1.00 82.37 ? 434 TRP A CZ3 1 ATOM 3236 C CH2 . TRP A 1 434 ? 37.170 -51.931 19.376 1.00 76.80 ? 434 TRP A CH2 1 ATOM 3237 N N . PRO A 1 435 ? 33.202 -58.298 20.978 1.00 83.24 ? 435 PRO A N 1 ATOM 3238 C CA . PRO A 1 435 ? 32.039 -59.186 20.975 1.00 88.72 ? 435 PRO A CA 1 ATOM 3239 C C . PRO A 1 435 ? 32.024 -60.061 19.727 1.00 90.90 ? 435 PRO A C 1 ATOM 3240 O O . PRO A 1 435 ? 32.136 -59.546 18.619 1.00 90.68 ? 435 PRO A O 1 ATOM 3241 C CB . PRO A 1 435 ? 30.875 -58.205 20.960 1.00 86.46 ? 435 PRO A CB 1 ATOM 3242 C CG . PRO A 1 435 ? 31.388 -57.063 21.764 1.00 85.01 ? 435 PRO A CG 1 ATOM 3243 C CD . PRO A 1 435 ? 32.852 -56.943 21.433 1.00 80.79 ? 435 PRO A CD 1 ATOM 3244 N N . GLU A 1 436 ? 31.891 -61.370 19.907 1.00 92.55 ? 436 GLU A N 1 ATOM 3245 C CA . GLU A 1 436 ? 32.044 -62.293 18.793 1.00 102.85 ? 436 GLU A CA 1 ATOM 3246 C C . GLU A 1 436 ? 30.908 -62.157 17.779 1.00 101.00 ? 436 GLU A C 1 ATOM 3247 O O . GLU A 1 436 ? 30.985 -62.717 16.685 1.00 104.30 ? 436 GLU A O 1 ATOM 3248 C CB . GLU A 1 436 ? 32.151 -63.736 19.297 1.00 120.48 ? 436 GLU A CB 1 ATOM 3249 C CG . GLU A 1 436 ? 33.297 -64.557 18.679 1.00 133.75 ? 436 GLU A CG 1 ATOM 3250 C CD . GLU A 1 436 ? 34.618 -64.407 19.440 1.00 141.40 ? 436 GLU A CD 1 ATOM 3251 O OE1 . GLU A 1 436 ? 35.306 -65.431 19.660 1.00 140.93 ? 436 GLU A OE1 1 ATOM 3252 O OE2 . GLU A 1 436 ? 34.963 -63.266 19.825 1.00 141.30 ? 436 GLU A OE2 1 ATOM 3253 N N . LYS A 1 437 ? 29.860 -61.417 18.141 1.00 95.22 ? 437 LYS A N 1 ATOM 3254 C CA . LYS A 1 437 ? 28.724 -61.192 17.240 1.00 82.01 ? 437 LYS A CA 1 ATOM 3255 C C . LYS A 1 437 ? 28.674 -59.768 16.695 1.00 77.28 ? 437 LYS A C 1 ATOM 3256 O O . LYS A 1 437 ? 27.673 -59.359 16.113 1.00 67.01 ? 437 LYS A O 1 ATOM 3257 C CB . LYS A 1 437 ? 27.391 -61.511 17.928 1.00 77.24 ? 437 LYS A CB 1 ATOM 3258 C CG . LYS A 1 437 ? 27.288 -62.934 18.424 1.00 92.94 ? 437 LYS A CG 1 ATOM 3259 C CD . LYS A 1 437 ? 25.850 -63.432 18.420 1.00 109.01 ? 437 LYS A CD 1 ATOM 3260 C CE . LYS A 1 437 ? 25.066 -62.956 19.631 1.00 114.45 ? 437 LYS A CE 1 ATOM 3261 N NZ . LYS A 1 437 ? 23.936 -63.893 19.922 1.00 115.78 ? 437 LYS A NZ 1 ATOM 3262 N N . MET A 1 438 ? 29.751 -59.016 16.900 1.00 85.31 ? 438 MET A N 1 ATOM 3263 C CA . MET A 1 438 ? 29.817 -57.626 16.464 1.00 79.93 ? 438 MET A CA 1 ATOM 3264 C C . MET A 1 438 ? 29.917 -57.598 14.944 1.00 83.85 ? 438 MET A C 1 ATOM 3265 O O . MET A 1 438 ? 30.971 -57.884 14.376 1.00 82.71 ? 438 MET A O 1 ATOM 3266 C CB . MET A 1 438 ? 31.011 -56.910 17.120 1.00 73.74 ? 438 MET A CB 1 ATOM 3267 C CG . MET A 1 438 ? 31.034 -55.400 16.921 1.00 76.53 ? 438 MET A CG 1 ATOM 3268 S SD . MET A 1 438 ? 32.527 -54.556 17.497 1.00 83.27 ? 438 MET A SD 1 ATOM 3269 C CE . MET A 1 438 ? 32.200 -54.459 19.252 1.00 292.80 ? 438 MET A CE 1 ATOM 3270 N N . ARG A 1 439 ? 28.804 -57.277 14.292 1.00 81.72 ? 439 ARG A N 1 ATOM 3271 C CA . ARG A 1 439 ? 28.753 -57.232 12.837 1.00 84.79 ? 439 ARG A CA 1 ATOM 3272 C C . ARG A 1 439 ? 28.915 -55.802 12.333 1.00 92.48 ? 439 ARG A C 1 ATOM 3273 O O . ARG A 1 439 ? 29.236 -55.580 11.169 1.00 97.80 ? 439 ARG A O 1 ATOM 3274 C CB . ARG A 1 439 ? 27.430 -57.800 12.307 1.00 87.48 ? 439 ARG A CB 1 ATOM 3275 C CG . ARG A 1 439 ? 26.988 -59.165 12.845 1.00 88.48 ? 439 ARG A CG 1 ATOM 3276 C CD . ARG A 1 439 ? 25.528 -59.439 12.445 1.00 99.16 ? 439 ARG A CD 1 ATOM 3277 N NE . ARG A 1 439 ? 24.583 -58.442 12.976 1.00 108.96 ? 439 ARG A NE 1 ATOM 3278 C CZ . ARG A 1 439 ? 24.155 -57.352 12.329 1.00 103.58 ? 439 ARG A CZ 1 ATOM 3279 N NH1 . ARG A 1 439 ? 24.573 -57.083 11.097 1.00 103.13 ? 439 ARG A NH1 1 ATOM 3280 N NH2 . ARG A 1 439 ? 23.302 -56.519 12.920 1.00 91.75 ? 439 ARG A NH2 1 ATOM 3281 N N . PHE A 1 440 ? 28.675 -54.828 13.204 1.00 94.53 ? 440 PHE A N 1 ATOM 3282 C CA . PHE A 1 440 ? 28.714 -53.425 12.799 1.00 83.74 ? 440 PHE A CA 1 ATOM 3283 C C . PHE A 1 440 ? 29.649 -52.644 13.704 1.00 75.24 ? 440 PHE A C 1 ATOM 3284 O O . PHE A 1 440 ? 29.442 -52.600 14.910 1.00 86.19 ? 440 PHE A O 1 ATOM 3285 C CB . PHE A 1 440 ? 27.305 -52.818 12.840 1.00 73.35 ? 440 PHE A CB 1 ATOM 3286 C CG . PHE A 1 440 ? 27.257 -51.347 12.510 1.00 80.74 ? 440 PHE A CG 1 ATOM 3287 C CD1 . PHE A 1 440 ? 26.573 -50.896 11.396 1.00 91.20 ? 440 PHE A CD1 1 ATOM 3288 C CD2 . PHE A 1 440 ? 27.882 -50.414 13.321 1.00 82.25 ? 440 PHE A CD2 1 ATOM 3289 C CE1 . PHE A 1 440 ? 26.518 -49.545 11.092 1.00 86.43 ? 440 PHE A CE1 1 ATOM 3290 C CE2 . PHE A 1 440 ? 27.835 -49.065 13.021 1.00 78.12 ? 440 PHE A CE2 1 ATOM 3291 C CZ . PHE A 1 440 ? 27.155 -48.634 11.905 1.00 84.14 ? 440 PHE A CZ 1 ATOM 3292 N N . LEU A 1 441 ? 30.674 -52.033 13.121 1.00 62.80 ? 441 LEU A N 1 ATOM 3293 C CA . LEU A 1 441 ? 31.575 -51.162 13.864 1.00 64.74 ? 441 LEU A CA 1 ATOM 3294 C C . LEU A 1 441 ? 31.703 -49.810 13.167 1.00 73.34 ? 441 LEU A C 1 ATOM 3295 O O . LEU A 1 441 ? 32.062 -49.742 11.989 1.00 78.74 ? 441 LEU A O 1 ATOM 3296 C CB . LEU A 1 441 ? 32.955 -51.807 14.020 1.00 64.45 ? 441 LEU A CB 1 ATOM 3297 C CG . LEU A 1 441 ? 33.955 -50.999 14.859 1.00 76.13 ? 441 LEU A CG 1 ATOM 3298 C CD1 . LEU A 1 441 ? 33.393 -50.773 16.247 1.00 85.06 ? 441 LEU A CD1 1 ATOM 3299 C CD2 . LEU A 1 441 ? 35.324 -51.665 14.948 1.00 74.51 ? 441 LEU A CD2 1 ATOM 3300 N N . ASN A 1 442 ? 31.407 -48.733 13.887 1.00 62.13 ? 442 ASN A N 1 ATOM 3301 C CA . ASN A 1 442 ? 31.537 -47.399 13.319 1.00 58.13 ? 442 ASN A CA 1 ATOM 3302 C C . ASN A 1 442 ? 32.713 -46.705 13.991 1.00 68.13 ? 442 ASN A C 1 ATOM 3303 O O . ASN A 1 442 ? 32.667 -46.436 15.178 1.00 75.49 ? 442 ASN A O 1 ATOM 3304 C CB . ASN A 1 442 ? 30.230 -46.627 13.510 1.00 64.62 ? 442 ASN A CB 1 ATOM 3305 C CG . ASN A 1 442 ? 30.195 -45.300 12.753 1.00 80.33 ? 442 ASN A CG 1 ATOM 3306 O OD1 . ASN A 1 442 ? 31.241 -44.731 12.412 1.00 75.61 ? 442 ASN A OD1 1 ATOM 3307 N ND2 . ASN A 1 442 ? 28.969 -44.791 12.507 1.00 88.41 ? 442 ASN A ND2 1 ATOM 3308 N N . LEU A 1 443 ? 33.778 -46.459 13.230 1.00 79.77 ? 443 LEU A N 1 ATOM 3309 C CA . LEU A 1 443 ? 34.998 -45.818 13.732 1.00 70.35 ? 443 LEU A CA 1 ATOM 3310 C C . LEU A 1 443 ? 35.228 -44.488 13.016 1.00 70.33 ? 443 LEU A C 1 ATOM 3311 O O . LEU A 1 443 ? 36.353 -43.997 12.934 1.00 71.79 ? 443 LEU A O 1 ATOM 3312 C CB . LEU A 1 443 ? 36.219 -46.723 13.521 1.00 69.93 ? 443 LEU A CB 1 ATOM 3313 C CG . LEU A 1 443 ? 36.284 -48.037 14.298 1.00 75.64 ? 443 LEU A CG 1 ATOM 3314 C CD1 . LEU A 1 443 ? 37.659 -48.709 14.206 1.00 68.64 ? 443 LEU A CD1 1 ATOM 3315 C CD2 . LEU A 1 443 ? 35.954 -47.741 15.729 1.00 81.78 ? 443 LEU A CD2 1 ATOM 3316 N N . SER A 1 444 ? 34.154 -43.915 12.490 1.00 68.60 ? 444 SER A N 1 ATOM 3317 C CA . SER A 1 444 ? 34.243 -42.677 11.726 1.00 81.55 ? 444 SER A CA 1 ATOM 3318 C C . SER A 1 444 ? 34.739 -41.500 12.563 1.00 85.11 ? 444 SER A C 1 ATOM 3319 O O . SER A 1 444 ? 34.614 -41.493 13.787 1.00 91.48 ? 444 SER A O 1 ATOM 3320 C CB . SER A 1 444 ? 32.879 -42.345 11.111 1.00 87.09 ? 444 SER A CB 1 ATOM 3321 O OG . SER A 1 444 ? 32.878 -41.054 10.527 1.00 90.89 ? 444 SER A OG 1 ATOM 3322 N N . SER A 1 445 ? 35.306 -40.506 11.889 1.00 84.21 ? 445 SER A N 1 ATOM 3323 C CA . SER A 1 445 ? 35.686 -39.255 12.536 1.00 88.18 ? 445 SER A CA 1 ATOM 3324 C C . SER A 1 445 ? 36.530 -39.502 13.791 1.00 83.08 ? 445 SER A C 1 ATOM 3325 O O . SER A 1 445 ? 36.534 -38.715 14.734 1.00 67.06 ? 445 SER A O 1 ATOM 3326 C CB . SER A 1 445 ? 34.432 -38.448 12.866 1.00 90.88 ? 445 SER A CB 1 ATOM 3327 O OG . SER A 1 445 ? 33.530 -38.469 11.768 1.00 92.90 ? 445 SER A OG 1 ATOM 3328 N N . THR A 1 446 ? 37.281 -40.593 13.760 1.00 85.55 ? 446 THR A N 1 ATOM 3329 C CA . THR A 1 446 ? 37.944 -41.109 14.939 1.00 76.50 ? 446 THR A CA 1 ATOM 3330 C C . THR A 1 446 ? 39.437 -40.752 14.994 1.00 74.74 ? 446 THR A C 1 ATOM 3331 O O . THR A 1 446 ? 40.161 -41.231 15.862 1.00 68.65 ? 446 THR A O 1 ATOM 3332 C CB . THR A 1 446 ? 37.737 -42.635 15.005 1.00 77.65 ? 446 THR A CB 1 ATOM 3333 O OG1 . THR A 1 446 ? 37.569 -43.048 16.361 1.00 92.33 ? 446 THR A OG1 1 ATOM 3334 C CG2 . THR A 1 446 ? 38.890 -43.383 14.360 1.00 67.97 ? 446 THR A CG2 1 ATOM 3335 N N . GLY A 1 447 ? 39.893 -39.912 14.067 1.00 82.73 ? 447 GLY A N 1 ATOM 3336 C CA . GLY A 1 447 ? 41.266 -39.425 14.070 1.00 87.90 ? 447 GLY A CA 1 ATOM 3337 C C . GLY A 1 447 ? 42.383 -40.371 13.621 1.00 90.66 ? 447 GLY A C 1 ATOM 3338 O O . GLY A 1 447 ? 43.546 -39.960 13.531 1.00 87.09 ? 447 GLY A O 1 ATOM 3339 N N . ILE A 1 448 ? 42.051 -41.627 13.329 1.00 86.61 ? 448 ILE A N 1 ATOM 3340 C CA . ILE A 1 448 ? 43.081 -42.623 13.025 1.00 87.30 ? 448 ILE A CA 1 ATOM 3341 C C . ILE A 1 448 ? 43.742 -42.442 11.658 1.00 98.12 ? 448 ILE A C 1 ATOM 3342 O O . ILE A 1 448 ? 43.211 -41.749 10.790 1.00 101.34 ? 448 ILE A O 1 ATOM 3343 C CB . ILE A 1 448 ? 42.540 -44.055 13.143 1.00 86.10 ? 448 ILE A CB 1 ATOM 3344 C CG1 . ILE A 1 448 ? 41.414 -44.299 12.137 1.00 84.86 ? 448 ILE A CG1 1 ATOM 3345 C CG2 . ILE A 1 448 ? 42.075 -44.325 14.558 1.00 88.42 ? 448 ILE A CG2 1 ATOM 3346 C CD1 . ILE A 1 448 ? 40.849 -45.707 12.197 1.00 79.42 ? 448 ILE A CD1 1 ATOM 3347 N N . ARG A 1 449 ? 44.902 -43.074 11.480 1.00 99.13 ? 449 ARG A N 1 ATOM 3348 C CA . ARG A 1 449 ? 45.676 -42.960 10.244 1.00 95.51 ? 449 ARG A CA 1 ATOM 3349 C C . ARG A 1 449 ? 46.294 -44.281 9.772 1.00 98.40 ? 449 ARG A C 1 ATOM 3350 O O . ARG A 1 449 ? 47.255 -44.291 9.006 1.00 107.10 ? 449 ARG A O 1 ATOM 3351 C CB . ARG A 1 449 ? 46.754 -41.885 10.392 1.00 87.56 ? 449 ARG A CB 1 ATOM 3352 C CG . ARG A 1 449 ? 47.137 -41.594 11.819 1.00 89.41 ? 449 ARG A CG 1 ATOM 3353 C CD . ARG A 1 449 ? 47.713 -40.190 11.951 1.00 106.96 ? 449 ARG A CD 1 ATOM 3354 N NE . ARG A 1 449 ? 49.165 -40.174 11.785 1.00 126.02 ? 449 ARG A NE 1 ATOM 3355 C CZ . ARG A 1 449 ? 49.920 -39.087 11.914 1.00 129.37 ? 449 ARG A CZ 1 ATOM 3356 N NH1 . ARG A 1 449 ? 49.357 -37.919 12.201 1.00 126.21 ? 449 ARG A NH1 1 ATOM 3357 N NH2 . ARG A 1 449 ? 51.237 -39.169 11.753 1.00 126.33 ? 449 ARG A NH2 1 ATOM 3358 N N . VAL A 1 450 ? 45.719 -45.388 10.217 1.00 87.45 ? 450 VAL A N 1 ATOM 3359 C CA . VAL A 1 450 ? 46.208 -46.716 9.891 1.00 93.74 ? 450 VAL A CA 1 ATOM 3360 C C . VAL A 1 450 ? 45.068 -47.646 10.260 1.00 97.30 ? 450 VAL A C 1 ATOM 3361 O O . VAL A 1 450 ? 44.296 -47.333 11.157 1.00 98.72 ? 450 VAL A O 1 ATOM 3362 C CB . VAL A 1 450 ? 47.477 -47.078 10.738 1.00 87.99 ? 450 VAL A CB 1 ATOM 3363 C CG1 . VAL A 1 450 ? 47.648 -48.598 10.896 1.00 85.41 ? 450 VAL A CG1 1 ATOM 3364 C CG2 . VAL A 1 450 ? 48.746 -46.443 10.155 1.00 78.92 ? 450 VAL A CG2 1 ATOM 3365 N N . VAL A 1 451 ? 44.928 -48.773 9.575 1.00 98.50 ? 451 VAL A N 1 ATOM 3366 C CA . VAL A 1 451 ? 44.003 -49.795 10.059 1.00 96.50 ? 451 VAL A CA 1 ATOM 3367 C C . VAL A 1 451 ? 44.695 -51.150 10.223 1.00 98.48 ? 451 VAL A C 1 ATOM 3368 O O . VAL A 1 451 ? 45.157 -51.743 9.249 1.00 104.21 ? 451 VAL A O 1 ATOM 3369 C CB . VAL A 1 451 ? 42.744 -49.926 9.179 1.00 88.69 ? 451 VAL A CB 1 ATOM 3370 C CG1 . VAL A 1 451 ? 41.832 -51.010 9.735 1.00 86.07 ? 451 VAL A CG1 1 ATOM 3371 C CG2 . VAL A 1 451 ? 42.004 -48.595 9.105 1.00 73.53 ? 451 VAL A CG2 1 ATOM 3372 N N . LYS A 1 452 ? 44.772 -51.623 11.464 1.00 91.13 ? 452 LYS A N 1 ATOM 3373 C CA . LYS A 1 452 ? 45.429 -52.891 11.775 1.00 98.25 ? 452 LYS A CA 1 ATOM 3374 C C . LYS A 1 452 ? 44.407 -54.023 11.944 1.00 101.17 ? 452 LYS A C 1 ATOM 3375 O O . LYS A 1 452 ? 43.204 -53.816 11.774 1.00 94.22 ? 452 LYS A O 1 ATOM 3376 C CB . LYS A 1 452 ? 46.282 -52.764 13.044 1.00 95.21 ? 452 LYS A CB 1 ATOM 3377 C CG . LYS A 1 452 ? 47.464 -51.799 12.965 1.00 100.77 ? 452 LYS A CG 1 ATOM 3378 C CD . LYS A 1 452 ? 48.734 -52.512 12.505 1.00 115.52 ? 452 LYS A CD 1 ATOM 3379 C CE . LYS A 1 452 ? 49.944 -52.170 13.385 1.00 117.78 ? 452 LYS A CE 1 ATOM 3380 N NZ . LYS A 1 452 ? 50.150 -50.707 13.588 1.00 115.76 ? 452 LYS A NZ 1 ATOM 3381 N N . THR A 1 453 ? 44.903 -55.213 12.287 1.00 100.43 ? 453 THR A N 1 ATOM 3382 C CA . THR A 1 453 ? 44.070 -56.402 12.475 1.00 97.67 ? 453 THR A CA 1 ATOM 3383 C C . THR A 1 453 ? 43.333 -56.405 13.814 1.00 100.71 ? 453 THR A C 1 ATOM 3384 O O . THR A 1 453 ? 42.856 -57.443 14.280 1.00 94.40 ? 453 THR A O 1 ATOM 3385 C CB . THR A 1 453 ? 44.910 -57.680 12.369 1.00 101.81 ? 453 THR A CB 1 ATOM 3386 O OG1 . THR A 1 453 ? 46.253 -57.404 12.795 1.00 94.92 ? 453 THR A OG1 1 ATOM 3387 C CG2 . THR A 1 453 ? 44.927 -58.187 10.931 1.00 101.44 ? 453 THR A CG2 1 ATOM 3388 N N . CYS A 1 454 ? 43.260 -55.235 14.436 1.00 103.51 ? 454 CYS A N 1 ATOM 3389 C CA . CYS A 1 454 ? 42.440 -55.040 15.617 1.00 90.98 ? 454 CYS A CA 1 ATOM 3390 C C . CYS A 1 454 ? 40.995 -55.335 15.234 1.00 96.66 ? 454 CYS A C 1 ATOM 3391 O O . CYS A 1 454 ? 40.360 -56.220 15.807 1.00 102.55 ? 454 CYS A O 1 ATOM 3392 C CB . CYS A 1 454 ? 42.583 -53.601 16.100 1.00 84.20 ? 454 CYS A CB 1 ATOM 3393 S SG . CYS A 1 454 ? 41.685 -53.202 17.600 1.00 106.84 ? 454 CYS A SG 1 ATOM 3394 N N . ILE A 1 455 ? 40.498 -54.599 14.240 1.00 93.28 ? 455 ILE A N 1 ATOM 3395 C CA . ILE A 1 455 ? 39.166 -54.802 13.672 1.00 92.78 ? 455 ILE A CA 1 ATOM 3396 C C . ILE A 1 455 ? 38.908 -56.272 13.359 1.00 102.58 ? 455 ILE A C 1 ATOM 3397 O O . ILE A 1 455 ? 39.666 -56.885 12.608 1.00 99.35 ? 455 ILE A O 1 ATOM 3398 C CB . ILE A 1 455 ? 38.997 -54.005 12.364 1.00 93.52 ? 455 ILE A CB 1 ATOM 3399 C CG1 . ILE A 1 455 ? 38.940 -52.509 12.646 1.00 87.36 ? 455 ILE A CG1 1 ATOM 3400 C CG2 . ILE A 1 455 ? 37.734 -54.425 11.638 1.00 101.29 ? 455 ILE A CG2 1 ATOM 3401 C CD1 . ILE A 1 455 ? 40.198 -51.958 13.215 1.00 89.14 ? 455 ILE A CD1 1 ATOM 3402 N N . PRO A 1 456 ? 37.821 -56.834 13.919 1.00 111.93 ? 456 PRO A N 1 ATOM 3403 C CA . PRO A 1 456 ? 37.476 -58.265 13.857 1.00 115.02 ? 456 PRO A CA 1 ATOM 3404 C C . PRO A 1 456 ? 36.979 -58.725 12.486 1.00 127.12 ? 456 PRO A C 1 ATOM 3405 O O . PRO A 1 456 ? 36.226 -58.004 11.827 1.00 135.06 ? 456 PRO A O 1 ATOM 3406 C CB . PRO A 1 456 ? 36.334 -58.404 14.876 1.00 105.03 ? 456 PRO A CB 1 ATOM 3407 C CG . PRO A 1 456 ? 36.278 -57.096 15.613 1.00 110.17 ? 456 PRO A CG 1 ATOM 3408 C CD . PRO A 1 456 ? 36.833 -56.066 14.692 1.00 109.98 ? 456 PRO A CD 1 ATOM 3409 N N . GLN A 1 457 ? 37.381 -59.924 12.074 1.00 124.13 ? 457 GLN A N 1 ATOM 3410 C CA . GLN A 1 457 ? 36.938 -60.480 10.800 1.00 120.53 ? 457 GLN A CA 1 ATOM 3411 C C . GLN A 1 457 ? 35.417 -60.538 10.683 1.00 127.33 ? 457 GLN A C 1 ATOM 3412 O O . GLN A 1 457 ? 34.874 -60.512 9.574 1.00 142.04 ? 457 GLN A O 1 ATOM 3413 C CB . GLN A 1 457 ? 37.514 -61.882 10.589 1.00 120.48 ? 457 GLN A CB 1 ATOM 3414 C CG . GLN A 1 457 ? 38.915 -61.917 10.004 1.00 122.94 ? 457 GLN A CG 1 ATOM 3415 C CD . GLN A 1 457 ? 39.269 -63.281 9.442 1.00 124.87 ? 457 GLN A CD 1 ATOM 3416 O OE1 . GLN A 1 457 ? 40.446 -63.615 9.278 1.00 127.44 ? 457 GLN A OE1 1 ATOM 3417 N NE2 . GLN A 1 457 ? 38.246 -64.081 9.147 1.00 119.62 ? 457 GLN A NE2 1 ATOM 3418 N N . THR A 1 458 ? 34.734 -60.618 11.823 1.00 114.19 ? 458 THR A N 1 ATOM 3419 C CA . THR A 1 458 ? 33.282 -60.815 11.851 1.00 106.49 ? 458 THR A CA 1 ATOM 3420 C C . THR A 1 458 ? 32.494 -59.637 11.279 1.00 103.55 ? 458 THR A C 1 ATOM 3421 O O . THR A 1 458 ? 31.268 -59.691 11.160 1.00 99.56 ? 458 THR A O 1 ATOM 3422 C CB . THR A 1 458 ? 32.791 -61.066 13.280 1.00 98.11 ? 458 THR A CB 1 ATOM 3423 O OG1 . THR A 1 458 ? 33.253 -60.010 14.132 1.00 95.64 ? 458 THR A OG1 1 ATOM 3424 C CG2 . THR A 1 458 ? 33.311 -62.397 13.795 1.00 92.62 ? 458 THR A CG2 1 ATOM 3425 N N . LEU A 1 459 ? 33.213 -58.589 10.902 1.00 101.23 ? 459 LEU A N 1 ATOM 3426 C CA . LEU A 1 459 ? 32.609 -57.305 10.578 1.00 97.59 ? 459 LEU A CA 1 ATOM 3427 C C . LEU A 1 459 ? 31.946 -57.214 9.187 1.00 102.21 ? 459 LEU A C 1 ATOM 3428 O O . LEU A 1 459 ? 32.631 -57.091 8.173 1.00 107.26 ? 459 LEU A O 1 ATOM 3429 C CB . LEU A 1 459 ? 33.672 -56.216 10.739 1.00 88.93 ? 459 LEU A CB 1 ATOM 3430 C CG . LEU A 1 459 ? 33.215 -54.948 11.446 1.00 88.52 ? 459 LEU A CG 1 ATOM 3431 C CD1 . LEU A 1 459 ? 32.359 -55.294 12.659 1.00 81.86 ? 459 LEU A CD1 1 ATOM 3432 C CD2 . LEU A 1 459 ? 34.423 -54.122 11.837 1.00 93.14 ? 459 LEU A CD2 1 ATOM 3433 N N . GLU A 1 460 ? 30.612 -57.254 9.157 1.00 101.56 ? 460 GLU A N 1 ATOM 3434 C CA . GLU A 1 460 ? 29.834 -57.046 7.926 1.00 101.04 ? 460 GLU A CA 1 ATOM 3435 C C . GLU A 1 460 ? 29.771 -55.579 7.490 1.00 96.32 ? 460 GLU A C 1 ATOM 3436 O O . GLU A 1 460 ? 29.586 -55.284 6.313 1.00 99.64 ? 460 GLU A O 1 ATOM 3437 C CB . GLU A 1 460 ? 28.398 -57.559 8.085 1.00 98.53 ? 460 GLU A CB 1 ATOM 3438 C CG . GLU A 1 460 ? 28.259 -59.044 8.360 1.00 108.09 ? 460 GLU A CG 1 ATOM 3439 C CD . GLU A 1 460 ? 26.804 -59.472 8.421 1.00 114.16 ? 460 GLU A CD 1 ATOM 3440 O OE1 . GLU A 1 460 ? 25.928 -58.597 8.246 1.00 107.14 ? 460 GLU A OE1 1 ATOM 3441 O OE2 . GLU A 1 460 ? 26.538 -60.676 8.640 1.00 120.74 ? 460 GLU A OE2 1 ATOM 3442 N N . VAL A 1 461 ? 29.882 -54.661 8.443 1.00 91.31 ? 461 VAL A N 1 ATOM 3443 C CA . VAL A 1 461 ? 29.877 -53.237 8.123 1.00 87.68 ? 461 VAL A CA 1 ATOM 3444 C C . VAL A 1 461 ? 30.983 -52.512 8.862 1.00 91.02 ? 461 VAL A C 1 ATOM 3445 O O . VAL A 1 461 ? 31.133 -52.656 10.070 1.00 98.29 ? 461 VAL A O 1 ATOM 3446 C CB . VAL A 1 461 ? 28.548 -52.559 8.480 1.00 75.73 ? 461 VAL A CB 1 ATOM 3447 C CG1 . VAL A 1 461 ? 28.619 -51.073 8.130 1.00 69.53 ? 461 VAL A CG1 1 ATOM 3448 C CG2 . VAL A 1 461 ? 27.389 -53.241 7.763 1.00 61.40 ? 461 VAL A CG2 1 ATOM 3449 N N . LEU A 1 462 ? 31.762 -51.731 8.131 1.00 85.03 ? 462 LEU A N 1 ATOM 3450 C CA . LEU A 1 462 ? 32.822 -50.952 8.739 1.00 80.84 ? 462 LEU A CA 1 ATOM 3451 C C . LEU A 1 462 ? 32.702 -49.529 8.228 1.00 88.21 ? 462 LEU A C 1 ATOM 3452 O O . LEU A 1 462 ? 32.472 -49.300 7.044 1.00 88.80 ? 462 LEU A O 1 ATOM 3453 C CB . LEU A 1 462 ? 34.190 -51.544 8.404 1.00 83.75 ? 462 LEU A CB 1 ATOM 3454 C CG . LEU A 1 462 ? 35.421 -50.945 9.095 1.00 92.51 ? 462 LEU A CG 1 ATOM 3455 C CD1 . LEU A 1 462 ? 35.279 -50.949 10.606 1.00 94.22 ? 462 LEU A CD1 1 ATOM 3456 C CD2 . LEU A 1 462 ? 36.684 -51.687 8.690 1.00 98.96 ? 462 LEU A CD2 1 ATOM 3457 N N . ASP A 1 463 ? 32.800 -48.570 9.136 1.00 90.90 ? 463 ASP A N 1 ATOM 3458 C CA . ASP A 1 463 ? 32.808 -47.176 8.742 1.00 80.88 ? 463 ASP A CA 1 ATOM 3459 C C . ASP A 1 463 ? 34.061 -46.616 9.337 1.00 79.38 ? 463 ASP A C 1 ATOM 3460 O O . ASP A 1 463 ? 34.182 -46.537 10.550 1.00 85.10 ? 463 ASP A O 1 ATOM 3461 C CB . ASP A 1 463 ? 31.580 -46.424 9.264 1.00 66.00 ? 463 ASP A CB 1 ATOM 3462 C CG . ASP A 1 463 ? 31.514 -44.994 8.746 1.00 73.44 ? 463 ASP A CG 1 ATOM 3463 O OD1 . ASP A 1 463 ? 32.576 -44.462 8.354 1.00 67.41 ? 463 ASP A OD1 1 ATOM 3464 O OD2 . ASP A 1 463 ? 30.408 -44.399 8.728 1.00 81.58 ? 463 ASP A OD2 1 ATOM 3465 N N . VAL A 1 464 ? 35.012 -46.271 8.483 1.00 73.73 ? 464 VAL A N 1 ATOM 3466 C CA . VAL A 1 464 ? 36.269 -45.720 8.949 1.00 77.82 ? 464 VAL A CA 1 ATOM 3467 C C . VAL A 1 464 ? 36.531 -44.436 8.182 1.00 84.79 ? 464 VAL A C 1 ATOM 3468 O O . VAL A 1 464 ? 37.672 -44.109 7.861 1.00 90.43 ? 464 VAL A O 1 ATOM 3469 C CB . VAL A 1 464 ? 37.430 -46.717 8.765 1.00 76.83 ? 464 VAL A CB 1 ATOM 3470 C CG1 . VAL A 1 464 ? 38.355 -46.677 9.963 1.00 72.95 ? 464 VAL A CG1 1 ATOM 3471 C CG2 . VAL A 1 464 ? 36.895 -48.119 8.610 1.00 78.24 ? 464 VAL A CG2 1 ATOM 3472 N N . SER A 1 465 ? 35.454 -43.708 7.897 1.00 87.93 ? 465 SER A N 1 ATOM 3473 C CA . SER A 1 465 ? 35.533 -42.479 7.107 1.00 92.53 ? 465 SER A CA 1 ATOM 3474 C C . SER A 1 465 ? 36.002 -41.272 7.917 1.00 99.79 ? 465 SER A C 1 ATOM 3475 O O . SER A 1 465 ? 36.185 -41.356 9.130 1.00 109.28 ? 465 SER A O 1 ATOM 3476 C CB . SER A 1 465 ? 34.189 -42.179 6.428 1.00 81.24 ? 465 SER A CB 1 ATOM 3477 O OG . SER A 1 465 ? 33.200 -41.810 7.366 1.00 78.02 ? 465 SER A OG 1 ATOM 3478 N N . ASN A 1 466 ? 36.201 -40.154 7.228 1.00 95.13 ? 466 ASN A N 1 ATOM 3479 C CA . ASN A 1 466 ? 36.636 -38.915 7.858 1.00 99.77 ? 466 ASN A CA 1 ATOM 3480 C C . ASN A 1 466 ? 37.813 -39.110 8.810 1.00 105.54 ? 466 ASN A C 1 ATOM 3481 O O . ASN A 1 466 ? 37.778 -38.654 9.954 1.00 109.95 ? 466 ASN A O 1 ATOM 3482 C CB . ASN A 1 466 ? 35.468 -38.248 8.589 1.00 102.90 ? 466 ASN A CB 1 ATOM 3483 C CG . ASN A 1 466 ? 35.773 -36.814 8.999 1.00 108.41 ? 466 ASN A CG 1 ATOM 3484 O OD1 . ASN A 1 466 ? 36.771 -36.229 8.572 1.00 110.47 ? 466 ASN A OD1 1 ATOM 3485 N ND2 . ASN A 1 466 ? 34.907 -36.241 9.830 1.00 106.41 ? 466 ASN A ND2 1 ATOM 3486 N N . ASN A 1 467 ? 38.855 -39.787 8.338 1.00 103.98 ? 467 ASN A N 1 ATOM 3487 C CA . ASN A 1 467 ? 40.044 -40.007 9.156 1.00 106.01 ? 467 ASN A CA 1 ATOM 3488 C C . ASN A 1 467 ? 41.324 -39.558 8.458 1.00 104.09 ? 467 ASN A C 1 ATOM 3489 O O . ASN A 1 467 ? 41.316 -38.600 7.684 1.00 104.31 ? 467 ASN A O 1 ATOM 3490 C CB . ASN A 1 467 ? 40.152 -41.478 9.572 1.00 107.45 ? 467 ASN A CB 1 ATOM 3491 C CG . ASN A 1 467 ? 39.069 -41.890 10.551 1.00 107.96 ? 467 ASN A CG 1 ATOM 3492 O OD1 . ASN A 1 467 ? 38.628 -43.036 10.562 1.00 108.84 ? 467 ASN A OD1 1 ATOM 3493 N ND2 . ASN A 1 467 ? 38.634 -40.951 11.379 1.00 109.02 ? 467 ASN A ND2 1 ATOM 3494 N N . ASN A 1 468 ? 42.420 -40.255 8.744 1.00 100.91 ? 468 ASN A N 1 ATOM 3495 C CA . ASN A 1 468 ? 43.697 -39.999 8.085 1.00 101.72 ? 468 ASN A CA 1 ATOM 3496 C C . ASN A 1 468 ? 44.324 -41.270 7.493 1.00 103.28 ? 468 ASN A C 1 ATOM 3497 O O . ASN A 1 468 ? 45.549 -41.392 7.376 1.00 93.51 ? 468 ASN A O 1 ATOM 3498 C CB . ASN A 1 468 ? 44.657 -39.293 9.038 1.00 97.33 ? 468 ASN A CB 1 ATOM 3499 C CG . ASN A 1 468 ? 44.271 -37.849 9.277 1.00 99.50 ? 468 ASN A CG 1 ATOM 3500 O OD1 . ASN A 1 468 ? 43.136 -37.554 9.644 1.00 93.55 ? 468 ASN A OD1 1 ATOM 3501 N ND2 . ASN A 1 468 ? 45.215 -36.938 9.059 1.00 105.35 ? 468 ASN A ND2 1 ATOM 3502 N N . LEU A 1 469 ? 43.459 -42.207 7.118 1.00 105.51 ? 469 LEU A N 1 ATOM 3503 C CA . LEU A 1 469 ? 43.865 -43.451 6.477 1.00 108.46 ? 469 LEU A CA 1 ATOM 3504 C C . LEU A 1 469 ? 44.580 -43.222 5.145 1.00 118.57 ? 469 LEU A C 1 ATOM 3505 O O . LEU A 1 469 ? 44.057 -42.544 4.253 1.00 114.42 ? 469 LEU A O 1 ATOM 3506 C CB . LEU A 1 469 ? 42.636 -44.323 6.237 1.00 100.48 ? 469 LEU A CB 1 ATOM 3507 C CG . LEU A 1 469 ? 42.309 -45.421 7.242 1.00 91.95 ? 469 LEU A CG 1 ATOM 3508 C CD1 . LEU A 1 469 ? 42.669 -45.016 8.667 1.00 87.34 ? 469 LEU A CD1 1 ATOM 3509 C CD2 . LEU A 1 469 ? 40.841 -45.784 7.106 1.00 89.30 ? 469 LEU A CD2 1 ATOM 3510 N N . ASP A 1 470 ? 45.772 -43.798 5.012 1.00 124.91 ? 470 ASP A N 1 ATOM 3511 C CA . ASP A 1 470 ? 46.514 -43.732 3.759 1.00 131.18 ? 470 ASP A CA 1 ATOM 3512 C C . ASP A 1 470 ? 46.277 -44.991 2.939 1.00 130.84 ? 470 ASP A C 1 ATOM 3513 O O . ASP A 1 470 ? 46.340 -44.974 1.708 1.00 124.66 ? 470 ASP A O 1 ATOM 3514 C CB . ASP A 1 470 ? 48.013 -43.529 4.011 1.00 133.95 ? 470 ASP A CB 1 ATOM 3515 C CG . ASP A 1 470 ? 48.471 -42.108 3.701 1.00 135.42 ? 470 ASP A CG 1 ATOM 3516 O OD1 . ASP A 1 470 ? 49.115 -41.913 2.648 1.00 134.02 ? 470 ASP A OD1 1 ATOM 3517 O OD2 . ASP A 1 470 ? 48.179 -41.187 4.497 1.00 134.37 ? 470 ASP A OD2 1 ATOM 3518 N N . SER A 1 471 ? 45.984 -46.082 3.633 1.00 132.92 ? 471 SER A N 1 ATOM 3519 C CA . SER A 1 471 ? 45.822 -47.368 2.976 1.00 129.93 ? 471 SER A CA 1 ATOM 3520 C C . SER A 1 471 ? 44.914 -48.277 3.784 1.00 121.94 ? 471 SER A C 1 ATOM 3521 O O . SER A 1 471 ? 45.143 -48.492 4.974 1.00 123.55 ? 471 SER A O 1 ATOM 3522 C CB . SER A 1 471 ? 47.189 -48.033 2.800 1.00 126.93 ? 471 SER A CB 1 ATOM 3523 O OG . SER A 1 471 ? 47.947 -47.950 3.998 1.00 122.86 ? 471 SER A OG 1 ATOM 3524 N N . PHE A 1 472 ? 43.879 -48.802 3.142 1.00 109.88 ? 472 PHE A N 1 ATOM 3525 C CA . PHE A 1 472 ? 43.098 -49.862 3.755 1.00 107.32 ? 472 PHE A CA 1 ATOM 3526 C C . PHE A 1 472 ? 43.501 -51.206 3.143 1.00 111.56 ? 472 PHE A C 1 ATOM 3527 O O . PHE A 1 472 ? 43.217 -51.489 1.980 1.00 118.67 ? 472 PHE A O 1 ATOM 3528 C CB . PHE A 1 472 ? 41.603 -49.607 3.593 1.00 109.37 ? 472 PHE A CB 1 ATOM 3529 C CG . PHE A 1 472 ? 40.743 -50.561 4.367 1.00 115.26 ? 472 PHE A CG 1 ATOM 3530 C CD1 . PHE A 1 472 ? 40.258 -50.214 5.620 1.00 115.31 ? 472 PHE A CD1 1 ATOM 3531 C CD2 . PHE A 1 472 ? 40.428 -51.812 3.845 1.00 118.96 ? 472 PHE A CD2 1 ATOM 3532 C CE1 . PHE A 1 472 ? 39.469 -51.091 6.342 1.00 118.35 ? 472 PHE A CE1 1 ATOM 3533 C CE2 . PHE A 1 472 ? 39.639 -52.696 4.555 1.00 124.53 ? 472 PHE A CE2 1 ATOM 3534 C CZ . PHE A 1 472 ? 39.157 -52.335 5.811 1.00 126.84 ? 472 PHE A CZ 1 ATOM 3535 N N . SER A 1 473 ? 44.179 -52.027 3.934 1.00 108.96 ? 473 SER A N 1 ATOM 3536 C CA . SER A 1 473 ? 44.746 -53.275 3.444 1.00 117.23 ? 473 SER A CA 1 ATOM 3537 C C . SER A 1 473 ? 44.379 -54.424 4.374 1.00 119.35 ? 473 SER A C 1 ATOM 3538 O O . SER A 1 473 ? 45.241 -54.989 5.052 1.00 117.30 ? 473 SER A O 1 ATOM 3539 C CB . SER A 1 473 ? 46.266 -53.144 3.346 1.00 116.83 ? 473 SER A CB 1 ATOM 3540 O OG . SER A 1 473 ? 46.796 -52.466 4.473 1.00 105.67 ? 473 SER A OG 1 ATOM 3541 N N . LEU A 1 474 ? 43.101 -54.785 4.381 1.00 119.08 ? 474 LEU A N 1 ATOM 3542 C CA . LEU A 1 474 ? 42.564 -55.600 5.458 1.00 112.00 ? 474 LEU A CA 1 ATOM 3543 C C . LEU A 1 474 ? 41.584 -56.676 5.018 1.00 116.53 ? 474 LEU A C 1 ATOM 3544 O O . LEU A 1 474 ? 40.512 -56.373 4.502 1.00 118.79 ? 474 LEU A O 1 ATOM 3545 C CB . LEU A 1 474 ? 41.855 -54.683 6.442 1.00 94.33 ? 474 LEU A CB 1 ATOM 3546 C CG . LEU A 1 474 ? 41.916 -55.107 7.894 1.00 71.15 ? 474 LEU A CG 1 ATOM 3547 C CD1 . LEU A 1 474 ? 43.369 -55.327 8.259 1.00 63.67 ? 474 LEU A CD1 1 ATOM 3548 C CD2 . LEU A 1 474 ? 41.289 -54.010 8.711 1.00 65.53 ? 474 LEU A CD2 1 ATOM 3549 N N . PHE A 1 475 ? 41.938 -57.932 5.262 1.00 117.06 ? 475 PHE A N 1 ATOM 3550 C CA . PHE A 1 475 ? 41.051 -59.045 4.953 1.00 117.83 ? 475 PHE A CA 1 ATOM 3551 C C . PHE A 1 475 ? 39.847 -59.055 5.888 1.00 117.25 ? 475 PHE A C 1 ATOM 3552 O O . PHE A 1 475 ? 39.992 -59.234 7.098 1.00 116.56 ? 475 PHE A O 1 ATOM 3553 C CB . PHE A 1 475 ? 41.809 -60.368 5.061 1.00 119.17 ? 475 PHE A CB 1 ATOM 3554 C CG . PHE A 1 475 ? 41.069 -61.545 4.483 1.00 123.38 ? 475 PHE A CG 1 ATOM 3555 C CD1 . PHE A 1 475 ? 41.269 -62.824 4.989 1.00 127.58 ? 475 PHE A CD1 1 ATOM 3556 C CD2 . PHE A 1 475 ? 40.172 -61.375 3.438 1.00 116.61 ? 475 PHE A CD2 1 ATOM 3557 C CE1 . PHE A 1 475 ? 40.591 -63.914 4.460 1.00 125.59 ? 475 PHE A CE1 1 ATOM 3558 C CE2 . PHE A 1 475 ? 39.491 -62.458 2.907 1.00 116.41 ? 475 PHE A CE2 1 ATOM 3559 C CZ . PHE A 1 475 ? 39.700 -63.728 3.418 1.00 120.15 ? 475 PHE A CZ 1 ATOM 3560 N N . LEU A 1 476 ? 38.663 -58.847 5.320 1.00 111.21 ? 476 LEU A N 1 ATOM 3561 C CA . LEU A 1 476 ? 37.413 -58.907 6.071 1.00 110.21 ? 476 LEU A CA 1 ATOM 3562 C C . LEU A 1 476 ? 36.369 -59.596 5.209 1.00 117.46 ? 476 LEU A C 1 ATOM 3563 O O . LEU A 1 476 ? 35.547 -58.927 4.579 1.00 123.48 ? 476 LEU A O 1 ATOM 3564 C CB . LEU A 1 476 ? 36.926 -57.501 6.454 1.00 102.14 ? 476 LEU A CB 1 ATOM 3565 C CG . LEU A 1 476 ? 37.854 -56.632 7.313 1.00 91.54 ? 476 LEU A CG 1 ATOM 3566 C CD1 . LEU A 1 476 ? 37.441 -55.168 7.277 1.00 86.96 ? 476 LEU A CD1 1 ATOM 3567 C CD2 . LEU A 1 476 ? 37.896 -57.147 8.734 1.00 75.11 ? 476 LEU A CD2 1 ATOM 3568 N N . PRO A 1 477 ? 36.401 -60.941 5.175 1.00 111.72 ? 477 PRO A N 1 ATOM 3569 C CA . PRO A 1 477 ? 35.529 -61.745 4.304 1.00 101.52 ? 477 PRO A CA 1 ATOM 3570 C C . PRO A 1 477 ? 34.078 -61.269 4.268 1.00 107.94 ? 477 PRO A C 1 ATOM 3571 O O . PRO A 1 477 ? 33.632 -60.747 3.246 1.00 116.64 ? 477 PRO A O 1 ATOM 3572 C CB . PRO A 1 477 ? 35.614 -63.143 4.919 1.00 92.21 ? 477 PRO A CB 1 ATOM 3573 C CG . PRO A 1 477 ? 36.982 -63.196 5.524 1.00 97.72 ? 477 PRO A CG 1 ATOM 3574 C CD . PRO A 1 477 ? 37.289 -61.785 6.000 1.00 104.09 ? 477 PRO A CD 1 ATOM 3575 N N . ARG A 1 478 ? 33.359 -61.442 5.371 1.00 108.54 ? 478 ARG A N 1 ATOM 3576 C CA . ARG A 1 478 ? 31.928 -61.153 5.416 1.00 115.03 ? 478 ARG A CA 1 ATOM 3577 C C . ARG A 1 478 ? 31.562 -59.723 4.996 1.00 110.17 ? 478 ARG A C 1 ATOM 3578 O O . ARG A 1 478 ? 30.410 -59.449 4.644 1.00 106.84 ? 478 ARG A O 1 ATOM 3579 C CB . ARG A 1 478 ? 31.378 -61.463 6.815 1.00 119.17 ? 478 ARG A CB 1 ATOM 3580 C CG . ARG A 1 478 ? 31.979 -62.724 7.437 1.00 119.74 ? 478 ARG A CG 1 ATOM 3581 C CD . ARG A 1 478 ? 31.127 -63.284 8.571 1.00 121.76 ? 478 ARG A CD 1 ATOM 3582 N NE . ARG A 1 478 ? 31.783 -64.396 9.264 1.00 129.81 ? 478 ARG A NE 1 ATOM 3583 C CZ . ARG A 1 478 ? 31.500 -65.685 9.075 1.00 139.65 ? 478 ARG A CZ 1 ATOM 3584 N NH1 . ARG A 1 478 ? 30.559 -66.052 8.211 1.00 140.37 ? 478 ARG A NH1 1 ATOM 3585 N NH2 . ARG A 1 478 ? 32.160 -66.614 9.757 1.00 142.08 ? 478 ARG A NH2 1 ATOM 3586 N N . LEU A 1 479 ? 32.554 -58.832 5.005 1.00 105.77 ? 479 LEU A N 1 ATOM 3587 C CA . LEU A 1 479 ? 32.337 -57.390 4.813 1.00 104.78 ? 479 LEU A CA 1 ATOM 3588 C C . LEU A 1 479 ? 31.468 -56.989 3.618 1.00 106.66 ? 479 LEU A C 1 ATOM 3589 O O . LEU A 1 479 ? 31.907 -57.039 2.471 1.00 109.69 ? 479 LEU A O 1 ATOM 3590 C CB . LEU A 1 479 ? 33.674 -56.646 4.739 1.00 104.23 ? 479 LEU A CB 1 ATOM 3591 C CG . LEU A 1 479 ? 33.574 -55.119 4.731 1.00 105.56 ? 479 LEU A CG 1 ATOM 3592 C CD1 . LEU A 1 479 ? 33.017 -54.619 6.050 1.00 109.95 ? 479 LEU A CD1 1 ATOM 3593 C CD2 . LEU A 1 479 ? 34.926 -54.498 4.470 1.00 110.88 ? 479 LEU A CD2 1 ATOM 3594 N N . GLN A 1 480 ? 30.244 -56.559 3.905 1.00 105.41 ? 480 GLN A N 1 ATOM 3595 C CA . GLN A 1 480 ? 29.332 -56.059 2.883 1.00 105.52 ? 480 GLN A CA 1 ATOM 3596 C C . GLN A 1 480 ? 29.582 -54.580 2.588 1.00 105.16 ? 480 GLN A C 1 ATOM 3597 O O . GLN A 1 480 ? 30.021 -54.220 1.499 1.00 97.62 ? 480 GLN A O 1 ATOM 3598 C CB . GLN A 1 480 ? 27.884 -56.284 3.318 1.00 97.89 ? 480 GLN A CB 1 ATOM 3599 C CG . GLN A 1 480 ? 27.545 -57.751 3.536 1.00 94.70 ? 480 GLN A CG 1 ATOM 3600 C CD . GLN A 1 480 ? 26.188 -57.955 4.179 1.00 91.39 ? 480 GLN A CD 1 ATOM 3601 O OE1 . GLN A 1 480 ? 25.369 -57.039 4.237 1.00 92.58 ? 480 GLN A OE1 1 ATOM 3602 N NE2 . GLN A 1 480 ? 25.947 -59.162 4.673 1.00 83.92 ? 480 GLN A NE2 1 ATOM 3603 N N . GLU A 1 481 ? 29.314 -53.726 3.569 1.00 110.72 ? 481 GLU A N 1 ATOM 3604 C CA . GLU A 1 481 ? 29.511 -52.290 3.395 1.00 113.74 ? 481 GLU A CA 1 ATOM 3605 C C . GLU A 1 481 ? 30.873 -51.837 3.905 1.00 100.12 ? 481 GLU A C 1 ATOM 3606 O O . GLU A 1 481 ? 31.419 -52.422 4.836 1.00 90.39 ? 481 GLU A O 1 ATOM 3607 C CB . GLU A 1 481 ? 28.393 -51.509 4.091 1.00 124.83 ? 481 GLU A CB 1 ATOM 3608 C CG . GLU A 1 481 ? 26.999 -52.005 3.728 1.00 135.40 ? 481 GLU A CG 1 ATOM 3609 C CD . GLU A 1 481 ? 25.911 -51.008 4.062 1.00 139.79 ? 481 GLU A CD 1 ATOM 3610 O OE1 . GLU A 1 481 ? 26.241 -49.888 4.516 1.00 141.87 ? 481 GLU A OE1 1 ATOM 3611 O OE2 . GLU A 1 481 ? 24.725 -51.350 3.863 1.00 138.24 ? 481 GLU A OE2 1 ATOM 3612 N N . LEU A 1 482 ? 31.426 -50.803 3.278 1.00 98.15 ? 482 LEU A N 1 ATOM 3613 C CA . LEU A 1 482 ? 32.680 -50.222 3.742 1.00 98.52 ? 482 LEU A CA 1 ATOM 3614 C C . LEU A 1 482 ? 32.728 -48.722 3.520 1.00 109.74 ? 482 LEU A C 1 ATOM 3615 O O . LEU A 1 482 ? 33.364 -48.252 2.580 1.00 109.68 ? 482 LEU A O 1 ATOM 3616 C CB . LEU A 1 482 ? 33.884 -50.856 3.055 1.00 95.57 ? 482 LEU A CB 1 ATOM 3617 C CG . LEU A 1 482 ? 35.186 -50.242 3.575 1.00 91.59 ? 482 LEU A CG 1 ATOM 3618 C CD1 . LEU A 1 482 ? 35.659 -50.996 4.810 1.00 93.55 ? 482 LEU A CD1 1 ATOM 3619 C CD2 . LEU A 1 482 ? 36.262 -50.220 2.514 1.00 85.75 ? 482 LEU A CD2 1 ATOM 3620 N N . TYR A 1 483 ? 32.055 -47.976 4.391 1.00 122.81 ? 483 TYR A N 1 ATOM 3621 C CA . TYR A 1 483 ? 32.109 -46.521 4.345 1.00 128.49 ? 483 TYR A CA 1 ATOM 3622 C C . TYR A 1 483 ? 33.510 -46.065 4.747 1.00 123.78 ? 483 TYR A C 1 ATOM 3623 O O . TYR A 1 483 ? 33.941 -46.284 5.876 1.00 133.37 ? 483 TYR A O 1 ATOM 3624 C CB . TYR A 1 483 ? 31.018 -45.907 5.239 1.00 138.17 ? 483 TYR A CB 1 ATOM 3625 C CG . TYR A 1 483 ? 29.624 -45.976 4.628 1.00 157.24 ? 483 TYR A CG 1 ATOM 3626 C CD1 . TYR A 1 483 ? 28.879 -47.155 4.653 1.00 162.88 ? 483 TYR A CD1 1 ATOM 3627 C CD2 . TYR A 1 483 ? 29.059 -44.863 4.012 1.00 164.23 ? 483 TYR A CD2 1 ATOM 3628 C CE1 . TYR A 1 483 ? 27.605 -47.216 4.080 1.00 162.86 ? 483 TYR A CE1 1 ATOM 3629 C CE2 . TYR A 1 483 ? 27.791 -44.917 3.434 1.00 162.05 ? 483 TYR A CE2 1 ATOM 3630 C CZ . TYR A 1 483 ? 27.070 -46.090 3.472 1.00 156.99 ? 483 TYR A CZ 1 ATOM 3631 O OH . TYR A 1 483 ? 25.815 -46.126 2.901 1.00 143.53 ? 483 TYR A OH 1 ATOM 3632 N N . ILE A 1 484 ? 34.232 -45.463 3.808 1.00 113.84 ? 484 ILE A N 1 ATOM 3633 C CA . ILE A 1 484 ? 35.604 -45.025 4.059 1.00 111.85 ? 484 ILE A CA 1 ATOM 3634 C C . ILE A 1 484 ? 35.940 -43.724 3.311 1.00 110.99 ? 484 ILE A C 1 ATOM 3635 O O . ILE A 1 484 ? 37.061 -43.536 2.834 1.00 113.32 ? 484 ILE A O 1 ATOM 3636 C CB . ILE A 1 484 ? 36.635 -46.150 3.734 1.00 108.79 ? 484 ILE A CB 1 ATOM 3637 C CG1 . ILE A 1 484 ? 38.058 -45.724 4.114 1.00 106.89 ? 484 ILE A CG1 1 ATOM 3638 C CG2 . ILE A 1 484 ? 36.560 -46.565 2.271 1.00 109.42 ? 484 ILE A CG2 1 ATOM 3639 C CD1 . ILE A 1 484 ? 39.141 -46.481 3.368 1.00 102.07 ? 484 ILE A CD1 1 ATOM 3640 N N . SER A 1 485 ? 34.963 -42.821 3.234 1.00 103.38 ? 485 SER A N 1 ATOM 3641 C CA . SER A 1 485 ? 35.140 -41.534 2.561 1.00 98.87 ? 485 SER A CA 1 ATOM 3642 C C . SER A 1 485 ? 36.078 -40.570 3.287 1.00 91.75 ? 485 SER A C 1 ATOM 3643 O O . SER A 1 485 ? 36.817 -40.957 4.183 1.00 87.45 ? 485 SER A O 1 ATOM 3644 C CB . SER A 1 485 ? 33.787 -40.857 2.353 1.00 104.95 ? 485 SER A CB 1 ATOM 3645 O OG . SER A 1 485 ? 33.041 -41.531 1.362 1.00 106.49 ? 485 SER A OG 1 ATOM 3646 N N . ARG A 1 486 ? 36.035 -39.309 2.874 1.00 96.59 ? 486 ARG A N 1 ATOM 3647 C CA . ARG A 1 486 ? 36.878 -38.254 3.434 1.00 101.63 ? 486 ARG A CA 1 ATOM 3648 C C . ARG A 1 486 ? 38.193 -38.754 4.054 1.00 106.81 ? 486 ARG A C 1 ATOM 3649 O O . ARG A 1 486 ? 38.448 -38.560 5.244 1.00 106.18 ? 486 ARG A O 1 ATOM 3650 C CB . ARG A 1 486 ? 36.081 -37.413 4.437 1.00 100.13 ? 486 ARG A CB 1 ATOM 3651 C CG . ARG A 1 486 ? 34.773 -36.856 3.884 1.00 102.85 ? 486 ARG A CG 1 ATOM 3652 C CD . ARG A 1 486 ? 33.925 -36.244 4.990 1.00 113.12 ? 486 ARG A CD 1 ATOM 3653 N NE . ARG A 1 486 ? 34.672 -35.249 5.759 1.00 131.11 ? 486 ARG A NE 1 ATOM 3654 C CZ . ARG A 1 486 ? 34.278 -34.750 6.929 1.00 143.16 ? 486 ARG A CZ 1 ATOM 3655 N NH1 . ARG A 1 486 ? 33.140 -35.155 7.479 1.00 145.53 ? 486 ARG A NH1 1 ATOM 3656 N NH2 . ARG A 1 486 ? 35.025 -33.847 7.556 1.00 147.57 ? 486 ARG A NH2 1 ATOM 3657 N N . ASN A 1 487 ? 39.027 -39.388 3.235 1.00 115.09 ? 487 ASN A N 1 ATOM 3658 C CA . ASN A 1 487 ? 40.349 -39.841 3.668 1.00 123.19 ? 487 ASN A CA 1 ATOM 3659 C C . ASN A 1 487 ? 41.471 -39.319 2.758 1.00 126.85 ? 487 ASN A C 1 ATOM 3660 O O . ASN A 1 487 ? 41.227 -38.527 1.843 1.00 122.73 ? 487 ASN A O 1 ATOM 3661 C CB . ASN A 1 487 ? 40.397 -41.374 3.743 1.00 124.60 ? 487 ASN A CB 1 ATOM 3662 C CG . ASN A 1 487 ? 39.762 -41.925 5.015 1.00 117.12 ? 487 ASN A CG 1 ATOM 3663 O OD1 . ASN A 1 487 ? 38.782 -42.670 4.961 1.00 115.41 ? 487 ASN A OD1 1 ATOM 3664 N ND2 . ASN A 1 487 ? 40.327 -41.569 6.164 1.00 106.68 ? 487 ASN A ND2 1 ATOM 3665 N N . LYS A 1 488 ? 42.698 -39.765 3.019 1.00 129.27 ? 488 LYS A N 1 ATOM 3666 C CA . LYS A 1 488 ? 43.849 -39.398 2.199 1.00 131.70 ? 488 LYS A CA 1 ATOM 3667 C C . LYS A 1 488 ? 44.295 -40.570 1.330 1.00 139.58 ? 488 LYS A C 1 ATOM 3668 O O . LYS A 1 488 ? 45.483 -40.722 1.048 1.00 145.03 ? 488 LYS A O 1 ATOM 3669 C CB . LYS A 1 488 ? 45.018 -38.955 3.079 1.00 131.17 ? 488 LYS A CB 1 ATOM 3670 C CG . LYS A 1 488 ? 45.044 -37.476 3.428 1.00 134.69 ? 488 LYS A CG 1 ATOM 3671 C CD . LYS A 1 488 ? 46.269 -37.166 4.284 1.00 137.72 ? 488 LYS A CD 1 ATOM 3672 C CE . LYS A 1 488 ? 46.526 -35.672 4.420 1.00 131.64 ? 488 LYS A CE 1 ATOM 3673 N NZ . LYS A 1 488 ? 47.815 -35.408 5.128 1.00 122.88 ? 488 LYS A NZ 1 ATOM 3674 N N . LEU A 1 489 ? 43.339 -41.390 0.901 1.00 140.27 ? 489 LEU A N 1 ATOM 3675 C CA . LEU A 1 489 ? 43.635 -42.621 0.167 1.00 142.55 ? 489 LEU A CA 1 ATOM 3676 C C . LEU A 1 489 ? 44.033 -42.368 -1.300 1.00 151.24 ? 489 LEU A C 1 ATOM 3677 O O . LEU A 1 489 ? 43.171 -42.125 -2.148 1.00 155.11 ? 489 LEU A O 1 ATOM 3678 C CB . LEU A 1 489 ? 42.428 -43.571 0.238 1.00 134.01 ? 489 LEU A CB 1 ATOM 3679 C CG . LEU A 1 489 ? 42.651 -45.075 0.440 1.00 128.02 ? 489 LEU A CG 1 ATOM 3680 C CD1 . LEU A 1 489 ? 43.027 -45.388 1.879 1.00 119.01 ? 489 LEU A CD1 1 ATOM 3681 C CD2 . LEU A 1 489 ? 41.411 -45.856 0.050 1.00 127.37 ? 489 LEU A CD2 1 ATOM 3682 N N . LYS A 1 490 ? 45.336 -42.424 -1.590 1.00 150.35 ? 490 LYS A N 1 ATOM 3683 C CA . LYS A 1 490 ? 45.847 -42.308 -2.963 1.00 138.76 ? 490 LYS A CA 1 ATOM 3684 C C . LYS A 1 490 ? 45.348 -43.470 -3.812 1.00 140.33 ? 490 LYS A C 1 ATOM 3685 O O . LYS A 1 490 ? 44.821 -43.285 -4.910 1.00 130.41 ? 490 LYS A O 1 ATOM 3686 C CB . LYS A 1 490 ? 47.378 -42.345 -2.974 1.00 117.75 ? 490 LYS A CB 1 ATOM 3687 C CG . LYS A 1 490 ? 48.088 -41.012 -2.810 1.00 102.01 ? 490 LYS A CG 1 ATOM 3688 C CD . LYS A 1 490 ? 49.585 -41.267 -2.707 1.00 98.84 ? 490 LYS A CD 1 ATOM 3689 C CE . LYS A 1 490 ? 50.381 -40.023 -2.340 1.00 101.12 ? 490 LYS A CE 1 ATOM 3690 N NZ . LYS A 1 490 ? 51.808 -40.360 -1.983 1.00 97.91 ? 490 LYS A NZ 1 ATOM 3691 N N . THR A 1 491 ? 45.535 -44.671 -3.276 1.00 144.73 ? 491 THR A N 1 ATOM 3692 C CA . THR A 1 491 ? 45.233 -45.911 -3.973 1.00 139.24 ? 491 THR A CA 1 ATOM 3693 C C . THR A 1 491 ? 43.938 -46.547 -3.471 1.00 131.81 ? 491 THR A C 1 ATOM 3694 O O . THR A 1 491 ? 43.600 -46.429 -2.292 1.00 134.70 ? 491 THR A O 1 ATOM 3695 C CB . THR A 1 491 ? 46.368 -46.914 -3.750 1.00 139.77 ? 491 THR A CB 1 ATOM 3696 O OG1 . THR A 1 491 ? 45.887 -48.238 -4.010 1.00 141.29 ? 491 THR A OG1 1 ATOM 3697 C CG2 . THR A 1 491 ? 46.879 -46.829 -2.299 1.00 133.30 ? 491 THR A CG2 1 ATOM 3698 N N . LEU A 1 492 ? 43.224 -47.234 -4.360 1.00 117.11 ? 492 LEU A N 1 ATOM 3699 C CA . LEU A 1 492 ? 42.010 -47.954 -3.971 1.00 113.51 ? 492 LEU A CA 1 ATOM 3700 C C . LEU A 1 492 ? 42.323 -49.364 -3.444 1.00 124.35 ? 492 LEU A C 1 ATOM 3701 O O . LEU A 1 492 ? 43.293 -49.989 -3.876 1.00 126.47 ? 492 LEU A O 1 ATOM 3702 C CB . LEU A 1 492 ? 41.012 -48.008 -5.135 1.00 106.24 ? 492 LEU A CB 1 ATOM 3703 C CG . LEU A 1 492 ? 39.630 -48.628 -4.882 1.00 101.11 ? 492 LEU A CG 1 ATOM 3704 C CD1 . LEU A 1 492 ? 38.532 -47.870 -5.597 1.00 92.83 ? 492 LEU A CD1 1 ATOM 3705 C CD2 . LEU A 1 492 ? 39.591 -50.097 -5.262 1.00 105.50 ? 492 LEU A CD2 1 ATOM 3706 N N . PRO A 1 493 ? 41.515 -49.853 -2.482 1.00 129.31 ? 493 PRO A N 1 ATOM 3707 C CA . PRO A 1 493 ? 41.661 -51.183 -1.867 1.00 132.48 ? 493 PRO A CA 1 ATOM 3708 C C . PRO A 1 493 ? 41.441 -52.380 -2.805 1.00 133.48 ? 493 PRO A C 1 ATOM 3709 O O . PRO A 1 493 ? 40.592 -52.345 -3.700 1.00 117.24 ? 493 PRO A O 1 ATOM 3710 C CB . PRO A 1 493 ? 40.581 -51.175 -0.768 1.00 126.04 ? 493 PRO A CB 1 ATOM 3711 C CG . PRO A 1 493 ? 39.647 -50.048 -1.160 1.00 119.44 ? 493 PRO A CG 1 ATOM 3712 C CD . PRO A 1 493 ? 40.577 -49.024 -1.707 1.00 121.65 ? 493 PRO A CD 1 ATOM 3713 N N . ASP A 1 494 ? 42.208 -53.442 -2.568 1.00 144.73 ? 494 ASP A N 1 ATOM 3714 C CA . ASP A 1 494 ? 42.109 -54.677 -3.341 1.00 153.23 ? 494 ASP A CA 1 ATOM 3715 C C . ASP A 1 494 ? 40.729 -55.314 -3.224 1.00 148.16 ? 494 ASP A C 1 ATOM 3716 O O . ASP A 1 494 ? 40.181 -55.437 -2.130 1.00 144.45 ? 494 ASP A O 1 ATOM 3717 C CB . ASP A 1 494 ? 43.176 -55.672 -2.882 1.00 165.28 ? 494 ASP A CB 1 ATOM 3718 C CG . ASP A 1 494 ? 42.983 -57.054 -3.479 1.00 178.23 ? 494 ASP A CG 1 ATOM 3719 O OD1 . ASP A 1 494 ? 42.583 -57.150 -4.661 1.00 184.40 ? 494 ASP A OD1 1 ATOM 3720 O OD2 . ASP A 1 494 ? 43.238 -58.046 -2.763 1.00 182.10 ? 494 ASP A OD2 1 ATOM 3721 N N . ALA A 1 495 ? 40.183 -55.740 -4.356 1.00 151.06 ? 495 ALA A N 1 ATOM 3722 C CA . ALA A 1 495 ? 38.833 -56.290 -4.393 1.00 156.91 ? 495 ALA A CA 1 ATOM 3723 C C . ALA A 1 495 ? 38.735 -57.719 -3.852 1.00 160.94 ? 495 ALA A C 1 ATOM 3724 O O . ALA A 1 495 ? 37.670 -58.336 -3.917 1.00 165.75 ? 495 ALA A O 1 ATOM 3725 C CB . ALA A 1 495 ? 38.268 -56.213 -5.809 1.00 161.27 ? 495 ALA A CB 1 ATOM 3726 N N . SER A 1 496 ? 39.834 -58.251 -3.324 1.00 158.88 ? 496 SER A N 1 ATOM 3727 C CA . SER A 1 496 ? 39.797 -59.582 -2.725 1.00 158.08 ? 496 SER A CA 1 ATOM 3728 C C . SER A 1 496 ? 39.495 -59.453 -1.244 1.00 156.79 ? 496 SER A C 1 ATOM 3729 O O . SER A 1 496 ? 38.970 -60.378 -0.621 1.00 160.07 ? 496 SER A O 1 ATOM 3730 C CB . SER A 1 496 ? 41.122 -60.325 -2.919 1.00 156.36 ? 496 SER A CB 1 ATOM 3731 O OG . SER A 1 496 ? 41.904 -60.305 -1.735 1.00 155.36 ? 496 SER A OG 1 ATOM 3732 N N . LEU A 1 497 ? 39.825 -58.288 -0.693 1.00 147.94 ? 497 LEU A N 1 ATOM 3733 C CA . LEU A 1 497 ? 39.702 -58.035 0.738 1.00 137.05 ? 497 LEU A CA 1 ATOM 3734 C C . LEU A 1 497 ? 38.272 -58.229 1.231 1.00 139.50 ? 497 LEU A C 1 ATOM 3735 O O . LEU A 1 497 ? 38.031 -58.312 2.436 1.00 143.88 ? 497 LEU A O 1 ATOM 3736 C CB . LEU A 1 497 ? 40.182 -56.618 1.071 1.00 121.06 ? 497 LEU A CB 1 ATOM 3737 C CG . LEU A 1 497 ? 41.647 -56.273 0.792 1.00 106.29 ? 497 LEU A CG 1 ATOM 3738 C CD1 . LEU A 1 497 ? 41.910 -54.781 0.972 1.00 101.36 ? 497 LEU A CD1 1 ATOM 3739 C CD2 . LEU A 1 497 ? 42.558 -57.087 1.683 1.00 92.31 ? 497 LEU A CD2 1 ATOM 3740 N N . PHE A 1 498 ? 37.330 -58.307 0.297 1.00 136.00 ? 498 PHE A N 1 ATOM 3741 C CA . PHE A 1 498 ? 35.916 -58.391 0.644 1.00 136.90 ? 498 PHE A CA 1 ATOM 3742 C C . PHE A 1 498 ? 35.095 -58.994 -0.485 1.00 130.26 ? 498 PHE A C 1 ATOM 3743 O O . PHE A 1 498 ? 34.419 -58.274 -1.219 1.00 127.08 ? 498 PHE A O 1 ATOM 3744 C CB . PHE A 1 498 ? 35.386 -57.005 1.008 1.00 147.44 ? 498 PHE A CB 1 ATOM 3745 C CG . PHE A 1 498 ? 36.262 -55.878 0.533 1.00 153.63 ? 498 PHE A CG 1 ATOM 3746 C CD1 . PHE A 1 498 ? 36.230 -55.466 -0.791 1.00 155.41 ? 498 PHE A CD1 1 ATOM 3747 C CD2 . PHE A 1 498 ? 37.118 -55.230 1.415 1.00 149.92 ? 498 PHE A CD2 1 ATOM 3748 C CE1 . PHE A 1 498 ? 37.037 -54.428 -1.227 1.00 155.10 ? 498 PHE A CE1 1 ATOM 3749 C CE2 . PHE A 1 498 ? 37.927 -54.193 0.986 1.00 150.19 ? 498 PHE A CE2 1 ATOM 3750 C CZ . PHE A 1 498 ? 37.888 -53.791 -0.336 1.00 153.09 ? 498 PHE A CZ 1 ATOM 3751 N N . PRO A 1 499 ? 35.155 -60.326 -0.619 1.00 131.43 ? 499 PRO A N 1 ATOM 3752 C CA . PRO A 1 499 ? 34.532 -61.104 -1.696 1.00 135.75 ? 499 PRO A CA 1 ATOM 3753 C C . PRO A 1 499 ? 33.002 -61.019 -1.774 1.00 142.51 ? 499 PRO A C 1 ATOM 3754 O O . PRO A 1 499 ? 32.459 -61.270 -2.854 1.00 146.20 ? 499 PRO A O 1 ATOM 3755 C CB . PRO A 1 499 ? 34.973 -62.541 -1.386 1.00 131.39 ? 499 PRO A CB 1 ATOM 3756 C CG . PRO A 1 499 ? 36.235 -62.386 -0.615 1.00 129.55 ? 499 PRO A CG 1 ATOM 3757 C CD . PRO A 1 499 ? 36.013 -61.169 0.232 1.00 129.64 ? 499 PRO A CD 1 ATOM 3758 N N . VAL A 1 500 ? 32.322 -60.682 -0.677 1.00 138.41 ? 500 VAL A N 1 ATOM 3759 C CA . VAL A 1 500 ? 30.854 -60.579 -0.693 1.00 125.23 ? 500 VAL A CA 1 ATOM 3760 C C . VAL A 1 500 ? 30.341 -59.140 -0.592 1.00 108.62 ? 500 VAL A C 1 ATOM 3761 O O . VAL A 1 500 ? 29.145 -58.904 -0.396 1.00 95.56 ? 500 VAL A O 1 ATOM 3762 C CB . VAL A 1 500 ? 30.202 -61.445 0.400 1.00 118.01 ? 500 VAL A CB 1 ATOM 3763 C CG1 . VAL A 1 500 ? 29.845 -62.817 -0.157 1.00 114.44 ? 500 VAL A CG1 1 ATOM 3764 C CG2 . VAL A 1 500 ? 31.127 -61.557 1.602 1.00 116.43 ? 500 VAL A CG2 1 ATOM 3765 N N . LEU A 1 501 ? 31.269 -58.197 -0.742 1.00 105.96 ? 501 LEU A N 1 ATOM 3766 C CA . LEU A 1 501 ? 30.996 -56.762 -0.745 1.00 107.44 ? 501 LEU A CA 1 ATOM 3767 C C . LEU A 1 501 ? 29.623 -56.412 -1.355 1.00 112.21 ? 501 LEU A C 1 ATOM 3768 O O . LEU A 1 501 ? 29.178 -57.057 -2.293 1.00 111.93 ? 501 LEU A O 1 ATOM 3769 C CB . LEU A 1 501 ? 32.138 -56.055 -1.493 1.00 106.62 ? 501 LEU A CB 1 ATOM 3770 C CG . LEU A 1 501 ? 32.603 -54.630 -1.157 1.00 114.36 ? 501 LEU A CG 1 ATOM 3771 C CD1 . LEU A 1 501 ? 31.704 -53.600 -1.829 1.00 121.85 ? 501 LEU A CD1 1 ATOM 3772 C CD2 . LEU A 1 501 ? 32.717 -54.367 0.355 1.00 106.87 ? 501 LEU A CD2 1 ATOM 3773 N N . LEU A 1 502 ? 28.946 -55.409 -0.797 1.00 120.01 ? 502 LEU A N 1 ATOM 3774 C CA . LEU A 1 502 ? 27.676 -54.917 -1.345 1.00 118.88 ? 502 LEU A CA 1 ATOM 3775 C C . LEU A 1 502 ? 27.755 -53.429 -1.646 1.00 116.43 ? 502 LEU A C 1 ATOM 3776 O O . LEU A 1 502 ? 27.114 -52.930 -2.567 1.00 108.17 ? 502 LEU A O 1 ATOM 3777 C CB . LEU A 1 502 ? 26.529 -55.126 -0.358 1.00 109.44 ? 502 LEU A CB 1 ATOM 3778 C CG . LEU A 1 502 ? 26.021 -56.536 -0.103 1.00 105.74 ? 502 LEU A CG 1 ATOM 3779 C CD1 . LEU A 1 502 ? 24.657 -56.454 0.563 1.00 96.97 ? 502 LEU A CD1 1 ATOM 3780 C CD2 . LEU A 1 502 ? 25.952 -57.318 -1.399 1.00 102.90 ? 502 LEU A CD2 1 ATOM 3781 N N . VAL A 1 503 ? 28.530 -52.720 -0.836 1.00 115.54 ? 503 VAL A N 1 ATOM 3782 C CA . VAL A 1 503 ? 28.614 -51.276 -0.939 1.00 107.00 ? 503 VAL A CA 1 ATOM 3783 C C . VAL A 1 503 ? 30.035 -50.806 -0.653 1.00 101.10 ? 503 VAL A C 1 ATOM 3784 O O . VAL A 1 503 ? 30.793 -51.480 0.044 1.00 100.70 ? 503 VAL A O 1 ATOM 3785 C CB . VAL A 1 503 ? 27.626 -50.604 0.037 1.00 104.40 ? 503 VAL A CB 1 ATOM 3786 C CG1 . VAL A 1 503 ? 27.752 -49.086 -0.023 1.00 103.88 ? 503 VAL A CG1 1 ATOM 3787 C CG2 . VAL A 1 503 ? 26.192 -51.042 -0.267 1.00 101.82 ? 503 VAL A CG2 1 ATOM 3788 N N . MET A 1 504 ? 30.400 -49.659 -1.215 1.00 101.54 ? 504 MET A N 1 ATOM 3789 C CA . MET A 1 504 ? 31.681 -49.039 -0.907 1.00 109.00 ? 504 MET A CA 1 ATOM 3790 C C . MET A 1 504 ? 31.636 -47.524 -1.079 1.00 108.32 ? 504 MET A C 1 ATOM 3791 O O . MET A 1 504 ? 31.915 -47.006 -2.157 1.00 93.44 ? 504 MET A O 1 ATOM 3792 C CB . MET A 1 504 ? 32.808 -49.634 -1.757 1.00 107.33 ? 504 MET A CB 1 ATOM 3793 C CG . MET A 1 504 ? 34.176 -49.050 -1.438 1.00 105.53 ? 504 MET A CG 1 ATOM 3794 S SD . MET A 1 504 ? 35.492 -49.726 -2.458 1.00 141.79 ? 504 MET A SD 1 ATOM 3795 C CE . MET A 1 504 ? 35.281 -51.484 -2.161 1.00 111.67 ? 504 MET A CE 1 ATOM 3796 N N . LYS A 1 505 ? 31.278 -46.818 -0.011 1.00 118.28 ? 505 LYS A N 1 ATOM 3797 C CA . LYS A 1 505 ? 31.328 -45.363 -0.016 1.00 118.64 ? 505 LYS A CA 1 ATOM 3798 C C . LYS A 1 505 ? 32.779 -44.927 0.183 1.00 119.63 ? 505 LYS A C 1 ATOM 3799 O O . LYS A 1 505 ? 33.260 -44.829 1.310 1.00 127.34 ? 505 LYS A O 1 ATOM 3800 C CB . LYS A 1 505 ? 30.400 -44.778 1.065 1.00 110.74 ? 505 LYS A CB 1 ATOM 3801 C CG . LYS A 1 505 ? 30.618 -43.287 1.361 1.00 113.97 ? 505 LYS A CG 1 ATOM 3802 C CD . LYS A 1 505 ? 29.326 -42.559 1.772 1.00 115.33 ? 505 LYS A CD 1 ATOM 3803 C CE . LYS A 1 505 ? 29.573 -41.072 2.053 1.00 107.33 ? 505 LYS A CE 1 ATOM 3804 N NZ . LYS A 1 505 ? 28.428 -40.222 1.617 1.00 97.54 ? 505 LYS A NZ 1 ATOM 3805 N N . ILE A 1 506 ? 33.483 -44.683 -0.916 1.00 112.38 ? 506 ILE A N 1 ATOM 3806 C CA . ILE A 1 506 ? 34.905 -44.363 -0.839 1.00 108.64 ? 506 ILE A CA 1 ATOM 3807 C C . ILE A 1 506 ? 35.262 -43.087 -1.617 1.00 101.79 ? 506 ILE A C 1 ATOM 3808 O O . ILE A 1 506 ? 36.087 -43.105 -2.524 1.00 94.52 ? 506 ILE A O 1 ATOM 3809 C CB . ILE A 1 506 ? 35.783 -45.590 -1.260 1.00 104.52 ? 506 ILE A CB 1 ATOM 3810 C CG1 . ILE A 1 506 ? 37.271 -45.235 -1.303 1.00 106.73 ? 506 ILE A CG1 1 ATOM 3811 C CG2 . ILE A 1 506 ? 35.329 -46.177 -2.595 1.00 93.81 ? 506 ILE A CG2 1 ATOM 3812 C CD1 . ILE A 1 506 ? 38.103 -46.260 -2.044 1.00 102.83 ? 506 ILE A CD1 1 ATOM 3813 N N . ALA A 1 507 ? 34.388 -42.095 -1.389 1.00 102.42 ? 507 ALA A N 1 ATOM 3814 C CA . ALA A 1 507 ? 34.585 -40.798 -2.045 1.00 100.11 ? 507 ALA A CA 1 ATOM 3815 C C . ALA A 1 507 ? 35.531 -39.840 -1.311 1.00 110.54 ? 507 ALA A C 1 ATOM 3816 O O . ALA A 1 507 ? 36.333 -40.246 -0.469 1.00 113.65 ? 507 ALA A O 1 ATOM 3817 C CB . ALA A 1 507 ? 33.241 -40.115 -2.282 1.00 81.68 ? 507 ALA A CB 1 ATOM 3818 N N . SER A 1 508 ? 35.419 -38.562 -1.657 1.00 108.34 ? 508 SER A N 1 ATOM 3819 C CA . SER A 1 508 ? 36.293 -37.511 -1.143 1.00 112.18 ? 508 SER A CA 1 ATOM 3820 C C . SER A 1 508 ? 37.716 -37.961 -0.767 1.00 120.32 ? 508 SER A C 1 ATOM 3821 O O . SER A 1 508 ? 38.239 -37.579 0.286 1.00 117.48 ? 508 SER A O 1 ATOM 3822 C CB . SER A 1 508 ? 35.622 -36.801 0.027 1.00 107.61 ? 508 SER A CB 1 ATOM 3823 O OG . SER A 1 508 ? 35.905 -35.415 -0.018 1.00 107.23 ? 508 SER A OG 1 ATOM 3824 N N . ASN A 1 509 ? 38.378 -38.627 -1.580 1.00 133.66 ? 509 ASN A N 1 ATOM 3825 C CA . ASN A 1 509 ? 39.688 -39.255 -1.388 1.00 138.28 ? 509 ASN A CA 1 ATOM 3826 C C . ASN A 1 509 ? 40.794 -38.692 -2.293 1.00 140.56 ? 509 ASN A C 1 ATOM 3827 O O . ASN A 1 509 ? 40.630 -37.629 -2.892 1.00 144.95 ? 509 ASN A O 1 ATOM 3828 C CB . ASN A 1 509 ? 39.577 -40.774 -1.566 1.00 137.04 ? 509 ASN A CB 1 ATOM 3829 C CG . ASN A 1 509 ? 39.353 -41.509 -0.250 1.00 127.73 ? 509 ASN A CG 1 ATOM 3830 O OD1 . ASN A 1 509 ? 40.078 -41.297 0.723 1.00 123.61 ? 509 ASN A OD1 1 ATOM 3831 N ND2 . ASN A 1 509 ? 38.361 -42.393 -0.225 1.00 122.69 ? 509 ASN A ND2 1 ATOM 3832 N N . GLN A 1 510 ? 41.917 -39.407 -2.377 1.00 135.07 ? 510 GLN A N 1 ATOM 3833 C CA . GLN A 1 510 ? 43.053 -38.987 -3.202 1.00 132.08 ? 510 GLN A CA 1 ATOM 3834 C C . GLN A 1 510 ? 43.295 -39.912 -4.392 1.00 136.07 ? 510 GLN A C 1 ATOM 3835 O O . GLN A 1 510 ? 44.422 -40.043 -4.875 1.00 138.11 ? 510 GLN A O 1 ATOM 3836 C CB . GLN A 1 510 ? 44.336 -38.872 -2.369 1.00 120.82 ? 510 GLN A CB 1 ATOM 3837 C CG . GLN A 1 510 ? 44.452 -37.566 -1.622 1.00 119.33 ? 510 GLN A CG 1 ATOM 3838 C CD . GLN A 1 510 ? 43.768 -36.418 -2.354 1.00 125.05 ? 510 GLN A CD 1 ATOM 3839 O OE1 . GLN A 1 510 ? 42.714 -35.935 -1.926 1.00 120.45 ? 510 GLN A OE1 1 ATOM 3840 N NE2 . GLN A 1 510 ? 44.358 -35.985 -3.468 1.00 125.87 ? 510 GLN A NE2 1 ATOM 3841 N N . LEU A 1 511 ? 42.232 -40.547 -4.865 1.00 133.34 ? 511 LEU A N 1 ATOM 3842 C CA . LEU A 1 511 ? 42.353 -41.467 -5.983 1.00 136.38 ? 511 LEU A CA 1 ATOM 3843 C C . LEU A 1 511 ? 42.652 -40.733 -7.287 1.00 145.74 ? 511 LEU A C 1 ATOM 3844 O O . LEU A 1 511 ? 41.856 -39.900 -7.726 1.00 147.26 ? 511 LEU A O 1 ATOM 3845 C CB . LEU A 1 511 ? 41.078 -42.300 -6.132 1.00 122.99 ? 511 LEU A CB 1 ATOM 3846 C CG . LEU A 1 511 ? 40.792 -43.309 -5.017 1.00 107.91 ? 511 LEU A CG 1 ATOM 3847 C CD1 . LEU A 1 511 ? 39.617 -44.183 -5.406 1.00 105.78 ? 511 LEU A CD1 1 ATOM 3848 C CD2 . LEU A 1 511 ? 42.019 -44.167 -4.706 1.00 95.32 ? 511 LEU A CD2 1 ATOM 3849 N N . LYS A 1 512 ? 43.804 -41.035 -7.891 1.00 144.98 ? 512 LYS A N 1 ATOM 3850 C CA . LYS A 1 512 ? 44.101 -40.587 -9.252 1.00 132.70 ? 512 LYS A CA 1 ATOM 3851 C C . LYS A 1 512 ? 43.387 -41.495 -10.251 1.00 136.50 ? 512 LYS A C 1 ATOM 3852 O O . LYS A 1 512 ? 42.457 -41.057 -10.924 1.00 140.88 ? 512 LYS A O 1 ATOM 3853 C CB . LYS A 1 512 ? 45.609 -40.545 -9.526 1.00 123.32 ? 512 LYS A CB 1 ATOM 3854 C CG . LYS A 1 512 ? 46.310 -39.313 -8.963 1.00 119.98 ? 512 LYS A CG 1 ATOM 3855 C CD . LYS A 1 512 ? 47.626 -39.027 -9.684 1.00 126.11 ? 512 LYS A CD 1 ATOM 3856 C CE . LYS A 1 512 ? 48.651 -40.148 -9.495 1.00 126.41 ? 512 LYS A CE 1 ATOM 3857 N NZ . LYS A 1 512 ? 49.824 -40.026 -10.426 1.00 117.91 ? 512 LYS A NZ 1 ATOM 3858 N N . SER A 1 513 ? 43.807 -42.758 -10.336 1.00 141.19 ? 513 SER A N 1 ATOM 3859 C CA . SER A 1 513 ? 43.109 -43.736 -11.182 1.00 149.98 ? 513 SER A CA 1 ATOM 3860 C C . SER A 1 513 ? 43.267 -45.193 -10.720 1.00 145.13 ? 513 SER A C 1 ATOM 3861 O O . SER A 1 513 ? 44.379 -45.662 -10.461 1.00 131.78 ? 513 SER A O 1 ATOM 3862 C CB . SER A 1 513 ? 43.503 -43.585 -12.661 1.00 161.30 ? 513 SER A CB 1 ATOM 3863 O OG . SER A 1 513 ? 44.842 -43.991 -12.895 1.00 168.23 ? 513 SER A OG 1 ATOM 3864 N N . VAL A 1 514 ? 42.137 -45.895 -10.635 1.00 156.21 ? 514 VAL A N 1 ATOM 3865 C CA . VAL A 1 514 ? 42.086 -47.276 -10.149 1.00 167.29 ? 514 VAL A CA 1 ATOM 3866 C C . VAL A 1 514 ? 42.411 -48.291 -11.246 1.00 176.57 ? 514 VAL A C 1 ATOM 3867 O O . VAL A 1 514 ? 42.031 -48.105 -12.403 1.00 175.79 ? 514 VAL A O 1 ATOM 3868 C CB . VAL A 1 514 ? 40.698 -47.614 -9.543 1.00 160.12 ? 514 VAL A CB 1 ATOM 3869 C CG1 . VAL A 1 514 ? 40.166 -46.438 -8.741 1.00 155.95 ? 514 VAL A CG1 1 ATOM 3870 C CG2 . VAL A 1 514 ? 39.706 -48.005 -10.633 1.00 156.96 ? 514 VAL A CG2 1 ATOM 3871 N N . PRO A 1 515 ? 43.111 -49.379 -10.880 1.00 183.75 ? 515 PRO A N 1 ATOM 3872 C CA . PRO A 1 515 ? 43.551 -50.389 -11.848 1.00 194.57 ? 515 PRO A CA 1 ATOM 3873 C C . PRO A 1 515 ? 42.398 -50.922 -12.689 1.00 204.02 ? 515 PRO A C 1 ATOM 3874 O O . PRO A 1 515 ? 41.330 -51.226 -12.154 1.00 199.77 ? 515 PRO A O 1 ATOM 3875 C CB . PRO A 1 515 ? 44.110 -51.505 -10.961 1.00 189.82 ? 515 PRO A CB 1 ATOM 3876 C CG . PRO A 1 515 ? 44.508 -50.823 -9.711 1.00 184.09 ? 515 PRO A CG 1 ATOM 3877 C CD . PRO A 1 515 ? 43.506 -49.727 -9.506 1.00 180.07 ? 515 PRO A CD 1 ATOM 3878 N N . ASP A 1 516 ? 42.620 -51.023 -13.997 1.00 215.31 ? 516 ASP A N 1 ATOM 3879 C CA . ASP A 1 516 ? 41.635 -51.605 -14.901 1.00 216.98 ? 516 ASP A CA 1 ATOM 3880 C C . ASP A 1 516 ? 41.477 -53.091 -14.588 1.00 215.81 ? 516 ASP A C 1 ATOM 3881 O O . ASP A 1 516 ? 42.462 -53.829 -14.502 1.00 210.32 ? 516 ASP A O 1 ATOM 3882 C CB . ASP A 1 516 ? 42.045 -51.399 -16.367 1.00 216.68 ? 516 ASP A CB 1 ATOM 3883 C CG . ASP A 1 516 ? 41.782 -49.979 -16.863 1.00 212.19 ? 516 ASP A CG 1 ATOM 3884 O OD1 . ASP A 1 516 ? 41.085 -49.213 -16.163 1.00 208.24 ? 516 ASP A OD1 1 ATOM 3885 O OD2 . ASP A 1 516 ? 42.270 -49.631 -17.961 1.00 211.82 ? 516 ASP A OD2 1 ATOM 3886 N N . GLY A 1 517 ? 40.233 -53.520 -14.409 1.00 217.54 ? 517 GLY A N 1 ATOM 3887 C CA . GLY A 1 517 ? 39.947 -54.895 -14.045 1.00 219.27 ? 517 GLY A CA 1 ATOM 3888 C C . GLY A 1 517 ? 39.952 -55.077 -12.542 1.00 216.00 ? 517 GLY A C 1 ATOM 3889 O O . GLY A 1 517 ? 40.618 -55.971 -12.017 1.00 218.77 ? 517 GLY A O 1 ATOM 3890 N N . ILE A 1 518 ? 39.208 -54.222 -11.846 1.00 207.37 ? 518 ILE A N 1 ATOM 3891 C CA . ILE A 1 518 ? 39.153 -54.268 -10.389 1.00 196.65 ? 518 ILE A CA 1 ATOM 3892 C C . ILE A 1 518 ? 37.780 -54.706 -9.866 1.00 181.55 ? 518 ILE A C 1 ATOM 3893 O O . ILE A 1 518 ? 37.694 -55.394 -8.847 1.00 181.29 ? 518 ILE A O 1 ATOM 3894 C CB . ILE A 1 518 ? 39.583 -52.920 -9.752 1.00 139.37 ? 518 ILE A CB 1 ATOM 3895 C CG1 . ILE A 1 518 ? 39.630 -53.036 -8.224 1.00 124.76 ? 518 ILE A CG1 1 ATOM 3896 C CG2 . ILE A 1 518 ? 38.666 -51.788 -10.207 1.00 137.94 ? 518 ILE A CG2 1 ATOM 3897 C CD1 . ILE A 1 518 ? 40.510 -54.157 -7.729 1.00 117.55 ? 518 ILE A CD1 1 ATOM 3898 N N . PHE A 1 519 ? 36.712 -54.321 -10.562 1.00 165.96 ? 519 PHE A N 1 ATOM 3899 C CA . PHE A 1 519 ? 35.379 -54.787 -10.191 1.00 157.72 ? 519 PHE A CA 1 ATOM 3900 C C . PHE A 1 519 ? 35.087 -56.124 -10.857 1.00 165.03 ? 519 PHE A C 1 ATOM 3901 O O . PHE A 1 519 ? 33.956 -56.396 -11.259 1.00 161.68 ? 519 PHE A O 1 ATOM 3902 C CB . PHE A 1 519 ? 34.293 -53.773 -10.559 1.00 150.48 ? 519 PHE A CB 1 ATOM 3903 C CG . PHE A 1 519 ? 34.692 -52.345 -10.335 1.00 147.27 ? 519 PHE A CG 1 ATOM 3904 C CD1 . PHE A 1 519 ? 34.209 -51.342 -11.159 1.00 148.76 ? 519 PHE A CD1 1 ATOM 3905 C CD2 . PHE A 1 519 ? 35.560 -52.002 -9.313 1.00 141.34 ? 519 PHE A CD2 1 ATOM 3906 C CE1 . PHE A 1 519 ? 34.577 -50.023 -10.961 1.00 144.45 ? 519 PHE A CE1 1 ATOM 3907 C CE2 . PHE A 1 519 ? 35.933 -50.686 -9.112 1.00 136.70 ? 519 PHE A CE2 1 ATOM 3908 C CZ . PHE A 1 519 ? 35.443 -49.696 -9.936 1.00 138.38 ? 519 PHE A CZ 1 ATOM 3909 N N . ASP A 1 520 ? 36.121 -56.951 -10.976 1.00 177.12 ? 520 ASP A N 1 ATOM 3910 C CA . ASP A 1 520 ? 35.983 -58.291 -11.535 1.00 188.08 ? 520 ASP A CA 1 ATOM 3911 C C . ASP A 1 520 ? 35.486 -59.275 -10.480 1.00 188.95 ? 520 ASP A C 1 ATOM 3912 O O . ASP A 1 520 ? 34.503 -59.984 -10.695 1.00 189.89 ? 520 ASP A O 1 ATOM 3913 C CB . ASP A 1 520 ? 37.317 -58.775 -12.110 1.00 196.02 ? 520 ASP A CB 1 ATOM 3914 C CG . ASP A 1 520 ? 37.683 -58.077 -13.406 1.00 199.67 ? 520 ASP A CG 1 ATOM 3915 O OD1 . ASP A 1 520 ? 36.874 -57.257 -13.894 1.00 198.97 ? 520 ASP A OD1 1 ATOM 3916 O OD2 . ASP A 1 520 ? 38.782 -58.352 -13.936 1.00 201.03 ? 520 ASP A OD2 1 ATOM 3917 N N . ARG A 1 521 ? 36.170 -59.317 -9.341 1.00 187.24 ? 521 ARG A N 1 ATOM 3918 C CA . ARG A 1 521 ? 35.776 -60.209 -8.257 1.00 184.63 ? 521 ARG A CA 1 ATOM 3919 C C . ARG A 1 521 ? 34.763 -59.550 -7.319 1.00 172.74 ? 521 ARG A C 1 ATOM 3920 O O . ARG A 1 521 ? 34.307 -60.166 -6.355 1.00 172.24 ? 521 ARG A O 1 ATOM 3921 C CB . ARG A 1 521 ? 36.998 -60.734 -7.492 1.00 191.48 ? 521 ARG A CB 1 ATOM 3922 C CG . ARG A 1 521 ? 38.108 -59.716 -7.274 1.00 198.10 ? 521 ARG A CG 1 ATOM 3923 C CD . ARG A 1 521 ? 38.942 -59.495 -8.535 1.00 204.25 ? 521 ARG A CD 1 ATOM 3924 N NE . ARG A 1 521 ? 40.120 -58.670 -8.276 1.00 204.09 ? 521 ARG A NE 1 ATOM 3925 C CZ . ARG A 1 521 ? 40.885 -58.132 -9.222 1.00 201.48 ? 521 ARG A CZ 1 ATOM 3926 N NH1 . ARG A 1 521 ? 40.598 -58.326 -10.503 1.00 197.84 ? 521 ARG A NH1 1 ATOM 3927 N NH2 . ARG A 1 521 ? 41.937 -57.397 -8.885 1.00 201.88 ? 521 ARG A NH2 1 ATOM 3928 N N . LEU A 1 522 ? 34.411 -58.300 -7.609 1.00 164.18 ? 522 LEU A N 1 ATOM 3929 C CA . LEU A 1 522 ? 33.299 -57.640 -6.925 1.00 154.04 ? 522 LEU A CA 1 ATOM 3930 C C . LEU A 1 522 ? 31.999 -57.965 -7.649 1.00 152.94 ? 522 LEU A C 1 ATOM 3931 O O . LEU A 1 522 ? 31.234 -57.070 -8.021 1.00 142.19 ? 522 LEU A O 1 ATOM 3932 C CB . LEU A 1 522 ? 33.505 -56.126 -6.848 1.00 142.51 ? 522 LEU A CB 1 ATOM 3933 C CG . LEU A 1 522 ? 34.686 -55.660 -5.991 1.00 130.92 ? 522 LEU A CG 1 ATOM 3934 C CD1 . LEU A 1 522 ? 34.582 -54.177 -5.685 1.00 115.15 ? 522 LEU A CD1 1 ATOM 3935 C CD2 . LEU A 1 522 ? 34.759 -56.464 -4.705 1.00 132.85 ? 522 LEU A CD2 1 ATOM 3936 N N . THR A 1 523 ? 31.774 -59.263 -7.847 1.00 160.48 ? 523 THR A N 1 ATOM 3937 C CA . THR A 1 523 ? 30.595 -59.780 -8.538 1.00 161.74 ? 523 THR A CA 1 ATOM 3938 C C . THR A 1 523 ? 29.342 -59.544 -7.704 1.00 148.22 ? 523 THR A C 1 ATOM 3939 O O . THR A 1 523 ? 28.282 -60.110 -7.972 1.00 142.00 ? 523 THR A O 1 ATOM 3940 C CB . THR A 1 523 ? 30.727 -61.302 -8.803 1.00 180.26 ? 523 THR A CB 1 ATOM 3941 O OG1 . THR A 1 523 ? 30.969 -61.987 -7.567 1.00 178.46 ? 523 THR A OG1 1 ATOM 3942 C CG2 . THR A 1 523 ? 31.873 -61.593 -9.762 1.00 180.13 ? 523 THR A CG2 1 ATOM 3943 N N . SER A 1 524 ? 29.474 -58.694 -6.695 1.00 137.48 ? 524 SER A N 1 ATOM 3944 C CA . SER A 1 524 ? 28.453 -58.566 -5.676 1.00 119.57 ? 524 SER A CA 1 ATOM 3945 C C . SER A 1 524 ? 28.090 -57.101 -5.466 1.00 111.45 ? 524 SER A C 1 ATOM 3946 O O . SER A 1 524 ? 26.941 -56.769 -5.158 1.00 100.87 ? 524 SER A O 1 ATOM 3947 C CB . SER A 1 524 ? 28.984 -59.174 -4.382 1.00 111.34 ? 524 SER A CB 1 ATOM 3948 O OG . SER A 1 524 ? 29.991 -60.137 -4.657 1.00 108.57 ? 524 SER A OG 1 ATOM 3949 N N . LEU A 1 525 ? 29.084 -56.232 -5.638 1.00 116.83 ? 525 LEU A N 1 ATOM 3950 C CA . LEU A 1 525 ? 28.897 -54.787 -5.503 1.00 116.10 ? 525 LEU A CA 1 ATOM 3951 C C . LEU A 1 525 ? 27.620 -54.327 -6.199 1.00 115.96 ? 525 LEU A C 1 ATOM 3952 O O . LEU A 1 525 ? 27.427 -54.572 -7.388 1.00 131.55 ? 525 LEU A O 1 ATOM 3953 C CB . LEU A 1 525 ? 30.131 -54.041 -6.036 1.00 112.24 ? 525 LEU A CB 1 ATOM 3954 C CG . LEU A 1 525 ? 30.022 -52.704 -6.778 1.00 108.61 ? 525 LEU A CG 1 ATOM 3955 C CD1 . LEU A 1 525 ? 29.160 -51.696 -6.050 1.00 103.85 ? 525 LEU A CD1 1 ATOM 3956 C CD2 . LEU A 1 525 ? 31.408 -52.134 -7.014 1.00 109.73 ? 525 LEU A CD2 1 ATOM 3957 N N . GLN A 1 526 ? 26.745 -53.666 -5.451 1.00 101.94 ? 526 GLN A N 1 ATOM 3958 C CA . GLN A 1 526 ? 25.466 -53.236 -5.998 1.00 109.88 ? 526 GLN A CA 1 ATOM 3959 C C . GLN A 1 526 ? 25.223 -51.726 -5.874 1.00 114.57 ? 526 GLN A C 1 ATOM 3960 O O . GLN A 1 526 ? 24.166 -51.230 -6.262 1.00 118.74 ? 526 GLN A O 1 ATOM 3961 C CB . GLN A 1 526 ? 24.323 -54.038 -5.365 1.00 117.24 ? 526 GLN A CB 1 ATOM 3962 C CG . GLN A 1 526 ? 24.226 -53.913 -3.852 1.00 125.39 ? 526 GLN A CG 1 ATOM 3963 C CD . GLN A 1 526 ? 23.409 -55.027 -3.219 1.00 127.05 ? 526 GLN A CD 1 ATOM 3964 O OE1 . GLN A 1 526 ? 22.645 -54.796 -2.276 1.00 126.35 ? 526 GLN A OE1 1 ATOM 3965 N NE2 . GLN A 1 526 ? 23.569 -56.245 -3.732 1.00 124.35 ? 526 GLN A NE2 1 ATOM 3966 N N . LYS A 1 527 ? 26.209 -51.003 -5.345 1.00 119.80 ? 527 LYS A N 1 ATOM 3967 C CA . LYS A 1 527 ? 26.130 -49.543 -5.189 1.00 117.69 ? 527 LYS A CA 1 ATOM 3968 C C . LYS A 1 527 ? 27.489 -48.984 -4.752 1.00 106.19 ? 527 LYS A C 1 ATOM 3969 O O . LYS A 1 527 ? 28.221 -49.618 -3.985 1.00 87.45 ? 527 LYS A O 1 ATOM 3970 C CB . LYS A 1 527 ? 25.027 -49.150 -4.193 1.00 117.00 ? 527 LYS A CB 1 ATOM 3971 C CG . LYS A 1 527 ? 24.593 -47.685 -4.259 1.00 118.69 ? 527 LYS A CG 1 ATOM 3972 C CD . LYS A 1 527 ? 23.245 -47.467 -3.565 1.00 116.98 ? 527 LYS A CD 1 ATOM 3973 C CE . LYS A 1 527 ? 22.676 -46.077 -3.858 1.00 114.93 ? 527 LYS A CE 1 ATOM 3974 N NZ . LYS A 1 527 ? 21.205 -45.981 -3.593 1.00 106.58 ? 527 LYS A NZ 1 ATOM 3975 N N . ILE A 1 528 ? 27.837 -47.803 -5.247 1.00 108.25 ? 528 ILE A N 1 ATOM 3976 C CA . ILE A 1 528 ? 29.182 -47.288 -5.028 1.00 112.50 ? 528 ILE A CA 1 ATOM 3977 C C . ILE A 1 528 ? 29.230 -45.767 -5.069 1.00 120.59 ? 528 ILE A C 1 ATOM 3978 O O . ILE A 1 528 ? 28.365 -45.117 -5.671 1.00 126.98 ? 528 ILE A O 1 ATOM 3979 C CB . ILE A 1 528 ? 30.179 -47.873 -6.063 1.00 122.07 ? 528 ILE A CB 1 ATOM 3980 C CG1 . ILE A 1 528 ? 31.628 -47.721 -5.586 1.00 112.26 ? 528 ILE A CG1 1 ATOM 3981 C CG2 . ILE A 1 528 ? 29.977 -47.235 -7.437 1.00 118.76 ? 528 ILE A CG2 1 ATOM 3982 C CD1 . ILE A 1 528 ? 32.639 -48.431 -6.481 1.00 98.94 ? 528 ILE A CD1 1 ATOM 3983 N N . TRP A 1 529 ? 30.247 -45.217 -4.407 1.00 115.42 ? 529 TRP A N 1 ATOM 3984 C CA . TRP A 1 529 ? 30.471 -43.779 -4.322 1.00 106.12 ? 529 TRP A CA 1 ATOM 3985 C C . TRP A 1 529 ? 31.879 -43.487 -4.814 1.00 107.06 ? 529 TRP A C 1 ATOM 3986 O O . TRP A 1 529 ? 32.815 -44.183 -4.436 1.00 113.20 ? 529 TRP A O 1 ATOM 3987 C CB . TRP A 1 529 ? 30.333 -43.307 -2.867 1.00 99.43 ? 529 TRP A CB 1 ATOM 3988 C CG . TRP A 1 529 ? 28.933 -42.937 -2.454 1.00 101.00 ? 529 TRP A CG 1 ATOM 3989 C CD1 . TRP A 1 529 ? 28.400 -41.679 -2.402 1.00 109.64 ? 529 TRP A CD1 1 ATOM 3990 C CD2 . TRP A 1 529 ? 27.893 -43.830 -2.027 1.00 97.34 ? 529 TRP A CD2 1 ATOM 3991 N NE1 . TRP A 1 529 ? 27.093 -41.733 -1.978 1.00 111.13 ? 529 TRP A NE1 1 ATOM 3992 C CE2 . TRP A 1 529 ? 26.755 -43.040 -1.743 1.00 101.35 ? 529 TRP A CE2 1 ATOM 3993 C CE3 . TRP A 1 529 ? 27.811 -45.218 -1.860 1.00 86.57 ? 529 TRP A CE3 1 ATOM 3994 C CZ2 . TRP A 1 529 ? 25.548 -43.593 -1.305 1.00 88.51 ? 529 TRP A CZ2 1 ATOM 3995 C CZ3 . TRP A 1 529 ? 26.609 -45.766 -1.425 1.00 84.49 ? 529 TRP A CZ3 1 ATOM 3996 C CH2 . TRP A 1 529 ? 25.493 -44.953 -1.155 1.00 81.07 ? 529 TRP A CH2 1 ATOM 3997 N N . LEU A 1 530 ? 32.037 -42.473 -5.660 1.00 107.99 ? 530 LEU A N 1 ATOM 3998 C CA . LEU A 1 530 ? 33.373 -42.059 -6.103 1.00 109.78 ? 530 LEU A CA 1 ATOM 3999 C C . LEU A 1 530 ? 33.524 -40.539 -6.251 1.00 110.54 ? 530 LEU A C 1 ATOM 4000 O O . LEU A 1 530 ? 34.643 -40.039 -6.420 1.00 112.95 ? 530 LEU A O 1 ATOM 4001 C CB . LEU A 1 530 ? 33.770 -42.753 -7.413 1.00 107.39 ? 530 LEU A CB 1 ATOM 4002 C CG . LEU A 1 530 ? 34.387 -44.152 -7.384 1.00 98.45 ? 530 LEU A CG 1 ATOM 4003 C CD1 . LEU A 1 530 ? 33.361 -45.209 -7.021 1.00 89.99 ? 530 LEU A CD1 1 ATOM 4004 C CD2 . LEU A 1 530 ? 34.995 -44.457 -8.739 1.00 95.22 ? 530 LEU A CD2 1 ATOM 4005 N N . HIS A 1 531 ? 32.405 -39.817 -6.180 1.00 106.02 ? 531 HIS A N 1 ATOM 4006 C CA . HIS A 1 531 ? 32.405 -38.366 -6.383 1.00 118.52 ? 531 HIS A CA 1 ATOM 4007 C C . HIS A 1 531 ? 33.494 -37.604 -5.611 1.00 122.98 ? 531 HIS A C 1 ATOM 4008 O O . HIS A 1 531 ? 34.351 -38.206 -4.966 1.00 110.04 ? 531 HIS A O 1 ATOM 4009 C CB . HIS A 1 531 ? 31.011 -37.755 -6.143 1.00 125.08 ? 531 HIS A CB 1 ATOM 4010 C CG . HIS A 1 531 ? 30.408 -38.088 -4.810 1.00 133.16 ? 531 HIS A CG 1 ATOM 4011 N ND1 . HIS A 1 531 ? 30.764 -37.439 -3.647 1.00 135.47 ? 531 HIS A ND1 1 ATOM 4012 C CD2 . HIS A 1 531 ? 29.445 -38.976 -4.464 1.00 133.85 ? 531 HIS A CD2 1 ATOM 4013 C CE1 . HIS A 1 531 ? 30.060 -37.925 -2.640 1.00 131.70 ? 531 HIS A CE1 1 ATOM 4014 N NE2 . HIS A 1 531 ? 29.251 -38.858 -3.109 1.00 131.67 ? 531 HIS A NE2 1 ATOM 4015 N N . THR A 1 532 ? 33.458 -36.277 -5.704 1.00 139.61 ? 532 THR A N 1 ATOM 4016 C CA . THR A 1 532 ? 34.502 -35.423 -5.137 1.00 147.51 ? 532 THR A CA 1 ATOM 4017 C C . THR A 1 532 ? 35.847 -36.147 -5.055 1.00 150.38 ? 532 THR A C 1 ATOM 4018 O O . THR A 1 532 ? 36.212 -36.698 -4.018 1.00 141.97 ? 532 THR A O 1 ATOM 4019 C CB . THR A 1 532 ? 34.095 -34.882 -3.758 1.00 149.00 ? 532 THR A CB 1 ATOM 4020 O OG1 . THR A 1 532 ? 32.843 -34.195 -3.875 1.00 148.88 ? 532 THR A OG1 1 ATOM 4021 C CG2 . THR A 1 532 ? 35.153 -33.922 -3.223 1.00 150.21 ? 532 THR A CG2 1 ATOM 4022 N N . ASN A 1 533 ? 36.581 -36.139 -6.163 1.00 162.94 ? 533 ASN A N 1 ATOM 4023 C CA . ASN A 1 533 ? 37.807 -36.917 -6.273 1.00 165.23 ? 533 ASN A CA 1 ATOM 4024 C C . ASN A 1 533 ? 38.687 -36.381 -7.400 1.00 167.97 ? 533 ASN A C 1 ATOM 4025 O O . ASN A 1 533 ? 38.220 -36.226 -8.527 1.00 169.22 ? 533 ASN A O 1 ATOM 4026 C CB . ASN A 1 533 ? 37.447 -38.382 -6.534 1.00 163.39 ? 533 ASN A CB 1 ATOM 4027 C CG . ASN A 1 533 ? 38.422 -39.351 -5.899 1.00 162.60 ? 533 ASN A CG 1 ATOM 4028 O OD1 . ASN A 1 533 ? 39.613 -39.065 -5.776 1.00 169.54 ? 533 ASN A OD1 1 ATOM 4029 N ND2 . ASN A 1 533 ? 37.918 -40.514 -5.499 1.00 153.77 ? 533 ASN A ND2 1 ATOM 4030 N N . PRO A 1 534 ? 39.960 -36.072 -7.097 1.00 169.78 ? 534 PRO A N 1 ATOM 4031 C CA . PRO A 1 534 ? 40.896 -35.655 -8.147 1.00 171.34 ? 534 PRO A CA 1 ATOM 4032 C C . PRO A 1 534 ? 41.320 -36.853 -8.985 1.00 171.41 ? 534 PRO A C 1 ATOM 4033 O O . PRO A 1 534 ? 42.260 -37.545 -8.604 1.00 171.84 ? 534 PRO A O 1 ATOM 4034 C CB . PRO A 1 534 ? 42.102 -35.126 -7.357 1.00 169.60 ? 534 PRO A CB 1 ATOM 4035 C CG . PRO A 1 534 ? 41.612 -34.919 -5.962 1.00 167.26 ? 534 PRO A CG 1 ATOM 4036 C CD . PRO A 1 534 ? 40.557 -35.956 -5.758 1.00 168.01 ? 534 PRO A CD 1 ATOM 4037 N N . TRP A 1 535 ? 40.637 -37.093 -10.102 1.00 171.32 ? 535 TRP A N 1 ATOM 4038 C CA . TRP A 1 535 ? 40.917 -38.256 -10.943 1.00 172.92 ? 535 TRP A CA 1 ATOM 4039 C C . TRP A 1 535 ? 41.955 -37.963 -12.027 1.00 177.32 ? 535 TRP A C 1 ATOM 4040 O O . TRP A 1 535 ? 42.928 -37.243 -11.796 1.00 180.82 ? 535 TRP A O 1 ATOM 4041 C CB . TRP A 1 535 ? 39.632 -38.785 -11.594 1.00 173.41 ? 535 TRP A CB 1 ATOM 4042 C CG . TRP A 1 535 ? 38.683 -39.483 -10.651 1.00 171.34 ? 535 TRP A CG 1 ATOM 4043 C CD1 . TRP A 1 535 ? 37.557 -38.958 -10.082 1.00 169.58 ? 535 TRP A CD1 1 ATOM 4044 C CD2 . TRP A 1 535 ? 38.772 -40.835 -10.185 1.00 170.48 ? 535 TRP A CD2 1 ATOM 4045 N NE1 . TRP A 1 535 ? 36.943 -39.897 -9.287 1.00 165.98 ? 535 TRP A NE1 1 ATOM 4046 C CE2 . TRP A 1 535 ? 37.670 -41.058 -9.332 1.00 169.90 ? 535 TRP A CE2 1 ATOM 4047 C CE3 . TRP A 1 535 ? 39.678 -41.880 -10.400 1.00 169.61 ? 535 TRP A CE3 1 ATOM 4048 C CZ2 . TRP A 1 535 ? 37.451 -42.278 -8.695 1.00 171.00 ? 535 TRP A CZ2 1 ATOM 4049 C CZ3 . TRP A 1 535 ? 39.459 -43.091 -9.768 1.00 169.24 ? 535 TRP A CZ3 1 ATOM 4050 C CH2 . TRP A 1 535 ? 38.355 -43.280 -8.925 1.00 170.37 ? 535 TRP A CH2 1 ATOM 4051 N N . ASP A 1 536 ? 41.732 -38.532 -13.210 1.00 175.21 ? 536 ASP A N 1 ATOM 4052 C CA . ASP A 1 536 ? 42.659 -38.414 -14.334 1.00 171.80 ? 536 ASP A CA 1 ATOM 4053 C C . ASP A 1 536 ? 42.007 -38.966 -15.601 1.00 168.55 ? 536 ASP A C 1 ATOM 4054 O O . ASP A 1 536 ? 42.219 -40.121 -15.967 1.00 163.62 ? 536 ASP A O 1 ATOM 4055 C CB . ASP A 1 536 ? 43.956 -39.175 -14.035 1.00 165.80 ? 536 ASP A CB 1 ATOM 4056 C CG . ASP A 1 536 ? 45.028 -38.942 -15.084 1.00 161.05 ? 536 ASP A CG 1 ATOM 4057 O OD1 . ASP A 1 536 ? 44.824 -38.077 -15.961 1.00 159.74 ? 536 ASP A OD1 1 ATOM 4058 O OD2 . ASP A 1 536 ? 46.076 -39.621 -15.027 1.00 156.74 ? 536 ASP A OD2 1 ATOM 4059 N N . CYS A 1 537 ? 41.210 -38.137 -16.266 1.00 172.38 ? 537 CYS A N 1 ATOM 4060 C CA . CYS A 1 537 ? 40.431 -38.593 -17.415 1.00 182.65 ? 537 CYS A CA 1 ATOM 4061 C C . CYS A 1 537 ? 41.185 -38.498 -18.739 1.00 191.59 ? 537 CYS A C 1 ATOM 4062 O O . CYS A 1 537 ? 40.721 -37.860 -19.689 1.00 183.72 ? 537 CYS A O 1 ATOM 4063 C CB . CYS A 1 537 ? 39.106 -37.837 -17.494 1.00 180.93 ? 537 CYS A CB 1 ATOM 4064 S SG . CYS A 1 537 ? 38.075 -38.091 -16.039 1.00 169.69 ? 537 CYS A SG 1 ATOM 4065 N N . SER A 1 538 ? 42.347 -39.147 -18.785 1.00 202.53 ? 538 SER A N 1 ATOM 4066 C CA . SER A 1 538 ? 43.156 -39.226 -19.996 1.00 210.42 ? 538 SER A CA 1 ATOM 4067 C C . SER A 1 538 ? 42.727 -40.434 -20.814 1.00 210.91 ? 538 SER A C 1 ATOM 4068 O O . SER A 1 538 ? 42.816 -41.571 -20.348 1.00 210.27 ? 538 SER A O 1 ATOM 4069 C CB . SER A 1 538 ? 44.639 -39.351 -19.648 1.00 214.98 ? 538 SER A CB 1 ATOM 4070 O OG . SER A 1 538 ? 44.980 -38.557 -18.527 1.00 216.17 ? 538 SER A OG 1 ATOM 4071 N N . CYS A 1 539 ? 42.275 -40.181 -22.039 1.00 207.49 ? 539 CYS A N 1 ATOM 4072 C CA . CYS A 1 539 ? 41.713 -41.223 -22.894 1.00 198.97 ? 539 CYS A CA 1 ATOM 4073 C C . CYS A 1 539 ? 42.594 -42.475 -22.986 1.00 186.61 ? 539 CYS A C 1 ATOM 4074 O O . CYS A 1 539 ? 42.074 -43.591 -23.004 1.00 179.12 ? 539 CYS A O 1 ATOM 4075 C CB . CYS A 1 539 ? 41.415 -40.667 -24.290 1.00 208.34 ? 539 CYS A CB 1 ATOM 4076 S SG . CYS A 1 539 ? 39.772 -41.083 -24.937 1.00 350.30 ? 539 CYS A SG 1 ATOM 4077 N N . PRO A 1 540 ? 43.927 -42.295 -23.050 1.00 185.04 ? 540 PRO A N 1 ATOM 4078 C CA . PRO A 1 540 ? 44.836 -43.449 -23.136 1.00 186.07 ? 540 PRO A CA 1 ATOM 4079 C C . PRO A 1 540 ? 44.922 -44.318 -21.872 1.00 178.79 ? 540 PRO A C 1 ATOM 4080 O O . PRO A 1 540 ? 45.453 -45.428 -21.958 1.00 177.63 ? 540 PRO A O 1 ATOM 4081 C CB . PRO A 1 540 ? 46.200 -42.805 -23.423 1.00 186.64 ? 540 PRO A CB 1 ATOM 4082 C CG . PRO A 1 540 ? 45.880 -41.467 -23.995 1.00 186.03 ? 540 PRO A CG 1 ATOM 4083 C CD . PRO A 1 540 ? 44.634 -41.025 -23.295 1.00 181.85 ? 540 PRO A CD 1 ATOM 4084 N N . ARG A 1 541 ? 44.424 -43.837 -20.733 1.00 169.85 ? 541 ARG A N 1 ATOM 4085 C CA . ARG A 1 541 ? 44.492 -44.616 -19.490 1.00 163.98 ? 541 ARG A CA 1 ATOM 4086 C C . ARG A 1 541 ? 43.143 -44.920 -18.823 1.00 148.51 ? 541 ARG A C 1 ATOM 4087 O O . ARG A 1 541 ? 42.960 -46.000 -18.253 1.00 135.78 ? 541 ARG A O 1 ATOM 4088 C CB . ARG A 1 541 ? 45.457 -43.978 -18.473 1.00 164.54 ? 541 ARG A CB 1 ATOM 4089 C CG . ARG A 1 541 ? 45.535 -42.456 -18.505 1.00 162.30 ? 541 ARG A CG 1 ATOM 4090 C CD . ARG A 1 541 ? 46.588 -41.972 -19.498 1.00 161.27 ? 541 ARG A CD 1 ATOM 4091 N NE . ARG A 1 541 ? 47.942 -42.349 -19.096 1.00 157.89 ? 541 ARG A NE 1 ATOM 4092 C CZ . ARG A 1 541 ? 49.029 -42.133 -19.832 1.00 153.18 ? 541 ARG A CZ 1 ATOM 4093 N NH1 . ARG A 1 541 ? 48.922 -41.540 -21.015 1.00 154.33 ? 541 ARG A NH1 1 ATOM 4094 N NH2 . ARG A 1 541 ? 50.224 -42.512 -19.389 1.00 143.71 ? 541 ARG A NH2 1 ATOM 4095 N N . ILE A 1 542 ? 42.206 -43.977 -18.895 1.00 145.37 ? 542 ILE A N 1 ATOM 4096 C CA . ILE A 1 542 ? 40.932 -44.117 -18.190 1.00 147.78 ? 542 ILE A CA 1 ATOM 4097 C C . ILE A 1 542 ? 39.943 -45.021 -18.935 1.00 159.07 ? 542 ILE A C 1 ATOM 4098 O O . ILE A 1 542 ? 38.772 -44.683 -19.109 1.00 149.46 ? 542 ILE A O 1 ATOM 4099 C CB . ILE A 1 542 ? 40.298 -42.736 -17.864 1.00 134.17 ? 542 ILE A CB 1 ATOM 4100 C CG1 . ILE A 1 542 ? 39.270 -42.869 -16.739 1.00 134.00 ? 542 ILE A CG1 1 ATOM 4101 C CG2 . ILE A 1 542 ? 39.688 -42.092 -19.109 1.00 132.90 ? 542 ILE A CG2 1 ATOM 4102 C CD1 . ILE A 1 542 ? 38.539 -41.581 -16.429 1.00 135.12 ? 542 ILE A CD1 1 ATOM 4103 N N . ASP A 1 543 ? 40.429 -46.186 -19.353 1.00 178.85 ? 543 ASP A N 1 ATOM 4104 C CA . ASP A 1 543 ? 39.630 -47.141 -20.122 1.00 191.49 ? 543 ASP A CA 1 ATOM 4105 C C . ASP A 1 543 ? 38.465 -47.726 -19.319 1.00 194.05 ? 543 ASP A C 1 ATOM 4106 O O . ASP A 1 543 ? 37.304 -47.338 -19.499 1.00 182.88 ? 543 ASP A O 1 ATOM 4107 C CB . ASP A 1 543 ? 40.518 -48.288 -20.628 1.00 193.21 ? 543 ASP A CB 1 ATOM 4108 C CG . ASP A 1 543 ? 41.494 -47.848 -21.706 1.00 190.31 ? 543 ASP A CG 1 ATOM 4109 O OD1 . ASP A 1 543 ? 41.038 -47.351 -22.760 1.00 191.62 ? 543 ASP A OD1 1 ATOM 4110 O OD2 . ASP A 1 543 ? 42.716 -48.016 -21.503 1.00 184.27 ? 543 ASP A OD2 1 ATOM 4111 N N . TYR A 1 544 ? 38.799 -48.666 -18.435 1.00 203.34 ? 544 TYR A N 1 ATOM 4112 C CA . TYR A 1 544 ? 37.809 -49.453 -17.704 1.00 204.54 ? 544 TYR A CA 1 ATOM 4113 C C . TYR A 1 544 ? 36.775 -48.596 -16.994 1.00 197.55 ? 544 TYR A C 1 ATOM 4114 O O . TYR A 1 544 ? 35.609 -48.565 -17.389 1.00 198.62 ? 544 TYR A O 1 ATOM 4115 C CB . TYR A 1 544 ? 38.494 -50.385 -16.701 1.00 207.35 ? 544 TYR A CB 1 ATOM 4116 C CG . TYR A 1 544 ? 37.537 -51.277 -15.946 1.00 210.95 ? 544 TYR A CG 1 ATOM 4117 C CD1 . TYR A 1 544 ? 36.345 -51.696 -16.526 1.00 214.68 ? 544 TYR A CD1 1 ATOM 4118 C CD2 . TYR A 1 544 ? 37.832 -51.720 -14.665 1.00 211.05 ? 544 TYR A CD2 1 ATOM 4119 C CE1 . TYR A 1 544 ? 35.467 -52.515 -15.845 1.00 214.49 ? 544 TYR A CE1 1 ATOM 4120 C CE2 . TYR A 1 544 ? 36.961 -52.544 -13.977 1.00 212.43 ? 544 TYR A CE2 1 ATOM 4121 C CZ . TYR A 1 544 ? 35.779 -52.937 -14.573 1.00 213.96 ? 544 TYR A CZ 1 ATOM 4122 O OH . TYR A 1 544 ? 34.905 -53.757 -13.895 1.00 214.20 ? 544 TYR A OH 1 ATOM 4123 N N . LEU A 1 545 ? 37.209 -47.916 -15.939 1.00 186.93 ? 545 LEU A N 1 ATOM 4124 C CA . LEU A 1 545 ? 36.339 -47.031 -15.178 1.00 180.37 ? 545 LEU A CA 1 ATOM 4125 C C . LEU A 1 545 ? 35.295 -46.370 -16.076 1.00 180.32 ? 545 LEU A C 1 ATOM 4126 O O . LEU A 1 545 ? 34.099 -46.373 -15.768 1.00 173.68 ? 545 LEU A O 1 ATOM 4127 C CB . LEU A 1 545 ? 37.174 -45.959 -14.472 1.00 175.62 ? 545 LEU A CB 1 ATOM 4128 C CG . LEU A 1 545 ? 36.424 -44.959 -13.589 1.00 166.54 ? 545 LEU A CG 1 ATOM 4129 C CD1 . LEU A 1 545 ? 35.812 -45.655 -12.381 1.00 157.59 ? 545 LEU A CD1 1 ATOM 4130 C CD2 . LEU A 1 545 ? 37.345 -43.828 -13.159 1.00 163.02 ? 545 LEU A CD2 1 ATOM 4131 N N . SER A 1 546 ? 35.761 -45.820 -17.194 1.00 185.67 ? 546 SER A N 1 ATOM 4132 C CA . SER A 1 546 ? 34.917 -45.059 -18.110 1.00 182.29 ? 546 SER A CA 1 ATOM 4133 C C . SER A 1 546 ? 33.706 -45.835 -18.619 1.00 180.03 ? 546 SER A C 1 ATOM 4134 O O . SER A 1 546 ? 32.616 -45.277 -18.737 1.00 172.92 ? 546 SER A O 1 ATOM 4135 C CB . SER A 1 546 ? 35.744 -44.548 -19.293 1.00 179.89 ? 546 SER A CB 1 ATOM 4136 O OG . SER A 1 546 ? 36.661 -43.551 -18.875 1.00 174.68 ? 546 SER A OG 1 ATOM 4137 N N . ARG A 1 547 ? 33.895 -47.118 -18.920 1.00 183.56 ? 547 ARG A N 1 ATOM 4138 C CA . ARG A 1 547 ? 32.813 -47.920 -19.489 1.00 185.76 ? 547 ARG A CA 1 ATOM 4139 C C . ARG A 1 547 ? 32.007 -48.708 -18.445 1.00 180.37 ? 547 ARG A C 1 ATOM 4140 O O . ARG A 1 547 ? 30.842 -49.033 -18.676 1.00 171.35 ? 547 ARG A O 1 ATOM 4141 C CB . ARG A 1 547 ? 33.335 -48.860 -20.586 1.00 192.27 ? 547 ARG A CB 1 ATOM 4142 C CG . ARG A 1 547 ? 34.488 -48.305 -21.422 1.00 190.48 ? 547 ARG A CG 1 ATOM 4143 C CD . ARG A 1 547 ? 34.501 -48.900 -22.829 1.00 183.47 ? 547 ARG A CD 1 ATOM 4144 N NE . ARG A 1 547 ? 35.773 -49.547 -23.153 1.00 182.94 ? 547 ARG A NE 1 ATOM 4145 C CZ . ARG A 1 547 ? 36.950 -48.928 -23.199 1.00 181.23 ? 547 ARG A CZ 1 ATOM 4146 N NH1 . ARG A 1 547 ? 37.034 -47.632 -22.927 1.00 181.35 ? 547 ARG A NH1 1 ATOM 4147 N NH2 . ARG A 1 547 ? 38.047 -49.609 -23.508 1.00 176.47 ? 547 ARG A NH2 1 ATOM 4148 N N . TRP A 1 548 ? 32.618 -49.018 -17.303 1.00 183.38 ? 548 TRP A N 1 ATOM 4149 C CA . TRP A 1 548 ? 31.898 -49.742 -16.253 1.00 172.21 ? 548 TRP A CA 1 ATOM 4150 C C . TRP A 1 548 ? 30.880 -48.844 -15.566 1.00 147.13 ? 548 TRP A C 1 ATOM 4151 O O . TRP A 1 548 ? 29.784 -49.283 -15.209 1.00 133.88 ? 548 TRP A O 1 ATOM 4152 C CB . TRP A 1 548 ? 32.848 -50.339 -15.213 1.00 178.46 ? 548 TRP A CB 1 ATOM 4153 C CG . TRP A 1 548 ? 32.135 -51.288 -14.299 1.00 185.30 ? 548 TRP A CG 1 ATOM 4154 C CD1 . TRP A 1 548 ? 32.088 -52.650 -14.405 1.00 189.95 ? 548 TRP A CD1 1 ATOM 4155 C CD2 . TRP A 1 548 ? 31.335 -50.947 -13.160 1.00 187.30 ? 548 TRP A CD2 1 ATOM 4156 N NE1 . TRP A 1 548 ? 31.321 -53.177 -13.394 1.00 188.97 ? 548 TRP A NE1 1 ATOM 4157 C CE2 . TRP A 1 548 ? 30.847 -52.152 -12.616 1.00 189.34 ? 548 TRP A CE2 1 ATOM 4158 C CE3 . TRP A 1 548 ? 30.992 -49.739 -12.541 1.00 182.56 ? 548 TRP A CE3 1 ATOM 4159 C CZ2 . TRP A 1 548 ? 30.032 -52.184 -11.483 1.00 186.39 ? 548 TRP A CZ2 1 ATOM 4160 C CZ3 . TRP A 1 548 ? 30.181 -49.773 -11.417 1.00 175.12 ? 548 TRP A CZ3 1 ATOM 4161 C CH2 . TRP A 1 548 ? 29.711 -50.986 -10.900 1.00 177.17 ? 548 TRP A CH2 1 ATOM 4162 N N . LEU A 1 549 ? 31.251 -47.583 -15.382 1.00 141.26 ? 549 LEU A N 1 ATOM 4163 C CA . LEU A 1 549 ? 30.357 -46.611 -14.773 1.00 146.21 ? 549 LEU A CA 1 ATOM 4164 C C . LEU A 1 549 ? 29.085 -46.416 -15.600 1.00 144.13 ? 549 LEU A C 1 ATOM 4165 O O . LEU A 1 549 ? 28.077 -45.905 -15.099 1.00 133.23 ? 549 LEU A O 1 ATOM 4166 C CB . LEU A 1 549 ? 31.083 -45.277 -14.567 1.00 151.97 ? 549 LEU A CB 1 ATOM 4167 C CG . LEU A 1 549 ? 32.125 -45.262 -13.443 1.00 146.84 ? 549 LEU A CG 1 ATOM 4168 C CD1 . LEU A 1 549 ? 32.874 -43.935 -13.395 1.00 144.85 ? 549 LEU A CD1 1 ATOM 4169 C CD2 . LEU A 1 549 ? 31.467 -45.565 -12.101 1.00 134.67 ? 549 LEU A CD2 1 ATOM 4170 N N . ASN A 1 550 ? 29.142 -46.843 -16.862 1.00 151.34 ? 550 ASN A N 1 ATOM 4171 C CA . ASN A 1 550 ? 28.028 -46.689 -17.798 1.00 152.69 ? 550 ASN A CA 1 ATOM 4172 C C . ASN A 1 550 ? 27.104 -47.909 -17.824 1.00 139.31 ? 550 ASN A C 1 ATOM 4173 O O . ASN A 1 550 ? 25.878 -47.776 -17.710 1.00 122.05 ? 550 ASN A O 1 ATOM 4174 C CB . ASN A 1 550 ? 28.546 -46.417 -19.219 1.00 165.32 ? 550 ASN A CB 1 ATOM 4175 C CG . ASN A 1 550 ? 29.576 -45.296 -19.273 1.00 168.70 ? 550 ASN A CG 1 ATOM 4176 O OD1 . ASN A 1 550 ? 30.034 -44.801 -18.242 1.00 174.82 ? 550 ASN A OD1 1 ATOM 4177 N ND2 . ASN A 1 550 ? 29.951 -44.897 -20.488 1.00 160.02 ? 550 ASN A ND2 1 ATOM 4178 N N . LYS A 1 551 ? 27.703 -49.090 -17.990 1.00 141.91 ? 551 LYS A N 1 ATOM 4179 C CA . LYS A 1 551 ? 26.956 -50.344 -18.040 1.00 143.72 ? 551 LYS A CA 1 ATOM 4180 C C . LYS A 1 551 ? 25.957 -50.387 -16.896 1.00 155.65 ? 551 LYS A C 1 ATOM 4181 O O . LYS A 1 551 ? 24.785 -50.718 -17.091 1.00 157.63 ? 551 LYS A O 1 ATOM 4182 C CB . LYS A 1 551 ? 27.898 -51.555 -17.945 1.00 137.06 ? 551 LYS A CB 1 ATOM 4183 C CG . LYS A 1 551 ? 28.892 -51.701 -19.094 1.00 140.10 ? 551 LYS A CG 1 ATOM 4184 C CD . LYS A 1 551 ? 29.434 -53.130 -19.205 1.00 139.32 ? 551 LYS A CD 1 ATOM 4185 C CE . LYS A 1 551 ? 30.319 -53.324 -20.453 1.00 139.31 ? 551 LYS A CE 1 ATOM 4186 N NZ . LYS A 1 551 ? 29.640 -53.088 -21.778 1.00 129.33 ? 551 LYS A NZ 1 ATOM 4187 N N . ASN A 1 552 ? 26.440 -50.024 -15.708 1.00 158.46 ? 552 ASN A N 1 ATOM 4188 C CA . ASN A 1 552 ? 25.671 -50.105 -14.471 1.00 146.27 ? 552 ASN A CA 1 ATOM 4189 C C . ASN A 1 552 ? 25.457 -48.758 -13.795 1.00 146.89 ? 552 ASN A C 1 ATOM 4190 O O . ASN A 1 552 ? 25.670 -48.634 -12.594 1.00 146.43 ? 552 ASN A O 1 ATOM 4191 C CB . ASN A 1 552 ? 26.390 -51.021 -13.486 1.00 135.93 ? 552 ASN A CB 1 ATOM 4192 C CG . ASN A 1 552 ? 26.687 -52.377 -14.069 1.00 135.48 ? 552 ASN A CG 1 ATOM 4193 O OD1 . ASN A 1 552 ? 25.778 -53.174 -14.294 1.00 142.32 ? 552 ASN A OD1 1 ATOM 4194 N ND2 . ASN A 1 552 ? 27.965 -52.654 -14.313 1.00 129.46 ? 552 ASN A ND2 1 ATOM 4195 N N . SER A 1 553 ? 25.039 -47.749 -14.548 1.00 153.57 ? 553 SER A N 1 ATOM 4196 C CA . SER A 1 553 ? 24.785 -46.447 -13.948 1.00 158.47 ? 553 SER A CA 1 ATOM 4197 C C . SER A 1 553 ? 23.862 -46.606 -12.745 1.00 154.45 ? 553 SER A C 1 ATOM 4198 O O . SER A 1 553 ? 23.810 -45.743 -11.871 1.00 148.42 ? 553 SER A O 1 ATOM 4199 C CB . SER A 1 553 ? 24.163 -45.491 -14.963 1.00 166.76 ? 553 SER A CB 1 ATOM 4200 O OG . SER A 1 553 ? 23.810 -44.269 -14.339 1.00 168.28 ? 553 SER A OG 1 ATOM 4201 N N . GLN A 1 554 ? 23.132 -47.718 -12.724 1.00 156.97 ? 554 GLN A N 1 ATOM 4202 C CA . GLN A 1 554 ? 22.270 -48.086 -11.605 1.00 153.34 ? 554 GLN A CA 1 ATOM 4203 C C . GLN A 1 554 ? 23.072 -48.194 -10.317 1.00 155.88 ? 554 GLN A C 1 ATOM 4204 O O . GLN A 1 554 ? 22.752 -47.565 -9.304 1.00 155.37 ? 554 GLN A O 1 ATOM 4205 C CB . GLN A 1 554 ? 21.615 -49.438 -11.888 1.00 147.80 ? 554 GLN A CB 1 ATOM 4206 C CG . GLN A 1 554 ? 22.563 -50.451 -12.530 1.00 143.10 ? 554 GLN A CG 1 ATOM 4207 C CD . GLN A 1 554 ? 22.108 -51.885 -12.339 1.00 135.30 ? 554 GLN A CD 1 ATOM 4208 O OE1 . GLN A 1 554 ? 21.334 -52.185 -11.428 1.00 129.95 ? 554 GLN A OE1 1 ATOM 4209 N NE2 . GLN A 1 554 ? 22.594 -52.782 -13.194 1.00 129.93 ? 554 GLN A NE2 1 ATOM 4210 N N . LYS A 1 555 ? 24.112 -49.017 -10.372 1.00 156.39 ? 555 LYS A N 1 ATOM 4211 C CA . LYS A 1 555 ? 24.985 -49.261 -9.238 1.00 155.09 ? 555 LYS A CA 1 ATOM 4212 C C . LYS A 1 555 ? 25.918 -48.075 -9.013 1.00 153.93 ? 555 LYS A C 1 ATOM 4213 O O . LYS A 1 555 ? 27.106 -48.165 -9.316 1.00 160.46 ? 555 LYS A O 1 ATOM 4214 C CB . LYS A 1 555 ? 25.824 -50.519 -9.504 1.00 155.34 ? 555 LYS A CB 1 ATOM 4215 C CG . LYS A 1 555 ? 25.031 -51.824 -9.603 1.00 148.65 ? 555 LYS A CG 1 ATOM 4216 C CD . LYS A 1 555 ? 25.919 -52.988 -10.049 1.00 140.47 ? 555 LYS A CD 1 ATOM 4217 C CE . LYS A 1 555 ? 25.408 -54.324 -9.511 1.00 133.59 ? 555 LYS A CE 1 ATOM 4218 N NZ . LYS A 1 555 ? 23.940 -54.520 -9.702 1.00 129.04 ? 555 LYS A NZ 1 ATOM 4219 N N . GLU A 1 556 ? 25.397 -46.971 -8.481 1.00 148.74 ? 556 GLU A N 1 ATOM 4220 C CA . GLU A 1 556 ? 26.218 -45.772 -8.335 1.00 151.15 ? 556 GLU A CA 1 ATOM 4221 C C . GLU A 1 556 ? 25.406 -44.512 -8.032 1.00 163.78 ? 556 GLU A C 1 ATOM 4222 O O . GLU A 1 556 ? 24.503 -44.152 -8.795 1.00 162.52 ? 556 GLU A O 1 ATOM 4223 C CB . GLU A 1 556 ? 27.021 -45.552 -9.624 1.00 141.27 ? 556 GLU A CB 1 ATOM 4224 C CG . GLU A 1 556 ? 28.371 -44.869 -9.453 1.00 135.99 ? 556 GLU A CG 1 ATOM 4225 C CD . GLU A 1 556 ? 28.333 -43.387 -9.775 1.00 132.78 ? 556 GLU A CD 1 ATOM 4226 O OE1 . GLU A 1 556 ? 27.335 -42.725 -9.424 1.00 130.54 ? 556 GLU A OE1 1 ATOM 4227 O OE2 . GLU A 1 556 ? 29.305 -42.883 -10.379 1.00 131.44 ? 556 GLU A OE2 1 ATOM 4228 N N . GLN A 1 557 ? 25.727 -43.849 -6.917 1.00 167.87 ? 557 GLN A N 1 ATOM 4229 C CA . GLN A 1 557 ? 25.297 -42.459 -6.702 1.00 166.35 ? 557 GLN A CA 1 ATOM 4230 C C . GLN A 1 557 ? 26.496 -41.538 -6.437 1.00 151.81 ? 557 GLN A C 1 ATOM 4231 O O . GLN A 1 557 ? 27.452 -41.920 -5.758 1.00 135.97 ? 557 GLN A O 1 ATOM 4232 C CB . GLN A 1 557 ? 24.213 -42.326 -5.615 1.00 166.90 ? 557 GLN A CB 1 ATOM 4233 C CG . GLN A 1 557 ? 22.758 -42.391 -6.146 1.00 168.79 ? 557 GLN A CG 1 ATOM 4234 C CD . GLN A 1 557 ? 22.306 -41.139 -6.916 1.00 140.59 ? 557 GLN A CD 1 ATOM 4235 O OE1 . GLN A 1 557 ? 22.137 -41.176 -8.136 1.00 124.60 ? 557 GLN A OE1 1 ATOM 4236 N NE2 . GLN A 1 557 ? 22.095 -40.041 -6.199 1.00 128.91 ? 557 GLN A NE2 1 ATOM 4237 N N . GLY A 1 558 ? 26.431 -40.332 -6.998 1.00 152.88 ? 558 GLY A N 1 ATOM 4238 C CA . GLY A 1 558 ? 27.551 -39.408 -7.014 1.00 151.15 ? 558 GLY A CA 1 ATOM 4239 C C . GLY A 1 558 ? 28.256 -39.453 -8.359 1.00 153.50 ? 558 GLY A C 1 ATOM 4240 O O . GLY A 1 558 ? 28.630 -40.527 -8.831 1.00 157.62 ? 558 GLY A O 1 ATOM 4241 N N . SER A 1 559 ? 28.439 -38.294 -8.987 1.00 149.45 ? 559 SER A N 1 ATOM 4242 C CA . SER A 1 559 ? 29.068 -38.243 -10.309 1.00 144.48 ? 559 SER A CA 1 ATOM 4243 C C . SER A 1 559 ? 30.554 -37.865 -10.267 1.00 140.90 ? 559 SER A C 1 ATOM 4244 O O . SER A 1 559 ? 30.924 -36.778 -9.814 1.00 136.76 ? 559 SER A O 1 ATOM 4245 C CB . SER A 1 559 ? 28.290 -37.315 -11.252 1.00 141.82 ? 559 SER A CB 1 ATOM 4246 O OG . SER A 1 559 ? 27.856 -36.141 -10.588 1.00 138.56 ? 559 SER A OG 1 ATOM 4247 N N . ALA A 1 560 ? 31.395 -38.776 -10.751 1.00 140.23 ? 560 ALA A N 1 ATOM 4248 C CA . ALA A 1 560 ? 32.844 -38.588 -10.731 1.00 144.25 ? 560 ALA A CA 1 ATOM 4249 C C . ALA A 1 560 ? 33.286 -37.346 -11.505 1.00 165.04 ? 560 ALA A C 1 ATOM 4250 O O . ALA A 1 560 ? 32.960 -37.189 -12.680 1.00 169.16 ? 560 ALA A O 1 ATOM 4251 C CB . ALA A 1 560 ? 33.538 -39.823 -11.272 1.00 133.55 ? 560 ALA A CB 1 ATOM 4252 N N . LYS A 1 561 ? 34.037 -36.473 -10.835 1.00 177.62 ? 561 LYS A N 1 ATOM 4253 C CA . LYS A 1 561 ? 34.518 -35.223 -11.429 1.00 182.26 ? 561 LYS A CA 1 ATOM 4254 C C . LYS A 1 561 ? 35.926 -35.393 -12.004 1.00 188.36 ? 561 LYS A C 1 ATOM 4255 O O . LYS A 1 561 ? 36.861 -35.727 -11.278 1.00 190.49 ? 561 LYS A O 1 ATOM 4256 C CB . LYS A 1 561 ? 34.519 -34.110 -10.371 1.00 174.18 ? 561 LYS A CB 1 ATOM 4257 C CG . LYS A 1 561 ? 34.533 -32.684 -10.919 1.00 161.70 ? 561 LYS A CG 1 ATOM 4258 C CD . LYS A 1 561 ? 34.628 -31.669 -9.780 1.00 144.71 ? 561 LYS A CD 1 ATOM 4259 C CE . LYS A 1 561 ? 34.056 -30.312 -10.178 1.00 130.99 ? 561 LYS A CE 1 ATOM 4260 N NZ . LYS A 1 561 ? 32.567 -30.323 -10.343 1.00 113.58 ? 561 LYS A NZ 1 ATOM 4261 N N . CYS A 1 562 ? 36.075 -35.162 -13.306 1.00 190.62 ? 562 CYS A N 1 ATOM 4262 C CA . CYS A 1 562 ? 37.382 -35.269 -13.952 1.00 191.41 ? 562 CYS A CA 1 ATOM 4263 C C . CYS A 1 562 ? 38.320 -34.164 -13.479 1.00 184.76 ? 562 CYS A C 1 ATOM 4264 O O . CYS A 1 562 ? 37.923 -33.003 -13.362 1.00 182.05 ? 562 CYS A O 1 ATOM 4265 C CB . CYS A 1 562 ? 37.248 -35.222 -15.478 1.00 199.52 ? 562 CYS A CB 1 ATOM 4266 S SG . CYS A 1 562 ? 36.587 -36.726 -16.250 1.00 200.63 ? 562 CYS A SG 1 ATOM 4267 N N . SER A 1 563 ? 39.568 -34.533 -13.217 1.00 182.39 ? 563 SER A N 1 ATOM 4268 C CA . SER A 1 563 ? 40.551 -33.600 -12.681 1.00 182.87 ? 563 SER A CA 1 ATOM 4269 C C . SER A 1 563 ? 40.852 -32.449 -13.638 1.00 189.56 ? 563 SER A C 1 ATOM 4270 O O . SER A 1 563 ? 41.716 -32.566 -14.508 1.00 196.87 ? 563 SER A O 1 ATOM 4271 C CB . SER A 1 563 ? 41.843 -34.339 -12.328 1.00 181.89 ? 563 SER A CB 1 ATOM 4272 O OG . SER A 1 563 ? 42.280 -35.140 -13.411 1.00 184.19 ? 563 SER A OG 1 ATOM 4273 N N . GLY A 1 564 ? 40.135 -31.340 -13.474 1.00 185.72 ? 564 GLY A N 1 ATOM 4274 C CA . GLY A 1 564 ? 40.396 -30.141 -14.254 1.00 183.75 ? 564 GLY A CA 1 ATOM 4275 C C . GLY A 1 564 ? 39.370 -29.834 -15.330 1.00 175.82 ? 564 GLY A C 1 ATOM 4276 O O . GLY A 1 564 ? 39.264 -28.697 -15.790 1.00 174.45 ? 564 GLY A O 1 ATOM 4277 N N . SER A 1 565 ? 38.613 -30.848 -15.736 1.00 167.99 ? 565 SER A N 1 ATOM 4278 C CA . SER A 1 565 ? 37.623 -30.683 -16.791 1.00 157.88 ? 565 SER A CA 1 ATOM 4279 C C . SER A 1 565 ? 36.234 -30.488 -16.204 1.00 158.36 ? 565 SER A C 1 ATOM 4280 O O . SER A 1 565 ? 35.462 -29.655 -16.677 1.00 152.91 ? 565 SER A O 1 ATOM 4281 C CB . SER A 1 565 ? 37.625 -31.895 -17.721 1.00 145.49 ? 565 SER A CB 1 ATOM 4282 O OG . SER A 1 565 ? 38.922 -32.138 -18.240 1.00 141.72 ? 565 SER A OG 1 ATOM 4283 N N . GLY A 1 566 ? 35.926 -31.260 -15.165 1.00 164.06 ? 566 GLY A N 1 ATOM 4284 C CA . GLY A 1 566 ? 34.601 -31.251 -14.569 1.00 166.12 ? 566 GLY A CA 1 ATOM 4285 C C . GLY A 1 566 ? 33.671 -32.211 -15.290 1.00 166.80 ? 566 GLY A C 1 ATOM 4286 O O . GLY A 1 566 ? 32.573 -32.505 -14.817 1.00 164.40 ? 566 GLY A O 1 ATOM 4287 N N . LYS A 1 567 ? 34.124 -32.696 -16.444 1.00 165.70 ? 567 LYS A N 1 ATOM 4288 C CA . LYS A 1 567 ? 33.378 -33.652 -17.259 1.00 157.71 ? 567 LYS A CA 1 ATOM 4289 C C . LYS A 1 567 ? 33.212 -34.970 -16.508 1.00 155.29 ? 567 LYS A C 1 ATOM 4290 O O . LYS A 1 567 ? 34.176 -35.488 -15.955 1.00 158.92 ? 567 LYS A O 1 ATOM 4291 C CB . LYS A 1 567 ? 34.130 -33.890 -18.575 1.00 152.77 ? 567 LYS A CB 1 ATOM 4292 C CG . LYS A 1 567 ? 33.385 -34.712 -19.629 1.00 145.46 ? 567 LYS A CG 1 ATOM 4293 C CD . LYS A 1 567 ? 34.196 -34.803 -20.932 1.00 140.02 ? 567 LYS A CD 1 ATOM 4294 C CE . LYS A 1 567 ? 33.331 -35.220 -22.133 1.00 125.50 ? 567 LYS A CE 1 ATOM 4295 N NZ . LYS A 1 567 ? 34.018 -35.009 -23.443 1.00 106.93 ? 567 LYS A NZ 1 ATOM 4296 N N . PRO A 1 568 ? 31.984 -35.516 -16.480 1.00 148.99 ? 568 PRO A N 1 ATOM 4297 C CA . PRO A 1 568 ? 31.734 -36.810 -15.824 1.00 151.45 ? 568 PRO A CA 1 ATOM 4298 C C . PRO A 1 568 ? 32.572 -37.952 -16.420 1.00 164.66 ? 568 PRO A C 1 ATOM 4299 O O . PRO A 1 568 ? 32.900 -37.911 -17.605 1.00 172.41 ? 568 PRO A O 1 ATOM 4300 C CB . PRO A 1 568 ? 30.243 -37.052 -16.086 1.00 140.75 ? 568 PRO A CB 1 ATOM 4301 C CG . PRO A 1 568 ? 29.671 -35.692 -16.295 1.00 136.88 ? 568 PRO A CG 1 ATOM 4302 C CD . PRO A 1 568 ? 30.744 -34.898 -16.979 1.00 140.96 ? 568 PRO A CD 1 ATOM 4303 N N . VAL A 1 569 ? 32.910 -38.951 -15.605 1.00 165.44 ? 569 VAL A N 1 ATOM 4304 C CA . VAL A 1 569 ? 33.714 -40.093 -16.054 1.00 165.52 ? 569 VAL A CA 1 ATOM 4305 C C . VAL A 1 569 ? 32.863 -41.108 -16.822 1.00 163.64 ? 569 VAL A C 1 ATOM 4306 O O . VAL A 1 569 ? 33.385 -42.034 -17.450 1.00 157.67 ? 569 VAL A O 1 ATOM 4307 C CB . VAL A 1 569 ? 34.430 -40.789 -14.868 1.00 188.14 ? 569 VAL A CB 1 ATOM 4308 C CG1 . VAL A 1 569 ? 35.176 -42.027 -15.336 1.00 188.95 ? 569 VAL A CG1 1 ATOM 4309 C CG2 . VAL A 1 569 ? 35.389 -39.825 -14.186 1.00 188.54 ? 569 VAL A CG2 1 ATOM 4310 N N . ARG A 1 570 ? 31.548 -40.919 -16.769 1.00 167.64 ? 570 ARG A N 1 ATOM 4311 C CA . ARG A 1 570 ? 30.616 -41.746 -17.529 1.00 169.25 ? 570 ARG A CA 1 ATOM 4312 C C . ARG A 1 570 ? 30.561 -41.277 -18.985 1.00 164.16 ? 570 ARG A C 1 ATOM 4313 O O . ARG A 1 570 ? 29.747 -41.758 -19.774 1.00 154.27 ? 570 ARG A O 1 ATOM 4314 C CB . ARG A 1 570 ? 29.217 -41.707 -16.895 1.00 170.23 ? 570 ARG A CB 1 ATOM 4315 C CG . ARG A 1 570 ? 29.184 -42.163 -15.438 1.00 173.08 ? 570 ARG A CG 1 ATOM 4316 C CD . ARG A 1 570 ? 27.763 -42.390 -14.926 1.00 173.75 ? 570 ARG A CD 1 ATOM 4317 N NE . ARG A 1 570 ? 27.061 -41.145 -14.620 1.00 170.52 ? 570 ARG A NE 1 ATOM 4318 C CZ . ARG A 1 570 ? 25.939 -41.079 -13.907 1.00 164.20 ? 570 ARG A CZ 1 ATOM 4319 N NH1 . ARG A 1 570 ? 25.396 -42.188 -13.422 1.00 162.20 ? 570 ARG A NH1 1 ATOM 4320 N NH2 . ARG A 1 570 ? 25.363 -39.905 -13.674 1.00 158.37 ? 570 ARG A NH2 1 ATOM 4321 N N . SER A 1 571 ? 31.444 -40.342 -19.329 1.00 168.90 ? 571 SER A N 1 ATOM 4322 C CA . SER A 1 571 ? 31.468 -39.737 -20.660 1.00 171.63 ? 571 SER A CA 1 ATOM 4323 C C . SER A 1 571 ? 32.536 -40.336 -21.584 1.00 183.11 ? 571 SER A C 1 ATOM 4324 O O . SER A 1 571 ? 33.172 -41.341 -21.254 1.00 174.41 ? 571 SER A O 1 ATOM 4325 C CB . SER A 1 571 ? 31.645 -38.215 -20.560 1.00 157.86 ? 571 SER A CB 1 ATOM 4326 O OG . SER A 1 571 ? 30.532 -37.598 -19.932 1.00 140.12 ? 571 SER A OG 1 ATOM 4327 N N . ILE A 1 572 ? 32.719 -39.687 -22.734 1.00 201.77 ? 572 ILE A N 1 ATOM 4328 C CA . ILE A 1 572 ? 33.557 -40.177 -23.838 1.00 220.90 ? 572 ILE A CA 1 ATOM 4329 C C . ILE A 1 572 ? 34.447 -41.388 -23.523 1.00 229.82 ? 572 ILE A C 1 ATOM 4330 O O . ILE A 1 572 ? 35.172 -41.411 -22.524 1.00 226.08 ? 572 ILE A O 1 ATOM 4331 C CB . ILE A 1 572 ? 34.418 -39.039 -24.465 1.00 158.80 ? 572 ILE A CB 1 ATOM 4332 C CG1 . ILE A 1 572 ? 33.528 -37.970 -25.120 1.00 155.84 ? 572 ILE A CG1 1 ATOM 4333 C CG2 . ILE A 1 572 ? 35.407 -39.608 -25.473 1.00 159.28 ? 572 ILE A CG2 1 ATOM 4334 C CD1 . ILE A 1 572 ? 32.899 -38.383 -26.445 1.00 143.65 ? 572 ILE A CD1 1 ATOM 4335 N N . ILE A 1 573 ? 34.375 -42.390 -24.397 1.00 237.10 ? 573 ILE A N 1 ATOM 4336 C CA . ILE A 1 573 ? 35.230 -43.571 -24.318 1.00 237.05 ? 573 ILE A CA 1 ATOM 4337 C C . ILE A 1 573 ? 36.328 -43.508 -25.392 1.00 240.29 ? 573 ILE A C 1 ATOM 4338 O O . ILE A 1 573 ? 36.350 -42.580 -26.201 1.00 239.95 ? 573 ILE A O 1 ATOM 4339 C CB . ILE A 1 573 ? 34.403 -44.871 -24.419 1.00 230.27 ? 573 ILE A CB 1 ATOM 4340 C CG1 . ILE A 1 573 ? 33.187 -44.668 -25.329 1.00 222.85 ? 573 ILE A CG1 1 ATOM 4341 C CG2 . ILE A 1 573 ? 33.925 -45.298 -23.037 1.00 222.92 ? 573 ILE A CG2 1 ATOM 4342 C CD1 . ILE A 1 573 ? 33.533 -44.370 -26.766 1.00 221.33 ? 573 ILE A CD1 1 ATOM 4343 N N . CYS A 1 574 ? 37.235 -44.484 -25.400 1.00 241.06 ? 574 CYS A N 1 ATOM 4344 C CA . CYS A 1 574 ? 38.442 -44.391 -26.229 1.00 240.55 ? 574 CYS A CA 1 ATOM 4345 C C . CYS A 1 574 ? 38.715 -45.634 -27.087 1.00 236.31 ? 574 CYS A C 1 ATOM 4346 O O . CYS A 1 574 ? 38.573 -46.761 -26.612 1.00 231.54 ? 574 CYS A O 1 ATOM 4347 C CB . CYS A 1 574 ? 39.652 -44.085 -25.340 1.00 243.49 ? 574 CYS A CB 1 ATOM 4348 S SG . CYS A 1 574 ? 39.317 -42.852 -24.047 1.00 244.37 ? 574 CYS A SG 1 ATOM 4349 N N . PRO A 1 575 ? 39.122 -45.420 -28.355 1.00 239.69 ? 575 PRO A N 1 ATOM 4350 C CA . PRO A 1 575 ? 39.359 -46.435 -29.399 1.00 240.39 ? 575 PRO A CA 1 ATOM 4351 C C . PRO A 1 575 ? 40.481 -47.432 -29.090 1.00 236.03 ? 575 PRO A C 1 ATOM 4352 O O . PRO A 1 575 ? 40.778 -48.311 -29.905 1.00 229.59 ? 575 PRO A O 1 ATOM 4353 C CB . PRO A 1 575 ? 39.747 -45.587 -30.622 1.00 242.20 ? 575 PRO A CB 1 ATOM 4354 C CG . PRO A 1 575 ? 40.227 -44.295 -30.039 1.00 242.77 ? 575 PRO A CG 1 ATOM 4355 C CD . PRO A 1 575 ? 39.282 -44.063 -28.903 1.00 240.31 ? 575 PRO A CD 1 ATOM 4356 N N . GLU B 2 33 ? 79.703 -39.687 22.180 1.00 107.10 ? 33 GLU B N 1 ATOM 4357 C CA . GLU B 2 33 ? 80.208 -40.067 23.498 1.00 109.50 ? 33 GLU B CA 1 ATOM 4358 C C . GLU B 2 33 ? 80.993 -41.373 23.444 1.00 119.21 ? 33 GLU B C 1 ATOM 4359 O O . GLU B 2 33 ? 81.347 -41.931 24.490 1.00 128.31 ? 33 GLU B O 1 ATOM 4360 C CB . GLU B 2 33 ? 79.052 -40.222 24.481 1.00 99.55 ? 33 GLU B CB 1 ATOM 4361 C CG . GLU B 2 33 ? 78.045 -41.257 24.034 1.00 97.81 ? 33 GLU B CG 1 ATOM 4362 C CD . GLU B 2 33 ? 76.804 -41.293 24.900 1.00 105.60 ? 33 GLU B CD 1 ATOM 4363 O OE1 . GLU B 2 33 ? 76.933 -41.354 26.150 1.00 105.57 ? 33 GLU B OE1 1 ATOM 4364 O OE2 . GLU B 2 33 ? 75.696 -41.278 24.317 1.00 103.22 ? 33 GLU B OE2 1 ATOM 4365 N N . SER B 2 34 ? 81.246 -41.858 22.227 1.00 108.71 ? 34 SER B N 1 ATOM 4366 C CA . SER B 2 34 ? 81.995 -43.099 21.998 1.00 94.24 ? 34 SER B CA 1 ATOM 4367 C C . SER B 2 34 ? 81.367 -44.305 22.721 1.00 92.42 ? 34 SER B C 1 ATOM 4368 O O . SER B 2 34 ? 81.952 -44.863 23.651 1.00 92.52 ? 34 SER B O 1 ATOM 4369 C CB . SER B 2 34 ? 83.466 -42.910 22.396 1.00 86.40 ? 34 SER B CB 1 ATOM 4370 O OG . SER B 2 34 ? 84.297 -43.940 21.891 1.00 78.75 ? 34 SER B OG 1 ATOM 4371 N N . MET B 2 35 ? 80.178 -44.706 22.275 1.00 85.02 ? 35 MET B N 1 ATOM 4372 C CA . MET B 2 35 ? 79.403 -45.764 22.929 1.00 66.98 ? 35 MET B CA 1 ATOM 4373 C C . MET B 2 35 ? 79.231 -47.018 22.061 1.00 73.20 ? 35 MET B C 1 ATOM 4374 O O . MET B 2 35 ? 79.285 -46.955 20.832 1.00 74.90 ? 35 MET B O 1 ATOM 4375 C CB . MET B 2 35 ? 78.024 -45.225 23.332 1.00 46.21 ? 35 MET B CB 1 ATOM 4376 C CG . MET B 2 35 ? 76.947 -46.286 23.592 1.00 38.21 ? 35 MET B CG 1 ATOM 4377 S SD . MET B 2 35 ? 76.717 -46.736 25.327 1.00 92.52 ? 35 MET B SD 1 ATOM 4378 C CE . MET B 2 35 ? 75.696 -45.377 25.897 1.00 148.68 ? 35 MET B CE 1 ATOM 4379 N N . VAL B 2 36 ? 79.041 -48.154 22.728 1.00 65.84 ? 36 VAL B N 1 ATOM 4380 C CA . VAL B 2 36 ? 78.678 -49.410 22.094 1.00 64.21 ? 36 VAL B CA 1 ATOM 4381 C C . VAL B 2 36 ? 77.569 -50.034 22.933 1.00 73.64 ? 36 VAL B C 1 ATOM 4382 O O . VAL B 2 36 ? 77.761 -50.350 24.108 1.00 73.86 ? 36 VAL B O 1 ATOM 4383 C CB . VAL B 2 36 ? 79.863 -50.397 22.044 1.00 62.79 ? 36 VAL B CB 1 ATOM 4384 C CG1 . VAL B 2 36 ? 79.426 -51.748 21.428 1.00 43.48 ? 36 VAL B CG1 1 ATOM 4385 C CG2 . VAL B 2 36 ? 81.055 -49.777 21.303 1.00 64.32 ? 36 VAL B CG2 1 ATOM 4386 N N . ASP B 2 37 ? 76.400 -50.205 22.335 1.00 73.80 ? 37 ASP B N 1 ATOM 4387 C CA . ASP B 2 37 ? 75.274 -50.766 23.057 1.00 63.73 ? 37 ASP B CA 1 ATOM 4388 C C . ASP B 2 37 ? 75.049 -52.214 22.661 1.00 70.13 ? 37 ASP B C 1 ATOM 4389 O O . ASP B 2 37 ? 74.633 -52.501 21.545 1.00 79.53 ? 37 ASP B O 1 ATOM 4390 C CB . ASP B 2 37 ? 74.029 -49.948 22.770 1.00 62.66 ? 37 ASP B CB 1 ATOM 4391 C CG . ASP B 2 37 ? 72.826 -50.447 23.515 1.00 71.20 ? 37 ASP B CG 1 ATOM 4392 O OD1 . ASP B 2 37 ? 71.806 -49.714 23.533 1.00 69.07 ? 37 ASP B OD1 1 ATOM 4393 O OD2 . ASP B 2 37 ? 72.905 -51.567 24.077 1.00 69.57 ? 37 ASP B OD2 1 ATOM 4394 N N . TYR B 2 38 ? 75.324 -53.124 23.583 1.00 74.30 ? 38 TYR B N 1 ATOM 4395 C CA . TYR B 2 38 ? 75.136 -54.547 23.334 1.00 71.78 ? 38 TYR B CA 1 ATOM 4396 C C . TYR B 2 38 ? 74.100 -55.155 24.270 1.00 66.89 ? 38 TYR B C 1 ATOM 4397 O O . TYR B 2 38 ? 74.267 -56.282 24.731 1.00 70.92 ? 38 TYR B O 1 ATOM 4398 C CB . TYR B 2 38 ? 76.449 -55.306 23.508 1.00 69.46 ? 38 TYR B CB 1 ATOM 4399 C CG . TYR B 2 38 ? 77.351 -55.313 22.296 1.00 68.11 ? 38 TYR B CG 1 ATOM 4400 C CD1 . TYR B 2 38 ? 76.855 -55.026 21.036 1.00 62.02 ? 38 TYR B CD1 1 ATOM 4401 C CD2 . TYR B 2 38 ? 78.699 -55.650 22.415 1.00 62.67 ? 38 TYR B CD2 1 ATOM 4402 C CE1 . TYR B 2 38 ? 77.679 -55.047 19.933 1.00 63.91 ? 38 TYR B CE1 1 ATOM 4403 C CE2 . TYR B 2 38 ? 79.526 -55.672 21.325 1.00 61.49 ? 38 TYR B CE2 1 ATOM 4404 C CZ . TYR B 2 38 ? 79.014 -55.372 20.080 1.00 68.10 ? 38 TYR B CZ 1 ATOM 4405 O OH . TYR B 2 38 ? 79.841 -55.400 18.976 1.00 73.22 ? 38 TYR B OH 1 ATOM 4406 N N . SER B 2 39 ? 73.037 -54.419 24.568 1.00 49.91 ? 39 SER B N 1 ATOM 4407 C CA . SER B 2 39 ? 71.989 -54.991 25.401 1.00 62.52 ? 39 SER B CA 1 ATOM 4408 C C . SER B 2 39 ? 71.083 -55.927 24.597 1.00 71.58 ? 39 SER B C 1 ATOM 4409 O O . SER B 2 39 ? 71.011 -55.828 23.371 1.00 83.61 ? 39 SER B O 1 ATOM 4410 C CB . SER B 2 39 ? 71.177 -53.891 26.073 1.00 59.80 ? 39 SER B CB 1 ATOM 4411 O OG . SER B 2 39 ? 70.816 -52.908 25.136 1.00 56.63 ? 39 SER B OG 1 ATOM 4412 N N . ASN B 2 40 ? 70.410 -56.843 25.289 1.00 62.24 ? 40 ASN B N 1 ATOM 4413 C CA . ASN B 2 40 ? 69.503 -57.802 24.647 1.00 76.07 ? 40 ASN B CA 1 ATOM 4414 C C . ASN B 2 40 ? 70.146 -58.656 23.562 1.00 84.56 ? 40 ASN B C 1 ATOM 4415 O O . ASN B 2 40 ? 69.457 -59.388 22.855 1.00 87.27 ? 40 ASN B O 1 ATOM 4416 C CB . ASN B 2 40 ? 68.281 -57.100 24.073 1.00 76.35 ? 40 ASN B CB 1 ATOM 4417 C CG . ASN B 2 40 ? 67.503 -56.358 25.124 1.00 88.12 ? 40 ASN B CG 1 ATOM 4418 O OD1 . ASN B 2 40 ? 66.891 -56.965 25.999 1.00 81.27 ? 40 ASN B OD1 1 ATOM 4419 N ND2 . ASN B 2 40 ? 67.522 -55.029 25.048 1.00 99.09 ? 40 ASN B ND2 1 ATOM 4420 N N . ARG B 2 41 ? 71.463 -58.557 23.439 1.00 80.96 ? 41 ARG B N 1 ATOM 4421 C CA . ARG B 2 41 ? 72.213 -59.366 22.496 1.00 76.40 ? 41 ARG B CA 1 ATOM 4422 C C . ARG B 2 41 ? 72.422 -60.815 22.999 1.00 86.44 ? 41 ARG B C 1 ATOM 4423 O O . ARG B 2 41 ? 73.276 -61.532 22.477 1.00 93.31 ? 41 ARG B O 1 ATOM 4424 C CB . ARG B 2 41 ? 73.561 -58.689 22.179 1.00 76.27 ? 41 ARG B CB 1 ATOM 4425 C CG . ARG B 2 41 ? 73.546 -57.674 21.019 1.00 78.05 ? 41 ARG B CG 1 ATOM 4426 C CD . ARG B 2 41 ? 74.193 -58.221 19.705 1.00 99.49 ? 41 ARG B CD 1 ATOM 4427 N NE . ARG B 2 41 ? 75.653 -58.392 19.796 1.00 105.40 ? 41 ARG B NE 1 ATOM 4428 C CZ . ARG B 2 41 ? 76.316 -59.514 19.490 1.00 99.79 ? 41 ARG B CZ 1 ATOM 4429 N NH1 . ARG B 2 41 ? 75.644 -60.577 19.048 1.00 106.07 ? 41 ARG B NH1 1 ATOM 4430 N NH2 . ARG B 2 41 ? 77.653 -59.574 19.612 1.00 68.40 ? 41 ARG B NH2 1 ATOM 4431 N N . ASN B 2 42 ? 71.652 -61.242 24.005 1.00 85.96 ? 42 ASN B N 1 ATOM 4432 C CA . ASN B 2 42 ? 71.734 -62.618 24.536 1.00 79.11 ? 42 ASN B CA 1 ATOM 4433 C C . ASN B 2 42 ? 73.120 -63.076 25.013 1.00 74.66 ? 42 ASN B C 1 ATOM 4434 O O . ASN B 2 42 ? 73.407 -64.276 25.068 1.00 58.52 ? 42 ASN B O 1 ATOM 4435 C CB . ASN B 2 42 ? 71.208 -63.613 23.501 1.00 76.00 ? 42 ASN B CB 1 ATOM 4436 C CG . ASN B 2 42 ? 69.842 -64.157 23.856 1.00 91.93 ? 42 ASN B CG 1 ATOM 4437 O OD1 . ASN B 2 42 ? 69.691 -64.856 24.858 1.00 98.11 ? 42 ASN B OD1 1 ATOM 4438 N ND2 . ASN B 2 42 ? 68.837 -63.851 23.030 1.00 92.66 ? 42 ASN B ND2 1 ATOM 4439 N N . LEU B 2 43 ? 73.964 -62.114 25.375 1.00 78.24 ? 43 LEU B N 1 ATOM 4440 C CA . LEU B 2 43 ? 75.392 -62.350 25.559 1.00 78.28 ? 43 LEU B CA 1 ATOM 4441 C C . LEU B 2 43 ? 75.750 -63.172 26.790 1.00 87.98 ? 43 LEU B C 1 ATOM 4442 O O . LEU B 2 43 ? 74.908 -63.414 27.650 1.00 97.52 ? 43 LEU B O 1 ATOM 4443 C CB . LEU B 2 43 ? 76.124 -61.014 25.589 1.00 76.67 ? 43 LEU B CB 1 ATOM 4444 C CG . LEU B 2 43 ? 76.477 -60.449 24.218 1.00 78.93 ? 43 LEU B CG 1 ATOM 4445 C CD1 . LEU B 2 43 ? 76.386 -58.944 24.243 1.00 81.23 ? 43 LEU B CD1 1 ATOM 4446 C CD2 . LEU B 2 43 ? 77.870 -60.915 23.809 1.00 83.67 ? 43 LEU B CD2 1 ATOM 4447 N N . THR B 2 44 ? 77.012 -63.587 26.876 1.00 87.17 ? 44 THR B N 1 ATOM 4448 C CA . THR B 2 44 ? 77.462 -64.467 27.957 1.00 86.12 ? 44 THR B CA 1 ATOM 4449 C C . THR B 2 44 ? 78.823 -64.079 28.524 1.00 91.36 ? 44 THR B C 1 ATOM 4450 O O . THR B 2 44 ? 79.094 -64.270 29.706 1.00 93.14 ? 44 THR B O 1 ATOM 4451 C CB . THR B 2 44 ? 77.476 -65.937 27.498 1.00 78.02 ? 44 THR B CB 1 ATOM 4452 O OG1 . THR B 2 44 ? 76.338 -66.606 28.053 1.00 71.54 ? 44 THR B OG1 1 ATOM 4453 C CG2 . THR B 2 44 ? 78.757 -66.648 27.932 1.00 75.79 ? 44 THR B CG2 1 ATOM 4454 N N . HIS B 2 45 ? 79.667 -63.523 27.669 1.00 97.51 ? 45 HIS B N 1 ATOM 4455 C CA . HIS B 2 45 ? 80.998 -63.087 28.047 1.00 102.49 ? 45 HIS B CA 1 ATOM 4456 C C . HIS B 2 45 ? 81.115 -61.652 27.566 1.00 98.81 ? 45 HIS B C 1 ATOM 4457 O O . HIS B 2 45 ? 80.212 -61.152 26.896 1.00 97.22 ? 45 HIS B O 1 ATOM 4458 C CB . HIS B 2 45 ? 82.041 -63.971 27.360 1.00 118.53 ? 45 HIS B CB 1 ATOM 4459 C CG . HIS B 2 45 ? 81.869 -64.070 25.870 1.00 135.62 ? 45 HIS B CG 1 ATOM 4460 N ND1 . HIS B 2 45 ? 80.658 -64.361 25.273 1.00 139.94 ? 45 HIS B ND1 1 ATOM 4461 C CD2 . HIS B 2 45 ? 82.759 -63.929 24.857 1.00 138.45 ? 45 HIS B CD2 1 ATOM 4462 C CE1 . HIS B 2 45 ? 80.808 -64.383 23.960 1.00 138.34 ? 45 HIS B CE1 1 ATOM 4463 N NE2 . HIS B 2 45 ? 82.074 -64.126 23.681 1.00 139.61 ? 45 HIS B NE2 1 ATOM 4464 N N . VAL B 2 46 ? 82.214 -60.986 27.889 1.00 99.49 ? 46 VAL B N 1 ATOM 4465 C CA . VAL B 2 46 ? 82.401 -59.611 27.436 1.00 102.29 ? 46 VAL B CA 1 ATOM 4466 C C . VAL B 2 46 ? 83.144 -59.543 26.100 1.00 94.38 ? 46 VAL B C 1 ATOM 4467 O O . VAL B 2 46 ? 84.365 -59.687 26.067 1.00 101.90 ? 46 VAL B O 1 ATOM 4468 C CB . VAL B 2 46 ? 83.164 -58.783 28.477 1.00 110.53 ? 46 VAL B CB 1 ATOM 4469 C CG1 . VAL B 2 46 ? 83.071 -57.303 28.144 1.00 110.43 ? 46 VAL B CG1 1 ATOM 4470 C CG2 . VAL B 2 46 ? 82.613 -59.060 29.860 1.00 108.74 ? 46 VAL B CG2 1 ATOM 4471 N N . PRO B 2 47 ? 82.406 -59.290 25.001 1.00 79.34 ? 47 PRO B N 1 ATOM 4472 C CA . PRO B 2 47 ? 82.887 -59.309 23.611 1.00 63.92 ? 47 PRO B CA 1 ATOM 4473 C C . PRO B 2 47 ? 84.335 -58.871 23.481 1.00 64.18 ? 47 PRO B C 1 ATOM 4474 O O . PRO B 2 47 ? 84.612 -57.681 23.518 1.00 70.70 ? 47 PRO B O 1 ATOM 4475 C CB . PRO B 2 47 ? 81.983 -58.289 22.930 1.00 48.68 ? 47 PRO B CB 1 ATOM 4476 C CG . PRO B 2 47 ? 80.707 -58.401 23.648 1.00 55.66 ? 47 PRO B CG 1 ATOM 4477 C CD . PRO B 2 47 ? 81.028 -58.776 25.084 1.00 69.09 ? 47 PRO B CD 1 ATOM 4478 N N . LYS B 2 48 ? 85.239 -59.831 23.326 1.00 70.51 ? 48 LYS B N 1 ATOM 4479 C CA . LYS B 2 48 ? 86.687 -59.574 23.294 1.00 87.58 ? 48 LYS B CA 1 ATOM 4480 C C . LYS B 2 48 ? 87.148 -58.797 22.036 1.00 86.51 ? 48 LYS B C 1 ATOM 4481 O O . LYS B 2 48 ? 88.327 -58.413 21.912 1.00 69.05 ? 48 LYS B O 1 ATOM 4482 C CB . LYS B 2 48 ? 87.462 -60.901 23.466 1.00 99.37 ? 48 LYS B CB 1 ATOM 4483 C CG . LYS B 2 48 ? 87.074 -62.029 22.476 1.00 113.87 ? 48 LYS B CG 1 ATOM 4484 C CD . LYS B 2 48 ? 85.601 -62.479 22.591 1.00 93.60 ? 48 LYS B CD 1 ATOM 4485 C CE . LYS B 2 48 ? 85.041 -62.918 21.231 1.00 78.41 ? 48 LYS B CE 1 ATOM 4486 N NZ . LYS B 2 48 ? 83.588 -62.606 21.066 1.00 65.87 ? 48 LYS B NZ 1 ATOM 4487 N N . ASP B 2 49 ? 86.190 -58.552 21.136 1.00 85.42 ? 49 ASP B N 1 ATOM 4488 C CA . ASP B 2 49 ? 86.422 -57.918 19.838 1.00 69.63 ? 49 ASP B CA 1 ATOM 4489 C C . ASP B 2 49 ? 86.280 -56.388 19.844 1.00 75.58 ? 49 ASP B C 1 ATOM 4490 O O . ASP B 2 49 ? 86.829 -55.716 18.972 1.00 80.31 ? 49 ASP B O 1 ATOM 4491 C CB . ASP B 2 49 ? 85.506 -58.541 18.759 1.00 62.27 ? 49 ASP B CB 1 ATOM 4492 C CG . ASP B 2 49 ? 83.992 -58.294 19.013 1.00 105.82 ? 49 ASP B CG 1 ATOM 4493 O OD1 . ASP B 2 49 ? 83.585 -57.163 19.379 1.00 103.97 ? 49 ASP B OD1 1 ATOM 4494 O OD2 . ASP B 2 49 ? 83.193 -59.237 18.812 1.00 96.84 ? 49 ASP B OD2 1 ATOM 4495 N N . LEU B 2 50 ? 85.545 -55.846 20.816 1.00 67.49 ? 50 LEU B N 1 ATOM 4496 C CA . LEU B 2 50 ? 85.278 -54.404 20.897 1.00 60.25 ? 50 LEU B CA 1 ATOM 4497 C C . LEU B 2 50 ? 86.488 -53.515 20.601 1.00 74.44 ? 50 LEU B C 1 ATOM 4498 O O . LEU B 2 50 ? 87.651 -53.884 20.866 1.00 67.97 ? 50 LEU B O 1 ATOM 4499 C CB . LEU B 2 50 ? 84.715 -54.031 22.269 1.00 56.21 ? 50 LEU B CB 1 ATOM 4500 C CG . LEU B 2 50 ? 83.305 -54.506 22.641 1.00 61.59 ? 50 LEU B CG 1 ATOM 4501 C CD1 . LEU B 2 50 ? 83.262 -54.846 24.110 1.00 46.17 ? 50 LEU B CD1 1 ATOM 4502 C CD2 . LEU B 2 50 ? 82.201 -53.503 22.280 1.00 51.34 ? 50 LEU B CD2 1 ATOM 4503 N N . PRO B 2 51 ? 86.209 -52.333 20.033 1.00 74.95 ? 51 PRO B N 1 ATOM 4504 C CA . PRO B 2 51 ? 87.200 -51.288 19.754 1.00 76.83 ? 51 PRO B CA 1 ATOM 4505 C C . PRO B 2 51 ? 87.904 -50.876 21.045 1.00 78.43 ? 51 PRO B C 1 ATOM 4506 O O . PRO B 2 51 ? 87.254 -50.488 22.019 1.00 64.95 ? 51 PRO B O 1 ATOM 4507 C CB . PRO B 2 51 ? 86.345 -50.141 19.206 1.00 71.57 ? 51 PRO B CB 1 ATOM 4508 C CG . PRO B 2 51 ? 85.134 -50.808 18.635 1.00 64.38 ? 51 PRO B CG 1 ATOM 4509 C CD . PRO B 2 51 ? 84.872 -51.987 19.522 1.00 60.90 ? 51 PRO B CD 1 ATOM 4510 N N . PRO B 2 52 ? 89.235 -50.973 21.063 1.00 77.84 ? 52 PRO B N 1 ATOM 4511 C CA . PRO B 2 52 ? 90.040 -50.773 22.274 1.00 77.67 ? 52 PRO B CA 1 ATOM 4512 C C . PRO B 2 52 ? 89.771 -49.459 23.013 1.00 87.70 ? 52 PRO B C 1 ATOM 4513 O O . PRO B 2 52 ? 89.739 -49.453 24.244 1.00 103.97 ? 52 PRO B O 1 ATOM 4514 C CB . PRO B 2 52 ? 91.469 -50.801 21.742 1.00 74.61 ? 52 PRO B CB 1 ATOM 4515 C CG . PRO B 2 52 ? 91.396 -51.659 20.541 1.00 73.03 ? 52 PRO B CG 1 ATOM 4516 C CD . PRO B 2 52 ? 90.058 -51.368 19.914 1.00 73.83 ? 52 PRO B CD 1 ATOM 4517 N N . ARG B 2 53 ? 89.574 -48.367 22.281 1.00 78.13 ? 53 ARG B N 1 ATOM 4518 C CA . ARG B 2 53 ? 89.404 -47.059 22.909 1.00 67.54 ? 53 ARG B CA 1 ATOM 4519 C C . ARG B 2 53 ? 87.944 -46.703 23.199 1.00 65.46 ? 53 ARG B C 1 ATOM 4520 O O . ARG B 2 53 ? 87.620 -45.521 23.345 1.00 63.88 ? 53 ARG B O 1 ATOM 4521 C CB . ARG B 2 53 ? 90.046 -45.955 22.054 1.00 66.10 ? 53 ARG B CB 1 ATOM 4522 C CG . ARG B 2 53 ? 91.580 -45.825 22.147 1.00 73.55 ? 53 ARG B CG 1 ATOM 4523 C CD . ARG B 2 53 ? 91.969 -44.345 22.073 1.00 95.20 ? 53 ARG B CD 1 ATOM 4524 N NE . ARG B 2 53 ? 91.005 -43.591 21.259 1.00 114.37 ? 53 ARG B NE 1 ATOM 4525 C CZ . ARG B 2 53 ? 90.641 -42.326 21.477 1.00 114.76 ? 53 ARG B CZ 1 ATOM 4526 N NH1 . ARG B 2 53 ? 91.153 -41.652 22.502 1.00 122.08 ? 53 ARG B NH1 1 ATOM 4527 N NH2 . ARG B 2 53 ? 89.755 -41.740 20.673 1.00 93.83 ? 53 ARG B NH2 1 ATOM 4528 N N . THR B 2 54 ? 87.072 -47.716 23.267 1.00 70.16 ? 54 THR B N 1 ATOM 4529 C CA . THR B 2 54 ? 85.647 -47.512 23.573 1.00 70.96 ? 54 THR B CA 1 ATOM 4530 C C . THR B 2 54 ? 85.519 -46.848 24.923 1.00 78.80 ? 54 THR B C 1 ATOM 4531 O O . THR B 2 54 ? 86.340 -47.089 25.802 1.00 91.07 ? 54 THR B O 1 ATOM 4532 C CB . THR B 2 54 ? 84.860 -48.839 23.680 1.00 64.82 ? 54 THR B CB 1 ATOM 4533 O OG1 . THR B 2 54 ? 85.202 -49.703 22.600 1.00 74.60 ? 54 THR B OG1 1 ATOM 4534 C CG2 . THR B 2 54 ? 83.367 -48.586 23.653 1.00 60.19 ? 54 THR B CG2 1 ATOM 4535 N N . LYS B 2 55 ? 84.479 -46.042 25.109 1.00 77.79 ? 55 LYS B N 1 ATOM 4536 C CA . LYS B 2 55 ? 84.341 -45.296 26.356 1.00 79.57 ? 55 LYS B CA 1 ATOM 4537 C C . LYS B 2 55 ? 83.097 -45.639 27.169 1.00 78.62 ? 55 LYS B C 1 ATOM 4538 O O . LYS B 2 55 ? 83.178 -45.744 28.385 1.00 95.31 ? 55 LYS B O 1 ATOM 4539 C CB . LYS B 2 55 ? 84.469 -43.788 26.112 1.00 75.71 ? 55 LYS B CB 1 ATOM 4540 C CG . LYS B 2 55 ? 85.867 -43.414 25.644 1.00 74.40 ? 55 LYS B CG 1 ATOM 4541 C CD . LYS B 2 55 ? 86.070 -41.925 25.455 1.00 72.44 ? 55 LYS B CD 1 ATOM 4542 C CE . LYS B 2 55 ? 87.554 -41.630 25.260 1.00 78.19 ? 55 LYS B CE 1 ATOM 4543 N NZ . LYS B 2 55 ? 87.804 -40.224 24.840 1.00 90.48 ? 55 LYS B NZ 1 ATOM 4544 N N . ALA B 2 56 ? 81.958 -45.822 26.512 1.00 67.28 ? 56 ALA B N 1 ATOM 4545 C CA . ALA B 2 56 ? 80.752 -46.271 27.205 1.00 65.14 ? 56 ALA B CA 1 ATOM 4546 C C . ALA B 2 56 ? 80.268 -47.611 26.656 1.00 69.95 ? 56 ALA B C 1 ATOM 4547 O O . ALA B 2 56 ? 79.869 -47.700 25.501 1.00 73.40 ? 56 ALA B O 1 ATOM 4548 C CB . ALA B 2 56 ? 79.652 -45.229 27.097 1.00 59.65 ? 56 ALA B CB 1 ATOM 4549 N N . LEU B 2 57 ? 80.306 -48.649 27.486 1.00 68.18 ? 57 LEU B N 1 ATOM 4550 C CA . LEU B 2 57 ? 79.847 -49.979 27.085 1.00 69.47 ? 57 LEU B CA 1 ATOM 4551 C C . LEU B 2 57 ? 78.617 -50.430 27.880 1.00 71.36 ? 57 LEU B C 1 ATOM 4552 O O . LEU B 2 57 ? 78.626 -50.406 29.102 1.00 77.47 ? 57 LEU B O 1 ATOM 4553 C CB . LEU B 2 57 ? 80.981 -51.000 27.234 1.00 66.39 ? 57 LEU B CB 1 ATOM 4554 C CG . LEU B 2 57 ? 80.638 -52.493 27.157 1.00 63.08 ? 57 LEU B CG 1 ATOM 4555 C CD1 . LEU B 2 57 ? 79.753 -52.800 25.972 1.00 66.15 ? 57 LEU B CD1 1 ATOM 4556 C CD2 . LEU B 2 57 ? 81.908 -53.333 27.106 1.00 48.79 ? 57 LEU B CD2 1 ATOM 4557 N N . SER B 2 58 ? 77.556 -50.822 27.182 1.00 69.15 ? 58 SER B N 1 ATOM 4558 C CA . SER B 2 58 ? 76.385 -51.390 27.840 1.00 64.35 ? 58 SER B CA 1 ATOM 4559 C C . SER B 2 58 ? 76.211 -52.842 27.439 1.00 66.49 ? 58 SER B C 1 ATOM 4560 O O . SER B 2 58 ? 76.103 -53.162 26.263 1.00 74.29 ? 58 SER B O 1 ATOM 4561 C CB . SER B 2 58 ? 75.112 -50.612 27.504 1.00 56.49 ? 58 SER B CB 1 ATOM 4562 O OG . SER B 2 58 ? 73.961 -51.289 27.994 1.00 49.47 ? 58 SER B OG 1 ATOM 4563 N N . LEU B 2 59 ? 76.200 -53.718 28.431 1.00 61.99 ? 59 LEU B N 1 ATOM 4564 C CA . LEU B 2 59 ? 75.928 -55.128 28.218 1.00 60.90 ? 59 LEU B CA 1 ATOM 4565 C C . LEU B 2 59 ? 74.663 -55.482 28.987 1.00 68.69 ? 59 LEU B C 1 ATOM 4566 O O . LEU B 2 59 ? 74.401 -56.645 29.280 1.00 72.06 ? 59 LEU B O 1 ATOM 4567 C CB . LEU B 2 59 ? 77.122 -55.968 28.662 1.00 40.25 ? 59 LEU B CB 1 ATOM 4568 C CG . LEU B 2 59 ? 78.330 -55.631 27.795 1.00 49.40 ? 59 LEU B CG 1 ATOM 4569 C CD1 . LEU B 2 59 ? 79.643 -55.873 28.507 1.00 54.93 ? 59 LEU B CD1 1 ATOM 4570 C CD2 . LEU B 2 59 ? 78.250 -56.419 26.500 1.00 56.08 ? 59 LEU B CD2 1 ATOM 4571 N N . SER B 2 60 ? 73.883 -54.447 29.292 1.00 69.26 ? 60 SER B N 1 ATOM 4572 C CA . SER B 2 60 ? 72.657 -54.569 30.066 1.00 67.24 ? 60 SER B CA 1 ATOM 4573 C C . SER B 2 60 ? 71.768 -55.633 29.455 1.00 65.73 ? 60 SER B C 1 ATOM 4574 O O . SER B 2 60 ? 71.881 -55.929 28.273 1.00 80.31 ? 60 SER B O 1 ATOM 4575 C CB . SER B 2 60 ? 71.931 -53.219 30.101 1.00 73.89 ? 60 SER B CB 1 ATOM 4576 O OG . SER B 2 60 ? 70.579 -53.361 30.500 1.00 81.10 ? 60 SER B OG 1 ATOM 4577 N N . GLN B 2 61 ? 70.898 -56.217 30.268 1.00 56.53 ? 61 GLN B N 1 ATOM 4578 C CA . GLN B 2 61 ? 69.933 -57.212 29.804 1.00 58.60 ? 61 GLN B CA 1 ATOM 4579 C C . GLN B 2 61 ? 70.525 -58.384 29.009 1.00 67.20 ? 61 GLN B C 1 ATOM 4580 O O . GLN B 2 61 ? 70.023 -58.743 27.941 1.00 75.02 ? 61 GLN B O 1 ATOM 4581 C CB . GLN B 2 61 ? 68.804 -56.549 29.018 1.00 65.39 ? 61 GLN B CB 1 ATOM 4582 C CG . GLN B 2 61 ? 67.458 -56.629 29.710 1.00 85.34 ? 61 GLN B CG 1 ATOM 4583 C CD . GLN B 2 61 ? 67.194 -55.445 30.605 1.00 101.00 ? 61 GLN B CD 1 ATOM 4584 O OE1 . GLN B 2 61 ? 67.931 -54.453 30.570 1.00 109.37 ? 61 GLN B OE1 1 ATOM 4585 N NE2 . GLN B 2 61 ? 66.128 -55.528 31.409 1.00 95.22 ? 61 GLN B NE2 1 ATOM 4586 N N . ASN B 2 62 ? 71.586 -58.979 29.540 1.00 66.36 ? 62 ASN B N 1 ATOM 4587 C CA . ASN B 2 62 ? 72.151 -60.201 28.978 1.00 69.32 ? 62 ASN B CA 1 ATOM 4588 C C . ASN B 2 62 ? 72.210 -61.328 30.027 1.00 74.69 ? 62 ASN B C 1 ATOM 4589 O O . ASN B 2 62 ? 71.452 -61.315 31.011 1.00 69.05 ? 62 ASN B O 1 ATOM 4590 C CB . ASN B 2 62 ? 73.532 -59.931 28.367 1.00 64.97 ? 62 ASN B CB 1 ATOM 4591 C CG . ASN B 2 62 ? 73.464 -59.041 27.141 1.00 71.16 ? 62 ASN B CG 1 ATOM 4592 O OD1 . ASN B 2 62 ? 74.243 -58.102 26.998 1.00 81.53 ? 62 ASN B OD1 1 ATOM 4593 N ND2 . ASN B 2 62 ? 72.525 -59.327 26.254 1.00 67.76 ? 62 ASN B ND2 1 ATOM 4594 N N . SER B 2 63 ? 73.104 -62.294 29.817 1.00 67.79 ? 63 SER B N 1 ATOM 4595 C CA . SER B 2 63 ? 73.235 -63.425 30.728 1.00 67.35 ? 63 SER B CA 1 ATOM 4596 C C . SER B 2 63 ? 74.683 -63.638 31.151 1.00 74.35 ? 63 SER B C 1 ATOM 4597 O O . SER B 2 63 ? 75.115 -64.774 31.377 1.00 81.43 ? 63 SER B O 1 ATOM 4598 C CB . SER B 2 63 ? 72.673 -64.708 30.105 1.00 78.85 ? 63 SER B CB 1 ATOM 4599 O OG . SER B 2 63 ? 71.301 -64.578 29.768 1.00 82.70 ? 63 SER B OG 1 ATOM 4600 N N . ILE B 2 64 ? 75.427 -62.541 31.255 1.00 71.21 ? 64 ILE B N 1 ATOM 4601 C CA . ILE B 2 64 ? 76.766 -62.571 31.832 1.00 71.41 ? 64 ILE B CA 1 ATOM 4602 C C . ILE B 2 64 ? 76.668 -62.969 33.299 1.00 76.07 ? 64 ILE B C 1 ATOM 4603 O O . ILE B 2 64 ? 75.733 -62.562 33.985 1.00 58.99 ? 64 ILE B O 1 ATOM 4604 C CB . ILE B 2 64 ? 77.443 -61.207 31.717 1.00 72.84 ? 64 ILE B CB 1 ATOM 4605 C CG1 . ILE B 2 64 ? 77.576 -60.825 30.240 1.00 81.95 ? 64 ILE B CG1 1 ATOM 4606 C CG2 . ILE B 2 64 ? 78.797 -61.227 32.414 1.00 69.39 ? 64 ILE B CG2 1 ATOM 4607 C CD1 . ILE B 2 64 ? 77.889 -59.372 30.008 1.00 89.16 ? 64 ILE B CD1 1 ATOM 4608 N N . SER B 2 65 ? 77.625 -63.767 33.777 1.00 89.64 ? 65 SER B N 1 ATOM 4609 C CA . SER B 2 65 ? 77.546 -64.342 35.122 1.00 85.70 ? 65 SER B CA 1 ATOM 4610 C C . SER B 2 65 ? 78.777 -64.057 35.974 1.00 88.89 ? 65 SER B C 1 ATOM 4611 O O . SER B 2 65 ? 78.681 -63.911 37.194 1.00 101.44 ? 65 SER B O 1 ATOM 4612 C CB . SER B 2 65 ? 77.298 -65.851 35.048 1.00 88.83 ? 65 SER B CB 1 ATOM 4613 O OG . SER B 2 65 ? 75.998 -66.129 34.545 1.00 93.36 ? 65 SER B OG 1 ATOM 4614 N N . GLU B 2 66 ? 79.935 -63.991 35.334 1.00 83.83 ? 66 GLU B N 1 ATOM 4615 C CA . GLU B 2 66 ? 81.158 -63.621 36.033 1.00 79.25 ? 66 GLU B CA 1 ATOM 4616 C C . GLU B 2 66 ? 81.890 -62.555 35.236 1.00 83.75 ? 66 GLU B C 1 ATOM 4617 O O . GLU B 2 66 ? 81.769 -62.488 34.017 1.00 97.17 ? 66 GLU B O 1 ATOM 4618 C CB . GLU B 2 66 ? 82.050 -64.840 36.260 1.00 76.73 ? 66 GLU B CB 1 ATOM 4619 C CG . GLU B 2 66 ? 82.308 -65.666 35.014 1.00 97.24 ? 66 GLU B CG 1 ATOM 4620 C CD . GLU B 2 66 ? 83.310 -66.786 35.252 1.00 115.70 ? 66 GLU B CD 1 ATOM 4621 O OE1 . GLU B 2 66 ? 83.707 -66.989 36.421 1.00 116.04 ? 66 GLU B OE1 1 ATOM 4622 O OE2 . GLU B 2 66 ? 83.700 -67.461 34.271 1.00 122.57 ? 66 GLU B OE2 1 ATOM 4623 N N . LEU B 2 67 ? 82.632 -61.704 35.926 1.00 75.15 ? 67 LEU B N 1 ATOM 4624 C CA . LEU B 2 67 ? 83.355 -60.640 35.256 1.00 78.90 ? 67 LEU B CA 1 ATOM 4625 C C . LEU B 2 67 ? 84.820 -60.710 35.655 1.00 86.52 ? 67 LEU B C 1 ATOM 4626 O O . LEU B 2 67 ? 85.226 -60.102 36.648 1.00 82.96 ? 67 LEU B O 1 ATOM 4627 C CB . LEU B 2 67 ? 82.754 -59.275 35.610 1.00 76.55 ? 67 LEU B CB 1 ATOM 4628 C CG . LEU B 2 67 ? 83.412 -58.021 35.026 1.00 75.01 ? 67 LEU B CG 1 ATOM 4629 C CD1 . LEU B 2 67 ? 83.358 -58.047 33.519 1.00 61.06 ? 67 LEU B CD1 1 ATOM 4630 C CD2 . LEU B 2 67 ? 82.755 -56.758 35.553 1.00 79.01 ? 67 LEU B CD2 1 ATOM 4631 N N . ARG B 2 68 ? 85.600 -61.473 34.889 1.00 91.08 ? 68 ARG B N 1 ATOM 4632 C CA . ARG B 2 68 ? 87.028 -61.646 35.155 1.00 95.08 ? 68 ARG B CA 1 ATOM 4633 C C . ARG B 2 68 ? 87.826 -60.482 34.593 1.00 89.13 ? 68 ARG B C 1 ATOM 4634 O O . ARG B 2 68 ? 87.353 -59.773 33.704 1.00 87.87 ? 68 ARG B O 1 ATOM 4635 C CB . ARG B 2 68 ? 87.540 -62.952 34.551 1.00 104.73 ? 68 ARG B CB 1 ATOM 4636 C CG . ARG B 2 68 ? 87.004 -64.201 35.225 1.00 122.15 ? 68 ARG B CG 1 ATOM 4637 C CD . ARG B 2 68 ? 87.019 -64.064 36.745 1.00 134.85 ? 68 ARG B CD 1 ATOM 4638 N NE . ARG B 2 68 ? 86.863 -65.352 37.418 1.00 144.48 ? 68 ARG B NE 1 ATOM 4639 C CZ . ARG B 2 68 ? 86.247 -65.515 38.585 1.00 150.92 ? 68 ARG B CZ 1 ATOM 4640 N NH1 . ARG B 2 68 ? 85.711 -64.472 39.210 1.00 149.45 ? 68 ARG B NH1 1 ATOM 4641 N NH2 . ARG B 2 68 ? 86.157 -66.725 39.122 1.00 153.65 ? 68 ARG B NH2 1 ATOM 4642 N N . MET B 2 69 ? 89.036 -60.285 35.106 1.00 76.45 ? 69 MET B N 1 ATOM 4643 C CA . MET B 2 69 ? 89.877 -59.192 34.628 1.00 81.92 ? 69 MET B CA 1 ATOM 4644 C C . MET B 2 69 ? 90.107 -59.258 33.110 1.00 94.17 ? 69 MET B C 1 ATOM 4645 O O . MET B 2 69 ? 89.869 -58.274 32.400 1.00 91.23 ? 69 MET B O 1 ATOM 4646 C CB . MET B 2 69 ? 91.213 -59.152 35.379 1.00 82.54 ? 69 MET B CB 1 ATOM 4647 C CG . MET B 2 69 ? 92.005 -57.857 35.191 1.00 79.15 ? 69 MET B CG 1 ATOM 4648 S SD . MET B 2 69 ? 93.510 -57.798 36.188 1.00 120.80 ? 69 MET B SD 1 ATOM 4649 C CE . MET B 2 69 ? 94.451 -59.126 35.440 1.00 95.39 ? 69 MET B CE 1 ATOM 4650 N N . PRO B 2 70 ? 90.555 -60.422 32.601 1.00 98.73 ? 70 PRO B N 1 ATOM 4651 C CA . PRO B 2 70 ? 90.869 -60.495 31.171 1.00 87.35 ? 70 PRO B CA 1 ATOM 4652 C C . PRO B 2 70 ? 89.644 -60.195 30.321 1.00 74.13 ? 70 PRO B C 1 ATOM 4653 O O . PRO B 2 70 ? 89.790 -60.061 29.112 1.00 69.15 ? 70 PRO B O 1 ATOM 4654 C CB . PRO B 2 70 ? 91.305 -61.954 30.973 1.00 87.57 ? 70 PRO B CB 1 ATOM 4655 C CG . PRO B 2 70 ? 91.627 -62.464 32.333 1.00 91.14 ? 70 PRO B CG 1 ATOM 4656 C CD . PRO B 2 70 ? 90.723 -61.726 33.267 1.00 98.92 ? 70 PRO B CD 1 ATOM 4657 N N . ASP B 2 71 ? 88.471 -60.096 30.946 1.00 70.97 ? 71 ASP B N 1 ATOM 4658 C CA . ASP B 2 71 ? 87.236 -59.746 30.241 1.00 86.35 ? 71 ASP B CA 1 ATOM 4659 C C . ASP B 2 71 ? 87.153 -58.264 29.878 1.00 81.98 ? 71 ASP B C 1 ATOM 4660 O O . ASP B 2 71 ? 86.504 -57.914 28.889 1.00 83.26 ? 71 ASP B O 1 ATOM 4661 C CB . ASP B 2 71 ? 85.996 -60.120 31.064 1.00 98.86 ? 71 ASP B CB 1 ATOM 4662 C CG . ASP B 2 71 ? 85.693 -61.602 31.032 1.00 100.46 ? 71 ASP B CG 1 ATOM 4663 O OD1 . ASP B 2 71 ? 86.631 -62.392 30.790 1.00 103.34 ? 71 ASP B OD1 1 ATOM 4664 O OD2 . ASP B 2 71 ? 84.517 -61.971 31.253 1.00 91.97 ? 71 ASP B OD2 1 ATOM 4665 N N . ILE B 2 72 ? 87.789 -57.403 30.680 1.00 75.07 ? 72 ILE B N 1 ATOM 4666 C CA . ILE B 2 72 ? 87.763 -55.952 30.441 1.00 71.02 ? 72 ILE B CA 1 ATOM 4667 C C . ILE B 2 72 ? 89.130 -55.248 30.497 1.00 68.72 ? 72 ILE B C 1 ATOM 4668 O O . ILE B 2 72 ? 89.199 -54.027 30.350 1.00 64.92 ? 72 ILE B O 1 ATOM 4669 C CB . ILE B 2 72 ? 86.808 -55.206 31.410 1.00 75.34 ? 72 ILE B CB 1 ATOM 4670 C CG1 . ILE B 2 72 ? 87.008 -55.710 32.836 1.00 69.85 ? 72 ILE B CG1 1 ATOM 4671 C CG2 . ILE B 2 72 ? 85.332 -55.310 30.974 1.00 47.38 ? 72 ILE B CG2 1 ATOM 4672 C CD1 . ILE B 2 72 ? 86.387 -54.815 33.842 1.00 69.80 ? 72 ILE B CD1 1 ATOM 4673 N N . SER B 2 73 ? 90.205 -56.009 30.701 1.00 68.59 ? 73 SER B N 1 ATOM 4674 C CA . SER B 2 73 ? 91.571 -55.464 30.723 1.00 73.93 ? 73 SER B CA 1 ATOM 4675 C C . SER B 2 73 ? 91.856 -54.493 29.583 1.00 80.12 ? 73 SER B C 1 ATOM 4676 O O . SER B 2 73 ? 92.431 -53.426 29.795 1.00 77.44 ? 73 SER B O 1 ATOM 4677 C CB . SER B 2 73 ? 92.611 -56.588 30.639 1.00 83.02 ? 73 SER B CB 1 ATOM 4678 O OG . SER B 2 73 ? 92.424 -57.584 31.629 1.00 90.21 ? 73 SER B OG 1 ATOM 4679 N N . PHE B 2 74 ? 91.469 -54.889 28.371 1.00 89.31 ? 74 PHE B N 1 ATOM 4680 C CA . PHE B 2 74 ? 91.832 -54.177 27.140 1.00 90.22 ? 74 PHE B CA 1 ATOM 4681 C C . PHE B 2 74 ? 91.131 -52.825 26.943 1.00 95.57 ? 74 PHE B C 1 ATOM 4682 O O . PHE B 2 74 ? 91.654 -51.950 26.247 1.00 108.36 ? 74 PHE B O 1 ATOM 4683 C CB . PHE B 2 74 ? 91.586 -55.072 25.917 1.00 83.11 ? 74 PHE B CB 1 ATOM 4684 C CG . PHE B 2 74 ? 90.145 -55.468 25.738 1.00 83.72 ? 74 PHE B CG 1 ATOM 4685 C CD1 . PHE B 2 74 ? 89.341 -54.808 24.826 1.00 78.75 ? 74 PHE B CD1 1 ATOM 4686 C CD2 . PHE B 2 74 ? 89.589 -56.486 26.502 1.00 85.24 ? 74 PHE B CD2 1 ATOM 4687 C CE1 . PHE B 2 74 ? 88.016 -55.159 24.671 1.00 82.94 ? 74 PHE B CE1 1 ATOM 4688 C CE2 . PHE B 2 74 ? 88.261 -56.842 26.353 1.00 86.72 ? 74 PHE B CE2 1 ATOM 4689 C CZ . PHE B 2 74 ? 87.474 -56.176 25.438 1.00 88.05 ? 74 PHE B CZ 1 ATOM 4690 N N . LEU B 2 75 ? 89.951 -52.657 27.536 1.00 79.15 ? 75 LEU B N 1 ATOM 4691 C CA . LEU B 2 75 ? 89.192 -51.422 27.377 1.00 73.28 ? 75 LEU B CA 1 ATOM 4692 C C . LEU B 2 75 ? 89.737 -50.340 28.295 1.00 74.48 ? 75 LEU B C 1 ATOM 4693 O O . LEU B 2 75 ? 89.039 -49.859 29.179 1.00 79.35 ? 75 LEU B O 1 ATOM 4694 C CB . LEU B 2 75 ? 87.716 -51.667 27.673 1.00 69.34 ? 75 LEU B CB 1 ATOM 4695 C CG . LEU B 2 75 ? 87.087 -52.745 26.799 1.00 75.73 ? 75 LEU B CG 1 ATOM 4696 C CD1 . LEU B 2 75 ? 86.007 -53.510 27.538 1.00 73.61 ? 75 LEU B CD1 1 ATOM 4697 C CD2 . LEU B 2 75 ? 86.543 -52.119 25.526 1.00 84.92 ? 75 LEU B CD2 1 ATOM 4698 N N . SER B 2 76 ? 90.982 -49.949 28.063 1.00 73.59 ? 76 SER B N 1 ATOM 4699 C CA . SER B 2 76 ? 91.700 -49.049 28.959 1.00 74.54 ? 76 SER B CA 1 ATOM 4700 C C . SER B 2 76 ? 91.069 -47.670 29.105 1.00 78.82 ? 76 SER B C 1 ATOM 4701 O O . SER B 2 76 ? 91.384 -46.941 30.047 1.00 102.51 ? 76 SER B O 1 ATOM 4702 C CB . SER B 2 76 ? 93.156 -48.890 28.505 1.00 81.94 ? 76 SER B CB 1 ATOM 4703 O OG . SER B 2 76 ? 93.296 -47.795 27.612 1.00 81.54 ? 76 SER B OG 1 ATOM 4704 N N . GLU B 2 77 ? 90.179 -47.313 28.187 1.00 68.79 ? 77 GLU B N 1 ATOM 4705 C CA . GLU B 2 77 ? 89.630 -45.960 28.148 1.00 71.59 ? 77 GLU B CA 1 ATOM 4706 C C . GLU B 2 77 ? 88.227 -45.887 28.727 1.00 66.46 ? 77 GLU B C 1 ATOM 4707 O O . GLU B 2 77 ? 87.642 -44.808 28.792 1.00 66.03 ? 77 GLU B O 1 ATOM 4708 C CB . GLU B 2 77 ? 89.582 -45.462 26.706 1.00 91.08 ? 77 GLU B CB 1 ATOM 4709 C CG . GLU B 2 77 ? 90.093 -44.057 26.519 1.00 99.90 ? 77 GLU B CG 1 ATOM 4710 C CD . GLU B 2 77 ? 91.550 -44.046 26.112 1.00 106.14 ? 77 GLU B CD 1 ATOM 4711 O OE1 . GLU B 2 77 ? 91.815 -43.731 24.932 1.00 121.46 ? 77 GLU B OE1 1 ATOM 4712 O OE2 . GLU B 2 77 ? 92.421 -44.370 26.957 1.00 89.69 ? 77 GLU B OE2 1 ATOM 4713 N N . LEU B 2 78 ? 87.699 -47.041 29.133 1.00 75.74 ? 78 LEU B N 1 ATOM 4714 C CA . LEU B 2 78 ? 86.316 -47.176 29.594 1.00 81.59 ? 78 LEU B CA 1 ATOM 4715 C C . LEU B 2 78 ? 85.959 -46.188 30.701 1.00 83.81 ? 78 LEU B C 1 ATOM 4716 O O . LEU B 2 78 ? 86.657 -46.108 31.706 1.00 94.53 ? 78 LEU B O 1 ATOM 4717 C CB . LEU B 2 78 ? 86.056 -48.610 30.075 1.00 77.13 ? 78 LEU B CB 1 ATOM 4718 C CG . LEU B 2 78 ? 84.580 -48.957 30.264 1.00 77.81 ? 78 LEU B CG 1 ATOM 4719 C CD1 . LEU B 2 78 ? 83.826 -48.540 29.029 1.00 86.20 ? 78 LEU B CD1 1 ATOM 4720 C CD2 . LEU B 2 78 ? 84.384 -50.432 30.508 1.00 74.68 ? 78 LEU B CD2 1 ATOM 4721 N N . ARG B 2 79 ? 84.882 -45.433 30.503 1.00 70.59 ? 79 ARG B N 1 ATOM 4722 C CA . ARG B 2 79 ? 84.374 -44.534 31.528 1.00 69.37 ? 79 ARG B CA 1 ATOM 4723 C C . ARG B 2 79 ? 83.082 -45.102 32.085 1.00 64.05 ? 79 ARG B C 1 ATOM 4724 O O . ARG B 2 79 ? 82.818 -45.038 33.284 1.00 80.92 ? 79 ARG B O 1 ATOM 4725 C CB . ARG B 2 79 ? 84.081 -43.146 30.963 1.00 75.95 ? 79 ARG B CB 1 ATOM 4726 C CG . ARG B 2 79 ? 85.275 -42.334 30.495 1.00 96.15 ? 79 ARG B CG 1 ATOM 4727 C CD . ARG B 2 79 ? 84.807 -40.944 30.029 1.00 125.03 ? 79 ARG B CD 1 ATOM 4728 N NE . ARG B 2 79 ? 83.889 -40.988 28.876 1.00 148.54 ? 79 ARG B NE 1 ATOM 4729 C CZ . ARG B 2 79 ? 82.555 -40.894 28.944 1.00 146.83 ? 79 ARG B CZ 1 ATOM 4730 N NH1 . ARG B 2 79 ? 81.953 -40.754 30.122 1.00 147.02 ? 79 ARG B NH1 1 ATOM 4731 N NH2 . ARG B 2 79 ? 81.820 -40.945 27.829 1.00 130.93 ? 79 ARG B NH2 1 ATOM 4732 N N . VAL B 2 80 ? 82.274 -45.659 31.201 1.00 46.91 ? 80 VAL B N 1 ATOM 4733 C CA . VAL B 2 80 ? 80.951 -46.133 31.568 1.00 52.47 ? 80 VAL B CA 1 ATOM 4734 C C . VAL B 2 80 ? 80.790 -47.615 31.260 1.00 59.99 ? 80 VAL B C 1 ATOM 4735 O O . VAL B 2 80 ? 81.136 -48.075 30.174 1.00 55.16 ? 80 VAL B O 1 ATOM 4736 C CB . VAL B 2 80 ? 79.876 -45.334 30.820 1.00 52.21 ? 80 VAL B CB 1 ATOM 4737 C CG1 . VAL B 2 80 ? 78.492 -45.934 31.038 1.00 36.87 ? 80 VAL B CG1 1 ATOM 4738 C CG2 . VAL B 2 80 ? 79.951 -43.858 31.225 1.00 48.44 ? 80 VAL B CG2 1 ATOM 4739 N N . LEU B 2 81 ? 80.286 -48.365 32.233 1.00 63.16 ? 81 LEU B N 1 ATOM 4740 C CA . LEU B 2 81 ? 79.993 -49.780 32.041 1.00 64.63 ? 81 LEU B CA 1 ATOM 4741 C C . LEU B 2 81 ? 78.630 -50.068 32.650 1.00 58.16 ? 81 LEU B C 1 ATOM 4742 O O . LEU B 2 81 ? 78.453 -49.958 33.855 1.00 63.52 ? 81 LEU B O 1 ATOM 4743 C CB . LEU B 2 81 ? 81.073 -50.653 32.686 1.00 63.27 ? 81 LEU B CB 1 ATOM 4744 C CG . LEU B 2 81 ? 80.810 -52.158 32.791 1.00 59.54 ? 81 LEU B CG 1 ATOM 4745 C CD1 . LEU B 2 81 ? 80.895 -52.850 31.439 1.00 49.70 ? 81 LEU B CD1 1 ATOM 4746 C CD2 . LEU B 2 81 ? 81.791 -52.782 33.777 1.00 61.07 ? 81 LEU B CD2 1 ATOM 4747 N N . ARG B 2 82 ? 77.656 -50.395 31.812 1.00 56.88 ? 82 ARG B N 1 ATOM 4748 C CA . ARG B 2 82 ? 76.316 -50.680 32.299 1.00 62.80 ? 82 ARG B CA 1 ATOM 4749 C C . ARG B 2 82 ? 76.083 -52.177 32.211 1.00 72.21 ? 82 ARG B C 1 ATOM 4750 O O . ARG B 2 82 ? 76.155 -52.759 31.143 1.00 73.86 ? 82 ARG B O 1 ATOM 4751 C CB . ARG B 2 82 ? 75.257 -49.879 31.534 1.00 53.15 ? 82 ARG B CB 1 ATOM 4752 C CG . ARG B 2 82 ? 75.610 -48.386 31.411 1.00 70.35 ? 82 ARG B CG 1 ATOM 4753 C CD . ARG B 2 82 ? 74.414 -47.472 31.095 1.00 87.05 ? 82 ARG B CD 1 ATOM 4754 N NE . ARG B 2 82 ? 74.027 -47.495 29.681 1.00 103.93 ? 82 ARG B NE 1 ATOM 4755 C CZ . ARG B 2 82 ? 72.964 -48.141 29.197 1.00 115.98 ? 82 ARG B CZ 1 ATOM 4756 N NH1 . ARG B 2 82 ? 72.156 -48.824 30.014 1.00 125.05 ? 82 ARG B NH1 1 ATOM 4757 N NH2 . ARG B 2 82 ? 72.703 -48.101 27.892 1.00 103.67 ? 82 ARG B NH2 1 ATOM 4758 N N . LEU B 2 83 ? 75.838 -52.798 33.356 1.00 74.91 ? 83 LEU B N 1 ATOM 4759 C CA . LEU B 2 83 ? 75.705 -54.241 33.436 1.00 69.91 ? 83 LEU B CA 1 ATOM 4760 C C . LEU B 2 83 ? 74.411 -54.604 34.146 1.00 69.50 ? 83 LEU B C 1 ATOM 4761 O O . LEU B 2 83 ? 74.198 -55.757 34.532 1.00 65.94 ? 83 LEU B O 1 ATOM 4762 C CB . LEU B 2 83 ? 76.907 -54.834 34.164 1.00 68.98 ? 83 LEU B CB 1 ATOM 4763 C CG . LEU B 2 83 ? 78.042 -55.258 33.246 1.00 68.62 ? 83 LEU B CG 1 ATOM 4764 C CD1 . LEU B 2 83 ? 79.364 -55.354 34.002 1.00 60.72 ? 83 LEU B CD1 1 ATOM 4765 C CD2 . LEU B 2 83 ? 77.658 -56.586 32.601 1.00 69.28 ? 83 LEU B CD2 1 ATOM 4766 N N . SER B 2 84 ? 73.556 -53.601 34.322 1.00 66.35 ? 84 SER B N 1 ATOM 4767 C CA . SER B 2 84 ? 72.207 -53.812 34.825 1.00 71.08 ? 84 SER B CA 1 ATOM 4768 C C . SER B 2 84 ? 71.572 -55.060 34.219 1.00 68.76 ? 84 SER B C 1 ATOM 4769 O O . SER B 2 84 ? 71.877 -55.441 33.091 1.00 74.52 ? 84 SER B O 1 ATOM 4770 C CB . SER B 2 84 ? 71.351 -52.581 34.541 1.00 85.39 ? 84 SER B CB 1 ATOM 4771 O OG . SER B 2 84 ? 71.961 -51.779 33.538 1.00 103.54 ? 84 SER B OG 1 ATOM 4772 N N . HIS B 2 85 ? 70.701 -55.696 34.990 1.00 65.11 ? 85 HIS B N 1 ATOM 4773 C CA . HIS B 2 85 ? 70.033 -56.941 34.599 1.00 54.72 ? 85 HIS B CA 1 ATOM 4774 C C . HIS B 2 85 ? 70.910 -58.041 34.039 1.00 57.26 ? 85 HIS B C 1 ATOM 4775 O O . HIS B 2 85 ? 70.723 -58.469 32.909 1.00 56.41 ? 85 HIS B O 1 ATOM 4776 C CB . HIS B 2 85 ? 68.888 -56.671 33.637 1.00 42.67 ? 85 HIS B CB 1 ATOM 4777 C CG . HIS B 2 85 ? 67.777 -55.883 34.245 1.00 54.69 ? 85 HIS B CG 1 ATOM 4778 N ND1 . HIS B 2 85 ? 66.701 -56.478 34.867 1.00 68.19 ? 85 HIS B ND1 1 ATOM 4779 C CD2 . HIS B 2 85 ? 67.584 -54.547 34.349 1.00 55.67 ? 85 HIS B CD2 1 ATOM 4780 C CE1 . HIS B 2 85 ? 65.881 -55.541 35.310 1.00 72.70 ? 85 HIS B CE1 1 ATOM 4781 N NE2 . HIS B 2 85 ? 66.393 -54.360 35.008 1.00 67.66 ? 85 HIS B NE2 1 ATOM 4782 N N . ASN B 2 86 ? 71.854 -58.516 34.840 1.00 65.78 ? 86 ASN B N 1 ATOM 4783 C CA . ASN B 2 86 ? 72.534 -59.763 34.522 1.00 67.21 ? 86 ASN B CA 1 ATOM 4784 C C . ASN B 2 86 ? 72.436 -60.786 35.641 1.00 70.36 ? 86 ASN B C 1 ATOM 4785 O O . ASN B 2 86 ? 71.460 -60.811 36.385 1.00 73.69 ? 86 ASN B O 1 ATOM 4786 C CB . ASN B 2 86 ? 73.981 -59.526 34.130 1.00 69.82 ? 86 ASN B CB 1 ATOM 4787 C CG . ASN B 2 86 ? 74.116 -59.087 32.699 1.00 70.60 ? 86 ASN B CG 1 ATOM 4788 O OD1 . ASN B 2 86 ? 73.729 -57.976 32.338 1.00 75.89 ? 86 ASN B OD1 1 ATOM 4789 N ND2 . ASN B 2 86 ? 74.671 -59.953 31.871 1.00 62.94 ? 86 ASN B ND2 1 ATOM 4790 N N . ARG B 2 87 ? 73.449 -61.631 35.755 1.00 77.88 ? 87 ARG B N 1 ATOM 4791 C CA . ARG B 2 87 ? 73.354 -62.792 36.627 1.00 93.54 ? 87 ARG B CA 1 ATOM 4792 C C . ARG B 2 87 ? 74.639 -62.995 37.430 1.00 81.07 ? 87 ARG B C 1 ATOM 4793 O O . ARG B 2 87 ? 74.934 -64.108 37.883 1.00 73.20 ? 87 ARG B O 1 ATOM 4794 C CB . ARG B 2 87 ? 73.038 -64.045 35.794 1.00 119.14 ? 87 ARG B CB 1 ATOM 4795 C CG . ARG B 2 87 ? 72.015 -63.838 34.655 1.00 130.61 ? 87 ARG B CG 1 ATOM 4796 C CD . ARG B 2 87 ? 70.570 -64.120 35.087 1.00 140.39 ? 87 ARG B CD 1 ATOM 4797 N NE . ARG B 2 87 ? 69.607 -63.984 33.989 1.00 149.41 ? 87 ARG B NE 1 ATOM 4798 C CZ . ARG B 2 87 ? 69.396 -64.903 33.045 1.00 156.94 ? 87 ARG B CZ 1 ATOM 4799 N NH1 . ARG B 2 87 ? 70.085 -66.037 33.044 1.00 160.87 ? 87 ARG B NH1 1 ATOM 4800 N NH2 . ARG B 2 87 ? 68.495 -64.686 32.090 1.00 154.45 ? 87 ARG B NH2 1 ATOM 4801 N N . ILE B 2 88 ? 75.397 -61.914 37.595 1.00 71.25 ? 88 ILE B N 1 ATOM 4802 C CA . ILE B 2 88 ? 76.647 -61.947 38.345 1.00 74.70 ? 88 ILE B CA 1 ATOM 4803 C C . ILE B 2 88 ? 76.404 -62.166 39.836 1.00 83.56 ? 88 ILE B C 1 ATOM 4804 O O . ILE B 2 88 ? 75.580 -61.473 40.448 1.00 78.82 ? 88 ILE B O 1 ATOM 4805 C CB . ILE B 2 88 ? 77.418 -60.638 38.177 1.00 66.41 ? 88 ILE B CB 1 ATOM 4806 C CG1 . ILE B 2 88 ? 77.590 -60.317 36.702 1.00 69.01 ? 88 ILE B CG1 1 ATOM 4807 C CG2 . ILE B 2 88 ? 78.764 -60.715 38.868 1.00 62.78 ? 88 ILE B CG2 1 ATOM 4808 C CD1 . ILE B 2 88 ? 78.170 -58.949 36.462 1.00 80.83 ? 88 ILE B CD1 1 ATOM 4809 N N . ARG B 2 89 ? 77.130 -63.121 40.417 1.00 88.18 ? 89 ARG B N 1 ATOM 4810 C CA . ARG B 2 89 ? 76.962 -63.453 41.835 1.00 91.85 ? 89 ARG B CA 1 ATOM 4811 C C . ARG B 2 89 ? 78.012 -62.786 42.712 1.00 84.99 ? 89 ARG B C 1 ATOM 4812 O O . ARG B 2 89 ? 77.688 -62.186 43.731 1.00 78.25 ? 89 ARG B O 1 ATOM 4813 C CB . ARG B 2 89 ? 76.938 -64.970 42.053 1.00 96.38 ? 89 ARG B CB 1 ATOM 4814 C CG . ARG B 2 89 ? 75.595 -65.580 41.694 1.00 104.74 ? 89 ARG B CG 1 ATOM 4815 C CD . ARG B 2 89 ? 75.532 -67.082 41.890 1.00 115.36 ? 89 ARG B CD 1 ATOM 4816 N NE . ARG B 2 89 ? 74.248 -67.597 41.415 1.00 125.67 ? 89 ARG B NE 1 ATOM 4817 C CZ . ARG B 2 89 ? 74.086 -68.314 40.307 1.00 127.54 ? 89 ARG B CZ 1 ATOM 4818 N NH1 . ARG B 2 89 ? 75.136 -68.631 39.556 1.00 128.13 ? 89 ARG B NH1 1 ATOM 4819 N NH2 . ARG B 2 89 ? 72.873 -68.726 39.958 1.00 122.09 ? 89 ARG B NH2 1 ATOM 4820 N N . SER B 2 90 ? 79.268 -62.878 42.303 1.00 84.48 ? 90 SER B N 1 ATOM 4821 C CA . SER B 2 90 ? 80.332 -62.172 42.988 1.00 76.66 ? 90 SER B CA 1 ATOM 4822 C C . SER B 2 90 ? 80.894 -61.061 42.100 1.00 86.97 ? 90 SER B C 1 ATOM 4823 O O . SER B 2 90 ? 80.866 -61.158 40.872 1.00 83.91 ? 90 SER B O 1 ATOM 4824 C CB . SER B 2 90 ? 81.436 -63.144 43.368 1.00 75.80 ? 90 SER B CB 1 ATOM 4825 O OG . SER B 2 90 ? 82.221 -62.614 44.420 1.00 91.51 ? 90 SER B OG 1 ATOM 4826 N N . LEU B 2 91 ? 81.397 -60.000 42.722 1.00 90.91 ? 91 LEU B N 1 ATOM 4827 C CA . LEU B 2 91 ? 82.055 -58.934 41.977 1.00 84.43 ? 91 LEU B CA 1 ATOM 4828 C C . LEU B 2 91 ? 83.358 -58.527 42.657 1.00 76.52 ? 91 LEU B C 1 ATOM 4829 O O . LEU B 2 91 ? 83.343 -57.944 43.738 1.00 73.42 ? 91 LEU B O 1 ATOM 4830 C CB . LEU B 2 91 ? 81.142 -57.716 41.847 1.00 80.76 ? 91 LEU B CB 1 ATOM 4831 C CG . LEU B 2 91 ? 81.363 -56.880 40.586 1.00 76.15 ? 91 LEU B CG 1 ATOM 4832 C CD1 . LEU B 2 91 ? 81.085 -55.409 40.858 1.00 76.16 ? 91 LEU B CD1 1 ATOM 4833 C CD2 . LEU B 2 91 ? 82.777 -57.076 40.055 1.00 71.80 ? 91 LEU B CD2 1 ATOM 4834 N N . ASP B 2 92 ? 84.480 -58.828 42.012 1.00 63.44 ? 92 ASP B N 1 ATOM 4835 C CA . ASP B 2 92 ? 85.787 -58.463 42.531 1.00 68.18 ? 92 ASP B CA 1 ATOM 4836 C C . ASP B 2 92 ? 86.243 -57.122 41.940 1.00 74.61 ? 92 ASP B C 1 ATOM 4837 O O . ASP B 2 92 ? 86.559 -57.042 40.761 1.00 78.88 ? 92 ASP B O 1 ATOM 4838 C CB . ASP B 2 92 ? 86.785 -59.580 42.219 1.00 54.03 ? 92 ASP B CB 1 ATOM 4839 C CG . ASP B 2 92 ? 88.148 -59.364 42.873 1.00 85.93 ? 92 ASP B CG 1 ATOM 4840 O OD1 . ASP B 2 92 ? 88.409 -58.255 43.388 1.00 81.57 ? 92 ASP B OD1 1 ATOM 4841 O OD2 . ASP B 2 92 ? 88.966 -60.312 42.864 1.00 71.68 ? 92 ASP B OD2 1 ATOM 4842 N N . PHE B 2 93 ? 86.271 -56.071 42.759 1.00 73.88 ? 93 PHE B N 1 ATOM 4843 C CA . PHE B 2 93 ? 86.646 -54.736 42.286 1.00 70.43 ? 93 PHE B CA 1 ATOM 4844 C C . PHE B 2 93 ? 88.090 -54.601 41.807 1.00 76.26 ? 93 PHE B C 1 ATOM 4845 O O . PHE B 2 93 ? 88.477 -53.547 41.317 1.00 80.49 ? 93 PHE B O 1 ATOM 4846 C CB . PHE B 2 93 ? 86.392 -53.672 43.353 1.00 66.47 ? 93 PHE B CB 1 ATOM 4847 C CG . PHE B 2 93 ? 84.956 -53.301 43.509 1.00 65.90 ? 93 PHE B CG 1 ATOM 4848 C CD1 . PHE B 2 93 ? 84.329 -53.410 44.735 1.00 70.46 ? 93 PHE B CD1 1 ATOM 4849 C CD2 . PHE B 2 93 ? 84.227 -52.842 42.435 1.00 65.91 ? 93 PHE B CD2 1 ATOM 4850 C CE1 . PHE B 2 93 ? 82.993 -53.067 44.882 1.00 68.96 ? 93 PHE B CE1 1 ATOM 4851 C CE2 . PHE B 2 93 ? 82.889 -52.501 42.577 1.00 69.84 ? 93 PHE B CE2 1 ATOM 4852 C CZ . PHE B 2 93 ? 82.272 -52.615 43.804 1.00 63.34 ? 93 PHE B CZ 1 ATOM 4853 N N . HIS B 2 94 ? 88.896 -55.643 41.965 1.00 82.60 ? 94 HIS B N 1 ATOM 4854 C CA . HIS B 2 94 ? 90.272 -55.587 41.474 1.00 87.74 ? 94 HIS B CA 1 ATOM 4855 C C . HIS B 2 94 ? 90.256 -55.906 39.981 1.00 88.70 ? 94 HIS B C 1 ATOM 4856 O O . HIS B 2 94 ? 91.117 -55.476 39.207 1.00 96.41 ? 94 HIS B O 1 ATOM 4857 C CB . HIS B 2 94 ? 91.174 -56.558 42.244 1.00 91.71 ? 94 HIS B CB 1 ATOM 4858 C CG . HIS B 2 94 ? 92.621 -56.465 41.867 1.00 110.03 ? 94 HIS B CG 1 ATOM 4859 N ND1 . HIS B 2 94 ? 93.424 -55.411 42.250 1.00 119.05 ? 94 HIS B ND1 1 ATOM 4860 C CD2 . HIS B 2 94 ? 93.409 -57.291 41.136 1.00 115.65 ? 94 HIS B CD2 1 ATOM 4861 C CE1 . HIS B 2 94 ? 94.643 -55.592 41.774 1.00 119.11 ? 94 HIS B CE1 1 ATOM 4862 N NE2 . HIS B 2 94 ? 94.661 -56.725 41.093 1.00 117.99 ? 94 HIS B NE2 1 ATOM 4863 N N . VAL B 2 95 ? 89.247 -56.669 39.592 1.00 80.08 ? 95 VAL B N 1 ATOM 4864 C CA . VAL B 2 95 ? 88.977 -56.968 38.199 1.00 80.93 ? 95 VAL B CA 1 ATOM 4865 C C . VAL B 2 95 ? 89.123 -55.736 37.284 1.00 77.29 ? 95 VAL B C 1 ATOM 4866 O O . VAL B 2 95 ? 89.578 -55.857 36.150 1.00 68.87 ? 95 VAL B O 1 ATOM 4867 C CB . VAL B 2 95 ? 87.576 -57.603 38.089 1.00 79.35 ? 95 VAL B CB 1 ATOM 4868 C CG1 . VAL B 2 95 ? 86.789 -57.035 36.916 1.00 72.19 ? 95 VAL B CG1 1 ATOM 4869 C CG2 . VAL B 2 95 ? 87.684 -59.133 38.075 1.00 71.51 ? 95 VAL B CG2 1 ATOM 4870 N N . PHE B 2 96 ? 88.761 -54.557 37.790 1.00 78.75 ? 96 PHE B N 1 ATOM 4871 C CA . PHE B 2 96 ? 88.873 -53.308 37.028 1.00 73.83 ? 96 PHE B CA 1 ATOM 4872 C C . PHE B 2 96 ? 90.265 -52.658 37.085 1.00 79.33 ? 96 PHE B C 1 ATOM 4873 O O . PHE B 2 96 ? 90.396 -51.448 36.870 1.00 69.41 ? 96 PHE B O 1 ATOM 4874 C CB . PHE B 2 96 ? 87.846 -52.282 37.515 1.00 59.76 ? 96 PHE B CB 1 ATOM 4875 C CG . PHE B 2 96 ? 86.431 -52.755 37.451 1.00 63.97 ? 96 PHE B CG 1 ATOM 4876 C CD1 . PHE B 2 96 ? 85.728 -53.026 38.606 1.00 74.19 ? 96 PHE B CD1 1 ATOM 4877 C CD2 . PHE B 2 96 ? 85.797 -52.916 36.241 1.00 77.96 ? 96 PHE B CD2 1 ATOM 4878 C CE1 . PHE B 2 96 ? 84.417 -53.455 38.558 1.00 80.78 ? 96 PHE B CE1 1 ATOM 4879 C CE2 . PHE B 2 96 ? 84.484 -53.356 36.181 1.00 87.92 ? 96 PHE B CE2 1 ATOM 4880 C CZ . PHE B 2 96 ? 83.794 -53.625 37.345 1.00 88.42 ? 96 PHE B CZ 1 ATOM 4881 N N . LEU B 2 97 ? 91.301 -53.446 37.366 1.00 83.42 ? 97 LEU B N 1 ATOM 4882 C CA . LEU B 2 97 ? 92.623 -52.871 37.607 1.00 83.45 ? 97 LEU B CA 1 ATOM 4883 C C . LEU B 2 97 ? 93.083 -51.937 36.488 1.00 88.60 ? 97 LEU B C 1 ATOM 4884 O O . LEU B 2 97 ? 93.679 -50.897 36.756 1.00 88.18 ? 97 LEU B O 1 ATOM 4885 C CB . LEU B 2 97 ? 93.671 -53.960 37.875 1.00 85.80 ? 97 LEU B CB 1 ATOM 4886 C CG . LEU B 2 97 ? 95.157 -53.549 37.863 1.00 88.48 ? 97 LEU B CG 1 ATOM 4887 C CD1 . LEU B 2 97 ? 95.439 -52.271 38.648 1.00 81.50 ? 97 LEU B CD1 1 ATOM 4888 C CD2 . LEU B 2 97 ? 96.048 -54.680 38.363 1.00 87.24 ? 97 LEU B CD2 1 ATOM 4889 N N . PHE B 2 98 ? 92.788 -52.292 35.240 1.00 90.04 ? 98 PHE B N 1 ATOM 4890 C CA . PHE B 2 98 ? 93.343 -51.557 34.102 1.00 88.79 ? 98 PHE B CA 1 ATOM 4891 C C . PHE B 2 98 ? 92.407 -50.498 33.498 1.00 82.94 ? 98 PHE B C 1 ATOM 4892 O O . PHE B 2 98 ? 92.805 -49.736 32.607 1.00 83.41 ? 98 PHE B O 1 ATOM 4893 C CB . PHE B 2 98 ? 93.873 -52.525 33.033 1.00 84.25 ? 98 PHE B CB 1 ATOM 4894 C CG . PHE B 2 98 ? 95.078 -53.320 33.476 1.00 81.81 ? 98 PHE B CG 1 ATOM 4895 C CD1 . PHE B 2 98 ? 94.942 -54.634 33.906 1.00 88.43 ? 98 PHE B CD1 1 ATOM 4896 C CD2 . PHE B 2 98 ? 96.346 -52.750 33.470 1.00 83.27 ? 98 PHE B CD2 1 ATOM 4897 C CE1 . PHE B 2 98 ? 96.051 -55.373 34.319 1.00 93.28 ? 98 PHE B CE1 1 ATOM 4898 C CE2 . PHE B 2 98 ? 97.458 -53.480 33.883 1.00 89.81 ? 98 PHE B CE2 1 ATOM 4899 C CZ . PHE B 2 98 ? 97.308 -54.795 34.306 1.00 92.62 ? 98 PHE B CZ 1 ATOM 4900 N N . ASN B 2 99 ? 91.178 -50.443 33.996 1.00 75.82 ? 99 ASN B N 1 ATOM 4901 C CA . ASN B 2 99 ? 90.259 -49.371 33.640 1.00 80.87 ? 99 ASN B CA 1 ATOM 4902 C C . ASN B 2 99 ? 90.360 -48.221 34.657 1.00 83.19 ? 99 ASN B C 1 ATOM 4903 O O . ASN B 2 99 ? 89.440 -47.958 35.436 1.00 79.97 ? 99 ASN B O 1 ATOM 4904 C CB . ASN B 2 99 ? 88.826 -49.897 33.545 1.00 84.15 ? 99 ASN B CB 1 ATOM 4905 C CG . ASN B 2 99 ? 88.756 -51.317 33.007 1.00 81.59 ? 99 ASN B CG 1 ATOM 4906 O OD1 . ASN B 2 99 ? 89.213 -52.266 33.638 1.00 79.81 ? 99 ASN B OD1 1 ATOM 4907 N ND2 . ASN B 2 99 ? 88.162 -51.465 31.840 1.00 90.42 ? 99 ASN B ND2 1 ATOM 4908 N N . GLN B 2 100 ? 91.508 -47.552 34.637 1.00 81.59 ? 100 GLN B N 1 ATOM 4909 C CA . GLN B 2 100 ? 91.793 -46.396 35.481 1.00 79.83 ? 100 GLN B CA 1 ATOM 4910 C C . GLN B 2 100 ? 90.831 -45.218 35.292 1.00 79.24 ? 100 GLN B C 1 ATOM 4911 O O . GLN B 2 100 ? 90.946 -44.211 35.980 1.00 90.48 ? 100 GLN B O 1 ATOM 4912 C CB . GLN B 2 100 ? 93.217 -45.890 35.201 1.00 91.02 ? 100 GLN B CB 1 ATOM 4913 C CG . GLN B 2 100 ? 94.309 -46.936 35.319 1.00 111.83 ? 100 GLN B CG 1 ATOM 4914 C CD . GLN B 2 100 ? 94.530 -47.375 36.758 1.00 138.33 ? 100 GLN B CD 1 ATOM 4915 O OE1 . GLN B 2 100 ? 93.874 -46.880 37.682 1.00 136.10 ? 100 GLN B OE1 1 ATOM 4916 N NE2 . GLN B 2 100 ? 95.460 -48.309 36.956 1.00 151.71 ? 100 GLN B NE2 1 ATOM 4917 N N . ASP B 2 101 ? 89.901 -45.315 34.356 1.00 67.88 ? 101 ASP B N 1 ATOM 4918 C CA . ASP B 2 101 ? 89.110 -44.147 34.007 1.00 71.00 ? 101 ASP B CA 1 ATOM 4919 C C . ASP B 2 101 ? 87.635 -44.376 34.279 1.00 76.59 ? 101 ASP B C 1 ATOM 4920 O O . ASP B 2 101 ? 86.805 -43.485 34.064 1.00 79.37 ? 101 ASP B O 1 ATOM 4921 C CB . ASP B 2 101 ? 89.311 -43.789 32.531 1.00 91.89 ? 101 ASP B CB 1 ATOM 4922 C CG . ASP B 2 101 ? 90.635 -43.086 32.269 1.00 105.74 ? 101 ASP B CG 1 ATOM 4923 O OD1 . ASP B 2 101 ? 91.323 -42.715 33.247 1.00 111.35 ? 101 ASP B OD1 1 ATOM 4924 O OD2 . ASP B 2 101 ? 90.984 -42.904 31.081 1.00 105.27 ? 101 ASP B OD2 1 ATOM 4925 N N . LEU B 2 102 ? 87.315 -45.577 34.752 1.00 69.93 ? 102 LEU B N 1 ATOM 4926 C CA . LEU B 2 102 ? 85.928 -45.972 34.942 1.00 58.25 ? 102 LEU B CA 1 ATOM 4927 C C . LEU B 2 102 ? 85.238 -45.099 35.990 1.00 67.75 ? 102 LEU B C 1 ATOM 4928 O O . LEU B 2 102 ? 85.626 -45.096 37.173 1.00 70.97 ? 102 LEU B O 1 ATOM 4929 C CB . LEU B 2 102 ? 85.850 -47.454 35.315 1.00 57.46 ? 102 LEU B CB 1 ATOM 4930 C CG . LEU B 2 102 ? 84.453 -48.071 35.431 1.00 65.99 ? 102 LEU B CG 1 ATOM 4931 C CD1 . LEU B 2 102 ? 83.758 -48.195 34.081 1.00 57.83 ? 102 LEU B CD1 1 ATOM 4932 C CD2 . LEU B 2 102 ? 84.563 -49.427 36.101 1.00 79.13 ? 102 LEU B CD2 1 ATOM 4933 N N . GLU B 2 103 ? 84.225 -44.350 35.559 1.00 64.71 ? 103 GLU B N 1 ATOM 4934 C CA . GLU B 2 103 ? 83.479 -43.515 36.497 1.00 75.38 ? 103 GLU B CA 1 ATOM 4935 C C . GLU B 2 103 ? 82.013 -43.899 36.714 1.00 75.22 ? 103 GLU B C 1 ATOM 4936 O O . GLU B 2 103 ? 81.406 -43.498 37.708 1.00 79.40 ? 103 GLU B O 1 ATOM 4937 C CB . GLU B 2 103 ? 83.609 -42.032 36.156 1.00 74.17 ? 103 GLU B CB 1 ATOM 4938 C CG . GLU B 2 103 ? 83.550 -41.692 34.701 1.00 77.40 ? 103 GLU B CG 1 ATOM 4939 C CD . GLU B 2 103 ? 84.138 -40.319 34.436 1.00 93.50 ? 103 GLU B CD 1 ATOM 4940 O OE1 . GLU B 2 103 ? 83.386 -39.422 33.996 1.00 98.88 ? 103 GLU B OE1 1 ATOM 4941 O OE2 . GLU B 2 103 ? 85.349 -40.129 34.694 1.00 94.99 ? 103 GLU B OE2 1 ATOM 4942 N N . TYR B 2 104 ? 81.447 -44.680 35.804 1.00 67.29 ? 104 TYR B N 1 ATOM 4943 C CA . TYR B 2 104 ? 80.062 -45.110 35.956 1.00 58.13 ? 104 TYR B CA 1 ATOM 4944 C C . TYR B 2 104 ? 79.977 -46.626 35.823 1.00 61.41 ? 104 TYR B C 1 ATOM 4945 O O . TYR B 2 104 ? 80.282 -47.193 34.776 1.00 64.89 ? 104 TYR B O 1 ATOM 4946 C CB . TYR B 2 104 ? 79.165 -44.375 34.955 1.00 47.09 ? 104 TYR B CB 1 ATOM 4947 C CG . TYR B 2 104 ? 77.703 -44.769 34.915 1.00 51.09 ? 104 TYR B CG 1 ATOM 4948 C CD1 . TYR B 2 104 ? 76.701 -43.813 35.038 1.00 35.19 ? 104 TYR B CD1 1 ATOM 4949 C CD2 . TYR B 2 104 ? 77.322 -46.090 34.702 1.00 65.09 ? 104 TYR B CD2 1 ATOM 4950 C CE1 . TYR B 2 104 ? 75.350 -44.169 34.972 1.00 47.97 ? 104 TYR B CE1 1 ATOM 4951 C CE2 . TYR B 2 104 ? 75.983 -46.463 34.643 1.00 64.77 ? 104 TYR B CE2 1 ATOM 4952 C CZ . TYR B 2 104 ? 74.999 -45.502 34.774 1.00 60.41 ? 104 TYR B CZ 1 ATOM 4953 O OH . TYR B 2 104 ? 73.675 -45.894 34.698 1.00 58.11 ? 104 TYR B OH 1 ATOM 4954 N N . LEU B 2 105 ? 79.579 -47.272 36.913 1.00 62.98 ? 105 LEU B N 1 ATOM 4955 C CA . LEU B 2 105 ? 79.414 -48.715 36.955 1.00 67.01 ? 105 LEU B CA 1 ATOM 4956 C C . LEU B 2 105 ? 78.026 -49.044 37.500 1.00 64.17 ? 105 LEU B C 1 ATOM 4957 O O . LEU B 2 105 ? 77.679 -48.642 38.607 1.00 62.47 ? 105 LEU B O 1 ATOM 4958 C CB . LEU B 2 105 ? 80.506 -49.341 37.828 1.00 71.98 ? 105 LEU B CB 1 ATOM 4959 C CG . LEU B 2 105 ? 80.389 -50.823 38.191 1.00 68.25 ? 105 LEU B CG 1 ATOM 4960 C CD1 . LEU B 2 105 ? 80.020 -51.638 36.979 1.00 67.00 ? 105 LEU B CD1 1 ATOM 4961 C CD2 . LEU B 2 105 ? 81.690 -51.326 38.800 1.00 64.10 ? 105 LEU B CD2 1 ATOM 4962 N N . ASP B 2 106 ? 77.228 -49.753 36.706 1.00 63.84 ? 106 ASP B N 1 ATOM 4963 C CA . ASP B 2 106 ? 75.869 -50.126 37.100 1.00 73.60 ? 106 ASP B CA 1 ATOM 4964 C C . ASP B 2 106 ? 75.700 -51.643 37.077 1.00 74.51 ? 106 ASP B C 1 ATOM 4965 O O . ASP B 2 106 ? 75.480 -52.239 36.025 1.00 80.19 ? 106 ASP B O 1 ATOM 4966 C CB . ASP B 2 106 ? 74.825 -49.451 36.192 1.00 72.44 ? 106 ASP B CB 1 ATOM 4967 C CG . ASP B 2 106 ? 73.397 -49.923 36.472 1.00 71.87 ? 106 ASP B CG 1 ATOM 4968 O OD1 . ASP B 2 106 ? 73.079 -50.273 37.625 1.00 77.33 ? 106 ASP B OD1 1 ATOM 4969 O OD2 . ASP B 2 106 ? 72.582 -49.938 35.532 1.00 69.52 ? 106 ASP B OD2 1 ATOM 4970 N N . VAL B 2 107 ? 75.811 -52.264 38.244 1.00 67.67 ? 107 VAL B N 1 ATOM 4971 C CA . VAL B 2 107 ? 75.645 -53.703 38.347 1.00 63.33 ? 107 VAL B CA 1 ATOM 4972 C C . VAL B 2 107 ? 74.354 -54.021 39.101 1.00 68.82 ? 107 VAL B C 1 ATOM 4973 O O . VAL B 2 107 ? 74.241 -55.053 39.759 1.00 72.87 ? 107 VAL B O 1 ATOM 4974 C CB . VAL B 2 107 ? 76.851 -54.374 39.032 1.00 61.46 ? 107 VAL B CB 1 ATOM 4975 C CG1 . VAL B 2 107 ? 76.897 -55.835 38.673 1.00 63.16 ? 107 VAL B CG1 1 ATOM 4976 C CG2 . VAL B 2 107 ? 78.139 -53.708 38.600 1.00 57.88 ? 107 VAL B CG2 1 ATOM 4977 N N . SER B 2 108 ? 73.378 -53.126 38.993 1.00 64.99 ? 108 SER B N 1 ATOM 4978 C CA . SER B 2 108 ? 72.074 -53.345 39.602 1.00 63.00 ? 108 SER B CA 1 ATOM 4979 C C . SER B 2 108 ? 71.448 -54.626 39.075 1.00 60.68 ? 108 SER B C 1 ATOM 4980 O O . SER B 2 108 ? 72.002 -55.287 38.211 1.00 67.14 ? 108 SER B O 1 ATOM 4981 C CB . SER B 2 108 ? 71.151 -52.178 39.290 1.00 63.84 ? 108 SER B CB 1 ATOM 4982 O OG . SER B 2 108 ? 70.917 -52.114 37.898 1.00 66.93 ? 108 SER B OG 1 ATOM 4983 N N . HIS B 2 109 ? 70.293 -54.980 39.614 1.00 59.50 ? 109 HIS B N 1 ATOM 4984 C CA . HIS B 2 109 ? 69.515 -56.106 39.110 1.00 58.10 ? 109 HIS B CA 1 ATOM 4985 C C . HIS B 2 109 ? 70.324 -57.332 38.705 1.00 58.43 ? 109 HIS B C 1 ATOM 4986 O O . HIS B 2 109 ? 70.016 -57.984 37.720 1.00 65.45 ? 109 HIS B O 1 ATOM 4987 C CB . HIS B 2 109 ? 68.623 -55.647 37.956 1.00 48.19 ? 109 HIS B CB 1 ATOM 4988 C CG . HIS B 2 109 ? 67.626 -54.608 38.358 1.00 60.37 ? 109 HIS B CG 1 ATOM 4989 N ND1 . HIS B 2 109 ? 66.417 -54.925 38.941 1.00 63.22 ? 109 HIS B ND1 1 ATOM 4990 C CD2 . HIS B 2 109 ? 67.669 -53.255 38.288 1.00 64.13 ? 109 HIS B CD2 1 ATOM 4991 C CE1 . HIS B 2 109 ? 65.750 -53.811 39.197 1.00 61.83 ? 109 HIS B CE1 1 ATOM 4992 N NE2 . HIS B 2 109 ? 66.488 -52.784 38.812 1.00 62.63 ? 109 HIS B NE2 1 ATOM 4993 N N . ASN B 2 110 ? 71.360 -57.649 39.462 1.00 57.30 ? 110 ASN B N 1 ATOM 4994 C CA . ASN B 2 110 ? 72.019 -58.929 39.284 1.00 66.78 ? 110 ASN B CA 1 ATOM 4995 C C . ASN B 2 110 ? 71.628 -59.868 40.417 1.00 74.79 ? 110 ASN B C 1 ATOM 4996 O O . ASN B 2 110 ? 70.484 -59.858 40.880 1.00 70.57 ? 110 ASN B O 1 ATOM 4997 C CB . ASN B 2 110 ? 73.540 -58.780 39.212 1.00 69.34 ? 110 ASN B CB 1 ATOM 4998 C CG . ASN B 2 110 ? 74.011 -58.224 37.884 1.00 69.98 ? 110 ASN B CG 1 ATOM 4999 O OD1 . ASN B 2 110 ? 73.657 -57.113 37.509 1.00 68.99 ? 110 ASN B OD1 1 ATOM 5000 N ND2 . ASN B 2 110 ? 74.825 -58.993 37.172 1.00 74.29 ? 110 ASN B ND2 1 ATOM 5001 N N . ARG B 2 111 ? 72.586 -60.678 40.855 1.00 78.70 ? 111 ARG B N 1 ATOM 5002 C CA . ARG B 2 111 ? 72.375 -61.597 41.961 1.00 85.82 ? 111 ARG B CA 1 ATOM 5003 C C . ARG B 2 111 ? 73.554 -61.524 42.931 1.00 92.20 ? 111 ARG B C 1 ATOM 5004 O O . ARG B 2 111 ? 73.908 -62.503 43.596 1.00 100.85 ? 111 ARG B O 1 ATOM 5005 C CB . ARG B 2 111 ? 72.180 -63.021 41.447 1.00 86.70 ? 111 ARG B CB 1 ATOM 5006 C CG . ARG B 2 111 ? 70.907 -63.224 40.662 1.00 93.07 ? 111 ARG B CG 1 ATOM 5007 C CD . ARG B 2 111 ? 70.557 -64.695 40.615 1.00 116.53 ? 111 ARG B CD 1 ATOM 5008 N NE . ARG B 2 111 ? 69.894 -65.079 39.371 1.00 131.37 ? 111 ARG B NE 1 ATOM 5009 C CZ . ARG B 2 111 ? 70.492 -65.729 38.375 1.00 132.78 ? 111 ARG B CZ 1 ATOM 5010 N NH1 . ARG B 2 111 ? 71.774 -66.072 38.475 1.00 129.26 ? 111 ARG B NH1 1 ATOM 5011 N NH2 . ARG B 2 111 ? 69.806 -66.042 37.282 1.00 130.46 ? 111 ARG B NH2 1 ATOM 5012 N N . LEU B 2 112 ? 74.150 -60.343 43.005 1.00 83.04 ? 112 LEU B N 1 ATOM 5013 C CA . LEU B 2 112 ? 75.296 -60.104 43.862 1.00 79.56 ? 112 LEU B CA 1 ATOM 5014 C C . LEU B 2 112 ? 75.028 -60.468 45.323 1.00 84.11 ? 112 LEU B C 1 ATOM 5015 O O . LEU B 2 112 ? 73.911 -60.320 45.817 1.00 88.35 ? 112 LEU B O 1 ATOM 5016 C CB . LEU B 2 112 ? 75.719 -58.639 43.753 1.00 75.71 ? 112 LEU B CB 1 ATOM 5017 C CG . LEU B 2 112 ? 76.350 -58.211 42.429 1.00 61.79 ? 112 LEU B CG 1 ATOM 5018 C CD1 . LEU B 2 112 ? 76.682 -56.723 42.453 1.00 52.71 ? 112 LEU B CD1 1 ATOM 5019 C CD2 . LEU B 2 112 ? 77.587 -59.040 42.176 1.00 61.18 ? 112 LEU B CD2 1 ATOM 5020 N N . GLN B 2 113 ? 76.067 -60.940 46.006 1.00 81.50 ? 113 GLN B N 1 ATOM 5021 C CA . GLN B 2 113 ? 75.986 -61.263 47.423 1.00 77.10 ? 113 GLN B CA 1 ATOM 5022 C C . GLN B 2 113 ? 77.341 -61.054 48.111 1.00 87.69 ? 113 GLN B C 1 ATOM 5023 O O . GLN B 2 113 ? 77.398 -60.826 49.319 1.00 103.90 ? 113 GLN B O 1 ATOM 5024 C CB . GLN B 2 113 ? 75.486 -62.695 47.616 1.00 80.27 ? 113 GLN B CB 1 ATOM 5025 C CG . GLN B 2 113 ? 76.405 -63.761 47.039 1.00 97.72 ? 113 GLN B CG 1 ATOM 5026 C CD . GLN B 2 113 ? 75.794 -65.153 47.074 1.00 106.58 ? 113 GLN B CD 1 ATOM 5027 O OE1 . GLN B 2 113 ? 74.582 -65.306 47.265 1.00 103.21 ? 113 GLN B OE1 1 ATOM 5028 N NE2 . GLN B 2 113 ? 76.634 -66.181 46.886 1.00 104.10 ? 113 GLN B NE2 1 ATOM 5029 N N . ASN B 2 114 ? 78.426 -61.140 47.341 1.00 74.42 ? 114 ASN B N 1 ATOM 5030 C CA . ASN B 2 114 ? 79.770 -60.844 47.835 1.00 75.16 ? 114 ASN B CA 1 ATOM 5031 C C . ASN B 2 114 ? 80.388 -59.739 46.961 1.00 81.48 ? 114 ASN B C 1 ATOM 5032 O O . ASN B 2 114 ? 80.017 -59.588 45.798 1.00 89.26 ? 114 ASN B O 1 ATOM 5033 C CB . ASN B 2 114 ? 80.636 -62.122 47.845 1.00 75.01 ? 114 ASN B CB 1 ATOM 5034 C CG . ASN B 2 114 ? 81.897 -62.009 48.750 1.00 109.80 ? 114 ASN B CG 1 ATOM 5035 O OD1 . ASN B 2 114 ? 82.026 -61.092 49.565 1.00 106.44 ? 114 ASN B OD1 1 ATOM 5036 N ND2 . ASN B 2 114 ? 82.818 -62.965 48.602 1.00 105.07 ? 114 ASN B ND2 1 ATOM 5037 N N . ILE B 2 115 ? 81.325 -58.974 47.519 1.00 77.85 ? 115 ILE B N 1 ATOM 5038 C CA . ILE B 2 115 ? 81.888 -57.798 46.853 1.00 66.90 ? 115 ILE B CA 1 ATOM 5039 C C . ILE B 2 115 ? 83.252 -57.391 47.452 1.00 70.14 ? 115 ILE B C 1 ATOM 5040 O O . ILE B 2 115 ? 83.395 -57.275 48.667 1.00 62.91 ? 115 ILE B O 1 ATOM 5041 C CB . ILE B 2 115 ? 80.895 -56.607 46.955 1.00 53.39 ? 115 ILE B CB 1 ATOM 5042 C CG1 . ILE B 2 115 ? 79.940 -56.582 45.781 1.00 64.26 ? 115 ILE B CG1 1 ATOM 5043 C CG2 . ILE B 2 115 ? 81.601 -55.281 46.973 1.00 50.40 ? 115 ILE B CG2 1 ATOM 5044 C CD1 . ILE B 2 115 ? 79.307 -55.239 45.625 1.00 72.78 ? 115 ILE B CD1 1 ATOM 5045 N N . SER B 2 116 ? 84.260 -57.179 46.609 1.00 83.35 ? 116 SER B N 1 ATOM 5046 C CA . SER B 2 116 ? 85.533 -56.645 47.096 1.00 88.94 ? 116 SER B CA 1 ATOM 5047 C C . SER B 2 116 ? 85.246 -55.404 47.930 1.00 96.11 ? 116 SER B C 1 ATOM 5048 O O . SER B 2 116 ? 84.341 -54.637 47.612 1.00 90.13 ? 116 SER B O 1 ATOM 5049 C CB . SER B 2 116 ? 86.479 -56.298 45.939 1.00 83.82 ? 116 SER B CB 1 ATOM 5050 O OG . SER B 2 116 ? 87.575 -55.501 46.381 1.00 83.18 ? 116 SER B OG 1 ATOM 5051 N N . CYS B 2 117 ? 86.007 -55.204 49.000 1.00 104.38 ? 117 CYS B N 1 ATOM 5052 C CA . CYS B 2 117 ? 85.741 -54.085 49.900 1.00 102.08 ? 117 CYS B CA 1 ATOM 5053 C C . CYS B 2 117 ? 86.215 -52.735 49.350 1.00 104.96 ? 117 CYS B C 1 ATOM 5054 O O . CYS B 2 117 ? 85.754 -51.681 49.798 1.00 103.85 ? 117 CYS B O 1 ATOM 5055 C CB . CYS B 2 117 ? 86.326 -54.347 51.293 1.00 96.24 ? 117 CYS B CB 1 ATOM 5056 S SG . CYS B 2 117 ? 85.185 -55.100 52.512 1.00 170.39 ? 117 CYS B SG 1 ATOM 5057 N N . CYS B 2 118 ? 87.114 -52.757 48.368 1.00 104.00 ? 118 CYS B N 1 ATOM 5058 C CA . CYS B 2 118 ? 87.644 -51.503 47.840 1.00 95.59 ? 118 CYS B CA 1 ATOM 5059 C C . CYS B 2 118 ? 87.322 -51.218 46.368 1.00 96.60 ? 118 CYS B C 1 ATOM 5060 O O . CYS B 2 118 ? 88.068 -51.630 45.470 1.00 99.38 ? 118 CYS B O 1 ATOM 5061 C CB . CYS B 2 118 ? 89.144 -51.410 48.077 1.00 90.18 ? 118 CYS B CB 1 ATOM 5062 S SG . CYS B 2 118 ? 89.726 -49.714 48.060 1.00 134.81 ? 118 CYS B SG 1 ATOM 5063 N N . PRO B 2 119 ? 86.207 -50.499 46.128 1.00 84.19 ? 119 PRO B N 1 ATOM 5064 C CA . PRO B 2 119 ? 85.775 -49.986 44.828 1.00 72.66 ? 119 PRO B CA 1 ATOM 5065 C C . PRO B 2 119 ? 86.753 -48.961 44.288 1.00 78.93 ? 119 PRO B C 1 ATOM 5066 O O . PRO B 2 119 ? 87.378 -48.241 45.063 1.00 68.67 ? 119 PRO B O 1 ATOM 5067 C CB . PRO B 2 119 ? 84.453 -49.284 45.155 1.00 65.37 ? 119 PRO B CB 1 ATOM 5068 C CG . PRO B 2 119 ? 83.970 -49.938 46.364 1.00 66.66 ? 119 PRO B CG 1 ATOM 5069 C CD . PRO B 2 119 ? 85.201 -50.225 47.166 1.00 79.20 ? 119 PRO B CD 1 ATOM 5070 N N . MET B 2 120 ? 86.864 -48.889 42.965 1.00 88.11 ? 120 MET B N 1 ATOM 5071 C CA . MET B 2 120 ? 87.800 -47.975 42.314 1.00 73.19 ? 120 MET B CA 1 ATOM 5072 C C . MET B 2 120 ? 87.525 -46.510 42.668 1.00 65.85 ? 120 MET B C 1 ATOM 5073 O O . MET B 2 120 ? 86.383 -46.042 42.645 1.00 53.73 ? 120 MET B O 1 ATOM 5074 C CB . MET B 2 120 ? 87.811 -48.198 40.794 1.00 67.44 ? 120 MET B CB 1 ATOM 5075 C CG . MET B 2 120 ? 86.422 -48.351 40.170 1.00 86.51 ? 120 MET B CG 1 ATOM 5076 S SD . MET B 2 120 ? 85.992 -50.029 39.675 1.00 102.63 ? 120 MET B SD 1 ATOM 5077 C CE . MET B 2 120 ? 87.241 -50.926 40.584 1.00 60.60 ? 120 MET B CE 1 ATOM 5078 N N . ALA B 2 121 ? 88.588 -45.791 43.008 1.00 72.80 ? 121 ALA B N 1 ATOM 5079 C CA . ALA B 2 121 ? 88.469 -44.400 43.431 1.00 75.94 ? 121 ALA B CA 1 ATOM 5080 C C . ALA B 2 121 ? 87.950 -43.494 42.314 1.00 75.55 ? 121 ALA B C 1 ATOM 5081 O O . ALA B 2 121 ? 87.559 -42.350 42.553 1.00 67.76 ? 121 ALA B O 1 ATOM 5082 C CB . ALA B 2 121 ? 89.809 -43.896 43.956 1.00 75.11 ? 121 ALA B CB 1 ATOM 5083 N N . SER B 2 122 ? 87.945 -44.017 41.094 1.00 82.24 ? 122 SER B N 1 ATOM 5084 C CA . SER B 2 122 ? 87.495 -43.257 39.935 1.00 77.80 ? 122 SER B CA 1 ATOM 5085 C C . SER B 2 122 ? 85.971 -43.130 39.830 1.00 72.13 ? 122 SER B C 1 ATOM 5086 O O . SER B 2 122 ? 85.459 -42.366 39.014 1.00 56.24 ? 122 SER B O 1 ATOM 5087 C CB . SER B 2 122 ? 88.028 -43.894 38.670 1.00 73.97 ? 122 SER B CB 1 ATOM 5088 O OG . SER B 2 122 ? 87.969 -42.938 37.638 1.00 91.04 ? 122 SER B OG 1 ATOM 5089 N N . LEU B 2 123 ? 85.263 -43.878 40.671 1.00 74.38 ? 123 LEU B N 1 ATOM 5090 C CA . LEU B 2 123 ? 83.809 -43.958 40.631 1.00 76.07 ? 123 LEU B CA 1 ATOM 5091 C C . LEU B 2 123 ? 83.111 -42.632 40.929 1.00 77.23 ? 123 LEU B C 1 ATOM 5092 O O . LEU B 2 123 ? 83.521 -41.898 41.830 1.00 87.28 ? 123 LEU B O 1 ATOM 5093 C CB . LEU B 2 123 ? 83.321 -45.049 41.592 1.00 70.94 ? 123 LEU B CB 1 ATOM 5094 C CG . LEU B 2 123 ? 83.030 -46.420 40.974 1.00 69.63 ? 123 LEU B CG 1 ATOM 5095 C CD1 . LEU B 2 123 ? 83.463 -46.472 39.507 1.00 80.22 ? 123 LEU B CD1 1 ATOM 5096 C CD2 . LEU B 2 123 ? 83.676 -47.545 41.773 1.00 56.96 ? 123 LEU B CD2 1 ATOM 5097 N N . ARG B 2 124 ? 82.068 -42.336 40.151 1.00 66.43 ? 124 ARG B N 1 ATOM 5098 C CA . ARG B 2 124 ? 81.191 -41.196 40.399 1.00 64.82 ? 124 ARG B CA 1 ATOM 5099 C C . ARG B 2 124 ? 79.773 -41.715 40.479 1.00 66.62 ? 124 ARG B C 1 ATOM 5100 O O . ARG B 2 124 ? 78.897 -41.078 41.061 1.00 75.46 ? 124 ARG B O 1 ATOM 5101 C CB . ARG B 2 124 ? 81.304 -40.125 39.303 1.00 66.06 ? 124 ARG B CB 1 ATOM 5102 C CG . ARG B 2 124 ? 82.720 -39.643 39.069 1.00 77.34 ? 124 ARG B CG 1 ATOM 5103 C CD . ARG B 2 124 ? 82.795 -38.291 38.385 1.00 87.63 ? 124 ARG B CD 1 ATOM 5104 N NE . ARG B 2 124 ? 84.159 -37.763 38.456 1.00 107.58 ? 124 ARG B NE 1 ATOM 5105 C CZ . ARG B 2 124 ? 84.477 -36.479 38.319 1.00 120.28 ? 124 ARG B CZ 1 ATOM 5106 N NH1 . ARG B 2 124 ? 83.524 -35.581 38.096 1.00 124.18 ? 124 ARG B NH1 1 ATOM 5107 N NH2 . ARG B 2 124 ? 85.745 -36.090 38.410 1.00 120.08 ? 124 ARG B NH2 1 ATOM 5108 N N . HIS B 2 125 ? 79.555 -42.890 39.903 1.00 55.96 ? 125 HIS B N 1 ATOM 5109 C CA . HIS B 2 125 ? 78.242 -43.521 39.945 1.00 55.96 ? 125 HIS B CA 1 ATOM 5110 C C . HIS B 2 125 ? 78.404 -45.029 40.116 1.00 61.47 ? 125 HIS B C 1 ATOM 5111 O O . HIS B 2 125 ? 78.864 -45.727 39.219 1.00 64.83 ? 125 HIS B O 1 ATOM 5112 C CB . HIS B 2 125 ? 77.447 -43.166 38.687 1.00 54.71 ? 125 HIS B CB 1 ATOM 5113 C CG . HIS B 2 125 ? 76.140 -43.882 38.563 1.00 61.06 ? 125 HIS B CG 1 ATOM 5114 N ND1 . HIS B 2 125 ? 74.938 -43.216 38.464 1.00 68.10 ? 125 HIS B ND1 1 ATOM 5115 C CD2 . HIS B 2 125 ? 75.846 -45.203 38.493 1.00 64.79 ? 125 HIS B CD2 1 ATOM 5116 C CE1 . HIS B 2 125 ? 73.958 -44.096 38.347 1.00 71.21 ? 125 HIS B CE1 1 ATOM 5117 N NE2 . HIS B 2 125 ? 74.481 -45.310 38.363 1.00 67.34 ? 125 HIS B NE2 1 ATOM 5118 N N . LEU B 2 126 ? 78.043 -45.520 41.294 1.00 62.61 ? 126 LEU B N 1 ATOM 5119 C CA . LEU B 2 126 ? 78.157 -46.933 41.601 1.00 61.12 ? 126 LEU B CA 1 ATOM 5120 C C . LEU B 2 126 ? 76.790 -47.485 41.989 1.00 61.70 ? 126 LEU B C 1 ATOM 5121 O O . LEU B 2 126 ? 76.247 -47.131 43.024 1.00 59.08 ? 126 LEU B O 1 ATOM 5122 C CB . LEU B 2 126 ? 79.169 -47.138 42.725 1.00 63.46 ? 126 LEU B CB 1 ATOM 5123 C CG . LEU B 2 126 ? 79.284 -48.537 43.329 1.00 69.08 ? 126 LEU B CG 1 ATOM 5124 C CD1 . LEU B 2 126 ? 79.406 -49.581 42.253 1.00 76.20 ? 126 LEU B CD1 1 ATOM 5125 C CD2 . LEU B 2 126 ? 80.481 -48.598 44.242 1.00 73.04 ? 126 LEU B CD2 1 ATOM 5126 N N . ASP B 2 127 ? 76.229 -48.346 41.145 1.00 68.11 ? 127 ASP B N 1 ATOM 5127 C CA . ASP B 2 127 ? 74.899 -48.890 41.392 1.00 67.93 ? 127 ASP B CA 1 ATOM 5128 C C . ASP B 2 127 ? 74.937 -50.386 41.684 1.00 69.29 ? 127 ASP B C 1 ATOM 5129 O O . ASP B 2 127 ? 75.225 -51.186 40.791 1.00 59.06 ? 127 ASP B O 1 ATOM 5130 C CB . ASP B 2 127 ? 73.976 -48.614 40.206 1.00 65.54 ? 127 ASP B CB 1 ATOM 5131 C CG . ASP B 2 127 ? 72.524 -48.844 40.539 1.00 64.45 ? 127 ASP B CG 1 ATOM 5132 O OD1 . ASP B 2 127 ? 72.252 -49.555 41.517 1.00 61.21 ? 127 ASP B OD1 1 ATOM 5133 O OD2 . ASP B 2 127 ? 71.651 -48.317 39.823 1.00 70.94 ? 127 ASP B OD2 1 ATOM 5134 N N . LEU B 2 128 ? 74.647 -50.739 42.941 1.00 67.89 ? 128 LEU B N 1 ATOM 5135 C CA . LEU B 2 128 ? 74.517 -52.130 43.390 1.00 59.28 ? 128 LEU B CA 1 ATOM 5136 C C . LEU B 2 128 ? 73.115 -52.420 43.925 1.00 53.99 ? 128 LEU B C 1 ATOM 5137 O O . LEU B 2 128 ? 72.919 -53.342 44.711 1.00 55.94 ? 128 LEU B O 1 ATOM 5138 C CB . LEU B 2 128 ? 75.540 -52.451 44.483 1.00 54.36 ? 128 LEU B CB 1 ATOM 5139 C CG . LEU B 2 128 ? 76.936 -51.882 44.274 1.00 62.87 ? 128 LEU B CG 1 ATOM 5140 C CD1 . LEU B 2 128 ? 77.744 -52.066 45.524 1.00 57.94 ? 128 LEU B CD1 1 ATOM 5141 C CD2 . LEU B 2 128 ? 77.607 -52.542 43.085 1.00 77.45 ? 128 LEU B CD2 1 ATOM 5142 N N . SER B 2 129 ? 72.138 -51.628 43.507 1.00 56.13 ? 129 SER B N 1 ATOM 5143 C CA . SER B 2 129 ? 70.776 -51.817 43.988 1.00 58.71 ? 129 SER B CA 1 ATOM 5144 C C . SER B 2 129 ? 70.178 -53.079 43.382 1.00 53.65 ? 129 SER B C 1 ATOM 5145 O O . SER B 2 129 ? 70.701 -53.615 42.414 1.00 56.19 ? 129 SER B O 1 ATOM 5146 C CB . SER B 2 129 ? 69.911 -50.590 43.683 1.00 59.15 ? 129 SER B CB 1 ATOM 5147 O OG . SER B 2 129 ? 69.765 -50.411 42.290 1.00 74.44 ? 129 SER B OG 1 ATOM 5148 N N . PHE B 2 130 ? 69.091 -53.555 43.971 1.00 49.34 ? 130 PHE B N 1 ATOM 5149 C CA . PHE B 2 130 ? 68.400 -54.753 43.507 1.00 53.79 ? 130 PHE B CA 1 ATOM 5150 C C . PHE B 2 130 ? 69.330 -55.932 43.282 1.00 60.31 ? 130 PHE B C 1 ATOM 5151 O O . PHE B 2 130 ? 69.452 -56.446 42.176 1.00 72.66 ? 130 PHE B O 1 ATOM 5152 C CB . PHE B 2 130 ? 67.570 -54.446 42.261 1.00 43.61 ? 130 PHE B CB 1 ATOM 5153 C CG . PHE B 2 130 ? 66.633 -53.299 42.450 1.00 52.81 ? 130 PHE B CG 1 ATOM 5154 C CD1 . PHE B 2 130 ? 67.064 -51.996 42.246 1.00 52.04 ? 130 PHE B CD1 1 ATOM 5155 C CD2 . PHE B 2 130 ? 65.331 -53.513 42.871 1.00 58.17 ? 130 PHE B CD2 1 ATOM 5156 C CE1 . PHE B 2 130 ? 66.207 -50.927 42.440 1.00 54.82 ? 130 PHE B CE1 1 ATOM 5157 C CE2 . PHE B 2 130 ? 64.467 -52.443 43.073 1.00 64.50 ? 130 PHE B CE2 1 ATOM 5158 C CZ . PHE B 2 130 ? 64.905 -51.151 42.855 1.00 60.57 ? 130 PHE B CZ 1 ATOM 5159 N N . ASN B 2 131 ? 70.000 -56.348 44.342 1.00 57.68 ? 131 ASN B N 1 ATOM 5160 C CA . ASN B 2 131 ? 70.765 -57.580 44.311 1.00 65.89 ? 131 ASN B CA 1 ATOM 5161 C C . ASN B 2 131 ? 70.373 -58.427 45.501 1.00 76.47 ? 131 ASN B C 1 ATOM 5162 O O . ASN B 2 131 ? 69.337 -58.185 46.119 1.00 78.83 ? 131 ASN B O 1 ATOM 5163 C CB . ASN B 2 131 ? 72.261 -57.306 44.318 1.00 59.60 ? 131 ASN B CB 1 ATOM 5164 C CG . ASN B 2 131 ? 72.692 -56.477 43.143 1.00 61.96 ? 131 ASN B CG 1 ATOM 5165 O OD1 . ASN B 2 131 ? 72.570 -55.256 43.160 1.00 69.21 ? 131 ASN B OD1 1 ATOM 5166 N ND2 . ASN B 2 131 ? 73.197 -57.131 42.109 1.00 53.12 ? 131 ASN B ND2 1 ATOM 5167 N N . ASP B 2 132 ? 71.195 -59.416 45.826 1.00 79.05 ? 132 ASP B N 1 ATOM 5168 C CA . ASP B 2 132 ? 70.847 -60.320 46.907 1.00 89.78 ? 132 ASP B CA 1 ATOM 5169 C C . ASP B 2 132 ? 71.797 -60.200 48.094 1.00 86.30 ? 132 ASP B C 1 ATOM 5170 O O . ASP B 2 132 ? 72.193 -61.193 48.692 1.00 81.46 ? 132 ASP B O 1 ATOM 5171 C CB . ASP B 2 132 ? 70.755 -61.762 46.408 1.00 100.09 ? 132 ASP B CB 1 ATOM 5172 C CG . ASP B 2 132 ? 69.539 -62.484 46.962 1.00 117.33 ? 132 ASP B CG 1 ATOM 5173 O OD1 . ASP B 2 132 ? 68.535 -62.591 46.218 1.00 127.63 ? 132 ASP B OD1 1 ATOM 5174 O OD2 . ASP B 2 132 ? 69.570 -62.911 48.143 1.00 112.97 ? 132 ASP B OD2 1 ATOM 5175 N N . PHE B 2 133 ? 72.144 -58.971 48.441 1.00 86.05 ? 133 PHE B N 1 ATOM 5176 C CA . PHE B 2 133 ? 72.982 -58.735 49.597 1.00 78.55 ? 133 PHE B CA 1 ATOM 5177 C C . PHE B 2 133 ? 72.207 -58.976 50.869 1.00 91.84 ? 133 PHE B C 1 ATOM 5178 O O . PHE B 2 133 ? 71.091 -58.478 51.031 1.00 99.19 ? 133 PHE B O 1 ATOM 5179 C CB . PHE B 2 133 ? 73.527 -57.316 49.589 1.00 64.03 ? 133 PHE B CB 1 ATOM 5180 C CG . PHE B 2 133 ? 74.575 -57.094 48.556 1.00 69.16 ? 133 PHE B CG 1 ATOM 5181 C CD1 . PHE B 2 133 ? 74.336 -56.256 47.473 1.00 72.73 ? 133 PHE B CD1 1 ATOM 5182 C CD2 . PHE B 2 133 ? 75.798 -57.743 48.650 1.00 67.58 ? 133 PHE B CD2 1 ATOM 5183 C CE1 . PHE B 2 133 ? 75.304 -56.055 46.515 1.00 81.69 ? 133 PHE B CE1 1 ATOM 5184 C CE2 . PHE B 2 133 ? 76.777 -57.548 47.699 1.00 72.54 ? 133 PHE B CE2 1 ATOM 5185 C CZ . PHE B 2 133 ? 76.530 -56.703 46.628 1.00 86.22 ? 133 PHE B CZ 1 ATOM 5186 N N . ASP B 2 134 ? 72.812 -59.766 51.752 1.00 97.35 ? 134 ASP B N 1 ATOM 5187 C CA . ASP B 2 134 ? 72.321 -59.981 53.099 1.00 99.98 ? 134 ASP B CA 1 ATOM 5188 C C . ASP B 2 134 ? 72.308 -58.626 53.799 1.00 95.32 ? 134 ASP B C 1 ATOM 5189 O O . ASP B 2 134 ? 71.250 -58.100 54.154 1.00 80.76 ? 134 ASP B O 1 ATOM 5190 C CB . ASP B 2 134 ? 73.262 -60.946 53.830 1.00 111.34 ? 134 ASP B CB 1 ATOM 5191 C CG . ASP B 2 134 ? 72.562 -61.753 54.916 1.00 123.21 ? 134 ASP B CG 1 ATOM 5192 O OD1 . ASP B 2 134 ? 73.215 -62.638 55.514 1.00 123.64 ? 134 ASP B OD1 1 ATOM 5193 O OD2 . ASP B 2 134 ? 71.361 -61.513 55.171 1.00 129.59 ? 134 ASP B OD2 1 ATOM 5194 N N . VAL B 2 135 ? 73.495 -58.054 53.979 1.00 95.69 ? 135 VAL B N 1 ATOM 5195 C CA . VAL B 2 135 ? 73.618 -56.760 54.631 1.00 86.89 ? 135 VAL B CA 1 ATOM 5196 C C . VAL B 2 135 ? 74.351 -55.747 53.748 1.00 85.49 ? 135 VAL B C 1 ATOM 5197 O O . VAL B 2 135 ? 75.255 -56.109 52.995 1.00 93.97 ? 135 VAL B O 1 ATOM 5198 C CB . VAL B 2 135 ? 74.319 -56.891 56.004 1.00 81.47 ? 135 VAL B CB 1 ATOM 5199 C CG1 . VAL B 2 135 ? 75.822 -56.673 55.872 1.00 55.38 ? 135 VAL B CG1 1 ATOM 5200 C CG2 . VAL B 2 135 ? 73.711 -55.902 56.997 1.00 93.98 ? 135 VAL B CG2 1 ATOM 5201 N N . LEU B 2 136 ? 73.937 -54.485 53.834 1.00 80.62 ? 136 LEU B N 1 ATOM 5202 C CA . LEU B 2 136 ? 74.571 -53.385 53.100 1.00 76.88 ? 136 LEU B CA 1 ATOM 5203 C C . LEU B 2 136 ? 76.087 -53.557 52.902 1.00 77.62 ? 136 LEU B C 1 ATOM 5204 O O . LEU B 2 136 ? 76.839 -53.495 53.865 1.00 88.51 ? 136 LEU B O 1 ATOM 5205 C CB . LEU B 2 136 ? 74.291 -52.075 53.834 1.00 76.66 ? 136 LEU B CB 1 ATOM 5206 C CG . LEU B 2 136 ? 73.298 -51.070 53.246 1.00 80.00 ? 136 LEU B CG 1 ATOM 5207 C CD1 . LEU B 2 136 ? 72.425 -51.677 52.141 1.00 83.57 ? 136 LEU B CD1 1 ATOM 5208 C CD2 . LEU B 2 136 ? 72.464 -50.402 54.351 1.00 69.43 ? 136 LEU B CD2 1 ATOM 5209 N N . PRO B 2 137 ? 76.539 -53.735 51.643 1.00 79.92 ? 137 PRO B N 1 ATOM 5210 C CA . PRO B 2 137 ? 77.923 -54.074 51.268 1.00 75.48 ? 137 PRO B CA 1 ATOM 5211 C C . PRO B 2 137 ? 78.937 -52.928 51.377 1.00 77.24 ? 137 PRO B C 1 ATOM 5212 O O . PRO B 2 137 ? 80.046 -53.067 50.868 1.00 79.61 ? 137 PRO B O 1 ATOM 5213 C CB . PRO B 2 137 ? 77.802 -54.456 49.788 1.00 66.27 ? 137 PRO B CB 1 ATOM 5214 C CG . PRO B 2 137 ? 76.349 -54.415 49.463 1.00 63.17 ? 137 PRO B CG 1 ATOM 5215 C CD . PRO B 2 137 ? 75.709 -53.521 50.449 1.00 69.26 ? 137 PRO B CD 1 ATOM 5216 N N . VAL B 2 138 ? 78.564 -51.823 52.010 1.00 79.22 ? 138 VAL B N 1 ATOM 5217 C CA . VAL B 2 138 ? 79.449 -50.676 52.157 1.00 74.79 ? 138 VAL B CA 1 ATOM 5218 C C . VAL B 2 138 ? 80.540 -50.953 53.181 1.00 78.54 ? 138 VAL B C 1 ATOM 5219 O O . VAL B 2 138 ? 80.278 -50.922 54.384 1.00 82.49 ? 138 VAL B O 1 ATOM 5220 C CB . VAL B 2 138 ? 78.664 -49.449 52.635 1.00 69.77 ? 138 VAL B CB 1 ATOM 5221 C CG1 . VAL B 2 138 ? 79.594 -48.251 52.825 1.00 65.00 ? 138 VAL B CG1 1 ATOM 5222 C CG2 . VAL B 2 138 ? 77.550 -49.130 51.658 1.00 66.32 ? 138 VAL B CG2 1 ATOM 5223 N N . CYS B 2 139 ? 81.759 -51.221 52.710 1.00 76.09 ? 139 CYS B N 1 ATOM 5224 C CA . CYS B 2 139 ? 82.893 -51.462 53.605 1.00 76.20 ? 139 CYS B CA 1 ATOM 5225 C C . CYS B 2 139 ? 83.554 -50.143 54.002 1.00 79.14 ? 139 CYS B C 1 ATOM 5226 O O . CYS B 2 139 ? 83.234 -49.093 53.456 1.00 83.30 ? 139 CYS B O 1 ATOM 5227 C CB . CYS B 2 139 ? 83.948 -52.364 52.955 1.00 83.18 ? 139 CYS B CB 1 ATOM 5228 S SG . CYS B 2 139 ? 83.459 -54.014 52.394 1.00 114.15 ? 139 CYS B SG 1 ATOM 5229 N N . LYS B 2 140 ? 84.502 -50.203 54.932 1.00 82.48 ? 140 LYS B N 1 ATOM 5230 C CA . LYS B 2 140 ? 85.143 -48.993 55.435 1.00 85.03 ? 140 LYS B CA 1 ATOM 5231 C C . LYS B 2 140 ? 85.936 -48.232 54.363 1.00 79.40 ? 140 LYS B C 1 ATOM 5232 O O . LYS B 2 140 ? 86.122 -47.018 54.464 1.00 73.60 ? 140 LYS B O 1 ATOM 5233 C CB . LYS B 2 140 ? 86.036 -49.314 56.643 1.00 84.26 ? 140 LYS B CB 1 ATOM 5234 C CG . LYS B 2 140 ? 87.347 -50.012 56.303 1.00 74.42 ? 140 LYS B CG 1 ATOM 5235 C CD . LYS B 2 140 ? 88.316 -49.913 57.462 1.00 69.90 ? 140 LYS B CD 1 ATOM 5236 C CE . LYS B 2 140 ? 89.256 -51.108 57.512 1.00 72.06 ? 140 LYS B CE 1 ATOM 5237 N NZ . LYS B 2 140 ? 90.159 -51.070 58.717 1.00 75.21 ? 140 LYS B NZ 1 ATOM 5238 N N . GLU B 2 141 ? 86.397 -48.941 53.338 1.00 77.51 ? 141 GLU B N 1 ATOM 5239 C CA . GLU B 2 141 ? 87.252 -48.327 52.328 1.00 78.60 ? 141 GLU B CA 1 ATOM 5240 C C . GLU B 2 141 ? 86.472 -47.394 51.410 1.00 80.71 ? 141 GLU B C 1 ATOM 5241 O O . GLU B 2 141 ? 87.063 -46.556 50.724 1.00 80.02 ? 141 GLU B O 1 ATOM 5242 C CB . GLU B 2 141 ? 87.992 -49.386 51.508 1.00 78.08 ? 141 GLU B CB 1 ATOM 5243 C CG . GLU B 2 141 ? 89.146 -50.060 52.230 1.00 78.87 ? 141 GLU B CG 1 ATOM 5244 C CD . GLU B 2 141 ? 88.698 -51.257 53.045 1.00 94.57 ? 141 GLU B CD 1 ATOM 5245 O OE1 . GLU B 2 141 ? 87.482 -51.534 53.064 1.00 96.23 ? 141 GLU B OE1 1 ATOM 5246 O OE2 . GLU B 2 141 ? 89.557 -51.924 53.666 1.00 100.87 ? 141 GLU B OE2 1 ATOM 5247 N N . PHE B 2 142 ? 85.148 -47.546 51.402 1.00 79.75 ? 142 PHE B N 1 ATOM 5248 C CA . PHE B 2 142 ? 84.269 -46.697 50.597 1.00 76.83 ? 142 PHE B CA 1 ATOM 5249 C C . PHE B 2 142 ? 84.504 -45.217 50.881 1.00 66.08 ? 142 PHE B C 1 ATOM 5250 O O . PHE B 2 142 ? 83.973 -44.354 50.197 1.00 66.61 ? 142 PHE B O 1 ATOM 5251 C CB . PHE B 2 142 ? 82.795 -47.040 50.844 1.00 80.67 ? 142 PHE B CB 1 ATOM 5252 C CG . PHE B 2 142 ? 82.326 -48.276 50.132 1.00 79.62 ? 142 PHE B CG 1 ATOM 5253 C CD1 . PHE B 2 142 ? 81.117 -48.276 49.450 1.00 66.82 ? 142 PHE B CD1 1 ATOM 5254 C CD2 . PHE B 2 142 ? 83.093 -49.438 50.143 1.00 78.20 ? 142 PHE B CD2 1 ATOM 5255 C CE1 . PHE B 2 142 ? 80.678 -49.415 48.791 1.00 62.10 ? 142 PHE B CE1 1 ATOM 5256 C CE2 . PHE B 2 142 ? 82.658 -50.582 49.487 1.00 75.99 ? 142 PHE B CE2 1 ATOM 5257 C CZ . PHE B 2 142 ? 81.447 -50.570 48.810 1.00 67.58 ? 142 PHE B CZ 1 ATOM 5258 N N . GLY B 2 143 ? 85.299 -44.928 51.899 1.00 69.76 ? 143 GLY B N 1 ATOM 5259 C CA . GLY B 2 143 ? 85.617 -43.558 52.231 1.00 74.26 ? 143 GLY B CA 1 ATOM 5260 C C . GLY B 2 143 ? 86.531 -42.940 51.199 1.00 84.56 ? 143 GLY B C 1 ATOM 5261 O O . GLY B 2 143 ? 86.502 -41.724 51.025 1.00 89.37 ? 143 GLY B O 1 ATOM 5262 N N . ASN B 2 144 ? 87.328 -43.779 50.523 1.00 87.75 ? 144 ASN B N 1 ATOM 5263 C CA . ASN B 2 144 ? 88.306 -43.339 49.511 1.00 84.12 ? 144 ASN B CA 1 ATOM 5264 C C . ASN B 2 144 ? 87.624 -42.874 48.224 1.00 73.17 ? 144 ASN B C 1 ATOM 5265 O O . ASN B 2 144 ? 88.230 -42.183 47.402 1.00 69.70 ? 144 ASN B O 1 ATOM 5266 C CB . ASN B 2 144 ? 89.333 -44.452 49.209 1.00 90.24 ? 144 ASN B CB 1 ATOM 5267 C CG . ASN B 2 144 ? 90.528 -43.960 48.379 1.00 92.71 ? 144 ASN B CG 1 ATOM 5268 O OD1 . ASN B 2 144 ? 90.958 -42.820 48.525 1.00 85.72 ? 144 ASN B OD1 1 ATOM 5269 N ND2 . ASN B 2 144 ? 91.064 -44.835 47.504 1.00 104.04 ? 144 ASN B ND2 1 ATOM 5270 N N . LEU B 2 145 ? 86.360 -43.264 48.066 1.00 67.44 ? 145 LEU B N 1 ATOM 5271 C CA . LEU B 2 145 ? 85.551 -42.867 46.922 1.00 68.30 ? 145 LEU B CA 1 ATOM 5272 C C . LEU B 2 145 ? 85.121 -41.411 47.031 1.00 71.85 ? 145 LEU B C 1 ATOM 5273 O O . LEU B 2 145 ? 83.932 -41.102 46.972 1.00 74.95 ? 145 LEU B O 1 ATOM 5274 C CB . LEU B 2 145 ? 84.309 -43.750 46.810 1.00 64.20 ? 145 LEU B CB 1 ATOM 5275 C CG . LEU B 2 145 ? 84.495 -45.265 46.767 1.00 70.45 ? 145 LEU B CG 1 ATOM 5276 C CD1 . LEU B 2 145 ? 83.236 -45.915 46.216 1.00 66.88 ? 145 LEU B CD1 1 ATOM 5277 C CD2 . LEU B 2 145 ? 85.689 -45.641 45.919 1.00 75.67 ? 145 LEU B CD2 1 ATOM 5278 N N . THR B 2 146 ? 86.092 -40.520 47.179 1.00 66.88 ? 146 THR B N 1 ATOM 5279 C CA . THR B 2 146 ? 85.813 -39.101 47.335 1.00 71.23 ? 146 THR B CA 1 ATOM 5280 C C . THR B 2 146 ? 84.978 -38.526 46.180 1.00 74.47 ? 146 THR B C 1 ATOM 5281 O O . THR B 2 146 ? 84.156 -37.636 46.389 1.00 73.91 ? 146 THR B O 1 ATOM 5282 C CB . THR B 2 146 ? 87.122 -38.294 47.482 1.00 77.81 ? 146 THR B CB 1 ATOM 5283 O OG1 . THR B 2 146 ? 87.277 -37.414 46.362 1.00 89.90 ? 146 THR B OG1 1 ATOM 5284 C CG2 . THR B 2 146 ? 88.335 -39.228 47.580 1.00 61.73 ? 146 THR B CG2 1 ATOM 5285 N N . LYS B 2 147 ? 85.184 -39.039 44.966 1.00 82.07 ? 147 LYS B N 1 ATOM 5286 C CA . LYS B 2 147 ? 84.485 -38.524 43.778 1.00 80.10 ? 147 LYS B CA 1 ATOM 5287 C C . LYS B 2 147 ? 83.038 -39.035 43.659 1.00 75.85 ? 147 LYS B C 1 ATOM 5288 O O . LYS B 2 147 ? 82.289 -38.598 42.775 1.00 65.54 ? 147 LYS B O 1 ATOM 5289 C CB . LYS B 2 147 ? 85.266 -38.843 42.485 1.00 82.40 ? 147 LYS B CB 1 ATOM 5290 C CG . LYS B 2 147 ? 86.405 -37.856 42.097 1.00 53.17 ? 147 LYS B CG 1 ATOM 5291 C CD . LYS B 2 147 ? 87.197 -38.376 40.856 1.00 166.37 ? 147 LYS B CD 1 ATOM 5292 C CE . LYS B 2 147 ? 88.642 -37.813 40.719 1.00 92.74 ? 147 LYS B CE 1 ATOM 5293 N NZ . LYS B 2 147 ? 89.750 -38.637 41.374 1.00 87.73 ? 147 LYS B NZ 1 ATOM 5294 N N . LEU B 2 148 ? 82.644 -39.934 44.561 1.00 76.67 ? 148 LEU B N 1 ATOM 5295 C CA . LEU B 2 148 ? 81.354 -40.625 44.458 1.00 75.50 ? 148 LEU B CA 1 ATOM 5296 C C . LEU B 2 148 ? 80.145 -39.716 44.625 1.00 75.33 ? 148 LEU B C 1 ATOM 5297 O O . LEU B 2 148 ? 80.071 -38.941 45.576 1.00 80.17 ? 148 LEU B O 1 ATOM 5298 C CB . LEU B 2 148 ? 81.261 -41.771 45.465 1.00 71.39 ? 148 LEU B CB 1 ATOM 5299 C CG . LEU B 2 148 ? 80.014 -42.634 45.248 1.00 67.15 ? 148 LEU B CG 1 ATOM 5300 C CD1 . LEU B 2 148 ? 80.120 -43.328 43.913 1.00 50.28 ? 148 LEU B CD1 1 ATOM 5301 C CD2 . LEU B 2 148 ? 79.799 -43.650 46.374 1.00 71.16 ? 148 LEU B CD2 1 ATOM 5302 N N . THR B 2 149 ? 79.185 -39.839 43.712 1.00 71.39 ? 149 THR B N 1 ATOM 5303 C CA . THR B 2 149 ? 77.995 -38.993 43.748 1.00 73.22 ? 149 THR B CA 1 ATOM 5304 C C . THR B 2 149 ? 76.669 -39.780 43.727 1.00 68.90 ? 149 THR B C 1 ATOM 5305 O O . THR B 2 149 ? 75.664 -39.374 44.336 1.00 63.41 ? 149 THR B O 1 ATOM 5306 C CB . THR B 2 149 ? 78.036 -37.938 42.628 1.00 71.54 ? 149 THR B CB 1 ATOM 5307 O OG1 . THR B 2 149 ? 77.537 -36.703 43.138 1.00 84.73 ? 149 THR B OG1 1 ATOM 5308 C CG2 . THR B 2 149 ? 77.214 -38.367 41.410 1.00 63.12 ? 149 THR B CG2 1 ATOM 5309 N N . PHE B 2 150 ? 76.672 -40.914 43.041 1.00 58.24 ? 150 PHE B N 1 ATOM 5310 C CA . PHE B 2 150 ? 75.513 -41.789 43.057 1.00 61.24 ? 150 PHE B CA 1 ATOM 5311 C C . PHE B 2 150 ? 75.866 -43.125 43.686 1.00 67.92 ? 150 PHE B C 1 ATOM 5312 O O . PHE B 2 150 ? 76.825 -43.780 43.271 1.00 70.08 ? 150 PHE B O 1 ATOM 5313 C CB . PHE B 2 150 ? 74.999 -42.009 41.644 1.00 65.74 ? 150 PHE B CB 1 ATOM 5314 C CG . PHE B 2 150 ? 73.887 -43.004 41.553 1.00 61.57 ? 150 PHE B CG 1 ATOM 5315 C CD1 . PHE B 2 150 ? 72.596 -42.590 41.271 1.00 51.48 ? 150 PHE B CD1 1 ATOM 5316 C CD2 . PHE B 2 150 ? 74.134 -44.357 41.743 1.00 66.51 ? 150 PHE B CD2 1 ATOM 5317 C CE1 . PHE B 2 150 ? 71.573 -43.498 41.184 1.00 56.25 ? 150 PHE B CE1 1 ATOM 5318 C CE2 . PHE B 2 150 ? 73.111 -45.279 41.657 1.00 74.97 ? 150 PHE B CE2 1 ATOM 5319 C CZ . PHE B 2 150 ? 71.827 -44.849 41.374 1.00 68.18 ? 150 PHE B CZ 1 ATOM 5320 N N . LEU B 2 151 ? 75.078 -43.525 44.681 1.00 62.13 ? 151 LEU B N 1 ATOM 5321 C CA . LEU B 2 151 ? 75.267 -44.803 45.352 1.00 53.73 ? 151 LEU B CA 1 ATOM 5322 C C . LEU B 2 151 ? 73.962 -45.589 45.393 1.00 53.59 ? 151 LEU B C 1 ATOM 5323 O O . LEU B 2 151 ? 72.943 -45.085 45.848 1.00 54.42 ? 151 LEU B O 1 ATOM 5324 C CB . LEU B 2 151 ? 75.807 -44.584 46.759 1.00 55.40 ? 151 LEU B CB 1 ATOM 5325 C CG . LEU B 2 151 ? 76.091 -45.863 47.540 1.00 60.19 ? 151 LEU B CG 1 ATOM 5326 C CD1 . LEU B 2 151 ? 76.832 -46.849 46.659 1.00 64.11 ? 151 LEU B CD1 1 ATOM 5327 C CD2 . LEU B 2 151 ? 76.882 -45.550 48.791 1.00 53.45 ? 151 LEU B CD2 1 ATOM 5328 N N . GLY B 2 152 ? 74.000 -46.822 44.897 1.00 55.70 ? 152 GLY B N 1 ATOM 5329 C CA . GLY B 2 152 ? 72.816 -47.655 44.827 1.00 58.86 ? 152 GLY B CA 1 ATOM 5330 C C . GLY B 2 152 ? 73.044 -48.917 45.624 1.00 73.67 ? 152 GLY B C 1 ATOM 5331 O O . GLY B 2 152 ? 74.012 -49.631 45.396 1.00 82.88 ? 152 GLY B O 1 ATOM 5332 N N . LEU B 2 153 ? 72.152 -49.197 46.565 1.00 72.59 ? 153 LEU B N 1 ATOM 5333 C CA . LEU B 2 153 ? 72.349 -50.302 47.488 1.00 65.67 ? 153 LEU B CA 1 ATOM 5334 C C . LEU B 2 153 ? 71.080 -51.118 47.705 1.00 69.54 ? 153 LEU B C 1 ATOM 5335 O O . LEU B 2 153 ? 69.965 -50.642 47.468 1.00 56.44 ? 153 LEU B O 1 ATOM 5336 C CB . LEU B 2 153 ? 72.840 -49.756 48.823 1.00 68.61 ? 153 LEU B CB 1 ATOM 5337 C CG . LEU B 2 153 ? 74.136 -48.967 48.692 1.00 68.50 ? 153 LEU B CG 1 ATOM 5338 C CD1 . LEU B 2 153 ? 74.382 -48.150 49.924 1.00 65.52 ? 153 LEU B CD1 1 ATOM 5339 C CD2 . LEU B 2 153 ? 75.282 -49.920 48.443 1.00 73.34 ? 153 LEU B CD2 1 ATOM 5340 N N . SER B 2 154 ? 71.259 -52.355 48.157 1.00 74.99 ? 154 SER B N 1 ATOM 5341 C CA . SER B 2 154 ? 70.138 -53.180 48.585 1.00 69.48 ? 154 SER B CA 1 ATOM 5342 C C . SER B 2 154 ? 70.574 -54.138 49.673 1.00 74.02 ? 154 SER B C 1 ATOM 5343 O O . SER B 2 154 ? 71.732 -54.554 49.735 1.00 74.96 ? 154 SER B O 1 ATOM 5344 C CB . SER B 2 154 ? 69.558 -53.975 47.427 1.00 67.07 ? 154 SER B CB 1 ATOM 5345 O OG . SER B 2 154 ? 70.305 -55.140 47.176 1.00 78.90 ? 154 SER B OG 1 ATOM 5346 N N . ALA B 2 155 ? 69.629 -54.500 50.524 1.00 76.23 ? 155 ALA B N 1 ATOM 5347 C CA . ALA B 2 155 ? 69.936 -55.358 51.645 1.00 72.44 ? 155 ALA B CA 1 ATOM 5348 C C . ALA B 2 155 ? 68.656 -55.881 52.272 1.00 71.89 ? 155 ALA B C 1 ATOM 5349 O O . ALA B 2 155 ? 67.564 -55.439 51.927 1.00 74.65 ? 155 ALA B O 1 ATOM 5350 C CB . ALA B 2 155 ? 70.749 -54.592 52.656 1.00 71.22 ? 155 ALA B CB 1 ATOM 5351 N N . ALA B 2 156 ? 68.808 -56.826 53.194 1.00 76.03 ? 156 ALA B N 1 ATOM 5352 C CA . ALA B 2 156 ? 67.686 -57.427 53.903 1.00 79.03 ? 156 ALA B CA 1 ATOM 5353 C C . ALA B 2 156 ? 67.732 -57.120 55.414 1.00 84.51 ? 156 ALA B C 1 ATOM 5354 O O . ALA B 2 156 ? 66.759 -57.349 56.147 1.00 89.91 ? 156 ALA B O 1 ATOM 5355 C CB . ALA B 2 156 ? 67.665 -58.924 53.654 1.00 76.84 ? 156 ALA B CB 1 ATOM 5356 N N . LYS B 2 157 ? 68.866 -56.594 55.867 1.00 73.48 ? 157 LYS B N 1 ATOM 5357 C CA . LYS B 2 157 ? 69.056 -56.244 57.266 1.00 74.74 ? 157 LYS B CA 1 ATOM 5358 C C . LYS B 2 157 ? 69.688 -54.869 57.360 1.00 74.08 ? 157 LYS B C 1 ATOM 5359 O O . LYS B 2 157 ? 70.570 -54.542 56.572 1.00 78.47 ? 157 LYS B O 1 ATOM 5360 C CB . LYS B 2 157 ? 70.015 -57.223 57.940 1.00 78.18 ? 157 LYS B CB 1 ATOM 5361 C CG . LYS B 2 157 ? 69.558 -58.655 58.083 1.00 78.47 ? 157 LYS B CG 1 ATOM 5362 C CD . LYS B 2 157 ? 70.563 -59.372 58.978 1.00 91.00 ? 157 LYS B CD 1 ATOM 5363 C CE . LYS B 2 157 ? 70.643 -60.868 58.724 1.00 98.29 ? 157 LYS B CE 1 ATOM 5364 N NZ . LYS B 2 157 ? 71.739 -61.466 59.547 1.00 97.77 ? 157 LYS B NZ 1 ATOM 5365 N N . PHE B 2 158 ? 69.286 -54.084 58.353 1.00 69.05 ? 158 PHE B N 1 ATOM 5366 C CA . PHE B 2 158 ? 69.908 -52.779 58.569 1.00 71.66 ? 158 PHE B CA 1 ATOM 5367 C C . PHE B 2 158 ? 70.338 -52.495 60.021 1.00 77.52 ? 158 PHE B C 1 ATOM 5368 O O . PHE B 2 158 ? 69.567 -52.698 60.960 1.00 91.57 ? 158 PHE B O 1 ATOM 5369 C CB . PHE B 2 158 ? 68.995 -51.677 58.022 1.00 68.70 ? 158 PHE B CB 1 ATOM 5370 C CG . PHE B 2 158 ? 68.646 -51.863 56.577 1.00 71.97 ? 158 PHE B CG 1 ATOM 5371 C CD1 . PHE B 2 158 ? 67.470 -52.496 56.208 1.00 75.36 ? 158 PHE B CD1 1 ATOM 5372 C CD2 . PHE B 2 158 ? 69.513 -51.436 55.580 1.00 71.71 ? 158 PHE B CD2 1 ATOM 5373 C CE1 . PHE B 2 158 ? 67.156 -52.683 54.865 1.00 71.60 ? 158 PHE B CE1 1 ATOM 5374 C CE2 . PHE B 2 158 ? 69.203 -51.621 54.241 1.00 66.43 ? 158 PHE B CE2 1 ATOM 5375 C CZ . PHE B 2 158 ? 68.025 -52.245 53.886 1.00 61.87 ? 158 PHE B CZ 1 ATOM 5376 N N . ARG B 2 159 ? 71.580 -52.045 60.204 1.00 71.42 ? 159 ARG B N 1 ATOM 5377 C CA . ARG B 2 159 ? 72.019 -51.549 61.511 1.00 75.24 ? 159 ARG B CA 1 ATOM 5378 C C . ARG B 2 159 ? 72.349 -50.062 61.428 1.00 72.99 ? 159 ARG B C 1 ATOM 5379 O O . ARG B 2 159 ? 72.684 -49.563 60.361 1.00 74.47 ? 159 ARG B O 1 ATOM 5380 C CB . ARG B 2 159 ? 73.201 -52.346 62.061 1.00 75.38 ? 159 ARG B CB 1 ATOM 5381 C CG . ARG B 2 159 ? 72.829 -53.689 62.670 1.00 88.19 ? 159 ARG B CG 1 ATOM 5382 C CD . ARG B 2 159 ? 72.608 -54.736 61.597 1.00 109.96 ? 159 ARG B CD 1 ATOM 5383 N NE . ARG B 2 159 ? 73.685 -54.732 60.606 1.00 133.30 ? 159 ARG B NE 1 ATOM 5384 C CZ . ARG B 2 159 ? 74.898 -55.249 60.806 1.00 144.04 ? 159 ARG B CZ 1 ATOM 5385 N NH1 . ARG B 2 159 ? 75.204 -55.811 61.979 1.00 149.05 ? 159 ARG B NH1 1 ATOM 5386 N NH2 . ARG B 2 159 ? 75.810 -55.196 59.835 1.00 132.18 ? 159 ARG B NH2 1 ATOM 5387 N N . GLN B 2 160 ? 72.247 -49.353 62.547 1.00 83.99 ? 160 GLN B N 1 ATOM 5388 C CA . GLN B 2 160 ? 72.267 -47.893 62.499 1.00 91.54 ? 160 GLN B CA 1 ATOM 5389 C C . GLN B 2 160 ? 73.447 -47.368 61.705 1.00 92.92 ? 160 GLN B C 1 ATOM 5390 O O . GLN B 2 160 ? 73.338 -46.392 60.966 1.00 94.07 ? 160 GLN B O 1 ATOM 5391 C CB . GLN B 2 160 ? 72.278 -47.279 63.902 1.00 93.58 ? 160 GLN B CB 1 ATOM 5392 C CG . GLN B 2 160 ? 71.914 -45.800 63.885 1.00 100.99 ? 160 GLN B CG 1 ATOM 5393 C CD . GLN B 2 160 ? 72.407 -45.036 65.104 1.00 101.05 ? 160 GLN B CD 1 ATOM 5394 O OE1 . GLN B 2 160 ? 73.258 -45.519 65.853 1.00 78.20 ? 160 GLN B OE1 1 ATOM 5395 N NE2 . GLN B 2 160 ? 71.872 -43.826 65.300 1.00 110.13 ? 160 GLN B NE2 1 ATOM 5396 N N . LEU B 2 161 ? 74.576 -48.044 61.849 1.00 94.07 ? 161 LEU B N 1 ATOM 5397 C CA . LEU B 2 161 ? 75.845 -47.510 61.389 1.00 82.11 ? 161 LEU B CA 1 ATOM 5398 C C . LEU B 2 161 ? 76.317 -48.008 60.025 1.00 72.85 ? 161 LEU B C 1 ATOM 5399 O O . LEU B 2 161 ? 77.444 -47.734 59.638 1.00 70.75 ? 161 LEU B O 1 ATOM 5400 C CB . LEU B 2 161 ? 76.917 -47.810 62.436 1.00 73.84 ? 161 LEU B CB 1 ATOM 5401 C CG . LEU B 2 161 ? 76.903 -46.919 63.667 1.00 74.25 ? 161 LEU B CG 1 ATOM 5402 C CD1 . LEU B 2 161 ? 78.216 -47.082 64.403 1.00 61.36 ? 161 LEU B CD1 1 ATOM 5403 C CD2 . LEU B 2 161 ? 76.704 -45.486 63.243 1.00 58.02 ? 161 LEU B CD2 1 ATOM 5404 N N . ASP B 2 162 ? 75.469 -48.723 59.295 1.00 75.70 ? 162 ASP B N 1 ATOM 5405 C CA . ASP B 2 162 ? 75.924 -49.424 58.092 1.00 81.06 ? 162 ASP B CA 1 ATOM 5406 C C . ASP B 2 162 ? 76.529 -48.508 57.023 1.00 76.70 ? 162 ASP B C 1 ATOM 5407 O O . ASP B 2 162 ? 77.500 -48.881 56.377 1.00 74.13 ? 162 ASP B O 1 ATOM 5408 C CB . ASP B 2 162 ? 74.823 -50.318 57.504 1.00 82.97 ? 162 ASP B CB 1 ATOM 5409 C CG . ASP B 2 162 ? 74.707 -51.669 58.219 1.00 96.08 ? 162 ASP B CG 1 ATOM 5410 O OD1 . ASP B 2 162 ? 75.508 -51.958 59.138 1.00 85.32 ? 162 ASP B OD1 1 ATOM 5411 O OD2 . ASP B 2 162 ? 73.803 -52.452 57.855 1.00 108.63 ? 162 ASP B OD2 1 ATOM 5412 N N . LEU B 2 163 ? 75.979 -47.307 56.857 1.00 76.38 ? 163 LEU B N 1 ATOM 5413 C CA . LEU B 2 163 ? 76.473 -46.379 55.836 1.00 68.41 ? 163 LEU B CA 1 ATOM 5414 C C . LEU B 2 163 ? 77.461 -45.332 56.366 1.00 73.41 ? 163 LEU B C 1 ATOM 5415 O O . LEU B 2 163 ? 77.576 -44.237 55.816 1.00 69.87 ? 163 LEU B O 1 ATOM 5416 C CB . LEU B 2 163 ? 75.305 -45.682 55.131 1.00 47.30 ? 163 LEU B CB 1 ATOM 5417 C CG . LEU B 2 163 ? 74.366 -46.622 54.380 1.00 58.07 ? 163 LEU B CG 1 ATOM 5418 C CD1 . LEU B 2 163 ? 73.127 -45.893 53.859 1.00 43.09 ? 163 LEU B CD1 1 ATOM 5419 C CD2 . LEU B 2 163 ? 75.143 -47.273 53.260 1.00 59.40 ? 163 LEU B CD2 1 ATOM 5420 N N . LEU B 2 164 ? 78.180 -45.671 57.429 1.00 76.85 ? 164 LEU B N 1 ATOM 5421 C CA . LEU B 2 164 ? 79.080 -44.717 58.073 1.00 81.05 ? 164 LEU B CA 1 ATOM 5422 C C . LEU B 2 164 ? 80.281 -44.364 57.187 1.00 81.39 ? 164 LEU B C 1 ATOM 5423 O O . LEU B 2 164 ? 80.677 -43.204 57.107 1.00 80.70 ? 164 LEU B O 1 ATOM 5424 C CB . LEU B 2 164 ? 79.549 -45.245 59.437 1.00 80.17 ? 164 LEU B CB 1 ATOM 5425 C CG . LEU B 2 164 ? 79.501 -44.247 60.599 1.00 80.57 ? 164 LEU B CG 1 ATOM 5426 C CD1 . LEU B 2 164 ? 80.657 -44.443 61.582 1.00 67.05 ? 164 LEU B CD1 1 ATOM 5427 C CD2 . LEU B 2 164 ? 79.492 -42.825 60.062 1.00 88.95 ? 164 LEU B CD2 1 ATOM 5428 N N . PRO B 2 165 ? 80.867 -45.366 56.521 1.00 78.98 ? 165 PRO B N 1 ATOM 5429 C CA . PRO B 2 165 ? 82.004 -45.065 55.648 1.00 83.74 ? 165 PRO B CA 1 ATOM 5430 C C . PRO B 2 165 ? 81.715 -44.041 54.536 1.00 81.23 ? 165 PRO B C 1 ATOM 5431 O O . PRO B 2 165 ? 82.647 -43.369 54.087 1.00 77.45 ? 165 PRO B O 1 ATOM 5432 C CB . PRO B 2 165 ? 82.353 -46.431 55.065 1.00 84.59 ? 165 PRO B CB 1 ATOM 5433 C CG . PRO B 2 165 ? 81.916 -47.396 56.130 1.00 82.63 ? 165 PRO B CG 1 ATOM 5434 C CD . PRO B 2 165 ? 80.666 -46.816 56.685 1.00 75.34 ? 165 PRO B CD 1 ATOM 5435 N N . VAL B 2 166 ? 80.468 -43.902 54.097 1.00 75.41 ? 166 VAL B N 1 ATOM 5436 C CA . VAL B 2 166 ? 80.181 -42.898 53.065 1.00 79.32 ? 166 VAL B CA 1 ATOM 5437 C C . VAL B 2 166 ? 79.504 -41.615 53.588 1.00 83.70 ? 166 VAL B C 1 ATOM 5438 O O . VAL B 2 166 ? 78.968 -40.825 52.809 1.00 84.40 ? 166 VAL B O 1 ATOM 5439 C CB . VAL B 2 166 ? 79.421 -43.491 51.832 1.00 68.20 ? 166 VAL B CB 1 ATOM 5440 C CG1 . VAL B 2 166 ? 80.244 -44.607 51.180 1.00 78.49 ? 166 VAL B CG1 1 ATOM 5441 C CG2 . VAL B 2 166 ? 78.029 -43.994 52.202 1.00 52.90 ? 166 VAL B CG2 1 ATOM 5442 N N . ALA B 2 167 ? 79.568 -41.395 54.898 1.00 81.22 ? 167 ALA B N 1 ATOM 5443 C CA . ALA B 2 167 ? 78.904 -40.254 55.523 1.00 82.03 ? 167 ALA B CA 1 ATOM 5444 C C . ALA B 2 167 ? 79.604 -38.926 55.273 1.00 82.74 ? 167 ALA B C 1 ATOM 5445 O O . ALA B 2 167 ? 79.067 -37.865 55.588 1.00 80.03 ? 167 ALA B O 1 ATOM 5446 C CB . ALA B 2 167 ? 78.759 -40.487 57.005 1.00 87.93 ? 167 ALA B CB 1 ATOM 5447 N N . HIS B 2 168 ? 80.799 -38.978 54.702 1.00 87.53 ? 168 HIS B N 1 ATOM 5448 C CA . HIS B 2 168 ? 81.550 -37.754 54.460 1.00 96.83 ? 168 HIS B CA 1 ATOM 5449 C C . HIS B 2 168 ? 81.780 -37.459 52.986 1.00 108.35 ? 168 HIS B C 1 ATOM 5450 O O . HIS B 2 168 ? 82.729 -36.756 52.638 1.00 119.58 ? 168 HIS B O 1 ATOM 5451 C CB . HIS B 2 168 ? 82.893 -37.799 55.176 1.00 95.23 ? 168 HIS B CB 1 ATOM 5452 C CG . HIS B 2 168 ? 82.781 -37.808 56.666 1.00 96.31 ? 168 HIS B CG 1 ATOM 5453 N ND1 . HIS B 2 168 ? 83.041 -36.696 57.438 1.00 94.68 ? 168 HIS B ND1 1 ATOM 5454 C CD2 . HIS B 2 168 ? 82.445 -38.796 57.528 1.00 99.62 ? 168 HIS B CD2 1 ATOM 5455 C CE1 . HIS B 2 168 ? 82.869 -37.000 58.710 1.00 103.03 ? 168 HIS B CE1 1 ATOM 5456 N NE2 . HIS B 2 168 ? 82.508 -38.268 58.793 1.00 105.21 ? 168 HIS B NE2 1 ATOM 5457 N N . LEU B 2 169 ? 80.919 -37.991 52.123 1.00 103.78 ? 169 LEU B N 1 ATOM 5458 C CA . LEU B 2 169 ? 81.003 -37.714 50.691 1.00 95.09 ? 169 LEU B CA 1 ATOM 5459 C C . LEU B 2 169 ? 79.871 -36.789 50.301 1.00 105.61 ? 169 LEU B C 1 ATOM 5460 O O . LEU B 2 169 ? 78.830 -36.767 50.958 1.00 118.01 ? 169 LEU B O 1 ATOM 5461 C CB . LEU B 2 169 ? 80.895 -39.003 49.891 1.00 76.43 ? 169 LEU B CB 1 ATOM 5462 C CG . LEU B 2 169 ? 81.772 -40.143 50.400 1.00 72.49 ? 169 LEU B CG 1 ATOM 5463 C CD1 . LEU B 2 169 ? 81.278 -41.476 49.862 1.00 65.33 ? 169 LEU B CD1 1 ATOM 5464 C CD2 . LEU B 2 169 ? 83.227 -39.900 50.034 1.00 50.46 ? 169 LEU B CD2 1 ATOM 5465 N N . HIS B 2 170 ? 80.065 -36.022 49.238 1.00 99.08 ? 170 HIS B N 1 ATOM 5466 C CA . HIS B 2 170 ? 79.019 -35.105 48.805 1.00 104.66 ? 170 HIS B CA 1 ATOM 5467 C C . HIS B 2 170 ? 78.079 -35.791 47.802 1.00 93.87 ? 170 HIS B C 1 ATOM 5468 O O . HIS B 2 170 ? 78.048 -35.487 46.602 1.00 86.53 ? 170 HIS B O 1 ATOM 5469 C CB . HIS B 2 170 ? 79.620 -33.784 48.308 1.00 118.82 ? 170 HIS B CB 1 ATOM 5470 C CG . HIS B 2 170 ? 80.281 -32.988 49.395 1.00 129.30 ? 170 HIS B CG 1 ATOM 5471 N ND1 . HIS B 2 170 ? 81.573 -33.226 49.815 1.00 130.39 ? 170 HIS B ND1 1 ATOM 5472 C CD2 . HIS B 2 170 ? 79.818 -31.975 50.168 1.00 133.19 ? 170 HIS B CD2 1 ATOM 5473 C CE1 . HIS B 2 170 ? 81.880 -32.389 50.791 1.00 130.25 ? 170 HIS B CE1 1 ATOM 5474 N NE2 . HIS B 2 170 ? 80.833 -31.618 51.024 1.00 131.35 ? 170 HIS B NE2 1 ATOM 5475 N N . LEU B 2 171 ? 77.317 -36.734 48.343 1.00 75.98 ? 171 LEU B N 1 ATOM 5476 C CA . LEU B 2 171 ? 76.415 -37.561 47.572 1.00 75.01 ? 171 LEU B CA 1 ATOM 5477 C C . LEU B 2 171 ? 75.239 -36.779 46.994 1.00 79.69 ? 171 LEU B C 1 ATOM 5478 O O . LEU B 2 171 ? 74.770 -35.804 47.592 1.00 75.13 ? 171 LEU B O 1 ATOM 5479 C CB . LEU B 2 171 ? 75.891 -38.695 48.448 1.00 72.92 ? 171 LEU B CB 1 ATOM 5480 C CG . LEU B 2 171 ? 76.892 -39.779 48.825 1.00 75.45 ? 171 LEU B CG 1 ATOM 5481 C CD1 . LEU B 2 171 ? 76.277 -40.655 49.887 1.00 76.11 ? 171 LEU B CD1 1 ATOM 5482 C CD2 . LEU B 2 171 ? 77.295 -40.598 47.602 1.00 79.80 ? 171 LEU B CD2 1 ATOM 5483 N N . SER B 2 172 ? 74.762 -37.235 45.833 1.00 74.89 ? 172 SER B N 1 ATOM 5484 C CA . SER B 2 172 ? 73.593 -36.659 45.176 1.00 69.32 ? 172 SER B CA 1 ATOM 5485 C C . SER B 2 172 ? 72.405 -37.624 45.120 1.00 75.74 ? 172 SER B C 1 ATOM 5486 O O . SER B 2 172 ? 71.250 -37.206 45.273 1.00 73.16 ? 172 SER B O 1 ATOM 5487 C CB . SER B 2 172 ? 73.948 -36.170 43.777 1.00 66.77 ? 172 SER B CB 1 ATOM 5488 O OG . SER B 2 172 ? 74.358 -34.820 43.817 1.00 76.29 ? 172 SER B OG 1 ATOM 5489 N N . CYS B 2 173 ? 72.675 -38.908 44.895 1.00 69.82 ? 173 CYS B N 1 ATOM 5490 C CA . CYS B 2 173 ? 71.613 -39.898 45.026 1.00 62.26 ? 173 CYS B CA 1 ATOM 5491 C C . CYS B 2 173 ? 72.047 -41.125 45.807 1.00 61.06 ? 173 CYS B C 1 ATOM 5492 O O . CYS B 2 173 ? 73.108 -41.694 45.558 1.00 63.63 ? 173 CYS B O 1 ATOM 5493 C CB . CYS B 2 173 ? 71.026 -40.313 43.668 1.00 56.57 ? 173 CYS B CB 1 ATOM 5494 S SG . CYS B 2 173 ? 69.413 -41.188 43.813 1.00 76.98 ? 173 CYS B SG 1 ATOM 5495 N N . ILE B 2 174 ? 71.213 -41.499 46.772 1.00 59.56 ? 174 ILE B N 1 ATOM 5496 C CA . ILE B 2 174 ? 71.284 -42.793 47.428 1.00 59.78 ? 174 ILE B CA 1 ATOM 5497 C C . ILE B 2 174 ? 70.033 -43.564 47.042 1.00 63.70 ? 174 ILE B C 1 ATOM 5498 O O . ILE B 2 174 ? 68.922 -43.242 47.462 1.00 64.53 ? 174 ILE B O 1 ATOM 5499 C CB . ILE B 2 174 ? 71.377 -42.672 48.971 1.00 56.94 ? 174 ILE B CB 1 ATOM 5500 C CG1 . ILE B 2 174 ? 72.695 -42.005 49.365 1.00 61.46 ? 174 ILE B CG1 1 ATOM 5501 C CG2 . ILE B 2 174 ? 71.266 -44.047 49.635 1.00 46.73 ? 174 ILE B CG2 1 ATOM 5502 C CD1 . ILE B 2 174 ? 73.147 -42.339 50.751 1.00 63.57 ? 174 ILE B CD1 1 ATOM 5503 N N . LEU B 2 175 ? 70.214 -44.562 46.195 1.00 67.45 ? 175 LEU B N 1 ATOM 5504 C CA . LEU B 2 175 ? 69.117 -45.431 45.837 1.00 67.13 ? 175 LEU B CA 1 ATOM 5505 C C . LEU B 2 175 ? 69.227 -46.662 46.719 1.00 71.67 ? 175 LEU B C 1 ATOM 5506 O O . LEU B 2 175 ? 70.282 -47.285 46.788 1.00 77.26 ? 175 LEU B O 1 ATOM 5507 C CB . LEU B 2 175 ? 69.178 -45.810 44.354 1.00 54.33 ? 175 LEU B CB 1 ATOM 5508 C CG . LEU B 2 175 ? 68.124 -46.860 44.018 1.00 47.70 ? 175 LEU B CG 1 ATOM 5509 C CD1 . LEU B 2 175 ? 66.735 -46.269 44.123 1.00 50.02 ? 175 LEU B CD1 1 ATOM 5510 C CD2 . LEU B 2 175 ? 68.345 -47.445 42.671 1.00 48.68 ? 175 LEU B CD2 1 ATOM 5511 N N . LEU B 2 176 ? 68.139 -47.001 47.401 1.00 65.06 ? 176 LEU B N 1 ATOM 5512 C CA . LEU B 2 176 ? 68.143 -48.104 48.355 1.00 54.66 ? 176 LEU B CA 1 ATOM 5513 C C . LEU B 2 176 ? 66.866 -48.924 48.258 1.00 61.26 ? 176 LEU B C 1 ATOM 5514 O O . LEU B 2 176 ? 65.762 -48.379 48.299 1.00 58.99 ? 176 LEU B O 1 ATOM 5515 C CB . LEU B 2 176 ? 68.280 -47.540 49.756 1.00 55.49 ? 176 LEU B CB 1 ATOM 5516 C CG . LEU B 2 176 ? 68.304 -48.464 50.960 1.00 61.53 ? 176 LEU B CG 1 ATOM 5517 C CD1 . LEU B 2 176 ? 69.240 -49.644 50.737 1.00 69.20 ? 176 LEU B CD1 1 ATOM 5518 C CD2 . LEU B 2 176 ? 68.744 -47.625 52.152 1.00 60.32 ? 176 LEU B CD2 1 ATOM 5519 N N . ASP B 2 177 ? 67.004 -50.235 48.120 1.00 59.69 ? 177 ASP B N 1 ATOM 5520 C CA . ASP B 2 177 ? 65.814 -51.050 47.963 1.00 60.13 ? 177 ASP B CA 1 ATOM 5521 C C . ASP B 2 177 ? 65.670 -52.139 49.011 1.00 66.66 ? 177 ASP B C 1 ATOM 5522 O O . ASP B 2 177 ? 66.611 -52.868 49.337 1.00 68.89 ? 177 ASP B O 1 ATOM 5523 C CB . ASP B 2 177 ? 65.746 -51.668 46.584 1.00 59.57 ? 177 ASP B CB 1 ATOM 5524 C CG . ASP B 2 177 ? 66.507 -52.955 46.504 1.00 71.44 ? 177 ASP B CG 1 ATOM 5525 O OD1 . ASP B 2 177 ? 67.706 -52.889 46.205 1.00 88.14 ? 177 ASP B OD1 1 ATOM 5526 O OD2 . ASP B 2 177 ? 65.914 -54.029 46.733 1.00 65.24 ? 177 ASP B OD2 1 ATOM 5527 N N . LEU B 2 178 ? 64.445 -52.244 49.497 1.00 65.89 ? 178 LEU B N 1 ATOM 5528 C CA . LEU B 2 178 ? 64.079 -53.114 50.586 1.00 60.77 ? 178 LEU B CA 1 ATOM 5529 C C . LEU B 2 178 ? 63.173 -54.190 50.016 1.00 65.89 ? 178 LEU B C 1 ATOM 5530 O O . LEU B 2 178 ? 62.195 -54.598 50.643 1.00 63.78 ? 178 LEU B O 1 ATOM 5531 C CB . LEU B 2 178 ? 63.278 -52.306 51.602 1.00 62.44 ? 178 LEU B CB 1 ATOM 5532 C CG . LEU B 2 178 ? 63.788 -51.099 52.403 1.00 54.63 ? 178 LEU B CG 1 ATOM 5533 C CD1 . LEU B 2 178 ? 63.975 -51.507 53.840 1.00 41.93 ? 178 LEU B CD1 1 ATOM 5534 C CD2 . LEU B 2 178 ? 65.039 -50.438 51.832 1.00 56.74 ? 178 LEU B CD2 1 ATOM 5535 N N . VAL B 2 179 ? 63.456 -54.621 48.797 1.00 72.13 ? 179 VAL B N 1 ATOM 5536 C CA . VAL B 2 179 ? 62.672 -55.694 48.213 1.00 72.66 ? 179 VAL B CA 1 ATOM 5537 C C . VAL B 2 179 ? 62.997 -56.971 48.981 1.00 85.23 ? 179 VAL B C 1 ATOM 5538 O O . VAL B 2 179 ? 62.104 -57.749 49.323 1.00 88.80 ? 179 VAL B O 1 ATOM 5539 C CB . VAL B 2 179 ? 62.972 -55.877 46.716 1.00 57.28 ? 179 VAL B CB 1 ATOM 5540 C CG1 . VAL B 2 179 ? 62.052 -56.907 46.131 1.00 62.51 ? 179 VAL B CG1 1 ATOM 5541 C CG2 . VAL B 2 179 ? 62.791 -54.574 45.988 1.00 55.40 ? 179 VAL B CG2 1 ATOM 5542 N N . SER B 2 180 ? 64.282 -57.154 49.277 1.00 81.97 ? 180 SER B N 1 ATOM 5543 C CA . SER B 2 180 ? 64.763 -58.349 49.960 1.00 83.11 ? 180 SER B CA 1 ATOM 5544 C C . SER B 2 180 ? 64.365 -58.406 51.441 1.00 84.19 ? 180 SER B C 1 ATOM 5545 O O . SER B 2 180 ? 64.633 -59.394 52.118 1.00 80.53 ? 180 SER B O 1 ATOM 5546 C CB . SER B 2 180 ? 66.289 -58.435 49.839 1.00 85.26 ? 180 SER B CB 1 ATOM 5547 O OG . SER B 2 180 ? 66.685 -59.047 48.629 1.00 83.28 ? 180 SER B OG 1 ATOM 5548 N N . TYR B 2 181 ? 63.714 -57.354 51.929 1.00 83.45 ? 181 TYR B N 1 ATOM 5549 C CA . TYR B 2 181 ? 63.511 -57.147 53.366 1.00 81.27 ? 181 TYR B CA 1 ATOM 5550 C C . TYR B 2 181 ? 62.220 -57.724 53.948 1.00 83.69 ? 181 TYR B C 1 ATOM 5551 O O . TYR B 2 181 ? 61.129 -57.459 53.460 1.00 78.93 ? 181 TYR B O 1 ATOM 5552 C CB . TYR B 2 181 ? 63.591 -55.652 53.693 1.00 79.02 ? 181 TYR B CB 1 ATOM 5553 C CG . TYR B 2 181 ? 63.002 -55.267 55.029 1.00 78.16 ? 181 TYR B CG 1 ATOM 5554 C CD1 . TYR B 2 181 ? 63.825 -54.995 56.115 1.00 83.17 ? 181 TYR B CD1 1 ATOM 5555 C CD2 . TYR B 2 181 ? 61.624 -55.166 55.206 1.00 75.91 ? 181 TYR B CD2 1 ATOM 5556 C CE1 . TYR B 2 181 ? 63.294 -54.633 57.341 1.00 87.18 ? 181 TYR B CE1 1 ATOM 5557 C CE2 . TYR B 2 181 ? 61.082 -54.812 56.434 1.00 81.51 ? 181 TYR B CE2 1 ATOM 5558 C CZ . TYR B 2 181 ? 61.924 -54.546 57.498 1.00 86.46 ? 181 TYR B CZ 1 ATOM 5559 O OH . TYR B 2 181 ? 61.406 -54.191 58.723 1.00 92.04 ? 181 TYR B OH 1 ATOM 5560 N N . HIS B 2 182 ? 62.364 -58.497 55.019 1.00 94.61 ? 182 HIS B N 1 ATOM 5561 C CA . HIS B 2 182 ? 61.231 -59.025 55.759 1.00 92.65 ? 182 HIS B CA 1 ATOM 5562 C C . HIS B 2 182 ? 61.367 -58.512 57.184 1.00 87.27 ? 182 HIS B C 1 ATOM 5563 O O . HIS B 2 182 ? 62.462 -58.125 57.585 1.00 86.24 ? 182 HIS B O 1 ATOM 5564 C CB . HIS B 2 182 ? 61.229 -60.558 55.706 1.00 99.28 ? 182 HIS B CB 1 ATOM 5565 C CG . HIS B 2 182 ? 61.394 -61.112 54.319 1.00 116.01 ? 182 HIS B CG 1 ATOM 5566 N ND1 . HIS B 2 182 ? 60.357 -61.173 53.410 1.00 121.45 ? 182 HIS B ND1 1 ATOM 5567 C CD2 . HIS B 2 182 ? 62.478 -61.617 53.682 1.00 122.76 ? 182 HIS B CD2 1 ATOM 5568 C CE1 . HIS B 2 182 ? 60.795 -61.694 52.276 1.00 121.68 ? 182 HIS B CE1 1 ATOM 5569 N NE2 . HIS B 2 182 ? 62.079 -61.972 52.414 1.00 121.56 ? 182 HIS B NE2 1 ATOM 5570 N N . ILE B 2 183 ? 60.258 -58.468 57.923 1.00 90.86 ? 183 ILE B N 1 ATOM 5571 C CA . ILE B 2 183 ? 60.254 -58.058 59.330 1.00 87.30 ? 183 ILE B CA 1 ATOM 5572 C C . ILE B 2 183 ? 60.948 -59.120 60.161 1.00 95.64 ? 183 ILE B C 1 ATOM 5573 O O . ILE B 2 183 ? 60.916 -60.295 59.804 1.00 100.28 ? 183 ILE B O 1 ATOM 5574 C CB . ILE B 2 183 ? 58.819 -57.924 59.879 1.00 87.36 ? 183 ILE B CB 1 ATOM 5575 C CG1 . ILE B 2 183 ? 58.169 -56.621 59.424 1.00 87.29 ? 183 ILE B CG1 1 ATOM 5576 C CG2 . ILE B 2 183 ? 58.829 -57.949 61.393 1.00 100.43 ? 183 ILE B CG2 1 ATOM 5577 C CD1 . ILE B 2 183 ? 58.794 -55.393 60.040 1.00 93.51 ? 183 ILE B CD1 1 ATOM 5578 N N . LYS B 2 184 ? 61.575 -58.722 61.265 1.00 109.98 ? 184 LYS B N 1 ATOM 5579 C CA . LYS B 2 184 ? 62.182 -59.704 62.166 1.00 127.18 ? 184 LYS B CA 1 ATOM 5580 C C . LYS B 2 184 ? 61.709 -59.629 63.623 1.00 133.05 ? 184 LYS B C 1 ATOM 5581 O O . LYS B 2 184 ? 60.559 -59.287 63.897 1.00 135.09 ? 184 LYS B O 1 ATOM 5582 C CB . LYS B 2 184 ? 63.711 -59.678 62.072 1.00 130.08 ? 184 LYS B CB 1 ATOM 5583 C CG . LYS B 2 184 ? 64.276 -60.627 61.009 1.00 128.28 ? 184 LYS B CG 1 ATOM 5584 C CD . LYS B 2 184 ? 63.798 -62.075 61.220 1.00 126.97 ? 184 LYS B CD 1 ATOM 5585 C CE . LYS B 2 184 ? 64.240 -62.660 62.570 1.00 115.62 ? 184 LYS B CE 1 ATOM 5586 N NZ . LYS B 2 184 ? 63.771 -64.068 62.771 1.00 105.75 ? 184 LYS B NZ 1 ATOM 5587 N N . GLY B 2 185 ? 62.606 -59.962 64.547 1.00 138.91 ? 185 GLY B N 1 ATOM 5588 C CA . GLY B 2 185 ? 62.256 -60.131 65.948 1.00 148.61 ? 185 GLY B CA 1 ATOM 5589 C C . GLY B 2 185 ? 61.852 -58.889 66.723 1.00 155.99 ? 185 GLY B C 1 ATOM 5590 O O . GLY B 2 185 ? 62.163 -58.767 67.909 1.00 144.59 ? 185 GLY B O 1 ATOM 5591 N N . GLY B 2 186 ? 61.158 -57.968 66.059 1.00 170.14 ? 186 GLY B N 1 ATOM 5592 C CA . GLY B 2 186 ? 60.624 -56.786 66.713 1.00 179.98 ? 186 GLY B CA 1 ATOM 5593 C C . GLY B 2 186 ? 61.665 -55.780 67.170 1.00 188.75 ? 186 GLY B C 1 ATOM 5594 O O . GLY B 2 186 ? 61.360 -54.596 67.311 1.00 191.79 ? 186 GLY B O 1 ATOM 5595 N N . GLU B 2 187 ? 62.888 -56.251 67.407 1.00 190.50 ? 187 GLU B N 1 ATOM 5596 C CA . GLU B 2 187 ? 63.993 -55.400 67.851 1.00 185.46 ? 187 GLU B CA 1 ATOM 5597 C C . GLU B 2 187 ? 64.367 -54.397 66.765 1.00 175.27 ? 187 GLU B C 1 ATOM 5598 O O . GLU B 2 187 ? 65.423 -54.511 66.139 1.00 172.08 ? 187 GLU B O 1 ATOM 5599 C CB . GLU B 2 187 ? 65.204 -56.262 68.194 1.00 188.62 ? 187 GLU B CB 1 ATOM 5600 C CG . GLU B 2 187 ? 64.855 -57.518 68.973 1.00 194.73 ? 187 GLU B CG 1 ATOM 5601 C CD . GLU B 2 187 ? 65.971 -58.544 68.960 1.00 199.06 ? 187 GLU B CD 1 ATOM 5602 O OE1 . GLU B 2 187 ? 66.833 -58.470 68.058 1.00 199.91 ? 187 GLU B OE1 1 ATOM 5603 O OE2 . GLU B 2 187 ? 65.982 -59.424 69.849 1.00 200.18 ? 187 GLU B OE2 1 ATOM 5604 N N . THR B 2 188 ? 63.495 -53.411 66.567 1.00 166.26 ? 188 THR B N 1 ATOM 5605 C CA . THR B 2 188 ? 63.563 -52.492 65.428 1.00 150.58 ? 188 THR B CA 1 ATOM 5606 C C . THR B 2 188 ? 64.968 -52.197 64.891 1.00 128.49 ? 188 THR B C 1 ATOM 5607 O O . THR B 2 188 ? 65.884 -51.819 65.626 1.00 126.67 ? 188 THR B O 1 ATOM 5608 C CB . THR B 2 188 ? 62.772 -51.176 65.696 1.00 140.50 ? 188 THR B CB 1 ATOM 5609 O OG1 . THR B 2 188 ? 61.441 -51.310 65.179 1.00 137.19 ? 188 THR B OG1 1 ATOM 5610 C CG2 . THR B 2 188 ? 63.447 -49.978 65.034 1.00 136.58 ? 188 THR B CG2 1 ATOM 5611 N N . GLU B 2 189 ? 65.115 -52.396 63.588 1.00 106.04 ? 189 GLU B N 1 ATOM 5612 C CA . GLU B 2 189 ? 66.350 -52.098 62.895 1.00 90.16 ? 189 GLU B CA 1 ATOM 5613 C C . GLU B 2 189 ? 66.457 -50.576 62.713 1.00 82.53 ? 189 GLU B C 1 ATOM 5614 O O . GLU B 2 189 ? 65.451 -49.885 62.547 1.00 81.71 ? 189 GLU B O 1 ATOM 5615 C CB . GLU B 2 189 ? 66.382 -52.853 61.552 1.00 81.91 ? 189 GLU B CB 1 ATOM 5616 C CG . GLU B 2 189 ? 65.865 -54.312 61.643 1.00 62.98 ? 189 GLU B CG 1 ATOM 5617 C CD . GLU B 2 189 ? 65.901 -55.104 60.313 1.00 81.51 ? 189 GLU B CD 1 ATOM 5618 O OE1 . GLU B 2 189 ? 66.753 -54.822 59.440 1.00 74.24 ? 189 GLU B OE1 1 ATOM 5619 O OE2 . GLU B 2 189 ? 65.075 -56.035 60.150 1.00 91.10 ? 189 GLU B OE2 1 ATOM 5620 N N . SER B 2 190 ? 67.669 -50.045 62.785 1.00 69.70 ? 190 SER B N 1 ATOM 5621 C CA . SER B 2 190 ? 67.866 -48.626 62.557 1.00 69.28 ? 190 SER B CA 1 ATOM 5622 C C . SER B 2 190 ? 68.747 -48.485 61.336 1.00 79.04 ? 190 SER B C 1 ATOM 5623 O O . SER B 2 190 ? 69.299 -49.465 60.840 1.00 79.55 ? 190 SER B O 1 ATOM 5624 C CB . SER B 2 190 ? 68.545 -47.962 63.755 1.00 83.26 ? 190 SER B CB 1 ATOM 5625 O OG . SER B 2 190 ? 67.935 -48.340 64.982 1.00 106.92 ? 190 SER B OG 1 ATOM 5626 N N . LEU B 2 191 ? 68.882 -47.262 60.847 1.00 79.44 ? 191 LEU B N 1 ATOM 5627 C CA . LEU B 2 191 ? 69.810 -46.991 59.769 1.00 69.50 ? 191 LEU B CA 1 ATOM 5628 C C . LEU B 2 191 ? 69.975 -45.498 59.575 1.00 72.14 ? 191 LEU B C 1 ATOM 5629 O O . LEU B 2 191 ? 69.025 -44.786 59.268 1.00 74.18 ? 191 LEU B O 1 ATOM 5630 C CB . LEU B 2 191 ? 69.335 -47.632 58.475 1.00 69.86 ? 191 LEU B CB 1 ATOM 5631 C CG . LEU B 2 191 ? 70.310 -47.396 57.330 1.00 62.71 ? 191 LEU B CG 1 ATOM 5632 C CD1 . LEU B 2 191 ? 71.597 -48.148 57.645 1.00 52.76 ? 191 LEU B CD1 1 ATOM 5633 C CD2 . LEU B 2 191 ? 69.690 -47.807 55.988 1.00 53.18 ? 191 LEU B CD2 1 ATOM 5634 N N . GLN B 2 192 ? 71.193 -45.026 59.772 1.00 74.65 ? 192 GLN B N 1 ATOM 5635 C CA . GLN B 2 192 ? 71.485 -43.625 59.600 1.00 78.27 ? 192 GLN B CA 1 ATOM 5636 C C . GLN B 2 192 ? 71.786 -43.416 58.132 1.00 76.53 ? 192 GLN B C 1 ATOM 5637 O O . GLN B 2 192 ? 72.689 -44.057 57.597 1.00 79.33 ? 192 GLN B O 1 ATOM 5638 C CB . GLN B 2 192 ? 72.699 -43.249 60.445 1.00 94.54 ? 192 GLN B CB 1 ATOM 5639 C CG . GLN B 2 192 ? 73.161 -41.824 60.263 1.00 108.18 ? 192 GLN B CG 1 ATOM 5640 C CD . GLN B 2 192 ? 72.439 -40.872 61.178 1.00 118.56 ? 192 GLN B CD 1 ATOM 5641 O OE1 . GLN B 2 192 ? 72.686 -40.856 62.389 1.00 123.77 ? 192 GLN B OE1 1 ATOM 5642 N NE2 . GLN B 2 192 ? 71.539 -40.068 60.609 1.00 113.10 ? 192 GLN B NE2 1 ATOM 5643 N N . ILE B 2 193 ? 71.020 -42.538 57.484 1.00 74.69 ? 193 ILE B N 1 ATOM 5644 C CA . ILE B 2 193 ? 71.273 -42.156 56.093 1.00 75.32 ? 193 ILE B CA 1 ATOM 5645 C C . ILE B 2 193 ? 72.203 -40.948 55.965 1.00 74.88 ? 193 ILE B C 1 ATOM 5646 O O . ILE B 2 193 ? 71.891 -39.863 56.454 1.00 80.59 ? 193 ILE B O 1 ATOM 5647 C CB . ILE B 2 193 ? 69.974 -41.836 55.335 1.00 73.83 ? 193 ILE B CB 1 ATOM 5648 C CG1 . ILE B 2 193 ? 69.298 -43.118 54.850 1.00 79.62 ? 193 ILE B CG1 1 ATOM 5649 C CG2 . ILE B 2 193 ? 70.277 -40.970 54.138 1.00 72.24 ? 193 ILE B CG2 1 ATOM 5650 C CD1 . ILE B 2 193 ? 68.409 -43.767 55.871 1.00 85.97 ? 193 ILE B CD1 1 ATOM 5651 N N . PRO B 2 194 ? 73.345 -41.132 55.286 1.00 74.88 ? 194 PRO B N 1 ATOM 5652 C CA . PRO B 2 194 ? 74.314 -40.050 55.072 1.00 77.28 ? 194 PRO B CA 1 ATOM 5653 C C . PRO B 2 194 ? 73.637 -38.870 54.400 1.00 75.70 ? 194 PRO B C 1 ATOM 5654 O O . PRO B 2 194 ? 72.614 -39.071 53.753 1.00 68.53 ? 194 PRO B O 1 ATOM 5655 C CB . PRO B 2 194 ? 75.331 -40.675 54.113 1.00 75.88 ? 194 PRO B CB 1 ATOM 5656 C CG . PRO B 2 194 ? 75.184 -42.148 54.299 1.00 74.93 ? 194 PRO B CG 1 ATOM 5657 C CD . PRO B 2 194 ? 73.744 -42.379 54.612 1.00 76.19 ? 194 PRO B CD 1 ATOM 5658 N N . ASN B 2 195 ? 74.180 -37.665 54.544 1.00 80.24 ? 195 ASN B N 1 ATOM 5659 C CA . ASN B 2 195 ? 73.592 -36.513 53.861 1.00 86.63 ? 195 ASN B CA 1 ATOM 5660 C C . ASN B 2 195 ? 73.560 -36.738 52.353 1.00 79.09 ? 195 ASN B C 1 ATOM 5661 O O . ASN B 2 195 ? 74.597 -36.968 51.731 1.00 78.91 ? 195 ASN B O 1 ATOM 5662 C CB . ASN B 2 195 ? 74.344 -35.221 54.195 1.00 102.50 ? 195 ASN B CB 1 ATOM 5663 C CG . ASN B 2 195 ? 74.811 -35.180 55.630 1.00 129.62 ? 195 ASN B CG 1 ATOM 5664 O OD1 . ASN B 2 195 ? 75.289 -36.184 56.154 1.00 133.18 ? 195 ASN B OD1 1 ATOM 5665 N ND2 . ASN B 2 195 ? 74.667 -34.019 56.278 1.00 158.88 ? 195 ASN B ND2 1 ATOM 5666 N N . THR B 2 196 ? 72.363 -36.696 51.774 1.00 84.44 ? 196 THR B N 1 ATOM 5667 C CA . THR B 2 196 ? 72.190 -36.838 50.328 1.00 81.02 ? 196 THR B CA 1 ATOM 5668 C C . THR B 2 196 ? 71.253 -35.766 49.842 1.00 74.38 ? 196 THR B C 1 ATOM 5669 O O . THR B 2 196 ? 70.346 -35.366 50.564 1.00 78.86 ? 196 THR B O 1 ATOM 5670 C CB . THR B 2 196 ? 71.511 -38.158 49.951 1.00 87.18 ? 196 THR B CB 1 ATOM 5671 O OG1 . THR B 2 196 ? 71.968 -39.210 50.805 1.00 109.18 ? 196 THR B OG1 1 ATOM 5672 C CG2 . THR B 2 196 ? 71.835 -38.509 48.532 1.00 86.11 ? 196 THR B CG2 1 ATOM 5673 N N . THR B 2 197 ? 71.450 -35.305 48.616 1.00 65.63 ? 197 THR B N 1 ATOM 5674 C CA . THR B 2 197 ? 70.415 -34.498 47.984 1.00 69.94 ? 197 THR B CA 1 ATOM 5675 C C . THR B 2 197 ? 69.113 -35.314 47.830 1.00 71.80 ? 197 THR B C 1 ATOM 5676 O O . THR B 2 197 ? 68.044 -34.913 48.311 1.00 71.68 ? 197 THR B O 1 ATOM 5677 C CB . THR B 2 197 ? 70.860 -33.941 46.625 1.00 62.04 ? 197 THR B CB 1 ATOM 5678 O OG1 . THR B 2 197 ? 71.970 -33.060 46.819 1.00 62.86 ? 197 THR B OG1 1 ATOM 5679 C CG2 . THR B 2 197 ? 69.711 -33.172 45.970 1.00 46.09 ? 197 THR B CG2 1 ATOM 5680 N N . VAL B 2 198 ? 69.205 -36.468 47.182 1.00 60.59 ? 198 VAL B N 1 ATOM 5681 C CA . VAL B 2 198 ? 68.029 -37.303 46.994 1.00 61.38 ? 198 VAL B CA 1 ATOM 5682 C C . VAL B 2 198 ? 68.152 -38.631 47.732 1.00 70.32 ? 198 VAL B C 1 ATOM 5683 O O . VAL B 2 198 ? 69.210 -39.253 47.734 1.00 79.38 ? 198 VAL B O 1 ATOM 5684 C CB . VAL B 2 198 ? 67.772 -37.562 45.495 1.00 61.10 ? 198 VAL B CB 1 ATOM 5685 C CG1 . VAL B 2 198 ? 66.577 -38.468 45.298 1.00 51.81 ? 198 VAL B CG1 1 ATOM 5686 C CG2 . VAL B 2 198 ? 67.570 -36.246 44.759 1.00 58.99 ? 198 VAL B CG2 1 ATOM 5687 N N . LEU B 2 199 ? 67.072 -39.050 48.382 1.00 67.44 ? 199 LEU B N 1 ATOM 5688 C CA . LEU B 2 199 ? 66.992 -40.407 48.905 1.00 67.27 ? 199 LEU B CA 1 ATOM 5689 C C . LEU B 2 199 ? 65.826 -41.124 48.260 1.00 65.85 ? 199 LEU B C 1 ATOM 5690 O O . LEU B 2 199 ? 64.678 -40.738 48.457 1.00 70.76 ? 199 LEU B O 1 ATOM 5691 C CB . LEU B 2 199 ? 66.808 -40.421 50.417 1.00 69.60 ? 199 LEU B CB 1 ATOM 5692 C CG . LEU B 2 199 ? 66.688 -41.840 50.975 1.00 66.91 ? 199 LEU B CG 1 ATOM 5693 C CD1 . LEU B 2 199 ? 67.849 -42.695 50.514 1.00 68.45 ? 199 LEU B CD1 1 ATOM 5694 C CD2 . LEU B 2 199 ? 66.641 -41.802 52.465 1.00 73.79 ? 199 LEU B CD2 1 ATOM 5695 N N . HIS B 2 200 ? 66.123 -42.164 47.489 1.00 65.61 ? 200 HIS B N 1 ATOM 5696 C CA . HIS B 2 200 ? 65.089 -42.935 46.809 1.00 65.24 ? 200 HIS B CA 1 ATOM 5697 C C . HIS B 2 200 ? 65.013 -44.336 47.395 1.00 70.01 ? 200 HIS B C 1 ATOM 5698 O O . HIS B 2 200 ? 65.998 -45.089 47.391 1.00 71.35 ? 200 HIS B O 1 ATOM 5699 C CB . HIS B 2 200 ? 65.379 -43.020 45.311 1.00 70.25 ? 200 HIS B CB 1 ATOM 5700 C CG . HIS B 2 200 ? 64.253 -43.594 44.506 1.00 74.80 ? 200 HIS B CG 1 ATOM 5701 N ND1 . HIS B 2 200 ? 63.197 -44.273 45.077 1.00 82.88 ? 200 HIS B ND1 1 ATOM 5702 C CD2 . HIS B 2 200 ? 64.031 -43.610 43.170 1.00 56.35 ? 200 HIS B CD2 1 ATOM 5703 C CE1 . HIS B 2 200 ? 62.363 -44.666 44.131 1.00 66.74 ? 200 HIS B CE1 1 ATOM 5704 N NE2 . HIS B 2 200 ? 62.846 -44.275 42.965 1.00 52.65 ? 200 HIS B NE2 1 ATOM 5705 N N . LEU B 2 201 ? 63.833 -44.678 47.898 1.00 57.36 ? 201 LEU B N 1 ATOM 5706 C CA . LEU B 2 201 ? 63.619 -45.969 48.526 1.00 55.76 ? 201 LEU B CA 1 ATOM 5707 C C . LEU B 2 201 ? 62.602 -46.787 47.734 1.00 56.32 ? 201 LEU B C 1 ATOM 5708 O O . LEU B 2 201 ? 61.507 -46.315 47.434 1.00 51.23 ? 201 LEU B O 1 ATOM 5709 C CB . LEU B 2 201 ? 63.151 -45.776 49.970 1.00 52.24 ? 201 LEU B CB 1 ATOM 5710 C CG . LEU B 2 201 ? 64.093 -44.919 50.809 1.00 56.14 ? 201 LEU B CG 1 ATOM 5711 C CD1 . LEU B 2 201 ? 63.423 -44.466 52.087 1.00 57.11 ? 201 LEU B CD1 1 ATOM 5712 C CD2 . LEU B 2 201 ? 65.359 -45.695 51.102 1.00 61.63 ? 201 LEU B CD2 1 ATOM 5713 N N . VAL B 2 202 ? 62.973 -48.012 47.386 1.00 61.02 ? 202 VAL B N 1 ATOM 5714 C CA . VAL B 2 202 ? 62.074 -48.890 46.645 1.00 68.96 ? 202 VAL B CA 1 ATOM 5715 C C . VAL B 2 202 ? 61.734 -50.105 47.506 1.00 66.52 ? 202 VAL B C 1 ATOM 5716 O O . VAL B 2 202 ? 62.626 -50.728 48.083 1.00 68.82 ? 202 VAL B O 1 ATOM 5717 C CB . VAL B 2 202 ? 62.699 -49.352 45.291 1.00 52.39 ? 202 VAL B CB 1 ATOM 5718 C CG1 . VAL B 2 202 ? 61.649 -49.972 44.411 1.00 35.83 ? 202 VAL B CG1 1 ATOM 5719 C CG2 . VAL B 2 202 ? 63.369 -48.187 44.577 1.00 48.70 ? 202 VAL B CG2 1 ATOM 5720 N N . PHE B 2 203 ? 60.449 -50.441 47.587 1.00 58.40 ? 203 PHE B N 1 ATOM 5721 C CA . PHE B 2 203 ? 59.997 -51.554 48.418 1.00 58.46 ? 203 PHE B CA 1 ATOM 5722 C C . PHE B 2 203 ? 59.515 -52.735 47.591 1.00 67.97 ? 203 PHE B C 1 ATOM 5723 O O . PHE B 2 203 ? 59.410 -52.649 46.368 1.00 71.88 ? 203 PHE B O 1 ATOM 5724 C CB . PHE B 2 203 ? 58.888 -51.083 49.350 1.00 57.94 ? 203 PHE B CB 1 ATOM 5725 C CG . PHE B 2 203 ? 59.263 -49.879 50.157 1.00 63.81 ? 203 PHE B CG 1 ATOM 5726 C CD1 . PHE B 2 203 ? 58.829 -48.616 49.786 1.00 57.95 ? 203 PHE B CD1 1 ATOM 5727 C CD2 . PHE B 2 203 ? 60.076 -50.006 51.274 1.00 68.85 ? 203 PHE B CD2 1 ATOM 5728 C CE1 . PHE B 2 203 ? 59.182 -47.502 50.519 1.00 61.02 ? 203 PHE B CE1 1 ATOM 5729 C CE2 . PHE B 2 203 ? 60.434 -48.897 52.010 1.00 75.59 ? 203 PHE B CE2 1 ATOM 5730 C CZ . PHE B 2 203 ? 59.986 -47.638 51.628 1.00 70.83 ? 203 PHE B CZ 1 ATOM 5731 N N . HIS B 2 204 ? 59.229 -53.844 48.260 1.00 73.82 ? 204 HIS B N 1 ATOM 5732 C CA . HIS B 2 204 ? 58.675 -55.001 47.580 1.00 77.98 ? 204 HIS B CA 1 ATOM 5733 C C . HIS B 2 204 ? 57.393 -54.569 46.903 1.00 85.19 ? 204 HIS B C 1 ATOM 5734 O O . HIS B 2 204 ? 56.553 -53.923 47.524 1.00 93.54 ? 204 HIS B O 1 ATOM 5735 C CB . HIS B 2 204 ? 58.376 -56.096 48.582 1.00 80.79 ? 204 HIS B CB 1 ATOM 5736 C CG . HIS B 2 204 ? 58.035 -57.414 47.964 1.00 75.52 ? 204 HIS B CG 1 ATOM 5737 N ND1 . HIS B 2 204 ? 58.983 -58.384 47.708 1.00 73.27 ? 204 HIS B ND1 1 ATOM 5738 C CD2 . HIS B 2 204 ? 56.847 -57.938 47.581 1.00 64.47 ? 204 HIS B CD2 1 ATOM 5739 C CE1 . HIS B 2 204 ? 58.394 -59.447 47.192 1.00 70.88 ? 204 HIS B CE1 1 ATOM 5740 N NE2 . HIS B 2 204 ? 57.097 -59.201 47.104 1.00 70.91 ? 204 HIS B NE2 1 ATOM 5741 N N . PRO B 2 205 ? 57.234 -54.938 45.625 1.00 82.12 ? 205 PRO B N 1 ATOM 5742 C CA . PRO B 2 205 ? 56.196 -54.409 44.739 1.00 79.14 ? 205 PRO B CA 1 ATOM 5743 C C . PRO B 2 205 ? 54.912 -55.228 44.778 1.00 79.12 ? 205 PRO B C 1 ATOM 5744 O O . PRO B 2 205 ? 53.999 -54.962 43.992 1.00 79.33 ? 205 PRO B O 1 ATOM 5745 C CB . PRO B 2 205 ? 56.828 -54.556 43.348 1.00 61.58 ? 205 PRO B CB 1 ATOM 5746 C CG . PRO B 2 205 ? 58.095 -55.388 43.547 1.00 56.92 ? 205 PRO B CG 1 ATOM 5747 C CD . PRO B 2 205 ? 58.060 -55.933 44.931 1.00 72.23 ? 205 PRO B CD 1 ATOM 5748 N N . ASN B 2 206 ? 54.846 -56.209 45.670 1.00 72.21 ? 206 ASN B N 1 ATOM 5749 C CA . ASN B 2 206 ? 53.736 -57.145 45.667 1.00 76.63 ? 206 ASN B CA 1 ATOM 5750 C C . ASN B 2 206 ? 53.254 -57.512 47.046 1.00 78.11 ? 206 ASN B C 1 ATOM 5751 O O . ASN B 2 206 ? 53.040 -58.688 47.345 1.00 82.50 ? 206 ASN B O 1 ATOM 5752 C CB . ASN B 2 206 ? 54.128 -58.420 44.935 1.00 80.09 ? 206 ASN B CB 1 ATOM 5753 C CG . ASN B 2 206 ? 53.836 -58.347 43.475 1.00 85.40 ? 206 ASN B CG 1 ATOM 5754 O OD1 . ASN B 2 206 ? 52.756 -57.909 43.075 1.00 91.84 ? 206 ASN B OD1 1 ATOM 5755 N ND2 . ASN B 2 206 ? 54.796 -58.769 42.653 1.00 86.78 ? 206 ASN B ND2 1 ATOM 5756 N N . SER B 2 207 ? 53.084 -56.511 47.891 1.00 73.13 ? 207 SER B N 1 ATOM 5757 C CA . SER B 2 207 ? 52.632 -56.772 49.244 1.00 76.83 ? 207 SER B CA 1 ATOM 5758 C C . SER B 2 207 ? 52.340 -55.491 49.980 1.00 84.52 ? 207 SER B C 1 ATOM 5759 O O . SER B 2 207 ? 52.664 -54.390 49.521 1.00 83.78 ? 207 SER B O 1 ATOM 5760 C CB . SER B 2 207 ? 53.668 -57.584 50.026 1.00 58.83 ? 207 SER B CB 1 ATOM 5761 O OG . SER B 2 207 ? 54.963 -57.048 49.838 1.00 54.75 ? 207 SER B OG 1 ATOM 5762 N N . LEU B 2 208 ? 51.709 -55.655 51.132 1.00 81.20 ? 208 LEU B N 1 ATOM 5763 C CA . LEU B 2 208 ? 51.441 -54.541 51.996 1.00 69.07 ? 208 LEU B CA 1 ATOM 5764 C C . LEU B 2 208 ? 52.787 -54.002 52.441 1.00 68.96 ? 208 LEU B C 1 ATOM 5765 O O . LEU B 2 208 ? 53.722 -54.767 52.653 1.00 68.93 ? 208 LEU B O 1 ATOM 5766 C CB . LEU B 2 208 ? 50.581 -55.009 53.163 1.00 65.42 ? 208 LEU B CB 1 ATOM 5767 C CG . LEU B 2 208 ? 49.173 -55.371 52.679 1.00 56.51 ? 208 LEU B CG 1 ATOM 5768 C CD1 . LEU B 2 208 ? 48.287 -55.917 53.785 1.00 40.79 ? 208 LEU B CD1 1 ATOM 5769 C CD2 . LEU B 2 208 ? 48.541 -54.126 52.045 1.00 58.71 ? 208 LEU B CD2 1 ATOM 5770 N N . PHE B 2 209 ? 52.897 -52.680 52.519 1.00 71.68 ? 209 PHE B N 1 ATOM 5771 C CA . PHE B 2 209 ? 54.122 -52.032 52.958 1.00 69.43 ? 209 PHE B CA 1 ATOM 5772 C C . PHE B 2 209 ? 54.363 -52.406 54.403 1.00 72.65 ? 209 PHE B C 1 ATOM 5773 O O . PHE B 2 209 ? 53.503 -52.177 55.256 1.00 68.82 ? 209 PHE B O 1 ATOM 5774 C CB . PHE B 2 209 ? 53.978 -50.516 52.837 1.00 70.69 ? 209 PHE B CB 1 ATOM 5775 C CG . PHE B 2 209 ? 55.035 -49.742 53.577 1.00 71.53 ? 209 PHE B CG 1 ATOM 5776 C CD1 . PHE B 2 209 ? 56.204 -49.349 52.935 1.00 67.60 ? 209 PHE B CD1 1 ATOM 5777 C CD2 . PHE B 2 209 ? 54.858 -49.399 54.910 1.00 61.18 ? 209 PHE B CD2 1 ATOM 5778 C CE1 . PHE B 2 209 ? 57.176 -48.634 53.614 1.00 68.77 ? 209 PHE B CE1 1 ATOM 5779 C CE2 . PHE B 2 209 ? 55.826 -48.689 55.589 1.00 59.80 ? 209 PHE B CE2 1 ATOM 5780 C CZ . PHE B 2 209 ? 56.988 -48.305 54.941 1.00 62.60 ? 209 PHE B CZ 1 ATOM 5781 N N . SER B 2 210 ? 55.522 -52.986 54.695 1.00 75.06 ? 210 SER B N 1 ATOM 5782 C CA . SER B 2 210 ? 55.753 -53.462 56.054 1.00 77.72 ? 210 SER B CA 1 ATOM 5783 C C . SER B 2 210 ? 57.159 -53.189 56.553 1.00 74.89 ? 210 SER B C 1 ATOM 5784 O O . SER B 2 210 ? 57.822 -54.080 57.057 1.00 83.86 ? 210 SER B O 1 ATOM 5785 C CB . SER B 2 210 ? 55.428 -54.955 56.170 1.00 71.75 ? 210 SER B CB 1 ATOM 5786 O OG . SER B 2 210 ? 56.459 -55.751 55.612 1.00 74.02 ? 210 SER B OG 1 ATOM 5787 N N . VAL B 2 211 ? 57.619 -51.956 56.425 1.00 67.11 ? 211 VAL B N 1 ATOM 5788 C CA . VAL B 2 211 ? 58.946 -51.643 56.921 1.00 71.42 ? 211 VAL B CA 1 ATOM 5789 C C . VAL B 2 211 ? 58.926 -51.017 58.320 1.00 74.17 ? 211 VAL B C 1 ATOM 5790 O O . VAL B 2 211 ? 58.208 -50.042 58.580 1.00 67.55 ? 211 VAL B O 1 ATOM 5791 C CB . VAL B 2 211 ? 59.728 -50.773 55.942 1.00 65.25 ? 211 VAL B CB 1 ATOM 5792 C CG1 . VAL B 2 211 ? 61.116 -50.510 56.477 1.00 70.89 ? 211 VAL B CG1 1 ATOM 5793 C CG2 . VAL B 2 211 ? 59.823 -51.470 54.635 1.00 61.60 ? 211 VAL B CG2 1 ATOM 5794 N N . GLN B 2 212 ? 59.725 -51.604 59.210 1.00 70.69 ? 212 GLN B N 1 ATOM 5795 C CA . GLN B 2 212 ? 59.844 -51.146 60.585 1.00 76.72 ? 212 GLN B CA 1 ATOM 5796 C C . GLN B 2 212 ? 61.226 -50.567 60.904 1.00 76.78 ? 212 GLN B C 1 ATOM 5797 O O . GLN B 2 212 ? 61.510 -50.240 62.046 1.00 91.14 ? 212 GLN B O 1 ATOM 5798 C CB . GLN B 2 212 ? 59.529 -52.291 61.551 1.00 89.22 ? 212 GLN B CB 1 ATOM 5799 C CG . GLN B 2 212 ? 58.049 -52.501 61.847 1.00 95.27 ? 212 GLN B CG 1 ATOM 5800 C CD . GLN B 2 212 ? 57.799 -53.713 62.734 1.00 100.97 ? 212 GLN B CD 1 ATOM 5801 O OE1 . GLN B 2 212 ? 56.948 -54.547 62.431 1.00 90.57 ? 212 GLN B OE1 1 ATOM 5802 N NE2 . GLN B 2 212 ? 58.551 -53.819 63.831 1.00 110.55 ? 212 GLN B NE2 1 ATOM 5803 N N . VAL B 2 213 ? 62.086 -50.456 59.902 1.00 68.21 ? 213 VAL B N 1 ATOM 5804 C CA . VAL B 2 213 ? 63.392 -49.839 60.076 1.00 64.51 ? 213 VAL B CA 1 ATOM 5805 C C . VAL B 2 213 ? 63.271 -48.363 60.449 1.00 69.94 ? 213 VAL B C 1 ATOM 5806 O O . VAL B 2 213 ? 62.568 -47.594 59.787 1.00 65.89 ? 213 VAL B O 1 ATOM 5807 C CB . VAL B 2 213 ? 64.236 -49.953 58.781 1.00 78.59 ? 213 VAL B CB 1 ATOM 5808 C CG1 . VAL B 2 213 ? 65.390 -48.971 58.795 1.00 70.45 ? 213 VAL B CG1 1 ATOM 5809 C CG2 . VAL B 2 213 ? 64.736 -51.375 58.586 1.00 79.42 ? 213 VAL B CG2 1 ATOM 5810 N N . ASN B 2 214 ? 63.964 -47.978 61.518 1.00 81.53 ? 214 ASN B N 1 ATOM 5811 C CA . ASN B 2 214 ? 64.052 -46.582 61.945 1.00 93.93 ? 214 ASN B CA 1 ATOM 5812 C C . ASN B 2 214 ? 65.118 -45.848 61.113 1.00 94.79 ? 214 ASN B C 1 ATOM 5813 O O . ASN B 2 214 ? 66.316 -46.064 61.303 1.00 102.77 ? 214 ASN B O 1 ATOM 5814 C CB . ASN B 2 214 ? 64.370 -46.527 63.450 1.00 102.04 ? 214 ASN B CB 1 ATOM 5815 C CG . ASN B 2 214 ? 64.137 -45.145 64.074 1.00 119.68 ? 214 ASN B CG 1 ATOM 5816 O OD1 . ASN B 2 214 ? 63.568 -44.253 63.449 1.00 102.08 ? 214 ASN B OD1 1 ATOM 5817 N ND2 . ASN B 2 214 ? 64.574 -44.981 65.337 1.00 154.70 ? 214 ASN B ND2 1 ATOM 5818 N N . MET B 2 215 ? 64.689 -44.997 60.182 1.00 80.40 ? 215 MET B N 1 ATOM 5819 C CA . MET B 2 215 ? 65.634 -44.318 59.293 1.00 82.16 ? 215 MET B CA 1 ATOM 5820 C C . MET B 2 215 ? 65.861 -42.850 59.584 1.00 79.33 ? 215 MET B C 1 ATOM 5821 O O . MET B 2 215 ? 65.004 -42.016 59.312 1.00 83.06 ? 215 MET B O 1 ATOM 5822 C CB . MET B 2 215 ? 65.198 -44.441 57.838 1.00 85.47 ? 215 MET B CB 1 ATOM 5823 C CG . MET B 2 215 ? 65.218 -45.846 57.334 1.00 92.48 ? 215 MET B CG 1 ATOM 5824 S SD . MET B 2 215 ? 65.638 -45.910 55.602 1.00 74.65 ? 215 MET B SD 1 ATOM 5825 C CE . MET B 2 215 ? 65.588 -47.686 55.375 1.00 60.13 ? 215 MET B CE 1 ATOM 5826 N N . SER B 2 216 ? 67.038 -42.527 60.095 1.00 75.07 ? 216 SER B N 1 ATOM 5827 C CA . SER B 2 216 ? 67.393 -41.132 60.286 1.00 82.54 ? 216 SER B CA 1 ATOM 5828 C C . SER B 2 216 ? 68.035 -40.506 59.044 1.00 84.24 ? 216 SER B C 1 ATOM 5829 O O . SER B 2 216 ? 68.687 -41.183 58.246 1.00 83.08 ? 216 SER B O 1 ATOM 5830 C CB . SER B 2 216 ? 68.310 -40.983 61.494 1.00 83.38 ? 216 SER B CB 1 ATOM 5831 O OG . SER B 2 216 ? 67.638 -41.416 62.660 1.00 95.01 ? 216 SER B OG 1 ATOM 5832 N N . VAL B 2 217 ? 67.820 -39.207 58.881 1.00 78.40 ? 217 VAL B N 1 ATOM 5833 C CA . VAL B 2 217 ? 68.537 -38.429 57.893 1.00 85.40 ? 217 VAL B CA 1 ATOM 5834 C C . VAL B 2 217 ? 68.784 -37.052 58.477 1.00 85.16 ? 217 VAL B C 1 ATOM 5835 O O . VAL B 2 217 ? 67.950 -36.539 59.213 1.00 78.94 ? 217 VAL B O 1 ATOM 5836 C CB . VAL B 2 217 ? 67.736 -38.280 56.585 1.00 92.70 ? 217 VAL B CB 1 ATOM 5837 C CG1 . VAL B 2 217 ? 68.452 -37.344 55.623 1.00 85.13 ? 217 VAL B CG1 1 ATOM 5838 C CG2 . VAL B 2 217 ? 67.531 -39.629 55.937 1.00 105.15 ? 217 VAL B CG2 1 ATOM 5839 N N . ASN B 2 218 ? 69.925 -36.456 58.152 1.00 93.08 ? 218 ASN B N 1 ATOM 5840 C CA . ASN B 2 218 ? 70.196 -35.081 58.546 1.00 107.61 ? 218 ASN B CA 1 ATOM 5841 C C . ASN B 2 218 ? 69.801 -34.120 57.431 1.00 100.37 ? 218 ASN B C 1 ATOM 5842 O O . ASN B 2 218 ? 68.776 -33.438 57.504 1.00 95.70 ? 218 ASN B O 1 ATOM 5843 C CB . ASN B 2 218 ? 71.678 -34.892 58.875 1.00 126.52 ? 218 ASN B CB 1 ATOM 5844 C CG . ASN B 2 218 ? 72.424 -36.208 58.987 1.00 137.99 ? 218 ASN B CG 1 ATOM 5845 O OD1 . ASN B 2 218 ? 73.041 -36.501 60.016 1.00 142.35 ? 218 ASN B OD1 1 ATOM 5846 N ND2 . ASN B 2 218 ? 72.376 -37.012 57.923 1.00 131.43 ? 218 ASN B ND2 1 ATOM 5847 N N . ALA B 2 219 ? 70.628 -34.074 56.393 1.00 90.64 ? 219 ALA B N 1 ATOM 5848 C CA . ALA B 2 219 ? 70.400 -33.166 55.281 1.00 82.38 ? 219 ALA B CA 1 ATOM 5849 C C . ALA B 2 219 ? 69.779 -33.915 54.110 1.00 83.06 ? 219 ALA B C 1 ATOM 5850 O O . ALA B 2 219 ? 70.392 -34.832 53.566 1.00 91.92 ? 219 ALA B O 1 ATOM 5851 C CB . ALA B 2 219 ? 71.705 -32.508 54.863 1.00 75.94 ? 219 ALA B CB 1 ATOM 5852 N N . LEU B 2 220 ? 68.565 -33.519 53.727 1.00 66.09 ? 220 LEU B N 1 ATOM 5853 C CA . LEU B 2 220 ? 67.830 -34.200 52.670 1.00 50.93 ? 220 LEU B CA 1 ATOM 5854 C C . LEU B 2 220 ? 67.048 -33.211 51.816 1.00 59.85 ? 220 LEU B C 1 ATOM 5855 O O . LEU B 2 220 ? 66.345 -32.358 52.338 1.00 71.62 ? 220 LEU B O 1 ATOM 5856 C CB . LEU B 2 220 ? 66.875 -35.229 53.268 1.00 51.86 ? 220 LEU B CB 1 ATOM 5857 C CG . LEU B 2 220 ? 66.364 -36.235 52.250 1.00 61.41 ? 220 LEU B CG 1 ATOM 5858 C CD1 . LEU B 2 220 ? 67.543 -36.823 51.489 1.00 70.46 ? 220 LEU B CD1 1 ATOM 5859 C CD2 . LEU B 2 220 ? 65.550 -37.312 52.916 1.00 58.92 ? 220 LEU B CD2 1 ATOM 5860 N N . GLY B 2 221 ? 67.176 -33.317 50.501 1.00 55.44 ? 221 GLY B N 1 ATOM 5861 C CA . GLY B 2 221 ? 66.501 -32.385 49.627 1.00 58.00 ? 221 GLY B CA 1 ATOM 5862 C C . GLY B 2 221 ? 65.210 -32.979 49.113 1.00 70.33 ? 221 GLY B C 1 ATOM 5863 O O . GLY B 2 221 ? 64.197 -32.292 48.969 1.00 74.48 ? 221 GLY B O 1 ATOM 5864 N N . HIS B 2 222 ? 65.250 -34.276 48.846 1.00 68.52 ? 222 HIS B N 1 ATOM 5865 C CA . HIS B 2 222 ? 64.138 -34.956 48.216 1.00 64.55 ? 222 HIS B CA 1 ATOM 5866 C C . HIS B 2 222 ? 64.099 -36.384 48.722 1.00 68.46 ? 222 HIS B C 1 ATOM 5867 O O . HIS B 2 222 ? 65.053 -37.146 48.564 1.00 71.04 ? 222 HIS B O 1 ATOM 5868 C CB . HIS B 2 222 ? 64.316 -34.920 46.696 1.00 76.18 ? 222 HIS B CB 1 ATOM 5869 C CG . HIS B 2 222 ? 63.117 -35.375 45.922 1.00 85.87 ? 222 HIS B CG 1 ATOM 5870 N ND1 . HIS B 2 222 ? 61.830 -35.014 46.258 1.00 90.01 ? 222 HIS B ND1 1 ATOM 5871 C CD2 . HIS B 2 222 ? 63.014 -36.135 44.806 1.00 79.06 ? 222 HIS B CD2 1 ATOM 5872 C CE1 . HIS B 2 222 ? 60.985 -35.547 45.394 1.00 78.87 ? 222 HIS B CE1 1 ATOM 5873 N NE2 . HIS B 2 222 ? 61.678 -36.234 44.504 1.00 72.74 ? 222 HIS B NE2 1 ATOM 5874 N N . LEU B 2 223 ? 63.002 -36.726 49.378 1.00 70.28 ? 223 LEU B N 1 ATOM 5875 C CA . LEU B 2 223 ? 62.759 -38.098 49.766 1.00 72.58 ? 223 LEU B CA 1 ATOM 5876 C C . LEU B 2 223 ? 61.864 -38.676 48.705 1.00 77.30 ? 223 LEU B C 1 ATOM 5877 O O . LEU B 2 223 ? 60.950 -38.005 48.237 1.00 90.92 ? 223 LEU B O 1 ATOM 5878 C CB . LEU B 2 223 ? 62.045 -38.162 51.108 1.00 69.47 ? 223 LEU B CB 1 ATOM 5879 C CG . LEU B 2 223 ? 61.589 -39.571 51.459 1.00 58.82 ? 223 LEU B CG 1 ATOM 5880 C CD1 . LEU B 2 223 ? 62.803 -40.448 51.758 1.00 56.37 ? 223 LEU B CD1 1 ATOM 5881 C CD2 . LEU B 2 223 ? 60.665 -39.501 52.635 1.00 50.93 ? 223 LEU B CD2 1 ATOM 5882 N N . GLN B 2 224 ? 62.112 -39.915 48.313 1.00 71.80 ? 224 GLN B N 1 ATOM 5883 C CA . GLN B 2 224 ? 61.251 -40.531 47.320 1.00 65.91 ? 224 GLN B CA 1 ATOM 5884 C C . GLN B 2 224 ? 61.009 -42.014 47.550 1.00 60.72 ? 224 GLN B C 1 ATOM 5885 O O . GLN B 2 224 ? 61.953 -42.806 47.601 1.00 55.81 ? 224 GLN B O 1 ATOM 5886 C CB . GLN B 2 224 ? 61.814 -40.301 45.936 1.00 68.38 ? 224 GLN B CB 1 ATOM 5887 C CG . GLN B 2 224 ? 60.776 -40.479 44.881 1.00 79.60 ? 224 GLN B CG 1 ATOM 5888 C CD . GLN B 2 224 ? 61.389 -40.776 43.557 1.00 75.68 ? 224 GLN B CD 1 ATOM 5889 O OE1 . GLN B 2 224 ? 62.477 -40.275 43.252 1.00 78.37 ? 224 GLN B OE1 1 ATOM 5890 N NE2 . GLN B 2 224 ? 60.714 -41.614 42.758 1.00 57.93 ? 224 GLN B NE2 1 ATOM 5891 N N . LEU B 2 225 ? 59.734 -42.376 47.684 1.00 57.31 ? 225 LEU B N 1 ATOM 5892 C CA . LEU B 2 225 ? 59.352 -43.749 47.995 1.00 61.84 ? 225 LEU B CA 1 ATOM 5893 C C . LEU B 2 225 ? 58.574 -44.342 46.840 1.00 60.79 ? 225 LEU B C 1 ATOM 5894 O O . LEU B 2 225 ? 57.705 -43.679 46.280 1.00 53.44 ? 225 LEU B O 1 ATOM 5895 C CB . LEU B 2 225 ? 58.469 -43.828 49.249 1.00 60.09 ? 225 LEU B CB 1 ATOM 5896 C CG . LEU B 2 225 ? 58.632 -42.941 50.481 1.00 62.35 ? 225 LEU B CG 1 ATOM 5897 C CD1 . LEU B 2 225 ? 57.862 -43.569 51.618 1.00 52.03 ? 225 LEU B CD1 1 ATOM 5898 C CD2 . LEU B 2 225 ? 60.079 -42.754 50.867 1.00 62.34 ? 225 LEU B CD2 1 ATOM 5899 N N . SER B 2 226 ? 58.861 -45.603 46.523 1.00 62.59 ? 226 SER B N 1 ATOM 5900 C CA . SER B 2 226 ? 58.214 -46.303 45.419 1.00 62.37 ? 226 SER B CA 1 ATOM 5901 C C . SER B 2 226 ? 57.664 -47.670 45.831 1.00 70.04 ? 226 SER B C 1 ATOM 5902 O O . SER B 2 226 ? 58.311 -48.407 46.568 1.00 72.28 ? 226 SER B O 1 ATOM 5903 C CB . SER B 2 226 ? 59.197 -46.466 44.267 1.00 61.85 ? 226 SER B CB 1 ATOM 5904 O OG . SER B 2 226 ? 59.666 -45.203 43.819 1.00 74.98 ? 226 SER B OG 1 ATOM 5905 N N . ASN B 2 227 ? 56.472 -47.998 45.332 1.00 71.21 ? 227 ASN B N 1 ATOM 5906 C CA . ASN B 2 227 ? 55.781 -49.245 45.662 1.00 59.75 ? 227 ASN B CA 1 ATOM 5907 C C . ASN B 2 227 ? 55.195 -49.219 47.076 1.00 70.75 ? 227 ASN B C 1 ATOM 5908 O O . ASN B 2 227 ? 55.671 -49.906 47.982 1.00 75.18 ? 227 ASN B O 1 ATOM 5909 C CB . ASN B 2 227 ? 56.696 -50.463 45.487 1.00 57.41 ? 227 ASN B CB 1 ATOM 5910 C CG . ASN B 2 227 ? 57.258 -50.598 44.066 1.00 62.39 ? 227 ASN B CG 1 ATOM 5911 O OD1 . ASN B 2 227 ? 56.835 -49.911 43.130 1.00 54.85 ? 227 ASN B OD1 1 ATOM 5912 N ND2 . ASN B 2 227 ? 58.222 -51.500 43.909 1.00 59.43 ? 227 ASN B ND2 1 ATOM 5913 N N . ILE B 2 228 ? 54.148 -48.425 47.254 1.00 65.97 ? 228 ILE B N 1 ATOM 5914 C CA . ILE B 2 228 ? 53.504 -48.284 48.548 1.00 54.92 ? 228 ILE B CA 1 ATOM 5915 C C . ILE B 2 228 ? 52.075 -48.796 48.481 1.00 59.09 ? 228 ILE B C 1 ATOM 5916 O O . ILE B 2 228 ? 51.217 -48.168 47.861 1.00 60.36 ? 228 ILE B O 1 ATOM 5917 C CB . ILE B 2 228 ? 53.464 -46.814 48.962 1.00 44.63 ? 228 ILE B CB 1 ATOM 5918 C CG1 . ILE B 2 228 ? 54.837 -46.183 48.760 1.00 43.58 ? 228 ILE B CG1 1 ATOM 5919 C CG2 . ILE B 2 228 ? 52.980 -46.672 50.415 1.00 44.71 ? 228 ILE B CG2 1 ATOM 5920 C CD1 . ILE B 2 228 ? 54.819 -44.686 48.846 1.00 52.03 ? 228 ILE B CD1 1 ATOM 5921 N N . LYS B 2 229 ? 51.820 -49.931 49.123 1.00 53.90 ? 229 LYS B N 1 ATOM 5922 C CA . LYS B 2 229 ? 50.481 -50.516 49.147 1.00 47.53 ? 229 LYS B CA 1 ATOM 5923 C C . LYS B 2 229 ? 49.916 -50.488 50.560 1.00 59.18 ? 229 LYS B C 1 ATOM 5924 O O . LYS B 2 229 ? 50.444 -51.147 51.454 1.00 60.70 ? 229 LYS B O 1 ATOM 5925 C CB . LYS B 2 229 ? 50.531 -51.955 48.647 1.00 40.19 ? 229 LYS B CB 1 ATOM 5926 C CG . LYS B 2 229 ? 49.201 -52.689 48.648 1.00 53.88 ? 229 LYS B CG 1 ATOM 5927 C CD . LYS B 2 229 ? 49.416 -54.128 48.187 1.00 69.20 ? 229 LYS B CD 1 ATOM 5928 C CE . LYS B 2 229 ? 48.123 -54.854 47.848 1.00 75.26 ? 229 LYS B CE 1 ATOM 5929 N NZ . LYS B 2 229 ? 48.394 -55.980 46.900 1.00 77.43 ? 229 LYS B NZ 1 ATOM 5930 N N . LEU B 2 230 ? 48.838 -49.735 50.760 1.00 58.56 ? 230 LEU B N 1 ATOM 5931 C CA . LEU B 2 230 ? 48.276 -49.551 52.093 1.00 55.02 ? 230 LEU B CA 1 ATOM 5932 C C . LEU B 2 230 ? 46.790 -49.837 52.155 1.00 56.31 ? 230 LEU B C 1 ATOM 5933 O O . LEU B 2 230 ? 46.040 -49.466 51.258 1.00 69.12 ? 230 LEU B O 1 ATOM 5934 C CB . LEU B 2 230 ? 48.498 -48.116 52.564 1.00 51.46 ? 230 LEU B CB 1 ATOM 5935 C CG . LEU B 2 230 ? 49.882 -47.540 52.308 1.00 60.54 ? 230 LEU B CG 1 ATOM 5936 C CD1 . LEU B 2 230 ? 49.835 -46.024 52.303 1.00 54.30 ? 230 LEU B CD1 1 ATOM 5937 C CD2 . LEU B 2 230 ? 50.844 -48.065 53.357 1.00 72.76 ? 230 LEU B CD2 1 ATOM 5938 N N . ASN B 2 231 ? 46.371 -50.507 53.218 1.00 50.94 ? 231 ASN B N 1 ATOM 5939 C CA . ASN B 2 231 ? 44.984 -50.427 53.648 1.00 64.99 ? 231 ASN B CA 1 ATOM 5940 C C . ASN B 2 231 ? 44.922 -49.612 54.936 1.00 61.58 ? 231 ASN B C 1 ATOM 5941 O O . ASN B 2 231 ? 45.820 -48.815 55.206 1.00 64.54 ? 231 ASN B O 1 ATOM 5942 C CB . ASN B 2 231 ? 44.345 -51.811 53.807 1.00 80.52 ? 231 ASN B CB 1 ATOM 5943 C CG . ASN B 2 231 ? 45.315 -52.848 54.311 1.00 76.16 ? 231 ASN B CG 1 ATOM 5944 O OD1 . ASN B 2 231 ? 45.892 -52.693 55.381 1.00 78.43 ? 231 ASN B OD1 1 ATOM 5945 N ND2 . ASN B 2 231 ? 45.487 -53.922 53.550 1.00 62.38 ? 231 ASN B ND2 1 ATOM 5946 N N . ASP B 2 232 ? 43.874 -49.785 55.727 1.00 54.29 ? 232 ASP B N 1 ATOM 5947 C CA . ASP B 2 232 ? 43.781 -49.016 56.965 1.00 67.94 ? 232 ASP B CA 1 ATOM 5948 C C . ASP B 2 232 ? 44.629 -49.653 58.065 1.00 82.65 ? 232 ASP B C 1 ATOM 5949 O O . ASP B 2 232 ? 45.120 -48.960 58.961 1.00 84.07 ? 232 ASP B O 1 ATOM 5950 C CB . ASP B 2 232 ? 42.330 -48.885 57.407 1.00 74.93 ? 232 ASP B CB 1 ATOM 5951 C CG . ASP B 2 232 ? 41.419 -48.456 56.274 1.00 83.21 ? 232 ASP B CG 1 ATOM 5952 O OD1 . ASP B 2 232 ? 41.778 -47.494 55.562 1.00 76.85 ? 232 ASP B OD1 1 ATOM 5953 O OD2 . ASP B 2 232 ? 40.352 -49.080 56.096 1.00 87.73 ? 232 ASP B OD2 1 ATOM 5954 N N . GLU B 2 233 ? 44.821 -50.970 57.963 1.00 88.59 ? 233 GLU B N 1 ATOM 5955 C CA . GLU B 2 233 ? 45.547 -51.758 58.960 1.00 84.53 ? 233 GLU B CA 1 ATOM 5956 C C . GLU B 2 233 ? 47.063 -51.528 58.985 1.00 82.46 ? 233 GLU B C 1 ATOM 5957 O O . GLU B 2 233 ? 47.718 -51.842 59.980 1.00 85.96 ? 233 GLU B O 1 ATOM 5958 C CB . GLU B 2 233 ? 45.258 -53.251 58.777 1.00 86.59 ? 233 GLU B CB 1 ATOM 5959 C CG . GLU B 2 233 ? 43.841 -53.669 59.157 1.00 104.11 ? 233 GLU B CG 1 ATOM 5960 C CD . GLU B 2 233 ? 43.743 -55.147 59.536 1.00 123.98 ? 233 GLU B CD 1 ATOM 5961 O OE1 . GLU B 2 233 ? 44.558 -55.948 59.029 1.00 129.74 ? 233 GLU B OE1 1 ATOM 5962 O OE2 . GLU B 2 233 ? 42.854 -55.505 60.345 1.00 127.24 ? 233 GLU B OE2 1 ATOM 5963 N N . ASN B 2 234 ? 47.619 -51.001 57.894 1.00 71.14 ? 234 ASN B N 1 ATOM 5964 C CA . ASN B 2 234 ? 49.053 -50.713 57.828 1.00 66.28 ? 234 ASN B CA 1 ATOM 5965 C C . ASN B 2 234 ? 49.340 -49.269 57.446 1.00 71.24 ? 234 ASN B C 1 ATOM 5966 O O . ASN B 2 234 ? 50.493 -48.908 57.189 1.00 61.01 ? 234 ASN B O 1 ATOM 5967 C CB . ASN B 2 234 ? 49.785 -51.667 56.875 1.00 62.43 ? 234 ASN B CB 1 ATOM 5968 C CG . ASN B 2 234 ? 49.603 -51.293 55.406 1.00 68.13 ? 234 ASN B CG 1 ATOM 5969 O OD1 . ASN B 2 234 ? 48.540 -50.828 54.995 1.00 77.78 ? 234 ASN B OD1 1 ATOM 5970 N ND2 . ASN B 2 234 ? 50.644 -51.498 54.612 1.00 56.32 ? 234 ASN B ND2 1 ATOM 5971 N N . CYS B 2 235 ? 48.286 -48.453 57.411 1.00 77.57 ? 235 CYS B N 1 ATOM 5972 C CA . CYS B 2 235 ? 48.415 -47.024 57.141 1.00 76.82 ? 235 CYS B CA 1 ATOM 5973 C C . CYS B 2 235 ? 49.442 -46.404 58.079 1.00 74.42 ? 235 CYS B C 1 ATOM 5974 O O . CYS B 2 235 ? 50.382 -45.747 57.627 1.00 59.63 ? 235 CYS B O 1 ATOM 5975 C CB . CYS B 2 235 ? 47.065 -46.303 57.290 1.00 81.97 ? 235 CYS B CB 1 ATOM 5976 S SG . CYS B 2 235 ? 47.006 -44.614 56.582 1.00 82.99 ? 235 CYS B SG 1 ATOM 5977 N N . GLN B 2 236 ? 49.268 -46.634 59.383 1.00 74.82 ? 236 GLN B N 1 ATOM 5978 C CA . GLN B 2 236 ? 50.136 -46.031 60.392 1.00 62.16 ? 236 GLN B CA 1 ATOM 5979 C C . GLN B 2 236 ? 51.589 -46.495 60.296 1.00 61.64 ? 236 GLN B C 1 ATOM 5980 O O . GLN B 2 236 ? 52.506 -45.712 60.547 1.00 63.41 ? 236 GLN B O 1 ATOM 5981 C CB . GLN B 2 236 ? 49.584 -46.271 61.800 1.00 65.17 ? 236 GLN B CB 1 ATOM 5982 C CG . GLN B 2 236 ? 50.463 -45.732 62.927 1.00 64.68 ? 236 GLN B CG 1 ATOM 5983 C CD . GLN B 2 236 ? 50.464 -44.206 63.029 1.00 64.74 ? 236 GLN B CD 1 ATOM 5984 O OE1 . GLN B 2 236 ? 49.407 -43.574 63.100 1.00 63.36 ? 236 GLN B OE1 1 ATOM 5985 N NE2 . GLN B 2 236 ? 51.660 -43.611 63.063 1.00 55.18 ? 236 GLN B NE2 1 ATOM 5986 N N . ARG B 2 237 ? 51.799 -47.759 59.941 1.00 63.78 ? 237 ARG B N 1 ATOM 5987 C CA . ARG B 2 237 ? 53.156 -48.269 59.710 1.00 71.80 ? 237 ARG B CA 1 ATOM 5988 C C . ARG B 2 237 ? 53.964 -47.341 58.796 1.00 66.62 ? 237 ARG B C 1 ATOM 5989 O O . ARG B 2 237 ? 55.136 -47.051 59.081 1.00 65.11 ? 237 ARG B O 1 ATOM 5990 C CB . ARG B 2 237 ? 53.115 -49.671 59.102 1.00 77.18 ? 237 ARG B CB 1 ATOM 5991 C CG . ARG B 2 237 ? 54.355 -50.527 59.339 1.00 77.36 ? 237 ARG B CG 1 ATOM 5992 C CD . ARG B 2 237 ? 54.086 -51.608 60.391 1.00 102.16 ? 237 ARG B CD 1 ATOM 5993 N NE . ARG B 2 237 ? 54.649 -52.902 59.997 1.00 121.44 ? 237 ARG B NE 1 ATOM 5994 C CZ . ARG B 2 237 ? 53.946 -53.913 59.484 1.00 126.35 ? 237 ARG B CZ 1 ATOM 5995 N NH1 . ARG B 2 237 ? 52.632 -53.799 59.304 1.00 129.40 ? 237 ARG B NH1 1 ATOM 5996 N NH2 . ARG B 2 237 ? 54.558 -55.046 59.157 1.00 118.07 ? 237 ARG B NH2 1 ATOM 5997 N N . LEU B 2 238 ? 53.334 -46.886 57.705 1.00 52.26 ? 238 LEU B N 1 ATOM 5998 C CA . LEU B 2 238 ? 53.972 -45.962 56.766 1.00 48.69 ? 238 LEU B CA 1 ATOM 5999 C C . LEU B 2 238 ? 54.205 -44.581 57.353 1.00 62.90 ? 238 LEU B C 1 ATOM 6000 O O . LEU B 2 238 ? 55.250 -43.979 57.122 1.00 70.26 ? 238 LEU B O 1 ATOM 6001 C CB . LEU B 2 238 ? 53.162 -45.803 55.479 1.00 43.93 ? 238 LEU B CB 1 ATOM 6002 C CG . LEU B 2 238 ? 53.795 -44.759 54.543 1.00 47.91 ? 238 LEU B CG 1 ATOM 6003 C CD1 . LEU B 2 238 ? 55.178 -45.216 54.101 1.00 43.75 ? 238 LEU B CD1 1 ATOM 6004 C CD2 . LEU B 2 238 ? 52.942 -44.447 53.339 1.00 39.33 ? 238 LEU B CD2 1 ATOM 6005 N N . MET B 2 239 ? 53.222 -44.070 58.091 1.00 65.64 ? 239 MET B N 1 ATOM 6006 C CA . MET B 2 239 ? 53.340 -42.747 58.705 1.00 63.90 ? 239 MET B CA 1 ATOM 6007 C C . MET B 2 239 ? 54.464 -42.695 59.737 1.00 66.96 ? 239 MET B C 1 ATOM 6008 O O . MET B 2 239 ? 55.154 -41.683 59.862 1.00 69.48 ? 239 MET B O 1 ATOM 6009 C CB . MET B 2 239 ? 52.006 -42.297 59.313 1.00 68.39 ? 239 MET B CB 1 ATOM 6010 C CG . MET B 2 239 ? 51.062 -41.595 58.319 1.00 61.72 ? 239 MET B CG 1 ATOM 6011 S SD . MET B 2 239 ? 49.388 -41.389 58.966 1.00 76.97 ? 239 MET B SD 1 ATOM 6012 C CE . MET B 2 239 ? 49.651 -40.225 60.306 1.00 137.20 ? 239 MET B CE 1 ATOM 6013 N N . THR B 2 240 ? 54.648 -43.796 60.462 1.00 65.52 ? 240 THR B N 1 ATOM 6014 C CA . THR B 2 240 ? 55.747 -43.924 61.417 1.00 59.14 ? 240 THR B CA 1 ATOM 6015 C C . THR B 2 240 ? 57.108 -43.970 60.722 1.00 69.15 ? 240 THR B C 1 ATOM 6016 O O . THR B 2 240 ? 58.069 -43.304 61.141 1.00 59.93 ? 240 THR B O 1 ATOM 6017 C CB . THR B 2 240 ? 55.625 -45.211 62.221 1.00 58.08 ? 240 THR B CB 1 ATOM 6018 O OG1 . THR B 2 240 ? 54.407 -45.197 62.977 1.00 62.49 ? 240 THR B OG1 1 ATOM 6019 C CG2 . THR B 2 240 ? 56.798 -45.348 63.136 1.00 47.01 ? 240 THR B CG2 1 ATOM 6020 N N . PHE B 2 241 ? 57.188 -44.786 59.674 1.00 73.23 ? 241 PHE B N 1 ATOM 6021 C CA . PHE B 2 241 ? 58.429 -44.951 58.942 1.00 66.78 ? 241 PHE B CA 1 ATOM 6022 C C . PHE B 2 241 ? 58.858 -43.619 58.340 1.00 69.51 ? 241 PHE B C 1 ATOM 6023 O O . PHE B 2 241 ? 60.056 -43.326 58.241 1.00 76.11 ? 241 PHE B O 1 ATOM 6024 C CB . PHE B 2 241 ? 58.274 -46.022 57.861 1.00 61.96 ? 241 PHE B CB 1 ATOM 6025 C CG . PHE B 2 241 ? 59.410 -46.062 56.874 1.00 67.59 ? 241 PHE B CG 1 ATOM 6026 C CD1 . PHE B 2 241 ? 60.514 -46.870 57.096 1.00 74.66 ? 241 PHE B CD1 1 ATOM 6027 C CD2 . PHE B 2 241 ? 59.372 -45.291 55.718 1.00 63.45 ? 241 PHE B CD2 1 ATOM 6028 C CE1 . PHE B 2 241 ? 61.562 -46.908 56.182 1.00 75.67 ? 241 PHE B CE1 1 ATOM 6029 C CE2 . PHE B 2 241 ? 60.421 -45.322 54.804 1.00 65.30 ? 241 PHE B CE2 1 ATOM 6030 C CZ . PHE B 2 241 ? 61.516 -46.129 55.034 1.00 63.54 ? 241 PHE B CZ 1 ATOM 6031 N N . LEU B 2 242 ? 57.874 -42.811 57.956 1.00 68.01 ? 242 LEU B N 1 ATOM 6032 C CA . LEU B 2 242 ? 58.129 -41.534 57.294 1.00 74.49 ? 242 LEU B CA 1 ATOM 6033 C C . LEU B 2 242 ? 58.500 -40.487 58.320 1.00 71.32 ? 242 LEU B C 1 ATOM 6034 O O . LEU B 2 242 ? 59.268 -39.565 58.039 1.00 62.21 ? 242 LEU B O 1 ATOM 6035 C CB . LEU B 2 242 ? 56.883 -41.046 56.545 1.00 66.33 ? 242 LEU B CB 1 ATOM 6036 C CG . LEU B 2 242 ? 56.516 -41.559 55.160 1.00 49.22 ? 242 LEU B CG 1 ATOM 6037 C CD1 . LEU B 2 242 ? 55.106 -41.127 54.805 1.00 48.52 ? 242 LEU B CD1 1 ATOM 6038 C CD2 . LEU B 2 242 ? 57.479 -41.023 54.154 1.00 50.38 ? 242 LEU B CD2 1 ATOM 6039 N N . SER B 2 243 ? 57.924 -40.634 59.507 1.00 75.76 ? 243 SER B N 1 ATOM 6040 C CA . SER B 2 243 ? 58.068 -39.644 60.567 1.00 83.51 ? 243 SER B CA 1 ATOM 6041 C C . SER B 2 243 ? 59.499 -39.164 60.768 1.00 81.03 ? 243 SER B C 1 ATOM 6042 O O . SER B 2 243 ? 59.725 -37.974 60.954 1.00 88.22 ? 243 SER B O 1 ATOM 6043 C CB . SER B 2 243 ? 57.511 -40.175 61.884 1.00 88.22 ? 243 SER B CB 1 ATOM 6044 O OG . SER B 2 243 ? 57.936 -39.355 62.959 1.00 102.99 ? 243 SER B OG 1 ATOM 6045 N N . GLU B 2 244 ? 60.461 -40.079 60.724 1.00 73.18 ? 244 GLU B N 1 ATOM 6046 C CA . GLU B 2 244 ? 61.847 -39.728 61.017 1.00 72.61 ? 244 GLU B CA 1 ATOM 6047 C C . GLU B 2 244 ? 62.682 -39.289 59.798 1.00 78.54 ? 244 GLU B C 1 ATOM 6048 O O . GLU B 2 244 ? 63.674 -38.577 59.946 1.00 88.46 ? 244 GLU B O 1 ATOM 6049 C CB . GLU B 2 244 ? 62.530 -40.868 61.768 1.00 76.03 ? 244 GLU B CB 1 ATOM 6050 C CG . GLU B 2 244 ? 63.701 -40.425 62.634 1.00 94.99 ? 244 GLU B CG 1 ATOM 6051 C CD . GLU B 2 244 ? 63.297 -39.427 63.705 1.00 110.34 ? 244 GLU B CD 1 ATOM 6052 O OE1 . GLU B 2 244 ? 62.198 -39.584 64.291 1.00 114.08 ? 244 GLU B OE1 1 ATOM 6053 O OE2 . GLU B 2 244 ? 64.084 -38.488 63.960 1.00 113.20 ? 244 GLU B OE2 1 ATOM 6054 N N . LEU B 2 245 ? 62.291 -39.708 58.599 1.00 75.41 ? 245 LEU B N 1 ATOM 6055 C CA . LEU B 2 245 ? 62.948 -39.219 57.389 1.00 79.73 ? 245 LEU B CA 1 ATOM 6056 C C . LEU B 2 245 ? 62.453 -37.805 57.118 1.00 80.57 ? 245 LEU B C 1 ATOM 6057 O O . LEU B 2 245 ? 63.051 -37.044 56.364 1.00 77.79 ? 245 LEU B O 1 ATOM 6058 C CB . LEU B 2 245 ? 62.645 -40.127 56.193 1.00 77.15 ? 245 LEU B CB 1 ATOM 6059 C CG . LEU B 2 245 ? 63.144 -41.572 56.287 1.00 77.59 ? 245 LEU B CG 1 ATOM 6060 C CD1 . LEU B 2 245 ? 62.415 -42.473 55.314 1.00 72.73 ? 245 LEU B CD1 1 ATOM 6061 C CD2 . LEU B 2 245 ? 64.633 -41.648 56.043 1.00 82.35 ? 245 LEU B CD2 1 ATOM 6062 N N . THR B 2 246 ? 61.358 -37.458 57.777 1.00 82.54 ? 246 THR B N 1 ATOM 6063 C CA . THR B 2 246 ? 60.643 -36.224 57.501 1.00 81.33 ? 246 THR B CA 1 ATOM 6064 C C . THR B 2 246 ? 60.830 -35.126 58.549 1.00 92.18 ? 246 THR B C 1 ATOM 6065 O O . THR B 2 246 ? 60.553 -33.954 58.280 1.00 86.95 ? 246 THR B O 1 ATOM 6066 C CB . THR B 2 246 ? 59.165 -36.517 57.362 1.00 76.18 ? 246 THR B CB 1 ATOM 6067 O OG1 . THR B 2 246 ? 58.887 -36.814 55.991 1.00 66.93 ? 246 THR B OG1 1 ATOM 6068 C CG2 . THR B 2 246 ? 58.345 -35.326 57.811 1.00 76.36 ? 246 THR B CG2 1 ATOM 6069 N N . ARG B 2 247 ? 61.280 -35.501 59.746 1.00 100.72 ? 247 ARG B N 1 ATOM 6070 C CA . ARG B 2 247 ? 61.618 -34.507 60.759 1.00 87.57 ? 247 ARG B CA 1 ATOM 6071 C C . ARG B 2 247 ? 62.559 -33.521 60.086 1.00 86.47 ? 247 ARG B C 1 ATOM 6072 O O . ARG B 2 247 ? 63.433 -33.912 59.305 1.00 81.96 ? 247 ARG B O 1 ATOM 6073 C CB . ARG B 2 247 ? 62.241 -35.153 62.003 1.00 81.54 ? 247 ARG B CB 1 ATOM 6074 C CG . ARG B 2 247 ? 61.203 -35.755 62.965 1.00 98.47 ? 247 ARG B CG 1 ATOM 6075 C CD . ARG B 2 247 ? 61.819 -36.291 64.252 1.00 107.46 ? 247 ARG B CD 1 ATOM 6076 N NE . ARG B 2 247 ? 62.632 -35.282 64.925 1.00 124.64 ? 247 ARG B NE 1 ATOM 6077 C CZ . ARG B 2 247 ? 63.312 -35.490 66.050 1.00 141.97 ? 247 ARG B CZ 1 ATOM 6078 N NH1 . ARG B 2 247 ? 63.280 -36.679 66.644 1.00 147.29 ? 247 ARG B NH1 1 ATOM 6079 N NH2 . ARG B 2 247 ? 64.026 -34.506 66.583 1.00 145.73 ? 247 ARG B NH2 1 ATOM 6080 N N . GLY B 2 248 ? 62.362 -32.242 60.361 1.00 86.88 ? 248 GLY B N 1 ATOM 6081 C CA . GLY B 2 248 ? 62.977 -31.227 59.536 1.00 99.26 ? 248 GLY B CA 1 ATOM 6082 C C . GLY B 2 248 ? 64.111 -30.371 60.071 1.00 116.28 ? 248 GLY B C 1 ATOM 6083 O O . GLY B 2 248 ? 63.936 -29.574 61.007 1.00 104.87 ? 248 GLY B O 1 ATOM 6084 N N . PRO B 2 249 ? 65.305 -30.550 59.491 1.00 128.23 ? 249 PRO B N 1 ATOM 6085 C CA . PRO B 2 249 ? 66.079 -29.324 59.333 1.00 132.88 ? 249 PRO B CA 1 ATOM 6086 C C . PRO B 2 249 ? 65.259 -28.383 58.444 1.00 124.16 ? 249 PRO B C 1 ATOM 6087 O O . PRO B 2 249 ? 64.122 -28.026 58.787 1.00 117.79 ? 249 PRO B O 1 ATOM 6088 C CB . PRO B 2 249 ? 67.337 -29.805 58.605 1.00 126.17 ? 249 PRO B CB 1 ATOM 6089 C CG . PRO B 2 249 ? 67.532 -31.194 59.119 1.00 124.50 ? 249 PRO B CG 1 ATOM 6090 C CD . PRO B 2 249 ? 66.135 -31.757 59.324 1.00 124.56 ? 249 PRO B CD 1 ATOM 6091 N N . THR B 2 250 ? 65.812 -28.001 57.300 1.00 112.59 ? 250 THR B N 1 ATOM 6092 C CA . THR B 2 250 ? 65.112 -27.072 56.423 1.00 120.50 ? 250 THR B CA 1 ATOM 6093 C C . THR B 2 250 ? 63.945 -27.749 55.691 1.00 116.11 ? 250 THR B C 1 ATOM 6094 O O . THR B 2 250 ? 63.289 -28.631 56.246 1.00 115.80 ? 250 THR B O 1 ATOM 6095 C CB . THR B 2 250 ? 66.078 -26.405 55.424 1.00 127.37 ? 250 THR B CB 1 ATOM 6096 O OG1 . THR B 2 250 ? 66.593 -27.389 54.517 1.00 133.22 ? 250 THR B OG1 1 ATOM 6097 C CG2 . THR B 2 250 ? 67.234 -25.733 56.175 1.00 118.47 ? 250 THR B CG2 1 ATOM 6098 N N . LEU B 2 251 ? 63.686 -27.324 54.456 1.00 105.81 ? 251 LEU B N 1 ATOM 6099 C CA . LEU B 2 251 ? 62.594 -27.879 53.658 1.00 91.03 ? 251 LEU B CA 1 ATOM 6100 C C . LEU B 2 251 ? 63.082 -29.041 52.815 1.00 88.66 ? 251 LEU B C 1 ATOM 6101 O O . LEU B 2 251 ? 64.277 -29.177 52.567 1.00 98.12 ? 251 LEU B O 1 ATOM 6102 C CB . LEU B 2 251 ? 61.980 -26.817 52.739 1.00 75.50 ? 251 LEU B CB 1 ATOM 6103 C CG . LEU B 2 251 ? 61.178 -25.693 53.391 1.00 75.29 ? 251 LEU B CG 1 ATOM 6104 C CD1 . LEU B 2 251 ? 60.069 -26.278 54.245 1.00 73.20 ? 251 LEU B CD1 1 ATOM 6105 C CD2 . LEU B 2 251 ? 62.081 -24.770 54.224 1.00 83.87 ? 251 LEU B CD2 1 ATOM 6106 N N . LEU B 2 252 ? 62.149 -29.877 52.380 1.00 74.72 ? 252 LEU B N 1 ATOM 6107 C CA . LEU B 2 252 ? 62.459 -30.959 51.460 1.00 71.76 ? 252 LEU B CA 1 ATOM 6108 C C . LEU B 2 252 ? 61.229 -31.288 50.637 1.00 79.19 ? 252 LEU B C 1 ATOM 6109 O O . LEU B 2 252 ? 60.103 -30.992 51.028 1.00 81.42 ? 252 LEU B O 1 ATOM 6110 C CB . LEU B 2 252 ? 62.944 -32.216 52.195 1.00 69.84 ? 252 LEU B CB 1 ATOM 6111 C CG . LEU B 2 252 ? 61.910 -33.209 52.749 1.00 71.86 ? 252 LEU B CG 1 ATOM 6112 C CD1 . LEU B 2 252 ? 62.521 -34.587 52.917 1.00 71.67 ? 252 LEU B CD1 1 ATOM 6113 C CD2 . LEU B 2 252 ? 61.316 -32.735 54.067 1.00 67.80 ? 252 LEU B CD2 1 ATOM 6114 N N . ASN B 2 253 ? 61.461 -31.897 49.485 1.00 82.89 ? 253 ASN B N 1 ATOM 6115 C CA . ASN B 2 253 ? 60.385 -32.370 48.646 1.00 77.06 ? 253 ASN B CA 1 ATOM 6116 C C . ASN B 2 253 ? 60.109 -33.838 48.969 1.00 73.91 ? 253 ASN B C 1 ATOM 6117 O O . ASN B 2 253 ? 60.999 -34.568 49.398 1.00 71.51 ? 253 ASN B O 1 ATOM 6118 C CB . ASN B 2 253 ? 60.750 -32.180 47.171 1.00 70.75 ? 253 ASN B CB 1 ATOM 6119 C CG . ASN B 2 253 ? 60.994 -30.713 46.801 1.00 83.54 ? 253 ASN B CG 1 ATOM 6120 O OD1 . ASN B 2 253 ? 60.458 -29.803 47.438 1.00 78.94 ? 253 ASN B OD1 1 ATOM 6121 N ND2 . ASN B 2 253 ? 61.802 -30.488 45.753 1.00 106.23 ? 253 ASN B ND2 1 ATOM 6122 N N . VAL B 2 254 ? 58.863 -34.259 48.794 1.00 70.75 ? 254 VAL B N 1 ATOM 6123 C CA . VAL B 2 254 ? 58.501 -35.662 48.953 1.00 62.64 ? 254 VAL B CA 1 ATOM 6124 C C . VAL B 2 254 ? 57.767 -36.181 47.706 1.00 70.70 ? 254 VAL B C 1 ATOM 6125 O O . VAL B 2 254 ? 56.888 -35.513 47.147 1.00 66.64 ? 254 VAL B O 1 ATOM 6126 C CB . VAL B 2 254 ? 57.681 -35.907 50.244 1.00 54.15 ? 254 VAL B CB 1 ATOM 6127 C CG1 . VAL B 2 254 ? 57.066 -37.292 50.249 1.00 50.59 ? 254 VAL B CG1 1 ATOM 6128 C CG2 . VAL B 2 254 ? 58.564 -35.753 51.448 1.00 56.68 ? 254 VAL B CG2 1 ATOM 6129 N N . THR B 2 255 ? 58.158 -37.368 47.259 1.00 64.61 ? 255 THR B N 1 ATOM 6130 C CA . THR B 2 255 ? 57.512 -37.991 46.123 1.00 52.87 ? 255 THR B CA 1 ATOM 6131 C C . THR B 2 255 ? 57.080 -39.422 46.420 1.00 59.17 ? 255 THR B C 1 ATOM 6132 O O . THR B 2 255 ? 57.898 -40.277 46.771 1.00 60.30 ? 255 THR B O 1 ATOM 6133 C CB . THR B 2 255 ? 58.422 -37.979 44.921 1.00 60.27 ? 255 THR B CB 1 ATOM 6134 O OG1 . THR B 2 255 ? 58.653 -36.622 44.536 1.00 81.86 ? 255 THR B OG1 1 ATOM 6135 C CG2 . THR B 2 255 ? 57.786 -38.728 43.768 1.00 57.97 ? 255 THR B CG2 1 ATOM 6136 N N . LEU B 2 256 ? 55.778 -39.660 46.286 1.00 52.39 ? 256 LEU B N 1 ATOM 6137 C CA . LEU B 2 256 ? 55.194 -40.987 46.424 1.00 46.43 ? 256 LEU B CA 1 ATOM 6138 C C . LEU B 2 256 ? 54.903 -41.580 45.031 1.00 49.99 ? 256 LEU B C 1 ATOM 6139 O O . LEU B 2 256 ? 54.210 -40.962 44.240 1.00 54.61 ? 256 LEU B O 1 ATOM 6140 C CB . LEU B 2 256 ? 53.911 -40.880 47.258 1.00 44.34 ? 256 LEU B CB 1 ATOM 6141 C CG . LEU B 2 256 ? 54.018 -41.049 48.786 1.00 53.67 ? 256 LEU B CG 1 ATOM 6142 C CD1 . LEU B 2 256 ? 55.361 -40.583 49.334 1.00 42.55 ? 256 LEU B CD1 1 ATOM 6143 C CD2 . LEU B 2 256 ? 52.844 -40.389 49.541 1.00 56.62 ? 256 LEU B CD2 1 ATOM 6144 N N . GLN B 2 257 ? 55.445 -42.758 44.724 1.00 53.61 ? 257 GLN B N 1 ATOM 6145 C CA . GLN B 2 257 ? 55.235 -43.404 43.415 1.00 51.10 ? 257 GLN B CA 1 ATOM 6146 C C . GLN B 2 257 ? 54.571 -44.758 43.550 1.00 55.97 ? 257 GLN B C 1 ATOM 6147 O O . GLN B 2 257 ? 54.965 -45.572 44.381 1.00 63.07 ? 257 GLN B O 1 ATOM 6148 C CB . GLN B 2 257 ? 56.552 -43.605 42.680 1.00 54.69 ? 257 GLN B CB 1 ATOM 6149 C CG . GLN B 2 257 ? 56.752 -42.728 41.484 1.00 69.42 ? 257 GLN B CG 1 ATOM 6150 C CD . GLN B 2 257 ? 58.089 -42.988 40.817 1.00 84.46 ? 257 GLN B CD 1 ATOM 6151 O OE1 . GLN B 2 257 ? 58.976 -42.135 40.839 1.00 94.08 ? 257 GLN B OE1 1 ATOM 6152 N NE2 . GLN B 2 257 ? 58.247 -44.178 40.229 1.00 78.70 ? 257 GLN B NE2 1 ATOM 6153 N N . HIS B 2 258 ? 53.561 -45.005 42.730 1.00 58.02 ? 258 HIS B N 1 ATOM 6154 C CA . HIS B 2 258 ? 52.850 -46.278 42.780 1.00 60.24 ? 258 HIS B CA 1 ATOM 6155 C C . HIS B 2 258 ? 52.149 -46.607 44.111 1.00 64.09 ? 258 HIS B C 1 ATOM 6156 O O . HIS B 2 258 ? 52.178 -47.749 44.562 1.00 72.48 ? 258 HIS B O 1 ATOM 6157 C CB . HIS B 2 258 ? 53.815 -47.384 42.388 1.00 53.00 ? 258 HIS B CB 1 ATOM 6158 C CG . HIS B 2 258 ? 54.684 -47.013 41.230 1.00 65.70 ? 258 HIS B CG 1 ATOM 6159 N ND1 . HIS B 2 258 ? 56.054 -46.901 41.330 1.00 70.68 ? 258 HIS B ND1 1 ATOM 6160 C CD2 . HIS B 2 258 ? 54.372 -46.687 39.954 1.00 60.85 ? 258 HIS B CD2 1 ATOM 6161 C CE1 . HIS B 2 258 ? 56.551 -46.540 40.161 1.00 53.45 ? 258 HIS B CE1 1 ATOM 6162 N NE2 . HIS B 2 258 ? 55.552 -46.404 39.310 1.00 55.22 ? 258 HIS B NE2 1 ATOM 6163 N N . ILE B 2 259 ? 51.499 -45.613 44.715 1.00 60.05 ? 259 ILE B N 1 ATOM 6164 C CA . ILE B 2 259 ? 50.758 -45.803 45.963 1.00 63.21 ? 259 ILE B CA 1 ATOM 6165 C C . ILE B 2 259 ? 49.354 -46.302 45.690 1.00 67.08 ? 259 ILE B C 1 ATOM 6166 O O . ILE B 2 259 ? 48.555 -45.605 45.079 1.00 80.61 ? 259 ILE B O 1 ATOM 6167 C CB . ILE B 2 259 ? 50.577 -44.480 46.725 1.00 58.70 ? 259 ILE B CB 1 ATOM 6168 C CG1 . ILE B 2 259 ? 51.721 -43.527 46.422 1.00 79.18 ? 259 ILE B CG1 1 ATOM 6169 C CG2 . ILE B 2 259 ? 50.436 -44.710 48.208 1.00 33.58 ? 259 ILE B CG2 1 ATOM 6170 C CD1 . ILE B 2 259 ? 51.530 -42.782 45.134 1.00 85.89 ? 259 ILE B CD1 1 ATOM 6171 N N . GLU B 2 260 ? 49.048 -47.506 46.145 1.00 55.12 ? 260 GLU B N 1 ATOM 6172 C CA . GLU B 2 260 ? 47.675 -47.968 46.154 1.00 53.82 ? 260 GLU B CA 1 ATOM 6173 C C . GLU B 2 260 ? 47.216 -47.883 47.579 1.00 63.59 ? 260 GLU B C 1 ATOM 6174 O O . GLU B 2 260 ? 47.820 -48.489 48.458 1.00 73.40 ? 260 GLU B O 1 ATOM 6175 C CB . GLU B 2 260 ? 47.580 -49.416 45.710 1.00 63.53 ? 260 GLU B CB 1 ATOM 6176 C CG . GLU B 2 260 ? 46.356 -50.102 46.273 1.00 70.18 ? 260 GLU B CG 1 ATOM 6177 C CD . GLU B 2 260 ? 46.469 -51.607 46.248 1.00 82.86 ? 260 GLU B CD 1 ATOM 6178 O OE1 . GLU B 2 260 ? 45.995 -52.252 47.218 1.00 97.01 ? 260 GLU B OE1 1 ATOM 6179 O OE2 . GLU B 2 260 ? 47.038 -52.134 45.265 1.00 75.42 ? 260 GLU B OE2 1 ATOM 6180 N N . THR B 2 261 ? 46.151 -47.136 47.824 1.00 65.99 ? 261 THR B N 1 ATOM 6181 C CA . THR B 2 261 ? 45.785 -46.830 49.199 1.00 66.92 ? 261 THR B CA 1 ATOM 6182 C C . THR B 2 261 ? 44.291 -46.616 49.355 1.00 59.78 ? 261 THR B C 1 ATOM 6183 O O . THR B 2 261 ? 43.608 -46.272 48.404 1.00 78.08 ? 261 THR B O 1 ATOM 6184 C CB . THR B 2 261 ? 46.553 -45.577 49.711 1.00 51.80 ? 261 THR B CB 1 ATOM 6185 O OG1 . THR B 2 261 ? 45.734 -44.853 50.621 1.00 52.30 ? 261 THR B OG1 1 ATOM 6186 C CG2 . THR B 2 261 ? 46.876 -44.640 48.573 1.00 57.40 ? 261 THR B CG2 1 ATOM 6187 N N . THR B 2 262 ? 43.785 -46.844 50.556 1.00 51.49 ? 262 THR B N 1 ATOM 6188 C CA . THR B 2 262 ? 42.442 -46.412 50.918 1.00 60.07 ? 262 THR B CA 1 ATOM 6189 C C . THR B 2 262 ? 42.271 -44.908 50.726 1.00 62.91 ? 262 THR B C 1 ATOM 6190 O O . THR B 2 262 ? 43.248 -44.169 50.654 1.00 64.10 ? 262 THR B O 1 ATOM 6191 C CB . THR B 2 262 ? 42.159 -46.726 52.396 1.00 62.90 ? 262 THR B CB 1 ATOM 6192 O OG1 . THR B 2 262 ? 41.959 -48.130 52.536 1.00 72.87 ? 262 THR B OG1 1 ATOM 6193 C CG2 . THR B 2 262 ? 40.909 -46.023 52.872 1.00 72.11 ? 262 THR B CG2 1 ATOM 6194 N N . TRP B 2 263 ? 41.030 -44.446 50.645 1.00 72.23 ? 263 TRP B N 1 ATOM 6195 C CA . TRP B 2 263 ? 40.795 -43.015 50.705 1.00 75.20 ? 263 TRP B CA 1 ATOM 6196 C C . TRP B 2 263 ? 41.053 -42.513 52.128 1.00 71.79 ? 263 TRP B C 1 ATOM 6197 O O . TRP B 2 263 ? 41.753 -41.513 52.311 1.00 59.13 ? 263 TRP B O 1 ATOM 6198 C CB . TRP B 2 263 ? 39.395 -42.619 50.205 1.00 71.29 ? 263 TRP B CB 1 ATOM 6199 C CG . TRP B 2 263 ? 39.218 -41.123 50.182 1.00 65.32 ? 263 TRP B CG 1 ATOM 6200 C CD1 . TRP B 2 263 ? 38.281 -40.386 50.861 1.00 61.46 ? 263 TRP B CD1 1 ATOM 6201 C CD2 . TRP B 2 263 ? 40.044 -40.179 49.488 1.00 56.55 ? 263 TRP B CD2 1 ATOM 6202 N NE1 . TRP B 2 263 ? 38.468 -39.048 50.619 1.00 57.70 ? 263 TRP B NE1 1 ATOM 6203 C CE2 . TRP B 2 263 ? 39.538 -38.893 49.773 1.00 55.35 ? 263 TRP B CE2 1 ATOM 6204 C CE3 . TRP B 2 263 ? 41.166 -40.296 48.652 1.00 44.96 ? 263 TRP B CE3 1 ATOM 6205 C CZ2 . TRP B 2 263 ? 40.105 -37.732 49.242 1.00 49.94 ? 263 TRP B CZ2 1 ATOM 6206 C CZ3 . TRP B 2 263 ? 41.731 -39.139 48.128 1.00 41.40 ? 263 TRP B CZ3 1 ATOM 6207 C CH2 . TRP B 2 263 ? 41.196 -37.875 48.422 1.00 41.56 ? 263 TRP B CH2 1 ATOM 6208 N N . LYS B 2 264 ? 40.498 -43.207 53.125 1.00 77.06 ? 264 LYS B N 1 ATOM 6209 C CA . LYS B 2 264 ? 40.751 -42.886 54.540 1.00 74.37 ? 264 LYS B CA 1 ATOM 6210 C C . LYS B 2 264 ? 42.240 -42.644 54.782 1.00 74.89 ? 264 LYS B C 1 ATOM 6211 O O . LYS B 2 264 ? 42.632 -41.671 55.438 1.00 72.20 ? 264 LYS B O 1 ATOM 6212 C CB . LYS B 2 264 ? 40.252 -44.021 55.450 1.00 62.75 ? 264 LYS B CB 1 ATOM 6213 C CG . LYS B 2 264 ? 40.251 -43.731 56.949 1.00 65.54 ? 264 LYS B CG 1 ATOM 6214 C CD . LYS B 2 264 ? 39.519 -44.843 57.717 1.00 72.48 ? 264 LYS B CD 1 ATOM 6215 C CE . LYS B 2 264 ? 38.754 -44.328 58.958 1.00 82.97 ? 264 LYS B CE 1 ATOM 6216 N NZ . LYS B 2 264 ? 39.463 -44.522 60.277 1.00 91.51 ? 264 LYS B NZ 1 ATOM 6217 N N . CYS B 2 265 ? 43.063 -43.533 54.231 1.00 69.50 ? 265 CYS B N 1 ATOM 6218 C CA . CYS B 2 265 ? 44.497 -43.479 54.442 1.00 64.58 ? 265 CYS B CA 1 ATOM 6219 C C . CYS B 2 265 ? 45.142 -42.343 53.657 1.00 59.21 ? 265 CYS B C 1 ATOM 6220 O O . CYS B 2 265 ? 46.194 -41.835 54.036 1.00 58.48 ? 265 CYS B O 1 ATOM 6221 C CB . CYS B 2 265 ? 45.150 -44.828 54.100 1.00 57.36 ? 265 CYS B CB 1 ATOM 6222 S SG . CYS B 2 265 ? 46.916 -44.934 54.551 1.00 106.50 ? 265 CYS B SG 1 ATOM 6223 N N . SER B 2 266 ? 44.522 -41.948 52.555 1.00 58.58 ? 266 SER B N 1 ATOM 6224 C CA . SER B 2 266 ? 45.078 -40.868 51.753 1.00 57.34 ? 266 SER B CA 1 ATOM 6225 C C . SER B 2 266 ? 44.880 -39.539 52.462 1.00 64.70 ? 266 SER B C 1 ATOM 6226 O O . SER B 2 266 ? 45.791 -38.712 52.525 1.00 65.22 ? 266 SER B O 1 ATOM 6227 C CB . SER B 2 266 ? 44.469 -40.857 50.352 1.00 55.15 ? 266 SER B CB 1 ATOM 6228 O OG . SER B 2 266 ? 44.963 -41.956 49.591 1.00 59.27 ? 266 SER B OG 1 ATOM 6229 N N . VAL B 2 267 ? 43.688 -39.355 53.019 1.00 64.67 ? 267 VAL B N 1 ATOM 6230 C CA . VAL B 2 267 ? 43.372 -38.179 53.817 1.00 61.17 ? 267 VAL B CA 1 ATOM 6231 C C . VAL B 2 267 ? 44.247 -38.109 55.086 1.00 67.10 ? 267 VAL B C 1 ATOM 6232 O O . VAL B 2 267 ? 44.582 -37.026 55.576 1.00 61.75 ? 267 VAL B O 1 ATOM 6233 C CB . VAL B 2 267 ? 41.872 -38.157 54.159 1.00 49.98 ? 267 VAL B CB 1 ATOM 6234 C CG1 . VAL B 2 267 ? 41.493 -36.844 54.819 1.00 55.82 ? 267 VAL B CG1 1 ATOM 6235 C CG2 . VAL B 2 267 ? 41.068 -38.352 52.896 1.00 41.02 ? 267 VAL B CG2 1 ATOM 6236 N N . LYS B 2 268 ? 44.629 -39.270 55.604 1.00 64.33 ? 268 LYS B N 1 ATOM 6237 C CA . LYS B 2 268 ? 45.619 -39.326 56.671 1.00 58.41 ? 268 LYS B CA 1 ATOM 6238 C C . LYS B 2 268 ? 47.014 -38.921 56.170 1.00 63.26 ? 268 LYS B C 1 ATOM 6239 O O . LYS B 2 268 ? 47.670 -38.064 56.750 1.00 69.75 ? 268 LYS B O 1 ATOM 6240 C CB . LYS B 2 268 ? 45.655 -40.723 57.290 1.00 52.91 ? 268 LYS B CB 1 ATOM 6241 C CG . LYS B 2 268 ? 44.413 -41.053 58.072 1.00 60.83 ? 268 LYS B CG 1 ATOM 6242 C CD . LYS B 2 268 ? 44.499 -42.413 58.740 1.00 71.77 ? 268 LYS B CD 1 ATOM 6243 C CE . LYS B 2 268 ? 43.351 -42.601 59.725 1.00 72.73 ? 268 LYS B CE 1 ATOM 6244 N NZ . LYS B 2 268 ? 43.259 -43.995 60.238 1.00 80.78 ? 268 LYS B NZ 1 ATOM 6245 N N . LEU B 2 269 ? 47.461 -39.541 55.088 1.00 60.69 ? 269 LEU B N 1 ATOM 6246 C CA . LEU B 2 269 ? 48.736 -39.191 54.484 1.00 59.47 ? 269 LEU B CA 1 ATOM 6247 C C . LEU B 2 269 ? 48.900 -37.680 54.302 1.00 68.09 ? 269 LEU B C 1 ATOM 6248 O O . LEU B 2 269 ? 49.919 -37.121 54.694 1.00 61.70 ? 269 LEU B O 1 ATOM 6249 C CB . LEU B 2 269 ? 48.912 -39.926 53.153 1.00 54.09 ? 269 LEU B CB 1 ATOM 6250 C CG . LEU B 2 269 ? 49.408 -41.371 53.220 1.00 47.70 ? 269 LEU B CG 1 ATOM 6251 C CD1 . LEU B 2 269 ? 50.313 -41.587 52.056 1.00 53.29 ? 269 LEU B CD1 1 ATOM 6252 C CD2 . LEU B 2 269 ? 50.196 -41.593 54.484 1.00 58.93 ? 269 LEU B CD2 1 ATOM 6253 N N . PHE B 2 270 ? 47.906 -37.019 53.709 1.00 79.09 ? 270 PHE B N 1 ATOM 6254 C CA . PHE B 2 270 ? 47.946 -35.561 53.566 1.00 74.38 ? 270 PHE B CA 1 ATOM 6255 C C . PHE B 2 270 ? 48.111 -34.880 54.922 1.00 67.43 ? 270 PHE B C 1 ATOM 6256 O O . PHE B 2 270 ? 48.993 -34.045 55.091 1.00 73.08 ? 270 PHE B O 1 ATOM 6257 C CB . PHE B 2 270 ? 46.692 -35.009 52.865 1.00 69.86 ? 270 PHE B CB 1 ATOM 6258 C CG . PHE B 2 270 ? 46.541 -35.461 51.439 1.00 60.57 ? 270 PHE B CG 1 ATOM 6259 C CD1 . PHE B 2 270 ? 45.345 -36.015 50.992 1.00 62.56 ? 270 PHE B CD1 1 ATOM 6260 C CD2 . PHE B 2 270 ? 47.588 -35.345 50.549 1.00 54.88 ? 270 PHE B CD2 1 ATOM 6261 C CE1 . PHE B 2 270 ? 45.200 -36.453 49.680 1.00 59.80 ? 270 PHE B CE1 1 ATOM 6262 C CE2 . PHE B 2 270 ? 47.448 -35.783 49.226 1.00 61.65 ? 270 PHE B CE2 1 ATOM 6263 C CZ . PHE B 2 270 ? 46.253 -36.338 48.798 1.00 55.25 ? 270 PHE B CZ 1 ATOM 6264 N N . GLN B 2 271 ? 47.260 -35.242 55.880 1.00 62.07 ? 271 GLN B N 1 ATOM 6265 C CA . GLN B 2 271 ? 47.269 -34.623 57.213 1.00 65.95 ? 271 GLN B CA 1 ATOM 6266 C C . GLN B 2 271 ? 48.606 -34.809 57.924 1.00 74.67 ? 271 GLN B C 1 ATOM 6267 O O . GLN B 2 271 ? 49.051 -33.934 58.663 1.00 72.49 ? 271 GLN B O 1 ATOM 6268 C CB . GLN B 2 271 ? 46.156 -35.197 58.092 1.00 64.38 ? 271 GLN B CB 1 ATOM 6269 C CG . GLN B 2 271 ? 44.759 -34.871 57.639 1.00 66.71 ? 271 GLN B CG 1 ATOM 6270 C CD . GLN B 2 271 ? 44.341 -33.478 58.030 1.00 69.23 ? 271 GLN B CD 1 ATOM 6271 O OE1 . GLN B 2 271 ? 43.985 -33.229 59.179 1.00 64.06 ? 271 GLN B OE1 1 ATOM 6272 N NE2 . GLN B 2 271 ? 44.367 -32.558 57.069 1.00 76.46 ? 271 GLN B NE2 1 ATOM 6273 N N . PHE B 2 272 ? 49.227 -35.965 57.709 1.00 78.61 ? 272 PHE B N 1 ATOM 6274 C CA . PHE B 2 272 ? 50.527 -36.279 58.286 1.00 78.24 ? 272 PHE B CA 1 ATOM 6275 C C . PHE B 2 272 ? 51.585 -35.307 57.788 1.00 72.34 ? 272 PHE B C 1 ATOM 6276 O O . PHE B 2 272 ? 52.502 -34.930 58.517 1.00 84.60 ? 272 PHE B O 1 ATOM 6277 C CB . PHE B 2 272 ? 50.926 -37.713 57.924 1.00 80.91 ? 272 PHE B CB 1 ATOM 6278 C CG . PHE B 2 272 ? 52.380 -38.014 58.142 1.00 75.51 ? 272 PHE B CG 1 ATOM 6279 C CD1 . PHE B 2 272 ? 52.833 -38.464 59.379 1.00 75.23 ? 272 PHE B CD1 1 ATOM 6280 C CD2 . PHE B 2 272 ? 53.296 -37.846 57.115 1.00 70.34 ? 272 PHE B CD2 1 ATOM 6281 C CE1 . PHE B 2 272 ? 54.170 -38.739 59.589 1.00 71.97 ? 272 PHE B CE1 1 ATOM 6282 C CE2 . PHE B 2 272 ? 54.639 -38.118 57.318 1.00 76.20 ? 272 PHE B CE2 1 ATOM 6283 C CZ . PHE B 2 272 ? 55.077 -38.566 58.557 1.00 75.07 ? 272 PHE B CZ 1 ATOM 6284 N N . PHE B 2 273 ? 51.442 -34.898 56.538 1.00 62.68 ? 273 PHE B N 1 ATOM 6285 C CA . PHE B 2 273 ? 52.430 -34.062 55.896 1.00 61.14 ? 273 PHE B CA 1 ATOM 6286 C C . PHE B 2 273 ? 52.263 -32.595 56.248 1.00 68.13 ? 273 PHE B C 1 ATOM 6287 O O . PHE B 2 273 ? 53.234 -31.848 56.299 1.00 73.69 ? 273 PHE B O 1 ATOM 6288 C CB . PHE B 2 273 ? 52.350 -34.231 54.382 1.00 45.20 ? 273 PHE B CB 1 ATOM 6289 C CG . PHE B 2 273 ? 53.065 -35.442 53.870 1.00 59.28 ? 273 PHE B CG 1 ATOM 6290 C CD1 . PHE B 2 273 ? 52.375 -36.442 53.207 1.00 68.33 ? 273 PHE B CD1 1 ATOM 6291 C CD2 . PHE B 2 273 ? 54.427 -35.577 54.039 1.00 65.25 ? 273 PHE B CD2 1 ATOM 6292 C CE1 . PHE B 2 273 ? 53.031 -37.556 52.725 1.00 64.88 ? 273 PHE B CE1 1 ATOM 6293 C CE2 . PHE B 2 273 ? 55.083 -36.691 53.566 1.00 72.67 ? 273 PHE B CE2 1 ATOM 6294 C CZ . PHE B 2 273 ? 54.383 -37.681 52.910 1.00 67.86 ? 273 PHE B CZ 1 ATOM 6295 N N . TRP B 2 274 ? 51.029 -32.186 56.492 1.00 66.01 ? 274 TRP B N 1 ATOM 6296 C CA . TRP B 2 274 ? 50.707 -30.765 56.557 1.00 71.12 ? 274 TRP B CA 1 ATOM 6297 C C . TRP B 2 274 ? 51.538 -29.989 57.601 1.00 70.17 ? 274 TRP B C 1 ATOM 6298 O O . TRP B 2 274 ? 52.031 -28.887 57.331 1.00 66.43 ? 274 TRP B O 1 ATOM 6299 C CB . TRP B 2 274 ? 49.199 -30.588 56.773 1.00 71.47 ? 274 TRP B CB 1 ATOM 6300 C CG . TRP B 2 274 ? 48.557 -29.660 55.784 1.00 68.74 ? 274 TRP B CG 1 ATOM 6301 C CD1 . TRP B 2 274 ? 48.133 -28.387 56.011 1.00 72.63 ? 274 TRP B CD1 1 ATOM 6302 C CD2 . TRP B 2 274 ? 48.268 -29.938 54.414 1.00 66.42 ? 274 TRP B CD2 1 ATOM 6303 N NE1 . TRP B 2 274 ? 47.601 -27.854 54.868 1.00 72.11 ? 274 TRP B NE1 1 ATOM 6304 C CE2 . TRP B 2 274 ? 47.673 -28.786 53.871 1.00 66.97 ? 274 TRP B CE2 1 ATOM 6305 C CE3 . TRP B 2 274 ? 48.459 -31.049 53.591 1.00 70.44 ? 274 TRP B CE3 1 ATOM 6306 C CZ2 . TRP B 2 274 ? 47.266 -28.712 52.546 1.00 73.45 ? 274 TRP B CZ2 1 ATOM 6307 C CZ3 . TRP B 2 274 ? 48.052 -30.976 52.278 1.00 69.18 ? 274 TRP B CZ3 1 ATOM 6308 C CH2 . TRP B 2 274 ? 47.465 -29.815 51.766 1.00 74.38 ? 274 TRP B CH2 1 ATOM 6309 N N . PRO B 2 275 ? 51.710 -30.567 58.794 1.00 67.62 ? 275 PRO B N 1 ATOM 6310 C CA . PRO B 2 275 ? 52.488 -29.887 59.828 1.00 72.15 ? 275 PRO B CA 1 ATOM 6311 C C . PRO B 2 275 ? 53.990 -29.922 59.540 1.00 80.49 ? 275 PRO B C 1 ATOM 6312 O O . PRO B 2 275 ? 54.752 -29.089 60.034 1.00 93.13 ? 275 PRO B O 1 ATOM 6313 C CB . PRO B 2 275 ? 52.184 -30.715 61.082 1.00 72.02 ? 275 PRO B CB 1 ATOM 6314 C CG . PRO B 2 275 ? 51.011 -31.575 60.737 1.00 65.35 ? 275 PRO B CG 1 ATOM 6315 C CD . PRO B 2 275 ? 51.145 -31.831 59.290 1.00 65.42 ? 275 PRO B CD 1 ATOM 6316 N N . ARG B 2 276 ? 54.406 -30.885 58.733 1.00 75.99 ? 276 ARG B N 1 ATOM 6317 C CA . ARG B 2 276 ? 55.816 -31.159 58.527 1.00 72.26 ? 276 ARG B CA 1 ATOM 6318 C C . ARG B 2 276 ? 56.459 -30.233 57.490 1.00 83.32 ? 276 ARG B C 1 ATOM 6319 O O . ARG B 2 276 ? 55.758 -29.514 56.769 1.00 84.02 ? 276 ARG B O 1 ATOM 6320 C CB . ARG B 2 276 ? 55.985 -32.644 58.192 1.00 63.80 ? 276 ARG B CB 1 ATOM 6321 C CG . ARG B 2 276 ? 55.219 -33.507 59.186 1.00 68.63 ? 276 ARG B CG 1 ATOM 6322 C CD . ARG B 2 276 ? 55.590 -34.969 59.139 1.00 74.23 ? 276 ARG B CD 1 ATOM 6323 N NE . ARG B 2 276 ? 55.514 -35.588 60.462 1.00 72.91 ? 276 ARG B NE 1 ATOM 6324 C CZ . ARG B 2 276 ? 56.579 -35.986 61.154 1.00 77.98 ? 276 ARG B CZ 1 ATOM 6325 N NH1 . ARG B 2 276 ? 57.792 -35.842 60.644 1.00 81.15 ? 276 ARG B NH1 1 ATOM 6326 N NH2 . ARG B 2 276 ? 56.438 -36.536 62.352 1.00 83.17 ? 276 ARG B NH2 1 ATOM 6327 N N . PRO B 2 277 ? 57.803 -30.221 57.448 1.00 84.51 ? 277 PRO B N 1 ATOM 6328 C CA . PRO B 2 277 ? 58.627 -29.384 56.563 1.00 77.35 ? 277 PRO B CA 1 ATOM 6329 C C . PRO B 2 277 ? 58.687 -29.879 55.131 1.00 81.43 ? 277 PRO B C 1 ATOM 6330 O O . PRO B 2 277 ? 59.779 -30.099 54.620 1.00 93.95 ? 277 PRO B O 1 ATOM 6331 C CB . PRO B 2 277 ? 60.027 -29.501 57.172 1.00 70.69 ? 277 PRO B CB 1 ATOM 6332 C CG . PRO B 2 277 ? 59.812 -30.024 58.556 1.00 75.60 ? 277 PRO B CG 1 ATOM 6333 C CD . PRO B 2 277 ? 58.626 -30.907 58.454 1.00 78.35 ? 277 PRO B CD 1 ATOM 6334 N N . VAL B 2 278 ? 57.542 -30.046 54.486 1.00 77.81 ? 278 VAL B N 1 ATOM 6335 C CA . VAL B 2 278 ? 57.538 -30.466 53.094 1.00 73.88 ? 278 VAL B CA 1 ATOM 6336 C C . VAL B 2 278 ? 56.995 -29.346 52.209 1.00 75.97 ? 278 VAL B C 1 ATOM 6337 O O . VAL B 2 278 ? 55.838 -28.937 52.348 1.00 64.91 ? 278 VAL B O 1 ATOM 6338 C CB . VAL B 2 278 ? 56.735 -31.765 52.902 1.00 64.90 ? 278 VAL B CB 1 ATOM 6339 C CG1 . VAL B 2 278 ? 56.706 -32.155 51.440 1.00 69.52 ? 278 VAL B CG1 1 ATOM 6340 C CG2 . VAL B 2 278 ? 57.336 -32.884 53.742 1.00 54.01 ? 278 VAL B CG2 1 ATOM 6341 N N . GLU B 2 279 ? 57.852 -28.845 51.317 1.00 84.39 ? 279 GLU B N 1 ATOM 6342 C CA . GLU B 2 279 ? 57.521 -27.720 50.439 1.00 83.68 ? 279 GLU B CA 1 ATOM 6343 C C . GLU B 2 279 ? 56.785 -28.176 49.181 1.00 79.20 ? 279 GLU B C 1 ATOM 6344 O O . GLU B 2 279 ? 55.747 -27.625 48.820 1.00 83.25 ? 279 GLU B O 1 ATOM 6345 C CB . GLU B 2 279 ? 58.787 -26.939 50.055 1.00 83.43 ? 279 GLU B CB 1 ATOM 6346 C CG . GLU B 2 279 ? 58.513 -25.534 49.522 1.00 82.36 ? 279 GLU B CG 1 ATOM 6347 C CD . GLU B 2 279 ? 59.759 -24.837 48.988 1.00 86.87 ? 279 GLU B CD 1 ATOM 6348 O OE1 . GLU B 2 279 ? 60.728 -25.530 48.589 1.00 78.90 ? 279 GLU B OE1 1 ATOM 6349 O OE2 . GLU B 2 279 ? 59.756 -23.584 48.958 1.00 90.67 ? 279 GLU B OE2 1 ATOM 6350 N N . TYR B 2 280 ? 57.333 -29.179 48.508 1.00 74.47 ? 280 TYR B N 1 ATOM 6351 C CA . TYR B 2 280 ? 56.655 -29.765 47.364 1.00 66.14 ? 280 TYR B CA 1 ATOM 6352 C C . TYR B 2 280 ? 56.319 -31.236 47.604 1.00 61.75 ? 280 TYR B C 1 ATOM 6353 O O . TYR B 2 280 ? 57.191 -32.040 47.910 1.00 65.84 ? 280 TYR B O 1 ATOM 6354 C CB . TYR B 2 280 ? 57.494 -29.605 46.103 1.00 60.57 ? 280 TYR B CB 1 ATOM 6355 C CG . TYR B 2 280 ? 57.624 -28.179 45.635 1.00 74.79 ? 280 TYR B CG 1 ATOM 6356 C CD1 . TYR B 2 280 ? 58.440 -27.289 46.310 1.00 83.37 ? 280 TYR B CD1 1 ATOM 6357 C CD2 . TYR B 2 280 ? 56.941 -27.722 44.509 1.00 76.06 ? 280 TYR B CD2 1 ATOM 6358 C CE1 . TYR B 2 280 ? 58.577 -25.977 45.889 1.00 86.20 ? 280 TYR B CE1 1 ATOM 6359 C CE2 . TYR B 2 280 ? 57.071 -26.404 44.078 1.00 78.95 ? 280 TYR B CE2 1 ATOM 6360 C CZ . TYR B 2 280 ? 57.898 -25.537 44.779 1.00 88.69 ? 280 TYR B CZ 1 ATOM 6361 O OH . TYR B 2 280 ? 58.061 -24.222 44.392 1.00 92.97 ? 280 TYR B OH 1 ATOM 6362 N N . LEU B 2 281 ? 55.041 -31.573 47.469 1.00 57.62 ? 281 LEU B N 1 ATOM 6363 C CA . LEU B 2 281 ? 54.574 -32.948 47.583 1.00 60.27 ? 281 LEU B CA 1 ATOM 6364 C C . LEU B 2 281 ? 54.102 -33.458 46.229 1.00 61.75 ? 281 LEU B C 1 ATOM 6365 O O . LEU B 2 281 ? 53.265 -32.826 45.588 1.00 74.24 ? 281 LEU B O 1 ATOM 6366 C CB . LEU B 2 281 ? 53.426 -33.019 48.578 1.00 61.99 ? 281 LEU B CB 1 ATOM 6367 C CG . LEU B 2 281 ? 52.886 -34.415 48.822 1.00 58.49 ? 281 LEU B CG 1 ATOM 6368 C CD1 . LEU B 2 281 ? 54.044 -35.341 49.104 1.00 61.58 ? 281 LEU B CD1 1 ATOM 6369 C CD2 . LEU B 2 281 ? 51.945 -34.372 49.988 1.00 60.83 ? 281 LEU B CD2 1 ATOM 6370 N N . ASN B 2 282 ? 54.644 -34.591 45.788 1.00 60.21 ? 282 ASN B N 1 ATOM 6371 C CA . ASN B 2 282 ? 54.288 -35.162 44.484 1.00 57.67 ? 282 ASN B CA 1 ATOM 6372 C C . ASN B 2 282 ? 53.837 -36.607 44.589 1.00 62.50 ? 282 ASN B C 1 ATOM 6373 O O . ASN B 2 282 ? 54.460 -37.413 45.277 1.00 68.33 ? 282 ASN B O 1 ATOM 6374 C CB . ASN B 2 282 ? 55.468 -35.088 43.519 1.00 44.69 ? 282 ASN B CB 1 ATOM 6375 C CG . ASN B 2 282 ? 56.114 -33.726 43.496 1.00 56.89 ? 282 ASN B CG 1 ATOM 6376 O OD1 . ASN B 2 282 ? 55.581 -32.788 42.910 1.00 73.79 ? 282 ASN B OD1 1 ATOM 6377 N ND2 . ASN B 2 282 ? 57.274 -33.606 44.136 1.00 58.82 ? 282 ASN B ND2 1 ATOM 6378 N N . ILE B 2 283 ? 52.756 -36.933 43.898 1.00 59.88 ? 283 ILE B N 1 ATOM 6379 C CA . ILE B 2 283 ? 52.242 -38.297 43.891 1.00 57.82 ? 283 ILE B CA 1 ATOM 6380 C C . ILE B 2 283 ? 52.051 -38.779 42.450 1.00 56.29 ? 283 ILE B C 1 ATOM 6381 O O . ILE B 2 283 ? 51.454 -38.087 41.634 1.00 54.44 ? 283 ILE B O 1 ATOM 6382 C CB . ILE B 2 283 ? 50.926 -38.397 44.699 1.00 44.73 ? 283 ILE B CB 1 ATOM 6383 C CG1 . ILE B 2 283 ? 51.178 -38.025 46.155 1.00 39.96 ? 283 ILE B CG1 1 ATOM 6384 C CG2 . ILE B 2 283 ? 50.325 -39.783 44.592 1.00 39.29 ? 283 ILE B CG2 1 ATOM 6385 C CD1 . ILE B 2 283 ? 49.924 -37.690 46.927 1.00 48.39 ? 283 ILE B CD1 1 ATOM 6386 N N . TYR B 2 284 ? 52.579 -39.959 42.146 1.00 61.71 ? 284 TYR B N 1 ATOM 6387 C CA . TYR B 2 284 ? 52.556 -40.519 40.794 1.00 57.21 ? 284 TYR B CA 1 ATOM 6388 C C . TYR B 2 284 ? 51.900 -41.893 40.792 1.00 51.33 ? 284 TYR B C 1 ATOM 6389 O O . TYR B 2 284 ? 52.298 -42.766 41.549 1.00 55.93 ? 284 TYR B O 1 ATOM 6390 C CB . TYR B 2 284 ? 53.983 -40.664 40.271 1.00 75.35 ? 284 TYR B CB 1 ATOM 6391 C CG . TYR B 2 284 ? 54.611 -39.388 39.755 1.00 99.77 ? 284 TYR B CG 1 ATOM 6392 C CD1 . TYR B 2 284 ? 54.331 -38.930 38.472 1.00 113.20 ? 284 TYR B CD1 1 ATOM 6393 C CD2 . TYR B 2 284 ? 55.504 -38.652 40.534 1.00 102.22 ? 284 TYR B CD2 1 ATOM 6394 C CE1 . TYR B 2 284 ? 54.908 -37.765 37.980 1.00 116.62 ? 284 TYR B CE1 1 ATOM 6395 C CE2 . TYR B 2 284 ? 56.088 -37.482 40.048 1.00 107.63 ? 284 TYR B CE2 1 ATOM 6396 C CZ . TYR B 2 284 ? 55.783 -37.046 38.769 1.00 109.70 ? 284 TYR B CZ 1 ATOM 6397 O OH . TYR B 2 284 ? 56.343 -35.895 38.262 1.00 101.63 ? 284 TYR B OH 1 ATOM 6398 N N . ASN B 2 285 ? 50.905 -42.098 39.936 1.00 58.09 ? 285 ASN B N 1 ATOM 6399 C CA . ASN B 2 285 ? 50.257 -43.409 39.834 1.00 53.28 ? 285 ASN B CA 1 ATOM 6400 C C . ASN B 2 285 ? 49.628 -43.809 41.179 1.00 46.77 ? 285 ASN B C 1 ATOM 6401 O O . ASN B 2 285 ? 49.961 -44.831 41.776 1.00 53.86 ? 285 ASN B O 1 ATOM 6402 C CB . ASN B 2 285 ? 51.260 -44.443 39.279 1.00 53.09 ? 285 ASN B CB 1 ATOM 6403 C CG . ASN B 2 285 ? 50.719 -45.862 39.221 1.00 61.25 ? 285 ASN B CG 1 ATOM 6404 O OD1 . ASN B 2 285 ? 49.510 -46.096 39.107 1.00 66.96 ? 285 ASN B OD1 1 ATOM 6405 N ND2 . ASN B 2 285 ? 51.647 -46.829 39.275 1.00 66.70 ? 285 ASN B ND2 1 ATOM 6406 N N . LEU B 2 286 ? 48.700 -42.972 41.631 1.00 41.08 ? 286 LEU B N 1 ATOM 6407 C CA . LEU B 2 286 ? 47.859 -43.241 42.794 1.00 52.95 ? 286 LEU B CA 1 ATOM 6408 C C . LEU B 2 286 ? 46.646 -44.122 42.448 1.00 56.59 ? 286 LEU B C 1 ATOM 6409 O O . LEU B 2 286 ? 46.034 -43.952 41.392 1.00 50.50 ? 286 LEU B O 1 ATOM 6410 C CB . LEU B 2 286 ? 47.378 -41.911 43.388 1.00 50.75 ? 286 LEU B CB 1 ATOM 6411 C CG . LEU B 2 286 ? 46.292 -41.916 44.460 1.00 44.73 ? 286 LEU B CG 1 ATOM 6412 C CD1 . LEU B 2 286 ? 46.849 -42.487 45.734 1.00 46.87 ? 286 LEU B CD1 1 ATOM 6413 C CD2 . LEU B 2 286 ? 45.792 -40.510 44.684 1.00 39.95 ? 286 LEU B CD2 1 ATOM 6414 N N . THR B 2 287 ? 46.297 -45.046 43.347 1.00 63.50 ? 287 THR B N 1 ATOM 6415 C CA . THR B 2 287 ? 45.116 -45.910 43.189 1.00 64.92 ? 287 THR B CA 1 ATOM 6416 C C . THR B 2 287 ? 44.209 -45.888 44.432 1.00 66.24 ? 287 THR B C 1 ATOM 6417 O O . THR B 2 287 ? 44.491 -46.572 45.411 1.00 77.48 ? 287 THR B O 1 ATOM 6418 C CB . THR B 2 287 ? 45.520 -47.382 42.901 1.00 47.65 ? 287 THR B CB 1 ATOM 6419 O OG1 . THR B 2 287 ? 46.468 -47.434 41.831 1.00 55.85 ? 287 THR B OG1 1 ATOM 6420 C CG2 . THR B 2 287 ? 44.319 -48.211 42.535 1.00 44.04 ? 287 THR B CG2 1 ATOM 6421 N N . ILE B 2 288 ? 43.129 -45.105 44.390 1.00 61.65 ? 288 ILE B N 1 ATOM 6422 C CA . ILE B 2 288 ? 42.145 -45.035 45.486 1.00 53.56 ? 288 ILE B CA 1 ATOM 6423 C C . ILE B 2 288 ? 41.410 -46.374 45.656 1.00 52.11 ? 288 ILE B C 1 ATOM 6424 O O . ILE B 2 288 ? 40.960 -46.963 44.675 1.00 45.53 ? 288 ILE B O 1 ATOM 6425 C CB . ILE B 2 288 ? 41.093 -43.941 45.222 1.00 57.96 ? 288 ILE B CB 1 ATOM 6426 C CG1 . ILE B 2 288 ? 41.738 -42.654 44.685 1.00 64.62 ? 288 ILE B CG1 1 ATOM 6427 C CG2 . ILE B 2 288 ? 40.280 -43.685 46.455 1.00 58.42 ? 288 ILE B CG2 1 ATOM 6428 C CD1 . ILE B 2 288 ? 42.750 -42.026 45.603 1.00 68.82 ? 288 ILE B CD1 1 ATOM 6429 N N . THR B 2 289 ? 41.250 -46.851 46.890 1.00 64.06 ? 289 THR B N 1 ATOM 6430 C CA . THR B 2 289 ? 41.069 -48.296 47.040 1.00 60.46 ? 289 THR B CA 1 ATOM 6431 C C . THR B 2 289 ? 39.770 -48.970 47.469 1.00 63.15 ? 289 THR B C 1 ATOM 6432 O O . THR B 2 289 ? 39.202 -49.708 46.665 1.00 91.86 ? 289 THR B O 1 ATOM 6433 C CB . THR B 2 289 ? 42.291 -48.972 47.664 1.00 66.19 ? 289 THR B CB 1 ATOM 6434 O OG1 . THR B 2 289 ? 43.080 -49.503 46.596 1.00 70.23 ? 289 THR B OG1 1 ATOM 6435 C CG2 . THR B 2 289 ? 41.893 -50.104 48.591 1.00 65.70 ? 289 THR B CG2 1 ATOM 6436 N N . GLU B 2 290 ? 39.288 -48.805 48.688 1.00 43.57 ? 290 GLU B N 1 ATOM 6437 C CA . GLU B 2 290 ? 38.189 -49.712 49.075 1.00 49.82 ? 290 GLU B CA 1 ATOM 6438 C C . GLU B 2 290 ? 36.854 -49.006 49.143 1.00 57.82 ? 290 GLU B C 1 ATOM 6439 O O . GLU B 2 290 ? 35.812 -49.597 48.867 1.00 56.95 ? 290 GLU B O 1 ATOM 6440 C CB . GLU B 2 290 ? 38.438 -50.409 50.420 1.00 55.47 ? 290 GLU B CB 1 ATOM 6441 C CG . GLU B 2 290 ? 39.599 -51.399 50.484 1.00 71.60 ? 290 GLU B CG 1 ATOM 6442 C CD . GLU B 2 290 ? 40.018 -51.705 51.927 1.00 89.61 ? 290 GLU B CD 1 ATOM 6443 O OE1 . GLU B 2 290 ? 39.361 -51.199 52.868 1.00 101.19 ? 290 GLU B OE1 1 ATOM 6444 O OE2 . GLU B 2 290 ? 41.002 -52.450 52.130 1.00 89.10 ? 290 GLU B OE2 1 ATOM 6445 N N . ARG B 2 291 ? 36.896 -47.743 49.546 1.00 59.01 ? 291 ARG B N 1 ATOM 6446 C CA . ARG B 2 291 ? 35.700 -46.948 49.744 1.00 54.75 ? 291 ARG B CA 1 ATOM 6447 C C . ARG B 2 291 ? 36.133 -45.500 49.815 1.00 66.62 ? 291 ARG B C 1 ATOM 6448 O O . ARG B 2 291 ? 37.294 -45.205 50.075 1.00 75.53 ? 291 ARG B O 1 ATOM 6449 C CB . ARG B 2 291 ? 34.967 -47.368 51.024 1.00 44.17 ? 291 ARG B CB 1 ATOM 6450 C CG . ARG B 2 291 ? 35.887 -47.818 52.160 1.00 68.20 ? 291 ARG B CG 1 ATOM 6451 C CD . ARG B 2 291 ? 35.179 -48.631 53.236 1.00 64.88 ? 291 ARG B CD 1 ATOM 6452 N NE . ARG B 2 291 ? 34.061 -47.879 53.797 1.00 90.42 ? 291 ARG B NE 1 ATOM 6453 C CZ . ARG B 2 291 ? 32.796 -47.994 53.394 1.00 114.23 ? 291 ARG B CZ 1 ATOM 6454 N NH1 . ARG B 2 291 ? 32.476 -48.838 52.419 1.00 125.32 ? 291 ARG B NH1 1 ATOM 6455 N NH2 . ARG B 2 291 ? 31.845 -47.266 53.968 1.00 113.79 ? 291 ARG B NH2 1 ATOM 6456 N N . ILE B 2 292 ? 35.198 -44.598 49.554 1.00 67.59 ? 292 ILE B N 1 ATOM 6457 C CA . ILE B 2 292 ? 35.443 -43.179 49.721 1.00 56.13 ? 292 ILE B CA 1 ATOM 6458 C C . ILE B 2 292 ? 34.344 -42.579 50.599 1.00 62.26 ? 292 ILE B C 1 ATOM 6459 O O . ILE B 2 292 ? 33.208 -42.402 50.159 1.00 68.77 ? 292 ILE B O 1 ATOM 6460 C CB . ILE B 2 292 ? 35.499 -42.458 48.370 1.00 50.39 ? 292 ILE B CB 1 ATOM 6461 C CG1 . ILE B 2 292 ? 36.570 -43.082 47.471 1.00 54.88 ? 292 ILE B CG1 1 ATOM 6462 C CG2 . ILE B 2 292 ? 35.766 -40.987 48.567 1.00 47.39 ? 292 ILE B CG2 1 ATOM 6463 C CD1 . ILE B 2 292 ? 36.696 -42.416 46.084 1.00 31.87 ? 292 ILE B CD1 1 ATOM 6464 N N . ASP B 2 293 ? 34.680 -42.296 51.855 1.00 62.31 ? 293 ASP B N 1 ATOM 6465 C CA . ASP B 2 293 ? 33.720 -41.731 52.798 1.00 58.61 ? 293 ASP B CA 1 ATOM 6466 C C . ASP B 2 293 ? 34.167 -40.348 53.228 1.00 63.54 ? 293 ASP B C 1 ATOM 6467 O O . ASP B 2 293 ? 35.247 -39.883 52.830 1.00 75.81 ? 293 ASP B O 1 ATOM 6468 C CB . ASP B 2 293 ? 33.546 -42.640 54.010 1.00 56.89 ? 293 ASP B CB 1 ATOM 6469 C CG . ASP B 2 293 ? 33.121 -44.048 53.625 1.00 74.27 ? 293 ASP B CG 1 ATOM 6470 O OD1 . ASP B 2 293 ? 33.903 -44.991 53.871 1.00 83.06 ? 293 ASP B OD1 1 ATOM 6471 O OD2 . ASP B 2 293 ? 32.017 -44.219 53.061 1.00 77.42 ? 293 ASP B OD2 1 ATOM 6472 N N . ARG B 2 294 ? 33.328 -39.677 54.011 1.00 55.44 ? 294 ARG B N 1 ATOM 6473 C CA . ARG B 2 294 ? 33.683 -38.355 54.513 1.00 74.43 ? 294 ARG B CA 1 ATOM 6474 C C . ARG B 2 294 ? 34.731 -38.507 55.603 1.00 87.50 ? 294 ARG B C 1 ATOM 6475 O O . ARG B 2 294 ? 34.473 -39.118 56.640 1.00 92.65 ? 294 ARG B O 1 ATOM 6476 C CB . ARG B 2 294 ? 32.457 -37.600 55.038 1.00 78.49 ? 294 ARG B CB 1 ATOM 6477 C CG . ARG B 2 294 ? 31.943 -36.518 54.099 1.00 96.57 ? 294 ARG B CG 1 ATOM 6478 C CD . ARG B 2 294 ? 30.642 -35.885 54.606 1.00 113.73 ? 294 ARG B CD 1 ATOM 6479 N NE . ARG B 2 294 ? 29.444 -36.637 54.221 1.00 123.54 ? 294 ARG B NE 1 ATOM 6480 C CZ . ARG B 2 294 ? 28.791 -36.468 53.073 1.00 116.74 ? 294 ARG B CZ 1 ATOM 6481 N NH1 . ARG B 2 294 ? 29.225 -35.572 52.192 1.00 108.69 ? 294 ARG B NH1 1 ATOM 6482 N NH2 . ARG B 2 294 ? 27.709 -37.193 52.803 1.00 107.72 ? 294 ARG B NH2 1 ATOM 6483 N N . GLU B 2 295 ? 35.921 -37.965 55.358 1.00 84.48 ? 295 GLU B N 1 ATOM 6484 C CA . GLU B 2 295 ? 37.016 -38.089 56.313 1.00 75.60 ? 295 GLU B CA 1 ATOM 6485 C C . GLU B 2 295 ? 37.297 -36.774 57.035 1.00 76.60 ? 295 GLU B C 1 ATOM 6486 O O . GLU B 2 295 ? 37.179 -35.692 56.455 1.00 80.36 ? 295 GLU B O 1 ATOM 6487 C CB . GLU B 2 295 ? 38.279 -38.602 55.615 1.00 73.28 ? 295 GLU B CB 1 ATOM 6488 C CG . GLU B 2 295 ? 38.105 -39.963 54.946 1.00 83.20 ? 295 GLU B CG 1 ATOM 6489 C CD . GLU B 2 295 ? 37.967 -41.103 55.938 1.00 91.53 ? 295 GLU B CD 1 ATOM 6490 O OE1 . GLU B 2 295 ? 38.691 -41.085 56.956 1.00 105.02 ? 295 GLU B OE1 1 ATOM 6491 O OE2 . GLU B 2 295 ? 37.145 -42.018 55.696 1.00 84.53 ? 295 GLU B OE2 1 ATOM 6492 N N . GLU B 2 296 ? 37.662 -36.877 58.308 1.00 75.50 ? 296 GLU B N 1 ATOM 6493 C CA . GLU B 2 296 ? 37.999 -35.702 59.098 1.00 80.47 ? 296 GLU B CA 1 ATOM 6494 C C . GLU B 2 296 ? 39.322 -35.109 58.643 1.00 78.34 ? 296 GLU B C 1 ATOM 6495 O O . GLU B 2 296 ? 40.290 -35.832 58.392 1.00 81.28 ? 296 GLU B O 1 ATOM 6496 C CB . GLU B 2 296 ? 38.059 -36.044 60.589 1.00 97.43 ? 296 GLU B CB 1 ATOM 6497 C CG . GLU B 2 296 ? 36.734 -36.526 61.156 1.00 119.48 ? 296 GLU B CG 1 ATOM 6498 C CD . GLU B 2 296 ? 35.558 -35.696 60.665 1.00 136.46 ? 296 GLU B CD 1 ATOM 6499 O OE1 . GLU B 2 296 ? 35.642 -34.448 60.736 1.00 142.37 ? 296 GLU B OE1 1 ATOM 6500 O OE2 . GLU B 2 296 ? 34.553 -36.292 60.207 1.00 138.84 ? 296 GLU B OE2 1 ATOM 6501 N N . PHE B 2 297 ? 39.354 -33.788 58.530 1.00 74.49 ? 297 PHE B N 1 ATOM 6502 C CA . PHE B 2 297 ? 40.577 -33.088 58.172 1.00 75.71 ? 297 PHE B CA 1 ATOM 6503 C C . PHE B 2 297 ? 40.430 -31.589 58.402 1.00 83.89 ? 297 PHE B C 1 ATOM 6504 O O . PHE B 2 297 ? 39.353 -31.025 58.213 1.00 88.80 ? 297 PHE B O 1 ATOM 6505 C CB . PHE B 2 297 ? 40.964 -33.367 56.715 1.00 68.29 ? 297 PHE B CB 1 ATOM 6506 C CG . PHE B 2 297 ? 39.960 -32.873 55.716 1.00 73.72 ? 297 PHE B CG 1 ATOM 6507 C CD1 . PHE B 2 297 ? 40.146 -31.661 55.069 1.00 75.97 ? 297 PHE B CD1 1 ATOM 6508 C CD2 . PHE B 2 297 ? 38.820 -33.620 55.431 1.00 73.07 ? 297 PHE B CD2 1 ATOM 6509 C CE1 . PHE B 2 297 ? 39.210 -31.202 54.151 1.00 79.51 ? 297 PHE B CE1 1 ATOM 6510 C CE2 . PHE B 2 297 ? 37.886 -33.174 54.524 1.00 70.17 ? 297 PHE B CE2 1 ATOM 6511 C CZ . PHE B 2 297 ? 38.080 -31.964 53.877 1.00 77.28 ? 297 PHE B CZ 1 ATOM 6512 N N . THR B 2 298 ? 41.516 -30.962 58.837 1.00 85.10 ? 298 THR B N 1 ATOM 6513 C CA . THR B 2 298 ? 41.619 -29.512 58.886 1.00 88.37 ? 298 THR B CA 1 ATOM 6514 C C . THR B 2 298 ? 42.983 -29.124 58.345 1.00 90.88 ? 298 THR B C 1 ATOM 6515 O O . THR B 2 298 ? 43.994 -29.737 58.690 1.00 98.09 ? 298 THR B O 1 ATOM 6516 C CB . THR B 2 298 ? 41.448 -28.928 60.327 1.00 86.91 ? 298 THR B CB 1 ATOM 6517 O OG1 . THR B 2 298 ? 41.828 -29.899 61.315 1.00 76.48 ? 298 THR B OG1 1 ATOM 6518 C CG2 . THR B 2 298 ? 40.003 -28.488 60.570 1.00 90.81 ? 298 THR B CG2 1 ATOM 6519 N N . TYR B 2 299 ? 43.010 -28.111 57.489 1.00 82.81 ? 299 TYR B N 1 ATOM 6520 C CA . TYR B 2 299 ? 44.269 -27.594 56.976 1.00 71.50 ? 299 TYR B CA 1 ATOM 6521 C C . TYR B 2 299 ? 44.711 -26.341 57.710 1.00 75.22 ? 299 TYR B C 1 ATOM 6522 O O . TYR B 2 299 ? 44.111 -25.275 57.559 1.00 63.05 ? 299 TYR B O 1 ATOM 6523 C CB . TYR B 2 299 ? 44.141 -27.301 55.498 1.00 65.74 ? 299 TYR B CB 1 ATOM 6524 C CG . TYR B 2 299 ? 43.884 -28.537 54.709 1.00 71.85 ? 299 TYR B CG 1 ATOM 6525 C CD1 . TYR B 2 299 ? 42.666 -28.741 54.085 1.00 63.63 ? 299 TYR B CD1 1 ATOM 6526 C CD2 . TYR B 2 299 ? 44.849 -29.524 54.618 1.00 76.19 ? 299 TYR B CD2 1 ATOM 6527 C CE1 . TYR B 2 299 ? 42.426 -29.874 53.373 1.00 63.37 ? 299 TYR B CE1 1 ATOM 6528 C CE2 . TYR B 2 299 ? 44.619 -30.663 53.906 1.00 85.02 ? 299 TYR B CE2 1 ATOM 6529 C CZ . TYR B 2 299 ? 43.405 -30.834 53.280 1.00 80.54 ? 299 TYR B CZ 1 ATOM 6530 O OH . TYR B 2 299 ? 43.173 -31.978 52.558 1.00 85.99 ? 299 TYR B OH 1 ATOM 6531 N N . SER B 2 300 ? 45.767 -26.482 58.504 1.00 81.94 ? 300 SER B N 1 ATOM 6532 C CA . SER B 2 300 ? 46.315 -25.364 59.249 1.00 83.33 ? 300 SER B CA 1 ATOM 6533 C C . SER B 2 300 ? 47.557 -24.875 58.542 1.00 84.16 ? 300 SER B C 1 ATOM 6534 O O . SER B 2 300 ? 47.993 -25.480 57.568 1.00 81.70 ? 300 SER B O 1 ATOM 6535 C CB . SER B 2 300 ? 46.686 -25.799 60.663 1.00 89.97 ? 300 SER B CB 1 ATOM 6536 O OG . SER B 2 300 ? 45.726 -26.696 61.188 1.00 100.52 ? 300 SER B OG 1 ATOM 6537 N N . GLU B 2 301 ? 48.123 -23.782 59.042 1.00 86.09 ? 301 GLU B N 1 ATOM 6538 C CA . GLU B 2 301 ? 49.399 -23.277 58.557 1.00 84.73 ? 301 GLU B CA 1 ATOM 6539 C C . GLU B 2 301 ? 50.287 -24.437 58.140 1.00 75.35 ? 301 GLU B C 1 ATOM 6540 O O . GLU B 2 301 ? 50.471 -25.388 58.902 1.00 77.77 ? 301 GLU B O 1 ATOM 6541 C CB . GLU B 2 301 ? 50.090 -22.473 59.655 1.00 100.84 ? 301 GLU B CB 1 ATOM 6542 C CG . GLU B 2 301 ? 50.225 -23.215 60.995 1.00 119.83 ? 301 GLU B CG 1 ATOM 6543 C CD . GLU B 2 301 ? 49.124 -22.872 62.004 1.00 127.87 ? 301 GLU B CD 1 ATOM 6544 O OE1 . GLU B 2 301 ? 47.982 -22.577 61.589 1.00 132.73 ? 301 GLU B OE1 1 ATOM 6545 O OE2 . GLU B 2 301 ? 49.408 -22.900 63.223 1.00 122.52 ? 301 GLU B OE2 1 ATOM 6546 N N . THR B 2 302 ? 50.829 -24.363 56.930 1.00 65.15 ? 302 THR B N 1 ATOM 6547 C CA . THR B 2 302 ? 51.659 -25.443 56.404 1.00 70.57 ? 302 THR B CA 1 ATOM 6548 C C . THR B 2 302 ? 52.848 -24.908 55.621 1.00 76.20 ? 302 THR B C 1 ATOM 6549 O O . THR B 2 302 ? 52.817 -23.787 55.129 1.00 85.83 ? 302 THR B O 1 ATOM 6550 C CB . THR B 2 302 ? 50.851 -26.370 55.481 1.00 68.33 ? 302 THR B CB 1 ATOM 6551 O OG1 . THR B 2 302 ? 51.728 -27.314 54.853 1.00 68.03 ? 302 THR B OG1 1 ATOM 6552 C CG2 . THR B 2 302 ? 50.148 -25.559 54.406 1.00 66.67 ? 302 THR B CG2 1 ATOM 6553 N N . ALA B 2 303 ? 53.896 -25.714 55.508 1.00 69.19 ? 303 ALA B N 1 ATOM 6554 C CA . ALA B 2 303 ? 55.038 -25.341 54.689 1.00 69.34 ? 303 ALA B CA 1 ATOM 6555 C C . ALA B 2 303 ? 54.771 -25.609 53.200 1.00 72.10 ? 303 ALA B C 1 ATOM 6556 O O . ALA B 2 303 ? 55.418 -25.021 52.322 1.00 72.63 ? 303 ALA B O 1 ATOM 6557 C CB . ALA B 2 303 ? 56.283 -26.073 55.155 1.00 64.95 ? 303 ALA B CB 1 ATOM 6558 N N . LEU B 2 304 ? 53.810 -26.494 52.933 1.00 60.50 ? 304 LEU B N 1 ATOM 6559 C CA . LEU B 2 304 ? 53.448 -26.875 51.576 1.00 57.91 ? 304 LEU B CA 1 ATOM 6560 C C . LEU B 2 304 ? 53.223 -25.707 50.631 1.00 65.12 ? 304 LEU B C 1 ATOM 6561 O O . LEU B 2 304 ? 52.372 -24.850 50.858 1.00 69.64 ? 304 LEU B O 1 ATOM 6562 C CB . LEU B 2 304 ? 52.189 -27.735 51.582 1.00 60.63 ? 304 LEU B CB 1 ATOM 6563 C CG . LEU B 2 304 ? 52.374 -29.240 51.439 1.00 68.38 ? 304 LEU B CG 1 ATOM 6564 C CD1 . LEU B 2 304 ? 51.097 -29.848 50.915 1.00 77.71 ? 304 LEU B CD1 1 ATOM 6565 C CD2 . LEU B 2 304 ? 53.513 -29.554 50.502 1.00 64.09 ? 304 LEU B CD2 1 ATOM 6566 N N . LYS B 2 305 ? 53.979 -25.699 49.547 1.00 70.44 ? 305 LYS B N 1 ATOM 6567 C CA . LYS B 2 305 ? 53.738 -24.760 48.470 1.00 76.86 ? 305 LYS B CA 1 ATOM 6568 C C . LYS B 2 305 ? 52.945 -25.443 47.358 1.00 76.49 ? 305 LYS B C 1 ATOM 6569 O O . LYS B 2 305 ? 52.149 -24.792 46.677 1.00 75.94 ? 305 LYS B O 1 ATOM 6570 C CB . LYS B 2 305 ? 55.064 -24.216 47.935 1.00 84.56 ? 305 LYS B CB 1 ATOM 6571 C CG . LYS B 2 305 ? 54.937 -23.252 46.767 1.00 94.95 ? 305 LYS B CG 1 ATOM 6572 C CD . LYS B 2 305 ? 56.284 -22.585 46.482 1.00 102.90 ? 305 LYS B CD 1 ATOM 6573 C CE . LYS B 2 305 ? 56.284 -21.788 45.179 1.00 92.78 ? 305 LYS B CE 1 ATOM 6574 N NZ . LYS B 2 305 ? 57.654 -21.282 44.887 1.00 84.43 ? 305 LYS B NZ 1 ATOM 6575 N N . SER B 2 306 ? 53.137 -26.755 47.198 1.00 69.85 ? 306 SER B N 1 ATOM 6576 C CA . SER B 2 306 ? 52.616 -27.457 46.021 1.00 71.77 ? 306 SER B CA 1 ATOM 6577 C C . SER B 2 306 ? 52.254 -28.922 46.191 1.00 64.06 ? 306 SER B C 1 ATOM 6578 O O . SER B 2 306 ? 53.118 -29.749 46.447 1.00 72.77 ? 306 SER B O 1 ATOM 6579 C CB . SER B 2 306 ? 53.619 -27.371 44.862 1.00 72.81 ? 306 SER B CB 1 ATOM 6580 O OG . SER B 2 306 ? 53.582 -28.562 44.084 1.00 66.25 ? 306 SER B OG 1 ATOM 6581 N N . LEU B 2 307 ? 50.981 -29.245 45.985 1.00 56.72 ? 307 LEU B N 1 ATOM 6582 C CA . LEU B 2 307 ? 50.570 -30.629 45.760 1.00 50.50 ? 307 LEU B CA 1 ATOM 6583 C C . LEU B 2 307 ? 50.484 -30.901 44.261 1.00 59.76 ? 307 LEU B C 1 ATOM 6584 O O . LEU B 2 307 ? 49.997 -30.075 43.486 1.00 66.27 ? 307 LEU B O 1 ATOM 6585 C CB . LEU B 2 307 ? 49.227 -30.921 46.417 1.00 55.54 ? 307 LEU B CB 1 ATOM 6586 C CG . LEU B 2 307 ? 48.843 -32.397 46.397 1.00 61.13 ? 307 LEU B CG 1 ATOM 6587 C CD1 . LEU B 2 307 ? 49.965 -33.221 46.990 1.00 59.56 ? 307 LEU B CD1 1 ATOM 6588 C CD2 . LEU B 2 307 ? 47.553 -32.608 47.167 1.00 62.60 ? 307 LEU B CD2 1 ATOM 6589 N N . MET B 2 308 ? 50.974 -32.058 43.847 1.00 59.39 ? 308 MET B N 1 ATOM 6590 C CA . MET B 2 308 ? 50.950 -32.416 42.441 1.00 55.83 ? 308 MET B CA 1 ATOM 6591 C C . MET B 2 308 ? 50.640 -33.900 42.293 1.00 65.64 ? 308 MET B C 1 ATOM 6592 O O . MET B 2 308 ? 51.453 -34.750 42.657 1.00 72.25 ? 308 MET B O 1 ATOM 6593 C CB . MET B 2 308 ? 52.294 -32.110 41.798 1.00 57.80 ? 308 MET B CB 1 ATOM 6594 C CG . MET B 2 308 ? 52.232 -32.012 40.289 1.00 66.33 ? 308 MET B CG 1 ATOM 6595 S SD . MET B 2 308 ? 53.348 -33.128 39.429 1.00 156.83 ? 308 MET B SD 1 ATOM 6596 C CE . MET B 2 308 ? 52.465 -34.653 39.660 1.00 25.28 ? 308 MET B CE 1 ATOM 6597 N N . ILE B 2 309 ? 49.459 -34.207 41.765 1.00 57.63 ? 309 ILE B N 1 ATOM 6598 C CA . ILE B 2 309 ? 49.037 -35.587 41.568 1.00 51.79 ? 309 ILE B CA 1 ATOM 6599 C C . ILE B 2 309 ? 48.891 -35.880 40.077 1.00 63.17 ? 309 ILE B C 1 ATOM 6600 O O . ILE B 2 309 ? 48.297 -35.092 39.340 1.00 67.70 ? 309 ILE B O 1 ATOM 6601 C CB . ILE B 2 309 ? 47.712 -35.868 42.291 1.00 46.20 ? 309 ILE B CB 1 ATOM 6602 C CG1 . ILE B 2 309 ? 47.778 -35.344 43.723 1.00 65.52 ? 309 ILE B CG1 1 ATOM 6603 C CG2 . ILE B 2 309 ? 47.428 -37.345 42.315 1.00 44.35 ? 309 ILE B CG2 1 ATOM 6604 C CD1 . ILE B 2 309 ? 46.710 -35.908 44.627 1.00 70.86 ? 309 ILE B CD1 1 ATOM 6605 N N . GLU B 2 310 ? 49.445 -37.006 39.633 1.00 60.68 ? 310 GLU B N 1 ATOM 6606 C CA . GLU B 2 310 ? 49.409 -37.368 38.220 1.00 58.14 ? 310 GLU B CA 1 ATOM 6607 C C . GLU B 2 310 ? 49.192 -38.849 38.014 1.00 58.40 ? 310 GLU B C 1 ATOM 6608 O O . GLU B 2 310 ? 49.932 -39.673 38.538 1.00 61.02 ? 310 GLU B O 1 ATOM 6609 C CB . GLU B 2 310 ? 50.688 -36.940 37.490 1.00 58.73 ? 310 GLU B CB 1 ATOM 6610 C CG . GLU B 2 310 ? 50.512 -36.861 35.972 1.00 71.68 ? 310 GLU B CG 1 ATOM 6611 C CD . GLU B 2 310 ? 51.802 -36.565 35.209 1.00 80.35 ? 310 GLU B CD 1 ATOM 6612 O OE1 . GLU B 2 310 ? 52.619 -35.730 35.674 1.00 83.85 ? 310 GLU B OE1 1 ATOM 6613 O OE2 . GLU B 2 310 ? 51.984 -37.168 34.126 1.00 70.30 ? 310 GLU B OE2 1 ATOM 6614 N N . HIS B 2 311 ? 48.184 -39.174 37.217 1.00 59.73 ? 311 HIS B N 1 ATOM 6615 C CA . HIS B 2 311 ? 47.845 -40.559 36.907 1.00 58.45 ? 311 HIS B CA 1 ATOM 6616 C C . HIS B 2 311 ? 47.141 -41.211 38.073 1.00 63.17 ? 311 HIS B C 1 ATOM 6617 O O . HIS B 2 311 ? 47.779 -41.779 38.951 1.00 66.50 ? 311 HIS B O 1 ATOM 6618 C CB . HIS B 2 311 ? 49.078 -41.378 36.528 1.00 51.76 ? 311 HIS B CB 1 ATOM 6619 C CG . HIS B 2 311 ? 48.743 -42.709 35.935 1.00 62.91 ? 311 HIS B CG 1 ATOM 6620 N ND1 . HIS B 2 311 ? 47.823 -42.857 34.920 1.00 65.00 ? 311 HIS B ND1 1 ATOM 6621 C CD2 . HIS B 2 311 ? 49.191 -43.953 36.219 1.00 75.07 ? 311 HIS B CD2 1 ATOM 6622 C CE1 . HIS B 2 311 ? 47.719 -44.133 34.605 1.00 68.90 ? 311 HIS B CE1 1 ATOM 6623 N NE2 . HIS B 2 311 ? 48.542 -44.821 35.376 1.00 71.80 ? 311 HIS B NE2 1 ATOM 6624 N N . VAL B 2 312 ? 45.820 -41.133 38.078 1.00 56.82 ? 312 VAL B N 1 ATOM 6625 C CA . VAL B 2 312 ? 45.056 -41.634 39.199 1.00 57.90 ? 312 VAL B CA 1 ATOM 6626 C C . VAL B 2 312 ? 44.069 -42.666 38.715 1.00 58.71 ? 312 VAL B C 1 ATOM 6627 O O . VAL B 2 312 ? 43.178 -42.352 37.930 1.00 65.98 ? 312 VAL B O 1 ATOM 6628 C CB . VAL B 2 312 ? 44.294 -40.507 39.894 1.00 60.25 ? 312 VAL B CB 1 ATOM 6629 C CG1 . VAL B 2 312 ? 43.483 -41.065 41.048 1.00 60.05 ? 312 VAL B CG1 1 ATOM 6630 C CG2 . VAL B 2 312 ? 45.264 -39.441 40.373 1.00 63.80 ? 312 VAL B CG2 1 ATOM 6631 N N . LYS B 2 313 ? 44.247 -43.904 39.164 1.00 52.83 ? 313 LYS B N 1 ATOM 6632 C CA . LYS B 2 313 ? 43.295 -44.967 38.873 1.00 51.72 ? 313 LYS B CA 1 ATOM 6633 C C . LYS B 2 313 ? 42.336 -44.983 40.109 1.00 66.53 ? 313 LYS B C 1 ATOM 6634 O O . LYS B 2 313 ? 42.789 -44.844 41.243 1.00 64.10 ? 313 LYS B O 1 ATOM 6635 C CB . LYS B 2 313 ? 44.023 -46.331 38.539 1.00 44.68 ? 313 LYS B CB 1 ATOM 6636 C CG . LYS B 2 313 ? 45.491 -46.261 37.804 1.00 62.85 ? 313 LYS B CG 1 ATOM 6637 C CD . LYS B 2 313 ? 46.052 -47.608 37.087 1.00 142.59 ? 313 LYS B CD 1 ATOM 6638 C CE . LYS B 2 313 ? 47.497 -47.469 36.375 1.00 144.86 ? 313 LYS B CE 1 ATOM 6639 N NZ . LYS B 2 313 ? 48.143 -48.542 35.399 1.00 24.01 ? 313 LYS B NZ 1 ATOM 6640 N N . ASN B 2 314 ? 41.019 -45.056 39.906 1.00 67.08 ? 314 ASN B N 1 ATOM 6641 C CA . ASN B 2 314 ? 40.078 -45.149 41.046 1.00 60.43 ? 314 ASN B CA 1 ATOM 6642 C C . ASN B 2 314 ? 39.124 -46.357 40.987 1.00 56.25 ? 314 ASN B C 1 ATOM 6643 O O . ASN B 2 314 ? 38.375 -46.523 40.032 1.00 65.64 ? 314 ASN B O 1 ATOM 6644 C CB . ASN B 2 314 ? 39.287 -43.848 41.228 1.00 52.78 ? 314 ASN B CB 1 ATOM 6645 C CG . ASN B 2 314 ? 38.221 -43.942 42.331 1.00 54.72 ? 314 ASN B CG 1 ATOM 6646 O OD1 . ASN B 2 314 ? 38.117 -44.942 43.037 1.00 59.34 ? 314 ASN B OD1 1 ATOM 6647 N ND2 . ASN B 2 314 ? 37.422 -42.889 42.471 1.00 50.98 ? 314 ASN B ND2 1 ATOM 6648 N N . GLN B 2 315 ? 39.154 -47.189 42.021 1.00 54.87 ? 315 GLN B N 1 ATOM 6649 C CA . GLN B 2 315 ? 38.413 -48.448 42.031 1.00 59.33 ? 315 GLN B CA 1 ATOM 6650 C C . GLN B 2 315 ? 37.061 -48.388 42.741 1.00 59.72 ? 315 GLN B C 1 ATOM 6651 O O . GLN B 2 315 ? 36.310 -49.360 42.721 1.00 63.09 ? 315 GLN B O 1 ATOM 6652 C CB . GLN B 2 315 ? 39.254 -49.552 42.666 1.00 62.10 ? 315 GLN B CB 1 ATOM 6653 C CG . GLN B 2 315 ? 40.606 -49.717 42.036 1.00 67.83 ? 315 GLN B CG 1 ATOM 6654 C CD . GLN B 2 315 ? 41.380 -50.853 42.650 1.00 74.08 ? 315 GLN B CD 1 ATOM 6655 O OE1 . GLN B 2 315 ? 40.979 -51.411 43.686 1.00 74.91 ? 315 GLN B OE1 1 ATOM 6656 N NE2 . GLN B 2 315 ? 42.501 -51.210 42.019 1.00 64.36 ? 315 GLN B NE2 1 ATOM 6657 N N . VAL B 2 316 ? 36.763 -47.266 43.383 1.00 55.37 ? 316 VAL B N 1 ATOM 6658 C CA . VAL B 2 316 ? 35.453 -47.069 43.993 1.00 63.14 ? 316 VAL B CA 1 ATOM 6659 C C . VAL B 2 316 ? 34.552 -46.340 42.989 1.00 63.51 ? 316 VAL B C 1 ATOM 6660 O O . VAL B 2 316 ? 35.011 -45.404 42.329 1.00 47.53 ? 316 VAL B O 1 ATOM 6661 C CB . VAL B 2 316 ? 35.569 -46.243 45.289 1.00 58.11 ? 316 VAL B CB 1 ATOM 6662 C CG1 . VAL B 2 316 ? 34.276 -46.278 46.057 1.00 54.27 ? 316 VAL B CG1 1 ATOM 6663 C CG2 . VAL B 2 316 ? 36.676 -46.781 46.138 1.00 59.65 ? 316 VAL B CG2 1 ATOM 6664 N N . PHE B 2 317 ? 33.289 -46.764 42.861 1.00 61.56 ? 317 PHE B N 1 ATOM 6665 C CA . PHE B 2 317 ? 32.392 -46.155 41.864 1.00 57.55 ? 317 PHE B CA 1 ATOM 6666 C C . PHE B 2 317 ? 31.235 -45.394 42.453 1.00 59.44 ? 317 PHE B C 1 ATOM 6667 O O . PHE B 2 317 ? 30.834 -44.356 41.912 1.00 66.55 ? 317 PHE B O 1 ATOM 6668 C CB . PHE B 2 317 ? 31.902 -47.171 40.832 1.00 54.93 ? 317 PHE B CB 1 ATOM 6669 C CG . PHE B 2 317 ? 32.991 -47.667 39.958 1.00 60.95 ? 317 PHE B CG 1 ATOM 6670 C CD1 . PHE B 2 317 ? 33.551 -48.909 40.168 1.00 57.27 ? 317 PHE B CD1 1 ATOM 6671 C CD2 . PHE B 2 317 ? 33.516 -46.859 38.976 1.00 68.30 ? 317 PHE B CD2 1 ATOM 6672 C CE1 . PHE B 2 317 ? 34.577 -49.352 39.386 1.00 57.11 ? 317 PHE B CE1 1 ATOM 6673 C CE2 . PHE B 2 317 ? 34.549 -47.303 38.189 1.00 70.40 ? 317 PHE B CE2 1 ATOM 6674 C CZ . PHE B 2 317 ? 35.084 -48.549 38.397 1.00 56.94 ? 317 PHE B CZ 1 ATOM 6675 N N . LEU B 2 318 ? 30.710 -45.910 43.559 1.00 55.47 ? 318 LEU B N 1 ATOM 6676 C CA . LEU B 2 318 ? 29.666 -45.225 44.308 1.00 58.31 ? 318 LEU B CA 1 ATOM 6677 C C . LEU B 2 318 ? 30.225 -44.548 45.569 1.00 66.05 ? 318 LEU B C 1 ATOM 6678 O O . LEU B 2 318 ? 30.734 -45.206 46.478 1.00 68.19 ? 318 LEU B O 1 ATOM 6679 C CB . LEU B 2 318 ? 28.545 -46.192 44.691 1.00 57.65 ? 318 LEU B CB 1 ATOM 6680 C CG . LEU B 2 318 ? 28.136 -47.275 43.700 1.00 56.73 ? 318 LEU B CG 1 ATOM 6681 C CD1 . LEU B 2 318 ? 26.926 -48.055 44.225 1.00 61.62 ? 318 LEU B CD1 1 ATOM 6682 C CD2 . LEU B 2 318 ? 27.832 -46.644 42.380 1.00 50.67 ? 318 LEU B CD2 1 ATOM 6683 N N . PHE B 2 319 ? 30.112 -43.229 45.620 1.00 67.27 ? 319 PHE B N 1 ATOM 6684 C CA . PHE B 2 319 ? 30.545 -42.477 46.783 1.00 70.00 ? 319 PHE B CA 1 ATOM 6685 C C . PHE B 2 319 ? 30.146 -41.024 46.638 1.00 76.04 ? 319 PHE B C 1 ATOM 6686 O O . PHE B 2 319 ? 29.936 -40.553 45.532 1.00 86.79 ? 319 PHE B O 1 ATOM 6687 C CB . PHE B 2 319 ? 32.052 -42.581 46.935 1.00 56.60 ? 319 PHE B CB 1 ATOM 6688 C CG . PHE B 2 319 ? 32.812 -42.000 45.797 1.00 55.11 ? 319 PHE B CG 1 ATOM 6689 C CD1 . PHE B 2 319 ? 33.216 -40.672 45.823 1.00 58.82 ? 319 PHE B CD1 1 ATOM 6690 C CD2 . PHE B 2 319 ? 33.146 -42.780 44.700 1.00 54.71 ? 319 PHE B CD2 1 ATOM 6691 C CE1 . PHE B 2 319 ? 33.943 -40.125 44.761 1.00 57.96 ? 319 PHE B CE1 1 ATOM 6692 C CE2 . PHE B 2 319 ? 33.873 -42.243 43.641 1.00 58.03 ? 319 PHE B CE2 1 ATOM 6693 C CZ . PHE B 2 319 ? 34.272 -40.912 43.672 1.00 53.19 ? 319 PHE B CZ 1 ATOM 6694 N N . SER B 2 320 ? 30.038 -40.302 47.744 1.00 75.25 ? 320 SER B N 1 ATOM 6695 C CA . SER B 2 320 ? 29.711 -38.890 47.633 1.00 75.43 ? 320 SER B CA 1 ATOM 6696 C C . SER B 2 320 ? 30.907 -38.105 47.107 1.00 77.67 ? 320 SER B C 1 ATOM 6697 O O . SER B 2 320 ? 31.941 -38.028 47.762 1.00 75.53 ? 320 SER B O 1 ATOM 6698 C CB . SER B 2 320 ? 29.258 -38.316 48.969 1.00 71.61 ? 320 SER B CB 1 ATOM 6699 O OG . SER B 2 320 ? 29.125 -36.909 48.865 1.00 73.73 ? 320 SER B OG 1 ATOM 6700 N N . LYS B 2 321 ? 30.767 -37.515 45.925 1.00 74.21 ? 321 LYS B N 1 ATOM 6701 C CA . LYS B 2 321 ? 31.893 -36.824 45.309 1.00 65.61 ? 321 LYS B CA 1 ATOM 6702 C C . LYS B 2 321 ? 32.405 -35.643 46.151 1.00 68.42 ? 321 LYS B C 1 ATOM 6703 O O . LYS B 2 321 ? 33.576 -35.262 46.042 1.00 67.18 ? 321 LYS B O 1 ATOM 6704 C CB . LYS B 2 321 ? 31.573 -36.406 43.867 1.00 63.08 ? 321 LYS B CB 1 ATOM 6705 C CG . LYS B 2 321 ? 31.499 -37.568 42.876 1.00 66.00 ? 321 LYS B CG 1 ATOM 6706 C CD . LYS B 2 321 ? 30.251 -38.419 43.122 1.00 75.61 ? 321 LYS B CD 1 ATOM 6707 C CE . LYS B 2 321 ? 30.301 -39.714 42.339 1.00 60.92 ? 321 LYS B CE 1 ATOM 6708 N NZ . LYS B 2 321 ? 31.712 -40.057 42.061 1.00 59.33 ? 321 LYS B NZ 1 ATOM 6709 N N . GLU B 2 322 ? 31.543 -35.076 46.996 1.00 67.77 ? 322 GLU B N 1 ATOM 6710 C CA . GLU B 2 322 ? 31.992 -34.065 47.955 1.00 69.38 ? 322 GLU B CA 1 ATOM 6711 C C . GLU B 2 322 ? 33.135 -34.630 48.796 1.00 66.17 ? 322 GLU B C 1 ATOM 6712 O O . GLU B 2 322 ? 34.198 -34.017 48.912 1.00 51.32 ? 322 GLU B O 1 ATOM 6713 C CB . GLU B 2 322 ? 30.847 -33.619 48.863 1.00 70.82 ? 322 GLU B CB 1 ATOM 6714 C CG . GLU B 2 322 ? 29.959 -32.543 48.266 1.00 95.19 ? 322 GLU B CG 1 ATOM 6715 C CD . GLU B 2 322 ? 28.476 -32.749 48.586 1.00 119.38 ? 322 GLU B CD 1 ATOM 6716 O OE1 . GLU B 2 322 ? 27.776 -31.741 48.841 1.00 122.09 ? 322 GLU B OE1 1 ATOM 6717 O OE2 . GLU B 2 322 ? 28.007 -33.916 48.574 1.00 124.48 ? 322 GLU B OE2 1 ATOM 6718 N N . ALA B 2 323 ? 32.904 -35.821 49.348 1.00 75.88 ? 323 ALA B N 1 ATOM 6719 C CA . ALA B 2 323 ? 33.833 -36.481 50.268 1.00 68.78 ? 323 ALA B CA 1 ATOM 6720 C C . ALA B 2 323 ? 35.239 -36.580 49.714 1.00 64.98 ? 323 ALA B C 1 ATOM 6721 O O . ALA B 2 323 ? 36.212 -36.617 50.471 1.00 73.13 ? 323 ALA B O 1 ATOM 6722 C CB . ALA B 2 323 ? 33.321 -37.864 50.636 1.00 59.70 ? 323 ALA B CB 1 ATOM 6723 N N . LEU B 2 324 ? 35.333 -36.632 48.391 1.00 61.50 ? 324 LEU B N 1 ATOM 6724 C CA . LEU B 2 324 ? 36.607 -36.750 47.705 1.00 56.26 ? 324 LEU B CA 1 ATOM 6725 C C . LEU B 2 324 ? 37.116 -35.376 47.283 1.00 61.08 ? 324 LEU B C 1 ATOM 6726 O O . LEU B 2 324 ? 38.241 -35.023 47.609 1.00 70.38 ? 324 LEU B O 1 ATOM 6727 C CB . LEU B 2 324 ? 36.482 -37.693 46.500 1.00 63.14 ? 324 LEU B CB 1 ATOM 6728 C CG . LEU B 2 324 ? 37.581 -37.687 45.426 1.00 67.59 ? 324 LEU B CG 1 ATOM 6729 C CD1 . LEU B 2 324 ? 38.846 -38.378 45.903 1.00 76.54 ? 324 LEU B CD1 1 ATOM 6730 C CD2 . LEU B 2 324 ? 37.083 -38.349 44.171 1.00 46.84 ? 324 LEU B CD2 1 ATOM 6731 N N . TYR B 2 325 ? 36.297 -34.592 46.582 1.00 60.08 ? 325 TYR B N 1 ATOM 6732 C CA . TYR B 2 325 ? 36.782 -33.325 46.016 1.00 71.81 ? 325 TYR B CA 1 ATOM 6733 C C . TYR B 2 325 ? 37.056 -32.221 47.049 1.00 73.56 ? 325 TYR B C 1 ATOM 6734 O O . TYR B 2 325 ? 37.915 -31.358 46.842 1.00 68.85 ? 325 TYR B O 1 ATOM 6735 C CB . TYR B 2 325 ? 35.861 -32.788 44.907 1.00 69.98 ? 325 TYR B CB 1 ATOM 6736 C CG . TYR B 2 325 ? 35.733 -33.692 43.698 1.00 67.64 ? 325 TYR B CG 1 ATOM 6737 C CD1 . TYR B 2 325 ? 34.503 -33.888 43.085 1.00 64.47 ? 325 TYR B CD1 1 ATOM 6738 C CD2 . TYR B 2 325 ? 36.834 -34.352 43.174 1.00 65.20 ? 325 TYR B CD2 1 ATOM 6739 C CE1 . TYR B 2 325 ? 34.372 -34.713 41.988 1.00 59.35 ? 325 TYR B CE1 1 ATOM 6740 C CE2 . TYR B 2 325 ? 36.713 -35.182 42.070 1.00 61.39 ? 325 TYR B CE2 1 ATOM 6741 C CZ . TYR B 2 325 ? 35.476 -35.359 41.482 1.00 59.84 ? 325 TYR B CZ 1 ATOM 6742 O OH . TYR B 2 325 ? 35.335 -36.191 40.390 1.00 57.04 ? 325 TYR B OH 1 ATOM 6743 N N . SER B 2 326 ? 36.337 -32.233 48.161 1.00 72.32 ? 326 SER B N 1 ATOM 6744 C CA . SER B 2 326 ? 36.521 -31.164 49.137 1.00 74.02 ? 326 SER B CA 1 ATOM 6745 C C . SER B 2 326 ? 37.896 -31.261 49.817 1.00 76.77 ? 326 SER B C 1 ATOM 6746 O O . SER B 2 326 ? 38.530 -30.247 50.109 1.00 68.45 ? 326 SER B O 1 ATOM 6747 C CB . SER B 2 326 ? 35.385 -31.161 50.151 1.00 60.79 ? 326 SER B CB 1 ATOM 6748 O OG . SER B 2 326 ? 35.353 -32.402 50.823 1.00 73.29 ? 326 SER B OG 1 ATOM 6749 N N . VAL B 2 327 ? 38.353 -32.488 50.046 1.00 78.38 ? 327 VAL B N 1 ATOM 6750 C CA . VAL B 2 327 ? 39.684 -32.745 50.593 1.00 68.22 ? 327 VAL B CA 1 ATOM 6751 C C . VAL B 2 327 ? 40.792 -31.986 49.855 1.00 67.08 ? 327 VAL B C 1 ATOM 6752 O O . VAL B 2 327 ? 41.807 -31.638 50.453 1.00 65.31 ? 327 VAL B O 1 ATOM 6753 C CB . VAL B 2 327 ? 39.981 -34.254 50.584 1.00 64.24 ? 327 VAL B CB 1 ATOM 6754 C CG1 . VAL B 2 327 ? 41.463 -34.529 50.771 1.00 55.07 ? 327 VAL B CG1 1 ATOM 6755 C CG2 . VAL B 2 327 ? 39.146 -34.950 51.647 1.00 69.48 ? 327 VAL B CG2 1 ATOM 6756 N N . PHE B 2 328 ? 40.596 -31.731 48.561 1.00 65.55 ? 328 PHE B N 1 ATOM 6757 C CA . PHE B 2 328 ? 41.525 -30.906 47.784 1.00 57.34 ? 328 PHE B CA 1 ATOM 6758 C C . PHE B 2 328 ? 41.082 -29.448 47.718 1.00 58.03 ? 328 PHE B C 1 ATOM 6759 O O . PHE B 2 328 ? 41.898 -28.544 47.810 1.00 50.34 ? 328 PHE B O 1 ATOM 6760 C CB . PHE B 2 328 ? 41.673 -31.426 46.352 1.00 57.55 ? 328 PHE B CB 1 ATOM 6761 C CG . PHE B 2 328 ? 42.155 -32.830 46.265 1.00 57.62 ? 328 PHE B CG 1 ATOM 6762 C CD1 . PHE B 2 328 ? 41.273 -33.859 45.980 1.00 55.01 ? 328 PHE B CD1 1 ATOM 6763 C CD2 . PHE B 2 328 ? 43.488 -33.129 46.469 1.00 54.04 ? 328 PHE B CD2 1 ATOM 6764 C CE1 . PHE B 2 328 ? 41.714 -35.163 45.904 1.00 52.04 ? 328 PHE B CE1 1 ATOM 6765 C CE2 . PHE B 2 328 ? 43.933 -34.434 46.393 1.00 54.31 ? 328 PHE B CE2 1 ATOM 6766 C CZ . PHE B 2 328 ? 43.042 -35.452 46.112 1.00 50.16 ? 328 PHE B CZ 1 ATOM 6767 N N . ALA B 2 329 ? 39.789 -29.217 47.533 1.00 61.12 ? 329 ALA B N 1 ATOM 6768 C CA . ALA B 2 329 ? 39.312 -27.863 47.302 1.00 62.18 ? 329 ALA B CA 1 ATOM 6769 C C . ALA B 2 329 ? 39.641 -26.953 48.479 1.00 68.09 ? 329 ALA B C 1 ATOM 6770 O O . ALA B 2 329 ? 40.071 -25.810 48.293 1.00 71.83 ? 329 ALA B O 1 ATOM 6771 C CB . ALA B 2 329 ? 37.830 -27.872 47.018 1.00 63.95 ? 329 ALA B CB 1 ATOM 6772 N N . GLU B 2 330 ? 39.460 -27.481 49.688 1.00 71.96 ? 330 GLU B N 1 ATOM 6773 C CA . GLU B 2 330 ? 39.728 -26.738 50.921 1.00 70.44 ? 330 GLU B CA 1 ATOM 6774 C C . GLU B 2 330 ? 41.207 -26.721 51.335 1.00 70.21 ? 330 GLU B C 1 ATOM 6775 O O . GLU B 2 330 ? 41.508 -26.489 52.502 1.00 80.33 ? 330 GLU B O 1 ATOM 6776 C CB . GLU B 2 330 ? 38.906 -27.299 52.095 1.00 62.63 ? 330 GLU B CB 1 ATOM 6777 C CG . GLU B 2 330 ? 37.463 -27.689 51.785 1.00 73.11 ? 330 GLU B CG 1 ATOM 6778 C CD . GLU B 2 330 ? 36.651 -27.936 53.053 1.00 76.21 ? 330 GLU B CD 1 ATOM 6779 O OE1 . GLU B 2 330 ? 35.842 -28.897 53.099 1.00 73.72 ? 330 GLU B OE1 1 ATOM 6780 O OE2 . GLU B 2 330 ? 36.828 -27.157 54.012 1.00 63.96 ? 330 GLU B OE2 1 ATOM 6781 N N . MET B 2 331 ? 42.126 -26.975 50.407 1.00 67.59 ? 331 MET B N 1 ATOM 6782 C CA . MET B 2 331 ? 43.555 -26.948 50.736 1.00 71.82 ? 331 MET B CA 1 ATOM 6783 C C . MET B 2 331 ? 44.079 -25.525 50.702 1.00 76.30 ? 331 MET B C 1 ATOM 6784 O O . MET B 2 331 ? 43.686 -24.734 49.839 1.00 83.51 ? 331 MET B O 1 ATOM 6785 C CB . MET B 2 331 ? 44.385 -27.827 49.792 1.00 66.47 ? 331 MET B CB 1 ATOM 6786 C CG . MET B 2 331 ? 44.233 -29.318 50.030 1.00 62.57 ? 331 MET B CG 1 ATOM 6787 S SD . MET B 2 331 ? 45.235 -30.343 48.935 1.00 66.52 ? 331 MET B SD 1 ATOM 6788 C CE . MET B 2 331 ? 45.209 -31.855 49.894 1.00 50.10 ? 331 MET B CE 1 ATOM 6789 N N . ASN B 2 332 ? 44.962 -25.206 51.646 1.00 71.99 ? 332 ASN B N 1 ATOM 6790 C CA . ASN B 2 332 ? 45.499 -23.854 51.776 1.00 69.70 ? 332 ASN B CA 1 ATOM 6791 C C . ASN B 2 332 ? 46.940 -23.723 51.297 1.00 67.74 ? 332 ASN B C 1 ATOM 6792 O O . ASN B 2 332 ? 47.797 -23.173 51.993 1.00 61.91 ? 332 ASN B O 1 ATOM 6793 C CB . ASN B 2 332 ? 45.359 -23.334 53.207 1.00 65.75 ? 332 ASN B CB 1 ATOM 6794 C CG . ASN B 2 332 ? 46.135 -24.166 54.214 1.00 69.99 ? 332 ASN B CG 1 ATOM 6795 O OD1 . ASN B 2 332 ? 46.484 -25.316 53.948 1.00 75.77 ? 332 ASN B OD1 1 ATOM 6796 N ND2 . ASN B 2 332 ? 46.402 -23.586 55.386 1.00 58.74 ? 332 ASN B ND2 1 ATOM 6797 N N . ILE B 2 333 ? 47.186 -24.223 50.092 1.00 63.74 ? 333 ILE B N 1 ATOM 6798 C CA . ILE B 2 333 ? 48.485 -24.109 49.457 1.00 69.77 ? 333 ILE B CA 1 ATOM 6799 C C . ILE B 2 333 ? 48.364 -23.188 48.242 1.00 76.06 ? 333 ILE B C 1 ATOM 6800 O O . ILE B 2 333 ? 47.260 -22.815 47.865 1.00 82.61 ? 333 ILE B O 1 ATOM 6801 C CB . ILE B 2 333 ? 48.986 -25.489 49.043 1.00 67.95 ? 333 ILE B CB 1 ATOM 6802 C CG1 . ILE B 2 333 ? 47.960 -26.165 48.130 1.00 64.38 ? 333 ILE B CG1 1 ATOM 6803 C CG2 . ILE B 2 333 ? 49.235 -26.341 50.277 1.00 62.00 ? 333 ILE B CG2 1 ATOM 6804 C CD1 . ILE B 2 333 ? 48.027 -27.679 48.145 1.00 63.77 ? 333 ILE B CD1 1 ATOM 6805 N N . LYS B 2 334 ? 49.492 -22.811 47.643 1.00 74.75 ? 334 LYS B N 1 ATOM 6806 C CA . LYS B 2 334 ? 49.484 -21.933 46.471 1.00 63.90 ? 334 LYS B CA 1 ATOM 6807 C C . LYS B 2 334 ? 49.283 -22.673 45.151 1.00 70.12 ? 334 LYS B C 1 ATOM 6808 O O . LYS B 2 334 ? 48.656 -22.149 44.235 1.00 72.03 ? 334 LYS B O 1 ATOM 6809 C CB . LYS B 2 334 ? 50.750 -21.068 46.407 1.00 61.07 ? 334 LYS B CB 1 ATOM 6810 C CG . LYS B 2 334 ? 50.629 -19.790 47.241 1.00 78.85 ? 334 LYS B CG 1 ATOM 6811 C CD . LYS B 2 334 ? 51.906 -18.952 47.260 1.00 85.59 ? 334 LYS B CD 1 ATOM 6812 C CE . LYS B 2 334 ? 51.926 -18.046 48.498 1.00 86.83 ? 334 LYS B CE 1 ATOM 6813 N NZ . LYS B 2 334 ? 53.288 -17.533 48.858 1.00 87.44 ? 334 LYS B NZ 1 ATOM 6814 N N . MET B 2 335 ? 49.806 -23.890 45.048 1.00 68.72 ? 335 MET B N 1 ATOM 6815 C CA . MET B 2 335 ? 49.692 -24.632 43.799 1.00 66.42 ? 335 MET B CA 1 ATOM 6816 C C . MET B 2 335 ? 49.129 -26.037 43.955 1.00 68.54 ? 335 MET B C 1 ATOM 6817 O O . MET B 2 335 ? 49.649 -26.838 44.728 1.00 77.11 ? 335 MET B O 1 ATOM 6818 C CB . MET B 2 335 ? 51.045 -24.706 43.110 1.00 69.84 ? 335 MET B CB 1 ATOM 6819 C CG . MET B 2 335 ? 51.756 -23.387 43.025 1.00 70.02 ? 335 MET B CG 1 ATOM 6820 S SD . MET B 2 335 ? 53.472 -23.678 42.611 1.00 75.23 ? 335 MET B SD 1 ATOM 6821 C CE . MET B 2 335 ? 53.262 -24.469 41.009 1.00 74.85 ? 335 MET B CE 1 ATOM 6822 N N . LEU B 2 336 ? 48.066 -26.321 43.203 1.00 65.49 ? 336 LEU B N 1 ATOM 6823 C CA . LEU B 2 336 ? 47.481 -27.653 43.128 1.00 59.37 ? 336 LEU B CA 1 ATOM 6824 C C . LEU B 2 336 ? 47.405 -28.102 41.681 1.00 67.00 ? 336 LEU B C 1 ATOM 6825 O O . LEU B 2 336 ? 46.770 -27.438 40.868 1.00 67.78 ? 336 LEU B O 1 ATOM 6826 C CB . LEU B 2 336 ? 46.075 -27.666 43.716 1.00 53.07 ? 336 LEU B CB 1 ATOM 6827 C CG . LEU B 2 336 ? 45.396 -29.037 43.667 1.00 61.45 ? 336 LEU B CG 1 ATOM 6828 C CD1 . LEU B 2 336 ? 46.213 -30.066 44.429 1.00 60.51 ? 336 LEU B CD1 1 ATOM 6829 C CD2 . LEU B 2 336 ? 43.984 -28.974 44.217 1.00 64.01 ? 336 LEU B CD2 1 ATOM 6830 N N . SER B 2 337 ? 48.067 -29.214 41.369 1.00 63.46 ? 337 SER B N 1 ATOM 6831 C CA . SER B 2 337 ? 47.897 -29.890 40.089 1.00 63.19 ? 337 SER B CA 1 ATOM 6832 C C . SER B 2 337 ? 47.292 -31.278 40.317 1.00 65.12 ? 337 SER B C 1 ATOM 6833 O O . SER B 2 337 ? 47.799 -32.052 41.120 1.00 62.02 ? 337 SER B O 1 ATOM 6834 C CB . SER B 2 337 ? 49.237 -30.036 39.353 1.00 66.13 ? 337 SER B CB 1 ATOM 6835 O OG . SER B 2 337 ? 49.840 -28.790 39.031 1.00 59.02 ? 337 SER B OG 1 ATOM 6836 N N . ILE B 2 338 ? 46.203 -31.589 39.621 1.00 65.71 ? 338 ILE B N 1 ATOM 6837 C CA . ILE B 2 338 ? 45.688 -32.956 39.591 1.00 60.63 ? 338 ILE B CA 1 ATOM 6838 C C . ILE B 2 338 ? 45.401 -33.384 38.164 1.00 59.77 ? 338 ILE B C 1 ATOM 6839 O O . ILE B 2 338 ? 44.436 -32.916 37.577 1.00 57.13 ? 338 ILE B O 1 ATOM 6840 C CB . ILE B 2 338 ? 44.385 -33.096 40.350 1.00 57.87 ? 338 ILE B CB 1 ATOM 6841 C CG1 . ILE B 2 338 ? 44.614 -32.928 41.853 1.00 51.94 ? 338 ILE B CG1 1 ATOM 6842 C CG2 . ILE B 2 338 ? 43.759 -34.453 40.024 1.00 55.32 ? 338 ILE B CG2 1 ATOM 6843 C CD1 . ILE B 2 338 ? 43.332 -32.917 42.664 1.00 47.79 ? 338 ILE B CD1 1 ATOM 6844 N N . SER B 2 339 ? 46.216 -34.290 37.622 1.00 66.51 ? 339 SER B N 1 ATOM 6845 C CA . SER B 2 339 ? 46.184 -34.616 36.187 1.00 62.93 ? 339 SER B CA 1 ATOM 6846 C C . SER B 2 339 ? 46.079 -36.111 35.852 1.00 56.87 ? 339 SER B C 1 ATOM 6847 O O . SER B 2 339 ? 46.524 -36.968 36.610 1.00 57.73 ? 339 SER B O 1 ATOM 6848 C CB . SER B 2 339 ? 47.426 -34.039 35.498 1.00 59.02 ? 339 SER B CB 1 ATOM 6849 O OG . SER B 2 339 ? 47.513 -32.638 35.691 1.00 66.53 ? 339 SER B OG 1 ATOM 6850 N N . ASP B 2 340 ? 45.503 -36.415 34.695 1.00 58.81 ? 340 ASP B N 1 ATOM 6851 C CA . ASP B 2 340 ? 45.390 -37.800 34.237 1.00 60.35 ? 340 ASP B CA 1 ATOM 6852 C C . ASP B 2 340 ? 44.631 -38.697 35.232 1.00 60.87 ? 340 ASP B C 1 ATOM 6853 O O . ASP B 2 340 ? 45.148 -39.708 35.704 1.00 53.24 ? 340 ASP B O 1 ATOM 6854 C CB . ASP B 2 340 ? 46.779 -38.362 33.947 1.00 63.01 ? 340 ASP B CB 1 ATOM 6855 C CG . ASP B 2 340 ? 46.742 -39.712 33.257 1.00 63.05 ? 340 ASP B CG 1 ATOM 6856 O OD1 . ASP B 2 340 ? 45.650 -40.171 32.837 1.00 70.13 ? 340 ASP B OD1 1 ATOM 6857 O OD2 . ASP B 2 340 ? 47.832 -40.312 33.139 1.00 49.95 ? 340 ASP B OD2 1 ATOM 6858 N N . THR B 2 341 ? 43.393 -38.319 35.528 1.00 62.15 ? 341 THR B N 1 ATOM 6859 C CA . THR B 2 341 ? 42.567 -39.032 36.481 1.00 64.27 ? 341 THR B CA 1 ATOM 6860 C C . THR B 2 341 ? 41.185 -39.180 35.878 1.00 64.80 ? 341 THR B C 1 ATOM 6861 O O . THR B 2 341 ? 40.883 -38.546 34.875 1.00 68.07 ? 341 THR B O 1 ATOM 6862 C CB . THR B 2 341 ? 42.394 -38.193 37.729 1.00 76.12 ? 341 THR B CB 1 ATOM 6863 O OG1 . THR B 2 341 ? 41.309 -37.283 37.517 1.00 79.80 ? 341 THR B OG1 1 ATOM 6864 C CG2 . THR B 2 341 ? 43.662 -37.403 38.016 1.00 81.56 ? 341 THR B CG2 1 ATOM 6865 N N . PRO B 2 342 ? 40.324 -39.996 36.504 1.00 61.05 ? 342 PRO B N 1 ATOM 6866 C CA . PRO B 2 342 ? 38.931 -40.123 36.060 1.00 54.63 ? 342 PRO B CA 1 ATOM 6867 C C . PRO B 2 342 ? 38.031 -39.006 36.587 1.00 66.73 ? 342 PRO B C 1 ATOM 6868 O O . PRO B 2 342 ? 36.818 -39.101 36.411 1.00 67.49 ? 342 PRO B O 1 ATOM 6869 C CB . PRO B 2 342 ? 38.471 -41.437 36.697 1.00 44.01 ? 342 PRO B CB 1 ATOM 6870 C CG . PRO B 2 342 ? 39.648 -41.966 37.476 1.00 52.40 ? 342 PRO B CG 1 ATOM 6871 C CD . PRO B 2 342 ? 40.608 -40.856 37.659 1.00 54.05 ? 342 PRO B CD 1 ATOM 6872 N N . PHE B 2 343 ? 38.593 -37.982 37.227 1.00 71.34 ? 343 PHE B N 1 ATOM 6873 C CA . PHE B 2 343 ? 37.763 -36.969 37.881 1.00 78.36 ? 343 PHE B CA 1 ATOM 6874 C C . PHE B 2 343 ? 36.891 -36.204 36.881 1.00 82.29 ? 343 PHE B C 1 ATOM 6875 O O . PHE B 2 343 ? 37.323 -35.911 35.769 1.00 89.16 ? 343 PHE B O 1 ATOM 6876 C CB . PHE B 2 343 ? 38.606 -36.006 38.729 1.00 81.95 ? 343 PHE B CB 1 ATOM 6877 C CG . PHE B 2 343 ? 39.414 -36.686 39.800 1.00 83.52 ? 343 PHE B CG 1 ATOM 6878 C CD1 . PHE B 2 343 ? 39.082 -37.959 40.239 1.00 80.93 ? 343 PHE B CD1 1 ATOM 6879 C CD2 . PHE B 2 343 ? 40.495 -36.045 40.383 1.00 79.78 ? 343 PHE B CD2 1 ATOM 6880 C CE1 . PHE B 2 343 ? 39.830 -38.589 41.224 1.00 70.93 ? 343 PHE B CE1 1 ATOM 6881 C CE2 . PHE B 2 343 ? 41.241 -36.674 41.374 1.00 75.40 ? 343 PHE B CE2 1 ATOM 6882 C CZ . PHE B 2 343 ? 40.908 -37.948 41.789 1.00 65.09 ? 343 PHE B CZ 1 ATOM 6883 N N . ILE B 2 344 ? 35.664 -35.886 37.290 1.00 72.98 ? 344 ILE B N 1 ATOM 6884 C CA . ILE B 2 344 ? 34.687 -35.243 36.415 1.00 58.04 ? 344 ILE B CA 1 ATOM 6885 C C . ILE B 2 344 ? 34.458 -33.774 36.768 1.00 60.08 ? 344 ILE B C 1 ATOM 6886 O O . ILE B 2 344 ? 33.690 -33.074 36.095 1.00 58.80 ? 344 ILE B O 1 ATOM 6887 C CB . ILE B 2 344 ? 33.336 -35.956 36.497 1.00 49.08 ? 344 ILE B CB 1 ATOM 6888 C CG1 . ILE B 2 344 ? 32.841 -35.964 37.937 1.00 54.58 ? 344 ILE B CG1 1 ATOM 6889 C CG2 . ILE B 2 344 ? 33.444 -37.374 35.997 1.00 46.52 ? 344 ILE B CG2 1 ATOM 6890 C CD1 . ILE B 2 344 ? 31.485 -36.621 38.104 1.00 61.16 ? 344 ILE B CD1 1 ATOM 6891 N N . HIS B 2 345 ? 35.134 -33.308 37.816 1.00 62.49 ? 345 HIS B N 1 ATOM 6892 C CA . HIS B 2 345 ? 34.817 -32.018 38.421 1.00 55.11 ? 345 HIS B CA 1 ATOM 6893 C C . HIS B 2 345 ? 35.811 -31.594 39.499 1.00 66.25 ? 345 HIS B C 1 ATOM 6894 O O . HIS B 2 345 ? 36.616 -32.396 39.977 1.00 80.05 ? 345 HIS B O 1 ATOM 6895 C CB . HIS B 2 345 ? 33.421 -32.085 39.046 1.00 43.59 ? 345 HIS B CB 1 ATOM 6896 C CG . HIS B 2 345 ? 32.795 -30.744 39.265 1.00 53.21 ? 345 HIS B CG 1 ATOM 6897 N ND1 . HIS B 2 345 ? 32.299 -29.979 38.232 1.00 61.10 ? 345 HIS B ND1 1 ATOM 6898 C CD2 . HIS B 2 345 ? 32.585 -30.029 40.394 1.00 50.59 ? 345 HIS B CD2 1 ATOM 6899 C CE1 . HIS B 2 345 ? 31.810 -28.853 38.716 1.00 50.71 ? 345 HIS B CE1 1 ATOM 6900 N NE2 . HIS B 2 345 ? 31.976 -28.856 40.025 1.00 46.78 ? 345 HIS B NE2 1 ATOM 6901 N N . MET B 2 346 ? 35.750 -30.321 39.873 1.00 56.92 ? 346 MET B N 1 ATOM 6902 C CA . MET B 2 346 ? 36.407 -29.840 41.083 1.00 58.46 ? 346 MET B CA 1 ATOM 6903 C C . MET B 2 346 ? 35.484 -28.839 41.757 1.00 70.76 ? 346 MET B C 1 ATOM 6904 O O . MET B 2 346 ? 34.894 -27.975 41.100 1.00 81.63 ? 346 MET B O 1 ATOM 6905 C CB . MET B 2 346 ? 37.779 -29.222 40.790 1.00 54.30 ? 346 MET B CB 1 ATOM 6906 C CG . MET B 2 346 ? 38.518 -28.670 42.012 1.00 55.69 ? 346 MET B CG 1 ATOM 6907 S SD . MET B 2 346 ? 38.760 -29.862 43.350 1.00 59.36 ? 346 MET B SD 1 ATOM 6908 C CE . MET B 2 346 ? 39.400 -31.298 42.475 1.00 30.20 ? 346 MET B CE 1 ATOM 6909 N N . VAL B 2 347 ? 35.344 -28.986 43.068 1.00 65.70 ? 347 VAL B N 1 ATOM 6910 C CA . VAL B 2 347 ? 34.463 -28.147 43.866 1.00 60.02 ? 347 VAL B CA 1 ATOM 6911 C C . VAL B 2 347 ? 35.052 -26.749 44.027 1.00 56.51 ? 347 VAL B C 1 ATOM 6912 O O . VAL B 2 347 ? 36.265 -26.582 44.024 1.00 62.45 ? 347 VAL B O 1 ATOM 6913 C CB . VAL B 2 347 ? 34.222 -28.800 45.244 1.00 59.51 ? 347 VAL B CB 1 ATOM 6914 C CG1 . VAL B 2 347 ? 33.787 -27.787 46.257 1.00 67.37 ? 347 VAL B CG1 1 ATOM 6915 C CG2 . VAL B 2 347 ? 33.191 -29.898 45.121 1.00 63.37 ? 347 VAL B CG2 1 ATOM 6916 N N . CYS B 2 348 ? 34.198 -25.740 44.146 1.00 52.37 ? 348 CYS B N 1 ATOM 6917 C CA . CYS B 2 348 ? 34.675 -24.393 44.462 1.00 56.31 ? 348 CYS B CA 1 ATOM 6918 C C . CYS B 2 348 ? 35.037 -24.292 45.967 1.00 65.21 ? 348 CYS B C 1 ATOM 6919 O O . CYS B 2 348 ? 34.284 -24.745 46.840 1.00 64.65 ? 348 CYS B O 1 ATOM 6920 C CB . CYS B 2 348 ? 33.643 -23.337 43.996 1.00 39.27 ? 348 CYS B CB 1 ATOM 6921 S SG . CYS B 2 348 ? 33.884 -21.596 44.481 1.00 143.77 ? 348 CYS B SG 1 ATOM 6922 N N . PRO B 2 349 ? 36.222 -23.742 46.273 1.00 59.58 ? 349 PRO B N 1 ATOM 6923 C CA . PRO B 2 349 ? 36.609 -23.571 47.678 1.00 60.85 ? 349 PRO B CA 1 ATOM 6924 C C . PRO B 2 349 ? 35.484 -22.911 48.498 1.00 70.15 ? 349 PRO B C 1 ATOM 6925 O O . PRO B 2 349 ? 34.867 -21.954 48.017 1.00 66.72 ? 349 PRO B O 1 ATOM 6926 C CB . PRO B 2 349 ? 37.819 -22.638 47.589 1.00 53.14 ? 349 PRO B CB 1 ATOM 6927 C CG . PRO B 2 349 ? 38.363 -22.815 46.192 1.00 43.77 ? 349 PRO B CG 1 ATOM 6928 C CD . PRO B 2 349 ? 37.268 -23.308 45.324 1.00 46.15 ? 349 PRO B CD 1 ATOM 6929 N N . PRO B 2 350 ? 35.229 -23.400 49.728 1.00 75.93 ? 350 PRO B N 1 ATOM 6930 C CA . PRO B 2 350 ? 34.108 -22.902 50.540 1.00 74.12 ? 350 PRO B CA 1 ATOM 6931 C C . PRO B 2 350 ? 34.386 -21.501 51.080 1.00 78.28 ? 350 PRO B C 1 ATOM 6932 O O . PRO B 2 350 ? 33.459 -20.710 51.290 1.00 66.15 ? 350 PRO B O 1 ATOM 6933 C CB . PRO B 2 350 ? 34.028 -23.904 51.709 1.00 62.88 ? 350 PRO B CB 1 ATOM 6934 C CG . PRO B 2 350 ? 35.093 -24.927 51.457 1.00 72.42 ? 350 PRO B CG 1 ATOM 6935 C CD . PRO B 2 350 ? 36.071 -24.334 50.489 1.00 77.88 ? 350 PRO B CD 1 ATOM 6936 N N . SER B 2 351 ? 35.667 -21.224 51.315 1.00 82.67 ? 351 SER B N 1 ATOM 6937 C CA . SER B 2 351 ? 36.138 -19.934 51.804 1.00 78.66 ? 351 SER B CA 1 ATOM 6938 C C . SER B 2 351 ? 37.221 -19.472 50.837 1.00 75.71 ? 351 SER B C 1 ATOM 6939 O O . SER B 2 351 ? 37.797 -20.299 50.128 1.00 73.34 ? 351 SER B O 1 ATOM 6940 C CB . SER B 2 351 ? 36.715 -20.074 53.222 1.00 73.07 ? 351 SER B CB 1 ATOM 6941 O OG . SER B 2 351 ? 35.738 -20.491 54.168 1.00 70.28 ? 351 SER B OG 1 ATOM 6942 N N . PRO B 2 352 ? 37.495 -18.154 50.788 1.00 69.41 ? 352 PRO B N 1 ATOM 6943 C CA . PRO B 2 352 ? 38.549 -17.614 49.918 1.00 69.65 ? 352 PRO B CA 1 ATOM 6944 C C . PRO B 2 352 ? 39.835 -18.423 50.028 1.00 71.68 ? 352 PRO B C 1 ATOM 6945 O O . PRO B 2 352 ? 40.416 -18.464 51.111 1.00 71.03 ? 352 PRO B O 1 ATOM 6946 C CB . PRO B 2 352 ? 38.772 -16.215 50.484 1.00 58.91 ? 352 PRO B CB 1 ATOM 6947 C CG . PRO B 2 352 ? 37.445 -15.828 51.006 1.00 57.42 ? 352 PRO B CG 1 ATOM 6948 C CD . PRO B 2 352 ? 36.763 -17.086 51.488 1.00 55.81 ? 352 PRO B CD 1 ATOM 6949 N N . SER B 2 353 ? 40.270 -19.060 48.944 1.00 61.15 ? 353 SER B N 1 ATOM 6950 C CA . SER B 2 353 ? 41.483 -19.866 49.010 1.00 68.71 ? 353 SER B CA 1 ATOM 6951 C C . SER B 2 353 ? 42.696 -19.038 48.636 1.00 69.85 ? 353 SER B C 1 ATOM 6952 O O . SER B 2 353 ? 42.599 -17.829 48.432 1.00 64.80 ? 353 SER B O 1 ATOM 6953 C CB . SER B 2 353 ? 41.395 -21.104 48.120 1.00 77.34 ? 353 SER B CB 1 ATOM 6954 O OG . SER B 2 353 ? 41.622 -20.756 46.770 1.00 88.83 ? 353 SER B OG 1 ATOM 6955 N N . SER B 2 354 ? 43.844 -19.698 48.558 1.00 76.36 ? 354 SER B N 1 ATOM 6956 C CA . SER B 2 354 ? 45.091 -19.005 48.289 1.00 87.91 ? 354 SER B CA 1 ATOM 6957 C C . SER B 2 354 ? 45.743 -19.628 47.076 1.00 89.21 ? 354 SER B C 1 ATOM 6958 O O . SER B 2 354 ? 46.851 -19.259 46.690 1.00 94.35 ? 354 SER B O 1 ATOM 6959 C CB . SER B 2 354 ? 46.021 -19.052 49.504 1.00 96.89 ? 354 SER B CB 1 ATOM 6960 O OG . SER B 2 354 ? 46.224 -20.383 49.936 1.00 101.14 ? 354 SER B OG 1 ATOM 6961 N N . PHE B 2 355 ? 45.037 -20.580 46.477 1.00 87.70 ? 355 PHE B N 1 ATOM 6962 C CA . PHE B 2 355 ? 45.447 -21.128 45.197 1.00 77.57 ? 355 PHE B CA 1 ATOM 6963 C C . PHE B 2 355 ? 45.778 -19.974 44.282 1.00 74.71 ? 355 PHE B C 1 ATOM 6964 O O . PHE B 2 355 ? 44.967 -19.070 44.096 1.00 84.28 ? 355 PHE B O 1 ATOM 6965 C CB . PHE B 2 355 ? 44.318 -21.934 44.562 1.00 76.41 ? 355 PHE B CB 1 ATOM 6966 C CG . PHE B 2 355 ? 44.037 -23.236 45.246 1.00 70.74 ? 355 PHE B CG 1 ATOM 6967 C CD1 . PHE B 2 355 ? 42.733 -23.641 45.473 1.00 71.48 ? 355 PHE B CD1 1 ATOM 6968 C CD2 . PHE B 2 355 ? 45.074 -24.056 45.653 1.00 69.22 ? 355 PHE B CD2 1 ATOM 6969 C CE1 . PHE B 2 355 ? 42.465 -24.834 46.097 1.00 79.69 ? 355 PHE B CE1 1 ATOM 6970 C CE2 . PHE B 2 355 ? 44.816 -25.258 46.277 1.00 79.40 ? 355 PHE B CE2 1 ATOM 6971 C CZ . PHE B 2 355 ? 43.507 -25.648 46.498 1.00 86.37 ? 355 PHE B CZ 1 ATOM 6972 N N . THR B 2 356 ? 46.975 -19.994 43.722 1.00 70.23 ? 356 THR B N 1 ATOM 6973 C CA . THR B 2 356 ? 47.329 -19.038 42.689 1.00 74.61 ? 356 THR B CA 1 ATOM 6974 C C . THR B 2 356 ? 47.715 -19.786 41.423 1.00 72.70 ? 356 THR B C 1 ATOM 6975 O O . THR B 2 356 ? 47.967 -19.178 40.383 1.00 74.86 ? 356 THR B O 1 ATOM 6976 C CB . THR B 2 356 ? 48.461 -18.097 43.135 1.00 72.38 ? 356 THR B CB 1 ATOM 6977 O OG1 . THR B 2 356 ? 49.677 -18.837 43.297 1.00 64.54 ? 356 THR B OG1 1 ATOM 6978 C CG2 . THR B 2 356 ? 48.089 -17.434 44.448 1.00 75.14 ? 356 THR B CG2 1 ATOM 6979 N N . PHE B 2 357 ? 47.739 -21.113 41.528 1.00 66.38 ? 357 PHE B N 1 ATOM 6980 C CA . PHE B 2 357 ? 48.069 -21.977 40.409 1.00 55.49 ? 357 PHE B CA 1 ATOM 6981 C C . PHE B 2 357 ? 47.234 -23.248 40.419 1.00 61.62 ? 357 PHE B C 1 ATOM 6982 O O . PHE B 2 357 ? 47.206 -23.982 41.399 1.00 65.80 ? 357 PHE B O 1 ATOM 6983 C CB . PHE B 2 357 ? 49.544 -22.326 40.438 1.00 63.43 ? 357 PHE B CB 1 ATOM 6984 C CG . PHE B 2 357 ? 49.961 -23.262 39.352 1.00 70.16 ? 357 PHE B CG 1 ATOM 6985 C CD1 . PHE B 2 357 ? 50.368 -22.774 38.122 1.00 64.00 ? 357 PHE B CD1 1 ATOM 6986 C CD2 . PHE B 2 357 ? 49.959 -24.635 39.564 1.00 72.34 ? 357 PHE B CD2 1 ATOM 6987 C CE1 . PHE B 2 357 ? 50.758 -23.641 37.120 1.00 70.92 ? 357 PHE B CE1 1 ATOM 6988 C CE2 . PHE B 2 357 ? 50.349 -25.507 38.565 1.00 74.11 ? 357 PHE B CE2 1 ATOM 6989 C CZ . PHE B 2 357 ? 50.746 -25.011 37.339 1.00 72.98 ? 357 PHE B CZ 1 ATOM 6990 N N . LEU B 2 358 ? 46.544 -23.497 39.314 1.00 68.79 ? 358 LEU B N 1 ATOM 6991 C CA . LEU B 2 358 ? 45.701 -24.675 39.180 1.00 64.97 ? 358 LEU B CA 1 ATOM 6992 C C . LEU B 2 358 ? 45.937 -25.334 37.826 1.00 73.52 ? 358 LEU B C 1 ATOM 6993 O O . LEU B 2 358 ? 45.906 -24.670 36.794 1.00 83.92 ? 358 LEU B O 1 ATOM 6994 C CB . LEU B 2 358 ? 44.233 -24.296 39.371 1.00 56.65 ? 358 LEU B CB 1 ATOM 6995 C CG . LEU B 2 358 ? 43.875 -23.977 40.824 1.00 58.24 ? 358 LEU B CG 1 ATOM 6996 C CD1 . LEU B 2 358 ? 42.431 -23.564 40.929 1.00 67.17 ? 358 LEU B CD1 1 ATOM 6997 C CD2 . LEU B 2 358 ? 44.162 -25.165 41.740 1.00 47.67 ? 358 LEU B CD2 1 ATOM 6998 N N . ASN B 2 359 ? 46.204 -26.636 37.846 1.00 71.34 ? 359 ASN B N 1 ATOM 6999 C CA . ASN B 2 359 ? 46.532 -27.400 36.649 1.00 66.64 ? 359 ASN B CA 1 ATOM 7000 C C . ASN B 2 359 ? 45.816 -28.735 36.716 1.00 64.97 ? 359 ASN B C 1 ATOM 7001 O O . ASN B 2 359 ? 46.289 -29.666 37.354 1.00 61.56 ? 359 ASN B O 1 ATOM 7002 C CB . ASN B 2 359 ? 48.054 -27.591 36.547 1.00 68.98 ? 359 ASN B CB 1 ATOM 7003 C CG . ASN B 2 359 ? 48.486 -28.464 35.359 1.00 74.55 ? 359 ASN B CG 1 ATOM 7004 O OD1 . ASN B 2 359 ? 47.662 -29.051 34.662 1.00 68.49 ? 359 ASN B OD1 1 ATOM 7005 N ND2 . ASN B 2 359 ? 49.809 -28.551 35.146 1.00 84.65 ? 359 ASN B ND2 1 ATOM 7006 N N . PHE B 2 360 ? 44.653 -28.807 36.077 1.00 65.24 ? 360 PHE B N 1 ATOM 7007 C CA . PHE B 2 360 ? 43.879 -30.041 36.017 1.00 62.24 ? 360 PHE B CA 1 ATOM 7008 C C . PHE B 2 360 ? 43.898 -30.614 34.612 1.00 65.79 ? 360 PHE B C 1 ATOM 7009 O O . PHE B 2 360 ? 42.869 -30.661 33.940 1.00 68.58 ? 360 PHE B O 1 ATOM 7010 C CB . PHE B 2 360 ? 42.441 -29.794 36.465 1.00 58.52 ? 360 PHE B CB 1 ATOM 7011 C CG . PHE B 2 360 ? 42.335 -29.234 37.855 1.00 67.99 ? 360 PHE B CG 1 ATOM 7012 C CD1 . PHE B 2 360 ? 42.046 -27.894 38.060 1.00 68.68 ? 360 PHE B CD1 1 ATOM 7013 C CD2 . PHE B 2 360 ? 42.544 -30.045 38.960 1.00 71.95 ? 360 PHE B CD2 1 ATOM 7014 C CE1 . PHE B 2 360 ? 41.948 -27.380 39.339 1.00 71.77 ? 360 PHE B CE1 1 ATOM 7015 C CE2 . PHE B 2 360 ? 42.449 -29.537 40.243 1.00 74.32 ? 360 PHE B CE2 1 ATOM 7016 C CZ . PHE B 2 360 ? 42.151 -28.202 40.434 1.00 72.09 ? 360 PHE B CZ 1 ATOM 7017 N N . THR B 2 361 ? 45.079 -31.049 34.178 1.00 64.36 ? 361 THR B N 1 ATOM 7018 C CA . THR B 2 361 ? 45.266 -31.571 32.826 1.00 65.09 ? 361 THR B CA 1 ATOM 7019 C C . THR B 2 361 ? 44.729 -32.989 32.666 1.00 61.73 ? 361 THR B C 1 ATOM 7020 O O . THR B 2 361 ? 44.872 -33.831 33.555 1.00 59.70 ? 361 THR B O 1 ATOM 7021 C CB . THR B 2 361 ? 46.758 -31.569 32.404 1.00 64.79 ? 361 THR B CB 1 ATOM 7022 O OG1 . THR B 2 361 ? 47.112 -30.296 31.857 1.00 66.56 ? 361 THR B OG1 1 ATOM 7023 C CG2 . THR B 2 361 ? 47.004 -32.624 31.351 1.00 60.64 ? 361 THR B CG2 1 ATOM 7024 N N . GLN B 2 362 ? 44.109 -33.241 31.522 1.00 56.00 ? 362 GLN B N 1 ATOM 7025 C CA . GLN B 2 362 ? 43.717 -34.587 31.138 1.00 51.68 ? 362 GLN B CA 1 ATOM 7026 C C . GLN B 2 362 ? 42.852 -35.302 32.173 1.00 57.11 ? 362 GLN B C 1 ATOM 7027 O O . GLN B 2 362 ? 43.196 -36.372 32.664 1.00 49.63 ? 362 GLN B O 1 ATOM 7028 C CB . GLN B 2 362 ? 44.950 -35.425 30.815 1.00 53.57 ? 362 GLN B CB 1 ATOM 7029 C CG . GLN B 2 362 ? 44.625 -36.743 30.127 1.00 69.34 ? 362 GLN B CG 1 ATOM 7030 C CD . GLN B 2 362 ? 45.869 -37.475 29.685 1.00 84.39 ? 362 GLN B CD 1 ATOM 7031 O OE1 . GLN B 2 362 ? 46.800 -36.868 29.161 1.00 101.04 ? 362 GLN B OE1 1 ATOM 7032 N NE2 . GLN B 2 362 ? 45.897 -38.784 29.899 1.00 79.81 ? 362 GLN B NE2 1 ATOM 7033 N N . ASN B 2 363 ? 41.717 -34.707 32.498 1.00 59.08 ? 363 ASN B N 1 ATOM 7034 C CA . ASN B 2 363 ? 40.729 -35.394 33.301 1.00 57.96 ? 363 ASN B CA 1 ATOM 7035 C C . ASN B 2 363 ? 39.467 -35.492 32.476 1.00 58.40 ? 363 ASN B C 1 ATOM 7036 O O . ASN B 2 363 ? 39.528 -35.634 31.263 1.00 63.67 ? 363 ASN B O 1 ATOM 7037 C CB . ASN B 2 363 ? 40.464 -34.627 34.593 1.00 61.99 ? 363 ASN B CB 1 ATOM 7038 C CG . ASN B 2 363 ? 41.712 -34.431 35.408 1.00 61.50 ? 363 ASN B CG 1 ATOM 7039 O OD1 . ASN B 2 363 ? 42.058 -33.305 35.758 1.00 72.58 ? 363 ASN B OD1 1 ATOM 7040 N ND2 . ASN B 2 363 ? 42.410 -35.526 35.706 1.00 45.60 ? 363 ASN B ND2 1 ATOM 7041 N N . VAL B 2 364 ? 38.323 -35.396 33.134 1.00 57.75 ? 364 VAL B N 1 ATOM 7042 C CA . VAL B 2 364 ? 37.051 -35.371 32.441 1.00 46.62 ? 364 VAL B CA 1 ATOM 7043 C C . VAL B 2 364 ? 36.193 -34.226 32.995 1.00 48.18 ? 364 VAL B C 1 ATOM 7044 O O . VAL B 2 364 ? 35.001 -34.399 33.252 1.00 55.88 ? 364 VAL B O 1 ATOM 7045 C CB . VAL B 2 364 ? 36.330 -36.734 32.546 1.00 49.56 ? 364 VAL B CB 1 ATOM 7046 C CG1 . VAL B 2 364 ? 35.287 -36.879 31.427 1.00 52.24 ? 364 VAL B CG1 1 ATOM 7047 C CG2 . VAL B 2 364 ? 37.352 -37.883 32.476 1.00 39.45 ? 364 VAL B CG2 1 ATOM 7048 N N . PHE B 2 365 ? 36.818 -33.058 33.175 1.00 44.11 ? 365 PHE B N 1 ATOM 7049 C CA . PHE B 2 365 ? 36.133 -31.853 33.667 1.00 51.01 ? 365 PHE B CA 1 ATOM 7050 C C . PHE B 2 365 ? 35.129 -31.274 32.667 1.00 54.28 ? 365 PHE B C 1 ATOM 7051 O O . PHE B 2 365 ? 35.231 -31.493 31.467 1.00 49.71 ? 365 PHE B O 1 ATOM 7052 C CB . PHE B 2 365 ? 37.144 -30.759 34.020 1.00 50.31 ? 365 PHE B CB 1 ATOM 7053 C CG . PHE B 2 365 ? 37.833 -30.960 35.340 1.00 67.98 ? 365 PHE B CG 1 ATOM 7054 C CD1 . PHE B 2 365 ? 37.882 -32.217 35.935 1.00 64.74 ? 365 PHE B CD1 1 ATOM 7055 C CD2 . PHE B 2 365 ? 38.468 -29.889 35.974 1.00 61.10 ? 365 PHE B CD2 1 ATOM 7056 C CE1 . PHE B 2 365 ? 38.524 -32.393 37.142 1.00 59.51 ? 365 PHE B CE1 1 ATOM 7057 C CE2 . PHE B 2 365 ? 39.121 -30.062 37.176 1.00 46.73 ? 365 PHE B CE2 1 ATOM 7058 C CZ . PHE B 2 365 ? 39.145 -31.311 37.764 1.00 53.00 ? 365 PHE B CZ 1 ATOM 7059 N N . THR B 2 366 ? 34.177 -30.501 33.166 1.00 57.45 ? 366 THR B N 1 ATOM 7060 C CA . THR B 2 366 ? 33.190 -29.886 32.293 1.00 56.53 ? 366 THR B CA 1 ATOM 7061 C C . THR B 2 366 ? 33.184 -28.372 32.444 1.00 67.85 ? 366 THR B C 1 ATOM 7062 O O . THR B 2 366 ? 33.892 -27.820 33.284 1.00 75.41 ? 366 THR B O 1 ATOM 7063 C CB . THR B 2 366 ? 31.781 -30.453 32.548 1.00 54.40 ? 366 THR B CB 1 ATOM 7064 O OG1 . THR B 2 366 ? 31.346 -30.121 33.880 1.00 59.68 ? 366 THR B OG1 1 ATOM 7065 C CG2 . THR B 2 366 ? 31.799 -31.965 32.360 1.00 36.22 ? 366 THR B CG2 1 ATOM 7066 N N . ASP B 2 367 ? 32.392 -27.707 31.614 1.00 75.04 ? 367 ASP B N 1 ATOM 7067 C CA . ASP B 2 367 ? 32.300 -26.252 31.626 1.00 80.25 ? 367 ASP B CA 1 ATOM 7068 C C . ASP B 2 367 ? 31.606 -25.726 32.880 1.00 75.40 ? 367 ASP B C 1 ATOM 7069 O O . ASP B 2 367 ? 31.584 -24.516 33.120 1.00 83.26 ? 367 ASP B O 1 ATOM 7070 C CB . ASP B 2 367 ? 31.585 -25.748 30.364 1.00 88.07 ? 367 ASP B CB 1 ATOM 7071 C CG . ASP B 2 367 ? 30.307 -26.513 30.073 1.00 92.35 ? 367 ASP B CG 1 ATOM 7072 O OD1 . ASP B 2 367 ? 30.157 -27.010 28.934 1.00 93.89 ? 367 ASP B OD1 1 ATOM 7073 O OD2 . ASP B 2 367 ? 29.461 -26.628 30.990 1.00 88.70 ? 367 ASP B OD2 1 ATOM 7074 N N . SER B 2 368 ? 31.041 -26.629 33.677 1.00 65.15 ? 368 SER B N 1 ATOM 7075 C CA . SER B 2 368 ? 30.429 -26.224 34.940 1.00 69.77 ? 368 SER B CA 1 ATOM 7076 C C . SER B 2 368 ? 31.476 -26.072 36.049 1.00 64.77 ? 368 SER B C 1 ATOM 7077 O O . SER B 2 368 ? 31.184 -25.551 37.123 1.00 64.20 ? 368 SER B O 1 ATOM 7078 C CB . SER B 2 368 ? 29.317 -27.186 35.362 1.00 69.83 ? 368 SER B CB 1 ATOM 7079 O OG . SER B 2 368 ? 29.816 -28.493 35.526 1.00 70.37 ? 368 SER B OG 1 ATOM 7080 N N . VAL B 2 369 ? 32.699 -26.512 35.780 1.00 58.60 ? 369 VAL B N 1 ATOM 7081 C CA . VAL B 2 369 ? 33.769 -26.342 36.741 1.00 66.94 ? 369 VAL B CA 1 ATOM 7082 C C . VAL B 2 369 ? 33.873 -24.871 37.133 1.00 72.48 ? 369 VAL B C 1 ATOM 7083 O O . VAL B 2 369 ? 33.884 -23.988 36.265 1.00 64.82 ? 369 VAL B O 1 ATOM 7084 C CB . VAL B 2 369 ? 35.124 -26.861 36.209 1.00 70.10 ? 369 VAL B CB 1 ATOM 7085 C CG1 . VAL B 2 369 ? 35.796 -25.821 35.329 1.00 70.53 ? 369 VAL B CG1 1 ATOM 7086 C CG2 . VAL B 2 369 ? 36.036 -27.251 37.374 1.00 65.12 ? 369 VAL B CG2 1 ATOM 7087 N N . PHE B 2 370 ? 33.925 -24.630 38.446 1.00 67.85 ? 370 PHE B N 1 ATOM 7088 C CA . PHE B 2 370 ? 34.044 -23.291 39.013 1.00 69.85 ? 370 PHE B CA 1 ATOM 7089 C C . PHE B 2 370 ? 32.984 -22.278 38.523 1.00 70.96 ? 370 PHE B C 1 ATOM 7090 O O . PHE B 2 370 ? 33.254 -21.074 38.444 1.00 63.78 ? 370 PHE B O 1 ATOM 7091 C CB . PHE B 2 370 ? 35.454 -22.729 38.789 1.00 66.23 ? 370 PHE B CB 1 ATOM 7092 C CG . PHE B 2 370 ? 36.548 -23.603 39.313 1.00 66.57 ? 370 PHE B CG 1 ATOM 7093 C CD1 . PHE B 2 370 ? 37.762 -23.676 38.656 1.00 68.49 ? 370 PHE B CD1 1 ATOM 7094 C CD2 . PHE B 2 370 ? 36.368 -24.351 40.459 1.00 73.76 ? 370 PHE B CD2 1 ATOM 7095 C CE1 . PHE B 2 370 ? 38.785 -24.481 39.134 1.00 69.47 ? 370 PHE B CE1 1 ATOM 7096 C CE2 . PHE B 2 370 ? 37.389 -25.158 40.948 1.00 72.68 ? 370 PHE B CE2 1 ATOM 7097 C CZ . PHE B 2 370 ? 38.596 -25.225 40.282 1.00 68.14 ? 370 PHE B CZ 1 ATOM 7098 N N . GLN B 2 371 ? 31.781 -22.746 38.208 1.00 65.39 ? 371 GLN B N 1 ATOM 7099 C CA . GLN B 2 371 ? 30.742 -21.815 37.789 1.00 73.45 ? 371 GLN B CA 1 ATOM 7100 C C . GLN B 2 371 ? 30.436 -20.840 38.906 1.00 74.53 ? 371 GLN B C 1 ATOM 7101 O O . GLN B 2 371 ? 30.158 -21.247 40.032 1.00 73.68 ? 371 GLN B O 1 ATOM 7102 C CB . GLN B 2 371 ? 29.471 -22.531 37.322 1.00 90.75 ? 371 GLN B CB 1 ATOM 7103 C CG . GLN B 2 371 ? 29.423 -22.768 35.810 1.00 107.15 ? 371 GLN B CG 1 ATOM 7104 C CD . GLN B 2 371 ? 30.018 -21.610 35.005 1.00 109.52 ? 371 GLN B CD 1 ATOM 7105 O OE1 . GLN B 2 371 ? 29.461 -20.506 34.962 1.00 107.42 ? 371 GLN B OE1 1 ATOM 7106 N NE2 . GLN B 2 371 ? 31.153 -21.866 34.359 1.00 101.25 ? 371 GLN B NE2 1 ATOM 7107 N N . GLY B 2 372 ? 30.502 -19.550 38.584 1.00 81.85 ? 372 GLY B N 1 ATOM 7108 C CA . GLY B 2 372 ? 30.247 -18.499 39.551 1.00 79.79 ? 372 GLY B CA 1 ATOM 7109 C C . GLY B 2 372 ? 31.018 -18.686 40.842 1.00 85.45 ? 372 GLY B C 1 ATOM 7110 O O . GLY B 2 372 ? 30.491 -18.468 41.932 1.00 87.34 ? 372 GLY B O 1 ATOM 7111 N N . CYS B 2 373 ? 32.275 -19.098 40.723 1.00 94.71 ? 373 CYS B N 1 ATOM 7112 C CA . CYS B 2 373 ? 33.107 -19.309 41.896 1.00 98.25 ? 373 CYS B CA 1 ATOM 7113 C C . CYS B 2 373 ? 33.849 -18.027 42.236 1.00 96.34 ? 373 CYS B C 1 ATOM 7114 O O . CYS B 2 373 ? 34.686 -17.551 41.463 1.00 94.65 ? 373 CYS B O 1 ATOM 7115 C CB . CYS B 2 373 ? 34.077 -20.463 41.668 1.00 98.40 ? 373 CYS B CB 1 ATOM 7116 S SG . CYS B 2 373 ? 35.134 -20.820 43.078 1.00 105.75 ? 373 CYS B SG 1 ATOM 7117 N N . SER B 2 374 ? 33.523 -17.472 43.400 1.00 96.38 ? 374 SER B N 1 ATOM 7118 C CA . SER B 2 374 ? 34.007 -16.153 43.800 1.00 102.50 ? 374 SER B CA 1 ATOM 7119 C C . SER B 2 374 ? 35.091 -16.272 44.856 1.00 95.49 ? 374 SER B C 1 ATOM 7120 O O . SER B 2 374 ? 35.291 -15.383 45.675 1.00 95.33 ? 374 SER B O 1 ATOM 7121 C CB . SER B 2 374 ? 32.844 -15.314 44.336 1.00 109.34 ? 374 SER B CB 1 ATOM 7122 O OG . SER B 2 374 ? 31.986 -16.092 45.156 1.00 114.08 ? 374 SER B OG 1 ATOM 7123 N N . THR B 2 375 ? 35.816 -17.373 44.810 1.00 89.83 ? 375 THR B N 1 ATOM 7124 C CA . THR B 2 375 ? 36.631 -17.771 45.932 1.00 76.45 ? 375 THR B CA 1 ATOM 7125 C C . THR B 2 375 ? 38.003 -18.225 45.403 1.00 83.73 ? 375 THR B C 1 ATOM 7126 O O . THR B 2 375 ? 38.774 -18.911 46.075 1.00 73.53 ? 375 THR B O 1 ATOM 7127 C CB . THR B 2 375 ? 35.865 -18.862 46.704 1.00 63.57 ? 375 THR B CB 1 ATOM 7128 O OG1 . THR B 2 375 ? 35.963 -18.635 48.110 1.00 69.55 ? 375 THR B OG1 1 ATOM 7129 C CG2 . THR B 2 375 ? 36.336 -20.253 46.336 1.00 42.29 ? 375 THR B CG2 1 ATOM 7130 N N . LEU B 2 376 ? 38.287 -17.816 44.170 1.00 89.52 ? 376 LEU B N 1 ATOM 7131 C CA . LEU B 2 376 ? 39.582 -18.036 43.545 1.00 84.30 ? 376 LEU B CA 1 ATOM 7132 C C . LEU B 2 376 ? 40.129 -16.696 43.048 1.00 84.58 ? 376 LEU B C 1 ATOM 7133 O O . LEU B 2 376 ? 40.690 -16.593 41.955 1.00 84.44 ? 376 LEU B O 1 ATOM 7134 C CB . LEU B 2 376 ? 39.459 -19.038 42.392 1.00 81.41 ? 376 LEU B CB 1 ATOM 7135 C CG . LEU B 2 376 ? 39.104 -20.488 42.755 1.00 81.11 ? 376 LEU B CG 1 ATOM 7136 C CD1 . LEU B 2 376 ? 38.707 -21.266 41.518 1.00 74.38 ? 376 LEU B CD1 1 ATOM 7137 C CD2 . LEU B 2 376 ? 40.242 -21.201 43.494 1.00 80.28 ? 376 LEU B CD2 1 ATOM 7138 N N . LYS B 2 377 ? 39.958 -15.666 43.867 1.00 84.67 ? 377 LYS B N 1 ATOM 7139 C CA . LYS B 2 377 ? 40.359 -14.322 43.484 1.00 77.74 ? 377 LYS B CA 1 ATOM 7140 C C . LYS B 2 377 ? 41.870 -14.127 43.538 1.00 78.61 ? 377 LYS B C 1 ATOM 7141 O O . LYS B 2 377 ? 42.377 -13.083 43.148 1.00 73.27 ? 377 LYS B O 1 ATOM 7142 C CB . LYS B 2 377 ? 39.660 -13.282 44.358 1.00 70.52 ? 377 LYS B CB 1 ATOM 7143 C CG . LYS B 2 377 ? 38.192 -13.057 44.040 1.00 75.33 ? 377 LYS B CG 1 ATOM 7144 C CD . LYS B 2 377 ? 37.593 -12.065 45.027 1.00 88.38 ? 377 LYS B CD 1 ATOM 7145 C CE . LYS B 2 377 ? 36.100 -11.887 44.835 1.00 93.25 ? 377 LYS B CE 1 ATOM 7146 N NZ . LYS B 2 377 ? 35.804 -11.084 43.630 1.00 102.87 ? 377 LYS B NZ 1 ATOM 7147 N N . ARG B 2 378 ? 42.596 -15.125 44.027 1.00 85.72 ? 378 ARG B N 1 ATOM 7148 C CA . ARG B 2 378 ? 44.054 -15.038 44.020 1.00 83.32 ? 378 ARG B CA 1 ATOM 7149 C C . ARG B 2 378 ? 44.616 -15.822 42.837 1.00 76.48 ? 378 ARG B C 1 ATOM 7150 O O . ARG B 2 378 ? 45.737 -15.561 42.391 1.00 80.32 ? 378 ARG B O 1 ATOM 7151 C CB . ARG B 2 378 ? 44.668 -15.497 45.358 1.00 65.05 ? 378 ARG B CB 1 ATOM 7152 C CG . ARG B 2 378 ? 44.637 -14.438 46.455 1.00 67.92 ? 378 ARG B CG 1 ATOM 7153 C CD . ARG B 2 378 ? 45.036 -15.021 47.813 1.00 96.34 ? 378 ARG B CD 1 ATOM 7154 N NE . ARG B 2 378 ? 45.273 -14.011 48.853 1.00 112.01 ? 378 ARG B NE 1 ATOM 7155 C CZ . ARG B 2 378 ? 45.709 -14.283 50.085 1.00 114.53 ? 378 ARG B CZ 1 ATOM 7156 N NH1 . ARG B 2 378 ? 45.960 -15.539 50.451 1.00 109.41 ? 378 ARG B NH1 1 ATOM 7157 N NH2 . ARG B 2 378 ? 45.899 -13.295 50.954 1.00 110.75 ? 378 ARG B NH2 1 ATOM 7158 N N . LEU B 2 379 ? 43.814 -16.756 42.325 1.00 62.30 ? 379 LEU B N 1 ATOM 7159 C CA . LEU B 2 379 ? 44.192 -17.621 41.195 1.00 69.30 ? 379 LEU B CA 1 ATOM 7160 C C . LEU B 2 379 ? 44.687 -16.874 39.963 1.00 71.00 ? 379 LEU B C 1 ATOM 7161 O O . LEU B 2 379 ? 43.940 -16.105 39.356 1.00 78.92 ? 379 LEU B O 1 ATOM 7162 C CB . LEU B 2 379 ? 43.012 -18.507 40.786 1.00 63.96 ? 379 LEU B CB 1 ATOM 7163 C CG . LEU B 2 379 ? 43.277 -19.496 39.659 1.00 60.19 ? 379 LEU B CG 1 ATOM 7164 C CD1 . LEU B 2 379 ? 44.513 -20.299 39.961 1.00 62.80 ? 379 LEU B CD1 1 ATOM 7165 C CD2 . LEU B 2 379 ? 42.080 -20.402 39.484 1.00 64.39 ? 379 LEU B CD2 1 ATOM 7166 N N . GLN B 2 380 ? 45.936 -17.133 39.583 1.00 61.72 ? 380 GLN B N 1 ATOM 7167 C CA . GLN B 2 380 ? 46.579 -16.411 38.489 1.00 60.71 ? 380 GLN B CA 1 ATOM 7168 C C . GLN B 2 380 ? 46.623 -17.229 37.213 1.00 70.13 ? 380 GLN B C 1 ATOM 7169 O O . GLN B 2 380 ? 46.413 -16.711 36.118 1.00 74.76 ? 380 GLN B O 1 ATOM 7170 C CB . GLN B 2 380 ? 48.009 -16.054 38.860 1.00 57.98 ? 380 GLN B CB 1 ATOM 7171 C CG . GLN B 2 380 ? 48.137 -15.224 40.095 1.00 81.42 ? 380 GLN B CG 1 ATOM 7172 C CD . GLN B 2 380 ? 49.474 -14.537 40.168 1.00 83.93 ? 380 GLN B CD 1 ATOM 7173 O OE1 . GLN B 2 380 ? 50.336 -14.741 39.304 1.00 74.12 ? 380 GLN B OE1 1 ATOM 7174 N NE2 . GLN B 2 380 ? 49.658 -13.706 41.195 1.00 78.64 ? 380 GLN B NE2 1 ATOM 7175 N N . THR B 2 381 ? 46.929 -18.510 37.359 1.00 67.23 ? 381 THR B N 1 ATOM 7176 C CA . THR B 2 381 ? 47.054 -19.382 36.212 1.00 63.89 ? 381 THR B CA 1 ATOM 7177 C C . THR B 2 381 ? 46.198 -20.612 36.426 1.00 67.20 ? 381 THR B C 1 ATOM 7178 O O . THR B 2 381 ? 46.371 -21.342 37.391 1.00 80.51 ? 381 THR B O 1 ATOM 7179 C CB . THR B 2 381 ? 48.513 -19.796 35.997 1.00 66.00 ? 381 THR B CB 1 ATOM 7180 O OG1 . THR B 2 381 ? 49.330 -18.622 35.879 1.00 62.71 ? 381 THR B OG1 1 ATOM 7181 C CG2 . THR B 2 381 ? 48.641 -20.651 34.739 1.00 63.65 ? 381 THR B CG2 1 ATOM 7182 N N . LEU B 2 382 ? 45.255 -20.828 35.528 1.00 66.25 ? 382 LEU B N 1 ATOM 7183 C CA . LEU B 2 382 ? 44.407 -22.003 35.593 1.00 71.18 ? 382 LEU B CA 1 ATOM 7184 C C . LEU B 2 382 ? 44.574 -22.802 34.303 1.00 69.64 ? 382 LEU B C 1 ATOM 7185 O O . LEU B 2 382 ? 44.596 -22.236 33.216 1.00 64.60 ? 382 LEU B O 1 ATOM 7186 C CB . LEU B 2 382 ? 42.948 -21.594 35.807 1.00 74.92 ? 382 LEU B CB 1 ATOM 7187 C CG . LEU B 2 382 ? 41.892 -22.675 35.583 1.00 73.98 ? 382 LEU B CG 1 ATOM 7188 C CD1 . LEU B 2 382 ? 41.799 -23.596 36.783 1.00 68.69 ? 382 LEU B CD1 1 ATOM 7189 C CD2 . LEU B 2 382 ? 40.561 -22.014 35.308 1.00 80.89 ? 382 LEU B CD2 1 ATOM 7190 N N . ILE B 2 383 ? 44.706 -24.117 34.433 1.00 74.23 ? 383 ILE B N 1 ATOM 7191 C CA . ILE B 2 383 ? 44.960 -24.985 33.290 1.00 65.83 ? 383 ILE B CA 1 ATOM 7192 C C . ILE B 2 383 ? 43.954 -26.129 33.241 1.00 69.04 ? 383 ILE B C 1 ATOM 7193 O O . ILE B 2 383 ? 43.899 -26.964 34.142 1.00 69.69 ? 383 ILE B O 1 ATOM 7194 C CB . ILE B 2 383 ? 46.394 -25.552 33.330 1.00 57.11 ? 383 ILE B CB 1 ATOM 7195 C CG1 . ILE B 2 383 ? 47.404 -24.414 33.475 1.00 59.40 ? 383 ILE B CG1 1 ATOM 7196 C CG2 . ILE B 2 383 ? 46.684 -26.357 32.084 1.00 58.19 ? 383 ILE B CG2 1 ATOM 7197 C CD1 . ILE B 2 383 ? 48.821 -24.853 33.330 1.00 62.85 ? 383 ILE B CD1 1 ATOM 7198 N N . LEU B 2 384 ? 43.164 -26.159 32.177 1.00 68.34 ? 384 LEU B N 1 ATOM 7199 C CA . LEU B 2 384 ? 42.122 -27.161 32.009 1.00 62.43 ? 384 LEU B CA 1 ATOM 7200 C C . LEU B 2 384 ? 42.313 -27.972 30.711 1.00 67.08 ? 384 LEU B C 1 ATOM 7201 O O . LEU B 2 384 ? 41.385 -28.604 30.200 1.00 71.18 ? 384 LEU B O 1 ATOM 7202 C CB . LEU B 2 384 ? 40.754 -26.474 32.077 1.00 52.47 ? 384 LEU B CB 1 ATOM 7203 C CG . LEU B 2 384 ? 40.484 -25.943 33.495 1.00 57.24 ? 384 LEU B CG 1 ATOM 7204 C CD1 . LEU B 2 384 ? 39.497 -24.805 33.508 1.00 60.69 ? 384 LEU B CD1 1 ATOM 7205 C CD2 . LEU B 2 384 ? 39.997 -27.059 34.422 1.00 60.08 ? 384 LEU B CD2 1 ATOM 7206 N N . GLN B 2 385 ? 43.539 -27.960 30.198 1.00 56.27 ? 385 GLN B N 1 ATOM 7207 C CA . GLN B 2 385 ? 43.880 -28.674 28.974 1.00 55.04 ? 385 GLN B CA 1 ATOM 7208 C C . GLN B 2 385 ? 43.563 -30.170 28.996 1.00 56.58 ? 385 GLN B C 1 ATOM 7209 O O . GLN B 2 385 ? 43.900 -30.880 29.933 1.00 69.10 ? 385 GLN B O 1 ATOM 7210 C CB . GLN B 2 385 ? 45.357 -28.473 28.654 1.00 52.46 ? 385 GLN B CB 1 ATOM 7211 C CG . GLN B 2 385 ? 45.960 -29.595 27.851 1.00 57.19 ? 385 GLN B CG 1 ATOM 7212 C CD . GLN B 2 385 ? 47.296 -29.208 27.255 1.00 70.43 ? 385 GLN B CD 1 ATOM 7213 O OE1 . GLN B 2 385 ? 47.927 -29.995 26.539 1.00 77.97 ? 385 GLN B OE1 1 ATOM 7214 N NE2 . GLN B 2 385 ? 47.734 -27.980 27.539 1.00 56.30 ? 385 GLN B NE2 1 ATOM 7215 N N . ARG B 2 386 ? 42.925 -30.639 27.937 1.00 61.86 ? 386 ARG B N 1 ATOM 7216 C CA . ARG B 2 386 ? 42.608 -32.058 27.761 1.00 69.50 ? 386 ARG B CA 1 ATOM 7217 C C . ARG B 2 386 ? 41.447 -32.535 28.629 1.00 69.60 ? 386 ARG B C 1 ATOM 7218 O O . ARG B 2 386 ? 41.536 -33.564 29.294 1.00 66.15 ? 386 ARG B O 1 ATOM 7219 C CB . ARG B 2 386 ? 43.847 -32.945 27.940 1.00 65.85 ? 386 ARG B CB 1 ATOM 7220 C CG . ARG B 2 386 ? 44.392 -33.534 26.640 1.00 63.50 ? 386 ARG B CG 1 ATOM 7221 C CD . ARG B 2 386 ? 45.798 -34.066 26.813 1.00 68.89 ? 386 ARG B CD 1 ATOM 7222 N NE . ARG B 2 386 ? 46.721 -32.984 27.145 1.00 91.44 ? 386 ARG B NE 1 ATOM 7223 C CZ . ARG B 2 386 ? 47.810 -33.130 27.897 1.00 108.05 ? 386 ARG B CZ 1 ATOM 7224 N NH1 . ARG B 2 386 ? 48.111 -34.320 28.404 1.00 104.45 ? 386 ARG B NH1 1 ATOM 7225 N NH2 . ARG B 2 386 ? 48.595 -32.087 28.154 1.00 113.83 ? 386 ARG B NH2 1 ATOM 7226 N N . ASN B 2 387 ? 40.353 -31.780 28.597 1.00 69.79 ? 387 ASN B N 1 ATOM 7227 C CA . ASN B 2 387 ? 39.127 -32.157 29.291 1.00 67.73 ? 387 ASN B CA 1 ATOM 7228 C C . ASN B 2 387 ? 37.898 -32.116 28.374 1.00 66.99 ? 387 ASN B C 1 ATOM 7229 O O . ASN B 2 387 ? 38.031 -32.174 27.149 1.00 75.49 ? 387 ASN B O 1 ATOM 7230 C CB . ASN B 2 387 ? 38.937 -31.281 30.529 1.00 69.52 ? 387 ASN B CB 1 ATOM 7231 C CG . ASN B 2 387 ? 39.982 -31.557 31.599 1.00 73.32 ? 387 ASN B CG 1 ATOM 7232 O OD1 . ASN B 2 387 ? 40.998 -30.860 31.694 1.00 74.77 ? 387 ASN B OD1 1 ATOM 7233 N ND2 . ASN B 2 387 ? 39.746 -32.590 32.396 1.00 66.73 ? 387 ASN B ND2 1 ATOM 7234 N N . GLY B 2 388 ? 36.708 -32.017 28.960 1.00 57.77 ? 388 GLY B N 1 ATOM 7235 C CA . GLY B 2 388 ? 35.482 -32.031 28.179 1.00 46.82 ? 388 GLY B CA 1 ATOM 7236 C C . GLY B 2 388 ? 34.703 -30.730 28.169 1.00 53.49 ? 388 GLY B C 1 ATOM 7237 O O . GLY B 2 388 ? 33.478 -30.755 28.122 1.00 67.21 ? 388 GLY B O 1 ATOM 7238 N N . LEU B 2 389 ? 35.389 -29.589 28.213 1.00 54.28 ? 389 LEU B N 1 ATOM 7239 C CA . LEU B 2 389 ? 34.695 -28.299 28.242 1.00 64.60 ? 389 LEU B CA 1 ATOM 7240 C C . LEU B 2 389 ? 33.937 -28.037 26.947 1.00 70.25 ? 389 LEU B C 1 ATOM 7241 O O . LEU B 2 389 ? 34.547 -27.912 25.889 1.00 75.85 ? 389 LEU B O 1 ATOM 7242 C CB . LEU B 2 389 ? 35.673 -27.149 28.487 1.00 64.49 ? 389 LEU B CB 1 ATOM 7243 C CG . LEU B 2 389 ? 36.492 -27.138 29.769 1.00 62.86 ? 389 LEU B CG 1 ATOM 7244 C CD1 . LEU B 2 389 ? 36.990 -25.729 30.070 1.00 61.06 ? 389 LEU B CD1 1 ATOM 7245 C CD2 . LEU B 2 389 ? 35.646 -27.654 30.890 1.00 65.13 ? 389 LEU B CD2 1 ATOM 7246 N N . LYS B 2 390 ? 32.613 -27.927 27.026 1.00 74.45 ? 390 LYS B N 1 ATOM 7247 C CA . LYS B 2 390 ? 31.795 -27.796 25.813 1.00 74.10 ? 390 LYS B CA 1 ATOM 7248 C C . LYS B 2 390 ? 31.590 -26.345 25.373 1.00 66.73 ? 390 LYS B C 1 ATOM 7249 O O . LYS B 2 390 ? 32.015 -25.951 24.289 1.00 69.03 ? 390 LYS B O 1 ATOM 7250 C CB . LYS B 2 390 ? 30.425 -28.452 26.015 1.00 72.73 ? 390 LYS B CB 1 ATOM 7251 C CG . LYS B 2 390 ? 30.010 -29.450 24.940 1.00 65.16 ? 390 LYS B CG 1 ATOM 7252 C CD . LYS B 2 390 ? 30.433 -30.872 25.323 1.00 67.45 ? 390 LYS B CD 1 ATOM 7253 C CE . LYS B 2 390 ? 29.535 -31.904 24.668 1.00 80.85 ? 390 LYS B CE 1 ATOM 7254 N NZ . LYS B 2 390 ? 29.421 -31.708 23.177 1.00 79.42 ? 390 LYS B NZ 1 ATOM 7255 N N . ASN B 2 391 ? 30.942 -25.559 26.229 1.00 49.43 ? 391 ASN B N 1 ATOM 7256 C CA . ASN B 2 391 ? 30.422 -24.254 25.853 1.00 49.66 ? 391 ASN B CA 1 ATOM 7257 C C . ASN B 2 391 ? 31.342 -23.050 26.086 1.00 67.27 ? 391 ASN B C 1 ATOM 7258 O O . ASN B 2 391 ? 31.331 -22.449 27.155 1.00 77.58 ? 391 ASN B O 1 ATOM 7259 C CB . ASN B 2 391 ? 29.078 -24.027 26.551 1.00 53.49 ? 391 ASN B CB 1 ATOM 7260 C CG . ASN B 2 391 ? 28.416 -22.724 26.138 1.00 66.38 ? 391 ASN B CG 1 ATOM 7261 O OD1 . ASN B 2 391 ? 27.284 -22.448 26.515 1.00 66.55 ? 391 ASN B OD1 1 ATOM 7262 N ND2 . ASN B 2 391 ? 29.116 -21.924 25.350 1.00 83.67 ? 391 ASN B ND2 1 ATOM 7263 N N . PHE B 2 392 ? 32.090 -22.668 25.057 1.00 76.24 ? 392 PHE B N 1 ATOM 7264 C CA . PHE B 2 392 ? 32.986 -21.509 25.115 1.00 77.46 ? 392 PHE B CA 1 ATOM 7265 C C . PHE B 2 392 ? 32.470 -20.302 25.911 1.00 77.11 ? 392 PHE B C 1 ATOM 7266 O O . PHE B 2 392 ? 33.253 -19.562 26.497 1.00 78.39 ? 392 PHE B O 1 ATOM 7267 C CB . PHE B 2 392 ? 33.363 -21.068 23.700 1.00 66.78 ? 392 PHE B CB 1 ATOM 7268 C CG . PHE B 2 392 ? 34.144 -19.785 23.643 1.00 68.84 ? 392 PHE B CG 1 ATOM 7269 C CD1 . PHE B 2 392 ? 35.530 -19.799 23.690 1.00 71.31 ? 392 PHE B CD1 1 ATOM 7270 C CD2 . PHE B 2 392 ? 33.493 -18.562 23.520 1.00 73.32 ? 392 PHE B CD2 1 ATOM 7271 C CE1 . PHE B 2 392 ? 36.254 -18.615 23.623 1.00 79.22 ? 392 PHE B CE1 1 ATOM 7272 C CE2 . PHE B 2 392 ? 34.209 -17.379 23.455 1.00 77.27 ? 392 PHE B CE2 1 ATOM 7273 C CZ . PHE B 2 392 ? 35.589 -17.404 23.504 1.00 79.41 ? 392 PHE B CZ 1 ATOM 7274 N N . PHE B 2 393 ? 31.164 -20.086 25.927 1.00 79.26 ? 393 PHE B N 1 ATOM 7275 C CA . PHE B 2 393 ? 30.632 -18.917 26.616 1.00 94.11 ? 393 PHE B CA 1 ATOM 7276 C C . PHE B 2 393 ? 30.408 -19.181 28.103 1.00 87.84 ? 393 PHE B C 1 ATOM 7277 O O . PHE B 2 393 ? 30.421 -18.251 28.920 1.00 81.51 ? 393 PHE B O 1 ATOM 7278 C CB . PHE B 2 393 ? 29.357 -18.408 25.937 1.00 107.41 ? 393 PHE B CB 1 ATOM 7279 C CG . PHE B 2 393 ? 29.581 -17.888 24.542 1.00 105.97 ? 393 PHE B CG 1 ATOM 7280 C CD1 . PHE B 2 393 ? 28.963 -18.485 23.460 1.00 98.08 ? 393 PHE B CD1 1 ATOM 7281 C CD2 . PHE B 2 393 ? 30.419 -16.808 24.318 1.00 107.66 ? 393 PHE B CD2 1 ATOM 7282 C CE1 . PHE B 2 393 ? 29.170 -18.015 22.186 1.00 99.53 ? 393 PHE B CE1 1 ATOM 7283 C CE2 . PHE B 2 393 ? 30.627 -16.333 23.041 1.00 106.05 ? 393 PHE B CE2 1 ATOM 7284 C CZ . PHE B 2 393 ? 30.001 -16.937 21.975 1.00 101.30 ? 393 PHE B CZ 1 ATOM 7285 N N . LYS B 2 394 ? 30.210 -20.450 28.451 1.00 80.43 ? 394 LYS B N 1 ATOM 7286 C CA . LYS B 2 394 ? 30.167 -20.838 29.854 1.00 76.43 ? 394 LYS B CA 1 ATOM 7287 C C . LYS B 2 394 ? 31.582 -20.704 30.434 1.00 68.55 ? 394 LYS B C 1 ATOM 7288 O O . LYS B 2 394 ? 31.760 -20.249 31.558 1.00 74.86 ? 394 LYS B O 1 ATOM 7289 C CB . LYS B 2 394 ? 29.605 -22.256 30.024 1.00 69.27 ? 394 LYS B CB 1 ATOM 7290 C CG . LYS B 2 394 ? 28.622 -22.398 31.187 1.00 73.11 ? 394 LYS B CG 1 ATOM 7291 C CD . LYS B 2 394 ? 28.317 -23.860 31.506 1.00 77.74 ? 394 LYS B CD 1 ATOM 7292 C CE . LYS B 2 394 ? 27.467 -24.015 32.777 1.00 84.86 ? 394 LYS B CE 1 ATOM 7293 N NZ . LYS B 2 394 ? 26.003 -23.763 32.567 1.00 87.13 ? 394 LYS B NZ 1 ATOM 7294 N N . VAL B 2 395 ? 32.580 -21.069 29.635 1.00 61.25 ? 395 VAL B N 1 ATOM 7295 C CA . VAL B 2 395 ? 33.993 -20.933 29.999 1.00 68.33 ? 395 VAL B CA 1 ATOM 7296 C C . VAL B 2 395 ? 34.421 -19.470 30.210 1.00 71.17 ? 395 VAL B C 1 ATOM 7297 O O . VAL B 2 395 ? 35.464 -19.190 30.801 1.00 74.97 ? 395 VAL B O 1 ATOM 7298 C CB . VAL B 2 395 ? 34.919 -21.596 28.926 1.00 63.42 ? 395 VAL B CB 1 ATOM 7299 C CG1 . VAL B 2 395 ? 36.396 -21.499 29.317 1.00 50.64 ? 395 VAL B CG1 1 ATOM 7300 C CG2 . VAL B 2 395 ? 34.523 -23.050 28.686 1.00 59.01 ? 395 VAL B CG2 1 ATOM 7301 N N . ALA B 2 396 ? 33.621 -18.534 29.721 1.00 73.83 ? 396 ALA B N 1 ATOM 7302 C CA . ALA B 2 396 ? 33.925 -17.124 29.923 1.00 75.54 ? 396 ALA B CA 1 ATOM 7303 C C . ALA B 2 396 ? 33.306 -16.686 31.231 1.00 83.09 ? 396 ALA B C 1 ATOM 7304 O O . ALA B 2 396 ? 33.895 -15.906 31.974 1.00 92.53 ? 396 ALA B O 1 ATOM 7305 C CB . ALA B 2 396 ? 33.383 -16.284 28.771 1.00 75.70 ? 396 ALA B CB 1 ATOM 7306 N N . LEU B 2 397 ? 32.112 -17.202 31.507 1.00 81.05 ? 397 LEU B N 1 ATOM 7307 C CA . LEU B 2 397 ? 31.375 -16.839 32.709 1.00 82.43 ? 397 LEU B CA 1 ATOM 7308 C C . LEU B 2 397 ? 32.078 -17.385 33.948 1.00 81.35 ? 397 LEU B C 1 ATOM 7309 O O . LEU B 2 397 ? 31.875 -16.894 35.060 1.00 85.48 ? 397 LEU B O 1 ATOM 7310 C CB . LEU B 2 397 ? 29.939 -17.367 32.627 1.00 82.89 ? 397 LEU B CB 1 ATOM 7311 C CG . LEU B 2 397 ? 28.966 -16.927 33.727 1.00 82.00 ? 397 LEU B CG 1 ATOM 7312 C CD1 . LEU B 2 397 ? 28.578 -15.460 33.569 1.00 80.15 ? 397 LEU B CD1 1 ATOM 7313 C CD2 . LEU B 2 397 ? 27.726 -17.821 33.771 1.00 69.60 ? 397 LEU B CD2 1 ATOM 7314 N N . MET B 2 398 ? 32.908 -18.401 33.739 1.00 72.70 ? 398 MET B N 1 ATOM 7315 C CA . MET B 2 398 ? 33.670 -19.027 34.810 1.00 73.42 ? 398 MET B CA 1 ATOM 7316 C C . MET B 2 398 ? 34.671 -18.075 35.454 1.00 79.72 ? 398 MET B C 1 ATOM 7317 O O . MET B 2 398 ? 34.853 -18.077 36.668 1.00 84.09 ? 398 MET B O 1 ATOM 7318 C CB . MET B 2 398 ? 34.420 -20.234 34.266 1.00 76.43 ? 398 MET B CB 1 ATOM 7319 C CG . MET B 2 398 ? 35.436 -20.816 35.232 1.00 71.64 ? 398 MET B CG 1 ATOM 7320 S SD . MET B 2 398 ? 36.146 -22.324 34.566 1.00 87.90 ? 398 MET B SD 1 ATOM 7321 C CE . MET B 2 398 ? 37.562 -21.675 33.684 1.00 38.68 ? 398 MET B CE 1 ATOM 7322 N N . THR B 2 399 ? 35.323 -17.264 34.633 1.00 82.65 ? 399 THR B N 1 ATOM 7323 C CA . THR B 2 399 ? 36.380 -16.381 35.111 1.00 82.82 ? 399 THR B CA 1 ATOM 7324 C C . THR B 2 399 ? 35.845 -15.046 35.628 1.00 74.17 ? 399 THR B C 1 ATOM 7325 O O . THR B 2 399 ? 36.615 -14.185 36.050 1.00 63.32 ? 399 THR B O 1 ATOM 7326 C CB . THR B 2 399 ? 37.425 -16.120 34.002 1.00 91.21 ? 399 THR B CB 1 ATOM 7327 O OG1 . THR B 2 399 ? 36.838 -15.342 32.949 1.00 90.26 ? 399 THR B OG1 1 ATOM 7328 C CG2 . THR B 2 399 ? 37.924 -17.439 33.430 1.00 94.64 ? 399 THR B CG2 1 ATOM 7329 N N . LYS B 2 400 ? 34.526 -14.883 35.594 1.00 74.72 ? 400 LYS B N 1 ATOM 7330 C CA . LYS B 2 400 ? 33.889 -13.625 35.973 1.00 80.44 ? 400 LYS B CA 1 ATOM 7331 C C . LYS B 2 400 ? 34.502 -12.994 37.228 1.00 82.63 ? 400 LYS B C 1 ATOM 7332 O O . LYS B 2 400 ? 34.813 -11.803 37.249 1.00 82.67 ? 400 LYS B O 1 ATOM 7333 C CB . LYS B 2 400 ? 32.377 -13.819 36.149 1.00 85.07 ? 400 LYS B CB 1 ATOM 7334 C CG . LYS B 2 400 ? 31.619 -12.541 36.490 1.00 89.25 ? 400 LYS B CG 1 ATOM 7335 C CD . LYS B 2 400 ? 30.104 -12.709 36.362 1.00 96.68 ? 400 LYS B CD 1 ATOM 7336 C CE . LYS B 2 400 ? 29.495 -13.447 37.549 1.00 101.65 ? 400 LYS B CE 1 ATOM 7337 N NZ . LYS B 2 400 ? 28.056 -13.079 37.745 1.00 103.02 ? 400 LYS B NZ 1 ATOM 7338 N N . ASN B 2 401 ? 34.680 -13.793 38.272 1.00 86.02 ? 401 ASN B N 1 ATOM 7339 C CA . ASN B 2 401 ? 35.214 -13.276 39.526 1.00 89.08 ? 401 ASN B CA 1 ATOM 7340 C C . ASN B 2 401 ? 36.560 -13.902 39.933 1.00 82.02 ? 401 ASN B C 1 ATOM 7341 O O . ASN B 2 401 ? 36.781 -14.299 41.074 1.00 79.98 ? 401 ASN B O 1 ATOM 7342 C CB . ASN B 2 401 ? 34.146 -13.354 40.618 1.00 93.89 ? 401 ASN B CB 1 ATOM 7343 C CG . ASN B 2 401 ? 33.295 -12.099 40.672 1.00 115.32 ? 401 ASN B CG 1 ATOM 7344 O OD1 . ASN B 2 401 ? 33.827 -10.990 40.780 1.00 120.42 ? 401 ASN B OD1 1 ATOM 7345 N ND2 . ASN B 2 401 ? 31.974 -12.257 40.588 1.00 132.75 ? 401 ASN B ND2 1 ATOM 7346 N N . MET B 2 402 ? 37.458 -13.968 38.958 1.00 76.00 ? 402 MET B N 1 ATOM 7347 C CA . MET B 2 402 ? 38.771 -14.561 39.127 1.00 69.07 ? 402 MET B CA 1 ATOM 7348 C C . MET B 2 402 ? 39.784 -13.452 39.020 1.00 68.26 ? 402 MET B C 1 ATOM 7349 O O . MET B 2 402 ? 40.727 -13.521 38.244 1.00 71.26 ? 402 MET B O 1 ATOM 7350 C CB . MET B 2 402 ? 39.023 -15.611 38.048 1.00 60.16 ? 402 MET B CB 1 ATOM 7351 C CG . MET B 2 402 ? 38.127 -16.824 38.171 1.00 58.19 ? 402 MET B CG 1 ATOM 7352 S SD . MET B 2 402 ? 38.848 -18.260 37.376 1.00 76.20 ? 402 MET B SD 1 ATOM 7353 C CE . MET B 2 402 ? 37.841 -19.590 38.041 1.00 46.79 ? 402 MET B CE 1 ATOM 7354 N N . SER B 2 403 ? 39.566 -12.432 39.835 1.00 66.19 ? 403 SER B N 1 ATOM 7355 C CA . SER B 2 403 ? 40.284 -11.163 39.782 1.00 68.02 ? 403 SER B CA 1 ATOM 7356 C C . SER B 2 403 ? 41.803 -11.176 39.537 1.00 79.22 ? 403 SER B C 1 ATOM 7357 O O . SER B 2 403 ? 42.396 -10.114 39.349 1.00 90.64 ? 403 SER B O 1 ATOM 7358 C CB . SER B 2 403 ? 39.971 -10.387 41.054 1.00 72.63 ? 403 SER B CB 1 ATOM 7359 O OG . SER B 2 403 ? 38.657 -10.698 41.487 1.00 86.47 ? 403 SER B OG 1 ATOM 7360 N N . SER B 2 404 ? 42.440 -12.343 39.528 1.00 77.24 ? 404 SER B N 1 ATOM 7361 C CA . SER B 2 404 ? 43.888 -12.386 39.322 1.00 74.10 ? 404 SER B CA 1 ATOM 7362 C C . SER B 2 404 ? 44.299 -13.209 38.110 1.00 79.89 ? 404 SER B C 1 ATOM 7363 O O . SER B 2 404 ? 45.489 -13.322 37.809 1.00 86.81 ? 404 SER B O 1 ATOM 7364 C CB . SER B 2 404 ? 44.602 -12.923 40.564 1.00 72.55 ? 404 SER B CB 1 ATOM 7365 O OG . SER B 2 404 ? 44.440 -12.063 41.670 1.00 70.41 ? 404 SER B OG 1 ATOM 7366 N N . LEU B 2 405 ? 43.319 -13.786 37.419 1.00 74.95 ? 405 LEU B N 1 ATOM 7367 C CA . LEU B 2 405 ? 43.595 -14.655 36.279 1.00 61.06 ? 405 LEU B CA 1 ATOM 7368 C C . LEU B 2 405 ? 44.345 -13.911 35.192 1.00 70.36 ? 405 LEU B C 1 ATOM 7369 O O . LEU B 2 405 ? 43.897 -12.863 34.733 1.00 79.54 ? 405 LEU B O 1 ATOM 7370 C CB . LEU B 2 405 ? 42.302 -15.218 35.698 1.00 46.75 ? 405 LEU B CB 1 ATOM 7371 C CG . LEU B 2 405 ? 42.530 -16.515 34.933 1.00 59.44 ? 405 LEU B CG 1 ATOM 7372 C CD1 . LEU B 2 405 ? 43.123 -17.539 35.874 1.00 71.60 ? 405 LEU B CD1 1 ATOM 7373 C CD2 . LEU B 2 405 ? 41.255 -17.053 34.290 1.00 61.33 ? 405 LEU B CD2 1 ATOM 7374 N N . GLU B 2 406 ? 45.488 -14.455 34.790 1.00 68.94 ? 406 GLU B N 1 ATOM 7375 C CA . GLU B 2 406 ? 46.252 -13.914 33.673 1.00 73.55 ? 406 GLU B CA 1 ATOM 7376 C C . GLU B 2 406 ? 46.402 -14.962 32.585 1.00 67.54 ? 406 GLU B C 1 ATOM 7377 O O . GLU B 2 406 ? 46.414 -14.641 31.404 1.00 82.76 ? 406 GLU B O 1 ATOM 7378 C CB . GLU B 2 406 ? 47.637 -13.448 34.120 1.00 83.03 ? 406 GLU B CB 1 ATOM 7379 C CG . GLU B 2 406 ? 47.628 -12.301 35.114 1.00 94.70 ? 406 GLU B CG 1 ATOM 7380 C CD . GLU B 2 406 ? 48.970 -11.603 35.193 1.00 101.09 ? 406 GLU B CD 1 ATOM 7381 O OE1 . GLU B 2 406 ? 49.081 -10.607 35.941 1.00 91.39 ? 406 GLU B OE1 1 ATOM 7382 O OE2 . GLU B 2 406 ? 49.911 -12.048 34.496 1.00 110.35 ? 406 GLU B OE2 1 ATOM 7383 N N . THR B 2 407 ? 46.517 -16.219 32.986 1.00 54.39 ? 407 THR B N 1 ATOM 7384 C CA . THR B 2 407 ? 46.693 -17.294 32.027 1.00 66.42 ? 407 THR B CA 1 ATOM 7385 C C . THR B 2 407 ? 45.593 -18.333 32.138 1.00 73.71 ? 407 THR B C 1 ATOM 7386 O O . THR B 2 407 ? 45.389 -18.915 33.195 1.00 76.97 ? 407 THR B O 1 ATOM 7387 C CB . THR B 2 407 ? 48.020 -18.030 32.222 1.00 70.25 ? 407 THR B CB 1 ATOM 7388 O OG1 . THR B 2 407 ? 49.116 -17.159 31.906 1.00 65.11 ? 407 THR B OG1 1 ATOM 7389 C CG2 . THR B 2 407 ? 48.052 -19.267 31.320 1.00 69.12 ? 407 THR B CG2 1 ATOM 7390 N N . LEU B 2 408 ? 44.898 -18.571 31.035 1.00 72.75 ? 408 LEU B N 1 ATOM 7391 C CA . LEU B 2 408 ? 43.856 -19.576 31.000 1.00 69.01 ? 408 LEU B CA 1 ATOM 7392 C C . LEU B 2 408 ? 44.136 -20.478 29.825 1.00 65.73 ? 408 LEU B C 1 ATOM 7393 O O . LEU B 2 408 ? 44.083 -20.038 28.686 1.00 72.43 ? 408 LEU B O 1 ATOM 7394 C CB . LEU B 2 408 ? 42.481 -18.914 30.851 1.00 72.32 ? 408 LEU B CB 1 ATOM 7395 C CG . LEU B 2 408 ? 41.194 -19.724 31.099 1.00 66.89 ? 408 LEU B CG 1 ATOM 7396 C CD1 . LEU B 2 408 ? 40.307 -19.814 29.870 1.00 66.45 ? 408 LEU B CD1 1 ATOM 7397 C CD2 . LEU B 2 408 ? 41.483 -21.096 31.658 1.00 54.58 ? 408 LEU B CD2 1 ATOM 7398 N N . ASP B 2 409 ? 44.469 -21.732 30.102 1.00 59.73 ? 409 ASP B N 1 ATOM 7399 C CA . ASP B 2 409 ? 44.603 -22.720 29.048 1.00 58.33 ? 409 ASP B CA 1 ATOM 7400 C C . ASP B 2 409 ? 43.433 -23.692 29.057 1.00 67.70 ? 409 ASP B C 1 ATOM 7401 O O . ASP B 2 409 ? 43.420 -24.648 29.822 1.00 74.91 ? 409 ASP B O 1 ATOM 7402 C CB . ASP B 2 409 ? 45.914 -23.497 29.161 1.00 52.13 ? 409 ASP B CB 1 ATOM 7403 C CG . ASP B 2 409 ? 46.034 -24.585 28.093 1.00 70.15 ? 409 ASP B CG 1 ATOM 7404 O OD1 . ASP B 2 409 ? 45.283 -24.518 27.095 1.00 74.29 ? 409 ASP B OD1 1 ATOM 7405 O OD2 . ASP B 2 409 ? 46.866 -25.510 28.241 1.00 74.06 ? 409 ASP B OD2 1 ATOM 7406 N N . VAL B 2 410 ? 42.454 -23.450 28.197 1.00 68.29 ? 410 VAL B N 1 ATOM 7407 C CA . VAL B 2 410 ? 41.368 -24.398 28.029 1.00 74.10 ? 410 VAL B CA 1 ATOM 7408 C C . VAL B 2 410 ? 41.483 -25.118 26.690 1.00 76.95 ? 410 VAL B C 1 ATOM 7409 O O . VAL B 2 410 ? 40.478 -25.397 26.032 1.00 78.47 ? 410 VAL B O 1 ATOM 7410 C CB . VAL B 2 410 ? 40.006 -23.710 28.127 1.00 70.83 ? 410 VAL B CB 1 ATOM 7411 C CG1 . VAL B 2 410 ? 39.594 -23.595 29.565 1.00 63.02 ? 410 VAL B CG1 1 ATOM 7412 C CG2 . VAL B 2 410 ? 40.062 -22.345 27.466 1.00 74.18 ? 410 VAL B CG2 1 ATOM 7413 N N . SER B 2 411 ? 42.715 -25.420 26.294 1.00 75.92 ? 411 SER B N 1 ATOM 7414 C CA . SER B 2 411 ? 42.965 -26.078 25.013 1.00 78.27 ? 411 SER B CA 1 ATOM 7415 C C . SER B 2 411 ? 42.641 -27.572 25.047 1.00 82.35 ? 411 SER B C 1 ATOM 7416 O O . SER B 2 411 ? 42.336 -28.132 26.095 1.00 99.03 ? 411 SER B O 1 ATOM 7417 C CB . SER B 2 411 ? 44.416 -25.879 24.580 1.00 75.38 ? 411 SER B CB 1 ATOM 7418 O OG . SER B 2 411 ? 45.242 -26.913 25.076 1.00 78.62 ? 411 SER B OG 1 ATOM 7419 N N . LEU B 2 412 ? 42.711 -28.208 23.888 1.00 67.36 ? 412 LEU B N 1 ATOM 7420 C CA . LEU B 2 412 ? 42.429 -29.628 23.765 1.00 68.36 ? 412 LEU B CA 1 ATOM 7421 C C . LEU B 2 412 ? 41.163 -30.103 24.486 1.00 73.19 ? 412 LEU B C 1 ATOM 7422 O O . LEU B 2 412 ? 41.076 -31.256 24.918 1.00 80.82 ? 412 LEU B O 1 ATOM 7423 C CB . LEU B 2 412 ? 43.662 -30.462 24.137 1.00 71.08 ? 412 LEU B CB 1 ATOM 7424 C CG . LEU B 2 412 ? 44.562 -30.706 22.911 1.00 72.66 ? 412 LEU B CG 1 ATOM 7425 C CD1 . LEU B 2 412 ? 46.028 -30.901 23.262 1.00 65.27 ? 412 LEU B CD1 1 ATOM 7426 C CD2 . LEU B 2 412 ? 44.042 -31.864 22.061 1.00 62.85 ? 412 LEU B CD2 1 ATOM 7427 N N . ASN B 2 413 ? 40.176 -29.218 24.591 1.00 66.44 ? 413 ASN B N 1 ATOM 7428 C CA . ASN B 2 413 ? 38.838 -29.622 25.020 1.00 69.86 ? 413 ASN B CA 1 ATOM 7429 C C . ASN B 2 413 ? 37.896 -29.838 23.820 1.00 75.52 ? 413 ASN B C 1 ATOM 7430 O O . ASN B 2 413 ? 38.345 -30.222 22.736 1.00 81.47 ? 413 ASN B O 1 ATOM 7431 C CB . ASN B 2 413 ? 38.254 -28.601 25.997 1.00 67.29 ? 413 ASN B CB 1 ATOM 7432 C CG . ASN B 2 413 ? 38.838 -28.725 27.394 1.00 72.60 ? 413 ASN B CG 1 ATOM 7433 O OD1 . ASN B 2 413 ? 39.970 -28.316 27.650 1.00 82.35 ? 413 ASN B OD1 1 ATOM 7434 N ND2 . ASN B 2 413 ? 38.057 -29.279 28.310 1.00 65.22 ? 413 ASN B ND2 1 ATOM 7435 N N . SER B 2 414 ? 36.601 -29.585 24.015 1.00 69.09 ? 414 SER B N 1 ATOM 7436 C CA . SER B 2 414 ? 35.601 -29.735 22.954 1.00 69.42 ? 414 SER B CA 1 ATOM 7437 C C . SER B 2 414 ? 34.763 -28.473 22.790 1.00 67.96 ? 414 SER B C 1 ATOM 7438 O O . SER B 2 414 ? 33.543 -28.542 22.596 1.00 68.89 ? 414 SER B O 1 ATOM 7439 C CB . SER B 2 414 ? 34.663 -30.905 23.253 1.00 79.54 ? 414 SER B CB 1 ATOM 7440 O OG . SER B 2 414 ? 35.387 -32.054 23.649 1.00 96.26 ? 414 SER B OG 1 ATOM 7441 N N . LEU B 2 415 ? 35.423 -27.325 22.865 1.00 59.36 ? 415 LEU B N 1 ATOM 7442 C CA . LEU B 2 415 ? 34.741 -26.036 22.809 1.00 65.08 ? 415 LEU B CA 1 ATOM 7443 C C . LEU B 2 415 ? 34.103 -25.666 21.443 1.00 81.14 ? 415 LEU B C 1 ATOM 7444 O O . LEU B 2 415 ? 34.533 -26.117 20.375 1.00 69.86 ? 415 LEU B O 1 ATOM 7445 C CB . LEU B 2 415 ? 35.708 -24.928 23.231 1.00 61.93 ? 415 LEU B CB 1 ATOM 7446 C CG . LEU B 2 415 ? 36.116 -24.827 24.690 1.00 60.64 ? 415 LEU B CG 1 ATOM 7447 C CD1 . LEU B 2 415 ? 37.222 -23.780 24.845 1.00 53.35 ? 415 LEU B CD1 1 ATOM 7448 C CD2 . LEU B 2 415 ? 34.898 -24.482 25.526 1.00 66.42 ? 415 LEU B CD2 1 ATOM 7449 N N . ASN B 2 416 ? 33.080 -24.820 21.500 1.00 74.48 ? 416 ASN B N 1 ATOM 7450 C CA . ASN B 2 416 ? 32.462 -24.285 20.304 1.00 71.60 ? 416 ASN B CA 1 ATOM 7451 C C . ASN B 2 416 ? 31.590 -23.075 20.603 1.00 83.96 ? 416 ASN B C 1 ATOM 7452 O O . ASN B 2 416 ? 30.863 -23.038 21.601 1.00 87.19 ? 416 ASN B O 1 ATOM 7453 C CB . ASN B 2 416 ? 31.662 -25.361 19.580 1.00 75.94 ? 416 ASN B CB 1 ATOM 7454 C CG . ASN B 2 416 ? 30.439 -25.800 20.347 1.00 72.94 ? 416 ASN B CG 1 ATOM 7455 O OD1 . ASN B 2 416 ? 30.480 -26.796 21.063 1.00 84.04 ? 416 ASN B OD1 1 ATOM 7456 N ND2 . ASN B 2 416 ? 29.339 -25.069 20.193 1.00 63.19 ? 416 ASN B ND2 1 ATOM 7457 N N . SER B 2 417 ? 31.663 -22.087 19.721 1.00 92.09 ? 417 SER B N 1 ATOM 7458 C CA . SER B 2 417 ? 31.020 -20.807 19.963 1.00 94.36 ? 417 SER B CA 1 ATOM 7459 C C . SER B 2 417 ? 29.632 -20.707 19.331 1.00 94.81 ? 417 SER B C 1 ATOM 7460 O O . SER B 2 417 ? 29.161 -19.617 19.018 1.00 88.70 ? 417 SER B O 1 ATOM 7461 C CB . SER B 2 417 ? 31.927 -19.672 19.483 1.00 91.34 ? 417 SER B CB 1 ATOM 7462 O OG . SER B 2 417 ? 32.557 -20.003 18.257 1.00 84.00 ? 417 SER B OG 1 ATOM 7463 N N . HIS B 2 418 ? 28.968 -21.846 19.161 1.00 98.68 ? 418 HIS B N 1 ATOM 7464 C CA . HIS B 2 418 ? 27.626 -21.851 18.587 1.00 101.22 ? 418 HIS B CA 1 ATOM 7465 C C . HIS B 2 418 ? 26.533 -21.682 19.638 1.00 109.66 ? 418 HIS B C 1 ATOM 7466 O O . HIS B 2 418 ? 25.352 -21.818 19.333 1.00 109.26 ? 418 HIS B O 1 ATOM 7467 C CB . HIS B 2 418 ? 27.379 -23.127 17.780 1.00 96.85 ? 418 HIS B CB 1 ATOM 7468 C CG . HIS B 2 418 ? 28.055 -23.137 16.443 1.00 101.92 ? 418 HIS B CG 1 ATOM 7469 N ND1 . HIS B 2 418 ? 28.968 -24.104 16.075 1.00 105.72 ? 418 HIS B ND1 1 ATOM 7470 C CD2 . HIS B 2 418 ? 27.957 -22.292 15.389 1.00 95.43 ? 418 HIS B CD2 1 ATOM 7471 C CE1 . HIS B 2 418 ? 29.396 -23.859 14.850 1.00 99.93 ? 418 HIS B CE1 1 ATOM 7472 N NE2 . HIS B 2 418 ? 28.802 -22.763 14.414 1.00 96.41 ? 418 HIS B NE2 1 ATOM 7473 N N . ALA B 2 419 ? 26.928 -21.381 20.871 1.00 114.20 ? 419 ALA B N 1 ATOM 7474 C CA . ALA B 2 419 ? 25.973 -21.224 21.961 1.00 109.90 ? 419 ALA B CA 1 ATOM 7475 C C . ALA B 2 419 ? 24.814 -20.320 21.569 1.00 118.65 ? 419 ALA B C 1 ATOM 7476 O O . ALA B 2 419 ? 25.016 -19.247 21.001 1.00 122.30 ? 419 ALA B O 1 ATOM 7477 C CB . ALA B 2 419 ? 26.663 -20.677 23.195 1.00 107.48 ? 419 ALA B CB 1 ATOM 7478 N N . TYR B 2 420 ? 23.603 -20.776 21.872 1.00 124.96 ? 420 TYR B N 1 ATOM 7479 C CA . TYR B 2 420 ? 22.381 -19.980 21.740 1.00 130.67 ? 420 TYR B CA 1 ATOM 7480 C C . TYR B 2 420 ? 22.516 -18.620 22.436 1.00 122.43 ? 420 TYR B C 1 ATOM 7481 O O . TYR B 2 420 ? 22.268 -17.569 21.841 1.00 106.57 ? 420 TYR B O 1 ATOM 7482 C CB . TYR B 2 420 ? 21.215 -20.766 22.349 1.00 144.15 ? 420 TYR B CB 1 ATOM 7483 C CG . TYR B 2 420 ? 21.656 -21.722 23.452 1.00 155.64 ? 420 TYR B CG 1 ATOM 7484 C CD1 . TYR B 2 420 ? 21.976 -21.251 24.729 1.00 157.34 ? 420 TYR B CD1 1 ATOM 7485 C CD2 . TYR B 2 420 ? 21.765 -23.090 23.213 1.00 154.56 ? 420 TYR B CD2 1 ATOM 7486 C CE1 . TYR B 2 420 ? 22.387 -22.114 25.734 1.00 155.03 ? 420 TYR B CE1 1 ATOM 7487 C CE2 . TYR B 2 420 ? 22.175 -23.962 24.213 1.00 155.16 ? 420 TYR B CE2 1 ATOM 7488 C CZ . TYR B 2 420 ? 22.485 -23.470 25.471 1.00 154.93 ? 420 TYR B CZ 1 ATOM 7489 O OH . TYR B 2 420 ? 22.895 -24.335 26.466 1.00 148.07 ? 420 TYR B OH 1 ATOM 7490 N N . ASP B 2 421 ? 22.913 -18.668 23.707 1.00 130.26 ? 421 ASP B N 1 ATOM 7491 C CA . ASP B 2 421 ? 23.143 -17.490 24.535 1.00 130.63 ? 421 ASP B CA 1 ATOM 7492 C C . ASP B 2 421 ? 24.616 -17.096 24.445 1.00 138.45 ? 421 ASP B C 1 ATOM 7493 O O . ASP B 2 421 ? 25.459 -17.697 25.113 1.00 145.45 ? 421 ASP B O 1 ATOM 7494 C CB . ASP B 2 421 ? 22.772 -17.814 25.988 1.00 121.70 ? 421 ASP B CB 1 ATOM 7495 C CG . ASP B 2 421 ? 22.720 -16.580 26.877 1.00 118.81 ? 421 ASP B CG 1 ATOM 7496 O OD1 . ASP B 2 421 ? 23.590 -15.694 26.735 1.00 115.27 ? 421 ASP B OD1 1 ATOM 7497 O OD2 . ASP B 2 421 ? 21.808 -16.504 27.730 1.00 118.68 ? 421 ASP B OD2 1 ATOM 7498 N N . ARG B 2 422 ? 24.926 -16.097 23.618 1.00 135.42 ? 422 ARG B N 1 ATOM 7499 C CA . ARG B 2 422 ? 26.319 -15.713 23.368 1.00 126.96 ? 422 ARG B CA 1 ATOM 7500 C C . ARG B 2 422 ? 26.781 -14.510 24.196 1.00 127.45 ? 422 ARG B C 1 ATOM 7501 O O . ARG B 2 422 ? 27.470 -13.633 23.678 1.00 126.78 ? 422 ARG B O 1 ATOM 7502 C CB . ARG B 2 422 ? 26.562 -15.455 21.869 1.00 119.28 ? 422 ARG B CB 1 ATOM 7503 C CG . ARG B 2 422 ? 26.283 -16.663 20.967 1.00 111.77 ? 422 ARG B CG 1 ATOM 7504 C CD . ARG B 2 422 ? 26.846 -16.496 19.556 1.00 111.46 ? 422 ARG B CD 1 ATOM 7505 N NE . ARG B 2 422 ? 26.385 -17.557 18.654 1.00 122.16 ? 422 ARG B NE 1 ATOM 7506 C CZ . ARG B 2 422 ? 26.695 -17.636 17.359 1.00 134.31 ? 422 ARG B CZ 1 ATOM 7507 N NH1 . ARG B 2 422 ? 27.475 -16.717 16.806 1.00 145.57 ? 422 ARG B NH1 1 ATOM 7508 N NH2 . ARG B 2 422 ? 26.229 -18.631 16.608 1.00 129.10 ? 422 ARG B NH2 1 ATOM 7509 N N . THR B 2 423 ? 26.420 -14.487 25.481 1.00 129.88 ? 423 THR B N 1 ATOM 7510 C CA . THR B 2 423 ? 26.769 -13.369 26.367 1.00 130.25 ? 423 THR B CA 1 ATOM 7511 C C . THR B 2 423 ? 28.197 -13.442 26.928 1.00 122.60 ? 423 THR B C 1 ATOM 7512 O O . THR B 2 423 ? 28.636 -14.479 27.446 1.00 106.63 ? 423 THR B O 1 ATOM 7513 C CB . THR B 2 423 ? 25.763 -13.200 27.535 1.00 98.32 ? 423 THR B CB 1 ATOM 7514 O OG1 . THR B 2 423 ? 24.453 -12.935 27.012 1.00 100.78 ? 423 THR B OG1 1 ATOM 7515 C CG2 . THR B 2 423 ? 26.187 -12.043 28.443 1.00 93.67 ? 423 THR B CG2 1 ATOM 7516 N N . CYS B 2 424 ? 28.899 -12.313 26.822 1.00 122.18 ? 424 CYS B N 1 ATOM 7517 C CA . CYS B 2 424 ? 30.302 -12.205 27.208 1.00 103.33 ? 424 CYS B CA 1 ATOM 7518 C C . CYS B 2 424 ? 30.414 -11.679 28.618 1.00 94.03 ? 424 CYS B C 1 ATOM 7519 O O . CYS B 2 424 ? 29.672 -10.773 28.997 1.00 83.97 ? 424 CYS B O 1 ATOM 7520 C CB . CYS B 2 424 ? 31.052 -11.261 26.262 1.00 91.08 ? 424 CYS B CB 1 ATOM 7521 S SG . CYS B 2 424 ? 32.773 -11.731 25.970 1.00 165.70 ? 424 CYS B SG 1 ATOM 7522 N N . ALA B 2 425 ? 31.349 -12.256 29.377 1.00 101.01 ? 425 ALA B N 1 ATOM 7523 C CA . ALA B 2 425 ? 31.635 -11.862 30.761 1.00 102.13 ? 425 ALA B CA 1 ATOM 7524 C C . ALA B 2 425 ? 33.058 -12.236 31.175 1.00 108.77 ? 425 ALA B C 1 ATOM 7525 O O . ALA B 2 425 ? 33.274 -12.704 32.294 1.00 106.83 ? 425 ALA B O 1 ATOM 7526 C CB . ALA B 2 425 ? 30.636 -12.501 31.720 1.00 88.52 ? 425 ALA B CB 1 ATOM 7527 N N . TRP B 2 426 ? 34.023 -12.025 30.279 1.00 111.90 ? 426 TRP B N 1 ATOM 7528 C CA . TRP B 2 426 ? 35.410 -12.421 30.538 1.00 101.07 ? 426 TRP B CA 1 ATOM 7529 C C . TRP B 2 426 ? 36.032 -11.661 31.697 1.00 100.75 ? 426 TRP B C 1 ATOM 7530 O O . TRP B 2 426 ? 35.627 -10.545 32.017 1.00 108.80 ? 426 TRP B O 1 ATOM 7531 C CB . TRP B 2 426 ? 36.290 -12.244 29.292 1.00 90.75 ? 426 TRP B CB 1 ATOM 7532 C CG . TRP B 2 426 ? 36.278 -13.415 28.345 1.00 80.74 ? 426 TRP B CG 1 ATOM 7533 C CD1 . TRP B 2 426 ? 35.783 -13.430 27.082 1.00 70.56 ? 426 TRP B CD1 1 ATOM 7534 C CD2 . TRP B 2 426 ? 36.784 -14.737 28.592 1.00 86.03 ? 426 TRP B CD2 1 ATOM 7535 N NE1 . TRP B 2 426 ? 35.942 -14.668 26.523 1.00 71.64 ? 426 TRP B NE1 1 ATOM 7536 C CE2 . TRP B 2 426 ? 36.556 -15.492 27.428 1.00 80.79 ? 426 TRP B CE2 1 ATOM 7537 C CE3 . TRP B 2 426 ? 37.404 -15.354 29.684 1.00 90.86 ? 426 TRP B CE3 1 ATOM 7538 C CZ2 . TRP B 2 426 ? 36.929 -16.834 27.319 1.00 81.71 ? 426 TRP B CZ2 1 ATOM 7539 C CZ3 . TRP B 2 426 ? 37.772 -16.689 29.575 1.00 87.15 ? 426 TRP B CZ3 1 ATOM 7540 C CH2 . TRP B 2 426 ? 37.533 -17.412 28.403 1.00 82.73 ? 426 TRP B CH2 1 ATOM 7541 N N . ALA B 2 427 ? 37.023 -12.279 32.326 1.00 94.08 ? 427 ALA B N 1 ATOM 7542 C CA . ALA B 2 427 ? 37.811 -11.595 33.332 1.00 93.93 ? 427 ALA B CA 1 ATOM 7543 C C . ALA B 2 427 ? 38.663 -10.559 32.623 1.00 88.51 ? 427 ALA B C 1 ATOM 7544 O O . ALA B 2 427 ? 39.442 -10.879 31.733 1.00 76.85 ? 427 ALA B O 1 ATOM 7545 C CB . ALA B 2 427 ? 38.680 -12.577 34.093 1.00 98.01 ? 427 ALA B CB 1 ATOM 7546 N N . GLU B 2 428 ? 38.507 -9.310 33.030 1.00 98.20 ? 428 GLU B N 1 ATOM 7547 C CA . GLU B 2 428 ? 39.140 -8.188 32.357 1.00 107.91 ? 428 GLU B CA 1 ATOM 7548 C C . GLU B 2 428 ? 40.662 -8.285 32.410 1.00 95.35 ? 428 GLU B C 1 ATOM 7549 O O . GLU B 2 428 ? 41.368 -7.464 31.835 1.00 102.31 ? 428 GLU B O 1 ATOM 7550 C CB . GLU B 2 428 ? 38.662 -6.881 32.999 1.00 130.31 ? 428 GLU B CB 1 ATOM 7551 C CG . GLU B 2 428 ? 37.136 -6.798 33.201 1.00 149.04 ? 428 GLU B CG 1 ATOM 7552 C CD . GLU B 2 428 ? 36.594 -7.800 34.230 1.00 157.49 ? 428 GLU B CD 1 ATOM 7553 O OE1 . GLU B 2 428 ? 35.531 -8.412 33.975 1.00 156.87 ? 428 GLU B OE1 1 ATOM 7554 O OE2 . GLU B 2 428 ? 37.232 -7.980 35.291 1.00 158.47 ? 428 GLU B OE2 1 ATOM 7555 N N . SER B 2 429 ? 41.163 -9.310 33.082 1.00 86.63 ? 429 SER B N 1 ATOM 7556 C CA . SER B 2 429 ? 42.579 -9.379 33.413 1.00 86.44 ? 429 SER B CA 1 ATOM 7557 C C . SER B 2 429 ? 43.376 -10.426 32.633 1.00 82.71 ? 429 SER B C 1 ATOM 7558 O O . SER B 2 429 ? 44.605 -10.473 32.742 1.00 89.09 ? 429 SER B O 1 ATOM 7559 C CB . SER B 2 429 ? 42.746 -9.609 34.922 1.00 87.80 ? 429 SER B CB 1 ATOM 7560 O OG . SER B 2 429 ? 42.018 -10.750 35.362 1.00 80.72 ? 429 SER B OG 1 ATOM 7561 N N . ILE B 2 430 ? 42.692 -11.267 31.860 1.00 67.88 ? 430 ILE B N 1 ATOM 7562 C CA . ILE B 2 430 ? 43.375 -12.326 31.111 1.00 70.42 ? 430 ILE B CA 1 ATOM 7563 C C . ILE B 2 430 ? 44.375 -11.750 30.108 1.00 78.86 ? 430 ILE B C 1 ATOM 7564 O O . ILE B 2 430 ? 44.055 -10.821 29.365 1.00 84.31 ? 430 ILE B O 1 ATOM 7565 C CB . ILE B 2 430 ? 42.390 -13.222 30.334 1.00 72.38 ? 430 ILE B CB 1 ATOM 7566 C CG1 . ILE B 2 430 ? 41.098 -13.454 31.126 1.00 76.13 ? 430 ILE B CG1 1 ATOM 7567 C CG2 . ILE B 2 430 ? 43.060 -14.531 29.963 1.00 73.75 ? 430 ILE B CG2 1 ATOM 7568 C CD1 . ILE B 2 430 ? 41.316 -13.975 32.518 1.00 76.71 ? 430 ILE B CD1 1 ATOM 7569 N N . LEU B 2 431 ? 45.586 -12.298 30.085 1.00 76.40 ? 431 LEU B N 1 ATOM 7570 C CA . LEU B 2 431 ? 46.604 -11.834 29.144 1.00 83.12 ? 431 LEU B CA 1 ATOM 7571 C C . LEU B 2 431 ? 46.972 -12.943 28.176 1.00 87.55 ? 431 LEU B C 1 ATOM 7572 O O . LEU B 2 431 ? 47.248 -12.693 27.006 1.00 104.99 ? 431 LEU B O 1 ATOM 7573 C CB . LEU B 2 431 ? 47.868 -11.348 29.865 1.00 86.60 ? 431 LEU B CB 1 ATOM 7574 C CG . LEU B 2 431 ? 47.754 -10.324 31.000 1.00 88.37 ? 431 LEU B CG 1 ATOM 7575 C CD1 . LEU B 2 431 ? 49.141 -9.911 31.468 1.00 79.79 ? 431 LEU B CD1 1 ATOM 7576 C CD2 . LEU B 2 431 ? 46.935 -9.109 30.579 1.00 90.63 ? 431 LEU B CD2 1 ATOM 7577 N N . VAL B 2 432 ? 46.980 -14.172 28.669 1.00 79.10 ? 432 VAL B N 1 ATOM 7578 C CA . VAL B 2 432 ? 47.283 -15.320 27.830 1.00 74.26 ? 432 VAL B CA 1 ATOM 7579 C C . VAL B 2 432 ? 46.123 -16.305 27.834 1.00 66.90 ? 432 VAL B C 1 ATOM 7580 O O . VAL B 2 432 ? 45.682 -16.768 28.878 1.00 76.35 ? 432 VAL B O 1 ATOM 7581 C CB . VAL B 2 432 ? 48.554 -16.026 28.300 1.00 72.04 ? 432 VAL B CB 1 ATOM 7582 C CG1 . VAL B 2 432 ? 48.966 -17.088 27.289 1.00 65.20 ? 432 VAL B CG1 1 ATOM 7583 C CG2 . VAL B 2 432 ? 49.662 -14.998 28.529 1.00 61.44 ? 432 VAL B CG2 1 ATOM 7584 N N . LEU B 2 433 ? 45.625 -16.620 26.655 1.00 64.82 ? 433 LEU B N 1 ATOM 7585 C CA . LEU B 2 433 ? 44.435 -17.441 26.545 1.00 76.05 ? 433 LEU B CA 1 ATOM 7586 C C . LEU B 2 433 ? 44.613 -18.492 25.454 1.00 84.55 ? 433 LEU B C 1 ATOM 7587 O O . LEU B 2 433 ? 44.437 -18.200 24.265 1.00 85.01 ? 433 LEU B O 1 ATOM 7588 C CB . LEU B 2 433 ? 43.223 -16.554 26.242 1.00 78.34 ? 433 LEU B CB 1 ATOM 7589 C CG . LEU B 2 433 ? 41.876 -17.254 26.086 1.00 72.21 ? 433 LEU B CG 1 ATOM 7590 C CD1 . LEU B 2 433 ? 41.618 -18.078 27.319 1.00 72.46 ? 433 LEU B CD1 1 ATOM 7591 C CD2 . LEU B 2 433 ? 40.753 -16.252 25.857 1.00 69.51 ? 433 LEU B CD2 1 ATOM 7592 N N . ASN B 2 434 ? 44.980 -19.709 25.854 1.00 81.28 ? 434 ASN B N 1 ATOM 7593 C CA . ASN B 2 434 ? 45.092 -20.801 24.898 1.00 79.97 ? 434 ASN B CA 1 ATOM 7594 C C . ASN B 2 434 ? 43.727 -21.433 24.634 1.00 89.85 ? 434 ASN B C 1 ATOM 7595 O O . ASN B 2 434 ? 43.139 -22.061 25.521 1.00 92.19 ? 434 ASN B O 1 ATOM 7596 C CB . ASN B 2 434 ? 46.124 -21.849 25.332 1.00 74.02 ? 434 ASN B CB 1 ATOM 7597 C CG . ASN B 2 434 ? 46.555 -22.741 24.176 1.00 97.45 ? 434 ASN B CG 1 ATOM 7598 O OD1 . ASN B 2 434 ? 45.752 -23.499 23.632 1.00 93.23 ? 434 ASN B OD1 1 ATOM 7599 N ND2 . ASN B 2 434 ? 47.811 -22.611 23.757 1.00 121.98 ? 434 ASN B ND2 1 ATOM 7600 N N . LEU B 2 435 ? 43.221 -21.228 23.417 1.00 83.77 ? 435 LEU B N 1 ATOM 7601 C CA . LEU B 2 435 ? 41.940 -21.774 22.993 1.00 68.02 ? 435 LEU B CA 1 ATOM 7602 C C . LEU B 2 435 ? 42.182 -22.813 21.925 1.00 68.05 ? 435 LEU B C 1 ATOM 7603 O O . LEU B 2 435 ? 41.242 -23.266 21.271 1.00 76.21 ? 435 LEU B O 1 ATOM 7604 C CB . LEU B 2 435 ? 41.044 -20.675 22.428 1.00 69.38 ? 435 LEU B CB 1 ATOM 7605 C CG . LEU B 2 435 ? 40.506 -19.660 23.437 1.00 81.68 ? 435 LEU B CG 1 ATOM 7606 C CD1 . LEU B 2 435 ? 40.044 -18.382 22.748 1.00 83.21 ? 435 LEU B CD1 1 ATOM 7607 C CD2 . LEU B 2 435 ? 39.382 -20.275 24.257 1.00 88.48 ? 435 LEU B CD2 1 ATOM 7608 N N . SER B 2 436 ? 43.447 -23.196 21.768 1.00 63.09 ? 436 SER B N 1 ATOM 7609 C CA . SER B 2 436 ? 43.881 -24.015 20.639 1.00 66.30 ? 436 SER B CA 1 ATOM 7610 C C . SER B 2 436 ? 43.386 -25.453 20.721 1.00 70.35 ? 436 SER B C 1 ATOM 7611 O O . SER B 2 436 ? 43.387 -26.051 21.788 1.00 83.96 ? 436 SER B O 1 ATOM 7612 C CB . SER B 2 436 ? 45.410 -23.991 20.524 1.00 70.01 ? 436 SER B CB 1 ATOM 7613 O OG . SER B 2 436 ? 46.011 -25.071 21.218 1.00 68.59 ? 436 SER B OG 1 ATOM 7614 N N . SER B 2 437 ? 42.966 -25.996 19.583 1.00 74.41 ? 437 SER B N 1 ATOM 7615 C CA . SER B 2 437 ? 42.553 -27.400 19.461 1.00 80.04 ? 437 SER B CA 1 ATOM 7616 C C . SER B 2 437 ? 41.173 -27.717 20.027 1.00 84.19 ? 437 SER B C 1 ATOM 7617 O O . SER B 2 437 ? 41.002 -28.673 20.783 1.00 93.56 ? 437 SER B O 1 ATOM 7618 C CB . SER B 2 437 ? 43.589 -28.354 20.062 1.00 77.23 ? 437 SER B CB 1 ATOM 7619 O OG . SER B 2 437 ? 44.765 -28.389 19.283 1.00 76.86 ? 437 SER B OG 1 ATOM 7620 N N . ASN B 2 438 ? 40.188 -26.916 19.657 1.00 79.03 ? 438 ASN B N 1 ATOM 7621 C CA . ASN B 2 438 ? 38.807 -27.282 19.906 1.00 82.69 ? 438 ASN B CA 1 ATOM 7622 C C . ASN B 2 438 ? 38.025 -27.204 18.603 1.00 89.39 ? 438 ASN B C 1 ATOM 7623 O O . ASN B 2 438 ? 38.562 -27.482 17.525 1.00 92.71 ? 438 ASN B O 1 ATOM 7624 C CB . ASN B 2 438 ? 38.170 -26.371 20.953 1.00 84.22 ? 438 ASN B CB 1 ATOM 7625 C CG . ASN B 2 438 ? 38.993 -26.263 22.212 1.00 79.48 ? 438 ASN B CG 1 ATOM 7626 O OD1 . ASN B 2 438 ? 40.002 -25.560 22.251 1.00 75.95 ? 438 ASN B OD1 1 ATOM 7627 N ND2 . ASN B 2 438 ? 38.553 -26.943 23.261 1.00 80.56 ? 438 ASN B ND2 1 ATOM 7628 N N . MET B 2 439 ? 36.765 -26.799 18.707 1.00 83.82 ? 439 MET B N 1 ATOM 7629 C CA . MET B 2 439 ? 35.885 -26.728 17.555 1.00 73.80 ? 439 MET B CA 1 ATOM 7630 C C . MET B 2 439 ? 35.300 -25.327 17.460 1.00 79.23 ? 439 MET B C 1 ATOM 7631 O O . MET B 2 439 ? 34.210 -25.110 16.925 1.00 77.32 ? 439 MET B O 1 ATOM 7632 C CB . MET B 2 439 ? 34.789 -27.782 17.670 1.00 65.98 ? 439 MET B CB 1 ATOM 7633 C CG . MET B 2 439 ? 35.318 -29.213 17.743 1.00 56.91 ? 439 MET B CG 1 ATOM 7634 S SD . MET B 2 439 ? 34.005 -30.433 17.632 1.00 141.00 ? 439 MET B SD 1 ATOM 7635 C CE . MET B 2 439 ? 33.344 -30.065 15.996 1.00 131.07 ? 439 MET B CE 1 ATOM 7636 N N . LEU B 2 440 ? 36.049 -24.371 17.988 1.00 83.04 ? 440 LEU B N 1 ATOM 7637 C CA . LEU B 2 440 ? 35.641 -22.983 17.934 1.00 85.22 ? 440 LEU B CA 1 ATOM 7638 C C . LEU B 2 440 ? 35.435 -22.520 16.509 1.00 84.00 ? 440 LEU B C 1 ATOM 7639 O O . LEU B 2 440 ? 36.270 -22.770 15.640 1.00 83.06 ? 440 LEU B O 1 ATOM 7640 C CB . LEU B 2 440 ? 36.696 -22.109 18.592 1.00 85.77 ? 440 LEU B CB 1 ATOM 7641 C CG . LEU B 2 440 ? 36.748 -22.335 20.089 1.00 87.52 ? 440 LEU B CG 1 ATOM 7642 C CD1 . LEU B 2 440 ? 37.925 -21.583 20.711 1.00 93.03 ? 440 LEU B CD1 1 ATOM 7643 C CD2 . LEU B 2 440 ? 35.411 -21.906 20.668 1.00 85.29 ? 440 LEU B CD2 1 ATOM 7644 N N . THR B 2 441 ? 34.320 -21.836 16.278 1.00 87.34 ? 441 THR B N 1 ATOM 7645 C CA . THR B 2 441 ? 34.085 -21.150 15.015 1.00 84.24 ? 441 THR B CA 1 ATOM 7646 C C . THR B 2 441 ? 34.560 -19.697 15.152 1.00 80.92 ? 441 THR B C 1 ATOM 7647 O O . THR B 2 441 ? 35.297 -19.364 16.079 1.00 66.89 ? 441 THR B O 1 ATOM 7648 C CB . THR B 2 441 ? 32.601 -21.221 14.636 1.00 90.22 ? 441 THR B CB 1 ATOM 7649 O OG1 . THR B 2 441 ? 31.970 -19.942 14.822 1.00 97.25 ? 441 THR B OG1 1 ATOM 7650 C CG2 . THR B 2 441 ? 31.913 -22.280 15.493 1.00 91.13 ? 441 THR B CG2 1 ATOM 7651 N N . GLY B 2 442 ? 34.136 -18.826 14.247 1.00 92.42 ? 442 GLY B N 1 ATOM 7652 C CA . GLY B 2 442 ? 34.652 -17.470 14.231 1.00 89.62 ? 442 GLY B CA 1 ATOM 7653 C C . GLY B 2 442 ? 34.030 -16.500 15.215 1.00 79.70 ? 442 GLY B C 1 ATOM 7654 O O . GLY B 2 442 ? 34.659 -15.505 15.593 1.00 76.20 ? 442 GLY B O 1 ATOM 7655 N N . SER B 2 443 ? 32.795 -16.777 15.625 1.00 76.37 ? 443 SER B N 1 ATOM 7656 C CA . SER B 2 443 ? 32.095 -15.922 16.582 1.00 83.01 ? 443 SER B CA 1 ATOM 7657 C C . SER B 2 443 ? 32.932 -15.761 17.834 1.00 83.51 ? 443 SER B C 1 ATOM 7658 O O . SER B 2 443 ? 32.626 -14.949 18.703 1.00 82.41 ? 443 SER B O 1 ATOM 7659 C CB . SER B 2 443 ? 30.757 -16.538 16.958 1.00 85.29 ? 443 SER B CB 1 ATOM 7660 O OG . SER B 2 443 ? 30.939 -17.878 17.364 1.00 83.38 ? 443 SER B OG 1 ATOM 7661 N N . VAL B 2 444 ? 33.986 -16.563 17.908 1.00 81.04 ? 444 VAL B N 1 ATOM 7662 C CA . VAL B 2 444 ? 34.933 -16.540 19.000 1.00 76.28 ? 444 VAL B CA 1 ATOM 7663 C C . VAL B 2 444 ? 35.567 -15.154 19.168 1.00 86.81 ? 444 VAL B C 1 ATOM 7664 O O . VAL B 2 444 ? 36.120 -14.840 20.223 1.00 89.81 ? 444 VAL B O 1 ATOM 7665 C CB . VAL B 2 444 ? 36.027 -17.594 18.766 1.00 73.09 ? 444 VAL B CB 1 ATOM 7666 C CG1 . VAL B 2 444 ? 37.037 -17.086 17.751 1.00 65.11 ? 444 VAL B CG1 1 ATOM 7667 C CG2 . VAL B 2 444 ? 36.707 -17.960 20.074 1.00 79.92 ? 444 VAL B CG2 1 ATOM 7668 N N . PHE B 2 445 ? 35.478 -14.321 18.135 1.00 94.38 ? 445 PHE B N 1 ATOM 7669 C CA . PHE B 2 445 ? 36.028 -12.967 18.210 1.00 96.85 ? 445 PHE B CA 1 ATOM 7670 C C . PHE B 2 445 ? 35.015 -11.933 18.720 1.00 100.63 ? 445 PHE B C 1 ATOM 7671 O O . PHE B 2 445 ? 35.370 -10.782 18.963 1.00 97.98 ? 445 PHE B O 1 ATOM 7672 C CB . PHE B 2 445 ? 36.602 -12.541 16.858 1.00 89.79 ? 445 PHE B CB 1 ATOM 7673 C CG . PHE B 2 445 ? 37.778 -13.361 16.414 1.00 82.69 ? 445 PHE B CG 1 ATOM 7674 C CD1 . PHE B 2 445 ? 37.589 -14.525 15.676 1.00 80.13 ? 445 PHE B CD1 1 ATOM 7675 C CD2 . PHE B 2 445 ? 39.075 -12.970 16.733 1.00 77.30 ? 445 PHE B CD2 1 ATOM 7676 C CE1 . PHE B 2 445 ? 38.673 -15.290 15.261 1.00 83.55 ? 445 PHE B CE1 1 ATOM 7677 C CE2 . PHE B 2 445 ? 40.170 -13.724 16.320 1.00 79.33 ? 445 PHE B CE2 1 ATOM 7678 C CZ . PHE B 2 445 ? 39.969 -14.890 15.585 1.00 85.69 ? 445 PHE B CZ 1 ATOM 7679 N N . ARG B 2 446 ? 33.761 -12.354 18.876 1.00 106.21 ? 446 ARG B N 1 ATOM 7680 C CA . ARG B 2 446 ? 32.717 -11.519 19.469 1.00 110.76 ? 446 ARG B CA 1 ATOM 7681 C C . ARG B 2 446 ? 32.942 -11.369 20.967 1.00 110.07 ? 446 ARG B C 1 ATOM 7682 O O . ARG B 2 446 ? 32.429 -10.439 21.600 1.00 103.08 ? 446 ARG B O 1 ATOM 7683 C CB . ARG B 2 446 ? 31.339 -12.150 19.251 1.00 116.80 ? 446 ARG B CB 1 ATOM 7684 C CG . ARG B 2 446 ? 30.681 -11.822 17.926 1.00 129.29 ? 446 ARG B CG 1 ATOM 7685 C CD . ARG B 2 446 ? 29.263 -12.383 17.859 1.00 134.41 ? 446 ARG B CD 1 ATOM 7686 N NE . ARG B 2 446 ? 28.533 -11.886 16.693 1.00 138.08 ? 446 ARG B NE 1 ATOM 7687 C CZ . ARG B 2 446 ? 28.437 -12.536 15.535 1.00 136.19 ? 446 ARG B CZ 1 ATOM 7688 N NH1 . ARG B 2 446 ? 29.022 -13.718 15.383 1.00 130.58 ? 446 ARG B NH1 1 ATOM 7689 N NH2 . ARG B 2 446 ? 27.754 -12.006 14.526 1.00 134.60 ? 446 ARG B NH2 1 ATOM 7690 N N . CYS B 2 447 ? 33.717 -12.298 21.521 1.00 105.13 ? 447 CYS B N 1 ATOM 7691 C CA . CYS B 2 447 ? 33.853 -12.437 22.963 1.00 101.04 ? 447 CYS B CA 1 ATOM 7692 C C . CYS B 2 447 ? 35.279 -12.827 23.362 1.00 85.89 ? 447 CYS B C 1 ATOM 7693 O O . CYS B 2 447 ? 35.608 -14.010 23.447 1.00 83.84 ? 447 CYS B O 1 ATOM 7694 C CB . CYS B 2 447 ? 32.851 -13.490 23.456 1.00 106.91 ? 447 CYS B CB 1 ATOM 7695 S SG . CYS B 2 447 ? 32.626 -13.638 25.256 1.00 106.99 ? 447 CYS B SG 1 ATOM 7696 N N . LEU B 2 448 ? 36.124 -11.833 23.602 1.00 72.80 ? 448 LEU B N 1 ATOM 7697 C CA . LEU B 2 448 ? 37.495 -12.091 24.034 1.00 73.58 ? 448 LEU B CA 1 ATOM 7698 C C . LEU B 2 448 ? 37.930 -11.092 25.096 1.00 81.20 ? 448 LEU B C 1 ATOM 7699 O O . LEU B 2 448 ? 37.570 -9.917 25.035 1.00 81.22 ? 448 LEU B O 1 ATOM 7700 C CB . LEU B 2 448 ? 38.465 -12.036 22.851 1.00 73.13 ? 448 LEU B CB 1 ATOM 7701 C CG . LEU B 2 448 ? 38.331 -13.084 21.744 1.00 73.67 ? 448 LEU B CG 1 ATOM 7702 C CD1 . LEU B 2 448 ? 38.805 -12.499 20.424 1.00 82.31 ? 448 LEU B CD1 1 ATOM 7703 C CD2 . LEU B 2 448 ? 39.069 -14.387 22.069 1.00 60.51 ? 448 LEU B CD2 1 ATOM 7704 N N . PRO B 2 449 ? 38.714 -11.563 26.075 1.00 89.62 ? 449 PRO B N 1 ATOM 7705 C CA . PRO B 2 449 ? 39.187 -10.745 27.197 1.00 98.65 ? 449 PRO B CA 1 ATOM 7706 C C . PRO B 2 449 ? 39.717 -9.381 26.747 1.00 98.87 ? 449 PRO B C 1 ATOM 7707 O O . PRO B 2 449 ? 40.558 -9.310 25.855 1.00 90.68 ? 449 PRO B O 1 ATOM 7708 C CB . PRO B 2 449 ? 40.313 -11.595 27.786 1.00 99.18 ? 449 PRO B CB 1 ATOM 7709 C CG . PRO B 2 449 ? 39.913 -12.993 27.480 1.00 92.11 ? 449 PRO B CG 1 ATOM 7710 C CD . PRO B 2 449 ? 39.209 -12.948 26.153 1.00 86.32 ? 449 PRO B CD 1 ATOM 7711 N N . PRO B 2 450 ? 39.218 -8.302 27.364 1.00 101.28 ? 450 PRO B N 1 ATOM 7712 C CA . PRO B 2 450 ? 39.577 -6.940 26.961 1.00 99.74 ? 450 PRO B CA 1 ATOM 7713 C C . PRO B 2 450 ? 41.063 -6.767 26.633 1.00 91.01 ? 450 PRO B C 1 ATOM 7714 O O . PRO B 2 450 ? 41.392 -6.417 25.504 1.00 92.50 ? 450 PRO B O 1 ATOM 7715 C CB . PRO B 2 450 ? 39.189 -6.110 28.186 1.00 104.09 ? 450 PRO B CB 1 ATOM 7716 C CG . PRO B 2 450 ? 38.019 -6.845 28.763 1.00 100.80 ? 450 PRO B CG 1 ATOM 7717 C CD . PRO B 2 450 ? 38.273 -8.312 28.497 1.00 101.52 ? 450 PRO B CD 1 ATOM 7718 N N . LYS B 2 451 ? 41.946 -7.026 27.591 1.00 81.51 ? 451 LYS B N 1 ATOM 7719 C CA . LYS B 2 451 ? 43.356 -6.688 27.422 1.00 81.99 ? 451 LYS B CA 1 ATOM 7720 C C . LYS B 2 451 ? 44.253 -7.867 27.007 1.00 84.08 ? 451 LYS B C 1 ATOM 7721 O O . LYS B 2 451 ? 45.393 -7.954 27.476 1.00 78.59 ? 451 LYS B O 1 ATOM 7722 C CB . LYS B 2 451 ? 43.909 -6.062 28.719 1.00 90.20 ? 451 LYS B CB 1 ATOM 7723 C CG . LYS B 2 451 ? 43.330 -4.694 29.118 1.00 97.31 ? 451 LYS B CG 1 ATOM 7724 C CD . LYS B 2 451 ? 44.012 -3.537 28.360 1.00 104.42 ? 451 LYS B CD 1 ATOM 7725 C CE . LYS B 2 451 ? 43.490 -2.147 28.774 1.00 99.60 ? 451 LYS B CE 1 ATOM 7726 N NZ . LYS B 2 451 ? 44.262 -1.485 29.885 1.00 91.78 ? 451 LYS B NZ 1 ATOM 7727 N N . VAL B 2 452 ? 43.776 -8.762 26.135 1.00 80.86 ? 452 VAL B N 1 ATOM 7728 C CA . VAL B 2 452 ? 44.583 -9.944 25.784 1.00 79.00 ? 452 VAL B CA 1 ATOM 7729 C C . VAL B 2 452 ? 45.911 -9.584 25.133 1.00 82.45 ? 452 VAL B C 1 ATOM 7730 O O . VAL B 2 452 ? 46.010 -8.577 24.438 1.00 99.99 ? 452 VAL B O 1 ATOM 7731 C CB . VAL B 2 452 ? 43.877 -10.916 24.821 1.00 77.02 ? 452 VAL B CB 1 ATOM 7732 C CG1 . VAL B 2 452 ? 44.446 -12.336 25.007 1.00 52.88 ? 452 VAL B CG1 1 ATOM 7733 C CG2 . VAL B 2 452 ? 42.380 -10.898 25.025 1.00 82.91 ? 452 VAL B CG2 1 ATOM 7734 N N . LYS B 2 453 ? 46.919 -10.427 25.339 1.00 68.09 ? 453 LYS B N 1 ATOM 7735 C CA . LYS B 2 453 ? 48.237 -10.210 24.757 1.00 72.41 ? 453 LYS B CA 1 ATOM 7736 C C . LYS B 2 453 ? 48.669 -11.416 23.935 1.00 86.54 ? 453 LYS B C 1 ATOM 7737 O O . LYS B 2 453 ? 49.507 -11.291 23.052 1.00 105.84 ? 453 LYS B O 1 ATOM 7738 C CB . LYS B 2 453 ? 49.284 -9.929 25.842 1.00 80.09 ? 453 LYS B CB 1 ATOM 7739 C CG . LYS B 2 453 ? 48.848 -8.916 26.916 1.00 101.76 ? 453 LYS B CG 1 ATOM 7740 C CD . LYS B 2 453 ? 48.688 -7.501 26.346 1.00 113.51 ? 453 LYS B CD 1 ATOM 7741 C CE . LYS B 2 453 ? 47.937 -6.564 27.295 1.00 110.33 ? 453 LYS B CE 1 ATOM 7742 N NZ . LYS B 2 453 ? 48.802 -6.018 28.364 1.00 110.86 ? 453 LYS B NZ 1 ATOM 7743 N N . VAL B 2 454 ? 48.114 -12.587 24.239 1.00 81.80 ? 454 VAL B N 1 ATOM 7744 C CA . VAL B 2 454 ? 48.433 -13.810 23.497 1.00 82.37 ? 454 VAL B CA 1 ATOM 7745 C C . VAL B 2 454 ? 47.140 -14.563 23.240 1.00 88.00 ? 454 VAL B C 1 ATOM 7746 O O . VAL B 2 454 ? 46.326 -14.722 24.145 1.00 93.18 ? 454 VAL B O 1 ATOM 7747 C CB . VAL B 2 454 ? 49.401 -14.743 24.269 1.00 75.54 ? 454 VAL B CB 1 ATOM 7748 C CG1 . VAL B 2 454 ? 49.924 -15.830 23.360 1.00 65.55 ? 454 VAL B CG1 1 ATOM 7749 C CG2 . VAL B 2 454 ? 50.559 -13.962 24.860 1.00 82.69 ? 454 VAL B CG2 1 ATOM 7750 N N . LEU B 2 455 ? 46.940 -15.023 22.010 1.00 88.07 ? 455 LEU B N 1 ATOM 7751 C CA . LEU B 2 455 ? 45.698 -15.705 21.670 1.00 82.36 ? 455 LEU B CA 1 ATOM 7752 C C . LEU B 2 455 ? 45.952 -16.899 20.765 1.00 82.77 ? 455 LEU B C 1 ATOM 7753 O O . LEU B 2 455 ? 45.985 -16.753 19.551 1.00 96.18 ? 455 LEU B O 1 ATOM 7754 C CB . LEU B 2 455 ? 44.731 -14.727 20.999 1.00 78.55 ? 455 LEU B CB 1 ATOM 7755 C CG . LEU B 2 455 ? 43.263 -15.140 20.901 1.00 77.00 ? 455 LEU B CG 1 ATOM 7756 C CD1 . LEU B 2 455 ? 42.735 -15.581 22.256 1.00 79.22 ? 455 LEU B CD1 1 ATOM 7757 C CD2 . LEU B 2 455 ? 42.420 -14.000 20.351 1.00 69.55 ? 455 LEU B CD2 1 ATOM 7758 N N . ASP B 2 456 ? 46.131 -18.080 21.352 1.00 76.85 ? 456 ASP B N 1 ATOM 7759 C CA . ASP B 2 456 ? 46.396 -19.278 20.562 1.00 81.41 ? 456 ASP B CA 1 ATOM 7760 C C . ASP B 2 456 ? 45.113 -20.002 20.132 1.00 82.40 ? 456 ASP B C 1 ATOM 7761 O O . ASP B 2 456 ? 44.531 -20.771 20.895 1.00 89.59 ? 456 ASP B O 1 ATOM 7762 C CB . ASP B 2 456 ? 47.335 -20.232 21.303 1.00 82.74 ? 456 ASP B CB 1 ATOM 7763 C CG . ASP B 2 456 ? 47.992 -21.233 20.369 1.00 93.83 ? 456 ASP B CG 1 ATOM 7764 O OD1 . ASP B 2 456 ? 47.296 -21.719 19.454 1.00 90.58 ? 456 ASP B OD1 1 ATOM 7765 O OD2 . ASP B 2 456 ? 49.200 -21.520 20.529 1.00 98.82 ? 456 ASP B OD2 1 ATOM 7766 N N . LEU B 2 457 ? 44.688 -19.753 18.899 1.00 74.95 ? 457 LEU B N 1 ATOM 7767 C CA . LEU B 2 457 ? 43.459 -20.334 18.366 1.00 74.84 ? 457 LEU B CA 1 ATOM 7768 C C . LEU B 2 457 ? 43.712 -21.394 17.298 1.00 72.94 ? 457 LEU B C 1 ATOM 7769 O O . LEU B 2 457 ? 42.811 -21.719 16.531 1.00 66.32 ? 457 LEU B O 1 ATOM 7770 C CB . LEU B 2 457 ? 42.558 -19.243 17.779 1.00 70.51 ? 457 LEU B CB 1 ATOM 7771 C CG . LEU B 2 457 ? 41.388 -18.754 18.632 1.00 72.66 ? 457 LEU B CG 1 ATOM 7772 C CD1 . LEU B 2 457 ? 40.865 -17.411 18.138 1.00 73.51 ? 457 LEU B CD1 1 ATOM 7773 C CD2 . LEU B 2 457 ? 40.280 -19.794 18.646 1.00 70.12 ? 457 LEU B CD2 1 ATOM 7774 N N . HIS B 2 458 ? 44.924 -21.937 17.247 1.00 71.87 ? 458 HIS B N 1 ATOM 7775 C CA . HIS B 2 458 ? 45.258 -22.907 16.211 1.00 70.07 ? 458 HIS B CA 1 ATOM 7776 C C . HIS B 2 458 ? 44.514 -24.221 16.390 1.00 68.67 ? 458 HIS B C 1 ATOM 7777 O O . HIS B 2 458 ? 44.071 -24.556 17.480 1.00 60.93 ? 458 HIS B O 1 ATOM 7778 C CB . HIS B 2 458 ? 46.771 -23.147 16.123 1.00 74.03 ? 458 HIS B CB 1 ATOM 7779 C CG . HIS B 2 458 ? 47.296 -24.149 17.106 1.00 70.49 ? 458 HIS B CG 1 ATOM 7780 N ND1 . HIS B 2 458 ? 47.942 -23.783 18.267 1.00 74.17 ? 458 HIS B ND1 1 ATOM 7781 C CD2 . HIS B 2 458 ? 47.297 -25.502 17.085 1.00 66.97 ? 458 HIS B CD2 1 ATOM 7782 C CE1 . HIS B 2 458 ? 48.304 -24.869 18.928 1.00 75.60 ? 458 HIS B CE1 1 ATOM 7783 N NE2 . HIS B 2 458 ? 47.926 -25.925 18.233 1.00 69.36 ? 458 HIS B NE2 1 ATOM 7784 N N . ASN B 2 459 ? 44.382 -24.955 15.296 1.00 79.58 ? 459 ASN B N 1 ATOM 7785 C CA . ASN B 2 459 ? 43.686 -26.230 15.305 1.00 80.16 ? 459 ASN B CA 1 ATOM 7786 C C . ASN B 2 459 ? 42.206 -26.078 15.654 1.00 75.29 ? 459 ASN B C 1 ATOM 7787 O O . ASN B 2 459 ? 41.617 -26.900 16.356 1.00 76.53 ? 459 ASN B O 1 ATOM 7788 C CB . ASN B 2 459 ? 44.387 -27.219 16.235 1.00 76.91 ? 459 ASN B CB 1 ATOM 7789 C CG . ASN B 2 459 ? 44.050 -28.659 15.910 1.00 81.36 ? 459 ASN B CG 1 ATOM 7790 O OD1 . ASN B 2 459 ? 43.568 -28.963 14.819 1.00 64.27 ? 459 ASN B OD1 1 ATOM 7791 N ND2 . ASN B 2 459 ? 44.302 -29.559 16.860 1.00 94.14 ? 459 ASN B ND2 1 ATOM 7792 N N . ASN B 2 460 ? 41.599 -25.024 15.140 1.00 72.29 ? 460 ASN B N 1 ATOM 7793 C CA . ASN B 2 460 ? 40.162 -24.876 15.272 1.00 87.94 ? 460 ASN B CA 1 ATOM 7794 C C . ASN B 2 460 ? 39.391 -24.909 13.946 1.00 89.72 ? 460 ASN B C 1 ATOM 7795 O O . ASN B 2 460 ? 39.843 -25.507 12.970 1.00 93.90 ? 460 ASN B O 1 ATOM 7796 C CB . ASN B 2 460 ? 39.833 -23.630 16.079 1.00 96.09 ? 460 ASN B CB 1 ATOM 7797 C CG . ASN B 2 460 ? 39.902 -23.879 17.561 1.00 87.89 ? 460 ASN B CG 1 ATOM 7798 O OD1 . ASN B 2 460 ? 40.741 -23.314 18.259 1.00 94.12 ? 460 ASN B OD1 1 ATOM 7799 N ND2 . ASN B 2 460 ? 39.023 -24.739 18.053 1.00 75.79 ? 460 ASN B ND2 1 ATOM 7800 N N . ARG B 2 461 ? 38.223 -24.279 13.922 1.00 78.51 ? 461 ARG B N 1 ATOM 7801 C CA . ARG B 2 461 ? 37.326 -24.417 12.786 1.00 81.69 ? 461 ARG B CA 1 ATOM 7802 C C . ARG B 2 461 ? 36.751 -23.078 12.337 1.00 94.13 ? 461 ARG B C 1 ATOM 7803 O O . ARG B 2 461 ? 35.544 -22.945 12.125 1.00 91.29 ? 461 ARG B O 1 ATOM 7804 C CB . ARG B 2 461 ? 36.209 -25.410 13.116 1.00 74.10 ? 461 ARG B CB 1 ATOM 7805 C CG . ARG B 2 461 ? 36.730 -26.762 13.553 1.00 81.81 ? 461 ARG B CG 1 ATOM 7806 C CD . ARG B 2 461 ? 35.849 -27.886 13.045 1.00 106.90 ? 461 ARG B CD 1 ATOM 7807 N NE . ARG B 2 461 ? 36.646 -29.037 12.614 1.00 125.01 ? 461 ARG B NE 1 ATOM 7808 C CZ . ARG B 2 461 ? 36.616 -30.233 13.196 1.00 125.96 ? 461 ARG B CZ 1 ATOM 7809 N NH1 . ARG B 2 461 ? 35.814 -30.439 14.233 1.00 129.43 ? 461 ARG B NH1 1 ATOM 7810 N NH2 . ARG B 2 461 ? 37.378 -31.221 12.736 1.00 114.54 ? 461 ARG B NH2 1 ATOM 7811 N N . ILE B 2 462 ? 37.634 -22.099 12.166 1.00 100.06 ? 462 ILE B N 1 ATOM 7812 C CA . ILE B 2 462 ? 37.233 -20.734 11.859 1.00 103.86 ? 462 ILE B CA 1 ATOM 7813 C C . ILE B 2 462 ? 37.294 -20.372 10.377 1.00 119.30 ? 462 ILE B C 1 ATOM 7814 O O . ILE B 2 462 ? 38.371 -20.372 9.784 1.00 123.21 ? 462 ILE B O 1 ATOM 7815 C CB . ILE B 2 462 ? 38.126 -19.738 12.602 1.00 94.72 ? 462 ILE B CB 1 ATOM 7816 C CG1 . ILE B 2 462 ? 38.102 -20.028 14.109 1.00 85.48 ? 462 ILE B CG1 1 ATOM 7817 C CG2 . ILE B 2 462 ? 37.701 -18.308 12.280 1.00 93.69 ? 462 ILE B CG2 1 ATOM 7818 C CD1 . ILE B 2 462 ? 39.283 -19.446 14.880 1.00 75.48 ? 462 ILE B CD1 1 ATOM 7819 N N . MET B 2 463 ? 36.134 -20.069 9.791 1.00 127.62 ? 463 MET B N 1 ATOM 7820 C CA . MET B 2 463 ? 36.050 -19.354 8.516 1.00 129.15 ? 463 MET B CA 1 ATOM 7821 C C . MET B 2 463 ? 35.287 -18.084 8.830 1.00 132.98 ? 463 MET B C 1 ATOM 7822 O O . MET B 2 463 ? 35.705 -16.970 8.508 1.00 118.98 ? 463 MET B O 1 ATOM 7823 C CB . MET B 2 463 ? 35.232 -20.130 7.495 1.00 131.03 ? 463 MET B CB 1 ATOM 7824 C CG . MET B 2 463 ? 35.343 -21.637 7.569 1.00 134.18 ? 463 MET B CG 1 ATOM 7825 S SD . MET B 2 463 ? 33.806 -22.418 7.016 1.00 114.32 ? 463 MET B SD 1 ATOM 7826 C CE . MET B 2 463 ? 33.123 -21.112 5.982 1.00 87.61 ? 463 MET B CE 1 ATOM 7827 N N . SER B 2 464 ? 34.143 -18.297 9.470 1.00 149.98 ? 464 SER B N 1 ATOM 7828 C CA . SER B 2 464 ? 33.277 -17.242 9.972 1.00 164.01 ? 464 SER B CA 1 ATOM 7829 C C . SER B 2 464 ? 34.029 -16.163 10.786 1.00 173.78 ? 464 SER B C 1 ATOM 7830 O O . SER B 2 464 ? 34.065 -16.250 12.005 1.00 177.51 ? 464 SER B O 1 ATOM 7831 C CB . SER B 2 464 ? 32.138 -17.885 10.805 1.00 82.45 ? 464 SER B CB 1 ATOM 7832 O OG . SER B 2 464 ? 32.360 -19.278 11.033 1.00 48.91 ? 464 SER B OG 1 ATOM 7833 N N . ILE B 2 465 ? 34.624 -15.157 10.131 1.00 174.02 ? 465 ILE B N 1 ATOM 7834 C CA . ILE B 2 465 ? 35.243 -14.023 10.857 1.00 173.80 ? 465 ILE B CA 1 ATOM 7835 C C . ILE B 2 465 ? 34.365 -12.765 10.889 1.00 170.02 ? 465 ILE B C 1 ATOM 7836 O O . ILE B 2 465 ? 33.855 -12.333 9.854 1.00 170.10 ? 465 ILE B O 1 ATOM 7837 C CB . ILE B 2 465 ? 36.636 -13.600 10.304 1.00 89.08 ? 465 ILE B CB 1 ATOM 7838 C CG1 . ILE B 2 465 ? 37.677 -14.692 10.515 1.00 89.47 ? 465 ILE B CG1 1 ATOM 7839 C CG2 . ILE B 2 465 ? 37.134 -12.312 11.004 1.00 73.47 ? 465 ILE B CG2 1 ATOM 7840 C CD1 . ILE B 2 465 ? 39.059 -14.123 10.846 1.00 79.48 ? 465 ILE B CD1 1 ATOM 7841 N N . PRO B 2 466 ? 34.203 -12.164 12.082 1.00 162.83 ? 466 PRO B N 1 ATOM 7842 C CA . PRO B 2 466 ? 33.393 -10.958 12.282 1.00 162.28 ? 466 PRO B CA 1 ATOM 7843 C C . PRO B 2 466 ? 34.205 -9.667 12.202 1.00 161.90 ? 466 PRO B C 1 ATOM 7844 O O . PRO B 2 466 ? 35.425 -9.702 12.013 1.00 159.04 ? 466 PRO B O 1 ATOM 7845 C CB . PRO B 2 466 ? 32.865 -11.124 13.717 1.00 158.44 ? 466 PRO B CB 1 ATOM 7846 C CG . PRO B 2 466 ? 33.427 -12.439 14.225 1.00 156.46 ? 466 PRO B CG 1 ATOM 7847 C CD . PRO B 2 466 ? 34.608 -12.742 13.369 1.00 157.94 ? 466 PRO B CD 1 ATOM 7848 N N . LYS B 2 467 ? 33.509 -8.542 12.359 1.00 162.15 ? 467 LYS B N 1 ATOM 7849 C CA . LYS B 2 467 ? 34.116 -7.211 12.373 1.00 161.51 ? 467 LYS B CA 1 ATOM 7850 C C . LYS B 2 467 ? 34.409 -6.745 13.804 1.00 177.34 ? 467 LYS B C 1 ATOM 7851 O O . LYS B 2 467 ? 34.263 -5.563 14.128 1.00 179.33 ? 467 LYS B O 1 ATOM 7852 C CB . LYS B 2 467 ? 33.201 -6.201 11.670 1.00 147.59 ? 467 LYS B CB 1 ATOM 7853 C CG . LYS B 2 467 ? 31.722 -6.310 12.049 1.00 141.93 ? 467 LYS B CG 1 ATOM 7854 C CD . LYS B 2 467 ? 31.064 -7.531 11.407 1.00 139.38 ? 467 LYS B CD 1 ATOM 7855 C CE . LYS B 2 467 ? 29.665 -7.782 11.947 1.00 135.82 ? 467 LYS B CE 1 ATOM 7856 N NZ . LYS B 2 467 ? 29.194 -9.156 11.607 1.00 130.06 ? 467 LYS B NZ 1 ATOM 7857 N N . ASP B 2 468 ? 34.822 -7.687 14.652 1.00 183.45 ? 468 ASP B N 1 ATOM 7858 C CA . ASP B 2 468 ? 35.133 -7.404 16.051 1.00 184.31 ? 468 ASP B CA 1 ATOM 7859 C C . ASP B 2 468 ? 36.600 -7.678 16.372 1.00 191.07 ? 468 ASP B C 1 ATOM 7860 O O . ASP B 2 468 ? 36.991 -7.676 17.540 1.00 194.74 ? 468 ASP B O 1 ATOM 7861 C CB . ASP B 2 468 ? 34.249 -8.244 16.977 1.00 180.42 ? 468 ASP B CB 1 ATOM 7862 C CG . ASP B 2 468 ? 32.889 -7.621 17.213 1.00 183.78 ? 468 ASP B CG 1 ATOM 7863 O OD1 . ASP B 2 468 ? 32.764 -6.389 17.055 1.00 189.21 ? 468 ASP B OD1 1 ATOM 7864 O OD2 . ASP B 2 468 ? 31.947 -8.364 17.563 1.00 181.03 ? 468 ASP B OD2 1 ATOM 7865 N N . VAL B 2 469 ? 37.405 -7.915 15.338 1.00 195.27 ? 469 VAL B N 1 ATOM 7866 C CA . VAL B 2 469 ? 38.819 -8.249 15.519 1.00 195.30 ? 469 VAL B CA 1 ATOM 7867 C C . VAL B 2 469 ? 39.670 -7.005 15.783 1.00 195.14 ? 469 VAL B C 1 ATOM 7868 O O . VAL B 2 469 ? 40.870 -7.104 16.047 1.00 191.15 ? 469 VAL B O 1 ATOM 7869 C CB . VAL B 2 469 ? 39.399 -9.006 14.294 1.00 156.48 ? 469 VAL B CB 1 ATOM 7870 C CG1 . VAL B 2 469 ? 40.577 -9.883 14.716 1.00 145.01 ? 469 VAL B CG1 1 ATOM 7871 C CG2 . VAL B 2 469 ? 38.319 -9.843 13.604 1.00 158.61 ? 469 VAL B CG2 1 ATOM 7872 N N . THR B 2 470 ? 39.043 -5.834 15.709 1.00 198.57 ? 470 THR B N 1 ATOM 7873 C CA . THR B 2 470 ? 39.740 -4.573 15.943 1.00 201.76 ? 470 THR B CA 1 ATOM 7874 C C . THR B 2 470 ? 39.212 -3.831 17.180 1.00 205.40 ? 470 THR B C 1 ATOM 7875 O O . THR B 2 470 ? 39.704 -2.754 17.522 1.00 208.29 ? 470 THR B O 1 ATOM 7876 C CB . THR B 2 470 ? 39.676 -3.650 14.705 1.00 201.45 ? 470 THR B CB 1 ATOM 7877 O OG1 . THR B 2 470 ? 38.318 -3.530 14.263 1.00 202.12 ? 470 THR B OG1 1 ATOM 7878 C CG2 . THR B 2 470 ? 40.524 -4.215 13.571 1.00 198.28 ? 470 THR B CG2 1 ATOM 7879 N N . HIS B 2 471 ? 38.209 -4.408 17.840 1.00 200.65 ? 471 HIS B N 1 ATOM 7880 C CA . HIS B 2 471 ? 37.686 -3.862 19.092 1.00 187.35 ? 471 HIS B CA 1 ATOM 7881 C C . HIS B 2 471 ? 38.434 -4.505 20.259 1.00 171.54 ? 471 HIS B C 1 ATOM 7882 O O . HIS B 2 471 ? 38.004 -4.439 21.412 1.00 170.01 ? 471 HIS B O 1 ATOM 7883 C CB . HIS B 2 471 ? 36.174 -4.109 19.212 1.00 183.06 ? 471 HIS B CB 1 ATOM 7884 C CG . HIS B 2 471 ? 35.365 -3.482 18.114 1.00 179.30 ? 471 HIS B CG 1 ATOM 7885 N ND1 . HIS B 2 471 ? 34.928 -4.188 17.011 1.00 176.83 ? 471 HIS B ND1 1 ATOM 7886 C CD2 . HIS B 2 471 ? 34.912 -2.217 17.950 1.00 174.00 ? 471 HIS B CD2 1 ATOM 7887 C CE1 . HIS B 2 471 ? 34.246 -3.384 16.216 1.00 171.67 ? 471 HIS B CE1 1 ATOM 7888 N NE2 . HIS B 2 471 ? 34.221 -2.182 16.762 1.00 171.54 ? 471 HIS B NE2 1 ATOM 7889 N N . LEU B 2 472 ? 39.564 -5.125 19.932 1.00 156.67 ? 472 LEU B N 1 ATOM 7890 C CA . LEU B 2 472 ? 40.376 -5.863 20.889 1.00 141.04 ? 472 LEU B CA 1 ATOM 7891 C C . LEU B 2 472 ? 41.847 -5.708 20.497 1.00 131.38 ? 472 LEU B C 1 ATOM 7892 O O . LEU B 2 472 ? 42.472 -6.632 19.963 1.00 119.26 ? 472 LEU B O 1 ATOM 7893 C CB . LEU B 2 472 ? 39.938 -7.325 20.895 1.00 135.62 ? 472 LEU B CB 1 ATOM 7894 C CG . LEU B 2 472 ? 38.437 -7.447 21.206 1.00 133.42 ? 472 LEU B CG 1 ATOM 7895 C CD1 . LEU B 2 472 ? 37.816 -8.732 20.667 1.00 124.68 ? 472 LEU B CD1 1 ATOM 7896 C CD2 . LEU B 2 472 ? 38.162 -7.276 22.710 1.00 132.72 ? 472 LEU B CD2 1 ATOM 7897 N N . GLN B 2 473 ? 42.379 -4.520 20.790 1.00 132.26 ? 473 GLN B N 1 ATOM 7898 C CA . GLN B 2 473 ? 43.626 -4.017 20.208 1.00 127.16 ? 473 GLN B CA 1 ATOM 7899 C C . GLN B 2 473 ? 44.791 -3.994 21.192 1.00 109.16 ? 473 GLN B C 1 ATOM 7900 O O . GLN B 2 473 ? 45.136 -2.943 21.731 1.00 92.66 ? 473 GLN B O 1 ATOM 7901 C CB . GLN B 2 473 ? 43.416 -2.582 19.699 1.00 137.45 ? 473 GLN B CB 1 ATOM 7902 C CG . GLN B 2 473 ? 41.999 -2.267 19.213 1.00 143.09 ? 473 GLN B CG 1 ATOM 7903 C CD . GLN B 2 473 ? 41.636 -0.789 19.349 1.00 144.86 ? 473 GLN B CD 1 ATOM 7904 O OE1 . GLN B 2 473 ? 42.460 0.031 19.758 1.00 147.12 ? 473 GLN B OE1 1 ATOM 7905 N NE2 . GLN B 2 473 ? 40.394 -0.447 19.013 1.00 138.60 ? 473 GLN B NE2 1 ATOM 7906 N N . ALA B 2 474 ? 45.416 -5.139 21.415 1.00 107.45 ? 474 ALA B N 1 ATOM 7907 C CA . ALA B 2 474 ? 46.513 -5.184 22.369 1.00 100.44 ? 474 ALA B CA 1 ATOM 7908 C C . ALA B 2 474 ? 47.299 -6.474 22.256 1.00 95.15 ? 474 ALA B C 1 ATOM 7909 O O . ALA B 2 474 ? 48.288 -6.659 22.985 1.00 88.32 ? 474 ALA B O 1 ATOM 7910 C CB . ALA B 2 474 ? 45.991 -5.010 23.785 1.00 90.70 ? 474 ALA B CB 1 ATOM 7911 N N . LEU B 2 475 ? 46.858 -7.358 21.352 1.00 75.46 ? 475 LEU B N 1 ATOM 7912 C CA . LEU B 2 475 ? 47.553 -8.618 21.120 1.00 74.77 ? 475 LEU B CA 1 ATOM 7913 C C . LEU B 2 475 ? 48.994 -8.391 20.667 1.00 89.72 ? 475 LEU B C 1 ATOM 7914 O O . LEU B 2 475 ? 49.337 -7.328 20.160 1.00 99.44 ? 475 LEU B O 1 ATOM 7915 C CB . LEU B 2 475 ? 46.836 -9.455 20.068 1.00 85.89 ? 475 LEU B CB 1 ATOM 7916 C CG . LEU B 2 475 ? 45.420 -9.973 20.283 1.00 87.89 ? 475 LEU B CG 1 ATOM 7917 C CD1 . LEU B 2 475 ? 44.367 -9.099 19.562 1.00 74.83 ? 475 LEU B CD1 1 ATOM 7918 C CD2 . LEU B 2 475 ? 45.388 -11.403 19.770 1.00 85.85 ? 475 LEU B CD2 1 ATOM 7919 N N . GLN B 2 476 ? 49.830 -9.405 20.843 1.00 96.62 ? 476 GLN B N 1 ATOM 7920 C CA . GLN B 2 476 ? 51.220 -9.350 20.411 1.00 100.50 ? 476 GLN B CA 1 ATOM 7921 C C . GLN B 2 476 ? 51.517 -10.642 19.688 1.00 98.81 ? 476 GLN B C 1 ATOM 7922 O O . GLN B 2 476 ? 52.284 -10.672 18.731 1.00 114.83 ? 476 GLN B O 1 ATOM 7923 C CB . GLN B 2 476 ? 52.168 -9.227 21.604 1.00 104.21 ? 476 GLN B CB 1 ATOM 7924 C CG . GLN B 2 476 ? 51.935 -8.020 22.487 1.00 105.69 ? 476 GLN B CG 1 ATOM 7925 C CD . GLN B 2 476 ? 53.082 -7.794 23.450 1.00 100.75 ? 476 GLN B CD 1 ATOM 7926 O OE1 . GLN B 2 476 ? 53.406 -6.652 23.782 1.00 101.49 ? 476 GLN B OE1 1 ATOM 7927 N NE2 . GLN B 2 476 ? 53.717 -8.885 23.890 1.00 84.33 ? 476 GLN B NE2 1 ATOM 7928 N N . GLU B 2 477 ? 50.915 -11.718 20.174 1.00 84.12 ? 477 GLU B N 1 ATOM 7929 C CA . GLU B 2 477 ? 51.027 -13.008 19.528 1.00 84.55 ? 477 GLU B CA 1 ATOM 7930 C C . GLU B 2 477 ? 49.637 -13.409 19.081 1.00 85.21 ? 477 GLU B C 1 ATOM 7931 O O . GLU B 2 477 ? 48.636 -13.027 19.699 1.00 74.89 ? 477 GLU B O 1 ATOM 7932 C CB . GLU B 2 477 ? 51.615 -14.060 20.470 1.00 94.40 ? 477 GLU B CB 1 ATOM 7933 C CG . GLU B 2 477 ? 53.049 -13.784 20.915 1.00 106.60 ? 477 GLU B CG 1 ATOM 7934 C CD . GLU B 2 477 ? 53.710 -15.001 21.549 1.00 112.48 ? 477 GLU B CD 1 ATOM 7935 O OE1 . GLU B 2 477 ? 53.294 -16.141 21.231 1.00 115.53 ? 477 GLU B OE1 1 ATOM 7936 O OE2 . GLU B 2 477 ? 54.648 -14.816 22.358 1.00 106.37 ? 477 GLU B OE2 1 ATOM 7937 N N . LEU B 2 478 ? 49.592 -14.153 17.980 1.00 89.04 ? 478 LEU B N 1 ATOM 7938 C CA . LEU B 2 478 ? 48.344 -14.616 17.395 1.00 79.34 ? 478 LEU B CA 1 ATOM 7939 C C . LEU B 2 478 ? 48.585 -15.883 16.604 1.00 86.62 ? 478 LEU B C 1 ATOM 7940 O O . LEU B 2 478 ? 49.568 -15.997 15.884 1.00 99.61 ? 478 LEU B O 1 ATOM 7941 C CB . LEU B 2 478 ? 47.745 -13.562 16.473 1.00 65.12 ? 478 LEU B CB 1 ATOM 7942 C CG . LEU B 2 478 ? 46.374 -14.013 15.985 1.00 66.33 ? 478 LEU B CG 1 ATOM 7943 C CD1 . LEU B 2 478 ? 45.594 -14.617 17.155 1.00 57.93 ? 478 LEU B CD1 1 ATOM 7944 C CD2 . LEU B 2 478 ? 45.612 -12.863 15.350 1.00 63.18 ? 478 LEU B CD2 1 ATOM 7945 N N . ASN B 2 479 ? 47.682 -16.839 16.740 1.00 79.09 ? 479 ASN B N 1 ATOM 7946 C CA . ASN B 2 479 ? 47.812 -18.084 16.020 1.00 73.74 ? 479 ASN B CA 1 ATOM 7947 C C . ASN B 2 479 ? 46.464 -18.549 15.511 1.00 76.77 ? 479 ASN B C 1 ATOM 7948 O O . ASN B 2 479 ? 45.678 -19.132 16.245 1.00 73.58 ? 479 ASN B O 1 ATOM 7949 C CB . ASN B 2 479 ? 48.462 -19.151 16.896 1.00 71.35 ? 479 ASN B CB 1 ATOM 7950 C CG . ASN B 2 479 ? 48.769 -20.417 16.127 1.00 83.40 ? 479 ASN B CG 1 ATOM 7951 O OD1 . ASN B 2 479 ? 48.221 -20.655 15.044 1.00 78.78 ? 479 ASN B OD1 1 ATOM 7952 N ND2 . ASN B 2 479 ? 49.655 -21.238 16.677 1.00 88.26 ? 479 ASN B ND2 1 ATOM 7953 N N . VAL B 2 480 ? 46.195 -18.261 14.246 1.00 86.18 ? 480 VAL B N 1 ATOM 7954 C CA . VAL B 2 480 ? 44.975 -18.716 13.609 1.00 87.44 ? 480 VAL B CA 1 ATOM 7955 C C . VAL B 2 480 ? 45.325 -19.826 12.636 1.00 88.23 ? 480 VAL B C 1 ATOM 7956 O O . VAL B 2 480 ? 44.560 -20.124 11.720 1.00 91.40 ? 480 VAL B O 1 ATOM 7957 C CB . VAL B 2 480 ? 44.288 -17.581 12.854 1.00 91.59 ? 480 VAL B CB 1 ATOM 7958 C CG1 . VAL B 2 480 ? 43.635 -16.616 13.831 1.00 91.16 ? 480 VAL B CG1 1 ATOM 7959 C CG2 . VAL B 2 480 ? 45.299 -16.858 11.987 1.00 96.83 ? 480 VAL B CG2 1 ATOM 7960 N N . ALA B 2 481 ? 46.490 -20.434 12.849 1.00 84.74 ? 481 ALA B N 1 ATOM 7961 C CA . ALA B 2 481 ? 46.968 -21.524 12.004 1.00 86.89 ? 481 ALA B CA 1 ATOM 7962 C C . ALA B 2 481 ? 45.972 -22.681 11.927 1.00 85.78 ? 481 ALA B C 1 ATOM 7963 O O . ALA B 2 481 ? 44.884 -22.612 12.489 1.00 87.37 ? 481 ALA B O 1 ATOM 7964 C CB . ALA B 2 481 ? 48.317 -22.017 12.498 1.00 87.66 ? 481 ALA B CB 1 ATOM 7965 N N . SER B 2 482 ? 46.359 -23.744 11.229 1.00 86.72 ? 482 SER B N 1 ATOM 7966 C CA . SER B 2 482 ? 45.518 -24.934 11.050 1.00 86.22 ? 482 SER B CA 1 ATOM 7967 C C . SER B 2 482 ? 44.013 -24.716 11.230 1.00 86.94 ? 482 SER B C 1 ATOM 7968 O O . SER B 2 482 ? 43.389 -25.392 12.052 1.00 85.92 ? 482 SER B O 1 ATOM 7969 C CB . SER B 2 482 ? 45.986 -26.077 11.958 1.00 73.93 ? 482 SER B CB 1 ATOM 7970 O OG . SER B 2 482 ? 47.076 -26.779 11.381 1.00 70.38 ? 482 SER B OG 1 ATOM 7971 N N . ASN B 2 483 ? 43.438 -23.793 10.456 1.00 79.76 ? 483 ASN B N 1 ATOM 7972 C CA . ASN B 2 483 ? 41.991 -23.564 10.467 1.00 75.66 ? 483 ASN B CA 1 ATOM 7973 C C . ASN B 2 483 ? 41.290 -23.818 9.121 1.00 87.25 ? 483 ASN B C 1 ATOM 7974 O O . ASN B 2 483 ? 41.696 -24.686 8.345 1.00 91.29 ? 483 ASN B O 1 ATOM 7975 C CB . ASN B 2 483 ? 41.658 -22.164 10.994 1.00 78.77 ? 483 ASN B CB 1 ATOM 7976 C CG . ASN B 2 483 ? 41.549 -22.119 12.515 1.00 81.34 ? 483 ASN B CG 1 ATOM 7977 O OD1 . ASN B 2 483 ? 42.539 -22.274 13.220 1.00 77.24 ? 483 ASN B OD1 1 ATOM 7978 N ND2 . ASN B 2 483 ? 40.339 -21.905 13.022 1.00 80.37 ? 483 ASN B ND2 1 ATOM 7979 N N . GLN B 2 484 ? 40.225 -23.063 8.864 1.00 89.19 ? 484 GLN B N 1 ATOM 7980 C CA . GLN B 2 484 ? 39.444 -23.203 7.638 1.00 91.94 ? 484 GLN B CA 1 ATOM 7981 C C . GLN B 2 484 ? 39.241 -21.850 6.945 1.00 97.48 ? 484 GLN B C 1 ATOM 7982 O O . GLN B 2 484 ? 38.280 -21.663 6.184 1.00 84.79 ? 484 GLN B O 1 ATOM 7983 C CB . GLN B 2 484 ? 38.077 -23.812 7.952 1.00 94.87 ? 484 GLN B CB 1 ATOM 7984 C CG . GLN B 2 484 ? 38.105 -25.174 8.621 1.00 101.37 ? 484 GLN B CG 1 ATOM 7985 C CD . GLN B 2 484 ? 36.714 -25.796 8.705 1.00 109.58 ? 484 GLN B CD 1 ATOM 7986 O OE1 . GLN B 2 484 ? 35.794 -25.378 7.995 1.00 110.32 ? 484 GLN B OE1 1 ATOM 7987 N NE2 . GLN B 2 484 ? 36.556 -26.799 9.572 1.00 105.30 ? 484 GLN B NE2 1 ATOM 7988 N N . LEU B 2 485 ? 40.144 -20.909 7.220 1.00 105.15 ? 485 LEU B N 1 ATOM 7989 C CA . LEU B 2 485 ? 40.039 -19.546 6.698 1.00 106.44 ? 485 LEU B CA 1 ATOM 7990 C C . LEU B 2 485 ? 40.405 -19.458 5.223 1.00 108.81 ? 485 LEU B C 1 ATOM 7991 O O . LEU B 2 485 ? 41.460 -19.947 4.807 1.00 108.14 ? 485 LEU B O 1 ATOM 7992 C CB . LEU B 2 485 ? 40.929 -18.588 7.497 1.00 99.31 ? 485 LEU B CB 1 ATOM 7993 C CG . LEU B 2 485 ? 40.331 -17.986 8.766 1.00 92.57 ? 485 LEU B CG 1 ATOM 7994 C CD1 . LEU B 2 485 ? 41.410 -17.305 9.585 1.00 86.11 ? 485 LEU B CD1 1 ATOM 7995 C CD2 . LEU B 2 485 ? 39.211 -17.015 8.418 1.00 89.99 ? 485 LEU B CD2 1 ATOM 7996 N N . LYS B 2 486 ? 39.533 -18.826 4.439 1.00 104.40 ? 486 LYS B N 1 ATOM 7997 C CA . LYS B 2 486 ? 39.798 -18.599 3.024 1.00 102.43 ? 486 LYS B CA 1 ATOM 7998 C C . LYS B 2 486 ? 40.286 -17.169 2.801 1.00 108.79 ? 486 LYS B C 1 ATOM 7999 O O . LYS B 2 486 ? 41.329 -16.948 2.182 1.00 106.19 ? 486 LYS B O 1 ATOM 8000 C CB . LYS B 2 486 ? 38.568 -18.933 2.169 1.00 96.05 ? 486 LYS B CB 1 ATOM 8001 C CG . LYS B 2 486 ? 38.246 -20.424 2.134 1.00 95.29 ? 486 LYS B CG 1 ATOM 8002 C CD . LYS B 2 486 ? 37.412 -20.793 0.930 1.00 108.71 ? 486 LYS B CD 1 ATOM 8003 C CE . LYS B 2 486 ? 37.618 -22.257 0.534 1.00 114.44 ? 486 LYS B CE 1 ATOM 8004 N NZ . LYS B 2 486 ? 37.219 -22.532 -0.896 1.00 113.77 ? 486 LYS B NZ 1 ATOM 8005 N N . SER B 2 487 ? 39.547 -16.196 3.323 1.00 114.60 ? 487 SER B N 1 ATOM 8006 C CA . SER B 2 487 ? 40.027 -14.817 3.314 1.00 114.36 ? 487 SER B CA 1 ATOM 8007 C C . SER B 2 487 ? 39.763 -14.105 4.630 1.00 112.50 ? 487 SER B C 1 ATOM 8008 O O . SER B 2 487 ? 39.117 -14.650 5.520 1.00 116.95 ? 487 SER B O 1 ATOM 8009 C CB . SER B 2 487 ? 39.451 -14.026 2.138 1.00 110.13 ? 487 SER B CB 1 ATOM 8010 O OG . SER B 2 487 ? 40.353 -14.026 1.043 1.00 105.08 ? 487 SER B OG 1 ATOM 8011 N N . VAL B 2 488 ? 40.282 -12.889 4.746 1.00 108.76 ? 488 VAL B N 1 ATOM 8012 C CA . VAL B 2 488 ? 40.166 -12.108 5.971 1.00 107.98 ? 488 VAL B CA 1 ATOM 8013 C C . VAL B 2 488 ? 39.637 -10.722 5.642 1.00 127.13 ? 488 VAL B C 1 ATOM 8014 O O . VAL B 2 488 ? 40.260 -9.992 4.872 1.00 134.70 ? 488 VAL B O 1 ATOM 8015 C CB . VAL B 2 488 ? 41.534 -11.958 6.667 1.00 85.36 ? 488 VAL B CB 1 ATOM 8016 C CG1 . VAL B 2 488 ? 41.886 -13.219 7.458 1.00 75.29 ? 488 VAL B CG1 1 ATOM 8017 C CG2 . VAL B 2 488 ? 42.626 -11.618 5.642 1.00 70.28 ? 488 VAL B CG2 1 ATOM 8018 N N . PRO B 2 489 ? 38.485 -10.347 6.225 1.00 134.67 ? 489 PRO B N 1 ATOM 8019 C CA . PRO B 2 489 ? 37.901 -9.040 5.900 1.00 136.66 ? 489 PRO B CA 1 ATOM 8020 C C . PRO B 2 489 ? 38.972 -7.948 5.825 1.00 139.59 ? 489 PRO B C 1 ATOM 8021 O O . PRO B 2 489 ? 39.875 -7.910 6.666 1.00 139.08 ? 489 PRO B O 1 ATOM 8022 C CB . PRO B 2 489 ? 36.938 -8.793 7.062 1.00 130.65 ? 489 PRO B CB 1 ATOM 8023 C CG . PRO B 2 489 ? 36.513 -10.164 7.476 1.00 130.51 ? 489 PRO B CG 1 ATOM 8024 C CD . PRO B 2 489 ? 37.713 -11.060 7.260 1.00 130.44 ? 489 PRO B CD 1 ATOM 8025 N N . ASP B 2 490 ? 38.875 -7.091 4.810 1.00 139.42 ? 490 ASP B N 1 ATOM 8026 C CA . ASP B 2 490 ? 39.874 -6.055 4.557 1.00 136.07 ? 490 ASP B CA 1 ATOM 8027 C C . ASP B 2 490 ? 39.882 -5.005 5.666 1.00 124.38 ? 490 ASP B C 1 ATOM 8028 O O . ASP B 2 490 ? 38.869 -4.345 5.902 1.00 115.19 ? 490 ASP B O 1 ATOM 8029 C CB . ASP B 2 490 ? 39.610 -5.370 3.204 1.00 143.41 ? 490 ASP B CB 1 ATOM 8030 C CG . ASP B 2 490 ? 39.686 -6.333 2.021 1.00 144.90 ? 490 ASP B CG 1 ATOM 8031 O OD1 . ASP B 2 490 ? 40.638 -7.141 1.951 1.00 146.71 ? 490 ASP B OD1 1 ATOM 8032 O OD2 . ASP B 2 490 ? 38.796 -6.270 1.147 1.00 141.15 ? 490 ASP B OD2 1 ATOM 8033 N N . GLY B 2 491 ? 41.020 -4.860 6.346 1.00 124.73 ? 491 GLY B N 1 ATOM 8034 C CA . GLY B 2 491 ? 41.190 -3.822 7.351 1.00 128.35 ? 491 GLY B CA 1 ATOM 8035 C C . GLY B 2 491 ? 41.211 -4.266 8.808 1.00 132.53 ? 491 GLY B C 1 ATOM 8036 O O . GLY B 2 491 ? 40.817 -3.502 9.696 1.00 135.41 ? 491 GLY B O 1 ATOM 8037 N N . VAL B 2 492 ? 41.675 -5.489 9.063 1.00 126.89 ? 492 VAL B N 1 ATOM 8038 C CA . VAL B 2 492 ? 41.776 -6.000 10.433 1.00 116.67 ? 492 VAL B CA 1 ATOM 8039 C C . VAL B 2 492 ? 43.159 -5.782 11.031 1.00 115.61 ? 492 VAL B C 1 ATOM 8040 O O . VAL B 2 492 ? 43.344 -4.896 11.868 1.00 125.46 ? 492 VAL B O 1 ATOM 8041 C CB . VAL B 2 492 ? 41.436 -7.496 10.518 1.00 103.82 ? 492 VAL B CB 1 ATOM 8042 C CG1 . VAL B 2 492 ? 39.934 -7.688 10.702 1.00 98.43 ? 492 VAL B CG1 1 ATOM 8043 C CG2 . VAL B 2 492 ? 41.956 -8.234 9.286 1.00 99.88 ? 492 VAL B CG2 1 ATOM 8044 N N . PHE B 2 493 ? 44.120 -6.593 10.596 1.00 102.90 ? 493 PHE B N 1 ATOM 8045 C CA . PHE B 2 493 ? 45.508 -6.497 11.046 1.00 99.41 ? 493 PHE B CA 1 ATOM 8046 C C . PHE B 2 493 ? 46.084 -5.077 11.029 1.00 101.96 ? 493 PHE B C 1 ATOM 8047 O O . PHE B 2 493 ? 47.250 -4.868 11.385 1.00 91.51 ? 493 PHE B O 1 ATOM 8048 C CB . PHE B 2 493 ? 46.399 -7.386 10.185 1.00 98.98 ? 493 PHE B CB 1 ATOM 8049 C CG . PHE B 2 493 ? 45.908 -8.786 10.047 1.00 101.42 ? 493 PHE B CG 1 ATOM 8050 C CD1 . PHE B 2 493 ? 45.235 -9.183 8.910 1.00 106.92 ? 493 PHE B CD1 1 ATOM 8051 C CD2 . PHE B 2 493 ? 46.131 -9.713 11.049 1.00 112.12 ? 493 PHE B CD2 1 ATOM 8052 C CE1 . PHE B 2 493 ? 44.784 -10.481 8.772 1.00 116.70 ? 493 PHE B CE1 1 ATOM 8053 C CE2 . PHE B 2 493 ? 45.680 -11.014 10.923 1.00 118.07 ? 493 PHE B CE2 1 ATOM 8054 C CZ . PHE B 2 493 ? 45.008 -11.400 9.780 1.00 120.97 ? 493 PHE B CZ 1 ATOM 8055 N N . ASP B 2 494 ? 45.279 -4.114 10.589 1.00 115.54 ? 494 ASP B N 1 ATOM 8056 C CA . ASP B 2 494 ? 45.674 -2.710 10.602 1.00 129.63 ? 494 ASP B CA 1 ATOM 8057 C C . ASP B 2 494 ? 45.635 -2.179 12.028 1.00 127.33 ? 494 ASP B C 1 ATOM 8058 O O . ASP B 2 494 ? 46.604 -1.584 12.506 1.00 126.45 ? 494 ASP B O 1 ATOM 8059 C CB . ASP B 2 494 ? 44.744 -1.856 9.726 1.00 135.93 ? 494 ASP B CB 1 ATOM 8060 C CG . ASP B 2 494 ? 44.576 -2.408 8.322 1.00 129.18 ? 494 ASP B CG 1 ATOM 8061 O OD1 . ASP B 2 494 ? 45.439 -3.194 7.872 1.00 129.54 ? 494 ASP B OD1 1 ATOM 8062 O OD2 . ASP B 2 494 ? 43.572 -2.046 7.670 1.00 120.03 ? 494 ASP B OD2 1 ATOM 8063 N N . ARG B 2 495 ? 44.505 -2.397 12.701 1.00 125.11 ? 495 ARG B N 1 ATOM 8064 C CA . ARG B 2 495 ? 44.300 -1.864 14.047 1.00 127.93 ? 495 ARG B CA 1 ATOM 8065 C C . ARG B 2 495 ? 44.996 -2.715 15.122 1.00 121.72 ? 495 ARG B C 1 ATOM 8066 O O . ARG B 2 495 ? 45.120 -2.296 16.278 1.00 120.36 ? 495 ARG B O 1 ATOM 8067 C CB . ARG B 2 495 ? 42.803 -1.703 14.351 1.00 125.48 ? 495 ARG B CB 1 ATOM 8068 C CG . ARG B 2 495 ? 42.451 -0.433 15.141 1.00 123.11 ? 495 ARG B CG 1 ATOM 8069 C CD . ARG B 2 495 ? 42.488 0.804 14.245 1.00 125.83 ? 495 ARG B CD 1 ATOM 8070 N NE . ARG B 2 495 ? 42.481 2.065 14.989 1.00 130.25 ? 495 ARG B NE 1 ATOM 8071 C CZ . ARG B 2 495 ? 42.526 3.269 14.417 1.00 134.09 ? 495 ARG B CZ 1 ATOM 8072 N NH1 . ARG B 2 495 ? 42.574 3.376 13.091 1.00 135.70 ? 495 ARG B NH1 1 ATOM 8073 N NH2 . ARG B 2 495 ? 42.520 4.369 15.166 1.00 127.55 ? 495 ARG B NH2 1 ATOM 8074 N N . LEU B 2 496 ? 45.457 -3.902 14.735 1.00 111.58 ? 496 LEU B N 1 ATOM 8075 C CA . LEU B 2 496 ? 46.225 -4.752 15.639 1.00 103.55 ? 496 LEU B CA 1 ATOM 8076 C C . LEU B 2 496 ? 47.634 -4.198 15.839 1.00 99.48 ? 496 LEU B C 1 ATOM 8077 O O . LEU B 2 496 ? 48.610 -4.943 15.762 1.00 95.27 ? 496 LEU B O 1 ATOM 8078 C CB . LEU B 2 496 ? 46.304 -6.189 15.104 1.00 101.89 ? 496 LEU B CB 1 ATOM 8079 C CG . LEU B 2 496 ? 45.028 -7.035 14.968 1.00 97.77 ? 496 LEU B CG 1 ATOM 8080 C CD1 . LEU B 2 496 ? 45.388 -8.512 15.014 1.00 92.58 ? 496 LEU B CD1 1 ATOM 8081 C CD2 . LEU B 2 496 ? 43.978 -6.723 16.036 1.00 92.05 ? 496 LEU B CD2 1 ATOM 8082 N N . THR B 2 497 ? 47.723 -2.896 16.112 1.00 103.77 ? 497 THR B N 1 ATOM 8083 C CA . THR B 2 497 ? 48.993 -2.157 16.179 1.00 115.55 ? 497 THR B CA 1 ATOM 8084 C C . THR B 2 497 ? 50.096 -2.792 17.036 1.00 116.97 ? 497 THR B C 1 ATOM 8085 O O . THR B 2 497 ? 51.286 -2.506 16.849 1.00 106.78 ? 497 THR B O 1 ATOM 8086 C CB . THR B 2 497 ? 48.768 -0.711 16.686 1.00 127.10 ? 497 THR B CB 1 ATOM 8087 O OG1 . THR B 2 497 ? 48.045 -0.739 17.926 1.00 124.78 ? 497 THR B OG1 1 ATOM 8088 C CG2 . THR B 2 497 ? 47.989 0.110 15.658 1.00 131.90 ? 497 THR B CG2 1 ATOM 8089 N N . SER B 2 498 ? 49.695 -3.646 17.973 1.00 123.30 ? 498 SER B N 1 ATOM 8090 C CA . SER B 2 498 ? 50.619 -4.231 18.942 1.00 112.57 ? 498 SER B CA 1 ATOM 8091 C C . SER B 2 498 ? 51.053 -5.636 18.512 1.00 99.66 ? 498 SER B C 1 ATOM 8092 O O . SER B 2 498 ? 51.956 -6.230 19.100 1.00 97.71 ? 498 SER B O 1 ATOM 8093 C CB . SER B 2 498 ? 49.972 -4.251 20.332 1.00 108.58 ? 498 SER B CB 1 ATOM 8094 O OG . SER B 2 498 ? 50.937 -4.050 21.351 1.00 114.00 ? 498 SER B OG 1 ATOM 8095 N N . LEU B 2 499 ? 50.405 -6.152 17.474 1.00 97.08 ? 499 LEU B N 1 ATOM 8096 C CA . LEU B 2 499 ? 50.743 -7.449 16.891 1.00 105.61 ? 499 LEU B CA 1 ATOM 8097 C C . LEU B 2 499 ? 52.237 -7.565 16.557 1.00 117.34 ? 499 LEU B C 1 ATOM 8098 O O . LEU B 2 499 ? 52.857 -6.589 16.137 1.00 132.31 ? 499 LEU B O 1 ATOM 8099 C CB . LEU B 2 499 ? 49.899 -7.665 15.632 1.00 100.24 ? 499 LEU B CB 1 ATOM 8100 C CG . LEU B 2 499 ? 49.938 -9.017 14.928 1.00 98.03 ? 499 LEU B CG 1 ATOM 8101 C CD1 . LEU B 2 499 ? 49.793 -10.154 15.915 1.00 89.26 ? 499 LEU B CD1 1 ATOM 8102 C CD2 . LEU B 2 499 ? 48.827 -9.061 13.914 1.00 104.79 ? 499 LEU B CD2 1 ATOM 8103 N N . GLN B 2 500 ? 52.809 -8.753 16.745 1.00 109.22 ? 500 GLN B N 1 ATOM 8104 C CA . GLN B 2 500 ? 54.228 -8.988 16.457 1.00 111.61 ? 500 GLN B CA 1 ATOM 8105 C C . GLN B 2 500 ? 54.486 -10.432 16.046 1.00 117.21 ? 500 GLN B C 1 ATOM 8106 O O . GLN B 2 500 ? 55.520 -10.762 15.457 1.00 115.51 ? 500 GLN B O 1 ATOM 8107 C CB . GLN B 2 500 ? 55.080 -8.682 17.681 1.00 105.90 ? 500 GLN B CB 1 ATOM 8108 C CG . GLN B 2 500 ? 54.824 -7.340 18.303 1.00 108.56 ? 500 GLN B CG 1 ATOM 8109 C CD . GLN B 2 500 ? 55.648 -7.158 19.544 1.00 110.56 ? 500 GLN B CD 1 ATOM 8110 O OE1 . GLN B 2 500 ? 56.594 -7.918 19.779 1.00 111.57 ? 500 GLN B OE1 1 ATOM 8111 N NE2 . GLN B 2 500 ? 55.299 -6.156 20.356 1.00 100.38 ? 500 GLN B NE2 1 ATOM 8112 N N . TYR B 2 501 ? 53.548 -11.296 16.403 1.00 115.84 ? 501 TYR B N 1 ATOM 8113 C CA . TYR B 2 501 ? 53.624 -12.698 16.060 1.00 110.60 ? 501 TYR B CA 1 ATOM 8114 C C . TYR B 2 501 ? 52.274 -13.073 15.503 1.00 108.38 ? 501 TYR B C 1 ATOM 8115 O O . TYR B 2 501 ? 51.244 -12.608 15.987 1.00 106.73 ? 501 TYR B O 1 ATOM 8116 C CB . TYR B 2 501 ? 53.938 -13.528 17.296 1.00 114.52 ? 501 TYR B CB 1 ATOM 8117 C CG . TYR B 2 501 ? 55.339 -13.316 17.814 1.00 132.12 ? 501 TYR B CG 1 ATOM 8118 C CD1 . TYR B 2 501 ? 55.771 -12.057 18.212 1.00 137.07 ? 501 TYR B CD1 1 ATOM 8119 C CD2 . TYR B 2 501 ? 56.233 -14.377 17.906 1.00 141.53 ? 501 TYR B CD2 1 ATOM 8120 C CE1 . TYR B 2 501 ? 57.052 -11.857 18.683 1.00 142.52 ? 501 TYR B CE1 1 ATOM 8121 C CE2 . TYR B 2 501 ? 57.518 -14.189 18.379 1.00 143.90 ? 501 TYR B CE2 1 ATOM 8122 C CZ . TYR B 2 501 ? 57.921 -12.926 18.766 1.00 145.87 ? 501 TYR B CZ 1 ATOM 8123 O OH . TYR B 2 501 ? 59.200 -12.734 19.236 1.00 149.74 ? 501 TYR B OH 1 ATOM 8124 N N . ILE B 2 502 ? 52.277 -13.894 14.464 1.00 101.01 ? 502 ILE B N 1 ATOM 8125 C CA . ILE B 2 502 ? 51.035 -14.312 13.841 1.00 84.56 ? 502 ILE B CA 1 ATOM 8126 C C . ILE B 2 502 ? 51.281 -15.560 13.036 1.00 76.03 ? 502 ILE B C 1 ATOM 8127 O O . ILE B 2 502 ? 52.146 -15.586 12.170 1.00 79.19 ? 502 ILE B O 1 ATOM 8128 C CB . ILE B 2 502 ? 50.431 -13.205 12.951 1.00 85.24 ? 502 ILE B CB 1 ATOM 8129 C CG1 . ILE B 2 502 ? 49.145 -13.694 12.289 1.00 78.27 ? 502 ILE B CG1 1 ATOM 8130 C CG2 . ILE B 2 502 ? 51.430 -12.744 11.901 1.00 92.40 ? 502 ILE B CG2 1 ATOM 8131 C CD1 . ILE B 2 502 ? 48.232 -12.574 11.871 1.00 73.69 ? 502 ILE B CD1 1 ATOM 8132 N N . TRP B 2 503 ? 50.533 -16.608 13.351 1.00 80.52 ? 503 TRP B N 1 ATOM 8133 C CA . TRP B 2 503 ? 50.657 -17.870 12.643 1.00 97.17 ? 503 TRP B CA 1 ATOM 8134 C C . TRP B 2 503 ? 49.526 -17.998 11.631 1.00 105.81 ? 503 TRP B C 1 ATOM 8135 O O . TRP B 2 503 ? 48.378 -18.257 12.000 1.00 109.51 ? 503 TRP B O 1 ATOM 8136 C CB . TRP B 2 503 ? 50.636 -19.041 13.625 1.00 100.62 ? 503 TRP B CB 1 ATOM 8137 C CG . TRP B 2 503 ? 51.934 -19.260 14.346 1.00 104.36 ? 503 TRP B CG 1 ATOM 8138 C CD1 . TRP B 2 503 ? 52.859 -20.227 14.084 1.00 107.92 ? 503 TRP B CD1 1 ATOM 8139 C CD2 . TRP B 2 503 ? 52.443 -18.504 15.453 1.00 108.81 ? 503 TRP B CD2 1 ATOM 8140 N NE1 . TRP B 2 503 ? 53.916 -20.119 14.956 1.00 118.72 ? 503 TRP B NE1 1 ATOM 8141 C CE2 . TRP B 2 503 ? 53.686 -19.071 15.808 1.00 115.00 ? 503 TRP B CE2 1 ATOM 8142 C CE3 . TRP B 2 503 ? 51.970 -17.405 16.180 1.00 101.01 ? 503 TRP B CE3 1 ATOM 8143 C CZ2 . TRP B 2 503 ? 54.463 -18.573 16.854 1.00 105.29 ? 503 TRP B CZ2 1 ATOM 8144 C CZ3 . TRP B 2 503 ? 52.741 -16.910 17.211 1.00 97.79 ? 503 TRP B CZ3 1 ATOM 8145 C CH2 . TRP B 2 503 ? 53.975 -17.494 17.541 1.00 102.76 ? 503 TRP B CH2 1 ATOM 8146 N N . LEU B 2 504 ? 49.851 -17.809 10.355 1.00 102.11 ? 504 LEU B N 1 ATOM 8147 C CA . LEU B 2 504 ? 48.833 -17.838 9.316 1.00 96.50 ? 504 LEU B CA 1 ATOM 8148 C C . LEU B 2 504 ? 48.795 -19.164 8.567 1.00 94.15 ? 504 LEU B C 1 ATOM 8149 O O . LEU B 2 504 ? 47.842 -19.432 7.830 1.00 89.62 ? 504 LEU B O 1 ATOM 8150 C CB . LEU B 2 504 ? 49.013 -16.669 8.346 1.00 92.09 ? 504 LEU B CB 1 ATOM 8151 C CG . LEU B 2 504 ? 48.451 -15.332 8.833 1.00 92.74 ? 504 LEU B CG 1 ATOM 8152 C CD1 . LEU B 2 504 ? 48.980 -14.174 8.001 1.00 89.36 ? 504 LEU B CD1 1 ATOM 8153 C CD2 . LEU B 2 504 ? 46.937 -15.361 8.805 1.00 90.02 ? 504 LEU B CD2 1 ATOM 8154 N N . HIS B 2 505 ? 49.808 -20.002 8.783 1.00 93.15 ? 505 HIS B N 1 ATOM 8155 C CA . HIS B 2 505 ? 49.966 -21.234 8.001 1.00 96.46 ? 505 HIS B CA 1 ATOM 8156 C C . HIS B 2 505 ? 48.778 -22.203 8.042 1.00 97.04 ? 505 HIS B C 1 ATOM 8157 O O . HIS B 2 505 ? 47.773 -21.946 8.696 1.00 108.46 ? 505 HIS B O 1 ATOM 8158 C CB . HIS B 2 505 ? 51.277 -21.957 8.344 1.00 100.48 ? 505 HIS B CB 1 ATOM 8159 C CG . HIS B 2 505 ? 51.308 -22.564 9.712 1.00 109.86 ? 505 HIS B CG 1 ATOM 8160 N ND1 . HIS B 2 505 ? 51.745 -21.876 10.822 1.00 116.30 ? 505 HIS B ND1 1 ATOM 8161 C CD2 . HIS B 2 505 ? 50.980 -23.806 10.143 1.00 112.12 ? 505 HIS B CD2 1 ATOM 8162 C CE1 . HIS B 2 505 ? 51.673 -22.662 11.883 1.00 117.36 ? 505 HIS B CE1 1 ATOM 8163 N NE2 . HIS B 2 505 ? 51.212 -23.838 11.497 1.00 114.67 ? 505 HIS B NE2 1 ATOM 8164 N N . ASP B 2 506 ? 48.912 -23.304 7.310 1.00 94.84 ? 506 ASP B N 1 ATOM 8165 C CA . ASP B 2 506 ? 47.887 -24.350 7.190 1.00 97.23 ? 506 ASP B CA 1 ATOM 8166 C C . ASP B 2 506 ? 46.430 -23.903 7.057 1.00 100.62 ? 506 ASP B C 1 ATOM 8167 O O . ASP B 2 506 ? 45.535 -24.524 7.647 1.00 88.42 ? 506 ASP B O 1 ATOM 8168 C CB . ASP B 2 506 ? 48.024 -25.375 8.311 1.00 95.55 ? 506 ASP B CB 1 ATOM 8169 C CG . ASP B 2 506 ? 49.189 -26.312 8.090 1.00 107.21 ? 506 ASP B CG 1 ATOM 8170 O OD1 . ASP B 2 506 ? 48.965 -27.400 7.518 1.00 113.05 ? 506 ASP B OD1 1 ATOM 8171 O OD2 . ASP B 2 506 ? 50.329 -25.955 8.466 1.00 107.62 ? 506 ASP B OD2 1 ATOM 8172 N N . ASN B 2 507 ? 46.204 -22.851 6.265 1.00 104.71 ? 507 ASN B N 1 ATOM 8173 C CA . ASN B 2 507 ? 44.862 -22.345 5.965 1.00 99.64 ? 507 ASN B CA 1 ATOM 8174 C C . ASN B 2 507 ? 44.585 -22.334 4.474 1.00 103.65 ? 507 ASN B C 1 ATOM 8175 O O . ASN B 2 507 ? 45.462 -21.996 3.683 1.00 110.48 ? 507 ASN B O 1 ATOM 8176 C CB . ASN B 2 507 ? 44.671 -20.930 6.513 1.00 101.23 ? 507 ASN B CB 1 ATOM 8177 C CG . ASN B 2 507 ? 44.082 -20.917 7.907 1.00 100.22 ? 507 ASN B CG 1 ATOM 8178 O OD1 . ASN B 2 507 ? 44.797 -21.028 8.901 1.00 96.39 ? 507 ASN B OD1 1 ATOM 8179 N ND2 . ASN B 2 507 ? 42.769 -20.765 7.988 1.00 101.36 ? 507 ASN B ND2 1 ATOM 8180 N N . PRO B 2 508 ? 43.356 -22.701 4.086 1.00 108.26 ? 508 PRO B N 1 ATOM 8181 C CA . PRO B 2 508 ? 42.903 -22.784 2.688 1.00 108.01 ? 508 PRO B CA 1 ATOM 8182 C C . PRO B 2 508 ? 42.511 -21.429 2.090 1.00 102.18 ? 508 PRO B C 1 ATOM 8183 O O . PRO B 2 508 ? 41.328 -21.212 1.808 1.00 100.80 ? 508 PRO B O 1 ATOM 8184 C CB . PRO B 2 508 ? 41.655 -23.669 2.794 1.00 107.97 ? 508 PRO B CB 1 ATOM 8185 C CG . PRO B 2 508 ? 41.136 -23.365 4.165 1.00 111.31 ? 508 PRO B CG 1 ATOM 8186 C CD . PRO B 2 508 ? 42.378 -23.305 5.007 1.00 107.32 ? 508 PRO B CD 1 ATOM 8187 N N . TRP B 2 509 ? 43.484 -20.547 1.874 1.00 98.14 ? 509 TRP B N 1 ATOM 8188 C CA . TRP B 2 509 ? 43.201 -19.183 1.419 1.00 106.80 ? 509 TRP B CA 1 ATOM 8189 C C . TRP B 2 509 ? 42.752 -19.081 -0.054 1.00 108.77 ? 509 TRP B C 1 ATOM 8190 O O . TRP B 2 509 ? 43.402 -19.631 -0.942 1.00 109.70 ? 509 TRP B O 1 ATOM 8191 C CB . TRP B 2 509 ? 44.424 -18.284 1.651 1.00 110.97 ? 509 TRP B CB 1 ATOM 8192 C CG . TRP B 2 509 ? 44.963 -18.279 3.065 1.00 111.84 ? 509 TRP B CG 1 ATOM 8193 C CD1 . TRP B 2 509 ? 46.034 -18.988 3.545 1.00 108.25 ? 509 TRP B CD1 1 ATOM 8194 C CD2 . TRP B 2 509 ? 44.468 -17.511 4.171 1.00 111.93 ? 509 TRP B CD2 1 ATOM 8195 N NE1 . TRP B 2 509 ? 46.228 -18.712 4.878 1.00 98.66 ? 509 TRP B NE1 1 ATOM 8196 C CE2 . TRP B 2 509 ? 45.279 -17.810 5.286 1.00 103.15 ? 509 TRP B CE2 1 ATOM 8197 C CE3 . TRP B 2 509 ? 43.416 -16.600 4.327 1.00 114.30 ? 509 TRP B CE3 1 ATOM 8198 C CZ2 . TRP B 2 509 ? 45.070 -17.231 6.537 1.00 102.96 ? 509 TRP B CZ2 1 ATOM 8199 C CZ3 . TRP B 2 509 ? 43.209 -16.029 5.573 1.00 109.45 ? 509 TRP B CZ3 1 ATOM 8200 C CH2 . TRP B 2 509 ? 44.032 -16.346 6.659 1.00 102.49 ? 509 TRP B CH2 1 ATOM 8201 N N . ASP B 2 510 ? 41.649 -18.370 -0.307 1.00 110.30 ? 510 ASP B N 1 ATOM 8202 C CA . ASP B 2 510 ? 41.206 -18.082 -1.677 1.00 103.21 ? 510 ASP B CA 1 ATOM 8203 C C . ASP B 2 510 ? 42.123 -17.036 -2.295 1.00 106.57 ? 510 ASP B C 1 ATOM 8204 O O . ASP B 2 510 ? 42.181 -15.901 -1.823 1.00 103.39 ? 510 ASP B O 1 ATOM 8205 C CB . ASP B 2 510 ? 39.754 -17.582 -1.710 1.00 93.73 ? 510 ASP B CB 1 ATOM 8206 C CG . ASP B 2 510 ? 39.225 -17.384 -3.141 1.00 104.74 ? 510 ASP B CG 1 ATOM 8207 O OD1 . ASP B 2 510 ? 38.892 -16.232 -3.503 1.00 113.99 ? 510 ASP B OD1 1 ATOM 8208 O OD2 . ASP B 2 510 ? 39.143 -18.372 -3.908 1.00 95.89 ? 510 ASP B OD2 1 ATOM 8209 N N . CYS B 2 511 ? 42.831 -17.418 -3.356 1.00 112.62 ? 511 CYS B N 1 ATOM 8210 C CA . CYS B 2 511 ? 43.839 -16.547 -3.958 1.00 119.47 ? 511 CYS B CA 1 ATOM 8211 C C . CYS B 2 511 ? 43.432 -15.904 -5.292 1.00 133.02 ? 511 CYS B C 1 ATOM 8212 O O . CYS B 2 511 ? 44.286 -15.578 -6.119 1.00 135.02 ? 511 CYS B O 1 ATOM 8213 C CB . CYS B 2 511 ? 45.174 -17.289 -4.089 1.00 111.77 ? 511 CYS B CB 1 ATOM 8214 S SG . CYS B 2 511 ? 46.013 -17.470 -2.502 1.00 143.61 ? 511 CYS B SG 1 ATOM 8215 N N . THR B 2 512 ? 42.130 -15.711 -5.487 1.00 137.44 ? 512 THR B N 1 ATOM 8216 C CA . THR B 2 512 ? 41.630 -14.988 -6.649 1.00 145.94 ? 512 THR B CA 1 ATOM 8217 C C . THR B 2 512 ? 41.828 -13.498 -6.419 1.00 154.81 ? 512 THR B C 1 ATOM 8218 O O . THR B 2 512 ? 41.420 -12.968 -5.386 1.00 156.95 ? 512 THR B O 1 ATOM 8219 C CB . THR B 2 512 ? 40.146 -15.259 -6.872 1.00 150.08 ? 512 THR B CB 1 ATOM 8220 O OG1 . THR B 2 512 ? 39.865 -16.627 -6.558 1.00 148.06 ? 512 THR B OG1 1 ATOM 8221 C CG2 . THR B 2 512 ? 39.760 -14.967 -8.321 1.00 154.95 ? 512 THR B CG2 1 ATOM 8222 N N . CYS B 2 513 ? 42.432 -12.825 -7.392 1.00 160.24 ? 513 CYS B N 1 ATOM 8223 C CA . CYS B 2 513 ? 42.947 -11.466 -7.192 1.00 164.29 ? 513 CYS B CA 1 ATOM 8224 C C . CYS B 2 513 ? 42.010 -10.383 -6.624 1.00 164.70 ? 513 CYS B C 1 ATOM 8225 O O . CYS B 2 513 ? 42.459 -9.535 -5.849 1.00 169.72 ? 513 CYS B O 1 ATOM 8226 C CB . CYS B 2 513 ? 43.657 -10.960 -8.452 1.00 165.91 ? 513 CYS B CB 1 ATOM 8227 S SG . CYS B 2 513 ? 45.465 -11.125 -8.385 1.00 158.93 ? 513 CYS B SG 1 ATOM 8228 N N . PRO B 2 514 ? 40.718 -10.397 -6.998 1.00 155.34 ? 514 PRO B N 1 ATOM 8229 C CA . PRO B 2 514 ? 39.837 -9.318 -6.522 1.00 152.69 ? 514 PRO B CA 1 ATOM 8230 C C . PRO B 2 514 ? 39.834 -9.075 -4.994 1.00 153.57 ? 514 PRO B C 1 ATOM 8231 O O . PRO B 2 514 ? 39.456 -7.978 -4.579 1.00 158.24 ? 514 PRO B O 1 ATOM 8232 C CB . PRO B 2 514 ? 38.449 -9.765 -6.997 1.00 142.72 ? 514 PRO B CB 1 ATOM 8233 C CG . PRO B 2 514 ? 38.714 -10.628 -8.174 1.00 141.17 ? 514 PRO B CG 1 ATOM 8234 C CD . PRO B 2 514 ? 40.018 -11.324 -7.906 1.00 144.64 ? 514 PRO B CD 1 ATOM 8235 N N . GLY B 2 515 ? 40.244 -10.051 -4.183 1.00 141.39 ? 515 GLY B N 1 ATOM 8236 C CA . GLY B 2 515 ? 40.156 -9.911 -2.736 1.00 136.97 ? 515 GLY B CA 1 ATOM 8237 C C . GLY B 2 515 ? 41.268 -10.527 -1.894 1.00 137.49 ? 515 GLY B C 1 ATOM 8238 O O . GLY B 2 515 ? 41.204 -10.505 -0.659 1.00 127.10 ? 515 GLY B O 1 ATOM 8239 N N . ILE B 2 516 ? 42.285 -11.080 -2.551 1.00 141.11 ? 516 ILE B N 1 ATOM 8240 C CA . ILE B 2 516 ? 43.439 -11.643 -1.850 1.00 135.75 ? 516 ILE B CA 1 ATOM 8241 C C . ILE B 2 516 ? 44.591 -10.639 -1.827 1.00 132.60 ? 516 ILE B C 1 ATOM 8242 O O . ILE B 2 516 ? 45.706 -10.960 -1.400 1.00 110.63 ? 516 ILE B O 1 ATOM 8243 C CB . ILE B 2 516 ? 43.913 -12.970 -2.490 1.00 135.66 ? 516 ILE B CB 1 ATOM 8244 C CG1 . ILE B 2 516 ? 44.915 -13.687 -1.582 1.00 137.81 ? 516 ILE B CG1 1 ATOM 8245 C CG2 . ILE B 2 516 ? 44.528 -12.724 -3.856 1.00 139.13 ? 516 ILE B CG2 1 ATOM 8246 C CD1 . ILE B 2 516 ? 44.359 -14.048 -0.223 1.00 141.24 ? 516 ILE B CD1 1 ATOM 8247 N N . ARG B 2 517 ? 44.305 -9.421 -2.288 1.00 146.05 ? 517 ARG B N 1 ATOM 8248 C CA . ARG B 2 517 ? 45.293 -8.342 -2.314 1.00 153.73 ? 517 ARG B CA 1 ATOM 8249 C C . ARG B 2 517 ? 45.700 -7.909 -0.902 1.00 161.98 ? 517 ARG B C 1 ATOM 8250 O O . ARG B 2 517 ? 46.889 -7.884 -0.570 1.00 164.08 ? 517 ARG B O 1 ATOM 8251 C CB . ARG B 2 517 ? 44.760 -7.136 -3.100 1.00 150.19 ? 517 ARG B CB 1 ATOM 8252 C CG . ARG B 2 517 ? 45.772 -6.003 -3.281 1.00 149.74 ? 517 ARG B CG 1 ATOM 8253 C CD . ARG B 2 517 ? 45.089 -4.638 -3.377 1.00 151.88 ? 517 ARG B CD 1 ATOM 8254 N NE . ARG B 2 517 ? 44.315 -4.319 -2.174 1.00 154.23 ? 517 ARG B NE 1 ATOM 8255 C CZ . ARG B 2 517 ? 44.786 -3.647 -1.123 1.00 151.28 ? 517 ARG B CZ 1 ATOM 8256 N NH1 . ARG B 2 517 ? 46.038 -3.209 -1.116 1.00 155.84 ? 517 ARG B NH1 1 ATOM 8257 N NH2 . ARG B 2 517 ? 44.003 -3.408 -0.076 1.00 139.06 ? 517 ARG B NH2 1 ATOM 8258 N N . TYR B 2 518 ? 44.707 -7.577 -0.078 1.00 160.71 ? 518 TYR B N 1 ATOM 8259 C CA . TYR B 2 518 ? 44.945 -7.053 1.268 1.00 151.01 ? 518 TYR B CA 1 ATOM 8260 C C . TYR B 2 518 ? 45.947 -7.876 2.064 1.00 139.12 ? 518 TYR B C 1 ATOM 8261 O O . TYR B 2 518 ? 46.856 -7.332 2.694 1.00 131.34 ? 518 TYR B O 1 ATOM 8262 C CB . TYR B 2 518 ? 43.635 -6.960 2.054 1.00 147.37 ? 518 TYR B CB 1 ATOM 8263 C CG . TYR B 2 518 ? 43.839 -6.583 3.505 1.00 145.74 ? 518 TYR B CG 1 ATOM 8264 C CD1 . TYR B 2 518 ? 44.186 -5.287 3.860 1.00 145.64 ? 518 TYR B CD1 1 ATOM 8265 C CD2 . TYR B 2 518 ? 43.693 -7.523 4.519 1.00 143.26 ? 518 TYR B CD2 1 ATOM 8266 C CE1 . TYR B 2 518 ? 44.379 -4.932 5.181 1.00 143.14 ? 518 TYR B CE1 1 ATOM 8267 C CE2 . TYR B 2 518 ? 43.884 -7.176 5.849 1.00 139.21 ? 518 TYR B CE2 1 ATOM 8268 C CZ . TYR B 2 518 ? 44.228 -5.876 6.172 1.00 134.94 ? 518 TYR B CZ 1 ATOM 8269 O OH . TYR B 2 518 ? 44.421 -5.514 7.485 1.00 118.68 ? 518 TYR B OH 1 ATOM 8270 N N . LEU B 2 519 ? 45.768 -9.190 2.036 1.00 136.66 ? 519 LEU B N 1 ATOM 8271 C CA . LEU B 2 519 ? 46.596 -10.082 2.830 1.00 142.11 ? 519 LEU B CA 1 ATOM 8272 C C . LEU B 2 519 ? 48.004 -10.147 2.255 1.00 142.52 ? 519 LEU B C 1 ATOM 8273 O O . LEU B 2 519 ? 48.982 -10.296 2.988 1.00 136.27 ? 519 LEU B O 1 ATOM 8274 C CB . LEU B 2 519 ? 45.975 -11.478 2.869 1.00 144.43 ? 519 LEU B CB 1 ATOM 8275 C CG . LEU B 2 519 ? 45.921 -12.170 4.233 1.00 135.57 ? 519 LEU B CG 1 ATOM 8276 C CD1 . LEU B 2 519 ? 45.202 -13.504 4.110 1.00 130.23 ? 519 LEU B CD1 1 ATOM 8277 C CD2 . LEU B 2 519 ? 47.314 -12.344 4.820 1.00 131.31 ? 519 LEU B CD2 1 ATOM 8278 N N . SER B 2 520 ? 48.098 -10.030 0.935 1.00 146.08 ? 520 SER B N 1 ATOM 8279 C CA . SER B 2 520 ? 49.383 -10.103 0.256 1.00 141.22 ? 520 SER B CA 1 ATOM 8280 C C . SER B 2 520 ? 50.218 -8.850 0.502 1.00 139.92 ? 520 SER B C 1 ATOM 8281 O O . SER B 2 520 ? 51.404 -8.943 0.818 1.00 137.29 ? 520 SER B O 1 ATOM 8282 C CB . SER B 2 520 ? 49.189 -10.326 -1.238 1.00 137.87 ? 520 SER B CB 1 ATOM 8283 O OG . SER B 2 520 ? 50.442 -10.436 -1.884 1.00 142.11 ? 520 SER B OG 1 ATOM 8284 N N . GLU B 2 521 ? 49.599 -7.682 0.352 1.00 139.32 ? 521 GLU B N 1 ATOM 8285 C CA . GLU B 2 521 ? 50.269 -6.426 0.675 1.00 140.03 ? 521 GLU B CA 1 ATOM 8286 C C . GLU B 2 521 ? 50.696 -6.460 2.137 1.00 135.19 ? 521 GLU B C 1 ATOM 8287 O O . GLU B 2 521 ? 51.734 -5.906 2.514 1.00 131.65 ? 521 GLU B O 1 ATOM 8288 C CB . GLU B 2 521 ? 49.345 -5.225 0.437 1.00 140.14 ? 521 GLU B CB 1 ATOM 8289 C CG . GLU B 2 521 ? 48.691 -5.172 -0.940 1.00 138.87 ? 521 GLU B CG 1 ATOM 8290 C CD . GLU B 2 521 ? 49.625 -4.678 -2.037 1.00 137.25 ? 521 GLU B CD 1 ATOM 8291 O OE1 . GLU B 2 521 ? 50.765 -4.274 -1.723 1.00 134.55 ? 521 GLU B OE1 1 ATOM 8292 O OE2 . GLU B 2 521 ? 49.211 -4.696 -3.218 1.00 134.38 ? 521 GLU B OE2 1 ATOM 8293 N N . TRP B 2 522 ? 49.885 -7.122 2.957 1.00 129.90 ? 522 TRP B N 1 ATOM 8294 C CA . TRP B 2 522 ? 50.154 -7.210 4.386 1.00 118.14 ? 522 TRP B CA 1 ATOM 8295 C C . TRP B 2 522 ? 51.372 -8.086 4.696 1.00 109.54 ? 522 TRP B C 1 ATOM 8296 O O . TRP B 2 522 ? 52.365 -7.586 5.218 1.00 106.42 ? 522 TRP B O 1 ATOM 8297 C CB . TRP B 2 522 ? 48.916 -7.681 5.159 1.00 115.09 ? 522 TRP B CB 1 ATOM 8298 C CG . TRP B 2 522 ? 48.871 -7.150 6.565 1.00 113.89 ? 522 TRP B CG 1 ATOM 8299 C CD1 . TRP B 2 522 ? 48.324 -5.970 6.978 1.00 112.94 ? 522 TRP B CD1 1 ATOM 8300 C CD2 . TRP B 2 522 ? 49.407 -7.776 7.739 1.00 116.12 ? 522 TRP B CD2 1 ATOM 8301 N NE1 . TRP B 2 522 ? 48.486 -5.823 8.334 1.00 116.77 ? 522 TRP B NE1 1 ATOM 8302 C CE2 . TRP B 2 522 ? 49.151 -6.918 8.824 1.00 118.20 ? 522 TRP B CE2 1 ATOM 8303 C CE3 . TRP B 2 522 ? 50.079 -8.982 7.977 1.00 109.62 ? 522 TRP B CE3 1 ATOM 8304 C CZ2 . TRP B 2 522 ? 49.543 -7.226 10.123 1.00 115.45 ? 522 TRP B CZ2 1 ATOM 8305 C CZ3 . TRP B 2 522 ? 50.466 -9.283 9.262 1.00 103.92 ? 522 TRP B CZ3 1 ATOM 8306 C CH2 . TRP B 2 522 ? 50.197 -8.412 10.319 1.00 110.06 ? 522 TRP B CH2 1 ATOM 8307 N N . ILE B 2 523 ? 51.308 -9.378 4.369 1.00 111.47 ? 523 ILE B N 1 ATOM 8308 C CA . ILE B 2 523 ? 52.410 -10.296 4.689 1.00 113.45 ? 523 ILE B CA 1 ATOM 8309 C C . ILE B 2 523 ? 53.757 -9.694 4.300 1.00 120.75 ? 523 ILE B C 1 ATOM 8310 O O . ILE B 2 523 ? 54.770 -9.935 4.958 1.00 114.81 ? 523 ILE B O 1 ATOM 8311 C CB . ILE B 2 523 ? 52.291 -11.663 3.970 1.00 107.78 ? 523 ILE B CB 1 ATOM 8312 C CG1 . ILE B 2 523 ? 50.870 -12.223 4.054 1.00 107.02 ? 523 ILE B CG1 1 ATOM 8313 C CG2 . ILE B 2 523 ? 53.307 -12.656 4.550 1.00 92.50 ? 523 ILE B CG2 1 ATOM 8314 C CD1 . ILE B 2 523 ? 50.689 -13.266 5.128 1.00 102.00 ? 523 ILE B CD1 1 ATOM 8315 N N . ASN B 2 524 ? 53.754 -8.918 3.218 1.00 132.81 ? 524 ASN B N 1 ATOM 8316 C CA . ASN B 2 524 ? 54.972 -8.316 2.683 1.00 132.54 ? 524 ASN B CA 1 ATOM 8317 C C . ASN B 2 524 ? 55.429 -7.109 3.489 1.00 133.04 ? 524 ASN B C 1 ATOM 8318 O O . ASN B 2 524 ? 56.612 -6.986 3.816 1.00 128.32 ? 524 ASN B O 1 ATOM 8319 C CB . ASN B 2 524 ? 54.780 -7.936 1.214 1.00 129.50 ? 524 ASN B CB 1 ATOM 8320 C CG . ASN B 2 524 ? 54.770 -9.146 0.293 1.00 126.02 ? 524 ASN B CG 1 ATOM 8321 O OD1 . ASN B 2 524 ? 55.460 -10.138 0.538 1.00 118.52 ? 524 ASN B OD1 1 ATOM 8322 N ND2 . ASN B 2 524 ? 53.991 -9.063 -0.780 1.00 128.43 ? 524 ASN B ND2 1 ATOM 8323 N N . LYS B 2 525 ? 54.489 -6.222 3.809 1.00 136.43 ? 525 LYS B N 1 ATOM 8324 C CA . LYS B 2 525 ? 54.796 -5.056 4.629 1.00 138.27 ? 525 LYS B CA 1 ATOM 8325 C C . LYS B 2 525 ? 55.184 -5.487 6.043 1.00 140.41 ? 525 LYS B C 1 ATOM 8326 O O . LYS B 2 525 ? 55.802 -4.725 6.781 1.00 145.20 ? 525 LYS B O 1 ATOM 8327 C CB . LYS B 2 525 ? 53.615 -4.079 4.673 1.00 135.07 ? 525 LYS B CB 1 ATOM 8328 C CG . LYS B 2 525 ? 54.038 -2.614 4.601 1.00 135.36 ? 525 LYS B CG 1 ATOM 8329 C CD . LYS B 2 525 ? 53.037 -1.669 5.251 1.00 128.31 ? 525 LYS B CD 1 ATOM 8330 C CE . LYS B 2 525 ? 53.340 -1.481 6.730 1.00 119.46 ? 525 LYS B CE 1 ATOM 8331 N NZ . LYS B 2 525 ? 52.790 -0.198 7.244 1.00 117.00 ? 525 LYS B NZ 1 ATOM 8332 N N . HIS B 2 526 ? 54.812 -6.711 6.412 1.00 138.22 ? 526 HIS B N 1 ATOM 8333 C CA . HIS B 2 526 ? 55.159 -7.277 7.715 1.00 133.13 ? 526 HIS B CA 1 ATOM 8334 C C . HIS B 2 526 ? 55.713 -8.684 7.533 1.00 130.30 ? 526 HIS B C 1 ATOM 8335 O O . HIS B 2 526 ? 55.088 -9.667 7.937 1.00 114.00 ? 526 HIS B O 1 ATOM 8336 C CB . HIS B 2 526 ? 53.939 -7.317 8.639 1.00 129.20 ? 526 HIS B CB 1 ATOM 8337 C CG . HIS B 2 526 ? 53.173 -6.033 8.681 1.00 133.92 ? 526 HIS B CG 1 ATOM 8338 N ND1 . HIS B 2 526 ? 53.707 -4.866 9.183 1.00 141.59 ? 526 HIS B ND1 1 ATOM 8339 C CD2 . HIS B 2 526 ? 51.915 -5.732 8.284 1.00 134.10 ? 526 HIS B CD2 1 ATOM 8340 C CE1 . HIS B 2 526 ? 52.810 -3.898 9.089 1.00 144.69 ? 526 HIS B CE1 1 ATOM 8341 N NE2 . HIS B 2 526 ? 51.714 -4.398 8.548 1.00 140.72 ? 526 HIS B NE2 1 ATOM 8342 N N . SER B 2 527 ? 56.888 -8.772 6.916 1.00 143.04 ? 527 SER B N 1 ATOM 8343 C CA . SER B 2 527 ? 57.506 -10.059 6.613 1.00 148.65 ? 527 SER B CA 1 ATOM 8344 C C . SER B 2 527 ? 58.002 -10.765 7.876 1.00 152.85 ? 527 SER B C 1 ATOM 8345 O O . SER B 2 527 ? 57.901 -11.989 7.992 1.00 153.65 ? 527 SER B O 1 ATOM 8346 C CB . SER B 2 527 ? 58.660 -9.879 5.619 1.00 147.05 ? 527 SER B CB 1 ATOM 8347 O OG . SER B 2 527 ? 58.243 -9.183 4.453 1.00 147.17 ? 527 SER B OG 1 ATOM 8348 N N . GLY B 2 528 ? 58.531 -9.988 8.818 1.00 152.77 ? 528 GLY B N 1 ATOM 8349 C CA . GLY B 2 528 ? 59.089 -10.534 10.044 1.00 143.61 ? 528 GLY B CA 1 ATOM 8350 C C . GLY B 2 528 ? 58.049 -10.978 11.056 1.00 137.36 ? 528 GLY B C 1 ATOM 8351 O O . GLY B 2 528 ? 58.342 -11.784 11.936 1.00 132.22 ? 528 GLY B O 1 ATOM 8352 N N . VAL B 2 529 ? 56.831 -10.457 10.925 1.00 139.43 ? 529 VAL B N 1 ATOM 8353 C CA . VAL B 2 529 ? 55.743 -10.737 11.865 1.00 133.59 ? 529 VAL B CA 1 ATOM 8354 C C . VAL B 2 529 ? 55.197 -12.166 11.744 1.00 124.22 ? 529 VAL B C 1 ATOM 8355 O O . VAL B 2 529 ? 54.762 -12.757 12.732 1.00 125.82 ? 529 VAL B O 1 ATOM 8356 C CB . VAL B 2 529 ? 54.585 -9.707 11.709 1.00 92.16 ? 529 VAL B CB 1 ATOM 8357 C CG1 . VAL B 2 529 ? 53.436 -10.021 12.657 1.00 90.81 ? 529 VAL B CG1 1 ATOM 8358 C CG2 . VAL B 2 529 ? 55.097 -8.287 11.938 1.00 90.95 ? 529 VAL B CG2 1 ATOM 8359 N N . VAL B 2 530 ? 55.242 -12.719 10.535 1.00 117.81 ? 530 VAL B N 1 ATOM 8360 C CA . VAL B 2 530 ? 54.678 -14.041 10.253 1.00 115.08 ? 530 VAL B CA 1 ATOM 8361 C C . VAL B 2 530 ? 55.606 -15.205 10.638 1.00 120.81 ? 530 VAL B C 1 ATOM 8362 O O . VAL B 2 530 ? 56.717 -15.325 10.117 1.00 131.06 ? 530 VAL B O 1 ATOM 8363 C CB . VAL B 2 530 ? 54.321 -14.173 8.760 1.00 104.61 ? 530 VAL B CB 1 ATOM 8364 C CG1 . VAL B 2 530 ? 53.438 -15.400 8.523 1.00 90.45 ? 530 VAL B CG1 1 ATOM 8365 C CG2 . VAL B 2 530 ? 53.646 -12.899 8.268 1.00 107.95 ? 530 VAL B CG2 1 ATOM 8366 N N . ARG B 2 531 ? 55.139 -16.069 11.537 1.00 109.21 ? 531 ARG B N 1 ATOM 8367 C CA . ARG B 2 531 ? 55.929 -17.209 11.986 1.00 100.38 ? 531 ARG B CA 1 ATOM 8368 C C . ARG B 2 531 ? 55.459 -18.480 11.302 1.00 98.30 ? 531 ARG B C 1 ATOM 8369 O O . ARG B 2 531 ? 54.376 -18.508 10.723 1.00 97.22 ? 531 ARG B O 1 ATOM 8370 C CB . ARG B 2 531 ? 55.821 -17.371 13.505 1.00 100.15 ? 531 ARG B CB 1 ATOM 8371 C CG . ARG B 2 531 ? 56.447 -16.237 14.321 1.00 103.97 ? 531 ARG B CG 1 ATOM 8372 C CD . ARG B 2 531 ? 57.806 -15.844 13.763 1.00 108.78 ? 531 ARG B CD 1 ATOM 8373 N NE . ARG B 2 531 ? 58.674 -15.205 14.750 1.00 112.37 ? 531 ARG B NE 1 ATOM 8374 C CZ . ARG B 2 531 ? 58.578 -13.932 15.130 1.00 116.08 ? 531 ARG B CZ 1 ATOM 8375 N NH1 . ARG B 2 531 ? 57.630 -13.148 14.625 1.00 108.36 ? 531 ARG B NH1 1 ATOM 8376 N NH2 . ARG B 2 531 ? 59.427 -13.444 16.030 1.00 118.97 ? 531 ARG B NH2 1 ATOM 8377 N N . ASN B 2 532 ? 56.268 -19.533 11.371 1.00 104.48 ? 532 ASN B N 1 ATOM 8378 C CA . ASN B 2 532 ? 55.872 -20.830 10.819 1.00 115.84 ? 532 ASN B CA 1 ATOM 8379 C C . ASN B 2 532 ? 55.485 -21.869 11.885 1.00 129.42 ? 532 ASN B C 1 ATOM 8380 O O . ASN B 2 532 ? 55.524 -21.590 13.090 1.00 127.83 ? 532 ASN B O 1 ATOM 8381 C CB . ASN B 2 532 ? 56.945 -21.390 9.865 1.00 116.84 ? 532 ASN B CB 1 ATOM 8382 C CG . ASN B 2 532 ? 58.180 -21.927 10.595 1.00 111.53 ? 532 ASN B CG 1 ATOM 8383 O OD1 . ASN B 2 532 ? 58.713 -21.285 11.501 1.00 116.96 ? 532 ASN B OD1 1 ATOM 8384 N ND2 . ASN B 2 532 ? 58.650 -23.104 10.178 1.00 96.32 ? 532 ASN B ND2 1 ATOM 8385 N N . SER B 2 533 ? 55.113 -23.064 11.427 1.00 133.47 ? 533 SER B N 1 ATOM 8386 C CA . SER B 2 533 ? 54.694 -24.157 12.309 1.00 127.48 ? 533 SER B CA 1 ATOM 8387 C C . SER B 2 533 ? 55.809 -24.625 13.254 1.00 114.49 ? 533 SER B C 1 ATOM 8388 O O . SER B 2 533 ? 55.621 -25.554 14.041 1.00 99.90 ? 533 SER B O 1 ATOM 8389 C CB . SER B 2 533 ? 54.176 -25.336 11.474 1.00 128.69 ? 533 SER B CB 1 ATOM 8390 O OG . SER B 2 533 ? 53.745 -26.403 12.300 1.00 126.76 ? 533 SER B OG 1 ATOM 8391 N N . ALA B 2 534 ? 56.965 -23.974 13.161 1.00 116.53 ? 534 ALA B N 1 ATOM 8392 C CA . ALA B 2 534 ? 58.123 -24.298 13.984 1.00 109.69 ? 534 ALA B CA 1 ATOM 8393 C C . ALA B 2 534 ? 58.392 -23.174 14.970 1.00 113.66 ? 534 ALA B C 1 ATOM 8394 O O . ALA B 2 534 ? 58.495 -23.410 16.174 1.00 112.03 ? 534 ALA B O 1 ATOM 8395 C CB . ALA B 2 534 ? 59.343 -24.533 13.114 1.00 104.03 ? 534 ALA B CB 1 ATOM 8396 N N . GLY B 2 535 ? 58.513 -21.953 14.455 1.00 115.63 ? 535 GLY B N 1 ATOM 8397 C CA . GLY B 2 535 ? 58.693 -20.791 15.307 1.00 120.17 ? 535 GLY B CA 1 ATOM 8398 C C . GLY B 2 535 ? 59.510 -19.656 14.715 1.00 125.82 ? 535 GLY B C 1 ATOM 8399 O O . GLY B 2 535 ? 59.600 -18.578 15.310 1.00 128.26 ? 535 GLY B O 1 ATOM 8400 N N . SER B 2 536 ? 60.106 -19.888 13.548 1.00 126.95 ? 536 SER B N 1 ATOM 8401 C CA . SER B 2 536 ? 60.936 -18.868 12.899 1.00 119.77 ? 536 SER B CA 1 ATOM 8402 C C . SER B 2 536 ? 60.216 -18.082 11.797 1.00 114.34 ? 536 SER B C 1 ATOM 8403 O O . SER B 2 536 ? 59.201 -18.525 11.247 1.00 94.98 ? 536 SER B O 1 ATOM 8404 C CB . SER B 2 536 ? 62.241 -19.474 12.366 1.00 109.92 ? 536 SER B CB 1 ATOM 8405 O OG . SER B 2 536 ? 62.040 -20.808 11.935 1.00 106.33 ? 536 SER B OG 1 ATOM 8406 N N . VAL B 2 537 ? 60.759 -16.905 11.494 1.00 124.56 ? 537 VAL B N 1 ATOM 8407 C CA . VAL B 2 537 ? 60.195 -16.003 10.493 1.00 129.40 ? 537 VAL B CA 1 ATOM 8408 C C . VAL B 2 537 ? 59.957 -16.711 9.163 1.00 129.96 ? 537 VAL B C 1 ATOM 8409 O O . VAL B 2 537 ? 60.842 -17.400 8.656 1.00 131.41 ? 537 VAL B O 1 ATOM 8410 C CB . VAL B 2 537 ? 61.116 -14.780 10.277 1.00 128.13 ? 537 VAL B CB 1 ATOM 8411 C CG1 . VAL B 2 537 ? 60.563 -13.555 10.991 1.00 124.02 ? 537 VAL B CG1 1 ATOM 8412 C CG2 . VAL B 2 537 ? 62.534 -15.095 10.749 1.00 122.88 ? 537 VAL B CG2 1 ATOM 8413 N N . ALA B 2 538 ? 58.762 -16.542 8.602 1.00 127.76 ? 538 ALA B N 1 ATOM 8414 C CA . ALA B 2 538 ? 58.399 -17.222 7.360 1.00 126.30 ? 538 ALA B CA 1 ATOM 8415 C C . ALA B 2 538 ? 57.118 -16.667 6.733 1.00 130.97 ? 538 ALA B C 1 ATOM 8416 O O . ALA B 2 538 ? 56.016 -17.046 7.137 1.00 135.56 ? 538 ALA B O 1 ATOM 8417 C CB . ALA B 2 538 ? 58.265 -18.733 7.599 1.00 112.82 ? 538 ALA B CB 1 ATOM 8418 N N . PRO B 2 539 ? 57.261 -15.757 5.753 1.00 124.60 ? 539 PRO B N 1 ATOM 8419 C CA . PRO B 2 539 ? 56.135 -15.245 4.958 1.00 125.24 ? 539 PRO B CA 1 ATOM 8420 C C . PRO B 2 539 ? 55.655 -16.243 3.897 1.00 132.68 ? 539 PRO B C 1 ATOM 8421 O O . PRO B 2 539 ? 54.593 -16.040 3.298 1.00 128.74 ? 539 PRO B O 1 ATOM 8422 C CB . PRO B 2 539 ? 56.714 -13.994 4.286 1.00 124.62 ? 539 PRO B CB 1 ATOM 8423 C CG . PRO B 2 539 ? 57.941 -13.654 5.075 1.00 125.85 ? 539 PRO B CG 1 ATOM 8424 C CD . PRO B 2 539 ? 58.482 -14.965 5.541 1.00 122.93 ? 539 PRO B CD 1 ATOM 8425 N N . ASP B 2 540 ? 56.433 -17.301 3.670 1.00 141.95 ? 540 ASP B N 1 ATOM 8426 C CA . ASP B 2 540 ? 56.048 -18.375 2.752 1.00 145.88 ? 540 ASP B CA 1 ATOM 8427 C C . ASP B 2 540 ? 54.929 -19.225 3.348 1.00 139.78 ? 540 ASP B C 1 ATOM 8428 O O . ASP B 2 540 ? 54.079 -19.750 2.623 1.00 138.28 ? 540 ASP B O 1 ATOM 8429 C CB . ASP B 2 540 ? 57.251 -19.274 2.434 1.00 147.85 ? 540 ASP B CB 1 ATOM 8430 C CG . ASP B 2 540 ? 57.948 -18.894 1.134 1.00 147.97 ? 540 ASP B CG 1 ATOM 8431 O OD1 . ASP B 2 540 ? 57.616 -17.827 0.568 1.00 149.24 ? 540 ASP B OD1 1 ATOM 8432 O OD2 . ASP B 2 540 ? 58.825 -19.668 0.679 1.00 139.70 ? 540 ASP B OD2 1 ATOM 8433 N N . SER B 2 541 ? 54.951 -19.340 4.675 1.00 129.40 ? 541 SER B N 1 ATOM 8434 C CA . SER B 2 541 ? 54.053 -20.200 5.451 1.00 113.46 ? 541 SER B CA 1 ATOM 8435 C C . SER B 2 541 ? 52.588 -20.187 5.006 1.00 105.05 ? 541 SER B C 1 ATOM 8436 O O . SER B 2 541 ? 51.950 -21.245 4.930 1.00 102.84 ? 541 SER B O 1 ATOM 8437 C CB . SER B 2 541 ? 54.153 -19.845 6.936 1.00 111.06 ? 541 SER B CB 1 ATOM 8438 O OG . SER B 2 541 ? 55.492 -19.962 7.398 1.00 110.37 ? 541 SER B OG 1 ATOM 8439 N N . ALA B 2 542 ? 52.056 -18.999 4.728 1.00 95.27 ? 542 ALA B N 1 ATOM 8440 C CA . ALA B 2 542 ? 50.701 -18.876 4.194 1.00 100.01 ? 542 ALA B CA 1 ATOM 8441 C C . ALA B 2 542 ? 50.652 -19.373 2.741 1.00 117.04 ? 542 ALA B C 1 ATOM 8442 O O . ALA B 2 542 ? 51.468 -18.953 1.920 1.00 118.08 ? 542 ALA B O 1 ATOM 8443 C CB . ALA B 2 542 ? 50.230 -17.433 4.288 1.00 86.28 ? 542 ALA B CB 1 ATOM 8444 N N . LYS B 2 543 ? 49.709 -20.268 2.430 1.00 123.88 ? 543 LYS B N 1 ATOM 8445 C CA . LYS B 2 543 ? 49.606 -20.853 1.081 1.00 126.56 ? 543 LYS B CA 1 ATOM 8446 C C . LYS B 2 543 ? 48.184 -20.790 0.472 1.00 130.88 ? 543 LYS B C 1 ATOM 8447 O O . LYS B 2 543 ? 47.218 -20.458 1.162 1.00 139.46 ? 543 LYS B O 1 ATOM 8448 C CB . LYS B 2 543 ? 50.114 -22.302 1.075 1.00 117.96 ? 543 LYS B CB 1 ATOM 8449 C CG . LYS B 2 543 ? 51.399 -22.554 1.872 1.00 116.01 ? 543 LYS B CG 1 ATOM 8450 C CD . LYS B 2 543 ? 52.677 -22.524 1.023 1.00 112.96 ? 543 LYS B CD 1 ATOM 8451 C CE . LYS B 2 543 ? 53.723 -23.494 1.597 1.00 105.35 ? 543 LYS B CE 1 ATOM 8452 N NZ . LYS B 2 543 ? 55.143 -23.158 1.277 1.00 97.88 ? 543 LYS B NZ 1 ATOM 8453 N N . CYS B 2 544 ? 48.065 -21.119 -0.818 1.00 120.27 ? 544 CYS B N 1 ATOM 8454 C CA . CYS B 2 544 ? 46.795 -20.997 -1.542 1.00 114.53 ? 544 CYS B CA 1 ATOM 8455 C C . CYS B 2 544 ? 46.074 -22.333 -1.772 1.00 109.84 ? 544 CYS B C 1 ATOM 8456 O O . CYS B 2 544 ? 46.709 -23.360 -2.014 1.00 101.40 ? 544 CYS B O 1 ATOM 8457 C CB . CYS B 2 544 ? 47.013 -20.321 -2.903 1.00 123.52 ? 544 CYS B CB 1 ATOM 8458 S SG . CYS B 2 544 ? 47.643 -18.616 -2.900 1.00 165.71 ? 544 CYS B SG 1 ATOM 8459 N N . SER B 2 545 ? 44.743 -22.304 -1.722 1.00 117.35 ? 545 SER B N 1 ATOM 8460 C CA . SER B 2 545 ? 43.928 -23.476 -2.035 1.00 122.48 ? 545 SER B CA 1 ATOM 8461 C C . SER B 2 545 ? 43.927 -23.726 -3.535 1.00 127.17 ? 545 SER B C 1 ATOM 8462 O O . SER B 2 545 ? 43.023 -23.260 -4.238 1.00 115.89 ? 545 SER B O 1 ATOM 8463 C CB . SER B 2 545 ? 42.475 -23.267 -1.603 1.00 124.74 ? 545 SER B CB 1 ATOM 8464 O OG . SER B 2 545 ? 42.330 -22.136 -0.770 1.00 129.88 ? 545 SER B OG 1 ATOM 8465 N N . GLY B 2 546 ? 44.930 -24.454 -4.025 1.00 135.21 ? 546 GLY B N 1 ATOM 8466 C CA . GLY B 2 546 ? 45.003 -24.789 -5.440 1.00 139.00 ? 546 GLY B CA 1 ATOM 8467 C C . GLY B 2 546 ? 46.406 -24.985 -5.991 1.00 135.89 ? 546 GLY B C 1 ATOM 8468 O O . GLY B 2 546 ? 46.758 -26.067 -6.462 1.00 129.73 ? 546 GLY B O 1 ATOM 8469 N N . SER B 2 547 ? 47.209 -23.929 -5.944 1.00 138.57 ? 547 SER B N 1 ATOM 8470 C CA . SER B 2 547 ? 48.577 -23.999 -6.439 1.00 136.27 ? 547 SER B CA 1 ATOM 8471 C C . SER B 2 547 ? 49.552 -24.378 -5.328 1.00 135.85 ? 547 SER B C 1 ATOM 8472 O O . SER B 2 547 ? 50.456 -25.188 -5.537 1.00 133.23 ? 547 SER B O 1 ATOM 8473 C CB . SER B 2 547 ? 48.986 -22.670 -7.088 1.00 133.05 ? 547 SER B CB 1 ATOM 8474 O OG . SER B 2 547 ? 48.641 -21.563 -6.273 1.00 126.07 ? 547 SER B OG 1 ATOM 8475 N N . GLY B 2 548 ? 49.349 -23.803 -4.145 1.00 137.17 ? 548 GLY B N 1 ATOM 8476 C CA . GLY B 2 548 ? 50.264 -23.980 -3.030 1.00 131.97 ? 548 GLY B CA 1 ATOM 8477 C C . GLY B 2 548 ? 51.224 -22.810 -2.993 1.00 130.66 ? 548 GLY B C 1 ATOM 8478 O O . GLY B 2 548 ? 52.211 -22.804 -2.252 1.00 122.49 ? 548 GLY B O 1 ATOM 8479 N N . LYS B 2 549 ? 50.918 -21.812 -3.816 1.00 138.17 ? 549 LYS B N 1 ATOM 8480 C CA . LYS B 2 549 ? 51.763 -20.636 -3.969 1.00 139.74 ? 549 LYS B CA 1 ATOM 8481 C C . LYS B 2 549 ? 51.651 -19.733 -2.751 1.00 135.63 ? 549 LYS B C 1 ATOM 8482 O O . LYS B 2 549 ? 50.546 -19.392 -2.330 1.00 135.81 ? 549 LYS B O 1 ATOM 8483 C CB . LYS B 2 549 ? 51.379 -19.848 -5.237 1.00 138.73 ? 549 LYS B CB 1 ATOM 8484 C CG . LYS B 2 549 ? 51.814 -20.479 -6.562 1.00 131.09 ? 549 LYS B CG 1 ATOM 8485 C CD . LYS B 2 549 ? 51.354 -19.636 -7.750 1.00 127.13 ? 549 LYS B CD 1 ATOM 8486 C CE . LYS B 2 549 ? 51.515 -20.374 -9.082 1.00 115.75 ? 549 LYS B CE 1 ATOM 8487 N NZ . LYS B 2 549 ? 50.658 -19.781 -10.153 1.00 106.35 ? 549 LYS B NZ 1 ATOM 8488 N N . PRO B 2 550 ? 52.800 -19.357 -2.174 1.00 134.14 ? 550 PRO B N 1 ATOM 8489 C CA . PRO B 2 550 ? 52.880 -18.332 -1.126 1.00 140.60 ? 550 PRO B CA 1 ATOM 8490 C C . PRO B 2 550 ? 52.062 -17.072 -1.449 1.00 137.51 ? 550 PRO B C 1 ATOM 8491 O O . PRO B 2 550 ? 52.330 -16.397 -2.441 1.00 136.89 ? 550 PRO B O 1 ATOM 8492 C CB . PRO B 2 550 ? 54.374 -18.019 -1.078 1.00 144.96 ? 550 PRO B CB 1 ATOM 8493 C CG . PRO B 2 550 ? 55.021 -19.346 -1.411 1.00 139.20 ? 550 PRO B CG 1 ATOM 8494 C CD . PRO B 2 550 ? 54.089 -20.048 -2.373 1.00 131.88 ? 550 PRO B CD 1 ATOM 8495 N N . VAL B 2 551 ? 51.082 -16.768 -0.600 1.00 137.01 ? 551 VAL B N 1 ATOM 8496 C CA . VAL B 2 551 ? 50.148 -15.665 -0.819 1.00 141.75 ? 551 VAL B CA 1 ATOM 8497 C C . VAL B 2 551 ? 50.842 -14.326 -1.056 1.00 149.70 ? 551 VAL B C 1 ATOM 8498 O O . VAL B 2 551 ? 50.281 -13.437 -1.699 1.00 149.68 ? 551 VAL B O 1 ATOM 8499 C CB . VAL B 2 551 ? 49.186 -15.502 0.382 1.00 138.70 ? 551 VAL B CB 1 ATOM 8500 C CG1 . VAL B 2 551 ? 48.070 -14.520 0.047 1.00 142.36 ? 551 VAL B CG1 1 ATOM 8501 C CG2 . VAL B 2 551 ? 48.614 -16.848 0.799 1.00 131.37 ? 551 VAL B CG2 1 ATOM 8502 N N . ARG B 2 552 ? 52.054 -14.181 -0.526 1.00 153.85 ? 552 ARG B N 1 ATOM 8503 C CA . ARG B 2 552 ? 52.798 -12.927 -0.641 1.00 151.76 ? 552 ARG B CA 1 ATOM 8504 C C . ARG B 2 552 ? 53.529 -12.807 -1.976 1.00 153.84 ? 552 ARG B C 1 ATOM 8505 O O . ARG B 2 552 ? 54.109 -11.765 -2.286 1.00 162.40 ? 552 ARG B O 1 ATOM 8506 C CB . ARG B 2 552 ? 53.772 -12.759 0.529 1.00 142.77 ? 552 ARG B CB 1 ATOM 8507 C CG . ARG B 2 552 ? 54.508 -14.025 0.935 1.00 138.38 ? 552 ARG B CG 1 ATOM 8508 C CD . ARG B 2 552 ? 55.505 -14.467 -0.116 1.00 143.07 ? 552 ARG B CD 1 ATOM 8509 N NE . ARG B 2 552 ? 56.731 -14.974 0.492 1.00 148.04 ? 552 ARG B NE 1 ATOM 8510 C CZ . ARG B 2 552 ? 57.796 -14.221 0.753 1.00 154.47 ? 552 ARG B CZ 1 ATOM 8511 N NH1 . ARG B 2 552 ? 57.787 -12.927 0.453 1.00 154.67 ? 552 ARG B NH1 1 ATOM 8512 N NH2 . ARG B 2 552 ? 58.872 -14.760 1.313 1.00 154.29 ? 552 ARG B NH2 1 ATOM 8513 N N . SER B 2 553 ? 53.499 -13.881 -2.759 1.00 144.09 ? 553 SER B N 1 ATOM 8514 C CA . SER B 2 553 ? 54.060 -13.863 -4.101 1.00 139.46 ? 553 SER B CA 1 ATOM 8515 C C . SER B 2 553 ? 53.123 -13.096 -5.026 1.00 142.65 ? 553 SER B C 1 ATOM 8516 O O . SER B 2 553 ? 53.559 -12.325 -5.884 1.00 149.55 ? 553 SER B O 1 ATOM 8517 C CB . SER B 2 553 ? 54.226 -15.289 -4.627 1.00 129.58 ? 553 SER B CB 1 ATOM 8518 O OG . SER B 2 553 ? 53.017 -15.763 -5.204 1.00 120.66 ? 553 SER B OG 1 ATOM 8519 N N . ILE B 2 554 ? 51.828 -13.312 -4.822 1.00 135.48 ? 554 ILE B N 1 ATOM 8520 C CA . ILE B 2 554 ? 50.781 -12.804 -5.703 1.00 136.58 ? 554 ILE B CA 1 ATOM 8521 C C . ILE B 2 554 ? 50.709 -11.271 -5.839 1.00 146.22 ? 554 ILE B C 1 ATOM 8522 O O . ILE B 2 554 ? 50.751 -10.538 -4.845 1.00 140.85 ? 554 ILE B O 1 ATOM 8523 C CB . ILE B 2 554 ? 49.414 -13.381 -5.284 1.00 127.84 ? 554 ILE B CB 1 ATOM 8524 C CG1 . ILE B 2 554 ? 49.459 -14.911 -5.347 1.00 116.02 ? 554 ILE B CG1 1 ATOM 8525 C CG2 . ILE B 2 554 ? 48.295 -12.823 -6.151 1.00 133.90 ? 554 ILE B CG2 1 ATOM 8526 C CD1 . ILE B 2 554 ? 48.114 -15.549 -5.624 1.00 113.15 ? 554 ILE B CD1 1 ATOM 8527 N N . ILE B 2 555 ? 50.599 -10.805 -7.086 1.00 157.12 ? 555 ILE B N 1 ATOM 8528 C CA . ILE B 2 555 ? 50.546 -9.376 -7.406 1.00 163.68 ? 555 ILE B CA 1 ATOM 8529 C C . ILE B 2 555 ? 49.258 -9.016 -8.155 1.00 162.19 ? 555 ILE B C 1 ATOM 8530 O O . ILE B 2 555 ? 49.092 -9.354 -9.326 1.00 163.99 ? 555 ILE B O 1 ATOM 8531 C CB . ILE B 2 555 ? 51.769 -8.932 -8.261 1.00 125.42 ? 555 ILE B CB 1 ATOM 8532 C CG1 . ILE B 2 555 ? 53.085 -9.491 -7.687 1.00 117.31 ? 555 ILE B CG1 1 ATOM 8533 C CG2 . ILE B 2 555 ? 51.798 -7.401 -8.435 1.00 126.00 ? 555 ILE B CG2 1 ATOM 8534 C CD1 . ILE B 2 555 ? 53.396 -9.077 -6.253 1.00 113.90 ? 555 ILE B CD1 1 ATOM 8535 N N . CYS B 2 556 ? 48.352 -8.322 -7.477 1.00 159.07 ? 556 CYS B N 1 ATOM 8536 C CA . CYS B 2 556 ? 47.064 -7.980 -8.061 1.00 161.36 ? 556 CYS B CA 1 ATOM 8537 C C . CYS B 2 556 ? 46.969 -6.490 -8.346 1.00 165.94 ? 556 CYS B C 1 ATOM 8538 O O . CYS B 2 556 ? 46.857 -5.688 -7.419 1.00 161.56 ? 556 CYS B O 1 ATOM 8539 C CB . CYS B 2 556 ? 45.935 -8.408 -7.129 1.00 163.19 ? 556 CYS B CB 1 ATOM 8540 S SG . CYS B 2 556 ? 45.977 -10.155 -6.673 1.00 196.02 ? 556 CYS B SG 1 ATOM 8541 N N . PRO B 2 557 ? 47.010 -6.123 -9.640 1.00 175.64 ? 557 PRO B N 1 ATOM 8542 C CA . PRO B 2 557 ? 47.029 -4.756 -10.189 1.00 181.45 ? 557 PRO B CA 1 ATOM 8543 C C . PRO B 2 557 ? 45.684 -4.014 -10.156 1.00 179.56 ? 557 PRO B C 1 ATOM 8544 O O . PRO B 2 557 ? 44.610 -4.617 -10.160 1.00 181.02 ? 557 PRO B O 1 ATOM 8545 C CB . PRO B 2 557 ? 47.462 -4.972 -11.648 1.00 183.50 ? 557 PRO B CB 1 ATOM 8546 C CG . PRO B 2 557 ? 47.995 -6.383 -11.705 1.00 178.07 ? 557 PRO B CG 1 ATOM 8547 C CD . PRO B 2 557 ? 47.211 -7.133 -10.692 1.00 172.81 ? 557 PRO B CD 1 ATOM 8548 N N . CYS C 3 1 ? 28.536 -42.247 40.877 1.00 65.49 ? 11 CYS C N 1 ATOM 8549 C CA . CYS C 3 1 ? 27.220 -41.928 41.415 1.00 62.30 ? 11 CYS C CA 1 ATOM 8550 C C . CYS C 3 1 ? 27.284 -42.164 42.899 1.00 64.07 ? 11 CYS C C 1 ATOM 8551 O O . CYS C 3 1 ? 28.245 -42.745 43.375 1.00 67.54 ? 11 CYS C O 1 ATOM 8552 C CB . CYS C 3 1 ? 26.166 -42.844 40.798 1.00 62.83 ? 11 CYS C CB 1 ATOM 8553 S SG . CYS C 3 1 ? 26.205 -42.915 39.006 1.00 77.56 ? 11 CYS C SG 1 ATOM 8554 N N . SER C 3 2 ? 26.275 -41.732 43.642 1.00 61.26 ? 12 SER C N 1 ATOM 8555 C CA . SER C 3 2 ? 26.279 -42.014 45.071 1.00 79.27 ? 12 SER C CA 1 ATOM 8556 C C . SER C 3 2 ? 25.040 -42.751 45.545 1.00 96.47 ? 12 SER C C 1 ATOM 8557 O O . SER C 3 2 ? 23.947 -42.535 45.032 1.00 98.76 ? 12 SER C O 1 ATOM 8558 C CB . SER C 3 2 ? 26.499 -40.746 45.895 1.00 65.91 ? 12 SER C CB 1 ATOM 8559 O OG . SER C 3 2 ? 25.913 -39.629 45.275 1.00 72.03 ? 12 SER C OG 1 ATOM 8560 N N . LYS C 3 3 ? 25.231 -43.630 46.524 1.00 98.45 ? 13 LYS C N 1 ATOM 8561 C CA . LYS C 3 3 ? 24.127 -44.297 47.190 1.00 100.79 ? 13 LYS C CA 1 ATOM 8562 C C . LYS C 3 3 ? 23.415 -43.298 48.097 1.00 112.10 ? 13 LYS C C 1 ATOM 8563 O O . LYS C 3 3 ? 23.851 -42.155 48.217 1.00 120.41 ? 13 LYS C O 1 ATOM 8564 C CB . LYS C 3 3 ? 24.654 -45.481 47.985 1.00 104.06 ? 13 LYS C CB 1 ATOM 8565 C CG . LYS C 3 3 ? 25.355 -46.511 47.116 1.00 103.29 ? 13 LYS C CG 1 ATOM 8566 C CD . LYS C 3 3 ? 26.482 -47.196 47.877 1.00 95.50 ? 13 LYS C CD 1 ATOM 8567 C CE . LYS C 3 3 ? 27.606 -46.211 48.224 1.00 83.89 ? 13 LYS C CE 1 ATOM 8568 N NZ . LYS C 3 3 ? 28.859 -46.903 48.655 1.00 71.40 ? 13 LYS C NZ 1 ATOM 8569 N N . LYS C 3 4 ? 22.323 -43.717 48.731 1.00 115.02 ? 14 LYS C N 1 ATOM 8570 C CA . LYS C 3 4 ? 21.469 -42.777 49.459 1.00 120.70 ? 14 LYS C CA 1 ATOM 8571 C C . LYS C 3 4 ? 22.063 -42.309 50.794 1.00 143.87 ? 14 LYS C C 1 ATOM 8572 O O . LYS C 3 4 ? 23.163 -41.754 50.830 1.00 150.44 ? 14 LYS C O 1 ATOM 8573 C CB . LYS C 3 4 ? 20.064 -43.353 49.646 1.00 109.14 ? 14 LYS C CB 1 ATOM 8574 C CG . LYS C 3 4 ? 19.024 -42.356 50.162 1.00 105.17 ? 14 LYS C CG 1 ATOM 8575 C CD . LYS C 3 4 ? 19.175 -40.974 49.540 1.00 101.59 ? 14 LYS C CD 1 ATOM 8576 C CE . LYS C 3 4 ? 18.062 -40.039 50.009 1.00 103.03 ? 14 LYS C CE 1 ATOM 8577 N NZ . LYS C 3 4 ? 18.409 -38.597 49.822 1.00 104.51 ? 14 LYS C NZ 1 ATOM 8578 N N . LYS C 3 5 ? 21.331 -42.518 51.886 1.00 151.32 ? 15 LYS C N 1 ATOM 8579 C CA . LYS C 3 5 ? 21.760 -42.025 53.194 1.00 151.98 ? 15 LYS C CA 1 ATOM 8580 C C . LYS C 3 5 ? 21.530 -43.061 54.309 1.00 156.95 ? 15 LYS C C 1 ATOM 8581 O O . LYS C 3 5 ? 21.235 -42.700 55.453 1.00 155.66 ? 15 LYS C O 1 ATOM 8582 C CB . LYS C 3 5 ? 21.057 -40.698 53.530 1.00 145.87 ? 15 LYS C CB 1 ATOM 8583 C CG . LYS C 3 5 ? 20.802 -39.767 52.333 1.00 136.52 ? 15 LYS C CG 1 ATOM 8584 C CD . LYS C 3 5 ? 22.077 -39.121 51.783 1.00 132.68 ? 15 LYS C CD 1 ATOM 8585 C CE . LYS C 3 5 ? 22.526 -37.928 52.624 1.00 130.41 ? 15 LYS C CE 1 ATOM 8586 N NZ . LYS C 3 5 ? 23.562 -37.100 51.938 1.00 122.18 ? 15 LYS C NZ 1 ATOM 8587 N N . LYS C 3 6 ? 21.667 -44.343 53.967 1.00 157.40 ? 16 LYS C N 1 ATOM 8588 C CA . LYS C 3 6 ? 21.540 -45.439 54.936 1.00 149.56 ? 16 LYS C CA 1 ATOM 8589 C C . LYS C 3 6 ? 22.826 -46.263 55.031 1.00 138.73 ? 16 LYS C C 1 ATOM 8590 O O . LYS C 3 6 ? 22.951 -47.140 55.884 1.00 133.09 ? 16 LYS C O 1 ATOM 8591 C CB . LYS C 3 6 ? 20.360 -46.357 54.584 1.00 145.16 ? 16 LYS C CB 1 ATOM 8592 C CG . LYS C 3 6 ? 18.984 -45.759 54.859 1.00 142.25 ? 16 LYS C CG 1 ATOM 8593 C CD . LYS C 3 6 ? 17.859 -46.704 54.443 1.00 138.40 ? 16 LYS C CD 1 ATOM 8594 C CE . LYS C 3 6 ? 16.498 -46.005 54.473 1.00 130.85 ? 16 LYS C CE 1 ATOM 8595 N NZ . LYS C 3 6 ? 15.404 -46.847 53.914 1.00 120.75 ? 16 LYS C NZ 1 ATOM 8596 O OXT . LYS C 3 6 ? 23.769 -46.080 54.258 1.00 134.55 ? 16 LYS C OXT 1 HETATM 8597 C C1 . NAG D 4 . ? -21.128 -22.339 10.943 1.00 141.17 ? 811 NAG A C1 1 HETATM 8598 C C2 . NAG D 4 . ? -22.351 -23.069 11.499 1.00 146.33 ? 811 NAG A C2 1 HETATM 8599 C C3 . NAG D 4 . ? -23.533 -22.097 11.439 1.00 147.79 ? 811 NAG A C3 1 HETATM 8600 C C4 . NAG D 4 . ? -23.218 -20.840 12.255 1.00 147.54 ? 811 NAG A C4 1 HETATM 8601 C C5 . NAG D 4 . ? -21.858 -20.208 11.907 1.00 149.31 ? 811 NAG A C5 1 HETATM 8602 C C6 . NAG D 4 . ? -21.455 -19.200 12.998 1.00 136.62 ? 811 NAG A C6 1 HETATM 8603 C C7 . NAG D 4 . ? -22.369 -25.559 11.268 1.00 115.20 ? 811 NAG A C7 1 HETATM 8604 C C8 . NAG D 4 . ? -21.280 -26.359 10.603 1.00 100.19 ? 811 NAG A C8 1 HETATM 8605 N N2 . NAG D 4 . ? -22.596 -24.324 10.782 1.00 139.78 ? 811 NAG A N2 1 HETATM 8606 O O3 . NAG D 4 . ? -24.723 -22.694 11.913 1.00 145.80 ? 811 NAG A O3 1 HETATM 8607 O O4 . NAG D 4 . ? -24.254 -19.891 12.081 1.00 140.85 ? 811 NAG A O4 1 HETATM 8608 O O5 . NAG D 4 . ? -20.822 -21.170 11.706 1.00 153.54 ? 811 NAG A O5 1 HETATM 8609 O O6 . NAG D 4 . ? -20.100 -18.800 12.913 1.00 123.91 ? 811 NAG A O6 1 HETATM 8610 O O7 . NAG D 4 . ? -23.016 -26.055 12.195 1.00 96.96 ? 811 NAG A O7 1 HETATM 8611 C C1 . NAG E 4 . ? 20.957 -62.836 24.638 1.00 95.81 ? 821 NAG A C1 1 HETATM 8612 C C2 . NAG E 4 . ? 21.358 -63.693 25.845 1.00 109.41 ? 821 NAG A C2 1 HETATM 8613 C C3 . NAG E 4 . ? 20.276 -64.706 26.220 1.00 117.09 ? 821 NAG A C3 1 HETATM 8614 C C4 . NAG E 4 . ? 18.916 -64.015 26.310 1.00 115.06 ? 821 NAG A C4 1 HETATM 8615 C C5 . NAG E 4 . ? 18.620 -63.263 25.019 1.00 109.03 ? 821 NAG A C5 1 HETATM 8616 C C6 . NAG E 4 . ? 17.298 -62.520 25.149 1.00 109.82 ? 821 NAG A C6 1 HETATM 8617 C C7 . NAG E 4 . ? 22.970 -64.951 24.457 1.00 114.13 ? 821 NAG A C7 1 HETATM 8618 C C8 . NAG E 4 . ? 24.298 -64.577 23.857 1.00 96.61 ? 821 NAG A C8 1 HETATM 8619 N N2 . NAG E 4 . ? 22.632 -64.373 25.619 1.00 114.50 ? 821 NAG A N2 1 HETATM 8620 O O3 . NAG E 4 . ? 20.615 -65.306 27.455 1.00 122.65 ? 821 NAG A O3 1 HETATM 8621 O O4 . NAG E 4 . ? 17.864 -64.928 26.573 1.00 114.04 ? 821 NAG A O4 1 HETATM 8622 O O5 . NAG E 4 . ? 19.637 -62.326 24.731 1.00 97.63 ? 821 NAG A O5 1 HETATM 8623 O O6 . NAG E 4 . ? 17.317 -61.794 26.357 1.00 104.29 ? 821 NAG A O6 1 HETATM 8624 O O7 . NAG E 4 . ? 22.251 -65.771 23.878 1.00 122.19 ? 821 NAG A O7 1 HETATM 8625 C C1 . NAG F 4 . ? 28.990 -43.568 11.731 1.00 71.60 ? 831 NAG A C1 1 HETATM 8626 C C2 . NAG F 4 . ? 27.679 -43.404 10.956 1.00 84.85 ? 831 NAG A C2 1 HETATM 8627 C C3 . NAG F 4 . ? 27.592 -42.069 10.210 1.00 87.66 ? 831 NAG A C3 1 HETATM 8628 C C4 . NAG F 4 . ? 28.024 -40.879 11.072 1.00 90.25 ? 831 NAG A C4 1 HETATM 8629 C C5 . NAG F 4 . ? 29.300 -41.163 11.888 1.00 91.18 ? 831 NAG A C5 1 HETATM 8630 C C6 . NAG F 4 . ? 29.581 -40.096 12.960 1.00 86.59 ? 831 NAG A C6 1 HETATM 8631 C C7 . NAG F 4 . ? 26.516 -45.381 10.144 1.00 92.15 ? 831 NAG A C7 1 HETATM 8632 C C8 . NAG F 4 . ? 26.559 -46.570 9.233 1.00 80.39 ? 831 NAG A C8 1 HETATM 8633 N N2 . NAG F 4 . ? 27.515 -44.506 10.019 1.00 90.51 ? 831 NAG A N2 1 HETATM 8634 O O3 . NAG F 4 . ? 26.284 -41.848 9.708 1.00 76.15 ? 831 NAG A O3 1 HETATM 8635 O O4 . NAG F 4 . ? 28.168 -39.767 10.196 1.00 82.87 ? 831 NAG A O4 1 HETATM 8636 O O5 . NAG F 4 . ? 29.278 -42.433 12.526 1.00 83.09 ? 831 NAG A O5 1 HETATM 8637 O O6 . NAG F 4 . ? 28.766 -40.245 14.113 1.00 80.28 ? 831 NAG A O6 1 HETATM 8638 O O7 . NAG F 4 . ? 25.592 -45.246 10.953 1.00 97.76 ? 831 NAG A O7 1 HETATM 8639 C C1 . NAG G 4 . ? 27.285 -38.706 10.596 1.00 93.18 ? 832 NAG A C1 1 HETATM 8640 C C2 . NAG G 4 . ? 27.756 -37.415 9.935 1.00 99.39 ? 832 NAG A C2 1 HETATM 8641 C C3 . NAG G 4 . ? 26.737 -36.277 9.914 1.00 106.65 ? 832 NAG A C3 1 HETATM 8642 C C4 . NAG G 4 . ? 25.284 -36.740 9.860 1.00 111.78 ? 832 NAG A C4 1 HETATM 8643 C C5 . NAG G 4 . ? 25.052 -37.986 10.699 1.00 111.62 ? 832 NAG A C5 1 HETATM 8644 C C6 . NAG G 4 . ? 23.623 -38.488 10.541 1.00 116.63 ? 832 NAG A C6 1 HETATM 8645 C C7 . NAG G 4 . ? 30.089 -36.903 9.804 1.00 121.16 ? 832 NAG A C7 1 HETATM 8646 C C8 . NAG G 4 . ? 30.582 -35.527 9.446 1.00 120.68 ? 832 NAG A C8 1 HETATM 8647 N N2 . NAG G 4 . ? 28.987 -36.965 10.543 1.00 111.82 ? 832 NAG A N2 1 HETATM 8648 O O3 . NAG G 4 . ? 27.007 -35.475 8.781 1.00 107.10 ? 832 NAG A O3 1 HETATM 8649 O O4 . NAG G 4 . ? 24.441 -35.711 10.333 1.00 109.80 ? 832 NAG A O4 1 HETATM 8650 O O5 . NAG G 4 . ? 25.940 -39.002 10.300 1.00 106.53 ? 832 NAG A O5 1 HETATM 8651 O O6 . NAG G 4 . ? 23.382 -39.476 11.520 1.00 126.22 ? 832 NAG A O6 1 HETATM 8652 O O7 . NAG G 4 . ? 30.679 -37.914 9.419 1.00 122.97 ? 832 NAG A O7 1 HETATM 8653 C C1 . NAG H 4 . ? 92.432 -44.541 47.087 1.00 64.24 ? 911 NAG B C1 1 HETATM 8654 C C2 . NAG H 4 . ? 93.220 -45.739 46.514 1.00 78.46 ? 911 NAG B C2 1 HETATM 8655 C C3 . NAG H 4 . ? 94.631 -45.410 45.961 1.00 84.38 ? 911 NAG B C3 1 HETATM 8656 C C4 . NAG H 4 . ? 94.506 -44.237 44.983 1.00 80.10 ? 911 NAG B C4 1 HETATM 8657 C C5 . NAG H 4 . ? 93.728 -43.069 45.596 1.00 79.04 ? 911 NAG B C5 1 HETATM 8658 C C6 . NAG H 4 . ? 93.432 -42.061 44.491 1.00 91.87 ? 911 NAG B C6 1 HETATM 8659 C C7 . NAG H 4 . ? 92.625 -47.966 47.197 1.00 99.85 ? 911 NAG B C7 1 HETATM 8660 C C8 . NAG H 4 . ? 93.186 -49.225 47.795 1.00 98.43 ? 911 NAG B C8 1 HETATM 8661 N N2 . NAG H 4 . ? 93.247 -46.823 47.481 1.00 83.88 ? 911 NAG B N2 1 HETATM 8662 O O3 . NAG H 4 . ? 95.286 -46.529 45.343 1.00 73.86 ? 911 NAG B O3 1 HETATM 8663 O O4 . NAG H 4 . ? 95.768 -43.764 44.534 1.00 76.34 ? 911 NAG B O4 1 HETATM 8664 O O5 . NAG H 4 . ? 92.493 -43.414 46.216 1.00 75.86 ? 911 NAG B O5 1 HETATM 8665 O O6 . NAG H 4 . ? 92.512 -41.110 44.970 1.00 96.34 ? 911 NAG B O6 1 HETATM 8666 O O7 . NAG H 4 . ? 91.631 -48.008 46.469 1.00 110.63 ? 911 NAG B O7 1 HETATM 8667 C C1 . NAG I 4 . ? 64.848 -43.597 65.695 1.00 127.51 ? 921 NAG B C1 1 HETATM 8668 C C2 . NAG I 4 . ? 64.345 -43.328 67.122 1.00 138.10 ? 921 NAG B C2 1 HETATM 8669 C C3 . NAG I 4 . ? 64.668 -41.892 67.528 1.00 131.83 ? 921 NAG B C3 1 HETATM 8670 C C4 . NAG I 4 . ? 66.170 -41.666 67.466 1.00 132.29 ? 921 NAG B C4 1 HETATM 8671 C C5 . NAG I 4 . ? 66.781 -42.057 66.107 1.00 132.51 ? 921 NAG B C5 1 HETATM 8672 C C6 . NAG I 4 . ? 68.315 -42.170 66.263 1.00 117.21 ? 921 NAG B C6 1 HETATM 8673 C C7 . NAG I 4 . ? 62.114 -44.402 66.681 1.00 147.29 ? 921 NAG B C7 1 HETATM 8674 C C8 . NAG I 4 . ? 62.136 -45.859 67.052 1.00 140.58 ? 921 NAG B C8 1 HETATM 8675 N N2 . NAG I 4 . ? 62.927 -43.599 67.372 1.00 146.92 ? 921 NAG B N2 1 HETATM 8676 O O3 . NAG I 4 . ? 64.205 -41.632 68.837 1.00 123.75 ? 921 NAG B O3 1 HETATM 8677 O O4 . NAG I 4 . ? 66.424 -40.310 67.776 1.00 130.58 ? 921 NAG B O4 1 HETATM 8678 O O5 . NAG I 4 . ? 66.243 -43.277 65.580 1.00 136.40 ? 921 NAG B O5 1 HETATM 8679 O O6 . NAG I 4 . ? 69.079 -42.186 65.068 1.00 91.23 ? 921 NAG B O6 1 HETATM 8680 O O7 . NAG I 4 . ? 61.352 -43.991 65.799 1.00 149.05 ? 921 NAG B O7 1 HETATM 8681 C C1 . NAG J 4 . ? 62.011 -29.079 45.482 1.00 99.77 ? 931 NAG B C1 1 HETATM 8682 C C2 . NAG J 4 . ? 63.442 -28.999 44.915 1.00 118.27 ? 931 NAG B C2 1 HETATM 8683 C C3 . NAG J 4 . ? 63.726 -27.985 43.798 1.00 121.44 ? 931 NAG B C3 1 HETATM 8684 C C4 . NAG J 4 . ? 62.509 -27.433 43.068 1.00 117.50 ? 931 NAG B C4 1 HETATM 8685 C C5 . NAG J 4 . ? 61.256 -27.388 43.920 1.00 106.35 ? 931 NAG B C5 1 HETATM 8686 C C6 . NAG J 4 . ? 60.100 -27.243 42.951 1.00 99.26 ? 931 NAG B C6 1 HETATM 8687 C C7 . NAG J 4 . ? 64.158 -28.125 47.133 1.00 102.68 ? 931 NAG B C7 1 HETATM 8688 C C8 . NAG J 4 . ? 63.441 -26.797 47.120 1.00 89.24 ? 931 NAG B C8 1 HETATM 8689 N N2 . NAG J 4 . ? 64.419 -28.713 45.962 1.00 120.97 ? 931 NAG B N2 1 HETATM 8690 O O3 . NAG J 4 . ? 64.560 -28.609 42.844 1.00 120.65 ? 931 NAG B O3 1 HETATM 8691 O O4 . NAG J 4 . ? 62.804 -26.142 42.562 1.00 124.48 ? 931 NAG B O4 1 HETATM 8692 O O5 . NAG J 4 . ? 61.023 -28.603 44.596 1.00 104.81 ? 931 NAG B O5 1 HETATM 8693 O O6 . NAG J 4 . ? 60.174 -28.321 42.038 1.00 93.54 ? 931 NAG B O6 1 HETATM 8694 O O7 . NAG J 4 . ? 64.510 -28.647 48.190 1.00 89.31 ? 931 NAG B O7 1 HETATM 8695 C C1 . NAG K 4 . ? 62.965 -26.183 41.115 1.00 139.79 ? 932 NAG B C1 1 HETATM 8696 C C2 . NAG K 4 . ? 61.646 -25.830 40.399 1.00 136.55 ? 932 NAG B C2 1 HETATM 8697 C C3 . NAG K 4 . ? 61.400 -24.323 40.504 1.00 135.70 ? 932 NAG B C3 1 HETATM 8698 C C4 . NAG K 4 . ? 62.424 -23.714 41.459 1.00 138.47 ? 932 NAG B C4 1 HETATM 8699 C C5 . NAG K 4 . ? 63.832 -23.973 40.913 1.00 145.44 ? 932 NAG B C5 1 HETATM 8700 C C6 . NAG K 4 . ? 64.922 -23.499 41.874 1.00 143.94 ? 932 NAG B C6 1 HETATM 8701 C C7 . NAG K 4 . ? 60.615 -27.131 38.579 1.00 102.18 ? 932 NAG B C7 1 HETATM 8702 C C8 . NAG K 4 . ? 59.192 -26.653 38.698 1.00 87.33 ? 932 NAG B C8 1 HETATM 8703 N N2 . NAG K 4 . ? 61.577 -26.301 39.014 1.00 120.51 ? 932 NAG B N2 1 HETATM 8704 O O3 . NAG K 4 . ? 60.093 -24.064 40.966 1.00 129.18 ? 932 NAG B O3 1 HETATM 8705 O O4 . NAG K 4 . ? 62.187 -22.336 41.644 1.00 129.74 ? 932 NAG B O4 1 HETATM 8706 O O5 . NAG K 4 . ? 64.012 -25.354 40.632 1.00 145.88 ? 932 NAG B O5 1 HETATM 8707 O O6 . NAG K 4 . ? 65.081 -24.413 42.938 1.00 137.66 ? 932 NAG B O6 1 HETATM 8708 O O7 . NAG K 4 . ? 60.848 -28.245 38.097 1.00 92.62 ? 932 NAG B O7 1 HETATM 8709 C C1 . NAG L 4 . ? 51.127 -48.173 39.153 1.00 61.96 ? 941 NAG B C1 1 HETATM 8710 C C2 . NAG L 4 . ? 52.138 -48.800 38.184 1.00 67.84 ? 941 NAG B C2 1 HETATM 8711 C C3 . NAG L 4 . ? 52.124 -50.322 38.138 1.00 62.27 ? 941 NAG B C3 1 HETATM 8712 C C4 . NAG L 4 . ? 51.799 -50.990 39.477 1.00 69.00 ? 941 NAG B C4 1 HETATM 8713 C C5 . NAG L 4 . ? 50.811 -50.224 40.353 1.00 60.86 ? 941 NAG B C5 1 HETATM 8714 C C6 . NAG L 4 . ? 50.831 -50.811 41.763 1.00 58.81 ? 941 NAG B C6 1 HETATM 8715 C C7 . NAG L 4 . ? 52.838 -47.568 36.170 1.00 80.15 ? 941 NAG B C7 1 HETATM 8716 C C8 . NAG L 4 . ? 52.288 -46.486 35.290 1.00 68.12 ? 941 NAG B C8 1 HETATM 8717 N N2 . NAG L 4 . ? 51.934 -48.317 36.826 1.00 79.92 ? 941 NAG B N2 1 HETATM 8718 O O3 . NAG L 4 . ? 53.412 -50.730 37.730 1.00 64.46 ? 941 NAG B O3 1 HETATM 8719 O O4 . NAG L 4 . ? 51.309 -52.298 39.229 1.00 73.35 ? 941 NAG B O4 1 HETATM 8720 O O5 . NAG L 4 . ? 51.105 -48.841 40.404 1.00 61.10 ? 941 NAG B O5 1 HETATM 8721 O O6 . NAG L 4 . ? 49.908 -50.150 42.602 1.00 69.13 ? 941 NAG B O6 1 HETATM 8722 O O7 . NAG L 4 . ? 54.062 -47.711 36.242 1.00 78.46 ? 941 NAG B O7 1 HETATM 8723 C C1 . NAG M 4 . ? 52.192 -53.265 39.816 1.00 74.39 ? 942 NAG B C1 1 HETATM 8724 C C2 . NAG M 4 . ? 51.414 -54.550 40.103 1.00 74.03 ? 942 NAG B C2 1 HETATM 8725 C C3 . NAG M 4 . ? 52.333 -55.744 40.406 1.00 76.68 ? 942 NAG B C3 1 HETATM 8726 C C4 . NAG M 4 . ? 53.530 -55.803 39.467 1.00 79.35 ? 942 NAG B C4 1 HETATM 8727 C C5 . NAG M 4 . ? 54.211 -54.451 39.465 1.00 82.51 ? 942 NAG B C5 1 HETATM 8728 C C6 . NAG M 4 . ? 55.419 -54.481 38.553 1.00 86.55 ? 942 NAG B C6 1 HETATM 8729 C C7 . NAG M 4 . ? 49.139 -54.465 40.931 1.00 71.58 ? 942 NAG B C7 1 HETATM 8730 C C8 . NAG M 4 . ? 48.189 -54.197 42.065 1.00 64.60 ? 942 NAG B C8 1 HETATM 8731 N N2 . NAG M 4 . ? 50.449 -54.322 41.167 1.00 76.69 ? 942 NAG B N2 1 HETATM 8732 O O3 . NAG M 4 . ? 51.647 -56.985 40.426 1.00 70.08 ? 942 NAG B O3 1 HETATM 8733 O O4 . NAG M 4 . ? 54.443 -56.750 39.968 1.00 89.87 ? 942 NAG B O4 1 HETATM 8734 O O5 . NAG M 4 . ? 53.319 -53.471 38.993 1.00 79.36 ? 942 NAG B O5 1 HETATM 8735 O O6 . NAG M 4 . ? 54.921 -54.475 37.238 1.00 86.40 ? 942 NAG B O6 1 HETATM 8736 O O7 . NAG M 4 . ? 48.695 -54.799 39.832 1.00 63.60 ? 942 NAG B O7 1 HETATM 8737 C C1 . BMA N 5 . ? 54.446 -57.952 39.182 1.00 102.39 ? 943 BMA B C1 1 HETATM 8738 C C2 . BMA N 5 . ? 55.890 -58.206 38.736 1.00 106.17 ? 943 BMA B C2 1 HETATM 8739 C C3 . BMA N 5 . ? 56.057 -59.599 38.112 1.00 112.20 ? 943 BMA B C3 1 HETATM 8740 C C4 . BMA N 5 . ? 55.349 -60.683 38.935 1.00 110.42 ? 943 BMA B C4 1 HETATM 8741 C C5 . BMA N 5 . ? 53.911 -60.258 39.231 1.00 104.31 ? 943 BMA B C5 1 HETATM 8742 C C6 . BMA N 5 . ? 53.151 -61.306 40.044 1.00 94.82 ? 943 BMA B C6 1 HETATM 8743 O O2 . BMA N 5 . ? 56.768 -58.030 39.843 1.00 91.39 ? 943 BMA B O2 1 HETATM 8744 O O3 . BMA N 5 . ? 57.431 -59.890 37.905 1.00 110.85 ? 943 BMA B O3 1 HETATM 8745 O O4 . BMA N 5 . ? 55.340 -61.917 38.247 1.00 106.73 ? 943 BMA B O4 1 HETATM 8746 O O5 . BMA N 5 . ? 53.938 -59.036 39.936 1.00 105.13 ? 943 BMA B O5 1 HETATM 8747 O O6 . BMA N 5 . ? 51.909 -60.784 40.476 1.00 86.89 ? 943 BMA B O6 1 HETATM 8748 C C1 . NAG O 4 . ? 50.190 -29.444 34.073 1.00 63.85 ? 951 NAG B C1 1 HETATM 8749 C C2 . NAG O 4 . ? 51.611 -29.040 33.672 1.00 71.68 ? 951 NAG B C2 1 HETATM 8750 C C3 . NAG O 4 . ? 52.313 -30.042 32.751 1.00 70.48 ? 951 NAG B C3 1 HETATM 8751 C C4 . NAG O 4 . ? 52.064 -31.505 33.126 1.00 69.86 ? 951 NAG B C4 1 HETATM 8752 C C5 . NAG O 4 . ? 50.602 -31.729 33.510 1.00 57.73 ? 951 NAG B C5 1 HETATM 8753 C C6 . NAG O 4 . ? 50.417 -33.116 34.099 1.00 57.04 ? 951 NAG B C6 1 HETATM 8754 C C7 . NAG O 4 . ? 52.155 -26.660 33.529 1.00 76.22 ? 951 NAG B C7 1 HETATM 8755 C C8 . NAG O 4 . ? 52.151 -25.432 32.659 1.00 63.34 ? 951 NAG B C8 1 HETATM 8756 N N2 . NAG O 4 . ? 51.586 -27.751 33.005 1.00 81.31 ? 951 NAG B N2 1 HETATM 8757 O O3 . NAG O 4 . ? 53.704 -29.775 32.715 1.00 64.95 ? 951 NAG B O3 1 HETATM 8758 O O4 . NAG O 4 . ? 52.462 -32.318 32.024 1.00 76.13 ? 951 NAG B O4 1 HETATM 8759 O O5 . NAG O 4 . ? 50.172 -30.794 34.476 1.00 62.46 ? 951 NAG B O5 1 HETATM 8760 O O6 . NAG O 4 . ? 51.417 -33.321 35.072 1.00 58.61 ? 951 NAG B O6 1 HETATM 8761 O O7 . NAG O 4 . ? 52.659 -26.628 34.657 1.00 66.31 ? 951 NAG B O7 1 HETATM 8762 C C1 . NAG P 4 . ? 53.310 -33.423 32.415 1.00 70.31 ? 952 NAG B C1 1 HETATM 8763 C C2 . NAG P 4 . ? 52.995 -34.657 31.553 1.00 67.22 ? 952 NAG B C2 1 HETATM 8764 C C3 . NAG P 4 . ? 54.062 -35.733 31.682 1.00 74.47 ? 952 NAG B C3 1 HETATM 8765 C C4 . NAG P 4 . ? 55.428 -35.128 31.381 1.00 83.98 ? 952 NAG B C4 1 HETATM 8766 C C5 . NAG P 4 . ? 55.680 -34.001 32.379 1.00 76.61 ? 952 NAG B C5 1 HETATM 8767 C C6 . NAG P 4 . ? 56.991 -33.279 32.102 1.00 78.96 ? 952 NAG B C6 1 HETATM 8768 C C7 . NAG P 4 . ? 50.694 -35.129 30.954 1.00 68.38 ? 952 NAG B C7 1 HETATM 8769 C C8 . NAG P 4 . ? 49.452 -35.930 31.264 1.00 61.44 ? 952 NAG B C8 1 HETATM 8770 N N2 . NAG P 4 . ? 51.696 -35.241 31.825 1.00 65.79 ? 952 NAG B N2 1 HETATM 8771 O O3 . NAG P 4 . ? 53.744 -36.849 30.872 1.00 71.74 ? 952 NAG B O3 1 HETATM 8772 O O4 . NAG P 4 . ? 56.426 -36.130 31.460 1.00 101.08 ? 952 NAG B O4 1 HETATM 8773 O O5 . NAG P 4 . ? 54.663 -33.022 32.332 1.00 71.40 ? 952 NAG B O5 1 HETATM 8774 O O6 . NAG P 4 . ? 56.871 -32.538 30.906 1.00 91.52 ? 952 NAG B O6 1 HETATM 8775 O O7 . NAG P 4 . ? 50.762 -34.399 29.952 1.00 64.96 ? 952 NAG B O7 1 HETATM 8776 C C1 . BMA Q 5 . ? 56.833 -36.504 30.129 1.00 115.19 ? 953 BMA B C1 1 HETATM 8777 C C2 . BMA Q 5 . ? 58.255 -35.978 29.920 1.00 113.66 ? 953 BMA B C2 1 HETATM 8778 C C3 . BMA Q 5 . ? 58.899 -36.535 28.648 1.00 124.60 ? 953 BMA B C3 1 HETATM 8779 C C4 . BMA Q 5 . ? 58.711 -38.050 28.586 1.00 134.44 ? 953 BMA B C4 1 HETATM 8780 C C5 . BMA Q 5 . ? 57.217 -38.347 28.682 1.00 132.60 ? 953 BMA B C5 1 HETATM 8781 C C6 . BMA Q 5 . ? 56.878 -39.823 28.441 1.00 136.79 ? 953 BMA B C6 1 HETATM 8782 O O2 . BMA Q 5 . ? 59.033 -36.350 31.044 1.00 95.28 ? 953 BMA B O2 1 HETATM 8783 O O3 . BMA Q 5 . ? 60.267 -36.174 28.574 1.00 119.55 ? 953 BMA B O3 1 HETATM 8784 O O4 . BMA Q 5 . ? 59.259 -38.591 27.401 1.00 138.69 ? 953 BMA B O4 1 HETATM 8785 O O5 . BMA Q 5 . ? 56.756 -37.909 29.946 1.00 126.16 ? 953 BMA B O5 1 HETATM 8786 O O6 . BMA Q 5 . ? 57.986 -40.669 28.679 1.00 136.48 ? 953 BMA B O6 1 HETATM 8787 C C1 . NAG R 4 . ? 31.334 -10.957 40.679 1.00 108.38 ? 961 NAG B C1 1 HETATM 8788 C C2 . NAG R 4 . ? 31.243 -9.999 41.869 1.00 115.95 ? 961 NAG B C2 1 HETATM 8789 C C3 . NAG R 4 . ? 30.084 -9.009 41.746 1.00 127.52 ? 961 NAG B C3 1 HETATM 8790 C C4 . NAG R 4 . ? 30.170 -8.295 40.390 1.00 136.87 ? 961 NAG B C4 1 HETATM 8791 C C5 . NAG R 4 . ? 30.225 -9.327 39.252 1.00 124.34 ? 961 NAG B C5 1 HETATM 8792 C C6 . NAG R 4 . ? 30.388 -8.688 37.869 1.00 121.94 ? 961 NAG B C6 1 HETATM 8793 C C7 . NAG R 4 . ? 32.235 -10.881 43.843 1.00 107.12 ? 961 NAG B C7 1 HETATM 8794 C C8 . NAG R 4 . ? 33.132 -9.673 43.882 1.00 105.74 ? 961 NAG B C8 1 HETATM 8795 N N2 . NAG R 4 . ? 31.148 -10.775 43.086 1.00 109.43 ? 961 NAG B N2 1 HETATM 8796 O O3 . NAG R 4 . ? 30.041 -8.104 42.841 1.00 116.30 ? 961 NAG B O3 1 HETATM 8797 O O4 . NAG R 4 . ? 29.076 -7.394 40.275 1.00 148.96 ? 961 NAG B O4 1 HETATM 8798 O O5 . NAG R 4 . ? 31.279 -10.263 39.438 1.00 120.47 ? 961 NAG B O5 1 HETATM 8799 O O6 . NAG R 4 . ? 31.749 -8.557 37.511 1.00 118.51 ? 961 NAG B O6 1 HETATM 8800 O O7 . NAG R 4 . ? 32.514 -11.899 44.475 1.00 98.51 ? 961 NAG B O7 1 HETATM 8801 C C1 . NAG S 4 . ? 29.456 -6.141 39.657 1.00 152.03 ? 962 NAG B C1 1 HETATM 8802 C C2 . NAG S 4 . ? 28.199 -5.542 38.993 1.00 151.76 ? 962 NAG B C2 1 HETATM 8803 C C3 . NAG S 4 . ? 28.054 -4.005 38.988 1.00 157.61 ? 962 NAG B C3 1 HETATM 8804 C C4 . NAG S 4 . ? 29.027 -3.253 39.906 1.00 165.97 ? 962 NAG B C4 1 HETATM 8805 C C5 . NAG S 4 . ? 30.354 -3.993 40.042 1.00 155.49 ? 962 NAG B C5 1 HETATM 8806 C C6 . NAG S 4 . ? 31.333 -3.258 40.953 1.00 143.78 ? 962 NAG B C6 1 HETATM 8807 C C7 . NAG S 4 . ? 27.051 -6.919 37.347 1.00 115.99 ? 962 NAG B C7 1 HETATM 8808 C C8 . NAG S 4 . ? 26.010 -7.126 38.417 1.00 94.12 ? 962 NAG B C8 1 HETATM 8809 N N2 . NAG S 4 . ? 28.042 -6.076 37.646 1.00 137.70 ? 962 NAG B N2 1 HETATM 8810 O O3 . NAG S 4 . ? 26.717 -3.662 39.314 1.00 147.75 ? 962 NAG B O3 1 HETATM 8811 O O4 . NAG S 4 . ? 29.281 -1.955 39.391 1.00 175.16 ? 962 NAG B O4 1 HETATM 8812 O O5 . NAG S 4 . ? 30.111 -5.277 40.566 1.00 154.37 ? 962 NAG B O5 1 HETATM 8813 O O6 . NAG S 4 . ? 32.631 -3.785 40.788 1.00 134.71 ? 962 NAG B O6 1 HETATM 8814 O O7 . NAG S 4 . ? 26.981 -7.506 36.261 1.00 107.44 ? 962 NAG B O7 1 HETATM 8815 C C1 . BMA T 5 . ? 28.219 -1.006 39.665 1.00 174.72 ? 963 BMA B C1 1 HETATM 8816 C C2 . BMA T 5 . ? 28.473 -0.209 40.949 1.00 168.92 ? 963 BMA B C2 1 HETATM 8817 C C3 . BMA T 5 . ? 29.555 0.852 40.725 1.00 166.52 ? 963 BMA B C3 1 HETATM 8818 C C4 . BMA T 5 . ? 30.228 0.663 39.366 1.00 165.54 ? 963 BMA B C4 1 HETATM 8819 C C5 . BMA T 5 . ? 29.188 0.662 38.241 1.00 170.14 ? 963 BMA B C5 1 HETATM 8820 C C6 . BMA T 5 . ? 29.770 0.119 36.932 1.00 164.05 ? 963 BMA B C6 1 HETATM 8821 O O2 . BMA T 5 . ? 28.829 -1.060 42.019 1.00 164.14 ? 963 BMA B O2 1 HETATM 8822 O O3 . BMA T 5 . ? 30.522 0.786 41.753 1.00 163.10 ? 963 BMA B O3 1 HETATM 8823 O O4 . BMA T 5 . ? 31.195 1.670 39.144 1.00 156.75 ? 963 BMA B O4 1 HETATM 8824 O O5 . BMA T 5 . ? 28.031 -0.080 38.610 1.00 175.66 ? 963 BMA B O5 1 HETATM 8825 O O6 . BMA T 5 . ? 28.911 0.381 35.840 1.00 154.05 ? 963 BMA B O6 1 HETATM 8826 C C1 . NDG U 6 . ? 48.721 -23.563 24.351 1.00 104.70 ? 971 NDG B C1 1 HETATM 8827 C C2 . NDG U 6 . ? 50.144 -23.161 23.955 1.00 110.32 ? 971 NDG B C2 1 HETATM 8828 C C3 . NDG U 6 . ? 50.851 -24.051 22.935 1.00 101.87 ? 971 NDG B C3 1 HETATM 8829 C C4 . NDG U 6 . ? 50.407 -25.512 22.920 1.00 104.81 ? 971 NDG B C4 1 HETATM 8830 C C5 . NDG U 6 . ? 48.927 -25.750 23.219 1.00 104.53 ? 971 NDG B C5 1 HETATM 8831 C C6 . NDG U 6 . ? 48.761 -27.218 23.632 1.00 97.55 ? 971 NDG B C6 1 HETATM 8832 C C7 . NDG U 6 . ? 51.042 -20.916 23.658 1.00 118.49 ? 971 NDG B C7 1 HETATM 8833 C C8 . NDG U 6 . ? 51.439 -20.037 22.502 1.00 117.91 ? 971 NDG B C8 1 HETATM 8834 O O . NDG U 6 . ? 48.381 -24.938 24.248 1.00 108.06 ? 971 NDG B O 1 HETATM 8835 O O3 . NDG U 6 . ? 52.240 -23.990 23.213 1.00 98.89 ? 971 NDG B O3 1 HETATM 8836 O O4 . NDG U 6 . ? 50.682 -26.025 21.626 1.00 116.61 ? 971 NDG B O4 1 HETATM 8837 O O6 . NDG U 6 . ? 47.417 -27.652 23.569 1.00 89.16 ? 971 NDG B O6 1 HETATM 8838 O O7 . NDG U 6 . ? 51.579 -20.808 24.760 1.00 119.10 ? 971 NDG B O7 1 HETATM 8839 N N2 . NDG U 6 . ? 50.091 -21.811 23.419 1.00 117.04 ? 971 NDG B N2 1 HETATM 8840 C C1 . NAG V 4 . ? 51.995 -26.633 21.536 1.00 126.89 ? 972 NAG B C1 1 HETATM 8841 C C2 . NAG V 4 . ? 51.969 -27.975 20.801 1.00 129.86 ? 972 NAG B C2 1 HETATM 8842 C C3 . NAG V 4 . ? 53.252 -28.712 21.149 1.00 137.41 ? 972 NAG B C3 1 HETATM 8843 C C4 . NAG V 4 . ? 54.440 -27.849 20.720 1.00 137.33 ? 972 NAG B C4 1 HETATM 8844 C C5 . NAG V 4 . ? 54.326 -26.379 21.159 1.00 131.00 ? 972 NAG B C5 1 HETATM 8845 C C6 . NAG V 4 . ? 55.318 -25.503 20.398 1.00 119.30 ? 972 NAG B C6 1 HETATM 8846 C C7 . NAG V 4 . ? 49.901 -29.115 20.163 1.00 115.26 ? 972 NAG B C7 1 HETATM 8847 C C8 . NAG V 4 . ? 50.135 -30.414 19.443 1.00 112.15 ? 972 NAG B C8 1 HETATM 8848 N N2 . NAG V 4 . ? 50.792 -28.778 21.103 1.00 124.35 ? 972 NAG B N2 1 HETATM 8849 O O3 . NAG V 4 . ? 53.285 -29.951 20.475 1.00 139.90 ? 972 NAG B O3 1 HETATM 8850 O O4 . NAG V 4 . ? 55.629 -28.406 21.246 1.00 135.35 ? 972 NAG B O4 1 HETATM 8851 O O5 . NAG V 4 . ? 53.027 -25.829 20.992 1.00 131.12 ? 972 NAG B O5 1 HETATM 8852 O O6 . NAG V 4 . ? 55.189 -24.158 20.807 1.00 113.46 ? 972 NAG B O6 1 HETATM 8853 O O7 . NAG V 4 . ? 48.922 -28.420 19.878 1.00 104.49 ? 972 NAG B O7 1 HETATM 8854 C C1 . NAG W 4 . ? 75.701 -34.286 57.283 1.00 140.37 ? 981 NAG B C1 1 HETATM 8855 C C2 . NAG W 4 . ? 76.546 -33.015 57.458 1.00 139.63 ? 981 NAG B C2 1 HETATM 8856 C C3 . NAG W 4 . ? 77.589 -33.227 58.552 1.00 135.42 ? 981 NAG B C3 1 HETATM 8857 C C4 . NAG W 4 . ? 76.897 -33.564 59.863 1.00 148.38 ? 981 NAG B C4 1 HETATM 8858 C C5 . NAG W 4 . ? 75.911 -34.741 59.737 1.00 157.94 ? 981 NAG B C5 1 HETATM 8859 C C6 . NAG W 4 . ? 74.988 -34.754 60.977 1.00 155.48 ? 981 NAG B C6 1 HETATM 8860 C C7 . NAG W 4 . ? 76.864 -32.724 54.980 1.00 128.01 ? 981 NAG B C7 1 HETATM 8861 C C8 . NAG W 4 . ? 75.797 -31.835 54.402 1.00 119.50 ? 981 NAG B C8 1 HETATM 8862 N N2 . NAG W 4 . ? 77.200 -32.499 56.253 1.00 135.40 ? 981 NAG B N2 1 HETATM 8863 O O3 . NAG W 4 . ? 78.376 -32.066 58.718 1.00 117.20 ? 981 NAG B O3 1 HETATM 8864 O O4 . NAG W 4 . ? 77.893 -33.826 60.832 1.00 144.78 ? 981 NAG B O4 1 HETATM 8865 O O5 . NAG W 4 . ? 75.130 -34.693 58.536 1.00 157.50 ? 981 NAG B O5 1 HETATM 8866 O O6 . NAG W 4 . ? 74.249 -35.942 61.211 1.00 151.92 ? 981 NAG B O6 1 HETATM 8867 O O7 . NAG W 4 . ? 77.405 -33.589 54.283 1.00 122.93 ? 981 NAG B O7 1 HETATM 8868 C C01 . PXS X 7 . ? 6.405 -38.448 33.297 1.00 120.99 ? 581 PXS C C01 1 HETATM 8869 C C02 . PXS X 7 . ? 7.593 -39.248 33.843 1.00 103.34 ? 581 PXS C C02 1 HETATM 8870 C C03 . PXS X 7 . ? 8.116 -40.372 32.948 1.00 79.84 ? 581 PXS C C03 1 HETATM 8871 C C04 . PXS X 7 . ? 9.194 -41.260 33.571 1.00 66.67 ? 581 PXS C C04 1 HETATM 8872 C C05 . PXS X 7 . ? 10.194 -41.849 32.574 1.00 54.90 ? 581 PXS C C05 1 HETATM 8873 C C06 . PXS X 7 . ? 11.369 -42.653 33.140 1.00 52.00 ? 581 PXS C C06 1 HETATM 8874 C C07 . PXS X 7 . ? 12.766 -42.187 32.678 1.00 67.27 ? 581 PXS C C07 1 HETATM 8875 C C08 . PXS X 7 . ? 13.945 -43.156 32.948 1.00 61.22 ? 581 PXS C C08 1 HETATM 8876 C C09 . PXS X 7 . ? 15.365 -42.574 32.798 1.00 53.70 ? 581 PXS C C09 1 HETATM 8877 C C10 . PXS X 7 . ? 16.557 -43.544 32.976 1.00 59.65 ? 581 PXS C C10 1 HETATM 8878 C C11 . PXS X 7 . ? 17.833 -43.169 32.205 1.00 62.36 ? 581 PXS C C11 1 HETATM 8879 C C12 . PXS X 7 . ? 19.162 -43.782 32.679 1.00 64.29 ? 581 PXS C C12 1 HETATM 8880 C C13 . PXS X 7 . ? 20.395 -42.892 32.416 1.00 67.63 ? 581 PXS C C13 1 HETATM 8881 C C14 . PXS X 7 . ? 21.805 -43.500 32.625 1.00 58.40 ? 581 PXS C C14 1 HETATM 8882 C C15 . PXS X 7 . ? 22.775 -42.553 33.365 1.00 54.89 ? 581 PXS C C15 1 HETATM 8883 C C16 . PXS X 7 . ? 23.109 -42.942 34.822 1.00 59.74 ? 581 PXS C C16 1 HETATM 8884 O O17 . PXS X 7 . ? 23.546 -41.948 35.721 1.00 61.92 ? 581 PXS C O17 1 HETATM 8885 C C18 . PXS X 7 . ? 24.564 -42.308 36.629 1.00 68.25 ? 581 PXS C C18 1 HETATM 8886 C C19 . PXS X 7 . ? 25.402 -41.170 37.236 1.00 77.33 ? 581 PXS C C19 1 HETATM 8887 C C20 . PXS X 7 . ? 25.451 -41.345 38.619 1.00 78.99 ? 581 PXS C C20 1 HETATM 8888 O O21 . PXS X 7 . ? 24.791 -40.067 36.909 1.00 79.60 ? 581 PXS C O21 1 HETATM 8889 C C22 . PXS X 7 . ? 25.385 -39.269 35.922 1.00 71.85 ? 581 PXS C C22 1 HETATM 8890 C C23 . PXS X 7 . ? 24.798 -37.859 35.712 1.00 67.97 ? 581 PXS C C23 1 HETATM 8891 C C24 . PXS X 7 . ? 24.568 -37.412 34.252 1.00 63.67 ? 581 PXS C C24 1 HETATM 8892 C C25 . PXS X 7 . ? 23.462 -38.126 33.438 1.00 67.15 ? 581 PXS C C25 1 HETATM 8893 C C26 . PXS X 7 . ? 22.338 -38.828 34.215 1.00 60.72 ? 581 PXS C C26 1 HETATM 8894 C C27 . PXS X 7 . ? 21.045 -37.996 34.327 1.00 55.00 ? 581 PXS C C27 1 HETATM 8895 C C28 . PXS X 7 . ? 19.841 -38.485 33.496 1.00 58.87 ? 581 PXS C C28 1 HETATM 8896 C C29 . PXS X 7 . ? 18.797 -39.328 34.264 1.00 62.24 ? 581 PXS C C29 1 HETATM 8897 C C30 . PXS X 7 . ? 17.398 -38.693 34.408 1.00 59.97 ? 581 PXS C C30 1 HETATM 8898 C C31 . PXS X 7 . ? 16.200 -39.619 34.157 1.00 70.72 ? 581 PXS C C31 1 HETATM 8899 C C32 . PXS X 7 . ? 14.814 -38.964 34.271 1.00 75.84 ? 581 PXS C C32 1 HETATM 8900 C C33 . PXS X 7 . ? 14.692 -37.536 33.696 1.00 76.76 ? 581 PXS C C33 1 HETATM 8901 C C34 . PXS X 7 . ? 13.254 -36.978 33.611 1.00 79.55 ? 581 PXS C C34 1 HETATM 8902 C C35 . PXS X 7 . ? 12.836 -35.982 34.705 1.00 86.42 ? 581 PXS C C35 1 HETATM 8903 C C36 . PXS X 7 . ? 11.861 -36.487 35.778 1.00 88.03 ? 581 PXS C C36 1 HETATM 8904 C C37 . PXS X 7 . ? 11.378 -35.431 36.780 1.00 96.19 ? 581 PXS C C37 1 HETATM 8905 O O38 . PXS X 7 . ? 26.355 -39.657 35.358 1.00 64.39 ? 581 PXS C O38 1 HETATM 8906 O O39 . PXS X 7 . ? 23.042 -44.075 35.168 1.00 63.98 ? 581 PXS C O39 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 . GLU A 26 ? 1.6495 1.4887 2.1971 0.0789 -0.1035 0.4232 26 GLU A N 2 C CA . GLU A 26 ? 1.7388 1.5714 2.2755 0.0892 -0.1083 0.4322 26 GLU A CA 3 C C . GLU A 26 ? 1.8260 1.6883 2.3137 0.1026 -0.0951 0.4364 26 GLU A C 4 O O . GLU A 26 ? 1.8273 1.6917 2.3026 0.1122 -0.0961 0.4496 26 GLU A O 5 C CB . GLU A 26 ? 1.6757 1.4985 2.2531 0.0834 -0.1130 0.4704 26 GLU A CB 6 C CG . GLU A 26 ? 1.5670 1.4190 2.1547 0.0779 -0.0980 0.5108 26 GLU A CG 7 C CD . GLU A 26 ? 1.4889 1.3725 2.0395 0.0912 -0.0843 0.5331 26 GLU A CD 8 O OE1 . GLU A 26 ? 1.4700 1.3483 1.9943 0.1035 -0.0885 0.5231 26 GLU A OE1 9 O OE2 . GLU A 26 ? 1.4370 1.3529 1.9849 0.0901 -0.0694 0.5606 26 GLU A OE2 10 N N . SER A 27 ? 1.7907 1.6749 2.2508 0.1040 -0.0841 0.4235 27 SER A N 11 C CA . SER A 27 ? 1.6784 1.5931 2.0941 0.1167 -0.0718 0.4281 27 SER A CA 12 C C . SER A 27 ? 1.6081 1.5258 1.9856 0.1227 -0.0717 0.3909 27 SER A C 13 O O . SER A 27 ? 1.5720 1.4856 1.9520 0.1157 -0.0719 0.3704 27 SER A O 14 C CB . SER A 27 ? 1.6069 1.5531 2.0248 0.1146 -0.0566 0.4559 27 SER A CB 15 O OG . SER A 27 ? 1.4697 1.4163 1.8987 0.1049 -0.0543 0.4416 27 SER A OG 16 N N . LEU A 28 ? 1.5731 1.4982 1.9160 0.1354 -0.0721 0.3830 28 LEU A N 17 C CA . LEU A 28 ? 1.5255 1.4591 1.8299 0.1417 -0.0706 0.3534 28 LEU A CA 18 C C . LEU A 28 ? 1.4934 1.4607 1.7675 0.1518 -0.0576 0.3674 28 LEU A C 19 O O . LEU A 28 ? 1.5107 1.4946 1.7804 0.1599 -0.0523 0.3945 28 LEU A O 20 C CB . LEU A 28 ? 1.4285 1.3505 1.7146 0.1494 -0.0805 0.3334 28 LEU A CB 21 C CG . LEU A 28 ? 1.1529 1.0721 1.4118 0.1512 -0.0847 0.2976 28 LEU A CG 22 C CD1 . LEU A 28 ? 1.0203 0.9322 1.2666 0.1589 -0.0939 0.2855 28 LEU A CD1 23 C CD2 . LEU A 28 ? 1.0674 1.0101 1.2921 0.1574 -0.0758 0.2925 28 LEU A CD2 24 N N . SER A 29 ? 1.4086 1.3866 1.6618 0.1524 -0.0530 0.3490 29 SER A N 25 C CA . SER A 29 ? 1.3374 1.3476 1.5604 0.1638 -0.0421 0.3576 29 SER A CA 26 C C . SER A 29 ? 1.3729 1.3895 1.5539 0.1768 -0.0458 0.3356 29 SER A C 27 O O . SER A 29 ? 1.4167 1.4272 1.5893 0.1830 -0.0521 0.3343 29 SER A O 28 C CB . SER A 29 ? 1.0577 1.0774 1.2840 0.1578 -0.0354 0.3517 29 SER A CB 29 O OG . SER A 29 ? 0.8843 0.8937 1.0893 0.1577 -0.0410 0.3176 29 SER A OG 30 N N . CYS A 30 ? 1.2504 1.2794 1.4066 0.1811 -0.0425 0.3189 30 CYS A N 31 C CA . CYS A 30 ? 1.3165 1.3495 1.4351 0.1917 -0.0477 0.2948 30 CYS A CA 32 C C . CYS A 30 ? 1.5453 1.6069 1.6358 0.2039 -0.0400 0.2953 30 CYS A C 33 O O . CYS A 30 ? 1.6137 1.6945 1.7137 0.2045 -0.0297 0.3154 30 CYS A O 34 C CB . CYS A 30 ? 1.1655 1.1977 1.2712 0.2011 -0.0537 0.2972 30 CYS A CB 35 S SG . CYS A 30 ? 2.8990 2.9162 2.9800 0.2028 -0.0668 0.2600 30 CYS A SG 36 N N . ASP A 31 ? 1.5988 1.6635 1.6561 0.2138 -0.0460 0.2726 31 ASP A N 37 C CA . ASP A 31 ? 1.4874 1.5785 1.5147 0.2287 -0.0415 0.2693 31 ASP A CA 38 C C . ASP A 31 ? 1.5165 1.6153 1.5092 0.2444 -0.0494 0.2554 31 ASP A C 39 O O . ASP A 31 ? 1.4723 1.5567 1.4650 0.2429 -0.0576 0.2493 31 ASP A O 40 C CB . ASP A 31 ? 1.3458 1.4318 1.3717 0.2228 -0.0414 0.2507 31 ASP A CB 41 C CG . ASP A 31 ? 1.3283 1.3919 1.3395 0.2190 -0.0540 0.2173 31 ASP A CG 42 O OD1 . ASP A 31 ? 1.2194 1.2688 1.2393 0.2085 -0.0556 0.2030 31 ASP A OD1 43 O OD2 . ASP A 31 ? 1.3583 1.4194 1.3499 0.2264 -0.0624 0.2061 31 ASP A OD2 44 N N . ALA A 32 ? 1.5604 1.6827 1.5243 0.2603 -0.0476 0.2498 32 ALA A N 45 C CA . ALA A 32 ? 1.4602 1.5947 1.3907 0.2782 -0.0551 0.2385 32 ALA A CA 46 C C . ALA A 32 ? 1.4041 1.5126 1.3256 0.2728 -0.0705 0.2079 32 ALA A C 47 O O . ALA A 32 ? 1.2341 1.3405 1.1467 0.2780 -0.0778 0.2046 32 ALA A O 48 C CB . ALA A 32 ? 1.3799 1.5447 1.2825 0.2972 -0.0514 0.2357 32 ALA A CB 49 N N . SER A 33 ? 1.3989 1.4894 1.3235 0.2623 -0.0751 0.1869 33 SER A N 50 C CA . SER A 33 ? 1.3037 1.3699 1.2237 0.2544 -0.0891 0.1598 33 SER A CA 51 C C . SER A 33 ? 1.2997 1.3498 1.2371 0.2443 -0.0933 0.1626 33 SER A C 52 O O . SER A 33 ? 1.2537 1.2998 1.1794 0.2478 -0.1036 0.1501 33 SER A O 53 C CB . SER A 33 ? 1.1553 1.2033 1.0855 0.2406 -0.0906 0.1444 33 SER A CB 54 O OG . SER A 33 ? 1.1779 1.2305 1.0840 0.2502 -0.0967 0.1263 33 SER A OG 55 N N . GLY A 34 ? 1.2196 1.2610 1.1862 0.2322 -0.0860 0.1783 34 GLY A N 56 C CA . GLY A 34 ? 1.1861 1.2119 1.1718 0.2233 -0.0900 0.1810 34 GLY A CA 57 C C . GLY A 34 ? 1.1611 1.1665 1.1756 0.2054 -0.0887 0.1777 34 GLY A C 58 O O . GLY A 34 ? 1.1839 1.1729 1.2130 0.1964 -0.0948 0.1700 34 GLY A O 59 N N . VAL A 35 ? 1.0460 1.0547 1.0683 0.2015 -0.0809 0.1832 35 VAL A N 60 C CA . VAL A 35 ? 1.0186 1.0094 1.0666 0.1856 -0.0801 0.1782 35 VAL A CA 61 C C . VAL A 35 ? 0.9522 0.9417 1.0314 0.1795 -0.0727 0.2018 35 VAL A C 62 O O . VAL A 35 ? 0.8696 0.8680 0.9593 0.1778 -0.0642 0.2151 35 VAL A O 63 C CB . VAL A 35 ? 0.8825 0.8744 0.9222 0.1833 -0.0782 0.1658 35 VAL A CB 64 C CG1 . VAL A 35 ? 0.7359 0.7100 0.8019 0.1673 -0.0781 0.1597 35 VAL A CG1 65 C CG2 . VAL A 35 ? 0.6555 0.6459 0.6665 0.1888 -0.0876 0.1426 35 VAL A CG2 66 N N . CYS A 36 ? 1.0673 1.0454 1.1626 0.1763 -0.0771 0.2068 36 CYS A N 67 C CA . CYS A 36 ? 1.0373 1.0099 1.1648 0.1703 -0.0733 0.2283 36 CYS A CA 68 C C . CYS A 36 ? 1.0366 0.9927 1.1912 0.1558 -0.0739 0.2208 36 CYS A C 69 O O . CYS A 36 ? 1.0870 1.0293 1.2409 0.1494 -0.0806 0.1978 36 CYS A O 70 C CB . CYS A 36 ? 0.8606 0.8236 0.9965 0.1723 -0.0801 0.2325 36 CYS A CB 71 S SG . CYS A 36 ? 2.1299 2.1136 2.2445 0.1894 -0.0777 0.2529 36 CYS A SG 72 N N . ASP A 37 ? 1.0779 1.0371 1.2569 0.1509 -0.0671 0.2410 37 ASP A N 73 C CA . ASP A 37 ? 1.0162 0.9608 1.2238 0.1377 -0.0683 0.2351 37 ASP A CA 74 C C . ASP A 37 ? 1.1072 1.0393 1.3531 0.1308 -0.0706 0.2531 37 ASP A C 75 O O . ASP A 37 ? 1.2415 1.1839 1.5040 0.1299 -0.0637 0.2793 37 ASP A O 76 C CB . ASP A 37 ? 0.9804 0.9394 1.1852 0.1363 -0.0596 0.2387 37 ASP A CB 77 C CG . ASP A 37 ? 1.1474 1.0951 1.3868 0.1232 -0.0597 0.2398 37 ASP A CG 78 O OD1 . ASP A 37 ? 1.1935 1.1197 1.4516 0.1155 -0.0685 0.2268 37 ASP A OD1 79 O OD2 . ASP A 37 ? 1.1875 1.1495 1.4358 0.1214 -0.0515 0.2531 37 ASP A OD2 80 N N . GLY A 38 ? 1.0313 0.9420 1.2923 0.1262 -0.0809 0.2394 38 GLY A N 81 C CA . GLY A 38 ? 1.0531 0.9482 1.3521 0.1200 -0.0859 0.2525 38 GLY A CA 82 C C . GLY A 38 ? 1.1232 1.0011 1.4483 0.1091 -0.0920 0.2365 38 GLY A C 83 O O . GLY A 38 ? 1.1010 0.9599 1.4459 0.1067 -0.1026 0.2265 38 GLY A O 84 N N . ARG A 39 ? 1.1974 1.0829 1.5227 0.1037 -0.0860 0.2333 39 ARG A N 85 C CA . ARG A 39 ? 1.1796 1.0516 1.5252 0.0945 -0.0916 0.2154 39 ARG A CA 86 C C . ARG A 39 ? 1.2224 1.0769 1.6120 0.0872 -0.0993 0.2249 39 ARG A C 87 O O . ARG A 39 ? 1.4729 1.3134 1.8741 0.0897 -0.1080 0.2249 39 ARG A O 88 C CB . ARG A 39 ? 1.2387 1.1239 1.5770 0.0910 -0.0833 0.2133 39 ARG A CB 89 C CG . ARG A 39 ? 1.2567 1.1345 1.5861 0.0874 -0.0879 0.1839 39 ARG A CG 90 C CD . ARG A 39 ? 1.2432 1.1302 1.5313 0.0943 -0.0856 0.1692 39 ARG A CD 91 N NE . ARG A 39 ? 1.1363 1.0371 1.4081 0.0949 -0.0779 0.1681 39 ARG A NE 92 C CZ . ARG A 39 ? 1.0800 0.9990 1.3453 0.0994 -0.0683 0.1873 39 ARG A CZ 93 N NH1 . ARG A 39 ? 1.1913 1.1178 1.4656 0.1028 -0.0645 0.2114 39 ARG A NH1 94 N NH2 . ARG A 39 ? 0.9510 0.8823 1.2010 0.1012 -0.0627 0.1830 39 ARG A NH2 95 N N . SER A 40 ? 0.9792 0.8342 1.3948 0.0785 -0.0971 0.2326 40 SER A N 96 C CA . SER A 40 ? 1.0085 0.8432 1.4673 0.0707 -0.1079 0.2333 40 SER A CA 97 C C . SER A 40 ? 1.2009 1.0281 1.6904 0.0687 -0.1110 0.2621 40 SER A C 98 O O . SER A 40 ? 1.2849 1.0972 1.8148 0.0604 -0.1191 0.2677 40 SER A O 99 C CB . SER A 40 ? 0.9962 0.8314 1.4751 0.0614 -0.1074 0.2271 40 SER A CB 100 O OG . SER A 40 ? 0.8919 0.7151 1.3682 0.0609 -0.1164 0.1952 40 SER A OG 101 N N . ARG A 41 ? 1.2746 1.1114 1.7462 0.0764 -0.1057 0.2802 41 ARG A N 102 C CA . ARG A 41 ? 1.3777 1.2044 1.8759 0.0760 -0.1107 0.3059 41 ARG A CA 103 C C . ARG A 41 ? 1.3833 1.1811 1.9012 0.0767 -0.1281 0.2865 41 ARG A C 104 O O . ARG A 41 ? 1.4936 1.2879 1.9871 0.0849 -0.1325 0.2642 41 ARG A O 105 C CB . ARG A 41 ? 1.4478 1.2904 1.9173 0.0867 -0.1030 0.3239 41 ARG A CB 106 C CG . ARG A 41 ? 1.5324 1.4061 1.9840 0.0887 -0.0865 0.3470 41 ARG A CG 107 C CD . ARG A 41 ? 1.5769 1.4661 1.9933 0.0921 -0.0791 0.3245 41 ARG A CD 108 N NE . ARG A 41 ? 1.5912 1.5103 1.9763 0.1012 -0.0657 0.3400 41 ARG A NE 109 C CZ . ARG A 41 ? 1.5166 1.4543 1.8757 0.1043 -0.0574 0.3295 41 ARG A CZ 110 N NH1 . ARG A 41 ? 1.4478 1.3767 1.8087 0.0980 -0.0605 0.3051 41 ARG A NH1 111 N NH2 . ARG A 41 ? 1.4657 1.4310 1.7968 0.1148 -0.0468 0.3431 41 ARG A NH2 112 N N . SER A 42 ? 1.2218 1.0000 1.7846 0.0687 -0.1388 0.2945 42 SER A N 113 C CA . SER A 42 ? 1.1797 0.9310 1.7620 0.0705 -0.1568 0.2705 42 SER A CA 114 C C . SER A 42 ? 1.1621 0.9040 1.7351 0.0811 -0.1638 0.2715 42 SER A C 115 O O . SER A 42 ? 1.1141 0.8417 1.7141 0.0806 -0.1712 0.2928 42 SER A O 116 C CB . SER A 42 ? 1.2152 0.9460 1.8495 0.0599 -0.1688 0.2771 42 SER A CB 117 O OG . SER A 42 ? 1.2331 0.9461 1.8788 0.0611 -0.1834 0.2428 42 SER A OG 118 N N . PHE A 43 ? 1.1325 0.8828 1.6677 0.0905 -0.1619 0.2489 43 PHE A N 119 C CA . PHE A 43 ? 1.1157 0.8607 1.6379 0.1017 -0.1682 0.2459 43 PHE A CA 120 C C . PHE A 43 ? 1.2050 0.9291 1.7433 0.1064 -0.1858 0.2178 43 PHE A C 121 O O . PHE A 43 ? 1.3274 1.0476 1.8721 0.1034 -0.1907 0.1932 43 PHE A O 122 C CB . PHE A 43 ? 0.9329 0.7002 1.4073 0.1097 -0.1576 0.2369 43 PHE A CB 123 C CG . PHE A 43 ? 0.9964 0.7857 1.4501 0.1097 -0.1419 0.2628 43 PHE A CG 124 C CD1 . PHE A 43 ? 1.0552 0.8658 1.4690 0.1136 -0.1315 0.2528 43 PHE A CD1 125 C CD2 . PHE A 43 ? 1.0534 0.8436 1.5283 0.1063 -0.1382 0.2972 43 PHE A CD2 126 C CE1 . PHE A 43 ? 1.0189 0.8512 1.4125 0.1159 -0.1182 0.2743 43 PHE A CE1 127 C CE2 . PHE A 43 ? 1.0494 0.8644 1.5037 0.1083 -0.1234 0.3207 43 PHE A CE2 128 C CZ . PHE A 43 ? 0.9821 0.8183 1.3950 0.1140 -0.1136 0.3080 43 PHE A CZ 129 N N . THR A 44 ? 1.1041 0.8166 1.6480 0.1150 -0.1954 0.2213 44 THR A N 130 C CA . THR A 44 ? 1.0618 0.7577 1.6174 0.1229 -0.2124 0.1943 44 THR A CA 131 C C . THR A 44 ? 1.1899 0.8985 1.7112 0.1352 -0.2109 0.1831 44 THR A C 132 O O . THR A 44 ? 1.3440 1.0467 1.8660 0.1442 -0.2226 0.1589 44 THR A O 133 C CB . THR A 44 ? 1.0752 0.7422 1.6745 0.1231 -0.2289 0.2069 44 THR A CB 134 O OG1 . THR A 44 ? 0.9098 0.5768 1.5084 0.1255 -0.2251 0.2393 44 THR A OG1 135 C CG2 . THR A 44 ? 1.0321 0.6860 1.6697 0.1100 -0.2328 0.2149 44 THR A CG2 136 N N . SER A 45 ? 1.0676 0.7955 1.5592 0.1362 -0.1967 0.2004 45 SER A N 137 C CA . SER A 45 ? 1.0421 0.7842 1.5008 0.1469 -0.1945 0.1923 45 SER A CA 138 C C . SER A 45 ? 1.0735 0.8407 1.4961 0.1450 -0.1778 0.2006 45 SER A C 139 O O . SER A 45 ? 1.0363 0.8093 1.4607 0.1378 -0.1677 0.2207 45 SER A O 140 C CB . SER A 45 ? 1.0983 0.8304 1.5662 0.1555 -0.2016 0.2109 45 SER A CB 141 O OG . SER A 45 ? 1.0293 0.7692 1.4923 0.1532 -0.1910 0.2451 45 SER A OG 142 N N . ILE A 46 ? 1.1170 0.8996 1.5078 0.1519 -0.1756 0.1846 46 ILE A N 143 C CA . ILE A 46 ? 1.1890 0.9938 1.5450 0.1521 -0.1624 0.1908 46 ILE A CA 144 C C . ILE A 46 ? 1.2404 1.0492 1.5954 0.1554 -0.1565 0.2236 46 ILE A C 145 O O . ILE A 46 ? 1.3711 1.1734 1.7325 0.1631 -0.1629 0.2339 46 ILE A O 146 C CB . ILE A 46 ? 1.0040 0.8233 1.3298 0.1596 -0.1639 0.1705 46 ILE A CB 147 C CG1 . ILE A 46 ? 0.9067 0.7262 1.2332 0.1566 -0.1691 0.1400 46 ILE A CG1 148 C CG2 . ILE A 46 ? 0.9120 0.7520 1.2035 0.1607 -0.1526 0.1771 46 ILE A CG2 149 C CD1 . ILE A 46 ? 0.5578 0.3870 0.8698 0.1479 -0.1605 0.1309 46 ILE A CD1 150 N N . PRO A 47 ? 1.1696 0.9902 1.5173 0.1502 -0.1443 0.2409 47 PRO A N 151 C CA . PRO A 47 ? 1.1474 0.9791 1.4898 0.1541 -0.1363 0.2730 47 PRO A CA 152 C C . PRO A 47 ? 1.1727 1.0120 1.4945 0.1669 -0.1387 0.2780 47 PRO A C 153 O O . PRO A 47 ? 1.0659 0.9185 1.3572 0.1728 -0.1376 0.2608 47 PRO A O 154 C CB . PRO A 47 ? 1.0685 0.9215 1.3866 0.1515 -0.1230 0.2746 47 PRO A CB 155 C CG . PRO A 47 ? 1.1162 0.9597 1.4501 0.1405 -0.1243 0.2572 47 PRO A CG 156 C CD . PRO A 47 ? 1.1628 0.9884 1.5090 0.1407 -0.1377 0.2314 47 PRO A CD 157 N N . SER A 48 ? 1.3447 1.1754 1.6850 0.1708 -0.1427 0.3023 48 SER A N 158 C CA . SER A 48 ? 1.3722 1.2100 1.6953 0.1837 -0.1451 0.3113 48 SER A CA 159 C C . SER A 48 ? 1.2235 1.0900 1.5099 0.1904 -0.1328 0.3211 48 SER A C 160 O O . SER A 48 ? 1.1485 1.0282 1.4292 0.1856 -0.1219 0.3311 48 SER A O 161 C CB . SER A 48 ? 1.3212 1.1441 1.6733 0.1856 -0.1509 0.3405 48 SER A CB 162 O OG . SER A 48 ? 1.1935 0.9881 1.5823 0.1796 -0.1638 0.3311 48 SER A OG 163 N N . GLY A 49 ? 1.1214 0.9985 1.3830 0.2026 -0.1355 0.3168 49 GLY A N 164 C CA . GLY A 49 ? 1.2112 1.1153 1.4373 0.2114 -0.1263 0.3240 49 GLY A CA 165 C C . GLY A 49 ? 1.1974 1.1145 1.4021 0.2067 -0.1192 0.3052 49 GLY A C 166 O O . GLY A 49 ? 0.9328 0.8568 1.1408 0.2008 -0.1100 0.3161 49 GLY A O 167 N N . LEU A 50 ? 1.2851 1.2059 1.4688 0.2094 -0.1243 0.2774 50 LEU A N 168 C CA . LEU A 50 ? 1.1198 1.0516 1.2810 0.2061 -0.1200 0.2581 50 LEU A CA 169 C C . LEU A 50 ? 1.2125 1.1645 1.3385 0.2186 -0.1205 0.2527 50 LEU A C 170 O O . LEU A 50 ? 1.1212 1.0745 1.2416 0.2270 -0.1274 0.2512 50 LEU A O 171 C CB . LEU A 50 ? 0.8204 0.7382 0.9911 0.1963 -0.1266 0.2293 50 LEU A CB 172 C CG . LEU A 50 ? 0.9273 0.8252 1.1324 0.1851 -0.1283 0.2296 50 LEU A CG 173 C CD1 . LEU A 50 ? 0.9740 0.8635 1.1833 0.1778 -0.1346 0.1996 50 LEU A CD1 174 C CD2 . LEU A 50 ? 0.9893 0.8904 1.2018 0.1785 -0.1182 0.2454 50 LEU A CD2 175 N N . THR A 51 ? 1.2940 1.2615 1.3966 0.2205 -0.1141 0.2489 51 THR A N 176 C CA . THR A 51 ? 1.3181 1.3062 1.3876 0.2340 -0.1147 0.2466 51 THR A CA 177 C C . THR A 51 ? 1.1668 1.1566 1.2171 0.2320 -0.1211 0.2164 51 THR A C 178 O O . THR A 51 ? 1.2530 1.2332 1.3099 0.2205 -0.1210 0.2010 51 THR A O 179 C CB . THR A 51 ? 1.4432 1.4516 1.4976 0.2413 -0.1039 0.2652 51 THR A CB 180 O OG1 . THR A 51 ? 1.4878 1.4942 1.5659 0.2387 -0.0967 0.2949 51 THR A OG1 181 C CG2 . THR A 51 ? 1.4509 1.4820 1.4735 0.2591 -0.1054 0.2680 51 THR A CG2 182 N N . ALA A 52 ? 0.9860 0.9884 1.0132 0.2431 -0.1271 0.2087 52 ALA A N 183 C CA . ALA A 52 ? 1.1115 1.1169 1.1204 0.2415 -0.1344 0.1819 52 ALA A CA 184 C C . ALA A 52 ? 1.1656 1.1817 1.1533 0.2444 -0.1300 0.1778 52 ALA A C 185 O O . ALA A 52 ? 0.9182 0.9385 0.8874 0.2457 -0.1368 0.1578 52 ALA A O 186 C CB . ALA A 52 ? 0.9137 0.9288 0.9080 0.2518 -0.1441 0.1739 52 ALA A CB 187 N N . ALA A 53 ? 1.2413 1.2620 1.2337 0.2454 -0.1192 0.1970 53 ALA A N 188 C CA . ALA A 53 ? 1.2424 1.2737 1.2182 0.2485 -0.1138 0.1946 53 ALA A CA 189 C C . ALA A 53 ? 1.3085 1.3240 1.3008 0.2325 -0.1111 0.1849 53 ALA A C 190 O O . ALA A 53 ? 1.2764 1.2946 1.2555 0.2318 -0.1109 0.1725 53 ALA A O 191 C CB . ALA A 53 ? 1.2131 1.2635 1.1847 0.2594 -0.1028 0.2224 53 ALA A CB 192 N N . MET A 54 ? 1.3464 1.3455 1.3679 0.2207 -0.1100 0.1902 54 MET A N 193 C CA . MET A 54 ? 1.1604 1.1445 1.2000 0.2059 -0.1079 0.1815 54 MET A CA 194 C C . MET A 54 ? 1.1295 1.1064 1.1591 0.1994 -0.1163 0.1538 54 MET A C 195 O O . MET A 54 ? 1.1850 1.1587 1.2131 0.1987 -0.1249 0.1416 54 MET A O 196 C CB . MET A 54 ? 0.9059 0.8738 0.9781 0.1968 -0.1080 0.1897 54 MET A CB 197 C CG . MET A 54 ? 0.8287 0.8008 0.9155 0.2014 -0.1015 0.2192 54 MET A CG 198 S SD . MET A 54 ? 1.6298 1.5790 1.7573 0.1913 -0.1050 0.2267 54 MET A SD 199 C CE . MET A 54 ? 0.8702 0.8256 1.0164 0.1916 -0.0945 0.2624 54 MET A CE 200 N N . LYS A 55 ? 0.9867 0.9625 1.0101 0.1948 -0.1139 0.1449 55 LYS A N 201 C CA . LYS A 55 ? 0.9415 0.9097 0.9570 0.1874 -0.1215 0.1211 55 LYS A CA 202 C C . LYS A 55 ? 1.0120 0.9653 1.0493 0.1726 -0.1195 0.1150 55 LYS A C 203 O O . LYS A 55 ? 1.0026 0.9477 1.0432 0.1637 -0.1259 0.0983 55 LYS A O 204 C CB . LYS A 55 ? 0.8552 0.8325 0.8448 0.1951 -0.1225 0.1136 55 LYS A CB 205 C CG . LYS A 55 ? 1.0524 1.0444 1.0177 0.2103 -0.1278 0.1131 55 LYS A CG 206 C CD . LYS A 55 ? 1.2848 1.2720 1.2417 0.2076 -0.1411 0.0929 55 LYS A CD 207 C CE . LYS A 55 ? 1.3894 1.3908 1.3189 0.2234 -0.1485 0.0871 55 LYS A CE 208 N NZ . LYS A 55 ? 1.3964 1.4097 1.3220 0.2345 -0.1496 0.0976 55 LYS A NZ 209 N N . SER A 56 ? 0.9233 0.8750 0.9765 0.1702 -0.1108 0.1295 56 SER A N 210 C CA . SER A 56 ? 0.8188 0.7578 0.8927 0.1577 -0.1090 0.1242 56 SER A CA 211 C C . SER A 56 ? 0.8800 0.8145 0.9813 0.1550 -0.1035 0.1423 56 SER A C 212 O O . SER A 56 ? 0.9936 0.9358 1.0984 0.1583 -0.0955 0.1599 56 SER A O 213 C CB . SER A 56 ? 0.7509 0.6920 0.8145 0.1559 -0.1053 0.1186 56 SER A CB 214 O OG . SER A 56 ? 0.7229 0.6534 0.8071 0.1448 -0.1028 0.1154 56 SER A OG 215 N N . LEU A 57 ? 0.9362 0.8590 1.0580 0.1494 -0.1084 0.1381 57 LEU A N 216 C CA . LEU A 57 ? 0.9364 0.8506 1.0880 0.1459 -0.1062 0.1524 57 LEU A CA 217 C C . LEU A 57 ? 0.9208 0.8234 1.0923 0.1347 -0.1065 0.1425 57 LEU A C 218 O O . LEU A 57 ? 0.9623 0.8599 1.1318 0.1298 -0.1119 0.1226 57 LEU A O 219 C CB . LEU A 57 ? 0.8688 0.7767 1.0316 0.1490 -0.1133 0.1533 57 LEU A CB 220 C CG . LEU A 57 ? 0.8440 0.7407 1.0382 0.1473 -0.1138 0.1690 57 LEU A CG 221 C CD1 . LEU A 57 ? 0.8893 0.7920 1.0906 0.1476 -0.1046 0.1936 57 LEU A CD1 222 C CD2 . LEU A 57 ? 0.9305 0.8256 1.1268 0.1551 -0.1200 0.1740 57 LEU A CD2 223 N N . ASP A 58 ? 0.9648 0.8652 1.1560 0.1310 -0.1009 0.1570 58 ASP A N 224 C CA . ASP A 58 ? 1.0015 0.8909 1.2151 0.1211 -0.1020 0.1487 58 ASP A CA 225 C C . ASP A 58 ? 1.1079 0.9864 1.3565 0.1178 -0.1038 0.1629 58 ASP A C 226 O O . ASP A 58 ? 1.2405 1.1234 1.5013 0.1170 -0.0974 0.1840 58 ASP A O 227 C CB . ASP A 58 ? 0.9066 0.8033 1.1129 0.1180 -0.0948 0.1491 58 ASP A CB 228 C CG . ASP A 58 ? 0.9387 0.8249 1.1665 0.1082 -0.0967 0.1385 58 ASP A CG 229 O OD1 . ASP A 58 ? 0.9079 0.7988 1.1284 0.1055 -0.0924 0.1339 58 ASP A OD1 230 O OD2 . ASP A 58 ? 0.8246 0.6982 1.0763 0.1044 -0.1032 0.1339 58 ASP A OD2 231 N N . LEU A 59 ? 1.0371 0.9022 1.3025 0.1161 -0.1130 0.1514 59 LEU A N 232 C CA . LEU A 59 ? 0.8642 0.7151 1.1649 0.1135 -0.1180 0.1614 59 LEU A CA 233 C C . LEU A 59 ? 0.8002 0.6394 1.1223 0.1061 -0.1239 0.1441 59 LEU A C 234 O O . LEU A 59 ? 0.9925 0.8191 1.3340 0.1068 -0.1339 0.1344 59 LEU A O 235 C CB . LEU A 59 ? 0.6751 0.5194 0.9803 0.1204 -0.1262 0.1621 59 LEU A CB 236 C CG . LEU A 59 ? 0.6662 0.5232 0.9454 0.1295 -0.1224 0.1731 59 LEU A CG 237 C CD1 . LEU A 59 ? 0.5841 0.4351 0.8665 0.1365 -0.1316 0.1686 59 LEU A CD1 238 C CD2 . LEU A 59 ? 0.7992 0.6639 1.0818 0.1310 -0.1139 0.2028 59 LEU A CD2 239 N N . SER A 60 ? 0.6414 0.4855 0.9598 0.1002 -0.1185 0.1394 60 SER A N 240 C CA . SER A 60 ? 0.8137 0.6489 1.1498 0.0940 -0.1240 0.1219 60 SER A CA 241 C C . SER A 60 ? 0.8949 0.7181 1.2701 0.0883 -0.1275 0.1323 60 SER A C 242 O O . SER A 60 ? 0.9931 0.8191 1.3802 0.0859 -0.1217 0.1560 60 SER A O 243 C CB . SER A 60 ? 0.8472 0.6919 1.1630 0.0905 -0.1180 0.1109 60 SER A CB 244 O OG . SER A 60 ? 0.9051 0.7570 1.1908 0.0942 -0.1185 0.0969 60 SER A OG 245 N N . PHE A 61 ? 0.9047 0.7159 1.3003 0.0863 -0.1377 0.1143 61 PHE A N 246 C CA . PHE A 61 ? 0.9174 0.7159 1.3515 0.0801 -0.1436 0.1182 61 PHE A CA 247 C C . PHE A 61 ? 0.8941 0.6792 1.3574 0.0807 -0.1499 0.1371 61 PHE A C 248 O O . PHE A 61 ? 0.9820 0.7631 1.4718 0.0741 -0.1486 0.1565 61 PHE A O 249 C CB . PHE A 61 ? 0.8255 0.6328 1.2632 0.0725 -0.1342 0.1289 61 PHE A CB 250 C CG . PHE A 61 ? 0.7885 0.6088 1.1952 0.0725 -0.1274 0.1138 61 PHE A CG 251 C CD1 . PHE A 61 ? 0.8048 0.6403 1.1813 0.0749 -0.1162 0.1238 61 PHE A CD1 252 C CD2 . PHE A 61 ? 0.9495 0.7666 1.3570 0.0710 -0.1333 0.0895 61 PHE A CD2 253 C CE1 . PHE A 61 ? 0.8860 0.7308 1.2353 0.0750 -0.1117 0.1098 61 PHE A CE1 254 C CE2 . PHE A 61 ? 0.9712 0.7992 1.3509 0.0707 -0.1277 0.0773 61 PHE A CE2 255 C CZ . PHE A 61 ? 0.9327 0.7730 1.2840 0.0723 -0.1174 0.0875 61 PHE A CZ 256 N N . ASN A 62 ? 0.8450 0.6236 1.3045 0.0884 -0.1571 0.1323 62 ASN A N 257 C CA . ASN A 62 ? 0.9503 0.7133 1.4382 0.0900 -0.1654 0.1485 62 ASN A CA 258 C C . ASN A 62 ? 1.1540 0.9010 1.6585 0.0961 -0.1819 0.1261 62 ASN A C 259 O O . ASN A 62 ? 1.2214 0.9716 1.7171 0.0985 -0.1860 0.0991 62 ASN A O 260 C CB . ASN A 62 ? 0.8969 0.6678 1.3656 0.0961 -0.1589 0.1690 62 ASN A CB 261 C CG . ASN A 62 ? 0.9668 0.7601 1.4008 0.0960 -0.1433 0.1778 62 ASN A CG 262 O OD1 . ASN A 62 ? 1.0103 0.8138 1.4193 0.0962 -0.1394 0.1591 62 ASN A OD1 263 N ND2 . ASN A 62 ? 0.9758 0.7775 1.4079 0.0964 -0.1349 0.2066 62 ASN A ND2 264 N N . LYS A 63 ? 1.2134 0.9442 1.7417 0.0995 -0.1916 0.1376 63 LYS A N 265 C CA . LYS A 63 ? 1.3198 1.0358 1.8628 0.1079 -0.2083 0.1163 63 LYS A CA 266 C C . LYS A 63 ? 1.4320 1.1534 1.9526 0.1189 -0.2088 0.1161 63 LYS A C 267 O O . LYS A 63 ? 1.6059 1.3118 2.1450 0.1252 -0.2202 0.1205 63 LYS A O 268 C CB . LYS A 63 ? 1.4349 1.1250 2.0251 0.1049 -0.2230 0.1250 63 LYS A CB 269 C CG . LYS A 63 ? 1.5047 1.1887 2.1210 0.0951 -0.2264 0.1186 63 LYS A CG 270 C CD . LYS A 63 ? 1.5758 1.2324 2.2425 0.0914 -0.2433 0.1267 63 LYS A CD 271 C CE . LYS A 63 ? 1.5242 1.1614 2.2052 0.1038 -0.2627 0.1103 63 LYS A CE 272 N NZ . LYS A 63 ? 1.4498 1.0759 2.1393 0.1065 -0.2650 0.1368 63 LYS A NZ 273 N N . ILE A 64 ? 1.3215 1.0644 1.8033 0.1211 -0.1972 0.1112 64 ILE A N 274 C CA . ILE A 64 ? 1.2025 0.9535 1.6620 0.1313 -0.1980 0.1076 64 ILE A CA 275 C C . ILE A 64 ? 1.1899 0.9409 1.6507 0.1396 -0.2097 0.0768 64 ILE A C 276 O O . ILE A 64 ? 1.1782 0.9474 1.6122 0.1428 -0.2058 0.0604 64 ILE A O 277 C CB . ILE A 64 ? 1.0609 0.8347 1.4802 0.1308 -0.1837 0.1110 64 ILE A CB 278 C CG1 . ILE A 64 ? 1.0583 0.8377 1.4731 0.1225 -0.1707 0.1348 64 ILE A CG1 279 C CG2 . ILE A 64 ? 0.8920 0.6721 1.2941 0.1406 -0.1848 0.1157 64 ILE A CG2 280 C CD1 . ILE A 64 ? 1.1094 0.8903 1.5214 0.1258 -0.1662 0.1632 64 ILE A CD1 281 N N . THR A 65 ? 1.2023 0.9335 1.6960 0.1431 -0.2248 0.0693 65 THR A N 282 C CA . THR A 65 ? 1.0592 0.7906 1.5583 0.1533 -0.2378 0.0396 65 THR A CA 283 C C . THR A 65 ? 0.9516 0.6992 1.4254 0.1641 -0.2374 0.0310 65 THR A C 284 O O . THR A 65 ? 0.8926 0.6563 1.3534 0.1701 -0.2395 0.0069 65 THR A O 285 C CB . THR A 65 ? 1.0398 0.7440 1.5793 0.1580 -0.2562 0.0372 65 THR A CB 286 O OG1 . THR A 65 ? 1.0915 0.7983 1.6339 0.1714 -0.2698 0.0073 65 THR A OG1 287 C CG2 . THR A 65 ? 0.9225 0.6117 1.4735 0.1600 -0.2589 0.0639 65 THR A CG2 288 N N . TYR A 66 ? 0.8706 0.6161 1.3377 0.1669 -0.2345 0.0516 66 TYR A N 289 C CA . TYR A 66 ? 0.8150 0.5747 1.2619 0.1778 -0.2359 0.0445 66 TYR A CA 290 C C . TYR A 66 ? 0.8299 0.6052 1.2467 0.1752 -0.2222 0.0626 66 TYR A C 291 O O . TYR A 66 ? 0.9025 0.6698 1.3219 0.1714 -0.2170 0.0888 66 TYR A O 292 C CB . TYR A 66 ? 0.7813 0.5226 1.2515 0.1892 -0.2513 0.0462 66 TYR A CB 293 C CG . TYR A 66 ? 0.8156 0.5717 1.2684 0.2022 -0.2547 0.0367 66 TYR A CG 294 C CD1 . TYR A 66 ? 0.9456 0.7185 1.3916 0.2110 -0.2604 0.0078 66 TYR A CD1 295 C CD2 . TYR A 66 ? 0.8412 0.5967 1.2852 0.2062 -0.2523 0.0570 66 TYR A CD2 296 C CE1 . TYR A 66 ? 0.9429 0.7322 1.3750 0.2228 -0.2636 -0.0005 66 TYR A CE1 297 C CE2 . TYR A 66 ? 0.8773 0.6472 1.3066 0.2182 -0.2560 0.0480 66 TYR A CE2 298 C CZ . TYR A 66 ? 0.9448 0.7317 1.3689 0.2262 -0.2616 0.0192 66 TYR A CZ 299 O OH . TYR A 66 ? 0.9325 0.7365 1.3434 0.2380 -0.2651 0.0107 66 TYR A OH 300 N N . ILE A 67 ? 0.6914 0.4902 1.0804 0.1774 -0.2171 0.0487 67 ILE A N 301 C CA . ILE A 67 ? 0.7403 0.5543 1.1012 0.1778 -0.2078 0.0613 67 ILE A CA 302 C C . ILE A 67 ? 0.8315 0.6538 1.1873 0.1906 -0.2158 0.0531 67 ILE A C 303 O O . ILE A 67 ? 0.8762 0.7096 1.2325 0.1965 -0.2222 0.0303 67 ILE A O 304 C CB . ILE A 67 ? 0.6388 0.4728 0.9724 0.1698 -0.1966 0.0542 67 ILE A CB 305 C CG1 . ILE A 67 ? 0.6069 0.4336 0.9430 0.1584 -0.1879 0.0656 67 ILE A CG1 306 C CG2 . ILE A 67 ? 0.5616 0.4117 0.8674 0.1724 -0.1907 0.0621 67 ILE A CG2 307 C CD1 . ILE A 67 ? 0.5389 0.3796 0.8573 0.1507 -0.1811 0.0520 67 ILE A CD1 308 N N . GLY A 68 ? 0.7290 0.5480 1.0803 0.1957 -0.2153 0.0722 68 GLY A N 309 C CA . GLY A 68 ? 0.7494 0.5729 1.0999 0.2088 -0.2242 0.0672 68 GLY A CA 310 C C . GLY A 68 ? 0.7294 0.5778 1.0498 0.2115 -0.2184 0.0655 68 GLY A C 311 O O . GLY A 68 ? 0.7690 0.6313 1.0683 0.2031 -0.2083 0.0653 68 GLY A O 312 N N . HIS A 69 ? 0.6167 0.4700 0.9359 0.2236 -0.2259 0.0637 69 HIS A N 313 C CA . HIS A 69 ? 0.7028 0.5811 0.9965 0.2271 -0.2227 0.0594 69 HIS A CA 314 C C . HIS A 69 ? 0.9410 0.8235 1.2131 0.2228 -0.2127 0.0798 69 HIS A C 315 O O . HIS A 69 ? 1.0034 0.9042 1.2532 0.2173 -0.2061 0.0746 69 HIS A O 316 C CB . HIS A 69 ? 0.7909 0.6735 1.0901 0.2421 -0.2337 0.0537 69 HIS A CB 317 C CG . HIS A 69 ? 0.8778 0.7697 1.1889 0.2485 -0.2425 0.0279 69 HIS A CG 318 N ND1 . HIS A 69 ? 0.9609 0.8341 1.2986 0.2559 -0.2538 0.0204 69 HIS A ND1 319 C CD2 . HIS A 69 ? 0.9166 0.8366 1.2172 0.2495 -0.2423 0.0082 69 HIS A CD2 320 C CE1 . HIS A 69 ? 0.9733 0.8641 1.3145 0.2626 -0.2598 -0.0042 69 HIS A CE1 321 N NE2 . HIS A 69 ? 0.9885 0.9089 1.3076 0.2584 -0.2523 -0.0109 69 HIS A NE2 322 N N . GLY A 70 ? 0.9894 0.8555 1.2690 0.2257 -0.2123 0.1032 70 GLY A N 323 C CA . GLY A 70 ? 0.9279 0.7997 1.1875 0.2248 -0.2034 0.1244 70 GLY A CA 324 C C . GLY A 70 ? 0.9391 0.8053 1.1966 0.2138 -0.1926 0.1383 70 GLY A C 325 O O . GLY A 70 ? 0.9439 0.8190 1.1822 0.2141 -0.1847 0.1536 70 GLY A O 326 N N . ASP A 71 ? 0.9054 0.7589 1.1817 0.2052 -0.1925 0.1321 71 ASP A N 327 C CA . ASP A 71 ? 0.9685 0.8165 1.2468 0.1950 -0.1829 0.1457 71 ASP A CA 328 C C . ASP A 71 ? 0.9624 0.8284 1.2106 0.1908 -0.1719 0.1478 71 ASP A C 329 O O . ASP A 71 ? 0.9382 0.8040 1.1829 0.1875 -0.1635 0.1663 71 ASP A O 330 C CB . ASP A 71 ? 1.0174 0.8535 1.3170 0.1863 -0.1852 0.1320 71 ASP A CB 331 C CG . ASP A 71 ? 1.1079 0.9211 1.4420 0.1891 -0.1959 0.1356 71 ASP A CG 332 O OD1 . ASP A 71 ? 1.1087 0.9089 1.4638 0.1816 -0.1973 0.1323 71 ASP A OD1 333 O OD2 . ASP A 71 ? 1.0973 0.9048 1.4381 0.1991 -0.2038 0.1414 71 ASP A OD2 334 N N . LEU A 72 ? 0.8822 0.7642 1.1100 0.1912 -0.1726 0.1291 72 LEU A N 335 C CA . LEU A 72 ? 0.8048 0.7011 1.0059 0.1872 -0.1646 0.1283 72 LEU A CA 336 C C . LEU A 72 ? 1.0099 0.9237 1.1866 0.1945 -0.1671 0.1229 72 LEU A C 337 O O . LEU A 72 ? 1.1680 1.0936 1.3279 0.1901 -0.1664 0.1089 72 LEU A O 338 C CB . LEU A 72 ? 0.7880 0.6855 0.9882 0.1763 -0.1624 0.1102 72 LEU A CB 339 C CG . LEU A 72 ? 0.8839 0.7668 1.1055 0.1680 -0.1600 0.1111 72 LEU A CG 340 C CD1 . LEU A 72 ? 0.7274 0.6143 0.9480 0.1603 -0.1609 0.0893 72 LEU A CD1 341 C CD2 . LEU A 72 ? 1.0518 0.9327 1.2694 0.1642 -0.1505 0.1296 72 LEU A CD2 342 N N . ARG A 73 ? 1.0006 0.9159 1.1765 0.2054 -0.1709 0.1344 73 ARG A N 343 C CA . ARG A 73 ? 0.9785 0.9110 1.1323 0.2133 -0.1741 0.1300 73 ARG A CA 344 C C . ARG A 73 ? 1.0981 1.0397 1.2287 0.2172 -0.1674 0.1446 73 ARG A C 345 O O . ARG A 73 ? 1.0750 1.0315 1.1829 0.2197 -0.1686 0.1361 73 ARG A O 346 C CB . ARG A 73 ? 0.9096 0.8410 1.0724 0.2249 -0.1822 0.1345 73 ARG A CB 347 C CG . ARG A 73 ? 1.0416 0.9711 1.2217 0.2248 -0.1907 0.1156 73 ARG A CG 348 C CD . ARG A 73 ? 1.2433 1.1939 1.4089 0.2248 -0.1947 0.0960 73 ARG A CD 349 N NE . ARG A 73 ? 1.3774 1.3304 1.5575 0.2198 -0.1987 0.0760 73 ARG A NE 350 C CZ . ARG A 73 ? 1.4985 1.4500 1.6962 0.2270 -0.2066 0.0683 73 ARG A CZ 351 N NH1 . ARG A 73 ? 1.5842 1.5290 1.7882 0.2390 -0.2121 0.0791 73 ARG A NH1 352 N NH2 . ARG A 73 ? 1.4782 1.4359 1.6868 0.2233 -0.2095 0.0496 73 ARG A NH2 353 N N . ALA A 74 ? 1.0617 0.9955 1.1992 0.2180 -0.1608 0.1665 74 ALA A N 354 C CA . ALA A 74 ? 0.9872 0.9327 1.1036 0.2240 -0.1537 0.1828 74 ALA A CA 355 C C . ALA A 74 ? 1.0950 1.0497 1.1911 0.2185 -0.1491 0.1709 74 ALA A C 356 O O . ALA A 74 ? 1.0232 0.9929 1.0940 0.2255 -0.1502 0.1668 74 ALA A O 357 C CB . ALA A 74 ? 0.7693 0.7067 0.9011 0.2246 -0.1471 0.2101 74 ALA A CB 358 N N . CYS A 75 ? 1.0342 0.9794 1.1418 0.2066 -0.1454 0.1641 75 CYS A N 359 C CA . CYS A 75 ? 1.0677 1.0187 1.1585 0.2010 -0.1413 0.1540 75 CYS A CA 360 C C . CYS A 75 ? 1.0121 0.9677 1.0917 0.1963 -0.1482 0.1290 75 CYS A C 361 O O . CYS A 75 ? 0.8856 0.8360 0.9692 0.1858 -0.1476 0.1162 75 CYS A O 362 C CB . CYS A 75 ? 1.0486 0.9884 1.1562 0.1905 -0.1347 0.1575 75 CYS A CB 363 S SG . CYS A 75 ? 1.2158 1.1374 1.3562 0.1807 -0.1396 0.1472 75 CYS A SG 364 N N . ALA A 76 ? 0.9358 0.9023 1.0017 0.2041 -0.1549 0.1235 76 ALA A N 365 C CA . ALA A 76 ? 0.7835 0.7565 0.8418 0.1994 -0.1627 0.1023 76 ALA A CA 366 C C . ALA A 76 ? 0.9543 0.9319 0.9928 0.1958 -0.1629 0.0923 76 ALA A C 367 O O . ALA A 76 ? 1.0300 1.0122 1.0631 0.1904 -0.1700 0.0759 76 ALA A O 368 C CB . ALA A 76 ? 0.6036 0.5879 0.6552 0.2093 -0.1705 0.1004 76 ALA A CB 369 N N . ASN A 77 ? 1.0200 0.9969 1.0484 0.1990 -0.1559 0.1025 77 ASN A N 370 C CA . ASN A 77 ? 1.1863 1.1666 1.1955 0.1977 -0.1571 0.0926 77 ASN A CA 371 C C . ASN A 77 ? 1.2017 1.1713 1.2192 0.1870 -0.1510 0.0904 77 ASN A C 372 O O . ASN A 77 ? 1.1829 1.1531 1.1862 0.1864 -0.1507 0.0845 77 ASN A O 373 C CB . ASN A 77 ? 1.3600 1.3524 1.3466 0.2125 -0.1551 0.1024 77 ASN A CB 374 C CG . ASN A 77 ? 1.4722 1.4762 1.4405 0.2214 -0.1656 0.0924 77 ASN A CG 375 O OD1 . ASN A 77 ? 1.4412 1.4437 1.4098 0.2141 -0.1748 0.0750 77 ASN A OD1 376 N ND2 . ASN A 77 ? 1.5042 1.5212 1.4571 0.2373 -0.1647 0.1040 77 ASN A ND2 377 N N . LEU A 78 ? 1.0791 1.0389 1.1202 0.1793 -0.1473 0.0943 78 LEU A N 378 C CA . LEU A 78 ? 0.7852 0.7348 0.8384 0.1697 -0.1411 0.0943 78 LEU A CA 379 C C . LEU A 78 ? 0.7809 0.7275 0.8299 0.1594 -0.1459 0.0754 78 LEU A C 380 O O . LEU A 78 ? 1.0010 0.9496 1.0541 0.1547 -0.1527 0.0638 78 LEU A O 381 C CB . LEU A 78 ? 0.4323 0.3726 0.5128 0.1656 -0.1391 0.1006 78 LEU A CB 382 C CG . LEU A 78 ? 0.8437 0.7740 0.9413 0.1592 -0.1318 0.1082 78 LEU A CG 383 C CD1 . LEU A 78 ? 0.7889 0.7237 0.8834 0.1662 -0.1239 0.1293 78 LEU A CD1 384 C CD2 . LEU A 78 ? 0.9468 0.8665 1.0720 0.1548 -0.1343 0.1074 78 LEU A CD2 385 N N . GLN A 79 ? 0.6954 0.6388 0.7365 0.1563 -0.1425 0.0730 79 GLN A N 386 C CA . GLN A 79 ? 0.7486 0.6873 0.7866 0.1461 -0.1470 0.0572 79 GLN A CA 387 C C . GLN A 79 ? 0.8200 0.7493 0.8772 0.1358 -0.1422 0.0557 79 GLN A C 388 O O . GLN A 79 ? 0.6587 0.5849 0.7192 0.1263 -0.1458 0.0437 79 GLN A O 389 C CB . GLN A 79 ? 0.8334 0.7731 0.8501 0.1501 -0.1480 0.0537 79 GLN A CB 390 C CG . GLN A 79 ? 1.0833 1.0305 1.0800 0.1574 -0.1572 0.0466 79 GLN A CG 391 C CD . GLN A 79 ? 1.2492 1.1983 1.2246 0.1658 -0.1580 0.0445 79 GLN A CD 392 O OE1 . GLN A 79 ? 1.3367 1.2906 1.2947 0.1728 -0.1670 0.0365 79 GLN A OE1 393 N NE2 . GLN A 79 ? 1.2198 1.1660 1.1971 0.1659 -0.1494 0.0507 79 GLN A NE2 394 N N . VAL A 80 ? 0.8246 0.7502 0.8948 0.1379 -0.1346 0.0686 80 VAL A N 395 C CA . VAL A 80 ? 0.7276 0.6444 0.8159 0.1296 -0.1303 0.0678 80 VAL A CA 396 C C . VAL A 80 ? 0.8997 0.8118 1.0116 0.1308 -0.1270 0.0793 80 VAL A C 397 O O . VAL A 80 ? 1.0191 0.9330 1.1331 0.1370 -0.1219 0.0958 80 VAL A O 398 C CB . VAL A 80 ? 0.5935 0.5091 0.6746 0.1297 -0.1243 0.0720 80 VAL A CB 399 C CG1 . VAL A 80 ? 0.5680 0.4752 0.6699 0.1216 -0.1203 0.0716 80 VAL A CG1 400 C CG2 . VAL A 80 ? 0.4324 0.3496 0.4915 0.1291 -0.1290 0.0600 80 VAL A CG2 401 N N . LEU A 81 ? 0.8131 0.7198 0.9433 0.1252 -0.1304 0.0710 81 LEU A N 402 C CA . LEU A 81 ? 0.7048 0.6039 0.8601 0.1261 -0.1298 0.0792 81 LEU A CA 403 C C . LEU A 81 ? 0.7261 0.6170 0.8989 0.1180 -0.1288 0.0721 81 LEU A C 404 O O . LEU A 81 ? 0.6792 0.5707 0.8549 0.1134 -0.1330 0.0566 81 LEU A O 405 C CB . LEU A 81 ? 0.6936 0.5944 0.8563 0.1302 -0.1367 0.0743 81 LEU A CB 406 C CG . LEU A 81 ? 0.7378 0.6285 0.9283 0.1316 -0.1396 0.0781 81 LEU A CG 407 C CD1 . LEU A 81 ? 0.7517 0.6345 0.9547 0.1324 -0.1341 0.0978 81 LEU A CD1 408 C CD2 . LEU A 81 ? 0.7135 0.6078 0.9064 0.1392 -0.1462 0.0767 81 LEU A CD2 409 N N . ILE A 82 ? 0.8311 0.7165 1.0153 0.1165 -0.1232 0.0839 82 ILE A N 410 C CA . ILE A 82 ? 0.8690 0.7472 1.0700 0.1092 -0.1224 0.0777 82 ILE A CA 411 C C . ILE A 82 ? 0.9258 0.7934 1.1581 0.1090 -0.1257 0.0830 82 ILE A C 412 O O . ILE A 82 ? 0.9977 0.8617 1.2429 0.1104 -0.1224 0.1012 82 ILE A O 413 C CB . ILE A 82 ? 1.0000 0.8805 1.1944 0.1068 -0.1147 0.0855 82 ILE A CB 414 C CG1 . ILE A 82 ? 0.9462 0.8332 1.1129 0.1062 -0.1142 0.0751 82 ILE A CG1 415 C CG2 . ILE A 82 ? 1.2823 1.1551 1.4993 0.1001 -0.1140 0.0828 82 ILE A CG2 416 C CD1 . ILE A 82 ? 0.3643 0.2558 0.5204 0.1075 -0.1072 0.0831 82 ILE A CD1 417 N N . LEU A 83 ? 0.8679 0.7313 1.1130 0.1076 -0.1328 0.0673 83 LEU A N 418 C CA . LEU A 83 ? 0.7748 0.6267 1.0496 0.1091 -0.1391 0.0682 83 LEU A CA 419 C C . LEU A 83 ? 0.9561 0.8018 1.2492 0.1039 -0.1424 0.0551 83 LEU A C 420 O O . LEU A 83 ? 0.8552 0.6925 1.1712 0.1061 -0.1507 0.0474 83 LEU A O 421 C CB . LEU A 83 ? 0.4861 0.3402 0.7612 0.1160 -0.1469 0.0596 83 LEU A CB 422 C CG . LEU A 83 ? 0.7237 0.5794 0.9913 0.1226 -0.1458 0.0757 83 LEU A CG 423 C CD1 . LEU A 83 ? 0.8045 0.6669 1.0658 0.1294 -0.1527 0.0652 83 LEU A CD1 424 C CD2 . LEU A 83 ? 0.7866 0.6288 1.0796 0.1237 -0.1469 0.0941 83 LEU A CD2 425 N N . LYS A 84 ? 1.1025 0.9524 1.3851 0.0981 -0.1367 0.0521 84 LYS A N 426 C CA . LYS A 84 ? 1.1049 0.9516 1.4004 0.0934 -0.1392 0.0388 84 LYS A CA 427 C C . LYS A 84 ? 1.1309 0.9642 1.4609 0.0922 -0.1440 0.0434 84 LYS A C 428 O O . LYS A 84 ? 1.2003 1.0281 1.5428 0.0907 -0.1407 0.0626 84 LYS A O 429 C CB . LYS A 84 ? 1.0393 0.8914 1.3188 0.0879 -0.1316 0.0396 84 LYS A CB 430 C CG . LYS A 84 ? 1.1023 0.9524 1.3928 0.0834 -0.1340 0.0259 84 LYS A CG 431 C CD . LYS A 84 ? 1.1617 1.0133 1.4469 0.0785 -0.1268 0.0320 84 LYS A CD 432 C CE . LYS A 84 ? 1.2367 1.0969 1.4892 0.0781 -0.1218 0.0301 84 LYS A CE 433 N NZ . LYS A 84 ? 1.1842 1.0494 1.4236 0.0767 -0.1260 0.0125 84 LYS A NZ 434 N N . SER A 85 ? 1.0824 0.9118 1.4283 0.0930 -0.1525 0.0258 85 SER A N 435 C CA . SER A 85 ? 1.0482 0.8642 1.4280 0.0912 -0.1592 0.0253 85 SER A CA 436 C C . SER A 85 ? 1.0030 0.8055 1.4075 0.0927 -0.1633 0.0425 85 SER A C 437 O O . SER A 85 ? 1.0846 0.8766 1.5164 0.0878 -0.1653 0.0522 85 SER A O 438 C CB . SER A 85 ? 1.1600 0.9766 1.5442 0.0834 -0.1534 0.0291 85 SER A CB 439 O OG . SER A 85 ? 1.2106 1.0181 1.6238 0.0819 -0.1622 0.0183 85 SER A OG 440 N N . SER A 86 ? 0.9697 0.7727 1.3660 0.0991 -0.1650 0.0472 86 SER A N 441 C CA . SER A 86 ? 0.9820 0.7703 1.4039 0.1019 -0.1719 0.0606 86 SER A CA 442 C C . SER A 86 ? 1.1424 0.9198 1.5879 0.1074 -0.1871 0.0403 86 SER A C 443 O O . SER A 86 ? 1.3382 1.1168 1.7897 0.1062 -0.1912 0.0218 86 SER A O 444 C CB . SER A 86 ? 0.9191 0.7122 1.3237 0.1080 -0.1690 0.0729 86 SER A CB 445 O OG . SER A 86 ? 0.8898 0.6910 1.2788 0.1043 -0.1567 0.0945 86 SER A OG 446 N N . ARG A 87 ? 0.9336 0.7011 1.3918 0.1148 -0.1962 0.0425 87 ARG A N 447 C CA . ARG A 87 ? 1.0718 0.8285 1.5537 0.1218 -0.2122 0.0218 87 ARG A CA 448 C C . ARG A 87 ? 1.0080 0.7741 1.4745 0.1336 -0.2174 0.0066 87 ARG A C 449 O O . ARG A 87 ? 1.0425 0.7995 1.5279 0.1430 -0.2317 -0.0073 87 ARG A O 450 C CB . ARG A 87 ? 1.2698 1.0019 1.7907 0.1206 -0.2227 0.0356 87 ARG A CB 451 C CG . ARG A 87 ? 1.2708 0.9948 1.8141 0.1087 -0.2200 0.0480 87 ARG A CG 452 C CD . ARG A 87 ? 1.3437 1.0629 1.9051 0.1090 -0.2306 0.0230 87 ARG A CD 453 N NE . ARG A 87 ? 1.4480 1.1592 2.0346 0.0975 -0.2295 0.0345 87 ARG A NE 454 C CZ . ARG A 87 ? 1.4037 1.0945 2.0294 0.0925 -0.2386 0.0499 87 ARG A CZ 455 N NH1 . ARG A 87 ? 1.1872 0.8611 1.8309 0.0984 -0.2500 0.0557 87 ARG A NH1 456 N NH2 . ARG A 87 ? 1.4987 1.1864 2.1467 0.0812 -0.2366 0.0601 87 ARG A NH2 457 N N . ILE A 88 ? 0.8980 0.6833 1.3309 0.1336 -0.2065 0.0087 88 ILE A N 458 C CA . ILE A 88 ? 0.8966 0.6931 1.3143 0.1436 -0.2097 0.0003 88 ILE A CA 459 C C . ILE A 88 ? 0.8005 0.6054 1.2230 0.1530 -0.2203 -0.0281 88 ILE A C 460 O O . ILE A 88 ? 0.7579 0.5779 1.1683 0.1508 -0.2170 -0.0428 88 ILE A O 461 C CB . ILE A 88 ? 0.6846 0.5015 1.0665 0.1406 -0.1971 0.0058 88 ILE A CB 462 C CG1 . ILE A 88 ? 0.7568 0.5686 1.1315 0.1339 -0.1868 0.0325 88 ILE A CG1 463 C CG2 . ILE A 88 ? 0.5545 0.3834 0.9245 0.1506 -0.2012 -0.0017 88 ILE A CG2 464 C CD1 . ILE A 88 ? 0.7228 0.5525 1.0630 0.1309 -0.1756 0.0371 88 ILE A CD1 465 N N . ASN A 89 ? 0.5290 0.3255 0.9685 0.1644 -0.2333 -0.0354 89 ASN A N 466 C CA . ASN A 89 ? 0.7330 0.5412 1.1758 0.1762 -0.2438 -0.0632 89 ASN A CA 467 C C . ASN A 89 ? 0.6991 0.5240 1.1283 0.1879 -0.2466 -0.0703 89 ASN A C 468 O O . ASN A 89 ? 0.7864 0.6303 1.2113 0.1976 -0.2519 -0.0924 89 ASN A O 469 C CB . ASN A 89 ? 0.9164 0.7033 1.3942 0.1822 -0.2603 -0.0756 89 ASN A CB 470 C CG . ASN A 89 ? 0.9500 0.7170 1.4495 0.1919 -0.2736 -0.0713 89 ASN A CG 471 O OD1 . ASN A 89 ? 1.0220 0.7886 1.5118 0.1926 -0.2693 -0.0547 89 ASN A OD1 472 N ND2 . ASN A 89 ? 0.9342 0.6840 1.4639 0.2001 -0.2912 -0.0868 89 ASN A ND2 473 N N . THR A 90 ? 0.6507 0.4713 1.0726 0.1876 -0.2428 -0.0516 90 THR A N 474 C CA . THR A 90 ? 0.7871 0.6264 1.1942 0.1978 -0.2443 -0.0578 90 THR A CA 475 C C . THR A 90 ? 0.8649 0.7080 1.2520 0.1929 -0.2341 -0.0359 90 THR A C 476 O O . THR A 90 ? 0.9858 0.8094 1.3810 0.1900 -0.2332 -0.0149 90 THR A O 477 C CB . THR A 90 ? 0.7295 0.5599 1.1589 0.2145 -0.2618 -0.0718 90 THR A CB 478 O OG1 . THR A 90 ? 0.7280 0.5593 1.1511 0.2213 -0.2630 -0.0613 90 THR A OG1 479 C CG2 . THR A 90 ? 0.5759 0.3734 1.0385 0.2146 -0.2733 -0.0690 90 THR A CG2 480 N N . ILE A 91 ? 0.8105 0.6801 1.1718 0.1920 -0.2268 -0.0405 91 ILE A N 481 C CA . ILE A 91 ? 0.6262 0.5026 0.9662 0.1879 -0.2180 -0.0233 91 ILE A CA 482 C C . ILE A 91 ? 0.6500 0.5460 0.9812 0.1985 -0.2225 -0.0315 91 ILE A C 483 O O . ILE A 91 ? 0.7798 0.7007 1.1019 0.2002 -0.2222 -0.0476 91 ILE A O 484 C CB . ILE A 91 ? 0.5174 0.4089 0.8335 0.1757 -0.2057 -0.0210 91 ILE A CB 485 C CG1 . ILE A 91 ? 0.4635 0.3387 0.7852 0.1650 -0.1999 -0.0121 91 ILE A CG1 486 C CG2 . ILE A 91 ? 0.5522 0.4536 0.8460 0.1741 -0.1994 -0.0080 91 ILE A CG2 487 C CD1 . ILE A 91 ? 0.4233 0.3121 0.7252 0.1546 -0.1905 -0.0152 91 ILE A CD1 488 N N . GLU A 92 ? 0.6740 0.5609 1.0083 0.2056 -0.2264 -0.0195 92 GLU A N 489 C CA . GLU A 92 ? 0.7591 0.6655 1.0849 0.2161 -0.2308 -0.0266 92 GLU A CA 490 C C . GLU A 92 ? 0.7133 0.6488 1.0142 0.2093 -0.2221 -0.0307 92 GLU A C 491 O O . GLU A 92 ? 0.5761 0.5110 0.8624 0.1974 -0.2125 -0.0207 92 GLU A O 492 C CB . GLU A 92 ? 0.8641 0.7571 1.1912 0.2224 -0.2336 -0.0085 92 GLU A CB 493 C CG . GLU A 92 ? 0.9060 0.7754 1.2603 0.2333 -0.2466 -0.0087 92 GLU A CG 494 C CD . GLU A 92 ? 0.9945 0.8762 1.3595 0.2467 -0.2582 -0.0342 92 GLU A CD 495 O OE1 . GLU A 92 ? 1.1310 1.0435 1.4811 0.2480 -0.2551 -0.0488 92 GLU A OE1 496 O OE2 . GLU A 92 ? 0.8719 0.7334 1.2610 0.2563 -0.2710 -0.0393 92 GLU A OE2 497 N N . GLY A 93 ? 0.7399 0.7015 1.0372 0.2170 -0.2263 -0.0455 93 GLY A N 498 C CA . GLY A 93 ? 0.6342 0.6252 0.9125 0.2096 -0.2196 -0.0506 93 GLY A CA 499 C C . GLY A 93 ? 0.7068 0.6991 0.9650 0.2009 -0.2122 -0.0349 93 GLY A C 500 O O . GLY A 93 ? 0.6266 0.6292 0.8709 0.1892 -0.2052 -0.0342 93 GLY A O 501 N N . ASP A 94 ? 0.7817 0.7636 1.0384 0.2075 -0.2148 -0.0226 94 ASP A N 502 C CA . ASP A 94 ? 0.7837 0.7689 1.0207 0.2029 -0.2096 -0.0089 94 ASP A CA 503 C C . ASP A 94 ? 0.6809 0.6419 0.9133 0.1976 -0.2036 0.0099 94 ASP A C 504 O O . ASP A 94 ? 0.6927 0.6536 0.9107 0.1982 -0.2010 0.0226 94 ASP A O 505 C CB . ASP A 94 ? 0.7098 0.7052 0.9443 0.2146 -0.2159 -0.0072 94 ASP A CB 506 C CG . ASP A 94 ? 0.8422 0.8172 1.0935 0.2271 -0.2231 -0.0013 94 ASP A CG 507 O OD1 . ASP A 94 ? 0.9379 0.8965 1.2074 0.2285 -0.2262 -0.0055 94 ASP A OD1 508 O OD2 . ASP A 94 ? 0.8982 0.8733 1.1453 0.2359 -0.2267 0.0073 94 ASP A OD2 509 N N . ALA A 95 ? 0.5545 0.4977 0.7995 0.1930 -0.2016 0.0111 95 ALA A N 510 C CA . ALA A 95 ? 0.6299 0.5530 0.8740 0.1877 -0.1955 0.0290 95 ALA A CA 511 C C . ALA A 95 ? 0.6744 0.6060 0.8940 0.1800 -0.1874 0.0362 95 ALA A C 512 O O . ALA A 95 ? 0.9152 0.8382 1.1273 0.1804 -0.1830 0.0532 95 ALA A O 513 C CB . ALA A 95 ? 0.7503 0.6588 1.0108 0.1814 -0.1944 0.0251 95 ALA A CB 514 N N . PHE A 96 ? 0.5780 0.5272 0.7856 0.1736 -0.1860 0.0237 96 PHE A N 515 C CA . PHE A 96 ? 0.7373 0.6908 0.9239 0.1654 -0.1798 0.0284 96 PHE A CA 516 C C . PHE A 96 ? 0.7442 0.7155 0.9132 0.1673 -0.1824 0.0267 96 PHE A C 517 O O . PHE A 96 ? 0.6628 0.6378 0.8146 0.1613 -0.1796 0.0281 96 PHE A O 518 C CB . PHE A 96 ? 0.7600 0.7160 0.9454 0.1540 -0.1762 0.0186 96 PHE A CB 519 C CG . PHE A 96 ? 0.8022 0.7419 1.0043 0.1514 -0.1740 0.0188 96 PHE A CG 520 C CD1 . PHE A 96 ? 0.8656 0.7873 1.0717 0.1513 -0.1697 0.0338 96 PHE A CD1 521 C CD2 . PHE A 96 ? 0.8165 0.7613 1.0303 0.1491 -0.1763 0.0043 96 PHE A CD2 522 C CE1 . PHE A 96 ? 0.7949 0.7024 1.0187 0.1478 -0.1685 0.0339 96 PHE A CE1 523 C CE2 . PHE A 96 ? 0.7961 0.7261 1.0257 0.1470 -0.1756 0.0030 96 PHE A CE2 524 C CZ . PHE A 96 ? 0.7221 0.6328 0.9576 0.1458 -0.1720 0.0177 96 PHE A CZ 525 N N . TYR A 97 ? 0.7254 0.7071 0.8994 0.1763 -0.1888 0.0229 97 TYR A N 526 C CA . TYR A 97 ? 0.7910 0.7923 0.9518 0.1784 -0.1928 0.0194 97 TYR A CA 527 C C . TYR A 97 ? 0.8277 0.8273 0.9680 0.1795 -0.1912 0.0301 97 TYR A C 528 O O . TYR A 97 ? 0.7098 0.7238 0.8373 0.1765 -0.1941 0.0249 97 TYR A O 529 C CB . TYR A 97 ? 0.8247 0.8354 0.9956 0.1904 -0.2001 0.0158 97 TYR A CB 530 C CG . TYR A 97 ? 1.0249 1.0533 1.2089 0.1903 -0.2040 -0.0005 97 TYR A CG 531 C CD1 . TYR A 97 ? 1.1304 1.1593 1.3212 0.1818 -0.2008 -0.0089 97 TYR A CD1 532 C CD2 . TYR A 97 ? 1.1532 1.1997 1.3425 0.2000 -0.2109 -0.0073 97 TYR A CD2 533 C CE1 . TYR A 97 ? 1.2261 1.2751 1.4278 0.1833 -0.2040 -0.0235 97 TYR A CE1 534 C CE2 . TYR A 97 ? 1.2126 1.2797 1.4137 0.2016 -0.2142 -0.0222 97 TYR A CE2 535 C CZ . TYR A 97 ? 1.2902 1.3591 1.4971 0.1934 -0.2105 -0.0300 97 TYR A CZ 536 O OH . TYR A 97 ? 1.3216 1.4144 1.5390 0.1963 -0.2133 -0.0444 97 TYR A OH 537 N N . SER A 98 ? 0.9512 0.9350 1.0889 0.1844 -0.1872 0.0451 98 SER A N 538 C CA . SER A 98 ? 0.9167 0.9030 1.0341 0.1889 -0.1862 0.0548 98 SER A CA 539 C C . SER A 98 ? 0.8061 0.7865 0.9103 0.1811 -0.1802 0.0571 98 SER A C 540 O O . SER A 98 ? 0.6961 0.6790 0.7822 0.1856 -0.1793 0.0638 98 SER A O 541 C CB . SER A 98 ? 0.8956 0.8740 1.0149 0.2012 -0.1857 0.0719 98 SER A CB 542 O OG . SER A 98 ? 0.9948 0.9553 1.1282 0.1995 -0.1802 0.0830 98 SER A OG 543 N N . LEU A 99 ? 0.8187 0.7929 0.9313 0.1706 -0.1768 0.0504 99 LEU A N 544 C CA . LEU A 99 ? 0.9360 0.9033 1.0383 0.1633 -0.1713 0.0519 99 LEU A CA 545 C C . LEU A 99 ? 0.8954 0.8718 0.9834 0.1556 -0.1750 0.0400 99 LEU A C 546 O O . LEU A 99 ? 1.0411 1.0118 1.1257 0.1472 -0.1720 0.0365 99 LEU A O 547 C CB . LEU A 99 ? 0.9613 0.9165 1.0802 0.1561 -0.1664 0.0509 99 LEU A CB 548 C CG . LEU A 99 ? 0.9037 0.8453 1.0385 0.1609 -0.1626 0.0644 99 LEU A CG 549 C CD1 . LEU A 99 ? 0.9442 0.8774 1.1004 0.1550 -0.1625 0.0570 99 LEU A CD1 550 C CD2 . LEU A 99 ? 0.9020 0.8374 1.0271 0.1617 -0.1554 0.0787 99 LEU A CD2 551 N N . GLY A 100 ? 0.6440 0.6341 0.7248 0.1585 -0.1823 0.0343 100 GLY A N 552 C CA . GLY A 100 ? 0.5710 0.5704 0.6438 0.1500 -0.1881 0.0230 100 GLY A CA 553 C C . GLY A 100 ? 0.7283 0.7209 0.7852 0.1451 -0.1882 0.0213 100 GLY A C 554 O O . GLY A 100 ? 0.9128 0.9114 0.9649 0.1377 -0.1950 0.0122 100 GLY A O 555 N N . SER A 101 ? 0.5402 0.5209 0.5901 0.1492 -0.1814 0.0299 101 SER A N 556 C CA . SER A 101 ? 0.5444 0.5189 0.5784 0.1469 -0.1818 0.0275 101 SER A CA 557 C C . SER A 101 ? 0.7755 0.7383 0.8171 0.1392 -0.1742 0.0288 101 SER A C 558 O O . SER A 101 ? 0.8389 0.7951 0.8699 0.1367 -0.1735 0.0267 101 SER A O 559 C CB . SER A 101 ? 0.7043 0.6795 0.7206 0.1606 -0.1801 0.0364 101 SER A CB 560 O OG . SER A 101 ? 0.8920 0.8781 0.8964 0.1684 -0.1889 0.0327 101 SER A OG 561 N N . LEU A 102 ? 0.8426 0.8029 0.9030 0.1366 -0.1694 0.0316 102 LEU A N 562 C CA . LEU A 102 ? 0.8425 0.7921 0.9131 0.1310 -0.1623 0.0339 102 LEU A CA 563 C C . LEU A 102 ? 0.7470 0.6955 0.8175 0.1190 -0.1645 0.0228 102 LEU A C 564 O O . LEU A 102 ? 0.7257 0.6830 0.8021 0.1130 -0.1695 0.0146 102 LEU A O 565 C CB . LEU A 102 ? 0.8583 0.8059 0.9503 0.1323 -0.1596 0.0372 102 LEU A CB 566 C CG . LEU A 102 ? 0.7701 0.7071 0.8771 0.1269 -0.1538 0.0382 102 LEU A CG 567 C CD1 . LEU A 102 ? 0.6308 0.5589 0.7349 0.1308 -0.1468 0.0515 102 LEU A CD1 568 C CD2 . LEU A 102 ? 0.7827 0.7196 0.9108 0.1291 -0.1555 0.0366 102 LEU A CD2 569 N N . GLU A 103 ? 0.7224 0.6617 0.7864 0.1159 -0.1609 0.0234 103 GLU A N 570 C CA . GLU A 103 ? 0.8110 0.7480 0.8746 0.1048 -0.1635 0.0141 103 GLU A CA 571 C C . GLU A 103 ? 0.8756 0.8049 0.9511 0.0992 -0.1571 0.0140 103 GLU A C 572 O O . GLU A 103 ? 0.8781 0.8085 0.9579 0.0901 -0.1588 0.0069 103 GLU A O 573 C CB . GLU A 103 ? 0.8465 0.7800 0.8909 0.1042 -0.1693 0.0101 103 GLU A CB 574 C CG . GLU A 103 ? 0.8931 0.8238 0.9218 0.1160 -0.1674 0.0163 103 GLU A CG 575 C CD . GLU A 103 ? 1.0713 1.0004 1.0810 0.1176 -0.1768 0.0086 103 GLU A CD 576 O OE1 . GLU A 103 ? 1.1480 1.0715 1.1574 0.1079 -0.1825 0.0005 103 GLU A OE1 577 O OE2 . GLU A 103 ? 1.1166 1.0501 1.1121 0.1291 -0.1794 0.0107 103 GLU A OE2 578 N N . HIS A 104 ? 0.8647 0.7874 0.9464 0.1046 -0.1500 0.0227 104 HIS A N 579 C CA . HIS A 104 ? 0.7633 0.6788 0.8586 0.1002 -0.1446 0.0228 104 HIS A CA 580 C C . HIS A 104 ? 0.8005 0.7150 0.9166 0.1035 -0.1423 0.0272 104 HIS A C 581 O O . HIS A 104 ? 0.9417 0.8537 1.0611 0.1106 -0.1394 0.0384 104 HIS A O 582 C CB . HIS A 104 ? 0.7225 0.6306 0.8097 0.1027 -0.1391 0.0295 104 HIS A CB 583 C CG . HIS A 104 ? 0.8325 0.7338 0.9322 0.0974 -0.1344 0.0285 104 HIS A CG 584 N ND1 . HIS A 104 ? 0.9211 0.8180 1.0122 0.0929 -0.1341 0.0234 104 HIS A ND1 585 C CD2 . HIS A 104 ? 0.7394 0.6370 0.8601 0.0965 -0.1309 0.0315 104 HIS A CD2 586 C CE1 . HIS A 104 ? 0.7994 0.6918 0.9051 0.0894 -0.1299 0.0233 104 HIS A CE1 587 N NE2 . HIS A 104 ? 0.7692 0.6617 0.8934 0.0914 -0.1282 0.0279 104 HIS A NE2 588 N N . LEU A 105 ? 0.7327 0.6498 0.8630 0.0992 -0.1443 0.0186 105 LEU A N 589 C CA . LEU A 105 ? 0.6596 0.5742 0.8110 0.1032 -0.1444 0.0198 105 LEU A CA 590 C C . LEU A 105 ? 0.7142 0.6235 0.8806 0.0986 -0.1430 0.0135 105 LEU A C 591 O O . LEU A 105 ? 0.7451 0.6613 0.9106 0.0934 -0.1450 0.0026 105 LEU A O 592 C CB . LEU A 105 ? 0.5687 0.4950 0.7248 0.1066 -0.1503 0.0132 105 LEU A CB 593 C CG . LEU A 105 ? 0.5164 0.4403 0.6950 0.1115 -0.1528 0.0101 105 LEU A CG 594 C CD1 . LEU A 105 ? 0.5841 0.4954 0.7722 0.1177 -0.1512 0.0235 105 LEU A CD1 595 C CD2 . LEU A 105 ? 0.6078 0.5466 0.7894 0.1155 -0.1587 0.0014 105 LEU A CD2 596 N N . ASP A 106 ? 0.7004 0.5988 0.8817 0.1006 -0.1400 0.0211 106 ASP A N 597 C CA . ASP A 106 ? 0.6718 0.5641 0.8680 0.0965 -0.1392 0.0156 106 ASP A CA 598 C C . ASP A 106 ? 0.6707 0.5563 0.8929 0.1008 -0.1431 0.0148 106 ASP A C 599 O O . ASP A 106 ? 0.5957 0.4714 0.8302 0.1032 -0.1416 0.0274 106 ASP A O 600 C CB . ASP A 106 ? 0.6503 0.5353 0.8425 0.0936 -0.1328 0.0248 106 ASP A CB 601 C CG . ASP A 106 ? 0.8494 0.7286 1.0571 0.0892 -0.1321 0.0193 106 ASP A CG 602 O OD1 . ASP A 106 ? 0.8979 0.7784 1.1184 0.0889 -0.1369 0.0074 106 ASP A OD1 603 O OD2 . ASP A 106 ? 0.9149 0.7899 1.1216 0.0870 -0.1269 0.0266 106 ASP A OD2 604 N N . LEU A 107 ? 0.6600 0.5519 0.8909 0.1023 -0.1489 0.0002 107 LEU A N 605 C CA . LEU A 107 ? 0.6858 0.5713 0.9416 0.1080 -0.1552 -0.0046 107 LEU A CA 606 C C . LEU A 107 ? 0.7021 0.5840 0.9727 0.1055 -0.1574 -0.0157 107 LEU A C 607 O O . LEU A 107 ? 0.6684 0.5470 0.9590 0.1109 -0.1648 -0.0252 107 LEU A O 608 C CB . LEU A 107 ? 0.5595 0.4571 0.8157 0.1150 -0.1617 -0.0148 107 LEU A CB 609 C CG . LEU A 107 ? 0.6027 0.5053 0.8478 0.1193 -0.1618 -0.0064 107 LEU A CG 610 C CD1 . LEU A 107 ? 0.6021 0.5191 0.8508 0.1264 -0.1686 -0.0189 107 LEU A CD1 611 C CD2 . LEU A 107 ? 0.7524 0.6393 1.0082 0.1231 -0.1616 0.0095 107 LEU A CD2 612 N N . SER A 108 ? 0.6815 0.5641 0.9422 0.0985 -0.1521 -0.0157 108 SER A N 613 C CA . SER A 108 ? 0.7616 0.6423 1.0349 0.0964 -0.1543 -0.0267 108 SER A CA 614 C C . SER A 108 ? 0.7338 0.5989 1.0365 0.0986 -0.1589 -0.0247 108 SER A C 615 O O . SER A 108 ? 0.7372 0.5910 1.0491 0.0981 -0.1570 -0.0092 108 SER A O 616 C CB . SER A 108 ? 0.7055 0.5873 0.9638 0.0888 -0.1477 -0.0245 108 SER A CB 617 O OG . SER A 108 ? 0.6164 0.4876 0.8760 0.0858 -0.1420 -0.0093 108 SER A OG 618 N N . ASP A 109 ? 0.8121 0.6779 1.1301 0.1011 -0.1656 -0.0404 109 ASP A N 619 C CA . ASP A 109 ? 0.8665 0.7170 1.2143 0.1016 -0.1717 -0.0418 109 ASP A CA 620 C C . ASP A 109 ? 0.8500 0.6878 1.2209 0.1078 -0.1800 -0.0380 109 ASP A C 621 O O . ASP A 109 ? 0.9389 0.7604 1.3329 0.1051 -0.1822 -0.0273 109 ASP A O 622 C CB . ASP A 109 ? 0.8625 0.7043 1.2143 0.0931 -0.1647 -0.0278 109 ASP A CB 623 C CG . ASP A 109 ? 1.0131 0.8644 1.3480 0.0881 -0.1594 -0.0348 109 ASP A CG 624 O OD1 . ASP A 109 ? 0.9123 0.7733 1.2438 0.0910 -0.1638 -0.0524 109 ASP A OD1 625 O OD2 . ASP A 109 ? 1.0330 0.8831 1.3575 0.0822 -0.1510 -0.0224 109 ASP A OD2 626 N N . ASN A 110 ? 0.7345 0.5801 1.1003 0.1161 -0.1851 -0.0463 110 ASN A N 627 C CA . ASN A 110 ? 0.8117 0.6450 1.1985 0.1235 -0.1945 -0.0446 110 ASN A CA 628 C C . ASN A 110 ? 0.9253 0.7639 1.3244 0.1342 -0.2069 -0.0686 110 ASN A C 629 O O . ASN A 110 ? 1.0092 0.8618 1.4010 0.1351 -0.2071 -0.0845 110 ASN A O 630 C CB . ASN A 110 ? 0.7964 0.6341 1.1673 0.1261 -0.1904 -0.0321 110 ASN A CB 631 C CG . ASN A 110 ? 0.6876 0.5200 1.0484 0.1182 -0.1797 -0.0084 110 ASN A CG 632 O OD1 . ASN A 110 ? 0.7326 0.5749 1.0711 0.1121 -0.1704 -0.0052 110 ASN A OD1 633 N ND2 . ASN A 110 ? 0.6026 0.4201 0.9802 0.1189 -0.1814 0.0086 110 ASN A ND2 634 N N . HIS A 111 ? 0.9455 0.7740 1.3629 0.1434 -0.2176 -0.0713 111 HIS A N 635 C CA . HIS A 111 ? 0.8565 0.6902 1.2868 0.1563 -0.2312 -0.0957 111 HIS A CA 636 C C . HIS A 111 ? 0.8264 0.6802 1.2399 0.1662 -0.2320 -0.1036 111 HIS A C 637 O O . HIS A 111 ? 0.8409 0.6923 1.2687 0.1790 -0.2442 -0.1155 111 HIS A O 638 C CB . HIS A 111 ? 0.8716 0.6791 1.3377 0.1618 -0.2461 -0.0972 111 HIS A CB 639 C CG . HIS A 111 ? 0.9124 0.6988 1.3999 0.1507 -0.2457 -0.0844 111 HIS A CG 640 N ND1 . HIS A 111 ? 1.0734 0.8345 1.5877 0.1477 -0.2515 -0.0672 111 HIS A ND1 641 C CD2 . HIS A 111 ? 0.7633 0.5518 1.2502 0.1417 -0.2401 -0.0851 111 HIS A CD2 642 C CE1 . HIS A 111 ? 1.0196 0.7695 1.5499 0.1369 -0.2492 -0.0577 111 HIS A CE1 643 N NE2 . HIS A 111 ? 0.8636 0.6297 1.3773 0.1335 -0.2424 -0.0690 111 HIS A NE2 644 N N . LEU A 112 ? 0.7643 0.6377 1.1490 0.1605 -0.2199 -0.0970 112 LEU A N 645 C CA . LEU A 112 ? 0.8530 0.7503 1.2213 0.1682 -0.2197 -0.1042 112 LEU A CA 646 C C . LEU A 112 ? 0.8627 0.7836 1.2311 0.1784 -0.2260 -0.1290 112 LEU A C 647 O O . LEU A 112 ? 0.7350 0.6758 1.0878 0.1738 -0.2195 -0.1342 112 LEU A O 648 C CB . LEU A 112 ? 0.7927 0.7035 1.1329 0.1580 -0.2063 -0.0902 112 LEU A CB 649 C CG . LEU A 112 ? 0.6922 0.5941 1.0252 0.1556 -0.2022 -0.0708 112 LEU A CG 650 C CD1 . LEU A 112 ? 0.6200 0.4961 0.9766 0.1606 -0.2098 -0.0622 112 LEU A CD1 651 C CD2 . LEU A 112 ? 0.4668 0.3673 0.7803 0.1427 -0.1901 -0.0545 112 LEU A CD2 652 N N . SER A 113 ? 0.9273 0.8466 1.3135 0.1933 -0.2393 -0.1441 113 SER A N 653 C CA . SER A 113 ? 0.8683 0.8092 1.2579 0.2061 -0.2474 -0.1695 113 SER A CA 654 C C . SER A 113 ? 0.7683 0.7483 1.1341 0.2087 -0.2403 -0.1742 113 SER A C 655 O O . SER A 113 ? 0.7825 0.7891 1.1438 0.2164 -0.2421 -0.1912 113 SER A O 656 C CB . SER A 113 ? 0.9983 0.9275 1.4126 0.2233 -0.2648 -0.1850 113 SER A CB 657 O OG . SER A 113 ? 1.0661 0.9571 1.5056 0.2192 -0.2722 -0.1766 113 SER A OG 658 N N . SER A 114 ? 0.8799 0.8646 1.2312 0.2024 -0.2323 -0.1584 114 SER A N 659 C CA . SER A 114 ? 0.9497 0.9709 1.2808 0.2028 -0.2258 -0.1598 114 SER A CA 660 C C . SER A 114 ? 0.9019 0.9184 1.2196 0.1927 -0.2177 -0.1394 114 SER A C 661 O O . SER A 114 ? 0.9250 0.9138 1.2501 0.1907 -0.2191 -0.1272 114 SER A O 662 C CB . SER A 114 ? 0.8982 0.9433 1.2363 0.2219 -0.2356 -0.1789 114 SER A CB 663 O OG . SER A 114 ? 0.8244 0.8508 1.1747 0.2297 -0.2434 -0.1758 114 SER A OG 664 N N . LEU A 115 ? 0.7833 0.8278 1.0820 0.1867 -0.2099 -0.1353 115 LEU A N 665 C CA . LEU A 115 ? 0.7066 0.7472 0.9906 0.1754 -0.2023 -0.1169 115 LEU A CA 666 C C . LEU A 115 ? 0.7735 0.8368 1.0532 0.1824 -0.2044 -0.1177 115 LEU A C 667 O O . LEU A 115 ? 0.8243 0.9168 1.1068 0.1927 -0.2083 -0.1315 115 LEU A O 668 C CB . LEU A 115 ? 0.5576 0.6075 0.8241 0.1603 -0.1926 -0.1093 115 LEU A CB 669 C CG . LEU A 115 ? 0.5017 0.5371 0.7716 0.1549 -0.1907 -0.1118 115 LEU A CG 670 C CD1 . LEU A 115 ? 0.4918 0.5343 0.7443 0.1405 -0.1820 -0.1035 115 LEU A CD1 671 C CD2 . LEU A 115 ? 0.6163 0.6153 0.8982 0.1537 -0.1925 -0.1041 115 LEU A CD2 672 N N . SER A 116 ? 0.7056 0.7578 0.9785 0.1777 -0.2020 -0.1032 116 SER A N 673 C CA . SER A 116 ? 0.6732 0.7453 0.9426 0.1843 -0.2045 -0.1033 116 SER A CA 674 C C . SER A 116 ? 0.7413 0.8296 0.9925 0.1715 -0.1973 -0.0923 116 SER A C 675 O O . SER A 116 ? 0.7560 0.8262 0.9971 0.1597 -0.1918 -0.0796 116 SER A O 676 C CB . SER A 116 ? 0.6064 0.6541 0.8849 0.1925 -0.2103 -0.0970 116 SER A CB 677 O OG . SER A 116 ? 0.7115 0.7797 0.9893 0.2021 -0.2147 -0.1005 116 SER A OG 678 N N . SER A 117 ? 0.7094 0.8326 0.9575 0.1741 -0.1980 -0.0975 117 SER A N 679 C CA . SER A 117 ? 0.7352 0.8754 0.9694 0.1614 -0.1931 -0.0879 117 SER A CA 680 C C . SER A 117 ? 0.9279 1.0509 1.1554 0.1595 -0.1938 -0.0759 117 SER A C 681 O O . SER A 117 ? 0.9988 1.1250 1.2142 0.1481 -0.1908 -0.0668 117 SER A O 682 C CB . SER A 117 ? 0.7110 0.8955 0.9471 0.1652 -0.1944 -0.0954 117 SER A CB 683 O OG . SER A 117 ? 0.7708 0.9647 1.0174 0.1822 -0.2013 -0.1047 117 SER A OG 684 N N . SER A 118 ? 0.8806 0.9848 1.1164 0.1712 -0.1987 -0.0760 118 SER A N 685 C CA . SER A 118 ? 0.7316 0.8227 0.9620 0.1734 -0.2003 -0.0652 118 SER A CA 686 C C . SER A 118 ? 0.7379 0.7980 0.9592 0.1651 -0.1956 -0.0510 118 SER A C 687 O O . SER A 118 ? 0.8480 0.9031 1.0589 0.1636 -0.1952 -0.0409 118 SER A O 688 C CB . SER A 118 ? 0.7316 0.8153 0.9755 0.1901 -0.2080 -0.0697 118 SER A CB 689 O OG . SER A 118 ? 0.7474 0.8629 0.9976 0.2000 -0.2129 -0.0826 118 SER A OG 690 N N . TRP A 119 ? 0.6873 0.7285 0.9128 0.1609 -0.1925 -0.0506 119 TRP A N 691 C CA . TRP A 119 ? 0.6524 0.6666 0.8712 0.1545 -0.1877 -0.0372 119 TRP A CA 692 C C . TRP A 119 ? 0.6468 0.6650 0.8465 0.1429 -0.1829 -0.0300 119 TRP A C 693 O O . TRP A 119 ? 0.6717 0.6744 0.8619 0.1412 -0.1804 -0.0184 119 TRP A O 694 C CB . TRP A 119 ? 0.5571 0.5545 0.7853 0.1512 -0.1855 -0.0396 119 TRP A CB 695 C CG . TRP A 119 ? 0.5997 0.5856 0.8486 0.1618 -0.1916 -0.0458 119 TRP A CG 696 C CD1 . TRP A 119 ? 0.5446 0.5237 0.8040 0.1734 -0.1982 -0.0443 119 TRP A CD1 697 C CD2 . TRP A 119 ? 0.6931 0.6706 0.9558 0.1622 -0.1932 -0.0547 119 TRP A CD2 698 N NE1 . TRP A 119 ? 0.5713 0.5370 0.8515 0.1807 -0.2046 -0.0521 119 TRP A NE1 699 C CE2 . TRP A 119 ? 0.5880 0.5530 0.8706 0.1741 -0.2018 -0.0592 119 TRP A CE2 700 C CE3 . TRP A 119 ? 0.6746 0.6539 0.9351 0.1540 -0.1890 -0.0599 119 TRP A CE3 701 C CZ2 . TRP A 119 ? 0.6625 0.6168 0.9635 0.1780 -0.2071 -0.0696 119 TRP A CZ2 702 C CZ3 . TRP A 119 ? 0.7156 0.6859 0.9931 0.1582 -0.1934 -0.0698 119 TRP A CZ3 703 C CH2 . TRP A 119 ? 0.7341 0.6919 1.0321 0.1700 -0.2027 -0.0751 119 TRP A CH2 704 N N . PHE A 120 ? 0.6488 0.6882 0.8433 0.1353 -0.1822 -0.0366 120 PHE A N 705 C CA . PHE A 120 ? 0.7296 0.7688 0.9087 0.1229 -0.1789 -0.0311 120 PHE A CA 706 C C . PHE A 120 ? 0.8568 0.9150 1.0271 0.1198 -0.1824 -0.0299 120 PHE A C 707 O O . PHE A 120 ? 0.8061 0.8611 0.9639 0.1108 -0.1820 -0.0252 120 PHE A O 708 C CB . PHE A 120 ? 0.7333 0.7785 0.9136 0.1143 -0.1758 -0.0368 120 PHE A CB 709 C CG . PHE A 120 ? 0.8233 0.8523 1.0140 0.1177 -0.1737 -0.0400 120 PHE A CG 710 C CD1 . PHE A 120 ? 0.7848 0.7870 0.9751 0.1182 -0.1710 -0.0317 120 PHE A CD1 711 C CD2 . PHE A 120 ? 0.9078 0.9503 1.1095 0.1208 -0.1749 -0.0512 120 PHE A CD2 712 C CE1 . PHE A 120 ? 0.8395 0.8270 1.0421 0.1204 -0.1700 -0.0343 120 PHE A CE1 713 C CE2 . PHE A 120 ? 0.7443 0.7712 0.9568 0.1242 -0.1745 -0.0556 120 PHE A CE2 714 C CZ . PHE A 120 ? 0.7255 0.7242 0.9395 0.1233 -0.1723 -0.0469 120 PHE A CZ 715 N N . GLY A 121 ? 0.8897 0.9674 1.0677 0.1278 -0.1867 -0.0348 121 GLY A N 716 C CA . GLY A 121 ? 0.9323 1.0327 1.1058 0.1250 -0.1908 -0.0348 121 GLY A CA 717 C C . GLY A 121 ? 0.9443 1.0334 1.1043 0.1234 -0.1930 -0.0267 121 GLY A C 718 O O . GLY A 121 ? 0.9720 1.0702 1.1246 0.1137 -0.1955 -0.0256 121 GLY A O 719 N N . PRO A 122 ? 0.9574 1.0275 1.1146 0.1335 -0.1929 -0.0209 122 PRO A N 720 C CA . PRO A 122 ? 0.8681 0.9280 1.0114 0.1362 -0.1948 -0.0129 122 PRO A CA 721 C C . PRO A 122 ? 0.8098 0.8511 0.9396 0.1288 -0.1912 -0.0074 122 PRO A C 722 O O . PRO A 122 ? 0.9075 0.9442 1.0237 0.1310 -0.1936 -0.0026 122 PRO A O 723 C CB . PRO A 122 ? 0.7981 0.8440 0.9463 0.1498 -0.1942 -0.0069 122 PRO A CB 724 C CG . PRO A 122 ? 0.9862 1.0226 1.1482 0.1499 -0.1906 -0.0100 122 PRO A CG 725 C CD . PRO A 122 ? 1.0064 1.0666 1.1761 0.1447 -0.1922 -0.0218 122 PRO A CD 726 N N . LEU A 123 ? 0.4818 0.5137 0.6146 0.1217 -0.1862 -0.0086 123 LEU A N 727 C CA . LEU A 123 ? 0.7122 0.7267 0.8326 0.1158 -0.1828 -0.0040 123 LEU A CA 728 C C . LEU A 123 ? 0.8229 0.8437 0.9346 0.1039 -0.1864 -0.0078 123 LEU A C 729 O O . LEU A 123 ? 0.9016 0.9132 1.0106 0.0961 -0.1835 -0.0083 123 LEU A O 730 C CB . LEU A 123 ? 0.7507 0.7505 0.8786 0.1141 -0.1763 -0.0030 123 LEU A CB 731 C CG . LEU A 123 ? 0.6694 0.6624 0.8125 0.1230 -0.1743 -0.0012 123 LEU A CG 732 C CD1 . LEU A 123 ? 0.6462 0.6240 0.7956 0.1192 -0.1689 -0.0004 123 LEU A CD1 733 C CD2 . LEU A 123 ? 0.6190 0.6037 0.7584 0.1333 -0.1746 0.0090 123 LEU A CD2 734 N N . SER A 124 ? 0.8118 0.8476 0.9204 0.1024 -0.1935 -0.0101 124 SER A N 735 C CA . SER A 124 ? 0.7264 0.7668 0.8289 0.0907 -0.1993 -0.0128 124 SER A CA 736 C C . SER A 124 ? 0.7435 0.7626 0.8308 0.0880 -0.1995 -0.0107 124 SER A C 737 O O . SER A 124 ? 0.7863 0.8045 0.8695 0.0780 -0.2052 -0.0133 124 SER A O 738 C CB . SER A 124 ? 0.7061 0.7638 0.8084 0.0913 -0.2083 -0.0150 124 SER A CB 739 O OG . SER A 124 ? 0.6965 0.7452 0.7858 0.1016 -0.2115 -0.0125 124 SER A OG 740 N N . SER A 125 ? 0.7101 0.7129 0.7900 0.0969 -0.1939 -0.0058 125 SER A N 741 C CA . SER A 125 ? 0.6810 0.6670 0.7462 0.0966 -0.1936 -0.0044 125 SER A CA 742 C C . SER A 125 ? 0.7720 0.7456 0.8404 0.0917 -0.1861 -0.0032 125 SER A C 743 O O . SER A 125 ? 0.7691 0.7295 0.8263 0.0915 -0.1853 -0.0025 125 SER A O 744 C CB . SER A 125 ? 0.6606 0.6404 0.7135 0.1103 -0.1923 0.0015 125 SER A CB 745 O OG . SER A 125 ? 0.7788 0.7674 0.8233 0.1142 -0.2015 -0.0015 125 SER A OG 746 N N . LEU A 126 ? 0.6547 0.6339 0.7384 0.0887 -0.1814 -0.0042 126 LEU A N 747 C CA . LEU A 126 ? 0.6163 0.5851 0.7057 0.0862 -0.1742 -0.0034 126 LEU A CA 748 C C . LEU A 126 ? 0.7158 0.6803 0.8006 0.0751 -0.1759 -0.0070 126 LEU A C 749 O O . LEU A 126 ? 0.7811 0.7572 0.8691 0.0664 -0.1808 -0.0107 126 LEU A O 750 C CB . LEU A 126 ? 0.5779 0.5558 0.6851 0.0877 -0.1710 -0.0058 126 LEU A CB 751 C CG . LEU A 126 ? 0.5849 0.5519 0.7024 0.0899 -0.1644 -0.0047 126 LEU A CG 752 C CD1 . LEU A 126 ? 0.6149 0.5679 0.7307 0.0985 -0.1605 0.0043 126 LEU A CD1 753 C CD2 . LEU A 126 ? 0.7197 0.6985 0.8541 0.0926 -0.1648 -0.0103 126 LEU A CD2 754 N N . LYS A 127 ? 0.7520 0.7008 0.8296 0.0756 -0.1721 -0.0050 127 LYS A N 755 C CA . LYS A 127 ? 0.8613 0.8036 0.9348 0.0663 -0.1737 -0.0081 127 LYS A CA 756 C C . LYS A 127 ? 0.8457 0.7847 0.9294 0.0638 -0.1666 -0.0088 127 LYS A C 757 O O . LYS A 127 ? 0.8474 0.7880 0.9330 0.0552 -0.1676 -0.0118 127 LYS A O 758 C CB . LYS A 127 ? 0.8060 0.7337 0.8625 0.0693 -0.1763 -0.0075 127 LYS A CB 759 C CG . LYS A 127 ? 0.8417 0.7712 0.8870 0.0705 -0.1862 -0.0099 127 LYS A CG 760 C CD . LYS A 127 ? 0.9443 0.8595 0.9731 0.0734 -0.1908 -0.0124 127 LYS A CD 761 C CE . LYS A 127 ? 1.1376 1.0541 1.1545 0.0782 -0.2018 -0.0161 127 LYS A CE 762 N NZ . LYS A 127 ? 1.1469 1.0708 1.1708 0.0673 -0.2125 -0.0201 127 LYS A NZ 763 N N . TYR A 128 ? 0.7412 0.6759 0.8322 0.0714 -0.1602 -0.0055 128 TYR A N 764 C CA . TYR A 128 ? 0.6533 0.5825 0.7546 0.0704 -0.1544 -0.0064 128 TYR A CA 765 C C . TYR A 128 ? 0.7356 0.6696 0.8540 0.0761 -0.1519 -0.0065 128 TYR A C 766 O O . TYR A 128 ? 0.8727 0.8045 0.9934 0.0836 -0.1510 -0.0008 128 TYR A O 767 C CB . TYR A 128 ? 0.5909 0.5055 0.6851 0.0739 -0.1500 -0.0013 128 TYR A CB 768 C CG . TYR A 128 ? 0.6955 0.6044 0.8028 0.0738 -0.1443 -0.0012 128 TYR A CG 769 C CD1 . TYR A 128 ? 0.6399 0.5429 0.7442 0.0686 -0.1432 -0.0045 128 TYR A CD1 770 C CD2 . TYR A 128 ? 0.8172 0.7256 0.9409 0.0789 -0.1411 0.0021 128 TYR A CD2 771 C CE1 . TYR A 128 ? 0.8243 0.7229 0.9416 0.0685 -0.1387 -0.0052 128 TYR A CE1 772 C CE2 . TYR A 128 ? 0.8718 0.7742 1.0101 0.0784 -0.1375 0.0014 128 TYR A CE2 773 C CZ . TYR A 128 ? 0.8274 0.7259 0.9624 0.0732 -0.1361 -0.0025 128 TYR A CZ 774 O OH . TYR A 128 ? 0.6364 0.5298 0.7865 0.0727 -0.1332 -0.0040 128 TYR A OH 775 N N . LEU A 129 ? 0.6875 0.6282 0.8179 0.0733 -0.1514 -0.0130 129 LEU A N 776 C CA . LEU A 129 ? 0.6709 0.6166 0.8189 0.0796 -0.1513 -0.0163 129 LEU A CA 777 C C . LEU A 129 ? 0.7346 0.6781 0.8940 0.0782 -0.1495 -0.0225 129 LEU A C 778 O O . LEU A 129 ? 0.8010 0.7568 0.9607 0.0740 -0.1507 -0.0296 129 LEU A O 779 C CB . LEU A 129 ? 0.5742 0.5401 0.7251 0.0805 -0.1558 -0.0217 129 LEU A CB 780 C CG . LEU A 129 ? 0.4909 0.4663 0.6592 0.0878 -0.1575 -0.0290 129 LEU A CG 781 C CD1 . LEU A 129 ? 0.5186 0.4815 0.6955 0.0966 -0.1578 -0.0238 129 LEU A CD1 782 C CD2 . LEU A 129 ? 0.4577 0.4582 0.6266 0.0880 -0.1613 -0.0345 129 LEU A CD2 783 N N . ASN A 130 ? 0.7212 0.6505 0.8910 0.0818 -0.1467 -0.0192 130 ASN A N 784 C CA . ASN A 130 ? 0.6937 0.6196 0.8764 0.0811 -0.1460 -0.0257 130 ASN A CA 785 C C . ASN A 130 ? 0.7392 0.6661 0.9432 0.0887 -0.1498 -0.0318 130 ASN A C 786 O O . ASN A 130 ? 0.7070 0.6223 0.9225 0.0935 -0.1502 -0.0253 130 ASN A O 787 C CB . ASN A 130 ? 0.6043 0.5145 0.7861 0.0787 -0.1414 -0.0187 130 ASN A CB 788 C CG . ASN A 130 ? 0.6445 0.5505 0.8411 0.0780 -0.1413 -0.0252 130 ASN A CG 789 O OD1 . ASN A 130 ? 0.5772 0.4920 0.7834 0.0799 -0.1450 -0.0362 130 ASN A OD1 790 N ND2 . ASN A 130 ? 0.6523 0.5468 0.8512 0.0761 -0.1373 -0.0189 130 ASN A ND2 791 N N . LEU A 131 ? 0.6778 0.6195 0.8869 0.0904 -0.1532 -0.0441 131 LEU A N 792 C CA . LEU A 131 ? 0.5958 0.5412 0.8237 0.0994 -0.1588 -0.0535 131 LEU A CA 793 C C . LEU A 131 ? 0.7107 0.6528 0.9533 0.1013 -0.1612 -0.0640 131 LEU A C 794 O O . LEU A 131 ? 0.5475 0.4901 0.8074 0.1099 -0.1676 -0.0737 131 LEU A O 795 C CB . LEU A 131 ? 0.4855 0.4552 0.7094 0.1033 -0.1621 -0.0614 131 LEU A CB 796 C CG . LEU A 131 ? 0.6663 0.6415 0.8827 0.1049 -0.1627 -0.0545 131 LEU A CG 797 C CD1 . LEU A 131 ? 0.6601 0.6629 0.8772 0.1098 -0.1664 -0.0640 131 LEU A CD1 798 C CD2 . LEU A 131 ? 0.7526 0.7100 0.9807 0.1118 -0.1649 -0.0482 131 LEU A CD2 799 N N . MET A 132 ? 0.8637 0.8021 1.0996 0.0944 -0.1574 -0.0632 132 MET A N 800 C CA . MET A 132 ? 0.8628 0.7993 1.1116 0.0962 -0.1600 -0.0738 132 MET A CA 801 C C . MET A 132 ? 0.8645 0.7827 1.1378 0.1011 -0.1645 -0.0742 132 MET A C 802 O O . MET A 132 ? 0.9660 0.8696 1.2439 0.0999 -0.1627 -0.0615 132 MET A O 803 C CB . MET A 132 ? 0.6768 0.6081 0.9153 0.0879 -0.1549 -0.0700 132 MET A CB 804 C CG . MET A 132 ? 0.6206 0.5674 0.8387 0.0823 -0.1522 -0.0702 132 MET A CG 805 S SD . MET A 132 ? 0.6545 0.5905 0.8646 0.0748 -0.1480 -0.0669 132 MET A SD 806 C CE . MET A 132 ? 0.7617 0.6759 0.9713 0.0722 -0.1436 -0.0522 132 MET A CE 807 N N . GLY A 133 ? 0.6537 0.5730 0.9435 0.1065 -0.1709 -0.0883 133 GLY A N 808 C CA . GLY A 133 ? 0.6399 0.5396 0.9558 0.1090 -0.1764 -0.0884 133 GLY A CA 809 C C . GLY A 133 ? 0.7947 0.6912 1.1290 0.1194 -0.1861 -0.0959 133 GLY A C 810 O O . GLY A 133 ? 0.9104 0.7884 1.2691 0.1213 -0.1923 -0.0943 133 GLY A O 811 N N . ASN A 134 ? 0.8793 0.7945 1.2033 0.1261 -0.1880 -0.1035 134 ASN A N 812 C CA . ASN A 134 ? 0.8572 0.7718 1.1964 0.1378 -0.1977 -0.1118 134 ASN A CA 813 C C . ASN A 134 ? 0.8522 0.7879 1.1946 0.1493 -0.2056 -0.1347 134 ASN A C 814 O O . ASN A 134 ? 0.9115 0.8721 1.2356 0.1486 -0.2009 -0.1399 134 ASN A O 815 C CB . ASN A 134 ? 0.8429 0.7632 1.1695 0.1386 -0.1944 -0.1012 134 ASN A CB 816 C CG . ASN A 134 ? 0.7659 0.6651 1.0932 0.1314 -0.1891 -0.0797 134 ASN A CG 817 O OD1 . ASN A 134 ? 0.5743 0.4724 0.8855 0.1218 -0.1798 -0.0674 134 ASN A OD1 818 N ND2 . ASN A 134 ? 0.8229 0.7066 1.1681 0.1373 -0.1956 -0.0749 134 ASN A ND2 819 N N . PRO A 135 ? 0.7987 0.7250 1.1650 0.1605 -0.2182 -0.1482 135 PRO A N 820 C CA . PRO A 135 ? 0.6357 0.5784 1.0104 0.1747 -0.2288 -0.1728 135 PRO A CA 821 C C . PRO A 135 ? 0.7505 0.7246 1.1116 0.1854 -0.2294 -0.1825 135 PRO A C 822 O O . PRO A 135 ? 0.8137 0.7977 1.1863 0.2014 -0.2409 -0.2020 135 PRO A O 823 C CB . PRO A 135 ? 0.7105 0.6272 1.1164 0.1829 -0.2433 -0.1796 135 PRO A CB 824 C CG . PRO A 135 ? 0.8748 0.7621 1.2899 0.1696 -0.2384 -0.1571 135 PRO A CG 825 C CD . PRO A 135 ? 0.9036 0.8000 1.2927 0.1600 -0.2240 -0.1383 135 PRO A CD 826 N N . TYR A 136 ? 0.6477 0.6385 0.9860 0.1776 -0.2182 -0.1697 136 TYR A N 827 C CA . TYR A 136 ? 0.7159 0.7406 1.0429 0.1866 -0.2184 -0.1779 136 TYR A CA 828 C C . TYR A 136 ? 0.6726 0.7295 0.9885 0.1899 -0.2163 -0.1901 136 TYR A C 829 O O . TYR A 136 ? 0.6381 0.6925 0.9461 0.1799 -0.2102 -0.1851 136 TYR A O 830 C CB . TYR A 136 ? 0.7476 0.7787 1.0574 0.1773 -0.2090 -0.1599 136 TYR A CB 831 C CG . TYR A 136 ? 0.6676 0.6912 0.9610 0.1597 -0.1976 -0.1425 136 TYR A CG 832 C CD1 . TYR A 136 ? 0.6872 0.7353 0.9632 0.1531 -0.1907 -0.1414 136 TYR A CD1 833 C CD2 . TYR A 136 ? 0.7926 0.7858 1.0884 0.1504 -0.1942 -0.1268 136 TYR A CD2 834 C CE1 . TYR A 136 ? 0.7618 0.8010 1.0235 0.1381 -0.1820 -0.1266 136 TYR A CE1 835 C CE2 . TYR A 136 ? 0.7705 0.7579 1.0508 0.1365 -0.1848 -0.1128 136 TYR A CE2 836 C CZ . TYR A 136 ? 0.7864 0.7952 1.0499 0.1306 -0.1794 -0.1135 136 TYR A CZ 837 O OH . TYR A 136 ? 0.9048 0.9058 1.1536 0.1176 -0.1717 -0.1006 136 TYR A OH 838 N N . GLN A 137 ? 0.7646 0.8533 1.0799 0.2048 -0.2214 -0.2058 137 GLN A N 839 C CA . GLN A 137 ? 0.8439 0.9678 1.1494 0.2104 -0.2199 -0.2176 137 GLN A CA 840 C C . GLN A 137 ? 0.8358 0.9902 1.1190 0.1998 -0.2076 -0.2035 137 GLN A C 841 O O . GLN A 137 ? 0.7877 0.9625 1.0597 0.1961 -0.2025 -0.2034 137 GLN A O 842 C CB . GLN A 137 ? 0.8996 1.0480 1.2149 0.2335 -0.2315 -0.2418 137 GLN A CB 843 C CG . GLN A 137 ? 0.8565 1.0492 1.1604 0.2426 -0.2299 -0.2542 137 GLN A CG 844 C CD . GLN A 137 ? 0.8047 1.0175 1.1204 0.2682 -0.2437 -0.2818 137 GLN A CD 845 O OE1 . GLN A 137 ? 0.6938 0.9100 1.0174 0.2799 -0.2505 -0.2886 137 GLN A OE1 846 N NE2 . GLN A 137 ? 0.6299 0.8561 0.9466 0.2783 -0.2489 -0.2987 137 GLN A NE2 847 N N . THR A 138 ? 0.8494 1.0070 1.1275 0.1951 -0.2039 -0.1916 138 THR A N 848 C CA . THR A 138 ? 0.7831 0.9655 1.0433 0.1830 -0.1937 -0.1765 138 THR A CA 849 C C . THR A 138 ? 0.8015 0.9605 1.0593 0.1724 -0.1906 -0.1599 138 THR A C 850 O O . THR A 138 ? 0.8204 0.9462 1.0890 0.1740 -0.1949 -0.1590 138 THR A O 851 C CB . THR A 138 ? 0.7537 0.9852 1.0105 0.1946 -0.1943 -0.1846 138 THR A CB 852 O OG1 . THR A 138 ? 0.7590 0.9902 1.0247 0.2048 -0.2001 -0.1892 138 THR A OG1 853 C CG2 . THR A 138 ? 0.7760 1.0334 1.0366 0.2109 -0.1996 -0.2049 138 THR A CG2 854 N N . LEU A 139 ? 0.7516 0.9285 0.9963 0.1616 -0.1837 -0.1464 139 LEU A N 855 C CA . LEU A 139 ? 0.5473 0.7060 0.7890 0.1536 -0.1819 -0.1326 139 LEU A CA 856 C C . LEU A 139 ? 0.5623 0.7409 0.8095 0.1649 -0.1864 -0.1376 139 LEU A C 857 O O . LEU A 139 ? 0.7348 0.9144 0.9767 0.1587 -0.1843 -0.1267 139 LEU A O 858 C CB . LEU A 139 ? 0.4516 0.6129 0.6777 0.1355 -0.1742 -0.1155 139 LEU A CB 859 C CG . LEU A 139 ? 0.6083 0.7458 0.8268 0.1229 -0.1697 -0.1076 139 LEU A CG 860 C CD1 . LEU A 139 ? 0.6872 0.8352 0.8915 0.1075 -0.1645 -0.0935 139 LEU A CD1 861 C CD2 . LEU A 139 ? 0.4902 0.5855 0.7128 0.1207 -0.1703 -0.1027 139 LEU A CD2 862 N N . GLY A 140 ? 0.5824 0.7777 0.8404 0.1825 -0.1933 -0.1552 140 GLY A N 863 C CA . GLY A 140 ? 0.8347 1.0502 1.0983 0.1953 -0.1984 -0.1617 140 GLY A CA 864 C C . GLY A 140 ? 0.8606 1.1243 1.1160 0.1936 -0.1936 -0.1585 140 GLY A C 865 O O . GLY A 140 ? 0.7914 1.0707 1.0361 0.1798 -0.1861 -0.1478 140 GLY A O 866 N N . VAL A 141 ? 0.7710 1.0583 1.0326 0.2076 -0.1986 -0.1670 141 VAL A N 867 C CA . VAL A 141 ? 0.6854 1.0256 0.9430 0.2098 -0.1953 -0.1667 141 VAL A CA 868 C C . VAL A 141 ? 0.6876 1.0372 0.9390 0.1954 -0.1904 -0.1492 141 VAL A C 869 O O . VAL A 141 ? 0.8205 1.2151 1.0713 0.1961 -0.1879 -0.1473 141 VAL A O 870 C CB . VAL A 141 ? 0.6495 1.0170 0.9172 0.2338 -0.2035 -0.1859 141 VAL A CB 871 C CG1 . VAL A 141 ? 0.8188 1.1685 1.0954 0.2496 -0.2118 -0.2053 141 VAL A CG1 872 C CG2 . VAL A 141 ? 0.5185 0.8709 0.7920 0.2387 -0.2087 -0.1841 141 VAL A CG2 873 N N . THR A 142 ? 0.5856 0.8955 0.8333 0.1832 -0.1895 -0.1367 142 THR A N 874 C CA . THR A 142 ? 0.5534 0.8691 0.7946 0.1689 -0.1861 -0.1209 142 THR A CA 875 C C . THR A 142 ? 0.5802 0.8636 0.8113 0.1497 -0.1813 -0.1065 142 THR A C 876 O O . THR A 142 ? 0.6545 0.8990 0.8851 0.1495 -0.1819 -0.1070 142 THR A O 877 C CB . THR A 142 ? 0.8047 1.1062 1.0499 0.1759 -0.1915 -0.1203 142 THR A CB 878 O OG1 . THR A 142 ? 0.7955 1.1039 1.0518 0.1974 -0.1987 -0.1368 142 THR A OG1 879 C CG2 . THR A 142 ? 0.7776 1.1085 1.0201 0.1677 -0.1899 -0.1107 142 THR A CG2 880 N N . SER A 143 ? 0.4789 0.7786 0.7031 0.1338 -0.1772 -0.0936 143 SER A N 881 C CA . SER A 143 ? 0.6220 0.8934 0.8363 0.1163 -0.1739 -0.0811 143 SER A CA 882 C C . SER A 143 ? 0.7744 1.0021 0.9856 0.1166 -0.1761 -0.0778 143 SER A C 883 O O . SER A 143 ? 0.9662 1.1924 1.1796 0.1220 -0.1796 -0.0773 143 SER A O 884 C CB . SER A 143 ? 0.6614 0.9543 0.8715 0.0997 -0.1722 -0.0676 143 SER A CB 885 O OG . SER A 143 ? 0.7291 1.0710 0.9449 0.1009 -0.1704 -0.0683 143 SER A OG 886 N N . LEU A 144 ? 0.7541 0.9482 0.9601 0.1114 -0.1739 -0.0750 144 LEU A N 887 C CA . LEU A 144 ? 0.6383 0.7948 0.8414 0.1121 -0.1751 -0.0702 144 LEU A CA 888 C C . LEU A 144 ? 0.6956 0.8403 0.8869 0.0989 -0.1743 -0.0578 144 LEU A C 889 O O . LEU A 144 ? 0.8045 0.9315 0.9926 0.1014 -0.1763 -0.0533 144 LEU A O 890 C CB . LEU A 144 ? 0.5231 0.6504 0.7283 0.1141 -0.1735 -0.0731 144 LEU A CB 891 C CG . LEU A 144 ? 0.5589 0.6929 0.7774 0.1284 -0.1766 -0.0873 144 LEU A CG 892 C CD1 . LEU A 144 ? 0.4986 0.6025 0.7214 0.1288 -0.1759 -0.0896 144 LEU A CD1 893 C CD2 . LEU A 144 ? 0.2984 0.4347 0.5262 0.1420 -0.1824 -0.0924 144 LEU A CD2 894 N N . PHE A 145 ? 0.6173 0.7720 0.8023 0.0857 -0.1724 -0.0522 145 PHE A N 895 C CA . PHE A 145 ? 0.5293 0.6651 0.7030 0.0735 -0.1730 -0.0422 145 PHE A CA 896 C C . PHE A 145 ? 0.6252 0.7806 0.7969 0.0632 -0.1767 -0.0357 145 PHE A C 897 O O . PHE A 145 ? 0.6287 0.7692 0.7918 0.0524 -0.1788 -0.0288 145 PHE A O 898 C CB . PHE A 145 ? 0.3980 0.5171 0.5653 0.0650 -0.1697 -0.0397 145 PHE A CB 899 C CG . PHE A 145 ? 0.5702 0.6784 0.7427 0.0732 -0.1665 -0.0470 145 PHE A CG 900 C CD1 . PHE A 145 ? 0.6130 0.6971 0.7887 0.0824 -0.1664 -0.0491 145 PHE A CD1 901 C CD2 . PHE A 145 ? 0.8447 0.9674 1.0198 0.0717 -0.1641 -0.0511 145 PHE A CD2 902 C CE1 . PHE A 145 ? 0.7828 0.8561 0.9662 0.0890 -0.1650 -0.0558 145 PHE A CE1 903 C CE2 . PHE A 145 ? 0.9070 1.0197 1.0879 0.0797 -0.1626 -0.0592 145 PHE A CE2 904 C CZ . PHE A 145 ? 0.9157 1.0029 1.1017 0.0879 -0.1635 -0.0619 145 PHE A CZ 905 N N . PRO A 146 ? 0.7075 0.8963 0.8881 0.0668 -0.1786 -0.0381 146 PRO A N 906 C CA . PRO A 146 ? 0.6709 0.8822 0.8530 0.0543 -0.1822 -0.0307 146 PRO A CA 907 C C . PRO A 146 ? 0.8476 1.0403 1.0229 0.0499 -0.1881 -0.0259 146 PRO A C 908 O O . PRO A 146 ? 0.8368 1.0331 1.0109 0.0363 -0.1924 -0.0190 146 PRO A O 909 C CB . PRO A 146 ? 0.5227 0.7752 0.7168 0.0621 -0.1826 -0.0352 146 PRO A CB 910 C CG . PRO A 146 ? 0.6326 0.8830 0.8305 0.0790 -0.1798 -0.0463 146 PRO A CG 911 C CD . PRO A 146 ? 0.7832 0.9892 0.9734 0.0823 -0.1791 -0.0471 146 PRO A CD 912 N N . ASN A 147 ? 0.9418 1.1154 1.1131 0.0616 -0.1890 -0.0293 147 ASN A N 913 C CA . ASN A 147 ? 1.0887 1.2489 1.2527 0.0607 -0.1948 -0.0260 147 ASN A CA 914 C C . ASN A 147 ? 0.9559 1.0784 1.1065 0.0612 -0.1937 -0.0236 147 ASN A C 915 O O . ASN A 147 ? 1.1000 1.2065 1.2444 0.0704 -0.1948 -0.0233 147 ASN A O 916 C CB . ASN A 147 ? 1.3233 1.4921 1.4914 0.0746 -0.1970 -0.0298 147 ASN A CB 917 C CG . ASN A 147 ? 1.4753 1.6758 1.6569 0.0823 -0.1952 -0.0359 147 ASN A CG 918 O OD1 . ASN A 147 ? 1.3954 1.5906 1.5808 0.0962 -0.1935 -0.0416 147 ASN A OD1 919 N ND2 . ASN A 147 ? 1.7706 2.0050 1.9603 0.0737 -0.1962 -0.0345 147 ASN A ND2 920 N N . LEU A 148 ? 0.7453 0.8553 0.8913 0.0520 -0.1915 -0.0214 148 LEU A N 921 C CA . LEU A 148 ? 0.7260 0.8032 0.8596 0.0531 -0.1900 -0.0195 148 LEU A CA 922 C C . LEU A 148 ? 0.7914 0.8593 0.9174 0.0401 -0.1949 -0.0161 148 LEU A C 923 O O . LEU A 148 ? 0.8070 0.8596 0.9283 0.0357 -0.1921 -0.0151 148 LEU A O 924 C CB . LEU A 148 ? 0.6400 0.7052 0.7758 0.0579 -0.1824 -0.0217 148 LEU A CB 925 C CG . LEU A 148 ? 0.6196 0.6800 0.7611 0.0720 -0.1793 -0.0244 148 LEU A CG 926 C CD1 . LEU A 148 ? 0.8012 0.8895 0.9551 0.0777 -0.1807 -0.0294 148 LEU A CD1 927 C CD2 . LEU A 148 ? 0.4887 0.5330 0.6331 0.0748 -0.1735 -0.0260 148 LEU A CD2 928 N N . THR A 149 ? 0.8104 0.8875 0.9366 0.0344 -0.2033 -0.0146 149 THR A N 929 C CA . THR A 149 ? 0.8012 0.8706 0.9235 0.0214 -0.2112 -0.0117 149 THR A CA 930 C C . THR A 149 ? 0.7439 0.7813 0.8514 0.0227 -0.2120 -0.0123 149 THR A C 931 O O . THR A 149 ? 0.7164 0.7436 0.8206 0.0126 -0.2188 -0.0108 149 THR A O 932 C CB . THR A 149 ? 0.8368 0.9150 0.9607 0.0186 -0.2220 -0.0118 149 THR A CB 933 O OG1 . THR A 149 ? 0.7779 0.8442 0.8916 0.0324 -0.2228 -0.0153 149 THR A OG1 934 C CG2 . THR A 149 ? 0.8180 0.9322 0.9585 0.0144 -0.2225 -0.0101 149 THR A CG2 935 N N . ASN A 150 ? 0.6904 0.7125 0.7898 0.0352 -0.2057 -0.0140 150 ASN A N 936 C CA . ASN A 150 ? 0.8125 0.8081 0.8976 0.0383 -0.2057 -0.0144 150 ASN A CA 937 C C . ASN A 150 ? 0.8673 0.8513 0.9520 0.0394 -0.1965 -0.0138 150 ASN A C 938 O O . ASN A 150 ? 0.7920 0.7563 0.8657 0.0434 -0.1952 -0.0139 150 ASN A O 939 C CB . ASN A 150 ? 1.0026 0.9896 1.0770 0.0515 -0.2065 -0.0151 150 ASN A CB 940 C CG . ASN A 150 ? 1.0031 0.9877 1.0692 0.0503 -0.2187 -0.0178 150 ASN A CG 941 O OD1 . ASN A 150 ? 1.1029 1.0700 1.1561 0.0523 -0.2233 -0.0200 150 ASN A OD1 942 N ND2 . ASN A 150 ? 0.8181 0.8211 0.8925 0.0475 -0.2251 -0.0186 150 ASN A ND2 943 N N . LEU A 151 ? 0.8977 0.8960 0.9945 0.0365 -0.1908 -0.0138 151 LEU A N 944 C CA . LEU A 151 ? 0.7315 0.7218 0.8305 0.0386 -0.1826 -0.0145 151 LEU A CA 945 C C . LEU A 151 ? 0.8123 0.7908 0.9055 0.0294 -0.1843 -0.0136 151 LEU A C 946 O O . LEU A 151 ? 0.8582 0.8447 0.9535 0.0185 -0.1900 -0.0117 151 LEU A O 947 C CB . LEU A 151 ? 0.6357 0.6469 0.7490 0.0401 -0.1779 -0.0168 151 LEU A CB 948 C CG . LEU A 151 ? 0.7821 0.7849 0.9001 0.0460 -0.1704 -0.0194 151 LEU A CG 949 C CD1 . LEU A 151 ? 0.8951 0.8821 1.0119 0.0571 -0.1674 -0.0181 151 LEU A CD1 950 C CD2 . LEU A 151 ? 0.6111 0.6361 0.7424 0.0477 -0.1678 -0.0241 151 LEU A CD2 951 N N . GLN A 152 ? 0.8122 0.7721 0.8993 0.0337 -0.1796 -0.0141 152 GLN A N 952 C CA . GLN A 152 ? 0.7565 0.7031 0.8370 0.0272 -0.1813 -0.0139 152 GLN A CA 953 C C . GLN A 152 ? 0.7422 0.6861 0.8279 0.0291 -0.1732 -0.0152 152 GLN A C 954 O O . GLN A 152 ? 0.7474 0.6863 0.8309 0.0230 -0.1738 -0.0151 152 GLN A O 955 C CB . GLN A 152 ? 0.7494 0.6751 0.8151 0.0315 -0.1853 -0.0144 152 GLN A CB 956 C CG . GLN A 152 ? 0.9261 0.8499 0.9851 0.0281 -0.1966 -0.0151 152 GLN A CG 957 C CD . GLN A 152 ? 1.1312 1.0402 1.1754 0.0387 -0.1994 -0.0174 152 GLN A CD 958 O OE1 . GLN A 152 ? 1.0388 0.9360 1.0758 0.0453 -0.1942 -0.0176 152 GLN A OE1 959 N NE2 . GLN A 152 ? 1.2373 1.1496 1.2771 0.0410 -0.2077 -0.0190 152 GLN A NE2 960 N N . THR A 153 ? 0.6141 0.5608 0.7074 0.0377 -0.1667 -0.0166 153 THR A N 961 C CA . THR A 153 ? 0.4742 0.4170 0.5743 0.0404 -0.1603 -0.0189 153 THR A CA 962 C C . THR A 153 ? 0.5025 0.4576 0.6173 0.0465 -0.1566 -0.0221 153 THR A C 963 O O . THR A 153 ? 0.6379 0.5890 0.7569 0.0543 -0.1548 -0.0208 153 THR A O 964 C CB . THR A 153 ? 0.5419 0.4649 0.6354 0.0458 -0.1569 -0.0169 153 THR A CB 965 O OG1 . THR A 153 ? 0.5880 0.4998 0.6686 0.0408 -0.1610 -0.0165 153 THR A OG1 966 C CG2 . THR A 153 ? 0.3549 0.2746 0.4595 0.0493 -0.1506 -0.0190 153 THR A CG2 967 N N . LEU A 154 ? 0.7093 0.6798 0.8320 0.0439 -0.1560 -0.0264 154 LEU A N 968 C CA . LEU A 154 ? 0.6877 0.6708 0.8249 0.0513 -0.1540 -0.0324 154 LEU A CA 969 C C . LEU A 154 ? 0.6226 0.6001 0.7670 0.0538 -0.1509 -0.0378 154 LEU A C 970 O O . LEU A 154 ? 0.6411 0.6196 0.7809 0.0483 -0.1505 -0.0384 154 LEU A O 971 C CB . LEU A 154 ? 0.6279 0.6390 0.7693 0.0492 -0.1565 -0.0349 154 LEU A CB 972 C CG . LEU A 154 ? 0.6243 0.6519 0.7795 0.0590 -0.1562 -0.0427 154 LEU A CG 973 C CD1 . LEU A 154 ? 0.7115 0.7260 0.8723 0.0678 -0.1567 -0.0425 154 LEU A CD1 974 C CD2 . LEU A 154 ? 0.6074 0.6661 0.7649 0.0573 -0.1583 -0.0436 154 LEU A CD2 975 N N . ARG A 155 ? 0.6568 0.6280 0.8137 0.0621 -0.1497 -0.0414 155 ARG A N 976 C CA . ARG A 155 ? 0.6237 0.5910 0.7910 0.0652 -0.1484 -0.0481 155 ARG A CA 977 C C . ARG A 155 ? 0.6816 0.6591 0.8655 0.0747 -0.1511 -0.0570 155 ARG A C 978 O O . ARG A 155 ? 0.8652 0.8331 1.0583 0.0805 -0.1522 -0.0555 155 ARG A O 979 C CB . ARG A 155 ? 0.5522 0.4962 0.7215 0.0656 -0.1455 -0.0434 155 ARG A CB 980 C CG . ARG A 155 ? 0.5370 0.4699 0.6898 0.0591 -0.1435 -0.0361 155 ARG A CG 981 C CD . ARG A 155 ? 0.5467 0.4624 0.7031 0.0604 -0.1399 -0.0329 155 ARG A CD 982 N NE . ARG A 155 ? 0.6015 0.5071 0.7417 0.0572 -0.1385 -0.0261 155 ARG A NE 983 C CZ . ARG A 155 ? 0.6402 0.5457 0.7668 0.0515 -0.1404 -0.0272 155 ARG A CZ 984 N NH1 . ARG A 155 ? 0.7805 0.6971 0.9078 0.0473 -0.1427 -0.0325 155 ARG A NH1 985 N NH2 . ARG A 155 ? 0.5744 0.4695 0.6869 0.0505 -0.1407 -0.0227 155 ARG A NH2 986 N N . ILE A 156 ? 0.6390 0.6364 0.8265 0.0770 -0.1529 -0.0663 156 ILE A N 987 C CA . ILE A 156 ? 0.6514 0.6599 0.8542 0.0880 -0.1569 -0.0775 156 ILE A CA 988 C C . ILE A 156 ? 0.6834 0.6950 0.8945 0.0921 -0.1585 -0.0886 156 ILE A C 989 O O . ILE A 156 ? 0.6493 0.6560 0.8536 0.0859 -0.1558 -0.0866 156 ILE A O 990 C CB . ILE A 156 ? 0.6143 0.6527 0.8142 0.0906 -0.1586 -0.0808 156 ILE A CB 991 C CG1 . ILE A 156 ? 0.5574 0.6187 0.7498 0.0865 -0.1570 -0.0833 156 ILE A CG1 992 C CG2 . ILE A 156 ? 0.5059 0.5441 0.6963 0.0849 -0.1576 -0.0700 156 ILE A CG2 993 C CD1 . ILE A 156 ? 0.6158 0.7118 0.8063 0.0884 -0.1578 -0.0849 156 ILE A CD1 994 N N . GLY A 157 ? 0.7549 0.7749 0.9808 0.1036 -0.1639 -0.1014 157 GLY A N 995 C CA . GLY A 157 ? 0.7669 0.7933 1.0013 0.1098 -0.1673 -0.1149 157 GLY A CA 996 C C . GLY A 157 ? 0.7914 0.7916 1.0436 0.1129 -0.1710 -0.1190 157 GLY A C 997 O O . GLY A 157 ? 0.7911 0.7680 1.0484 0.1091 -0.1696 -0.1089 157 GLY A O 998 N N . ASN A 158 ? 0.8434 0.8494 1.1057 0.1202 -0.1761 -0.1336 158 ASN A N 999 C CA . ASN A 158 ? 0.9107 0.8938 1.1929 0.1226 -0.1812 -0.1391 158 ASN A CA 1000 C C . ASN A 158 ? 0.8866 0.8797 1.1723 0.1273 -0.1850 -0.1535 158 ASN A C 1001 O O . ASN A 158 ? 0.9653 0.9854 1.2382 0.1308 -0.1841 -0.1602 158 ASN A O 1002 C CB . ASN A 158 ? 0.9719 0.9450 1.2757 0.1326 -0.1901 -0.1461 158 ASN A CB 1003 C CG . ASN A 158 ? 0.9640 0.9615 1.2719 0.1474 -0.1981 -0.1652 158 ASN A CG 1004 O OD1 . ASN A 158 ? 0.9487 0.9672 1.2511 0.1524 -0.1995 -0.1773 158 ASN A OD1 1005 N ND2 . ASN A 158 ? 1.0029 0.9993 1.3199 0.1555 -0.2037 -0.1680 158 ASN A ND2 1006 N N . VAL A 159 ? 0.7823 0.7553 1.0866 0.1278 -0.1899 -0.1581 159 VAL A N 1007 C CA . VAL A 159 ? 0.6908 0.6708 0.9998 0.1322 -0.1943 -0.1720 159 VAL A CA 1008 C C . VAL A 159 ? 0.8354 0.8345 1.1542 0.1487 -0.2052 -0.1948 159 VAL A C 1009 O O . VAL A 159 ? 0.8758 0.8986 1.1845 0.1543 -0.2057 -0.2052 159 VAL A O 1010 C CB . VAL A 159 ? 0.5312 0.4848 0.8595 0.1271 -0.1968 -0.1698 159 VAL A CB 1011 C CG1 . VAL A 159 ? 0.5047 0.4644 0.8454 0.1356 -0.2058 -0.1893 159 VAL A CG1 1012 C CG2 . VAL A 159 ? 0.4004 0.3443 0.7142 0.1135 -0.1859 -0.1521 159 VAL A CG2 1013 N N . GLU A 160 ? 0.9116 0.9017 1.2495 0.1575 -0.2143 -0.2026 160 GLU A N 1014 C CA . GLU A 160 ? 0.8536 0.8558 1.2059 0.1749 -0.2277 -0.2272 160 GLU A CA 1015 C C . GLU A 160 ? 0.8158 0.8415 1.1640 0.1886 -0.2320 -0.2374 160 GLU A C 1016 O O . GLU A 160 ? 0.9471 0.9864 1.3051 0.2051 -0.2434 -0.2595 160 GLU A O 1017 C CB . GLU A 160 ? 0.9336 0.9051 1.3181 0.1773 -0.2398 -0.2341 160 GLU A CB 1018 C CG . GLU A 160 ? 1.0374 0.9847 1.4290 0.1624 -0.2347 -0.2201 160 GLU A CG 1019 C CD . GLU A 160 ? 1.0949 1.0100 1.5191 0.1601 -0.2438 -0.2172 160 GLU A CD 1020 O OE1 . GLU A 160 ? 1.0292 0.9274 1.4642 0.1495 -0.2414 -0.2081 160 GLU A OE1 1021 O OE2 . GLU A 160 ? 1.0225 0.9301 1.4622 0.1687 -0.2535 -0.2234 160 GLU A OE2 1022 N N . THR A 161 ? 0.8147 0.8465 1.1494 0.1831 -0.2237 -0.2227 161 THR A N 1023 C CA . THR A 161 ? 0.8274 0.8816 1.1609 0.1965 -0.2283 -0.2322 161 THR A CA 1024 C C . THR A 161 ? 0.7776 0.8614 1.0870 0.1920 -0.2173 -0.2207 161 THR A C 1025 O O . THR A 161 ? 0.7408 0.8549 1.0465 0.2044 -0.2201 -0.2309 161 THR A O 1026 C CB . THR A 161 ? 0.7390 0.7673 1.0935 0.2014 -0.2371 -0.2326 161 THR A CB 1027 O OG1 . THR A 161 ? 0.7899 0.7844 1.1500 0.1858 -0.2318 -0.2124 161 THR A OG1 1028 C CG2 . THR A 161 ? 0.6863 0.7055 1.0663 0.2174 -0.2545 -0.2564 161 THR A CG2 1029 N N . PHE A 162 ? 0.7051 0.7817 0.9993 0.1747 -0.2056 -0.2000 162 PHE A N 1030 C CA . PHE A 162 ? 0.7017 0.8053 0.9756 0.1688 -0.1966 -0.1887 162 PHE A CA 1031 C C . PHE A 162 ? 0.7231 0.8649 0.9856 0.1749 -0.1952 -0.1974 162 PHE A C 1032 O O . PHE A 162 ? 0.8216 0.9629 1.0771 0.1689 -0.1918 -0.1953 162 PHE A O 1033 C CB . PHE A 162 ? 0.6656 0.7510 0.9264 0.1498 -0.1864 -0.1662 162 PHE A CB 1034 C CG . PHE A 162 ? 0.5559 0.6644 0.7997 0.1427 -0.1794 -0.1540 162 PHE A CG 1035 C CD1 . PHE A 162 ? 0.6770 0.7950 0.9229 0.1474 -0.1809 -0.1529 162 PHE A CD1 1036 C CD2 . PHE A 162 ? 0.3817 0.5021 0.6088 0.1314 -0.1722 -0.1434 162 PHE A CD2 1037 C CE1 . PHE A 162 ? 0.6560 0.7963 0.8887 0.1403 -0.1753 -0.1417 162 PHE A CE1 1038 C CE2 . PHE A 162 ? 0.5267 0.6678 0.7412 0.1238 -0.1671 -0.1315 162 PHE A CE2 1039 C CZ . PHE A 162 ? 0.5994 0.7509 0.8172 0.1279 -0.1686 -0.1307 162 PHE A CZ 1040 N N . SER A 163 ? 0.7364 0.9132 0.9971 0.1875 -0.1977 -0.2068 163 SER A N 1041 C CA . SER A 163 ? 0.8701 1.0878 1.1234 0.1987 -0.1984 -0.2187 163 SER A CA 1042 C C . SER A 163 ? 0.9407 1.2024 1.1780 0.1960 -0.1902 -0.2084 163 SER A C 1043 O O . SER A 163 ? 0.8643 1.1593 1.0912 0.1991 -0.1870 -0.2099 163 SER A O 1044 C CB . SER A 163 ? 0.8418 1.0688 1.1104 0.2218 -0.2114 -0.2453 163 SER A CB 1045 O OG . SER A 163 ? 0.8817 1.1214 1.1555 0.2319 -0.2152 -0.2500 163 SER A OG 1046 N N . GLU A 164 ? 0.8647 1.1279 1.1006 0.1902 -0.1870 -0.1973 164 GLU A N 1047 C CA . GLU A 164 ? 0.8454 1.1497 1.0691 0.1854 -0.1796 -0.1855 164 GLU A CA 1048 C C . GLU A 164 ? 0.9049 1.1929 1.1199 0.1635 -0.1717 -0.1615 164 GLU A C 1049 O O . GLU A 164 ? 0.9686 1.2169 1.1873 0.1556 -0.1724 -0.1555 164 GLU A O 1050 C CB . GLU A 164 ? 0.8485 1.1844 1.0784 0.2014 -0.1838 -0.1962 164 GLU A CB 1051 C CG . GLU A 164 ? 1.1153 1.4887 1.3474 0.2235 -0.1894 -0.2176 164 GLU A CG 1052 C CD . GLU A 164 ? 1.3428 1.7693 1.5722 0.2342 -0.1878 -0.2196 164 GLU A CD 1053 O OE1 . GLU A 164 ? 1.3107 1.7381 1.5412 0.2270 -0.1850 -0.2083 164 GLU A OE1 1054 O OE2 . GLU A 164 ? 1.4724 1.9419 1.6987 0.2505 -0.1893 -0.2325 164 GLU A OE2 1055 N N . ILE A 165 ? 0.8304 1.1501 1.0342 0.1542 -0.1649 -0.1478 165 ILE A N 1056 C CA . ILE A 165 ? 0.8454 1.1549 1.0421 0.1345 -0.1595 -0.1263 165 ILE A CA 1057 C C . ILE A 165 ? 0.8069 1.1646 1.0013 0.1337 -0.1561 -0.1185 165 ILE A C 1058 O O . ILE A 165 ? 0.6499 1.0440 0.8387 0.1334 -0.1525 -0.1143 165 ILE A O 1059 C CB . ILE A 165 ? 0.7477 1.0388 0.9340 0.1182 -0.1551 -0.1127 165 ILE A CB 1060 C CG1 . ILE A 165 ? 0.8829 1.1250 1.0719 0.1164 -0.1574 -0.1172 165 ILE A CG1 1061 C CG2 . ILE A 165 ? 0.6081 0.8991 0.7873 0.0994 -0.1510 -0.0916 165 ILE A CG2 1062 C CD1 . ILE A 165 ? 0.6016 0.8253 0.7804 0.1027 -0.1539 -0.1061 165 ILE A CD1 1063 N N . ARG A 166 ? 0.7069 1.0670 0.9064 0.1334 -0.1574 -0.1159 166 ARG A N 1064 C CA . ARG A 166 ? 0.6178 1.0263 0.8180 0.1336 -0.1548 -0.1093 166 ARG A CA 1065 C C . ARG A 166 ? 0.6783 1.0838 0.8746 0.1122 -0.1513 -0.0874 166 ARG A C 1066 O O . ARG A 166 ? 0.6240 0.9873 0.8166 0.0996 -0.1519 -0.0795 166 ARG A O 1067 C CB . ARG A 166 ? 0.6796 1.1029 0.8895 0.1512 -0.1598 -0.1238 166 ARG A CB 1068 C CG . ARG A 166 ? 0.8642 1.2998 1.0792 0.1742 -0.1650 -0.1469 166 ARG A CG 1069 C CD . ARG A 166 ? 1.0993 1.4831 1.3208 0.1799 -0.1717 -0.1591 166 ARG A CD 1070 N NE . ARG A 166 ? 1.2367 1.6147 1.4695 0.1955 -0.1793 -0.1728 166 ARG A NE 1071 C CZ . ARG A 166 ? 1.2598 1.6035 1.4971 0.1905 -0.1817 -0.1675 166 ARG A CZ 1072 N NH1 . ARG A 166 ? 1.1517 1.4648 1.3827 0.1711 -0.1769 -0.1499 166 ARG A NH1 1073 N NH2 . ARG A 166 ? 1.3166 1.6575 1.5646 0.2062 -0.1894 -0.1802 166 ARG A NH2 1074 N N . ARG A 167 ? 0.7811 1.2332 0.9792 0.1087 -0.1484 -0.0777 167 ARG A N 1075 C CA . ARG A 167 ? 0.8165 1.2700 1.0135 0.0875 -0.1465 -0.0564 167 ARG A CA 1076 C C . ARG A 167 ? 0.7885 1.2161 0.9894 0.0832 -0.1504 -0.0550 167 ARG A C 1077 O O . ARG A 167 ? 0.7808 1.1903 0.9796 0.0658 -0.1513 -0.0405 167 ARG A O 1078 C CB . ARG A 167 ? 0.8030 1.3173 1.0038 0.0848 -0.1424 -0.0454 167 ARG A CB 1079 C CG . ARG A 167 ? 0.8865 1.4057 1.0854 0.0614 -0.1400 -0.0212 167 ARG A CG 1080 C CD . ARG A 167 ? 1.0428 1.6260 1.2491 0.0584 -0.1360 -0.0082 167 ARG A CD 1081 N NE . ARG A 167 ? 1.1519 1.7817 1.3586 0.0803 -0.1328 -0.0218 167 ARG A NE 1082 C CZ . ARG A 167 ? 1.2284 1.8948 1.4308 0.0838 -0.1279 -0.0171 167 ARG A CZ 1083 N NH1 . ARG A 167 ? 1.2762 1.9369 1.4743 0.0658 -0.1255 0.0026 167 ARG A NH1 1084 N NH2 . ARG A 167 ? 1.2194 1.9287 1.4215 0.1064 -0.1262 -0.0323 167 ARG A NH2 1085 N N . ILE A 168 ? 0.7249 1.1501 0.9315 0.0999 -0.1538 -0.0704 168 ILE A N 1086 C CA . ILE A 168 ? 0.8175 1.2183 1.0270 0.0982 -0.1578 -0.0696 168 ILE A CA 1087 C C . ILE A 168 ? 0.9705 1.3139 1.1738 0.0917 -0.1594 -0.0683 168 ILE A C 1088 O O . ILE A 168 ? 1.1069 1.4279 1.3081 0.0821 -0.1614 -0.0600 168 ILE A O 1089 C CB . ILE A 168 ? 0.7020 1.1130 0.9197 0.1191 -0.1619 -0.0863 168 ILE A CB 1090 C CG1 . ILE A 168 ? 0.6545 1.0464 0.8737 0.1354 -0.1645 -0.1039 168 ILE A CG1 1091 C CG2 . ILE A 168 ? 0.2651 0.7346 0.4895 0.1265 -0.1609 -0.0876 168 ILE A CG2 1092 C CD1 . ILE A 168 ? 0.5796 0.9668 0.8077 0.1545 -0.1709 -0.1197 168 ILE A CD1 1093 N N . ASP A 169 ? 0.9225 1.2444 1.1234 0.0976 -0.1589 -0.0767 169 ASP A N 1094 C CA . ASP A 169 ? 0.9061 1.1771 1.1037 0.0957 -0.1604 -0.0779 169 ASP A CA 1095 C C . ASP A 169 ? 0.8544 1.0974 1.0438 0.0783 -0.1599 -0.0630 169 ASP A C 1096 O O . ASP A 169 ? 0.9924 1.2015 1.1802 0.0789 -0.1617 -0.0629 169 ASP A O 1097 C CB . ASP A 169 ? 0.9820 1.2392 1.1792 0.1017 -0.1597 -0.0871 169 ASP A CB 1098 C CG . ASP A 169 ? 0.9920 1.2669 1.1988 0.1222 -0.1632 -0.1059 169 ASP A CG 1099 O OD1 . ASP A 169 ? 1.0657 1.3502 1.2799 0.1327 -0.1669 -0.1124 169 ASP A OD1 1100 O OD2 . ASP A 169 ? 0.7765 1.0555 0.9837 0.1286 -0.1633 -0.1149 169 ASP A OD2 1101 N N . PHE A 170 ? 0.7500 1.0076 0.9346 0.0638 -0.1582 -0.0505 170 PHE A N 1102 C CA . PHE A 170 ? 0.6357 0.8663 0.8128 0.0482 -0.1599 -0.0382 170 PHE A CA 1103 C C . PHE A 170 ? 0.6241 0.8761 0.8039 0.0371 -0.1626 -0.0271 170 PHE A C 1104 O O . PHE A 170 ? 0.5911 0.8336 0.7667 0.0219 -0.1648 -0.0156 170 PHE A O 1105 C CB . PHE A 170 ? 0.5887 0.8035 0.7580 0.0386 -0.1580 -0.0325 170 PHE A CB 1106 C CG . PHE A 170 ? 0.7693 0.9644 0.9373 0.0484 -0.1559 -0.0430 170 PHE A CG 1107 C CD1 . PHE A 170 ? 0.8960 1.0525 1.0615 0.0512 -0.1567 -0.0463 170 PHE A CD1 1108 C CD2 . PHE A 170 ? 0.8153 1.0328 0.9857 0.0553 -0.1534 -0.0495 170 PHE A CD2 1109 C CE1 . PHE A 170 ? 0.8857 1.0253 1.0531 0.0592 -0.1553 -0.0551 170 PHE A CE1 1110 C CE2 . PHE A 170 ? 0.7659 0.9652 0.9371 0.0642 -0.1529 -0.0602 170 PHE A CE2 1111 C CZ . PHE A 170 ? 0.7947 0.9548 0.9655 0.0654 -0.1539 -0.0627 170 PHE A CZ 1112 N N . ALA A 171 ? 0.6100 0.8901 0.7980 0.0450 -0.1635 -0.0312 171 ALA A N 1113 C CA . ALA A 171 ? 0.6498 0.9541 0.8433 0.0354 -0.1665 -0.0216 171 ALA A CA 1114 C C . ALA A 171 ? 0.8658 1.1380 1.0550 0.0309 -0.1718 -0.0191 171 ALA A C 1115 O O . ALA A 171 ? 1.0081 1.2545 1.1939 0.0416 -0.1724 -0.0271 171 ALA A O 1116 C CB . ALA A 171 ? 0.6367 0.9835 0.8404 0.0472 -0.1658 -0.0279 171 ALA A CB 1117 N N . GLY A 172 ? 0.8755 1.1500 1.0656 0.0154 -0.1764 -0.0077 172 GLY A N 1118 C CA . GLY A 172 ? 1.0257 1.2729 1.2112 0.0117 -0.1828 -0.0062 172 GLY A CA 1119 C C . GLY A 172 ? 1.1188 1.3229 1.2919 0.0060 -0.1845 -0.0043 172 GLY A C 1120 O O . GLY A 172 ? 1.2437 1.4245 1.4110 0.0033 -0.1903 -0.0032 172 GLY A O 1121 N N . LEU A 173 ? 0.9787 1.1736 1.1475 0.0057 -0.1797 -0.0048 173 LEU A N 1122 C CA . LEU A 173 ? 0.8854 1.0435 1.0430 -0.0001 -0.1811 -0.0026 173 LEU A CA 1123 C C . LEU A 173 ? 0.8769 1.0409 1.0359 -0.0170 -0.1851 0.0088 173 LEU A C 1124 O O . LEU A 173 ? 1.0235 1.2148 1.1887 -0.0212 -0.1816 0.0138 173 LEU A O 1125 C CB . LEU A 173 ? 0.8908 1.0348 1.0441 0.0089 -0.1745 -0.0094 173 LEU A CB 1126 C CG . LEU A 173 ? 0.9315 1.0650 1.0856 0.0249 -0.1711 -0.0197 173 LEU A CG 1127 C CD1 . LEU A 173 ? 0.9465 1.0701 1.0998 0.0311 -0.1660 -0.0257 173 LEU A CD1 1128 C CD2 . LEU A 173 ? 0.9514 1.0549 1.0979 0.0275 -0.1742 -0.0195 173 LEU A CD2 1129 N N . THR A 174 ? 0.8201 0.9594 0.9739 -0.0261 -0.1931 0.0131 174 THR A N 1130 C CA . THR A 174 ? 0.8779 1.0182 1.0348 -0.0429 -0.1993 0.0245 174 THR A CA 1131 C C . THR A 174 ? 0.9115 1.0154 1.0564 -0.0455 -0.2013 0.0244 174 THR A C 1132 O O . THR A 174 ? 0.9727 1.0778 1.1188 -0.0555 -0.2026 0.0326 174 THR A O 1133 C CB . THR A 174 ? 0.8985 1.0447 1.0636 -0.0541 -0.2104 0.0308 174 THR A CB 1134 O OG1 . THR A 174 ? 0.8814 0.9937 1.0365 -0.0505 -0.2179 0.0244 174 THR A OG1 1135 C CG2 . THR A 174 ? 0.8350 1.0193 1.0123 -0.0507 -0.2083 0.0305 174 THR A CG2 1136 N N . SER A 175 ? 0.9197 0.9930 1.0531 -0.0358 -0.2015 0.0156 175 SER A N 1137 C CA . SER A 175 ? 0.8492 0.8895 0.9709 -0.0361 -0.2032 0.0142 175 SER A CA 1138 C C . SER A 175 ? 0.7511 0.7745 0.8641 -0.0209 -0.1954 0.0046 175 SER A C 1139 O O . SER A 175 ? 0.8570 0.8846 0.9711 -0.0114 -0.1927 -0.0004 175 SER A O 1140 C CB . SER A 175 ? 0.8545 0.8717 0.9713 -0.0430 -0.2160 0.0157 175 SER A CB 1141 O OG . SER A 175 ? 0.9622 0.9475 1.0665 -0.0408 -0.2183 0.0125 175 SER A OG 1142 N N . LEU A 176 ? 0.5633 0.5689 0.6693 -0.0191 -0.1921 0.0030 176 LEU A N 1143 C CA . LEU A 176 ? 0.5738 0.5625 0.6736 -0.0065 -0.1855 -0.0043 176 LEU A CA 1144 C C . LEU A 176 ? 0.6876 0.6510 0.7773 -0.0079 -0.1869 -0.0046 176 LEU A C 1145 O O . LEU A 176 ? 0.7521 0.7161 0.8420 -0.0168 -0.1897 0.0000 176 LEU A O 1146 C CB . LEU A 176 ? 0.5558 0.5618 0.6638 0.0008 -0.1763 -0.0084 176 LEU A CB 1147 C CG . LEU A 176 ? 0.6601 0.6856 0.7769 0.0083 -0.1738 -0.0117 176 LEU A CG 1148 C CD1 . LEU A 176 ? 0.7383 0.7826 0.8641 0.0149 -0.1674 -0.0168 176 LEU A CD1 1149 C CD2 . LEU A 176 ? 0.6241 0.6318 0.7367 0.0179 -0.1734 -0.0149 176 LEU A CD2 1150 N N . ASN A 177 ? 0.6626 0.6053 0.7440 0.0012 -0.1851 -0.0091 177 ASN A N 1151 C CA . ASN A 177 ? 0.6223 0.5425 0.6939 0.0021 -0.1861 -0.0105 177 ASN A CA 1152 C C . ASN A 177 ? 0.7013 0.6248 0.7773 0.0055 -0.1775 -0.0126 177 ASN A C 1153 O O . ASN A 177 ? 0.9166 0.8346 0.9901 0.0011 -0.1783 -0.0115 177 ASN A O 1154 C CB . ASN A 177 ? 0.8901 0.7922 0.9515 0.0121 -0.1863 -0.0141 177 ASN A CB 1155 C CG . ASN A 177 ? 0.9646 0.8604 1.0190 0.0109 -0.1966 -0.0142 177 ASN A CG 1156 O OD1 . ASN A 177 ? 0.8397 0.7221 0.8833 0.0195 -0.1985 -0.0173 177 ASN A OD1 1157 N ND2 . ASN A 177 ? 0.8511 0.7588 0.9122 0.0008 -0.2036 -0.0108 177 ASN A ND2 1158 N N . GLU A 178 ? 0.6144 0.5461 0.6977 0.0137 -0.1702 -0.0159 178 GLU A N 1159 C CA . GLU A 178 ? 0.5709 0.5054 0.6610 0.0184 -0.1631 -0.0196 178 GLU A CA 1160 C C . GLU A 178 ? 0.6261 0.5828 0.7288 0.0217 -0.1597 -0.0224 178 GLU A C 1161 O O . GLU A 178 ? 0.6636 0.6236 0.7703 0.0271 -0.1590 -0.0231 178 GLU A O 1162 C CB . GLU A 178 ? 0.7422 0.6596 0.8304 0.0270 -0.1587 -0.0218 178 GLU A CB 1163 C CG . GLU A 178 ? 1.0359 0.9339 1.1123 0.0265 -0.1608 -0.0211 178 GLU A CG 1164 C CD . GLU A 178 ? 1.3805 1.2701 1.4605 0.0334 -0.1543 -0.0234 178 GLU A CD 1165 O OE1 . GLU A 178 ? 1.4359 1.3141 1.5096 0.0390 -0.1530 -0.0220 178 GLU A OE1 1166 O OE2 . GLU A 178 ? 1.4404 1.3369 1.5304 0.0335 -0.1507 -0.0266 178 GLU A OE2 1167 N N . LEU A 179 ? 0.7018 0.6752 0.8101 0.0195 -0.1582 -0.0240 179 LEU A N 1168 C CA . LEU A 179 ? 0.5101 0.5052 0.6303 0.0257 -0.1552 -0.0295 179 LEU A CA 1169 C C . LEU A 179 ? 0.5068 0.4976 0.6319 0.0313 -0.1516 -0.0362 179 LEU A C 1170 O O . LEU A 179 ? 0.5705 0.5558 0.6899 0.0271 -0.1517 -0.0349 179 LEU A O 1171 C CB . LEU A 179 ? 0.4869 0.5108 0.6096 0.0199 -0.1569 -0.0263 179 LEU A CB 1172 C CG . LEU A 179 ? 0.5394 0.5906 0.6733 0.0281 -0.1544 -0.0333 179 LEU A CG 1173 C CD1 . LEU A 179 ? 0.4462 0.4922 0.5873 0.0378 -0.1540 -0.0389 179 LEU A CD1 1174 C CD2 . LEU A 179 ? 0.6458 0.7292 0.7817 0.0222 -0.1558 -0.0278 179 LEU A CD2 1175 N N . GLU A 180 ? 0.5607 0.5523 0.6970 0.0407 -0.1495 -0.0432 180 GLU A N 1176 C CA . GLU A 180 ? 0.6668 0.6546 0.8109 0.0463 -0.1476 -0.0509 180 GLU A CA 1177 C C . GLU A 180 ? 0.8095 0.8158 0.9675 0.0557 -0.1484 -0.0610 180 GLU A C 1178 O O . GLU A 180 ? 0.9250 0.9251 1.0934 0.0626 -0.1491 -0.0644 180 GLU A O 1179 C CB . GLU A 180 ? 0.4315 0.3934 0.5778 0.0488 -0.1456 -0.0499 180 GLU A CB 1180 C CG . GLU A 180 ? 0.6765 0.6351 0.8345 0.0541 -0.1448 -0.0581 180 GLU A CG 1181 C CD . GLU A 180 ? 0.7766 0.7131 0.9396 0.0556 -0.1424 -0.0553 180 GLU A CD 1182 O OE1 . GLU A 180 ? 0.8635 0.7885 1.0190 0.0537 -0.1409 -0.0469 180 GLU A OE1 1183 O OE2 . GLU A 180 ? 0.6459 0.5784 0.8209 0.0590 -0.1424 -0.0613 180 GLU A OE2 1184 N N . ILE A 181 ? 0.6842 0.7139 0.8420 0.0566 -0.1489 -0.0655 181 ILE A N 1185 C CA . ILE A 181 ? 0.5678 0.6181 0.7374 0.0675 -0.1507 -0.0773 181 ILE A CA 1186 C C . ILE A 181 ? 0.5987 0.6412 0.7770 0.0743 -0.1518 -0.0881 181 ILE A C 1187 O O . ILE A 181 ? 0.5867 0.6339 0.7592 0.0719 -0.1511 -0.0888 181 ILE A O 1188 C CB . ILE A 181 ? 0.4487 0.5348 0.6138 0.0668 -0.1506 -0.0767 181 ILE A CB 1189 C CG1 . ILE A 181 ? 0.4162 0.5116 0.5769 0.0603 -0.1506 -0.0669 181 ILE A CG1 1190 C CG2 . ILE A 181 ? 0.3381 0.4480 0.5139 0.0808 -0.1530 -0.0915 181 ILE A CG2 1191 C CD1 . ILE A 181 ? 0.3965 0.5227 0.5513 0.0537 -0.1498 -0.0595 181 ILE A CD1 1192 N N . LYS A 182 ? 0.6456 0.6754 0.8389 0.0824 -0.1545 -0.0958 182 LYS A N 1193 C CA . LYS A 182 ? 0.7634 0.7869 0.9690 0.0893 -0.1575 -0.1075 182 LYS A CA 1194 C C . LYS A 182 ? 0.8757 0.9231 1.0913 0.1024 -0.1629 -0.1234 182 LYS A C 1195 O O . LYS A 182 ? 0.9160 0.9593 1.1460 0.1109 -0.1677 -0.1309 182 LYS A O 1196 C CB . LYS A 182 ? 0.6675 0.6614 0.8865 0.0896 -0.1583 -0.1057 182 LYS A CB 1197 C CG . LYS A 182 ? 0.7200 0.7082 0.9579 0.0976 -0.1638 -0.1192 182 LYS A CG 1198 C CD . LYS A 182 ? 0.7934 0.7579 1.0369 0.0919 -0.1618 -0.1139 182 LYS A CD 1199 C CE . LYS A 182 ? 0.7638 0.7066 1.0127 0.0876 -0.1591 -0.1011 182 LYS A CE 1200 N NZ . LYS A 182 ? 0.6379 0.5622 0.8962 0.0837 -0.1575 -0.0969 182 LYS A NZ 1201 N N . ALA A 183 ? 0.8172 0.8901 1.0250 0.1047 -0.1626 -0.1284 183 ALA A N 1202 C CA . ALA A 183 ? 0.8014 0.9044 1.0147 0.1184 -0.1672 -0.1430 183 ALA A CA 1203 C C . ALA A 183 ? 0.8537 0.9662 1.0707 0.1271 -0.1712 -0.1573 183 ALA A C 1204 O O . ALA A 183 ? 0.9695 1.1152 1.1791 0.1337 -0.1712 -0.1629 183 ALA A O 1205 C CB . ALA A 183 ? 0.6604 0.7970 0.8608 0.1159 -0.1633 -0.1355 183 ALA A CB 1206 N N . LEU A 184 ? 0.6637 0.7490 0.8927 0.1275 -0.1747 -0.1630 184 LEU A N 1207 C CA . LEU A 184 ? 0.6646 0.7561 0.8989 0.1357 -0.1796 -0.1775 184 LEU A CA 1208 C C . LEU A 184 ? 0.7662 0.8876 1.0065 0.1536 -0.1871 -0.1972 184 LEU A C 1209 O O . LEU A 184 ? 0.9386 1.0816 1.1737 0.1612 -0.1891 -0.2069 184 LEU A O 1210 C CB . LEU A 184 ? 0.6095 0.6674 0.8617 0.1342 -0.1840 -0.1816 184 LEU A CB 1211 C CG . LEU A 184 ? 0.6972 0.7297 0.9423 0.1186 -0.1764 -0.1633 184 LEU A CG 1212 C CD1 . LEU A 184 ? 0.6458 0.6469 0.9111 0.1161 -0.1791 -0.1617 184 LEU A CD1 1213 C CD2 . LEU A 184 ? 0.5456 0.5825 0.7779 0.1139 -0.1733 -0.1608 184 LEU A CD2 1214 N N . SER A 185 ? 0.7384 0.8622 0.9889 0.1616 -0.1916 -0.2036 185 SER A N 1215 C CA . SER A 185 ? 0.5672 0.7172 0.8253 0.1811 -0.2005 -0.2250 185 SER A CA 1216 C C . SER A 185 ? 0.5760 0.7661 0.8201 0.1856 -0.1959 -0.2217 185 SER A C 1217 O O . SER A 185 ? 0.6816 0.8932 0.9322 0.2017 -0.2025 -0.2369 185 SER A O 1218 C CB . SER A 185 ? 0.6287 0.7554 0.9105 0.1899 -0.2111 -0.2370 185 SER A CB 1219 O OG . SER A 185 ? 0.6761 0.7669 0.9744 0.1846 -0.2155 -0.2381 185 SER A OG 1220 N N . LEU A 186 ? 0.6692 0.8698 0.8954 0.1714 -0.1854 -0.2018 186 LEU A N 1221 C CA . LEU A 186 ? 0.7545 0.9945 0.9689 0.1724 -0.1802 -0.1946 186 LEU A CA 1222 C C . LEU A 186 ? 1.0218 1.3073 1.2335 0.1910 -0.1839 -0.2109 186 LEU A C 1223 O O . LEU A 186 ? 1.1266 1.4322 1.3275 0.1912 -0.1810 -0.2093 186 LEU A O 1224 C CB . LEU A 186 ? 0.7351 0.9776 0.9326 0.1535 -0.1702 -0.1711 186 LEU A CB 1225 C CG . LEU A 186 ? 0.7724 1.0560 0.9593 0.1506 -0.1645 -0.1594 186 LEU A CG 1226 C CD1 . LEU A 186 ? 0.7131 1.0056 0.9082 0.1574 -0.1668 -0.1636 186 LEU A CD1 1227 C CD2 . LEU A 186 ? 0.7974 1.0715 0.9719 0.1295 -0.1571 -0.1352 186 LEU A CD2 1228 N N . ARG A 187 ? 1.1029 1.4059 1.3239 0.2077 -0.1905 -0.2265 187 ARG A N 1229 C CA . ARG A 187 ? 1.0556 1.4051 1.2741 0.2286 -0.1949 -0.2444 187 ARG A CA 1230 C C . ARG A 187 ? 0.9572 1.3563 1.1612 0.2265 -0.1857 -0.2305 187 ARG A C 1231 O O . ARG A 187 ? 0.9828 1.4278 1.1788 0.2394 -0.1851 -0.2374 187 ARG A O 1232 C CB . ARG A 187 ? 1.0295 1.3771 1.2652 0.2501 -0.2080 -0.2698 187 ARG A CB 1233 C CG . ARG A 187 ? 1.1485 1.4505 1.4026 0.2535 -0.2193 -0.2848 187 ARG A CG 1234 C CD . ARG A 187 ? 1.3362 1.6352 1.6094 0.2754 -0.2346 -0.3107 187 ARG A CD 1235 N NE . ARG A 187 ? 1.4982 1.8297 1.7717 0.2987 -0.2442 -0.3365 187 ARG A NE 1236 C CZ . ARG A 187 ? 1.4068 1.7294 1.6987 0.3189 -0.2611 -0.3639 187 ARG A CZ 1237 N NH1 . ARG A 187 ? 1.4007 1.6816 1.7137 0.3176 -0.2703 -0.3675 187 ARG A NH1 1238 N NH2 . ARG A 187 ? 1.2621 1.6178 1.5517 0.3410 -0.2698 -0.3878 187 ARG A NH2 1239 N N . ASN A 188 ? 0.9064 1.2975 1.1074 0.2100 -0.1786 -0.2102 188 ASN A N 1240 C CA . ASN A 188 ? 0.9667 1.4032 1.1579 0.2058 -0.1706 -0.1952 188 ASN A CA 1241 C C . ASN A 188 ? 0.8775 1.2938 1.0650 0.1819 -0.1634 -0.1699 188 ASN A C 1242 O O . ASN A 188 ? 1.0335 1.4140 1.2284 0.1763 -0.1657 -0.1686 188 ASN A O 1243 C CB . ASN A 188 ? 1.1088 1.5813 1.3068 0.2257 -0.1752 -0.2104 188 ASN A CB 1244 C CG . ASN A 188 ? 1.1915 1.7228 1.3804 0.2254 -0.1673 -0.1976 188 ASN A CG 1245 O OD1 . ASN A 188 ? 1.1707 1.7046 1.3540 0.2051 -0.1590 -0.1731 188 ASN A OD1 1246 N ND2 . ASN A 188 ? 1.2411 1.8216 1.4297 0.2483 -0.1703 -0.2141 188 ASN A ND2 1247 N N . TYR A 189 ? 0.6892 1.1289 0.8654 0.1685 -0.1555 -0.1497 189 TYR A N 1248 C CA . TYR A 189 ? 0.6015 1.0249 0.7742 0.1461 -0.1501 -0.1262 189 TYR A CA 1249 C C . TYR A 189 ? 0.6683 1.1436 0.8379 0.1425 -0.1446 -0.1120 189 TYR A C 1250 O O . TYR A 189 ? 0.8216 1.3281 0.9834 0.1384 -0.1400 -0.1006 189 TYR A O 1251 C CB . TYR A 189 ? 0.6701 1.0617 0.8343 0.1292 -0.1474 -0.1127 189 TYR A CB 1252 C CG . TYR A 189 ? 0.7829 1.1667 0.9418 0.1068 -0.1428 -0.0877 189 TYR A CG 1253 C CD1 . TYR A 189 ? 0.7393 1.0765 0.8991 0.0939 -0.1440 -0.0811 189 TYR A CD1 1254 C CD2 . TYR A 189 ? 0.9180 1.3425 1.0720 0.0989 -0.1381 -0.0707 189 TYR A CD2 1255 C CE1 . TYR A 189 ? 0.8034 1.1331 0.9588 0.0749 -0.1420 -0.0607 189 TYR A CE1 1256 C CE2 . TYR A 189 ? 0.9172 1.3333 1.0691 0.0781 -0.1361 -0.0484 189 TYR A CE2 1257 C CZ . TYR A 189 ? 0.8043 1.1721 0.9567 0.0666 -0.1386 -0.0447 189 TYR A CZ 1258 O OH . TYR A 189 ? 0.6268 0.9862 0.7776 0.0472 -0.1385 -0.0246 189 TYR A OH 1259 N N . GLN A 190 ? 0.7395 1.2259 0.9162 0.1443 -0.1454 -0.1121 190 GLN A N 1260 C CA . GLN A 190 ? 0.7177 1.2526 0.8944 0.1390 -0.1404 -0.0971 190 GLN A CA 1261 C C . GLN A 190 ? 0.8131 1.3454 0.9837 0.1146 -0.1352 -0.0699 190 GLN A C 1262 O O . GLN A 190 ? 0.7480 1.2336 0.9165 0.0990 -0.1363 -0.0614 190 GLN A O 1263 C CB . GLN A 190 ? 0.6633 1.1980 0.8492 0.1410 -0.1428 -0.0997 190 GLN A CB 1264 C CG . GLN A 190 ? 0.8364 1.4177 1.0248 0.1326 -0.1381 -0.0824 190 GLN A CG 1265 C CD . GLN A 190 ? 0.9845 1.5783 1.1824 0.1424 -0.1413 -0.0912 190 GLN A CD 1266 O OE1 . GLN A 190 ? 1.0918 1.6686 1.2938 0.1599 -0.1472 -0.1124 190 GLN A OE1 1267 N NE2 . GLN A 190 ? 0.9453 1.5682 1.1478 0.1312 -0.1382 -0.0749 190 GLN A NE2 1268 N N . SER A 191 ? 1.0250 1.6092 1.1935 0.1120 -0.1300 -0.0561 191 SER A N 1269 C CA . SER A 191 ? 1.0840 1.6697 1.2491 0.0889 -0.1262 -0.0290 191 SER A CA 1270 C C . SER A 191 ? 0.9118 1.4742 1.0836 0.0701 -0.1280 -0.0151 191 SER A C 1271 O O . SER A 191 ? 0.7255 1.3072 0.9056 0.0740 -0.1287 -0.0177 191 SER A O 1272 C CB . SER A 191 ? 1.1952 1.8480 1.3595 0.0908 -0.1202 -0.0154 191 SER A CB 1273 O OG . SER A 191 ? 1.1863 1.8867 1.3543 0.1132 -0.1195 -0.0315 191 SER A OG 1274 N N . GLN A 192 ? 0.9071 1.4274 1.0750 0.0513 -0.1298 -0.0018 192 GLN A N 1275 C CA . GLN A 192 ? 0.8302 1.3294 1.0032 0.0316 -0.1327 0.0137 192 GLN A CA 1276 C C . GLN A 192 ? 0.8246 1.2794 0.9997 0.0337 -0.1374 0.0014 192 GLN A C 1277 O O . GLN A 192 ? 0.7183 1.1643 0.8988 0.0220 -0.1404 0.0103 192 GLN A O 1278 C CB . GLN A 192 ? 0.7460 1.2974 0.9291 0.0241 -0.1303 0.0300 192 GLN A CB 1279 C CG . GLN A 192 ? 0.8174 1.4119 0.9995 0.0177 -0.1255 0.0486 192 GLN A CG 1280 C CD . GLN A 192 ? 0.8874 1.5219 1.0820 0.0019 -0.1245 0.0719 192 GLN A CD 1281 O OE1 . GLN A 192 ? 0.8797 1.4951 1.0825 -0.0109 -0.1293 0.0779 192 GLN A OE1 1282 N NE2 . GLN A 192 ? 0.8638 1.5561 1.0606 0.0029 -0.1185 0.0858 192 GLN A NE2 1283 N N . SER A 193 ? 0.8757 1.3032 1.0473 0.0483 -0.1386 -0.0182 193 SER A N 1284 C CA . SER A 193 ? 0.7565 1.1415 0.9298 0.0507 -0.1426 -0.0281 193 SER A CA 1285 C C . SER A 193 ? 0.7528 1.0933 0.9213 0.0331 -0.1455 -0.0164 193 SER A C 1286 O O . SER A 193 ? 0.9435 1.2708 1.1152 0.0275 -0.1486 -0.0133 193 SER A O 1287 C CB . SER A 193 ? 0.7672 1.1312 0.9397 0.0680 -0.1438 -0.0488 193 SER A CB 1288 O OG . SER A 193 ? 0.7747 1.1797 0.9515 0.0859 -0.1430 -0.0616 193 SER A OG 1289 N N . LEU A 194 ? 0.6211 0.9397 0.7818 0.0256 -0.1452 -0.0109 194 LEU A N 1290 C CA . LEU A 194 ? 0.5513 0.8274 0.7064 0.0111 -0.1489 -0.0018 194 LEU A CA 1291 C C . LEU A 194 ? 0.7854 1.0710 0.9424 -0.0078 -0.1518 0.0182 194 LEU A C 1292 O O . LEU A 194 ? 0.9100 1.1609 1.0628 -0.0193 -0.1568 0.0249 194 LEU A O 1293 C CB . LEU A 194 ? 0.5550 0.8018 0.7012 0.0111 -0.1485 -0.0045 194 LEU A CB 1294 C CG . LEU A 194 ? 0.5973 0.8152 0.7416 0.0239 -0.1479 -0.0211 194 LEU A CG 1295 C CD1 . LEU A 194 ? 0.8376 1.0267 0.9842 0.0259 -0.1503 -0.0263 194 LEU A CD1 1296 C CD2 . LEU A 194 ? 0.5466 0.7938 0.6959 0.0404 -0.1454 -0.0349 194 LEU A CD2 1297 N N . LYS A 195 ? 0.8069 1.1396 0.9711 -0.0110 -0.1496 0.0281 195 LYS A N 1298 C CA . LYS A 195 ? 0.8643 1.2077 1.0330 -0.0306 -0.1529 0.0496 195 LYS A CA 1299 C C . LYS A 195 ? 0.9426 1.2777 1.1193 -0.0411 -0.1591 0.0553 195 LYS A C 1300 O O . LYS A 195 ? 1.0070 1.3291 1.1865 -0.0584 -0.1655 0.0701 195 LYS A O 1301 C CB . LYS A 195 ? 0.7977 1.1973 0.9723 -0.0321 -0.1479 0.0620 195 LYS A CB 1302 C CG . LYS A 195 ? 0.8695 1.2763 1.0495 -0.0538 -0.1515 0.0871 195 LYS A CG 1303 C CD . LYS A 195 ? 0.9910 1.4613 1.1814 -0.0568 -0.1465 0.1026 195 LYS A CD 1304 C CE . LYS A 195 ? 0.9763 1.4535 1.1716 -0.0777 -0.1495 0.1296 195 LYS A CE 1305 N NZ . LYS A 195 ? 0.9247 1.3673 1.1280 -0.0974 -0.1602 0.1404 195 LYS A NZ 1306 N N . SER A 196 ? 0.8623 1.2040 1.0429 -0.0302 -0.1585 0.0433 196 SER A N 1307 C CA . SER A 196 ? 0.9097 1.2465 1.0976 -0.0379 -0.1646 0.0470 196 SER A CA 1308 C C . SER A 196 ? 0.9542 1.2372 1.1343 -0.0444 -0.1718 0.0453 196 SER A C 1309 O O . SER A 196 ? 0.9126 1.1865 1.0976 -0.0568 -0.1795 0.0534 196 SER A O 1310 C CB . SER A 196 ? 0.8914 1.2474 1.0841 -0.0225 -0.1623 0.0337 196 SER A CB 1311 O OG . SER A 196 ? 0.9452 1.2882 1.1310 -0.0045 -0.1581 0.0165 196 SER A OG 1312 N N . ILE A 197 ? 0.8900 1.1392 1.0587 -0.0353 -0.1697 0.0343 197 ILE A N 1313 C CA . ILE A 197 ? 0.7766 0.9776 0.9362 -0.0388 -0.1754 0.0319 197 ILE A CA 1314 C C . ILE A 197 ? 0.7201 0.9066 0.8781 -0.0556 -0.1819 0.0457 197 ILE A C 1315 O O . ILE A 197 ? 0.7817 0.9704 0.9365 -0.0585 -0.1794 0.0509 197 ILE A O 1316 C CB . ILE A 197 ? 0.6799 0.8533 0.8296 -0.0257 -0.1708 0.0188 197 ILE A CB 1317 C CG1 . ILE A 197 ? 0.5903 0.7762 0.7438 -0.0092 -0.1659 0.0055 197 ILE A CG1 1318 C CG2 . ILE A 197 ? 0.6173 0.7457 0.7575 -0.0279 -0.1760 0.0166 197 ILE A CG2 1319 C CD1 . ILE A 197 ? 0.5560 0.7163 0.7038 0.0029 -0.1622 -0.0065 197 ILE A CD1 1320 N N . ARG A 198 ? 0.7468 0.9175 0.9075 -0.0660 -0.1913 0.0509 198 ARG A N 1321 C CA . ARG A 198 ? 0.9186 1.0767 1.0818 -0.0831 -0.2006 0.0647 198 ARG A CA 1322 C C . ARG A 198 ? 0.8592 0.9749 1.0091 -0.0830 -0.2039 0.0616 198 ARG A C 1323 O O . ARG A 198 ? 0.8088 0.9194 0.9592 -0.0936 -0.2078 0.0727 198 ARG A O 1324 C CB . ARG A 198 ? 1.0491 1.2035 1.2210 -0.0931 -0.2117 0.0689 198 ARG A CB 1325 C CG . ARG A 198 ? 1.3115 1.4583 1.4917 -0.1128 -0.2234 0.0848 198 ARG A CG 1326 C CD . ARG A 198 ? 1.5510 1.7093 1.7464 -0.1240 -0.2339 0.0910 198 ARG A CD 1327 N NE . ARG A 198 ? 1.7427 1.8618 1.9320 -0.1233 -0.2463 0.0818 198 ARG A NE 1328 C CZ . ARG A 198 ? 1.8128 1.8968 1.9991 -0.1317 -0.2587 0.0843 198 ARG A CZ 1329 N NH1 . ARG A 198 ? 1.7960 1.8768 1.9849 -0.1422 -0.2602 0.0968 198 ARG A NH1 1330 N NH2 . ARG A 198 ? 1.8098 1.8621 1.9897 -0.1284 -0.2702 0.0738 198 ARG A NH2 1331 N N . ASP A 199 ? 0.7817 0.8685 0.9203 -0.0707 -0.2026 0.0475 199 ASP A N 1332 C CA . ASP A 199 ? 0.8179 0.8656 0.9439 -0.0690 -0.2061 0.0433 199 ASP A CA 1333 C C . ASP A 199 ? 0.8201 0.8545 0.9366 -0.0524 -0.1974 0.0294 199 ASP A C 1334 O O . ASP A 199 ? 0.8329 0.8675 0.9494 -0.0434 -0.1951 0.0215 199 ASP A O 1335 C CB . ASP A 199 ? 0.9856 1.0054 1.1091 -0.0750 -0.2193 0.0432 199 ASP A CB 1336 C CG . ASP A 199 ? 1.1420 1.1238 1.2533 -0.0744 -0.2253 0.0402 199 ASP A CG 1337 O OD1 . ASP A 199 ? 1.0572 1.0137 1.1636 -0.0748 -0.2361 0.0361 199 ASP A OD1 1338 O OD2 . ASP A 199 ? 1.1608 1.1393 1.2672 -0.0724 -0.2198 0.0411 199 ASP A OD2 1339 N N . ILE A 200 ? 0.7458 0.7694 0.8557 -0.0487 -0.1931 0.0272 200 ILE A N 1340 C CA . ILE A 200 ? 0.6642 0.6729 0.7672 -0.0347 -0.1859 0.0153 200 ILE A CA 1341 C C . ILE A 200 ? 0.6813 0.6585 0.7735 -0.0344 -0.1889 0.0136 200 ILE A C 1342 O O . ILE A 200 ? 0.7164 0.6942 0.8073 -0.0395 -0.1895 0.0188 200 ILE A O 1343 C CB . ILE A 200 ? 0.6408 0.6737 0.7489 -0.0272 -0.1764 0.0113 200 ILE A CB 1344 C CG1 . ILE A 200 ? 0.7137 0.7784 0.8321 -0.0240 -0.1734 0.0102 200 ILE A CG1 1345 C CG2 . ILE A 200 ? 0.5704 0.5843 0.6740 -0.0151 -0.1710 0.0003 200 ILE A CG2 1346 C CD1 . ILE A 200 ? 0.6767 0.7710 0.8009 -0.0160 -0.1660 0.0056 200 ILE A CD1 1347 N N . HIS A 201 ? 0.6822 0.6340 0.7664 -0.0276 -0.1907 0.0068 201 HIS A N 1348 C CA . HIS A 201 ? 0.6527 0.5761 0.7264 -0.0273 -0.1952 0.0054 201 HIS A CA 1349 C C . HIS A 201 ? 0.7748 0.6951 0.8462 -0.0205 -0.1875 0.0010 201 HIS A C 1350 O O . HIS A 201 ? 0.8160 0.7225 0.8814 -0.0229 -0.1906 0.0026 201 HIS A O 1351 C CB . HIS A 201 ? 0.7733 0.6738 0.8380 -0.0211 -0.2002 -0.0002 201 HIS A CB 1352 C CG . HIS A 201 ? 1.0346 0.9337 1.1006 -0.0283 -0.2111 0.0031 201 HIS A CG 1353 N ND1 . HIS A 201 ? 1.0751 0.9649 1.1356 -0.0216 -0.2149 -0.0023 201 HIS A ND1 1354 C CD2 . HIS A 201 ? 1.1083 1.0160 1.1819 -0.0417 -0.2195 0.0117 201 HIS A CD2 1355 C CE1 . HIS A 201 ? 1.1372 1.0285 1.2017 -0.0301 -0.2259 0.0011 201 HIS A CE1 1356 N NE2 . HIS A 201 ? 1.1667 1.0685 1.2402 -0.0432 -0.2290 0.0101 201 HIS A NE2 1357 N N . HIS A 202 ? 0.7402 0.6732 0.8173 -0.0118 -0.1783 -0.0048 202 HIS A N 1358 C CA . HIS A 202 ? 0.6365 0.5675 0.7143 -0.0048 -0.1716 -0.0103 202 HIS A CA 1359 C C . HIS A 202 ? 0.6635 0.6162 0.7523 0.0019 -0.1644 -0.0154 202 HIS A C 1360 O O . HIS A 202 ? 0.6718 0.6231 0.7649 0.0089 -0.1614 -0.0197 202 HIS A O 1361 C CB . HIS A 202 ? 0.6104 0.5157 0.6804 0.0022 -0.1712 -0.0151 202 HIS A CB 1362 C CG . HIS A 202 ? 0.6636 0.5668 0.7372 0.0097 -0.1644 -0.0211 202 HIS A CG 1363 N ND1 . HIS A 202 ? 0.7333 0.6221 0.8054 0.0176 -0.1610 -0.0249 202 HIS A ND1 1364 C CD2 . HIS A 202 ? 0.8339 0.7488 0.9133 0.0108 -0.1607 -0.0237 202 HIS A CD2 1365 C CE1 . HIS A 202 ? 0.7606 0.6513 0.8393 0.0220 -0.1559 -0.0293 202 HIS A CE1 1366 N NE2 . HIS A 202 ? 0.7802 0.6860 0.8630 0.0185 -0.1561 -0.0298 202 HIS A NE2 1367 N N . LEU A 203 ? 0.7072 0.6810 0.8007 0.0003 -0.1623 -0.0147 203 LEU A N 1368 C CA . LEU A 203 ? 0.5766 0.5726 0.6802 0.0082 -0.1570 -0.0215 203 LEU A CA 1369 C C . LEU A 203 ? 0.6843 0.6739 0.7899 0.0155 -0.1536 -0.0296 203 LEU A C 1370 O O . LEU A 203 ? 0.6987 0.6875 0.7993 0.0128 -0.1543 -0.0278 203 LEU A O 1371 C CB . LEU A 203 ? 0.4712 0.4993 0.5781 0.0035 -0.1573 -0.0163 203 LEU A CB 1372 C CG . LEU A 203 ? 0.6103 0.6660 0.7261 0.0131 -0.1529 -0.0247 203 LEU A CG 1373 C CD1 . LEU A 203 ? 0.7322 0.7911 0.8562 0.0208 -0.1518 -0.0316 203 LEU A CD1 1374 C CD2 . LEU A 203 ? 0.6570 0.7475 0.7737 0.0084 -0.1528 -0.0172 203 LEU A CD2 1375 N N . THR A 204 ? 0.7487 0.7334 0.8627 0.0246 -0.1505 -0.0380 204 THR A N 1376 C CA . THR A 204 ? 0.6938 0.6745 0.8141 0.0319 -0.1482 -0.0467 204 THR A CA 1377 C C . THR A 204 ? 0.7046 0.7094 0.8366 0.0399 -0.1474 -0.0557 204 THR A C 1378 O O . THR A 204 ? 0.7264 0.7344 0.8670 0.0450 -0.1472 -0.0592 204 THR A O 1379 C CB . THR A 204 ? 0.6316 0.5883 0.7558 0.0361 -0.1464 -0.0489 204 THR A CB 1380 O OG1 . THR A 204 ? 0.6815 0.6190 0.7934 0.0308 -0.1476 -0.0421 204 THR A OG1 1381 C CG2 . THR A 204 ? 0.5826 0.5356 0.7166 0.0424 -0.1448 -0.0574 204 THR A CG2 1382 N N . LEU A 205 ? 0.7226 0.7449 0.8542 0.0419 -0.1475 -0.0595 205 LEU A N 1383 C CA . LEU A 205 ? 0.6557 0.7030 0.7970 0.0520 -0.1478 -0.0705 205 LEU A CA 1384 C C . LEU A 205 ? 0.6843 0.7235 0.8348 0.0606 -0.1487 -0.0830 205 LEU A C 1385 O O . LEU A 205 ? 0.7381 0.7671 0.8837 0.0582 -0.1485 -0.0822 205 LEU A O 1386 C CB . LEU A 205 ? 0.6369 0.7151 0.7713 0.0500 -0.1476 -0.0665 205 LEU A CB 1387 C CG . LEU A 205 ? 0.6408 0.7454 0.7745 0.0469 -0.1472 -0.0596 205 LEU A CG 1388 C CD1 . LEU A 205 ? 0.6012 0.7410 0.7304 0.0473 -0.1462 -0.0562 205 LEU A CD1 1389 C CD2 . LEU A 205 ? 0.6642 0.7762 0.8095 0.0574 -0.1478 -0.0704 205 LEU A CD2 1390 N N . HIS A 206 ? 0.7304 0.7737 0.8955 0.0708 -0.1508 -0.0948 206 HIS A N 1391 C CA . HIS A 206 ? 0.6793 0.7202 0.8560 0.0798 -0.1538 -0.1087 206 HIS A CA 1392 C C . HIS A 206 ? 0.6495 0.7225 0.8300 0.0910 -0.1570 -0.1211 206 HIS A C 1393 O O . HIS A 206 ? 0.5759 0.6588 0.7657 0.0987 -0.1596 -0.1282 206 HIS A O 1394 C CB . HIS A 206 ? 0.7602 0.7789 0.9544 0.0839 -0.1560 -0.1141 206 HIS A CB 1395 C CG . HIS A 206 ? 0.7978 0.7899 0.9891 0.0753 -0.1524 -0.1016 206 HIS A CG 1396 N ND1 . HIS A 206 ? 0.7172 0.6871 0.9184 0.0747 -0.1522 -0.1016 206 HIS A ND1 1397 C CD2 . HIS A 206 ? 0.8333 0.8198 1.0133 0.0680 -0.1493 -0.0892 206 HIS A CD2 1398 C CE1 . HIS A 206 ? 0.6667 0.6202 0.8614 0.0682 -0.1484 -0.0894 206 HIS A CE1 1399 N NE2 . HIS A 206 ? 0.7330 0.6951 0.9145 0.0644 -0.1471 -0.0825 206 HIS A NE2 1400 N N . LEU A 207 ? 0.7302 0.8207 0.9030 0.0931 -0.1571 -0.1238 207 LEU A N 1401 C CA . LEU A 207 ? 0.6658 0.7889 0.8415 0.1064 -0.1605 -0.1374 207 LEU A CA 1402 C C . LEU A 207 ? 0.7852 0.9025 0.9676 0.1140 -0.1649 -0.1510 207 LEU A C 1403 O O . LEU A 207 ? 0.7224 0.8240 0.8987 0.1068 -0.1631 -0.1448 207 LEU A O 1404 C CB . LEU A 207 ? 0.5091 0.6655 0.6690 0.1033 -0.1567 -0.1273 207 LEU A CB 1405 C CG . LEU A 207 ? 0.5730 0.7391 0.7268 0.0941 -0.1529 -0.1124 207 LEU A CG 1406 C CD1 . LEU A 207 ? 0.6156 0.8072 0.7552 0.0866 -0.1493 -0.0979 207 LEU A CD1 1407 C CD2 . LEU A 207 ? 0.4278 0.6149 0.5910 0.1046 -0.1549 -0.1217 207 LEU A CD2 1408 N N . SER A 208 ? 0.7715 0.9014 0.9669 0.1291 -0.1718 -0.1704 208 SER A N 1409 C CA . SER A 208 ? 0.6600 0.7864 0.8643 0.1378 -0.1780 -0.1860 208 SER A CA 1410 C C . SER A 208 ? 0.7151 0.8730 0.9051 0.1441 -0.1777 -0.1893 208 SER A C 1411 O O . SER A 208 ? 0.8243 0.9788 1.0170 0.1486 -0.1816 -0.1984 208 SER A O 1412 C CB . SER A 208 ? 0.6867 0.8104 0.9129 0.1520 -0.1879 -0.2069 208 SER A CB 1413 O OG . SER A 208 ? 0.7053 0.8632 0.9294 0.1657 -0.1911 -0.2178 208 SER A OG 1414 N N . GLU A 209 ? 0.6005 0.7908 0.7762 0.1444 -0.1731 -0.1808 209 GLU A N 1415 C CA . GLU A 209 ? 0.6538 0.8800 0.8155 0.1510 -0.1720 -0.1811 209 GLU A CA 1416 C C . GLU A 209 ? 0.6622 0.9159 0.8081 0.1429 -0.1644 -0.1613 209 GLU A C 1417 O O . GLU A 209 ? 0.8024 1.0517 0.9499 0.1352 -0.1613 -0.1517 209 GLU A O 1418 C CB . GLU A 209 ? 0.8765 1.1300 1.0461 0.1727 -0.1802 -0.2058 209 GLU A CB 1419 C CG . GLU A 209 ? 0.9369 1.1865 1.1233 0.1820 -0.1860 -0.2199 209 GLU A CG 1420 C CD . GLU A 209 ? 1.0453 1.3323 1.2244 0.1871 -0.1825 -0.2158 209 GLU A CD 1421 O OE1 . GLU A 209 ? 1.1001 1.3856 1.2912 0.1945 -0.1868 -0.2256 209 GLU A OE1 1422 O OE2 . GLU A 209 ? 1.0125 1.3310 1.1748 0.1836 -0.1756 -0.2021 209 GLU A OE2 1423 N N . SER A 210 ? 0.6832 0.9668 0.8151 0.1448 -0.1619 -0.1549 210 SER A N 1424 C CA . SER A 210 ? 0.7015 1.0054 0.8192 0.1326 -0.1548 -0.1307 210 SER A CA 1425 C C . SER A 210 ? 0.7589 1.1067 0.8751 0.1377 -0.1517 -0.1268 210 SER A C 1426 O O . SER A 210 ? 0.6478 1.0119 0.7560 0.1254 -0.1462 -0.1050 210 SER A O 1427 C CB . SER A 210 ? 0.8434 1.1618 0.9474 0.1322 -0.1535 -0.1228 210 SER A CB 1428 O OG . SER A 210 ? 0.9945 1.3526 1.0962 0.1518 -0.1563 -0.1383 210 SER A OG 1429 N N . ALA A 211 ? 0.7878 1.1549 0.9130 0.1558 -0.1562 -0.1479 211 ALA A N 1430 C CA . ALA A 211 ? 0.7578 1.1742 0.8815 0.1658 -0.1541 -0.1485 211 ALA A CA 1431 C C . ALA A 211 ? 0.8812 1.3048 1.0039 0.1506 -0.1479 -0.1271 211 ALA A C 1432 O O . ALA A 211 ? 0.9067 1.3771 1.0247 0.1535 -0.1436 -0.1184 211 ALA A O 1433 C CB . ALA A 211 ? 0.6832 1.1070 0.8195 0.1869 -0.1619 -0.1764 211 ALA A CB 1434 N N . PHE A 212 ? 0.8219 1.2019 0.9495 0.1351 -0.1475 -0.1188 212 PHE A N 1435 C CA . PHE A 212 ? 0.8005 1.1866 0.9286 0.1219 -0.1432 -0.1010 212 PHE A CA 1436 C C . PHE A 212 ? 0.7695 1.1277 0.8909 0.0995 -0.1403 -0.0779 212 PHE A C 1437 O O . PHE A 212 ? 0.6166 0.9803 0.7382 0.0866 -0.1377 -0.0612 212 PHE A O 1438 C CB . PHE A 212 ? 0.8198 1.1868 0.9603 0.1256 -0.1464 -0.1120 212 PHE A CB 1439 C CG . PHE A 212 ? 0.8025 1.2066 0.9497 0.1457 -0.1492 -0.1295 212 PHE A CG 1440 C CD1 . PHE A 212 ? 0.7251 1.1170 0.8821 0.1632 -0.1567 -0.1548 212 PHE A CD1 1441 C CD2 . PHE A 212 ? 0.7979 1.2491 0.9429 0.1474 -0.1451 -0.1209 212 PHE A CD2 1442 C CE1 . PHE A 212 ? 0.6637 1.0881 0.8272 0.1832 -0.1610 -0.1727 212 PHE A CE1 1443 C CE2 . PHE A 212 ? 0.6994 1.1867 0.8502 0.1677 -0.1481 -0.1382 212 PHE A CE2 1444 C CZ . PHE A 212 ? 0.6403 1.1132 0.7997 0.1863 -0.1565 -0.1650 212 PHE A CZ 1445 N N . LEU A 213 ? 0.7243 1.0533 0.8406 0.0954 -0.1417 -0.0777 213 LEU A N 1446 C CA . LEU A 213 ? 0.5824 0.8807 0.6923 0.0761 -0.1407 -0.0585 213 LEU A CA 1447 C C . LEU A 213 ? 0.6645 0.9913 0.7680 0.0635 -0.1373 -0.0344 213 LEU A C 1448 O O . LEU A 213 ? 0.8061 1.1167 0.9105 0.0479 -0.1374 -0.0193 213 LEU A O 1449 C CB . LEU A 213 ? 0.5230 0.7926 0.6277 0.0762 -0.1428 -0.0627 213 LEU A CB 1450 C CG . LEU A 213 ? 0.5824 0.8207 0.6791 0.0591 -0.1431 -0.0450 213 LEU A CG 1451 C CD1 . LEU A 213 ? 0.4678 0.6669 0.5686 0.0484 -0.1443 -0.0415 213 LEU A CD1 1452 C CD2 . LEU A 213 ? 0.4967 0.7177 0.5878 0.0628 -0.1451 -0.0507 213 LEU A CD2 1453 N N . LEU A 214 ? 0.6669 1.0369 0.7648 0.0703 -0.1348 -0.0303 214 LEU A N 1454 C CA . LEU A 214 ? 0.7251 1.1268 0.8194 0.0581 -0.1314 -0.0050 214 LEU A CA 1455 C C . LEU A 214 ? 0.6596 1.0792 0.7626 0.0515 -0.1297 0.0030 214 LEU A C 1456 O O . LEU A 214 ? 0.6212 1.0350 0.7260 0.0333 -0.1300 0.0241 214 LEU A O 1457 C CB . LEU A 214 ? 0.8265 1.2802 0.9139 0.0696 -0.1281 -0.0026 214 LEU A CB 1458 C CG . LEU A 214 ? 0.8931 1.3409 0.9697 0.0633 -0.1284 0.0112 214 LEU A CG 1459 C CD1 . LEU A 214 ? 0.9086 1.4139 0.9778 0.0766 -0.1247 0.0140 214 LEU A CD1 1460 C CD2 . LEU A 214 ? 0.8059 1.2337 0.8826 0.0392 -0.1293 0.0389 214 LEU A CD2 1461 N N . GLU A 215 ? 0.6575 1.0991 0.7669 0.0669 -0.1291 -0.0144 215 GLU A N 1462 C CA . GLU A 215 ? 0.7298 1.1904 0.8481 0.0633 -0.1278 -0.0095 215 GLU A CA 1463 C C . GLU A 215 ? 0.8403 1.2542 0.9638 0.0480 -0.1310 -0.0045 215 GLU A C 1464 O O . GLU A 215 ? 0.7245 1.1477 0.8527 0.0344 -0.1306 0.0120 215 GLU A O 1465 C CB . GLU A 215 ? 0.6890 1.1782 0.8129 0.0854 -0.1280 -0.0323 215 GLU A CB 1466 C CG . GLU A 215 ? 0.7996 1.3547 0.9249 0.0924 -0.1235 -0.0254 215 GLU A CG 1467 C CD . GLU A 215 ? 0.9781 1.5531 1.1124 0.1073 -0.1247 -0.0423 215 GLU A CD 1468 O OE1 . GLU A 215 ? 0.9476 1.5553 1.0878 0.1019 -0.1218 -0.0302 215 GLU A OE1 1469 O OE2 . GLU A 215 ? 1.0542 1.6122 1.1911 0.1243 -0.1294 -0.0676 215 GLU A OE2 1470 N N . ILE A 216 ? 0.7502 1.1165 0.8733 0.0508 -0.1345 -0.0184 216 ILE A N 1471 C CA . ILE A 216 ? 0.6926 1.0157 0.8188 0.0396 -0.1374 -0.0157 216 ILE A CA 1472 C C . ILE A 216 ? 0.6899 0.9885 0.8105 0.0202 -0.1394 0.0040 216 ILE A C 1473 O O . ILE A 216 ? 0.8322 1.1186 0.9559 0.0074 -0.1417 0.0148 216 ILE A O 1474 C CB . ILE A 216 ? 0.7311 1.0138 0.8593 0.0489 -0.1400 -0.0350 216 ILE A CB 1475 C CG1 . ILE A 216 ? 0.7700 1.0723 0.9058 0.0684 -0.1404 -0.0555 216 ILE A CG1 1476 C CG2 . ILE A 216 ? 0.6994 0.9438 0.8299 0.0391 -0.1423 -0.0314 216 ILE A CG2 1477 C CD1 . ILE A 216 ? 0.7466 1.0120 0.8872 0.0772 -0.1437 -0.0730 216 ILE A CD1 1478 N N . PHE A 217 ? 0.6985 0.9891 0.8109 0.0189 -0.1395 0.0076 217 PHE A N 1479 C CA . PHE A 217 ? 0.6938 0.9607 0.8007 0.0021 -0.1427 0.0255 217 PHE A CA 1480 C C . PHE A 217 ? 0.7017 0.9942 0.8132 -0.0129 -0.1433 0.0480 217 PHE A C 1481 O O . PHE A 217 ? 0.7401 1.0075 0.8520 -0.0285 -0.1485 0.0615 217 PHE A O 1482 C CB . PHE A 217 ? 0.6967 0.9623 0.7945 0.0058 -0.1424 0.0260 217 PHE A CB 1483 C CG . PHE A 217 ? 0.7528 0.9925 0.8446 -0.0097 -0.1468 0.0434 217 PHE A CG 1484 C CD1 . PHE A 217 ? 0.6719 0.8623 0.7603 -0.0141 -0.1515 0.0391 217 PHE A CD1 1485 C CD2 . PHE A 217 ? 0.8839 1.1495 0.9739 -0.0189 -0.1468 0.0645 217 PHE A CD2 1486 C CE1 . PHE A 217 ? 0.6816 0.8472 0.7645 -0.0266 -0.1571 0.0533 217 PHE A CE1 1487 C CE2 . PHE A 217 ? 0.9050 1.1441 0.9907 -0.0328 -0.1525 0.0805 217 PHE A CE2 1488 C CZ . PHE A 217 ? 0.8104 0.9983 0.8923 -0.0361 -0.1582 0.0737 217 PHE A CZ 1489 N N . ALA A 218 ? 0.6961 1.0399 0.8122 -0.0077 -0.1387 0.0518 218 ALA A N 1490 C CA . ALA A 218 ? 0.7799 1.1540 0.9031 -0.0223 -0.1387 0.0748 218 ALA A CA 1491 C C . ALA A 218 ? 0.8129 1.1757 0.9456 -0.0298 -0.1418 0.0750 218 ALA A C 1492 O O . ALA A 218 ? 0.9702 1.3333 1.1098 -0.0471 -0.1458 0.0937 218 ALA A O 1493 C CB . ALA A 218 ? 0.7889 1.2262 0.9142 -0.0128 -0.1320 0.0788 218 ALA A CB 1494 N N . ASP A 219 ? 0.7250 1.0777 0.8591 -0.0166 -0.1409 0.0543 219 ASP A N 1495 C CA . ASP A 219 ? 0.7253 1.0718 0.8677 -0.0201 -0.1434 0.0521 219 ASP A CA 1496 C C . ASP A 219 ? 0.7266 1.0204 0.8668 -0.0315 -0.1502 0.0539 219 ASP A C 1497 O O . ASP A 219 ? 0.7514 1.0397 0.8982 -0.0386 -0.1539 0.0572 219 ASP A O 1498 C CB . ASP A 219 ? 0.8193 1.1739 0.9641 -0.0009 -0.1406 0.0300 219 ASP A CB 1499 C CG . ASP A 219 ? 0.8842 1.2978 1.0349 0.0093 -0.1357 0.0291 219 ASP A CG 1500 O OD1 . ASP A 219 ? 0.8352 1.2852 0.9900 -0.0009 -0.1340 0.0482 219 ASP A OD1 1501 O OD2 . ASP A 219 ? 0.8709 1.2949 1.0229 0.0277 -0.1343 0.0095 219 ASP A OD2 1502 N N . ILE A 220 ? 0.7843 1.0417 0.9152 -0.0323 -0.1523 0.0512 220 ILE A N 1503 C CA . ILE A 220 ? 0.7156 0.9235 0.8425 -0.0398 -0.1588 0.0504 220 ILE A CA 1504 C C . ILE A 220 ? 0.6603 0.8505 0.7839 -0.0555 -0.1652 0.0673 220 ILE A C 1505 O O . ILE A 220 ? 0.7169 0.8655 0.8346 -0.0594 -0.1711 0.0652 220 ILE A O 1506 C CB . ILE A 220 ? 0.6565 0.8320 0.7759 -0.0271 -0.1572 0.0324 220 ILE A CB 1507 C CG1 . ILE A 220 ? 0.5922 0.7708 0.7048 -0.0225 -0.1546 0.0314 220 ILE A CG1 1508 C CG2 . ILE A 220 ? 0.5346 0.7192 0.6591 -0.0124 -0.1532 0.0158 220 ILE A CG2 1509 C CD1 . ILE A 220 ? 0.7647 0.9056 0.8706 -0.0154 -0.1551 0.0187 220 ILE A CD1 1510 N N . LEU A 221 ? 0.7198 0.9425 0.8476 -0.0639 -0.1644 0.0845 221 LEU A N 1511 C CA . LEU A 221 ? 0.7435 0.9497 0.8693 -0.0784 -0.1710 0.1017 221 LEU A CA 1512 C C . LEU A 221 ? 0.8436 1.0211 0.9750 -0.0934 -0.1819 0.1101 221 LEU A C 1513 O O . LEU A 221 ? 0.8378 0.9825 0.9651 -0.1020 -0.1902 0.1167 221 LEU A O 1514 C CB . LEU A 221 ? 0.6903 0.9413 0.8211 -0.0848 -0.1677 0.1214 221 LEU A CB 1515 C CG . LEU A 221 ? 0.6972 0.9625 0.8180 -0.0740 -0.1615 0.1187 221 LEU A CG 1516 C CD1 . LEU A 221 ? 0.7256 1.0276 0.8509 -0.0847 -0.1607 0.1442 221 LEU A CD1 1517 C CD2 . LEU A 221 ? 0.5411 0.7571 0.6503 -0.0711 -0.1659 0.1094 221 LEU A CD2 1518 N N . SER A 222 ? 0.8709 1.0606 1.0117 -0.0958 -0.1828 0.1088 222 SER A N 1519 C CA . SER A 222 ? 0.9152 1.0826 1.0633 -0.1103 -0.1944 0.1167 222 SER A CA 1520 C C . SER A 222 ? 0.8352 0.9689 0.9780 -0.1026 -0.1978 0.0989 222 SER A C 1521 O O . SER A 222 ? 0.8058 0.9178 0.9526 -0.1116 -0.2083 0.1015 222 SER A O 1522 C CB . SER A 222 ? 0.8598 1.0679 1.0251 -0.1221 -0.1954 0.1328 222 SER A CB 1523 O OG . SER A 222 ? 0.8173 1.0596 0.9856 -0.1101 -0.1861 0.1227 222 SER A OG 1524 N N . SER A 223 ? 0.8071 0.9374 0.9416 -0.0856 -0.1895 0.0812 223 SER A N 1525 C CA . SER A 223 ? 0.7874 0.8910 0.9172 -0.0770 -0.1909 0.0658 223 SER A CA 1526 C C . SER A 223 ? 0.8441 0.9079 0.9606 -0.0686 -0.1912 0.0543 223 SER A C 1527 O O . SER A 223 ? 0.8707 0.9021 0.9819 -0.0695 -0.1985 0.0502 223 SER A O 1528 C CB . SER A 223 ? 0.6717 0.8020 0.8060 -0.0647 -0.1825 0.0554 223 SER A CB 1529 O OG . SER A 223 ? 0.7883 0.9400 0.9207 -0.0542 -0.1734 0.0500 223 SER A OG 1530 N N . VAL A 224 ? 0.8431 0.9116 0.9545 -0.0595 -0.1837 0.0487 224 VAL A N 1531 C CA . VAL A 224 ? 0.7811 0.8169 0.8819 -0.0507 -0.1828 0.0376 224 VAL A CA 1532 C C . VAL A 224 ? 0.7956 0.8007 0.8887 -0.0582 -0.1912 0.0434 224 VAL A C 1533 O O . VAL A 224 ? 0.9476 0.9599 1.0424 -0.0682 -0.1950 0.0564 224 VAL A O 1534 C CB . VAL A 224 ? 0.7331 0.7826 0.8324 -0.0393 -0.1738 0.0293 224 VAL A CB 1535 C CG1 . VAL A 224 ? 0.6302 0.6469 0.7206 -0.0318 -0.1734 0.0195 224 VAL A CG1 1536 C CG2 . VAL A 224 ? 0.6996 0.7740 0.8063 -0.0292 -0.1672 0.0203 224 VAL A CG2 1537 N N . ARG A 225 ? 0.7733 0.7454 0.8582 -0.0524 -0.1941 0.0340 225 ARG A N 1538 C CA . ARG A 225 ? 0.8467 0.7866 0.9235 -0.0565 -0.2033 0.0360 225 ARG A CA 1539 C C . ARG A 225 ? 0.7994 0.7246 0.8675 -0.0459 -0.1982 0.0269 225 ARG A C 1540 O O . ARG A 225 ? 0.6976 0.6003 0.7583 -0.0472 -0.2042 0.0281 225 ARG A O 1541 C CB . ARG A 225 ? 0.8545 0.7702 0.9278 -0.0562 -0.2118 0.0312 225 ARG A CB 1542 C CG . ARG A 225 ? 0.7755 0.6985 0.8576 -0.0683 -0.2210 0.0402 225 ARG A CG 1543 C CD . ARG A 225 ? 0.8619 0.7640 0.9393 -0.0640 -0.2281 0.0317 225 ARG A CD 1544 N NE . ARG A 225 ? 1.0186 0.9251 1.1053 -0.0756 -0.2391 0.0389 225 ARG A NE 1545 C CZ . ARG A 225 ? 1.0518 0.9380 1.1400 -0.0855 -0.2542 0.0443 225 ARG A CZ 1546 N NH1 . ARG A 225 ? 1.1609 1.0211 1.2404 -0.0843 -0.2597 0.0431 225 ARG A NH1 1547 N NH2 . ARG A 225 ? 0.8822 0.7737 0.9817 -0.0966 -0.2648 0.0507 225 ARG A NH2 1548 N N . TYR A 226 ? 0.6208 0.5584 0.6910 -0.0351 -0.1879 0.0174 226 TYR A N 1549 C CA . TYR A 226 ? 0.6110 0.5383 0.6765 -0.0253 -0.1827 0.0086 226 TYR A CA 1550 C C . TYR A 226 ? 0.7264 0.6782 0.7998 -0.0172 -0.1731 0.0017 226 TYR A C 1551 O O . TYR A 226 ? 0.7037 0.6615 0.7826 -0.0121 -0.1695 -0.0038 226 TYR A O 1552 C CB . TYR A 226 ? 0.5612 0.4601 0.6198 -0.0185 -0.1844 0.0006 226 TYR A CB 1553 C CG . TYR A 226 ? 0.6090 0.4999 0.6661 -0.0077 -0.1779 -0.0089 226 TYR A CG 1554 C CD1 . TYR A 226 ? 0.6382 0.5128 0.6922 0.0001 -0.1762 -0.0154 226 TYR A CD1 1555 C CD2 . TYR A 226 ? 0.6288 0.5306 0.6884 -0.0052 -0.1736 -0.0107 226 TYR A CD2 1556 C CE1 . TYR A 226 ? 0.7243 0.5937 0.7795 0.0087 -0.1704 -0.0223 226 TYR A CE1 1557 C CE2 . TYR A 226 ? 0.6210 0.5162 0.6818 0.0038 -0.1686 -0.0194 226 TYR A CE2 1558 C CZ . TYR A 226 ? 0.7199 0.5989 0.7794 0.0101 -0.1669 -0.0246 226 TYR A CZ 1559 O OH . TYR A 226 ? 0.8984 0.7730 0.9616 0.0179 -0.1620 -0.0315 226 TYR A OH 1560 N N . LEU A 227 ? 0.6501 0.6162 0.7241 -0.0153 -0.1700 0.0018 227 LEU A N 1561 C CA . LEU A 227 ? 0.5511 0.5411 0.6325 -0.0063 -0.1628 -0.0064 227 LEU A CA 1562 C C . LEU A 227 ? 0.6520 0.6286 0.7331 0.0033 -0.1597 -0.0175 227 LEU A C 1563 O O . LEU A 227 ? 0.6354 0.6014 0.7102 0.0026 -0.1616 -0.0163 227 LEU A O 1564 C CB . LEU A 227 ? 0.5112 0.5330 0.5941 -0.0095 -0.1618 0.0010 227 LEU A CB 1565 C CG . LEU A 227 ? 0.5564 0.6071 0.6459 0.0014 -0.1559 -0.0088 227 LEU A CG 1566 C CD1 . LEU A 227 ? 0.4821 0.5396 0.5806 0.0079 -0.1533 -0.0175 227 LEU A CD1 1567 C CD2 . LEU A 227 ? 0.5394 0.6255 0.6285 -0.0022 -0.1551 0.0013 227 LEU A CD2 1568 N N . GLU A 228 ? 0.7721 0.7484 0.8614 0.0119 -0.1556 -0.0278 228 GLU A N 1569 C CA . GLU A 228 ? 0.8024 0.7688 0.8958 0.0204 -0.1530 -0.0380 228 GLU A CA 1570 C C . GLU A 228 ? 0.7952 0.7855 0.8998 0.0288 -0.1501 -0.0475 228 GLU A C 1571 O O . GLU A 228 ? 0.7751 0.7745 0.8879 0.0323 -0.1489 -0.0511 228 GLU A O 1572 C CB . GLU A 228 ? 0.8135 0.7569 0.9092 0.0233 -0.1518 -0.0409 228 GLU A CB 1573 C CG . GLU A 228 ? 0.7911 0.7229 0.8928 0.0303 -0.1493 -0.0488 228 GLU A CG 1574 C CD . GLU A 228 ? 0.8680 0.7825 0.9734 0.0333 -0.1470 -0.0490 228 GLU A CD 1575 O OE1 . GLU A 228 ? 0.8187 0.7312 0.9368 0.0392 -0.1442 -0.0550 228 GLU A OE1 1576 O OE2 . GLU A 228 ? 0.9571 0.8611 1.0537 0.0298 -0.1486 -0.0427 228 GLU A OE2 1577 N N . LEU A 229 ? 0.8047 0.8056 0.9092 0.0330 -0.1501 -0.0524 229 LEU A N 1578 C CA . LEU A 229 ? 0.6540 0.6786 0.7682 0.0428 -0.1492 -0.0636 229 LEU A CA 1579 C C . LEU A 229 ? 0.5830 0.5940 0.7074 0.0509 -0.1493 -0.0762 229 LEU A C 1580 O O . LEU A 229 ? 0.6756 0.6732 0.7962 0.0501 -0.1499 -0.0764 229 LEU A O 1581 C CB . LEU A 229 ? 0.6057 0.6573 0.7127 0.0429 -0.1496 -0.0602 229 LEU A CB 1582 C CG . LEU A 229 ? 0.6163 0.7011 0.7299 0.0541 -0.1493 -0.0709 229 LEU A CG 1583 C CD1 . LEU A 229 ? 0.5877 0.6894 0.7081 0.0564 -0.1484 -0.0723 229 LEU A CD1 1584 C CD2 . LEU A 229 ? 0.7315 0.8421 0.8349 0.0531 -0.1491 -0.0635 229 LEU A CD2 1585 N N . ARG A 230 ? 0.5350 0.5496 0.6740 0.0585 -0.1496 -0.0865 230 ARG A N 1586 C CA . ARG A 230 ? 0.7536 0.7523 0.9067 0.0644 -0.1506 -0.0966 230 ARG A CA 1587 C C . ARG A 230 ? 0.8742 0.8885 1.0417 0.0760 -0.1544 -0.1131 230 ARG A C 1588 O O . ARG A 230 ? 0.8333 0.8659 1.0062 0.0823 -0.1561 -0.1194 230 ARG A O 1589 C CB . ARG A 230 ? 0.6830 0.6628 0.8445 0.0626 -0.1491 -0.0932 230 ARG A CB 1590 C CG . ARG A 230 ? 0.6139 0.5712 0.7662 0.0551 -0.1465 -0.0821 230 ARG A CG 1591 C CD . ARG A 230 ? 0.8413 0.7855 1.0010 0.0550 -0.1447 -0.0783 230 ARG A CD 1592 N NE . ARG A 230 ? 0.9208 0.8450 1.0743 0.0511 -0.1423 -0.0704 230 ARG A NE 1593 C CZ . ARG A 230 ? 1.0846 0.9977 1.2476 0.0533 -0.1410 -0.0723 230 ARG A CZ 1594 N NH1 . ARG A 230 ? 0.9972 0.9151 1.1775 0.0583 -0.1429 -0.0821 230 ARG A NH1 1595 N NH2 . ARG A 230 ? 1.2443 1.1432 1.4002 0.0510 -0.1384 -0.0650 230 ARG A NH2 1596 N N . ASP A 231 ? 0.8177 0.8245 0.9919 0.0796 -0.1566 -0.1210 231 ASP A N 1597 C CA . ASP A 231 ? 0.7277 0.7427 0.9193 0.0907 -0.1622 -0.1385 231 ASP A CA 1598 C C . ASP A 231 ? 0.7676 0.8150 0.9545 0.1003 -0.1653 -0.1483 231 ASP A C 1599 O O . ASP A 231 ? 0.6172 0.6754 0.8179 0.1113 -0.1710 -0.1636 231 ASP A O 1600 C CB . ASP A 231 ? 0.7745 0.7781 0.9856 0.0937 -0.1645 -0.1431 231 ASP A CB 1601 C CG . ASP A 231 ? 0.8571 0.8327 1.0768 0.0867 -0.1619 -0.1348 231 ASP A CG 1602 O OD1 . ASP A 231 ? 0.6369 0.6026 0.8571 0.0841 -0.1612 -0.1340 231 ASP A OD1 1603 O OD2 . ASP A 231 ? 1.0647 1.0301 1.2904 0.0845 -0.1604 -0.1287 231 ASP A OD2 1604 N N . THR A 232 ? 0.8070 0.8702 0.9748 0.0966 -0.1623 -0.1394 232 THR A N 1605 C CA . THR A 232 ? 0.7568 0.8560 0.9176 0.1052 -0.1637 -0.1448 232 THR A CA 1606 C C . THR A 232 ? 0.8311 0.9439 0.9897 0.1141 -0.1675 -0.1556 232 THR A C 1607 O O . THR A 232 ? 0.7709 0.8716 0.9220 0.1088 -0.1664 -0.1496 232 THR A O 1608 C CB . THR A 232 ? 0.6808 0.7946 0.8234 0.0958 -0.1584 -0.1264 232 THR A CB 1609 O OG1 . THR A 232 ? 0.6124 0.7031 0.7539 0.0841 -0.1552 -0.1137 232 THR A OG1 1610 C CG2 . THR A 232 ? 0.5122 0.6656 0.6524 0.1042 -0.1584 -0.1299 232 THR A CG2 1611 N N . ASN A 233 ? 0.7469 0.8856 0.9119 0.1289 -0.1726 -0.1724 233 ASN A N 1612 C CA . ASN A 233 ? 0.6989 0.8602 0.8574 0.1391 -0.1759 -0.1816 233 ASN A CA 1613 C C . ASN A 233 ? 0.7365 0.9300 0.8740 0.1371 -0.1706 -0.1672 233 ASN A C 1614 O O . ASN A 233 ? 0.7261 0.9510 0.8602 0.1435 -0.1695 -0.1679 233 ASN A O 1615 C CB . ASN A 233 ? 0.7682 0.9457 0.9415 0.1575 -0.1849 -0.2069 233 ASN A CB 1616 C CG . ASN A 233 ? 0.8112 1.0016 0.9821 0.1681 -0.1905 -0.2199 233 ASN A CG 1617 O OD1 . ASN A 233 ? 0.7852 0.9883 0.9678 0.1841 -0.1996 -0.2423 233 ASN A OD1 1618 N ND2 . ASN A 233 ? 0.8117 0.9984 0.9679 0.1601 -0.1861 -0.2065 233 ASN A ND2 1619 N N . LEU A 234 ? 0.7346 0.9202 0.8587 0.1280 -0.1675 -0.1532 234 LEU A N 1620 C CA . LEU A 234 ? 0.7657 0.9769 0.8713 0.1232 -0.1629 -0.1353 234 LEU A CA 1621 C C . LEU A 234 ? 0.7736 1.0119 0.8706 0.1353 -0.1657 -0.1423 234 LEU A C 1622 O O . LEU A 234 ? 0.7280 0.9892 0.8095 0.1327 -0.1625 -0.1271 234 LEU A O 1623 C CB . LEU A 234 ? 0.6623 0.8447 0.7590 0.1049 -0.1592 -0.1138 234 LEU A CB 1624 C CG . LEU A 234 ? 0.5904 0.7549 0.6920 0.0939 -0.1563 -0.1048 234 LEU A CG 1625 C CD1 . LEU A 234 ? 0.3369 0.4646 0.4336 0.0790 -0.1551 -0.0907 234 LEU A CD1 1626 C CD2 . LEU A 234 ? 0.6770 0.8749 0.7726 0.0918 -0.1529 -0.0934 234 LEU A CD2 1627 N N . ALA A 235 ? 0.7394 0.9761 0.8477 0.1490 -0.1724 -0.1654 235 ALA A N 1628 C CA . ALA A 235 ? 0.8216 1.0798 0.9236 0.1621 -0.1767 -0.1759 235 ALA A CA 1629 C C . ALA A 235 ? 0.8729 1.1794 0.9581 0.1696 -0.1736 -0.1678 235 ALA A C 1630 O O . ALA A 235 ? 1.0294 1.3487 1.1002 0.1697 -0.1724 -0.1580 235 ALA A O 1631 C CB . ALA A 235 ? 0.8754 1.1322 0.9954 0.1781 -0.1861 -0.2049 235 ALA A CB 1632 N N . ARG A 236 ? 0.7751 1.1107 0.8623 0.1765 -0.1722 -0.1712 236 ARG A N 1633 C CA . ARG A 236 ? 0.9384 1.3260 1.0106 0.1848 -0.1686 -0.1629 236 ARG A CA 1634 C C . ARG A 236 ? 0.8766 1.2758 0.9444 0.1714 -0.1606 -0.1399 236 ARG A C 1635 O O . ARG A 236 ? 0.8794 1.3171 0.9469 0.1803 -0.1587 -0.1421 236 ARG A O 1636 C CB . ARG A 236 ? 1.0843 1.5097 1.1605 0.2101 -0.1750 -0.1895 236 ARG A CB 1637 C CG . ARG A 236 ? 0.9644 1.4073 1.0341 0.2267 -0.1814 -0.2048 236 ARG A CG 1638 C CD . ARG A 236 ? 0.9977 1.4966 1.0468 0.2362 -0.1767 -0.1930 236 ARG A CD 1639 N NE . ARG A 236 ? 1.1551 1.6966 1.2029 0.2446 -0.1732 -0.1925 236 ARG A NE 1640 C CZ . ARG A 236 ? 1.1224 1.7090 1.1686 0.2695 -0.1779 -0.2136 236 ARG A CZ 1641 N NH1 . ARG A 236 ? 1.1930 1.7883 1.2385 0.2887 -0.1872 -0.2375 236 ARG A NH1 1642 N NH2 . ARG A 236 ? 0.8666 1.4916 0.9119 0.2760 -0.1739 -0.2114 236 ARG A NH2 1643 N N . PHE A 237 ? 0.8784 1.2449 0.9435 0.1505 -0.1567 -0.1185 237 PHE A N 1644 C CA . PHE A 237 ? 0.8843 1.2572 0.9470 0.1355 -0.1506 -0.0957 237 PHE A CA 1645 C C . PHE A 237 ? 0.8439 1.2530 0.8918 0.1308 -0.1458 -0.0718 237 PHE A C 1646 O O . PHE A 237 ? 0.8109 1.2084 0.8495 0.1242 -0.1463 -0.0594 237 PHE A O 1647 C CB . PHE A 237 ? 0.8434 1.1650 0.9104 0.1159 -0.1501 -0.0843 237 PHE A CB 1648 C CG . PHE A 237 ? 0.8603 1.1858 0.9235 0.0987 -0.1454 -0.0588 237 PHE A CG 1649 C CD1 . PHE A 237 ? 0.8261 1.1625 0.8974 0.0968 -0.1432 -0.0583 237 PHE A CD1 1650 C CD2 . PHE A 237 ? 0.8344 1.1526 0.8875 0.0846 -0.1444 -0.0354 237 PHE A CD2 1651 C CE1 . PHE A 237 ? 0.8083 1.1492 0.8781 0.0806 -0.1399 -0.0353 237 PHE A CE1 1652 C CE2 . PHE A 237 ? 0.8393 1.1602 0.8918 0.0681 -0.1419 -0.0120 237 PHE A CE2 1653 C CZ . PHE A 237 ? 0.8004 1.1333 0.8617 0.0659 -0.1396 -0.0121 237 PHE A CZ 1654 N N . GLN A 238 ? 0.7941 1.2479 0.8411 0.1342 -0.1415 -0.0643 238 GLN A N 1655 C CA . GLN A 238 ? 0.9142 1.4087 0.9497 0.1293 -0.1364 -0.0388 238 GLN A CA 1656 C C . GLN A 238 ? 0.8299 1.3204 0.8693 0.1079 -0.1321 -0.0127 238 GLN A C 1657 O O . GLN A 238 ? 0.7765 1.2717 0.8255 0.1070 -0.1307 -0.0170 238 GLN A O 1658 C CB . GLN A 238 ? 1.0189 1.5775 1.0498 0.1509 -0.1343 -0.0483 238 GLN A CB 1659 C CG . GLN A 238 ? 1.0151 1.6116 1.0305 0.1581 -0.1325 -0.0364 238 GLN A CG 1660 C CD . GLN A 238 ? 1.1926 1.7783 1.2036 0.1753 -0.1391 -0.0611 238 GLN A CD 1661 O OE1 . GLN A 238 ? 1.2133 1.7833 1.2156 0.1709 -0.1406 -0.0523 238 GLN A OE1 1662 N NE2 . GLN A 238 ? 1.2408 1.8336 1.2593 0.1952 -0.1442 -0.0927 238 GLN A NE2 1663 N N . PHE A 239 ? 0.8152 1.2963 0.8482 0.0911 -0.1312 0.0141 239 PHE A N 1664 C CA . PHE A 239 ? 0.8380 1.3202 0.8757 0.0707 -0.1286 0.0408 239 PHE A CA 1665 C C . PHE A 239 ? 0.8675 1.4149 0.9027 0.0733 -0.1226 0.0592 239 PHE A C 1666 O O . PHE A 239 ? 0.8922 1.4808 0.9183 0.0892 -0.1204 0.0556 239 PHE A O 1667 C CB . PHE A 239 ? 0.8043 1.2451 0.8382 0.0513 -0.1323 0.0614 239 PHE A CB 1668 C CG . PHE A 239 ? 0.7533 1.1951 0.7934 0.0296 -0.1319 0.0902 239 PHE A CG 1669 C CD1 . PHE A 239 ? 0.7942 1.1988 0.8438 0.0166 -0.1348 0.0896 239 PHE A CD1 1670 C CD2 . PHE A 239 ? 0.5889 1.0698 0.6261 0.0221 -0.1291 0.1185 239 PHE A CD2 1671 C CE1 . PHE A 239 ? 0.7368 1.1417 0.7937 -0.0033 -0.1361 0.1147 239 PHE A CE1 1672 C CE2 . PHE A 239 ? 0.5118 0.9934 0.5578 0.0010 -0.1300 0.1456 239 PHE A CE2 1673 C CZ . PHE A 239 ? 0.7176 1.1603 0.7737 -0.0117 -0.1340 0.1429 239 PHE A CZ 1674 N N . SER A 240 ? 0.8101 1.3687 0.8539 0.0579 -0.1200 0.0788 240 SER A N 1675 C CA . SER A 240 ? 0.7449 1.3643 0.7890 0.0552 -0.1139 0.1028 240 SER A CA 1676 C C . SER A 240 ? 0.6779 1.2878 0.7352 0.0329 -0.1141 0.1234 240 SER A C 1677 O O . SER A 240 ? 0.5320 1.1098 0.5976 0.0296 -0.1167 0.1097 240 SER A O 1678 C CB . SER A 240 ? 0.7345 1.4121 0.7771 0.0795 -0.1092 0.0847 240 SER A CB 1679 O OG . SER A 240 ? 0.8070 1.4762 0.8602 0.0843 -0.1099 0.0651 240 SER A OG 1680 N N . PRO A 241 ? 0.8073 1.4453 0.8675 0.0171 -0.1118 0.1572 241 PRO A N 1681 C CA . PRO A 241 ? 0.7798 1.4052 0.8544 -0.0071 -0.1141 0.1798 241 PRO A CA 1682 C C . PRO A 241 ? 0.7345 1.3687 0.8207 -0.0047 -0.1124 0.1663 241 PRO A C 1683 O O . PRO A 241 ? 0.6376 1.3159 0.7232 0.0137 -0.1069 0.1514 241 PRO A O 1684 C CB . PRO A 241 ? 0.8034 1.4830 0.8806 -0.0167 -0.1095 0.2153 241 PRO A CB 1685 C CG . PRO A 241 ? 0.7933 1.4869 0.8545 -0.0040 -0.1079 0.2158 241 PRO A CG 1686 C CD . PRO A 241 ? 0.7393 1.4271 0.7904 0.0221 -0.1072 0.1767 241 PRO A CD 1687 N N . LEU A 242 ? 0.9528 1.5447 1.0493 -0.0224 -0.1180 0.1709 242 LEU A N 1688 C CA . LEU A 242 ? 1.0504 1.6420 1.1572 -0.0207 -0.1177 0.1572 242 LEU A CA 1689 C C . LEU A 242 ? 1.2828 1.9231 1.4034 -0.0325 -0.1144 0.1811 242 LEU A C 1690 O O . LEU A 242 ? 1.3481 1.9965 1.4749 -0.0517 -0.1160 0.2116 242 LEU A O 1691 C CB . LEU A 242 ? 0.8620 1.3849 0.9721 -0.0321 -0.1258 0.1487 242 LEU A CB 1692 C CG . LEU A 242 ? 0.7707 1.2436 0.8687 -0.0244 -0.1296 0.1307 242 LEU A CG 1693 C CD1 . LEU A 242 ? 0.8184 1.2294 0.9194 -0.0368 -0.1373 0.1268 242 LEU A CD1 1694 C CD2 . LEU A 242 ? 0.6979 1.1814 0.7903 0.0003 -0.1259 0.1003 242 LEU A CD2 1695 N N . PRO A 243 ? 1.3824 2.0562 1.5093 -0.0210 -0.1101 0.1678 243 PRO A N 1696 C CA . PRO A 243 ? 1.4655 2.1846 1.6079 -0.0320 -0.1072 0.1879 243 PRO A CA 1697 C C . PRO A 243 ? 1.5714 2.2511 1.7273 -0.0593 -0.1152 0.2067 243 PRO A C 1698 O O . PRO A 243 ? 1.6550 2.3637 1.8234 -0.0772 -0.1151 0.2367 243 PRO A O 1699 C CB . PRO A 243 ? 1.3736 2.1110 1.5188 -0.0131 -0.1045 0.1611 243 PRO A CB 1700 C CG . PRO A 243 ? 1.3082 2.0393 1.4384 0.0119 -0.1032 0.1326 243 PRO A CG 1701 C CD . PRO A 243 ? 1.3095 1.9836 1.4302 0.0041 -0.1084 0.1331 243 PRO A CD 1702 N N . VAL A 244 ? 1.5177 2.1333 1.6715 -0.0619 -0.1224 0.1894 244 VAL A N 1703 C CA . VAL A 244 ? 1.4769 2.0518 1.6423 -0.0839 -0.1315 0.2003 244 VAL A CA 1704 C C . VAL A 244 ? 1.4432 2.0221 1.6191 -0.1086 -0.1365 0.2353 244 VAL A C 1705 O O . VAL A 244 ? 1.3986 1.9916 1.5687 -0.1106 -0.1346 0.2513 244 VAL A O 1706 C CB . VAL A 244 ? 1.4087 1.9105 1.5650 -0.0828 -0.1390 0.1806 244 VAL A CB 1707 C CG1 . VAL A 244 ? 1.2466 1.7382 1.3972 -0.0623 -0.1359 0.1485 244 VAL A CG1 1708 C CG2 . VAL A 244 ? 1.4616 1.9374 1.6047 -0.0824 -0.1408 0.1838 244 VAL A CG2 1709 N N . ASP A 245 ? 1.3769 1.9418 1.5691 -0.1273 -0.1441 0.2468 245 ASP A N 1710 C CA . ASP A 245 ? 1.3290 1.8902 1.5356 -0.1530 -0.1520 0.2794 245 ASP A CA 1711 C C . ASP A 245 ? 1.2282 1.7179 1.4285 -0.1627 -0.1642 0.2775 245 ASP A C 1712 O O . ASP A 245 ? 1.2058 1.6503 1.3931 -0.1512 -0.1664 0.2512 245 ASP A O 1713 C CB . ASP A 245 ? 1.4060 1.9855 1.6352 -0.1686 -0.1563 0.2914 245 ASP A CB 1714 C CG . ASP A 245 ? 1.5041 2.1537 1.7398 -0.1573 -0.1446 0.2902 245 ASP A CG 1715 O OD1 . ASP A 245 ? 1.5169 2.1843 1.7380 -0.1332 -0.1355 0.2672 245 ASP A OD1 1716 O OD2 . ASP A 245 ? 1.5293 2.2167 1.7859 -0.1722 -0.1454 0.3118 245 ASP A OD2 1717 N N . GLU A 246 ? 1.2506 1.7313 1.4609 -0.1834 -0.1726 0.3059 246 GLU A N 1718 C CA . GLU A 246 ? 1.3351 1.7496 1.5407 -0.1927 -0.1859 0.3056 246 GLU A CA 1719 C C . GLU A 246 ? 1.3576 1.7229 1.5664 -0.1957 -0.1962 0.2868 246 GLU A C 1720 O O . GLU A 246 ? 1.3325 1.6856 1.5592 -0.2145 -0.2077 0.3004 246 GLU A O 1721 C CB . GLU A 246 ? 1.5214 1.9369 1.7425 -0.2167 -0.1955 0.3415 246 GLU A CB 1722 C CG . GLU A 246 ? 1.6825 2.1410 1.8994 -0.2155 -0.1870 0.3643 246 GLU A CG 1723 C CD . GLU A 246 ? 1.7789 2.2550 2.0182 -0.2414 -0.1947 0.4052 246 GLU A CD 1724 O OE1 . GLU A 246 ? 1.7442 2.2470 2.0059 -0.2556 -0.1967 0.4191 246 GLU A OE1 1725 O OE2 . GLU A 246 ? 1.8233 2.2870 2.0590 -0.2478 -0.1991 0.4239 246 GLU A OE2 1726 N N . VAL A 247 ? 1.3619 1.7001 1.5543 -0.1771 -0.1927 0.2560 247 VAL A N 1727 C CA . VAL A 247 ? 1.2521 1.5437 1.4443 -0.1771 -0.2015 0.2373 247 VAL A CA 1728 C C . VAL A 247 ? 1.1732 1.4042 1.3501 -0.1730 -0.2094 0.2246 247 VAL A C 1729 O O . VAL A 247 ? 1.2347 1.4599 1.3954 -0.1581 -0.2023 0.2122 247 VAL A O 1730 C CB . VAL A 247 ? 1.1780 1.4864 1.3662 -0.1599 -0.1922 0.2132 247 VAL A CB 1731 C CG1 . VAL A 247 ? 1.2674 1.5231 1.4480 -0.1541 -0.1991 0.1904 247 VAL A CG1 1732 C CG2 . VAL A 247 ? 1.0700 1.4267 1.2768 -0.1675 -0.1897 0.2249 247 VAL A CG2 1733 N N . SER A 248 ? 1.0105 1.1982 1.1936 -0.1858 -0.2248 0.2276 248 SER A N 1734 C CA . SER A 248 ? 1.0240 1.1543 1.1935 -0.1816 -0.2339 0.2150 248 SER A CA 1735 C C . SER A 248 ? 0.9883 1.0961 1.1430 -0.1625 -0.2287 0.1844 248 SER A C 1736 O O . SER A 248 ? 1.0135 1.1153 1.1726 -0.1614 -0.2312 0.1738 248 SER A O 1737 C CB . SER A 248 ? 0.9895 1.0824 1.1709 -0.1994 -0.2536 0.2254 248 SER A CB 1738 O OG . SER A 248 ? 0.9476 0.9872 1.1156 -0.1941 -0.2632 0.2133 248 SER A OG 1739 N N . SER A 249 ? 0.7547 0.8511 0.8929 -0.1477 -0.2217 0.1713 249 SER A N 1740 C CA . SER A 249 ? 0.7075 0.7883 0.8339 -0.1299 -0.2152 0.1450 249 SER A CA 1741 C C . SER A 249 ? 0.8867 0.9148 1.0050 -0.1275 -0.2255 0.1318 249 SER A C 1742 O O . SER A 249 ? 1.0441 1.0422 1.1569 -0.1311 -0.2342 0.1358 249 SER A O 1743 C CB . SER A 249 ? 0.7351 0.8292 0.8497 -0.1144 -0.2034 0.1351 249 SER A CB 1744 O OG . SER A 249 ? 0.7502 0.8180 0.8546 -0.0997 -0.2004 0.1119 249 SER A OG 1745 N N . PRO A 250 ? 0.8799 0.8983 0.9965 -0.1197 -0.2244 0.1155 250 PRO A N 1746 C CA . PRO A 250 ? 0.7719 0.7481 0.8793 -0.1130 -0.2312 0.0997 250 PRO A CA 1747 C C . PRO A 250 ? 0.8698 0.8266 0.9623 -0.0982 -0.2252 0.0853 250 PRO A C 1748 O O . PRO A 250 ? 0.8267 0.7482 0.9103 -0.0929 -0.2316 0.0750 250 PRO A O 1749 C CB . PRO A 250 ? 0.5732 0.5621 0.6843 -0.1067 -0.2264 0.0890 250 PRO A CB 1750 C CG . PRO A 250 ? 0.6391 0.6730 0.7638 -0.1139 -0.2209 0.1012 250 PRO A CG 1751 C CD . PRO A 250 ? 0.8463 0.9018 0.9704 -0.1155 -0.2148 0.1121 250 PRO A CD 1752 N N . MET A 251 ? 0.8272 0.8085 0.9174 -0.0908 -0.2134 0.0841 251 MET A N 1753 C CA . MET A 251 ? 0.7488 0.7164 0.8279 -0.0762 -0.2068 0.0691 251 MET A CA 1754 C C . MET A 251 ? 0.8095 0.7426 0.8794 -0.0770 -0.2152 0.0697 251 MET A C 1755 O O . MET A 251 ? 0.9178 0.8514 0.9887 -0.0860 -0.2209 0.0838 251 MET A O 1756 C CB . MET A 251 ? 0.7501 0.7519 0.8302 -0.0691 -0.1952 0.0684 251 MET A CB 1757 C CG . MET A 251 ? 0.7299 0.7205 0.8017 -0.0548 -0.1891 0.0531 251 MET A CG 1758 S SD . MET A 251 ? 0.7228 0.7564 0.7988 -0.0440 -0.1768 0.0470 251 MET A SD 1759 C CE . MET A 251 ? 1.4222 1.4754 1.5082 -0.0427 -0.1733 0.0427 251 MET A CE 1760 N N . LYS A 252 ? 0.7908 0.6953 0.8520 -0.0671 -0.2163 0.0551 252 LYS A N 1761 C CA . LYS A 252 ? 0.7915 0.6632 0.8433 -0.0654 -0.2246 0.0531 252 LYS A CA 1762 C C . LYS A 252 ? 0.8144 0.6817 0.8581 -0.0515 -0.2161 0.0404 252 LYS A C 1763 O O . LYS A 252 ? 0.8535 0.7023 0.8899 -0.0490 -0.2206 0.0398 252 LYS A O 1764 C CB . LYS A 252 ? 0.6991 0.5393 0.7471 -0.0656 -0.2361 0.0471 252 LYS A CB 1765 C CG . LYS A 252 ? 0.7458 0.5870 0.8034 -0.0793 -0.2468 0.0577 252 LYS A CG 1766 C CD . LYS A 252 ? 0.8205 0.6492 0.8821 -0.0926 -0.2602 0.0730 252 LYS A CD 1767 C CE . LYS A 252 ? 0.9418 0.7286 0.9963 -0.0907 -0.2765 0.0664 252 LYS A CE 1768 N NZ . LYS A 252 ? 1.1356 0.9064 1.1895 -0.0974 -0.2864 0.0778 252 LYS A NZ 1769 N N . LYS A 253 ? 0.7670 0.6509 0.8135 -0.0424 -0.2048 0.0304 253 LYS A N 1770 C CA . LYS A 253 ? 0.7543 0.6364 0.7971 -0.0300 -0.1969 0.0186 253 LYS A CA 1771 C C . LYS A 253 ? 0.8856 0.8002 0.9356 -0.0256 -0.1864 0.0160 253 LYS A C 1772 O O . LYS A 253 ? 0.8672 0.8025 0.9247 -0.0272 -0.1827 0.0171 253 LYS A O 1773 C CB . LYS A 253 ? 0.6606 0.5247 0.7006 -0.0208 -0.1949 0.0062 253 LYS A CB 1774 C CG . LYS A 253 ? 0.6391 0.4897 0.6738 -0.0104 -0.1918 -0.0034 253 LYS A CG 1775 C CD . LYS A 253 ? 0.6965 0.5436 0.7336 -0.0008 -0.1851 -0.0138 253 LYS A CD 1776 C CE . LYS A 253 ? 0.8234 0.6502 0.8534 0.0077 -0.1860 -0.0208 253 LYS A CE 1777 N NZ . LYS A 253 ? 0.9007 0.7336 0.9377 0.0171 -0.1762 -0.0289 253 LYS A NZ 1778 N N . LEU A 254 ? 0.8452 0.7641 0.8929 -0.0189 -0.1826 0.0114 254 LEU A N 1779 C CA . LEU A 254 ? 0.7832 0.7303 0.8372 -0.0116 -0.1742 0.0051 254 LEU A CA 1780 C C . LEU A 254 ? 0.8616 0.7974 0.9154 -0.0005 -0.1707 -0.0085 254 LEU A C 1781 O O . LEU A 254 ? 0.9285 0.8470 0.9754 0.0008 -0.1741 -0.0088 254 LEU A O 1782 C CB . LEU A 254 ? 0.7527 0.7243 0.8054 -0.0154 -0.1744 0.0153 254 LEU A CB 1783 C CG . LEU A 254 ? 0.6269 0.6327 0.6847 -0.0066 -0.1672 0.0088 254 LEU A CG 1784 C CD1 . LEU A 254 ? 0.4788 0.5056 0.5453 -0.0060 -0.1633 0.0066 254 LEU A CD1 1785 C CD2 . LEU A 254 ? 0.6265 0.6553 0.6798 -0.0099 -0.1681 0.0211 254 LEU A CD2 1786 N N . ALA A 255 ? 0.8470 0.7923 0.9097 0.0074 -0.1645 -0.0194 255 ALA A N 1787 C CA . ALA A 255 ? 0.6840 0.6190 0.7506 0.0167 -0.1615 -0.0314 255 ALA A CA 1788 C C . ALA A 255 ? 0.7000 0.6572 0.7780 0.0251 -0.1568 -0.0419 255 ALA A C 1789 O O . ALA A 255 ? 0.5776 0.5507 0.6627 0.0262 -0.1546 -0.0436 255 ALA A O 1790 C CB . ALA A 255 ? 0.4527 0.3655 0.5203 0.0182 -0.1610 -0.0345 255 ALA A CB 1791 N N . PHE A 256 ? 0.7571 0.7153 0.8373 0.0318 -0.1564 -0.0499 256 PHE A N 1792 C CA . PHE A 256 ? 0.7669 0.7433 0.8590 0.0410 -0.1541 -0.0624 256 PHE A CA 1793 C C . PHE A 256 ? 0.8015 0.7602 0.9043 0.0463 -0.1529 -0.0721 256 PHE A C 1794 O O . PHE A 256 ? 0.8004 0.7443 0.8996 0.0467 -0.1539 -0.0724 256 PHE A O 1795 C CB . PHE A 256 ? 0.6570 0.6527 0.7444 0.0451 -0.1556 -0.0642 256 PHE A CB 1796 C CG . PHE A 256 ? 0.6356 0.6541 0.7143 0.0400 -0.1561 -0.0526 256 PHE A CG 1797 C CD1 . PHE A 256 ? 0.6544 0.6645 0.7209 0.0307 -0.1590 -0.0376 256 PHE A CD1 1798 C CD2 . PHE A 256 ? 0.6845 0.7340 0.7683 0.0447 -0.1541 -0.0560 256 PHE A CD2 1799 C CE1 . PHE A 256 ? 0.6866 0.7192 0.7476 0.0245 -0.1595 -0.0242 256 PHE A CE1 1800 C CE2 . PHE A 256 ? 0.6877 0.7628 0.7646 0.0399 -0.1537 -0.0434 256 PHE A CE2 1801 C CZ . PHE A 256 ? 0.6558 0.7225 0.7221 0.0289 -0.1561 -0.0264 256 PHE A CZ 1802 N N . ARG A 257 ? 0.7021 0.6627 0.8190 0.0503 -0.1510 -0.0789 257 ARG A N 1803 C CA . ARG A 257 ? 0.8276 0.7715 0.9569 0.0535 -0.1497 -0.0845 257 ARG A CA 1804 C C . ARG A 257 ? 0.9706 0.9214 1.1138 0.0612 -0.1516 -0.0974 257 ARG A C 1805 O O . ARG A 257 ? 1.1002 1.0441 1.2417 0.0622 -0.1525 -0.0993 257 ARG A O 1806 C CB . ARG A 257 ? 0.9655 0.9035 1.1047 0.0532 -0.1475 -0.0832 257 ARG A CB 1807 C CG . ARG A 257 ? 1.0423 0.9644 1.1702 0.0470 -0.1459 -0.0719 257 ARG A CG 1808 C CD . ARG A 257 ? 0.9858 0.8889 1.1107 0.0468 -0.1446 -0.0692 257 ARG A CD 1809 N NE . ARG A 257 ? 1.0379 0.9290 1.1483 0.0423 -0.1450 -0.0600 257 ARG A NE 1810 C CZ . ARG A 257 ? 1.1003 0.9872 1.1946 0.0377 -0.1489 -0.0548 257 ARG A CZ 1811 N NH1 . ARG A 257 ? 1.3598 1.2542 1.4498 0.0368 -0.1515 -0.0561 257 ARG A NH1 1812 N NH2 . ARG A 257 ? 0.7647 0.6398 0.8476 0.0343 -0.1511 -0.0483 257 ARG A NH2 1813 N N . GLY A 258 ? 0.7518 0.7158 0.9091 0.0673 -0.1532 -0.1072 258 GLY A N 1814 C CA . GLY A 258 ? 0.6882 0.6570 0.8618 0.0752 -0.1569 -0.1215 258 GLY A CA 1815 C C . GLY A 258 ? 0.7992 0.7935 0.9704 0.0831 -0.1608 -0.1317 258 GLY A C 1816 O O . GLY A 258 ? 0.9179 0.9219 1.1047 0.0917 -0.1653 -0.1458 258 GLY A O 1817 N N . SER A 259 ? 0.8513 0.8569 1.0030 0.0807 -0.1598 -0.1244 259 SER A N 1818 C CA . SER A 259 ? 0.8593 0.8947 1.0047 0.0878 -0.1620 -0.1300 259 SER A CA 1819 C C . SER A 259 ? 0.8500 0.8936 0.9995 0.0969 -0.1666 -0.1430 259 SER A C 1820 O O . SER A 259 ? 0.8672 0.8944 1.0176 0.0948 -0.1672 -0.1427 259 SER A O 1821 C CB . SER A 259 ? 0.7672 0.8122 0.8914 0.0804 -0.1593 -0.1138 259 SER A CB 1822 O OG . SER A 259 ? 0.7909 0.8245 0.9113 0.0709 -0.1561 -0.1014 259 SER A OG 1823 N N . VAL A 260 ? 0.7278 0.7987 0.8798 0.1081 -0.1703 -0.1553 260 VAL A N 1824 C CA . VAL A 260 ? 0.7543 0.8393 0.9041 0.1173 -0.1748 -0.1658 260 VAL A CA 1825 C C . VAL A 260 ? 0.7192 0.8309 0.8472 0.1180 -0.1725 -0.1556 260 VAL A C 1826 O O . VAL A 260 ? 0.8356 0.9720 0.9579 0.1205 -0.1707 -0.1525 260 VAL A O 1827 C CB . VAL A 260 ? 0.6720 0.7695 0.8402 0.1317 -0.1825 -0.1889 260 VAL A CB 1828 C CG1 . VAL A 260 ? 0.7137 0.8221 0.8802 0.1408 -0.1879 -0.2001 260 VAL A CG1 1829 C CG2 . VAL A 260 ? 0.5924 0.6631 0.7844 0.1290 -0.1850 -0.1953 260 VAL A CG2 1830 N N . LEU A 261 ? 0.6361 0.7436 0.7525 0.1157 -0.1726 -0.1490 261 LEU A N 1831 C CA . LEU A 261 ? 0.7528 0.8818 0.8489 0.1141 -0.1704 -0.1350 261 LEU A CA 1832 C C . LEU A 261 ? 0.8100 0.9580 0.9008 0.1260 -0.1748 -0.1446 261 LEU A C 1833 O O . LEU A 261 ? 0.7767 0.9123 0.8778 0.1315 -0.1793 -0.1586 261 LEU A O 1834 C CB . LEU A 261 ? 0.7679 0.8719 0.8522 0.0991 -0.1673 -0.1144 261 LEU A CB 1835 C CG . LEU A 261 ? 0.7976 0.8811 0.8863 0.0880 -0.1638 -0.1056 261 LEU A CG 1836 C CD1 . LEU A 261 ? 0.6712 0.7182 0.7593 0.0793 -0.1637 -0.0997 261 LEU A CD1 1837 C CD2 . LEU A 261 ? 0.9111 1.0114 0.9887 0.0803 -0.1608 -0.0884 261 LEU A CD2 1838 N N . THR A 262 ? 0.8346 1.0153 0.9104 0.1302 -0.1736 -0.1366 262 THR A N 1839 C CA . THR A 262 ? 0.8238 1.0240 0.8908 0.1411 -0.1773 -0.1423 262 THR A CA 1840 C C . THR A 262 ? 0.8544 1.0579 0.9016 0.1319 -0.1741 -0.1176 262 THR A C 1841 O O . THR A 262 ? 0.7899 0.9876 0.8320 0.1189 -0.1697 -0.0986 262 THR A O 1842 C CB . THR A 262 ? 0.7182 0.9615 0.7853 0.1590 -0.1801 -0.1576 262 THR A CB 1843 O OG1 . THR A 262 ? 0.5226 0.7930 0.5821 0.1565 -0.1746 -0.1446 262 THR A OG1 1844 C CG2 . THR A 262 ? 0.6950 0.9316 0.7839 0.1693 -0.1862 -0.1843 262 THR A CG2 1845 N N . ASP A 263 ? 0.8153 1.0272 0.8526 0.1385 -0.1772 -0.1177 263 ASP A N 1846 C CA . ASP A 263 ? 0.6934 0.9076 0.7128 0.1304 -0.1755 -0.0935 263 ASP A CA 1847 C C . ASP A 263 ? 0.6326 0.8795 0.6433 0.1264 -0.1706 -0.0752 263 ASP A C 1848 O O . ASP A 263 ? 0.7614 1.0014 0.7632 0.1130 -0.1686 -0.0510 263 ASP A O 1849 C CB . ASP A 263 ? 0.8558 1.0815 0.8657 0.1414 -0.1800 -0.0980 263 ASP A CB 1850 C CG . ASP A 263 ? 0.9552 1.1436 0.9705 0.1394 -0.1842 -0.1059 263 ASP A CG 1851 O OD1 . ASP A 263 ? 0.9726 1.1681 0.9867 0.1511 -0.1891 -0.1183 263 ASP A OD1 1852 O OD2 . ASP A 263 ? 0.9688 1.1224 0.9895 0.1267 -0.1828 -0.0996 263 ASP A OD2 1853 N N . GLU A 264 ? 0.6655 0.9481 0.6802 0.1382 -0.1692 -0.0871 264 GLU A N 1854 C CA . GLU A 264 ? 0.8188 1.1378 0.8275 0.1358 -0.1639 -0.0712 264 GLU A CA 1855 C C . GLU A 264 ? 0.8359 1.1344 0.8515 0.1189 -0.1601 -0.0584 264 GLU A C 1856 O O . GLU A 264 ? 0.8474 1.1608 0.8572 0.1082 -0.1563 -0.0352 264 GLU A O 1857 C CB . GLU A 264 ? 0.9748 1.3366 0.9872 0.1551 -0.1643 -0.0911 264 GLU A CB 1858 C CG . GLU A 264 ? 1.1929 1.5939 1.1926 0.1718 -0.1663 -0.0950 264 GLU A CG 1859 C CD . GLU A 264 ? 1.3944 1.8134 1.3773 0.1627 -0.1621 -0.0636 264 GLU A CD 1860 O OE1 . GLU A 264 ? 1.3290 1.7514 1.3114 0.1478 -0.1567 -0.0407 264 GLU A OE1 1861 O OE2 . GLU A 264 ? 1.5090 1.9380 1.4803 0.1702 -0.1648 -0.0614 264 GLU A OE2 1862 N N . SER A 265 ? 0.8492 1.1148 0.8785 0.1166 -0.1616 -0.0732 265 SER A N 1863 C CA . SER A 265 ? 0.8372 1.0840 0.8738 0.1033 -0.1587 -0.0648 265 SER A CA 1864 C C . SER A 265 ? 0.9459 1.1680 0.9746 0.0850 -0.1583 -0.0400 265 SER A C 1865 O O . SER A 265 ? 1.1445 1.3688 1.1738 0.0734 -0.1557 -0.0244 265 SER A O 1866 C CB . SER A 265 ? 0.8391 1.0530 0.8910 0.1049 -0.1609 -0.0841 265 SER A CB 1867 O OG . SER A 265 ? 0.7481 0.9778 0.8085 0.1221 -0.1643 -0.1085 265 SER A OG 1868 N N . PHE A 266 ? 0.8904 1.0886 0.9127 0.0831 -0.1618 -0.0373 266 PHE A N 1869 C CA . PHE A 266 ? 0.8292 1.0012 0.8440 0.0676 -0.1637 -0.0156 266 PHE A CA 1870 C C . PHE A 266 ? 0.8242 1.0265 0.8309 0.0605 -0.1619 0.0089 266 PHE A C 1871 O O . PHE A 266 ? 0.7536 0.9438 0.7604 0.0451 -0.1625 0.0280 266 PHE A O 1872 C CB . PHE A 266 ? 0.8285 0.9780 0.8363 0.0706 -0.1685 -0.0179 266 PHE A CB 1873 C CG . PHE A 266 ? 0.9518 1.0717 0.9521 0.0566 -0.1725 0.0023 266 PHE A CG 1874 C CD1 . PHE A 266 ? 1.0492 1.1262 1.0524 0.0512 -0.1758 -0.0024 266 PHE A CD1 1875 C CD2 . PHE A 266 ? 0.9266 1.0623 0.9176 0.0491 -0.1736 0.0264 266 PHE A CD2 1876 C CE1 . PHE A 266 ? 1.0244 1.0732 1.0207 0.0400 -0.1812 0.0140 266 PHE A CE1 1877 C CE2 . PHE A 266 ? 0.9189 1.0244 0.9049 0.0361 -0.1794 0.0446 266 PHE A CE2 1878 C CZ . PHE A 266 ? 0.9704 1.0317 0.9587 0.0322 -0.1838 0.0371 266 PHE A CZ 1879 N N . ASN A 267 ? 0.8180 1.0613 0.8181 0.0722 -0.1602 0.0084 267 ASN A N 1880 C CA . ASN A 267 ? 0.8476 1.1253 0.8396 0.0669 -0.1579 0.0336 267 ASN A CA 1881 C C . ASN A 267 ? 0.8318 1.1318 0.8309 0.0584 -0.1533 0.0449 267 ASN A C 1882 O O . ASN A 267 ? 0.9394 1.2490 0.9369 0.0447 -0.1528 0.0715 267 ASN A O 1883 C CB . ASN A 267 ? 0.9229 1.2438 0.9056 0.0845 -0.1567 0.0279 267 ASN A CB 1884 C CG . ASN A 267 ? 0.9647 1.2643 0.9406 0.0926 -0.1620 0.0176 267 ASN A CG 1885 O OD1 . ASN A 267 ? 0.9845 1.2440 0.9582 0.0822 -0.1663 0.0260 267 ASN A OD1 1886 N ND2 . ASN A 267 ? 0.8532 1.1802 0.8259 0.1121 -0.1626 -0.0017 267 ASN A ND2 1887 N N . GLU A 268 ? 0.7083 1.0149 0.7169 0.0662 -0.1507 0.0248 268 GLU A N 1888 C CA . GLU A 268 ? 0.7461 1.0753 0.7624 0.0609 -0.1465 0.0313 268 GLU A CA 1889 C C . GLU A 268 ? 0.8374 1.1260 0.8621 0.0444 -0.1483 0.0369 268 GLU A C 1890 O O . GLU A 268 ? 0.8946 1.1892 0.9217 0.0299 -0.1477 0.0582 268 GLU A O 1891 C CB . GLU A 268 ? 0.8631 1.2196 0.8855 0.0792 -0.1441 0.0061 268 GLU A CB 1892 C CG . GLU A 268 ? 1.0005 1.3976 1.0149 0.0989 -0.1437 -0.0048 268 GLU A CG 1893 C CD . GLU A 268 ? 1.1010 1.5548 1.1076 0.1005 -0.1387 0.0156 268 GLU A CD 1894 O OE1 . GLU A 268 ? 1.0474 1.5152 1.0587 0.0882 -0.1349 0.0341 268 GLU A OE1 1895 O OE2 . GLU A 268 ? 1.1935 1.6801 1.1898 0.1145 -0.1385 0.0134 268 GLU A OE2 1896 N N . LEU A 269 ? 0.8350 1.0845 0.8649 0.0470 -0.1508 0.0177 269 LEU A N 1897 C CA . LEU A 269 ? 0.7756 0.9845 0.8117 0.0339 -0.1531 0.0204 269 LEU A CA 1898 C C . LEU A 269 ? 0.8429 1.0302 0.8741 0.0164 -0.1574 0.0446 269 LEU A C 1899 O O . LEU A 269 ? 0.8378 1.0144 0.8743 0.0036 -0.1587 0.0554 269 LEU A O 1900 C CB . LEU A 269 ? 0.7444 0.9153 0.7841 0.0401 -0.1553 -0.0004 269 LEU A CB 1901 C CG . LEU A 269 ? 0.7799 0.9580 0.8300 0.0537 -0.1533 -0.0245 269 LEU A CG 1902 C CD1 . LEU A 269 ? 0.6851 0.8328 0.7387 0.0606 -0.1560 -0.0421 269 LEU A CD1 1903 C CD2 . LEU A 269 ? 0.7298 0.9034 0.7891 0.0483 -0.1514 -0.0249 269 LEU A CD2 1904 N N . LEU A 270 ? 0.7950 0.9752 0.8170 0.0162 -0.1608 0.0526 270 LEU A N 1905 C CA . LEU A 270 ? 0.6816 0.8403 0.6995 0.0005 -0.1668 0.0757 270 LEU A CA 1906 C C . LEU A 270 ? 0.8282 1.0176 0.8505 -0.0116 -0.1654 0.0998 270 LEU A C 1907 O O . LEU A 270 ? 0.9537 1.1228 0.9790 -0.0277 -0.1713 0.1178 270 LEU A O 1908 C CB . LEU A 270 ? 0.6356 0.7905 0.6427 0.0048 -0.1703 0.0810 270 LEU A CB 1909 C CG . LEU A 270 ? 0.6628 0.7756 0.6653 -0.0061 -0.1794 0.0936 270 LEU A CG 1910 C CD1 . LEU A 270 ? 0.6657 0.7942 0.6598 -0.0089 -0.1824 0.1154 270 LEU A CD1 1911 C CD2 . LEU A 270 ? 0.6291 0.7182 0.6390 -0.0222 -0.1841 0.1045 270 LEU A CD2 1912 N N . LYS A 271 ? 0.8623 1.1018 0.8858 -0.0034 -0.1583 0.0996 271 LYS A N 1913 C CA . LYS A 271 ? 0.7678 1.0455 0.7972 -0.0132 -0.1552 0.1215 271 LYS A CA 1914 C C . LYS A 271 ? 0.8276 1.0961 0.8692 -0.0229 -0.1553 0.1206 271 LYS A C 1915 O O . LYS A 271 ? 0.7317 1.0197 0.7808 -0.0362 -0.1553 0.1417 271 LYS A O 1916 C CB . LYS A 271 ? 0.7117 1.0492 0.7382 0.0019 -0.1472 0.1182 271 LYS A CB 1917 C CG . LYS A 271 ? 0.8401 1.2016 0.8547 0.0092 -0.1467 0.1280 271 LYS A CG 1918 C CD . LYS A 271 ? 0.8792 1.3043 0.8904 0.0261 -0.1389 0.1230 271 LYS A CD 1919 C CE . LYS A 271 ? 0.9070 1.3605 0.9047 0.0362 -0.1382 0.1312 271 LYS A CE 1920 N NZ . LYS A 271 ? 0.8427 1.3674 0.8372 0.0471 -0.1306 0.1395 271 LYS A NZ 1921 N N . LEU A 272 ? 0.7479 0.9882 0.7922 -0.0164 -0.1555 0.0973 272 LEU A N 1922 C CA . LEU A 272 ? 0.7869 1.0173 0.8414 -0.0239 -0.1559 0.0950 272 LEU A CA 1923 C C . LEU A 272 ? 0.8038 0.9970 0.8612 -0.0425 -0.1643 0.1109 272 LEU A C 1924 O O . LEU A 272 ? 0.7840 0.9805 0.8506 -0.0533 -0.1659 0.1197 272 LEU A O 1925 C CB . LEU A 272 ? 0.8563 1.0650 0.9129 -0.0118 -0.1543 0.0676 272 LEU A CB 1926 C CG . LEU A 272 ? 0.8035 1.0455 0.8623 0.0063 -0.1480 0.0484 272 LEU A CG 1927 C CD1 . LEU A 272 ? 0.7760 0.9869 0.8387 0.0152 -0.1486 0.0244 272 LEU A CD1 1928 C CD2 . LEU A 272 ? 0.6461 0.9314 0.7120 0.0059 -0.1436 0.0548 272 LEU A CD2 1929 N N . LEU A 273 ? 0.8068 0.9647 0.8568 -0.0454 -0.1708 0.1134 273 LEU A N 1930 C CA . LEU A 273 ? 0.7342 0.8522 0.7863 -0.0606 -0.1810 0.1250 273 LEU A CA 1931 C C . LEU A 273 ? 0.8155 0.9524 0.8759 -0.0779 -0.1850 0.1533 273 LEU A C 1932 O O . LEU A 273 ? 0.9002 1.0092 0.9667 -0.0918 -0.1945 0.1628 273 LEU A O 1933 C CB . LEU A 273 ? 0.7313 0.8120 0.7733 -0.0586 -0.1878 0.1227 273 LEU A CB 1934 C CG . LEU A 273 ? 0.7418 0.7988 0.7771 -0.0437 -0.1856 0.0975 273 LEU A CG 1935 C CD1 . LEU A 273 ? 0.6365 0.6471 0.6653 -0.0468 -0.1955 0.0975 273 LEU A CD1 1936 C CD2 . LEU A 273 ? 0.8911 0.9443 0.9324 -0.0384 -0.1811 0.0797 273 LEU A CD2 1937 N N . ARG A 274 ? 0.7611 0.9463 0.8223 -0.0768 -0.1785 0.1671 274 ARG A N 1938 C CA . ARG A 274 ? 0.8073 1.0168 0.8788 -0.0940 -0.1813 0.1968 274 ARG A CA 1939 C C . ARG A 274 ? 0.7607 0.9770 0.8463 -0.1037 -0.1819 0.1989 274 ARG A C 1940 O O . ARG A 274 ? 0.6197 0.8419 0.7175 -0.1215 -0.1878 0.2223 274 ARG A O 1941 C CB . ARG A 274 ? 0.8442 1.1118 0.9135 -0.0884 -0.1723 0.2103 274 ARG A CB 1942 C CG . ARG A 274 ? 0.9370 1.2043 0.9922 -0.0778 -0.1714 0.2090 274 ARG A CG 1943 C CD . ARG A 274 ? 0.9453 1.2757 0.9978 -0.0709 -0.1623 0.2225 274 ARG A CD 1944 N NE . ARG A 274 ? 1.0024 1.3363 1.0401 -0.0574 -0.1609 0.2174 274 ARG A NE 1945 C CZ . ARG A 274 ? 0.9085 1.2936 0.9388 -0.0426 -0.1525 0.2164 274 ARG A CZ 1946 N NH1 . ARG A 274 ? 0.8347 1.2730 0.8709 -0.0390 -0.1443 0.2201 274 ARG A NH1 1947 N NH2 . ARG A 274 ? 0.7877 1.1719 0.8044 -0.0303 -0.1528 0.2107 274 ARG A NH2 1948 N N . TYR A 275 ? 0.7802 0.9957 0.8654 -0.0921 -0.1766 0.1749 275 TYR A N 1949 C CA . TYR A 275 ? 0.8090 1.0326 0.9065 -0.0986 -0.1767 0.1741 275 TYR A CA 1950 C C . TYR A 275 ? 0.8192 0.9902 0.9181 -0.1041 -0.1860 0.1636 275 TYR A C 1951 O O . TYR A 275 ? 0.7968 0.9667 0.9068 -0.1143 -0.1902 0.1686 275 TYR A O 1952 C CB . TYR A 275 ? 0.7748 1.0367 0.8728 -0.0827 -0.1654 0.1572 275 TYR A CB 1953 C CG . TYR A 275 ? 0.8390 1.1613 0.9381 -0.0788 -0.1573 0.1706 275 TYR A CG 1954 C CD1 . TYR A 275 ? 0.8459 1.1863 0.9333 -0.0641 -0.1519 0.1641 275 TYR A CD1 1955 C CD2 . TYR A 275 ? 0.7481 1.1116 0.8600 -0.0895 -0.1553 0.1903 275 TYR A CD2 1956 C CE1 . TYR A 275 ? 0.7657 1.1643 0.8524 -0.0586 -0.1445 0.1759 275 TYR A CE1 1957 C CE2 . TYR A 275 ? 0.8570 1.2801 0.9695 -0.0848 -0.1472 0.2034 275 TYR A CE2 1958 C CZ . TYR A 275 ? 0.8702 1.3109 0.9691 -0.0688 -0.1418 0.1960 275 TYR A CZ 1959 O OH . TYR A 275 ? 0.9022 1.4053 1.0002 -0.0624 -0.1338 0.2088 275 TYR A OH 1960 N N . ILE A 276 ? 0.8239 0.9539 0.9116 -0.0967 -0.1895 0.1494 276 ILE A N 1961 C CA . ILE A 276 ? 0.8498 0.9309 0.9361 -0.0990 -0.1982 0.1382 276 ILE A CA 1962 C C . ILE A 276 ? 0.8232 0.8664 0.9052 -0.1076 -0.2104 0.1482 276 ILE A C 1963 O O . ILE A 276 ? 0.6869 0.6995 0.7579 -0.0986 -0.2123 0.1354 276 ILE A O 1964 C CB . ILE A 276 ? 0.5603 0.6247 0.6381 -0.0815 -0.1922 0.1112 276 ILE A CB 1965 C CG1 . ILE A 276 ? 0.5211 0.5930 0.5892 -0.0689 -0.1862 0.1038 276 ILE A CG1 1966 C CG2 . ILE A 276 ? 0.4791 0.5679 0.5636 -0.0752 -0.1845 0.1006 276 ILE A CG2 1967 C CD1 . ILE A 276 ? 0.4711 0.5325 0.5347 -0.0526 -0.1801 0.0790 276 ILE A CD1 1968 N N . LEU A 277 ? 0.7705 0.8160 0.8628 -0.1250 -0.2193 0.1712 277 LEU A N 1969 C CA . LEU A 277 ? 0.7297 0.7420 0.8202 -0.1342 -0.2324 0.1840 277 LEU A CA 1970 C C . LEU A 277 ? 0.9374 0.8957 1.0218 -0.1315 -0.2440 0.1683 277 LEU A C 1971 O O . LEU A 277 ? 0.8983 0.8251 0.9750 -0.1303 -0.2525 0.1687 277 LEU A O 1972 C CB . LEU A 277 ? 0.5854 0.6118 0.6922 -0.1549 -0.2407 0.2128 277 LEU A CB 1973 C CG . LEU A 277 ? 0.7004 0.7828 0.8117 -0.1572 -0.2297 0.2323 277 LEU A CG 1974 C CD1 . LEU A 277 ? 0.6645 0.7671 0.7954 -0.1788 -0.2366 0.2626 277 LEU A CD1 1975 C CD2 . LEU A 277 ? 0.4992 0.5846 0.5971 -0.1487 -0.2262 0.2358 277 LEU A CD2 1976 N N . GLU A 278 ? 0.9327 0.8824 1.0199 -0.1290 -0.2441 0.1541 278 GLU A N 1977 C CA . GLU A 278 ? 0.7395 0.6430 0.8215 -0.1262 -0.2555 0.1401 278 GLU A CA 1978 C C . GLU A 278 ? 0.8263 0.7117 0.8930 -0.1078 -0.2491 0.1175 278 GLU A C 1979 O O . GLU A 278 ? 0.8524 0.7009 0.9121 -0.1030 -0.2579 0.1060 278 GLU A O 1980 C CB . GLU A 278 ? 0.7819 0.6847 0.8732 -0.1313 -0.2595 0.1359 278 GLU A CB 1981 C CG . GLU A 278 ? 0.9464 0.8666 1.0559 -0.1507 -0.2672 0.1582 278 GLU A CG 1982 C CD . GLU A 278 ? 1.1006 1.0036 1.2156 -0.1642 -0.2809 0.1784 278 GLU A CD 1983 O OE1 . GLU A 278 ? 1.1261 1.0585 1.2543 -0.1781 -0.2804 0.2021 278 GLU A OE1 1984 O OE2 . GLU A 278 ? 1.1149 0.9761 1.2213 -0.1605 -0.2922 0.1712 278 GLU A OE2 1985 N N . LEU A 279 ? 0.8991 0.8120 0.9615 -0.0973 -0.2344 0.1111 279 LEU A N 1986 C CA . LEU A 279 ? 0.8102 0.7107 0.8613 -0.0806 -0.2275 0.0909 279 LEU A CA 1987 C C . LEU A 279 ? 0.7889 0.6513 0.8304 -0.0776 -0.2375 0.0875 279 LEU A C 1988 O O . LEU A 279 ? 0.7959 0.6518 0.8370 -0.0849 -0.2453 0.1017 279 LEU A O 1989 C CB . LEU A 279 ? 0.8416 0.7758 0.8910 -0.0719 -0.2143 0.0885 279 LEU A CB 1990 C CG . LEU A 279 ? 0.8812 0.8205 0.9272 -0.0560 -0.2035 0.0676 279 LEU A CG 1991 C CD1 . LEU A 279 ? 0.8571 0.8171 0.8991 -0.0474 -0.1964 0.0654 279 LEU A CD1 1992 C CD2 . LEU A 279 ? 0.8858 0.7884 0.9253 -0.0487 -0.2071 0.0529 279 LEU A CD2 1993 N N . SER A 280 ? 0.9067 0.7456 0.9408 -0.0663 -0.2373 0.0694 280 SER A N 1994 C CA . SER A 280 ? 0.9063 0.7098 0.9306 -0.0608 -0.2467 0.0631 280 SER A CA 1995 C C . SER A 280 ? 0.8949 0.6943 0.9111 -0.0445 -0.2379 0.0452 280 SER A C 1996 O O . SER A 280 ? 0.9494 0.7233 0.9573 -0.0378 -0.2442 0.0383 280 SER A O 1997 C CB . SER A 280 ? 1.0371 0.8098 1.0611 -0.0644 -0.2609 0.0603 280 SER A CB 1998 O OG . SER A 280 ? 1.0344 0.8070 1.0575 -0.0568 -0.2556 0.0462 280 SER A OG 1999 N N . GLU A 281 ? 0.8486 0.6731 0.8685 -0.0382 -0.2241 0.0377 281 GLU A N 2000 C CA . GLU A 281 ? 0.8482 0.6709 0.8641 -0.0243 -0.2160 0.0223 281 GLU A CA 2001 C C . GLU A 281 ? 0.8259 0.6808 0.8483 -0.0195 -0.2032 0.0185 281 GLU A C 2002 O O . GLU A 281 ? 0.7609 0.6355 0.7907 -0.0219 -0.1977 0.0192 281 GLU A O 2003 C CB . GLU A 281 ? 0.9794 0.7850 0.9933 -0.0174 -0.2158 0.0102 281 GLU A CB 2004 C CG . GLU A 281 ? 1.1582 0.9646 1.1714 -0.0043 -0.2067 -0.0037 281 GLU A CG 2005 C CD . GLU A 281 ? 1.2468 1.0375 1.2569 0.0027 -0.2070 -0.0128 281 GLU A CD 2006 O OE1 . GLU A 281 ? 1.0978 0.8799 1.1065 -0.0019 -0.2133 -0.0101 281 GLU A OE1 2007 O OE2 . GLU A 281 ? 1.2984 1.0871 1.3080 0.0129 -0.2011 -0.0222 281 GLU A OE2 2008 N N . VAL A 282 ? 0.8575 0.7174 0.8772 -0.0120 -0.1996 0.0135 282 VAL A N 2009 C CA . VAL A 282 ? 0.8308 0.7176 0.8569 -0.0045 -0.1892 0.0055 282 VAL A CA 2010 C C . VAL A 282 ? 0.6895 0.5659 0.7169 0.0069 -0.1849 -0.0100 282 VAL A C 2011 O O . VAL A 282 ? 0.6182 0.4748 0.6392 0.0107 -0.1890 -0.0130 282 VAL A O 2012 C CB . VAL A 282 ? 0.6869 0.5965 0.7113 -0.0041 -0.1880 0.0118 282 VAL A CB 2013 C CG1 . VAL A 282 ? 0.7245 0.6692 0.7568 -0.0012 -0.1799 0.0090 282 VAL A CG1 2014 C CG2 . VAL A 282 ? 0.5741 0.4804 0.5933 -0.0152 -0.1963 0.0304 282 VAL A CG2 2015 N N . GLU A 283 ? 0.6693 0.5600 0.7064 0.0124 -0.1770 -0.0194 283 GLU A N 2016 C CA . GLU A 283 ? 0.7673 0.6507 0.8097 0.0218 -0.1727 -0.0323 283 GLU A CA 2017 C C . GLU A 283 ? 0.7970 0.7036 0.8506 0.0284 -0.1667 -0.0413 283 GLU A C 2018 O O . GLU A 283 ? 0.8401 0.7672 0.8992 0.0271 -0.1641 -0.0404 283 GLU A O 2019 C CB . GLU A 283 ? 1.0062 0.8752 1.0511 0.0225 -0.1712 -0.0351 283 GLU A CB 2020 C CG . GLU A 283 ? 1.1741 1.0383 1.2270 0.0313 -0.1659 -0.0456 283 GLU A CG 2021 C CD . GLU A 283 ? 1.2238 1.0710 1.2741 0.0329 -0.1657 -0.0457 283 GLU A CD 2022 O OE1 . GLU A 283 ? 1.1497 0.9921 1.1951 0.0280 -0.1685 -0.0401 283 GLU A OE1 2023 O OE2 . GLU A 283 ? 1.2185 1.0591 1.2719 0.0395 -0.1630 -0.0511 283 GLU A OE2 2024 N N . PHE A 284 ? 0.7507 0.6548 0.8085 0.0360 -0.1654 -0.0507 284 PHE A N 2025 C CA . PHE A 284 ? 0.6857 0.6076 0.7565 0.0434 -0.1617 -0.0621 284 PHE A CA 2026 C C . PHE A 284 ? 0.7446 0.6532 0.8260 0.0483 -0.1592 -0.0706 284 PHE A C 2027 O O . PHE A 284 ? 0.8056 0.7010 0.8831 0.0505 -0.1607 -0.0717 284 PHE A O 2028 C CB . PHE A 284 ? 0.6286 0.5638 0.6955 0.0478 -0.1640 -0.0647 284 PHE A CB 2029 C CG . PHE A 284 ? 0.6873 0.6426 0.7457 0.0440 -0.1654 -0.0553 284 PHE A CG 2030 C CD1 . PHE A 284 ? 0.6550 0.6386 0.7201 0.0482 -0.1629 -0.0601 284 PHE A CD1 2031 C CD2 . PHE A 284 ? 0.6265 0.5735 0.6714 0.0365 -0.1698 -0.0410 284 PHE A CD2 2032 C CE1 . PHE A 284 ? 0.6995 0.7067 0.7572 0.0452 -0.1632 -0.0500 284 PHE A CE1 2033 C CE2 . PHE A 284 ? 0.7461 0.7142 0.7855 0.0318 -0.1706 -0.0294 284 PHE A CE2 2034 C CZ . PHE A 284 ? 0.7416 0.7418 0.7870 0.0363 -0.1666 -0.0335 284 PHE A CZ 2035 N N . ASP A 285 ? 0.6940 0.6069 0.7895 0.0501 -0.1555 -0.0756 285 ASP A N 2036 C CA . ASP A 285 ? 0.8062 0.7092 0.9150 0.0539 -0.1527 -0.0813 285 ASP A CA 2037 C C . ASP A 285 ? 0.9978 0.9112 1.1232 0.0604 -0.1532 -0.0932 285 ASP A C 2038 O O . ASP A 285 ? 1.3325 1.2533 1.4540 0.0636 -0.1562 -0.0977 285 ASP A O 2039 C CB . ASP A 285 ? 1.0411 0.9393 1.1573 0.0520 -0.1492 -0.0783 285 ASP A CB 2040 C CG . ASP A 285 ? 1.1795 1.0601 1.2853 0.0496 -0.1484 -0.0705 285 ASP A CG 2041 O OD1 . ASP A 285 ? 0.9883 0.8603 1.0789 0.0481 -0.1519 -0.0668 285 ASP A OD1 2042 O OD2 . ASP A 285 ? 1.3510 1.2268 1.4639 0.0501 -0.1449 -0.0683 285 ASP A OD2 2043 N N . ASP A 286 ? 0.7770 0.6904 0.9217 0.0624 -0.1511 -0.0982 286 ASP A N 2044 C CA . ASP A 286 ? 0.8207 0.7413 0.9851 0.0682 -0.1532 -0.1103 286 ASP A CA 2045 C C . ASP A 286 ? 0.8326 0.7729 0.9974 0.0731 -0.1573 -0.1196 286 ASP A C 2046 O O . ASP A 286 ? 0.8721 0.8209 1.0512 0.0767 -0.1590 -0.1272 286 ASP A O 2047 C CB . ASP A 286 ? 0.8529 0.7679 1.0402 0.0683 -0.1513 -0.1117 286 ASP A CB 2048 C CG . ASP A 286 ? 1.0946 0.9954 1.2831 0.0653 -0.1468 -0.1027 286 ASP A CG 2049 O OD1 . ASP A 286 ? 1.2839 1.1833 1.4866 0.0671 -0.1469 -0.1060 286 ASP A OD1 2050 O OD2 . ASP A 286 ? 1.0255 0.9186 1.2013 0.0619 -0.1434 -0.0927 286 ASP A OD2 2051 N N . CYS A 287 ? 0.6527 0.6009 0.8015 0.0743 -0.1594 -0.1187 287 CYS A N 2052 C CA . CYS A 287 ? 0.5226 0.4936 0.6668 0.0793 -0.1623 -0.1245 287 CYS A CA 2053 C C . CYS A 287 ? 0.6443 0.6250 0.7951 0.0876 -0.1670 -0.1374 287 CYS A C 2054 O O . CYS A 287 ? 0.7436 0.7139 0.8936 0.0874 -0.1677 -0.1372 287 CYS A O 2055 C CB . CYS A 287 ? 0.4532 0.4295 0.5744 0.0741 -0.1614 -0.1114 287 CYS A CB 2056 S SG . CYS A 287 ? 0.6958 0.6727 0.8101 0.0659 -0.1581 -0.0990 287 CYS A SG 2057 N N . THR A 288 ? 0.5371 0.5388 0.6949 0.0961 -0.1708 -0.1497 288 THR A N 2058 C CA . THR A 288 ? 0.6525 0.6669 0.8141 0.1053 -0.1764 -0.1627 288 THR A CA 2059 C C . THR A 288 ? 0.6371 0.6739 0.7769 0.1092 -0.1770 -0.1587 288 THR A C 2060 O O . THR A 288 ? 0.6025 0.6585 0.7349 0.1107 -0.1758 -0.1558 288 THR A O 2061 C CB . THR A 288 ? 0.7179 0.7411 0.9033 0.1147 -0.1826 -0.1821 288 THR A CB 2062 O OG1 . THR A 288 ? 0.7380 0.7414 0.9458 0.1119 -0.1840 -0.1862 288 THR A OG1 2063 C CG2 . THR A 288 ? 0.6778 0.7237 0.8608 0.1267 -0.1892 -0.1963 288 THR A CG2 2064 N N . LEU A 289 ? 0.5319 0.5677 0.6619 0.1107 -0.1788 -0.1570 289 LEU A N 2065 C CA . LEU A 289 ? 0.5656 0.6250 0.6772 0.1159 -0.1802 -0.1535 289 LEU A CA 2066 C C . LEU A 289 ? 0.5885 0.6670 0.7073 0.1299 -0.1868 -0.1722 289 LEU A C 2067 O O . LEU A 289 ? 0.6452 0.7156 0.7658 0.1324 -0.1900 -0.1769 289 LEU A O 2068 C CB . LEU A 289 ? 0.4851 0.5317 0.5777 0.1085 -0.1787 -0.1366 289 LEU A CB 2069 C CG . LEU A 289 ? 0.5255 0.5953 0.6000 0.1136 -0.1806 -0.1307 289 LEU A CG 2070 C CD1 . LEU A 289 ? 0.4171 0.5163 0.4844 0.1148 -0.1781 -0.1247 289 LEU A CD1 2071 C CD2 . LEU A 289 ? 0.3885 0.4397 0.4470 0.1055 -0.1806 -0.1136 289 LEU A CD2 2072 N N . ASN A 290 ? 0.5665 0.6707 0.6899 0.1398 -0.1895 -0.1840 290 ASN A N 2073 C CA . ASN A 290 ? 0.6447 0.7733 0.7721 0.1555 -0.1969 -0.2031 290 ASN A CA 2074 C C . ASN A 290 ? 0.7522 0.9058 0.8549 0.1601 -0.1959 -0.1933 290 ASN A C 2075 O O . ASN A 290 ? 0.7178 0.9031 0.8104 0.1675 -0.1952 -0.1927 290 ASN A O 2076 C CB . ASN A 290 ? 0.6034 0.7515 0.7433 0.1658 -0.2009 -0.2194 290 ASN A CB 2077 C CG . ASN A 290 ? 0.5609 0.6863 0.7295 0.1646 -0.2052 -0.2329 290 ASN A CG 2078 O OD1 . ASN A 290 ? 0.5637 0.6695 0.7474 0.1623 -0.2086 -0.2389 290 ASN A OD1 2079 N ND2 . ASN A 290 ? 0.3290 0.4588 0.5064 0.1663 -0.2054 -0.2373 290 ASN A ND2 2080 N N . GLY A 291 ? 0.6937 0.8339 0.7870 0.1561 -0.1959 -0.1849 291 GLY A N 2081 C CA . GLY A 291 ? 0.6941 0.8497 0.7636 0.1566 -0.1945 -0.1696 291 GLY A CA 2082 C C . GLY A 291 ? 0.7055 0.8378 0.7707 0.1527 -0.1963 -0.1646 291 GLY A C 2083 O O . GLY A 291 ? 0.8113 0.9224 0.8926 0.1521 -0.1988 -0.1757 291 GLY A O 2084 N N . LEU A 292 ? 0.6098 0.7466 0.6541 0.1502 -0.1954 -0.1471 292 LEU A N 2085 C CA . LEU A 292 ? 0.7203 0.8394 0.7584 0.1498 -0.1986 -0.1437 292 LEU A CA 2086 C C . LEU A 292 ? 0.7496 0.8591 0.7678 0.1396 -0.1964 -0.1179 292 LEU A C 2087 O O . LEU A 292 ? 0.7956 0.8985 0.8028 0.1414 -0.2000 -0.1117 292 LEU A O 2088 C CB . LEU A 292 ? 0.6970 0.8402 0.7319 0.1657 -0.2049 -0.1574 292 LEU A CB 2089 C CG . LEU A 292 ? 0.6600 0.8126 0.7153 0.1782 -0.2108 -0.1855 292 LEU A CG 2090 C CD1 . LEU A 292 ? 0.6139 0.7928 0.6603 0.1939 -0.2173 -0.1952 292 LEU A CD1 2091 C CD2 . LEU A 292 ? 0.7369 0.8583 0.8122 0.1726 -0.2123 -0.1942 292 LEU A CD2 2092 N N . GLY A 293 ? 0.6847 0.7934 0.6992 0.1290 -0.1916 -0.1030 293 GLY A N 2093 C CA . GLY A 293 ? 0.7673 0.8642 0.7665 0.1174 -0.1909 -0.0779 293 GLY A CA 2094 C C . GLY A 293 ? 0.8693 0.9963 0.8519 0.1209 -0.1916 -0.0629 293 GLY A C 2095 O O . GLY A 293 ? 0.8517 0.9677 0.8220 0.1129 -0.1935 -0.0420 293 GLY A O 2096 N N . ASP A 294 ? 0.8937 1.0594 0.8765 0.1335 -0.1906 -0.0732 294 ASP A N 2097 C CA . ASP A 294 ? 0.9946 1.1972 0.9616 0.1385 -0.1899 -0.0584 294 ASP A CA 2098 C C . ASP A 294 ? 1.0267 1.2443 0.9908 0.1272 -0.1843 -0.0375 294 ASP A C 2099 O O . ASP A 294 ? 1.0177 1.2736 0.9820 0.1342 -0.1806 -0.0404 294 ASP A O 2100 C CB . ASP A 294 ? 1.0768 1.3182 1.0447 0.1584 -0.1916 -0.0793 294 ASP A CB 2101 C CG . ASP A 294 ? 1.1202 1.3990 1.0695 0.1674 -0.1922 -0.0659 294 ASP A CG 2102 O OD1 . ASP A 294 ? 1.0733 1.3935 1.0201 0.1836 -0.1923 -0.0786 294 ASP A OD1 2103 O OD2 . ASP A 294 ? 1.0601 1.3269 0.9971 0.1589 -0.1932 -0.0429 294 ASP A OD2 2104 N N . PHE A 295 ? 0.9520 1.1401 0.9139 0.1103 -0.1844 -0.0172 295 PHE A N 2105 C CA . PHE A 295 ? 0.9268 1.1238 0.8892 0.0972 -0.1801 0.0026 295 PHE A CA 2106 C C . PHE A 295 ? 0.9352 1.1619 0.8846 0.0939 -0.1795 0.0298 295 PHE A C 2107 O O . PHE A 295 ? 0.8689 1.0831 0.8086 0.0915 -0.1842 0.0435 295 PHE A O 2108 C CB . PHE A 295 ? 0.8870 1.0385 0.8547 0.0805 -0.1820 0.0111 295 PHE A CB 2109 C CG . PHE A 295 ? 0.9496 1.0721 0.9297 0.0826 -0.1821 -0.0116 295 PHE A CG 2110 C CD1 . PHE A 295 ? 0.8903 0.9702 0.8712 0.0764 -0.1863 -0.0120 295 PHE A CD1 2111 C CD2 . PHE A 295 ? 1.0042 1.1430 0.9958 0.0912 -0.1784 -0.0318 295 PHE A CD2 2112 C CE1 . PHE A 295 ? 0.8858 0.9433 0.8785 0.0784 -0.1854 -0.0304 295 PHE A CE1 2113 C CE2 . PHE A 295 ? 0.8355 0.9484 0.8402 0.0922 -0.1785 -0.0498 295 PHE A CE2 2114 C CZ . PHE A 295 ? 0.7932 0.8671 0.7983 0.0855 -0.1814 -0.0482 295 PHE A CZ 2115 N N . ASN A 296 ? 0.8909 1.1577 0.8406 0.0939 -0.1737 0.0386 296 ASN A N 2116 C CA . ASN A 296 ? 0.8425 1.1388 0.7828 0.0872 -0.1721 0.0694 296 ASN A CA 2117 C C . ASN A 296 ? 0.8741 1.1757 0.8220 0.0704 -0.1684 0.0894 296 ASN A C 2118 O O . ASN A 296 ? 0.7905 1.1352 0.7406 0.0740 -0.1621 0.0919 296 ASN A O 2119 C CB . ASN A 296 ? 0.8019 1.1537 0.7322 0.1053 -0.1689 0.0667 296 ASN A CB 2120 C CG . ASN A 296 ? 1.1340 1.4800 1.0574 0.1218 -0.1740 0.0469 296 ASN A CG 2121 O OD1 . ASN A 296 ? 1.0675 1.4086 0.9797 0.1221 -0.1780 0.0606 296 ASN A OD1 2122 N ND2 . ASN A 296 ? 1.3545 1.6987 1.2861 0.1351 -0.1747 0.0145 296 ASN A ND2 2123 N N . PRO A 297 ? 0.8666 1.1243 0.8188 0.0526 -0.1732 0.1026 297 PRO A N 2124 C CA . PRO A 297 ? 0.8451 1.0970 0.8063 0.0343 -0.1724 0.1212 297 PRO A CA 2125 C C . PRO A 297 ? 0.8992 1.1889 0.8575 0.0258 -0.1704 0.1540 297 PRO A C 2126 O O . PRO A 297 ? 0.9821 1.2689 0.9320 0.0233 -0.1749 0.1723 297 PRO A O 2127 C CB . PRO A 297 ? 0.7225 0.9158 0.6854 0.0213 -0.1812 0.1260 297 PRO A CB 2128 C CG . PRO A 297 ? 0.7159 0.8845 0.6740 0.0346 -0.1842 0.1021 297 PRO A CG 2129 C CD . PRO A 297 ? 0.7951 1.0040 0.7440 0.0510 -0.1810 0.0972 297 PRO A CD 2130 N N . SER A 298 ? 0.9332 1.2586 0.8989 0.0215 -0.1640 0.1624 298 SER A N 2131 C CA . SER A 298 ? 0.8713 1.2316 0.8378 0.0098 -0.1621 0.1972 298 SER A CA 2132 C C . SER A 298 ? 0.9075 1.2263 0.8758 -0.0094 -0.1719 0.2227 298 SER A C 2133 O O . SER A 298 ? 0.8665 1.1313 0.8384 -0.0162 -0.1793 0.2127 298 SER A O 2134 C CB . SER A 298 ? 0.9822 1.3709 0.9611 0.0023 -0.1560 0.2027 298 SER A CB 2135 O OG . SER A 298 ? 1.1388 1.5564 1.1175 0.0207 -0.1491 0.1750 298 SER A OG 2136 N N . GLU A 299 ? 1.0327 1.3775 0.9987 -0.0175 -0.1726 0.2557 299 GLU A N 2137 C CA . GLU A 299 ? 1.1425 1.4481 1.1104 -0.0345 -0.1838 0.2809 299 GLU A CA 2138 C C . GLU A 299 ? 1.1102 1.3900 1.0951 -0.0575 -0.1897 0.2967 299 GLU A C 2139 O O . GLU A 299 ? 1.0404 1.2685 1.0290 -0.0698 -0.2019 0.3037 299 GLU A O 2140 C CB . GLU A 299 ? 1.3277 1.6691 1.2881 -0.0350 -0.1833 0.3125 299 GLU A CB 2141 C CG . GLU A 299 ? 1.4983 1.8342 1.4412 -0.0175 -0.1856 0.3014 299 GLU A CG 2142 C CD . GLU A 299 ? 1.5846 1.8548 1.5258 -0.0243 -0.1991 0.3009 299 GLU A CD 2143 O OE1 . GLU A 299 ? 1.6020 1.8526 1.5321 -0.0088 -0.2013 0.2772 299 GLU A OE1 2144 O OE2 . GLU A 299 ? 1.5554 1.7945 1.5071 -0.0445 -0.2083 0.3235 299 GLU A OE2 2145 N N . SER A 300 ? 1.0764 1.3927 1.0718 -0.0623 -0.1820 0.3011 300 SER A N 2146 C CA . SER A 300 ? 1.0377 1.3322 1.0504 -0.0824 -0.1873 0.3112 300 SER A CA 2147 C C . SER A 300 ? 1.1623 1.3940 1.1750 -0.0817 -0.1951 0.2843 300 SER A C 2148 O O . SER A 300 ? 1.2413 1.4278 1.2612 -0.0966 -0.2073 0.2938 300 SER A O 2149 C CB . SER A 300 ? 1.0163 1.3587 1.0382 -0.0815 -0.1765 0.3087 300 SER A CB 2150 O OG . SER A 300 ? 1.1196 1.5277 1.1346 -0.0696 -0.1656 0.3175 300 SER A OG 2151 N N . ASP A 301 ? 1.1391 1.3697 1.1442 -0.0634 -0.1887 0.2509 301 ASP A N 2152 C CA . ASP A 301 ? 1.0694 1.2491 1.0748 -0.0604 -0.1935 0.2239 301 ASP A CA 2153 C C . ASP A 301 ? 1.0605 1.1890 1.0584 -0.0608 -0.2048 0.2219 301 ASP A C 2154 O O . ASP A 301 ? 1.2211 1.3033 1.2223 -0.0659 -0.2127 0.2119 301 ASP A O 2155 C CB . ASP A 301 ? 1.1120 1.3063 1.1127 -0.0407 -0.1841 0.1912 301 ASP A CB 2156 C CG . ASP A 301 ? 1.1301 1.3771 1.1369 -0.0367 -0.1735 0.1904 301 ASP A CG 2157 O OD1 . ASP A 301 ? 1.0712 1.3353 1.0884 -0.0512 -0.1734 0.2112 301 ASP A OD1 2158 O OD2 . ASP A 301 ? 1.1300 1.4015 1.1321 -0.0186 -0.1663 0.1683 301 ASP A OD2 2159 N N . VAL A 302 ? 1.0548 1.1926 1.0420 -0.0541 -0.2060 0.2308 302 VAL A N 2160 C CA . VAL A 302 ? 1.0676 1.1587 1.0469 -0.0519 -0.2167 0.2268 302 VAL A CA 2161 C C . VAL A 302 ? 1.0523 1.1091 1.0385 -0.0711 -0.2308 0.2527 302 VAL A C 2162 O O . VAL A 302 ? 1.0656 1.0727 1.0496 -0.0721 -0.2422 0.2452 302 VAL A O 2163 C CB . VAL A 302 ? 0.8732 0.9835 0.8381 -0.0359 -0.2138 0.2237 302 VAL A CB 2164 C CG1 . VAL A 302 ? 0.7581 0.8215 0.7155 -0.0348 -0.2260 0.2234 302 VAL A CG1 2165 C CG2 . VAL A 302 ? 0.6752 0.8072 0.6353 -0.0161 -0.2034 0.1918 302 VAL A CG2 2166 N N . VAL A 303 ? 1.0604 1.1446 1.0563 -0.0861 -0.2309 0.2829 303 VAL A N 2167 C CA . VAL A 303 ? 1.1309 1.1833 1.1386 -0.1068 -0.2454 0.3079 303 VAL A CA 2168 C C . VAL A 303 ? 1.0687 1.0836 1.0872 -0.1152 -0.2522 0.2937 303 VAL A C 2169 O O . VAL A 303 ? 0.9928 0.9610 1.0166 -0.1253 -0.2679 0.2990 303 VAL A O 2170 C CB . VAL A 303 ? 1.0841 1.1802 1.1032 -0.1221 -0.2428 0.3447 303 VAL A CB 2171 C CG1 . VAL A 303 ? 1.0668 1.1276 1.0996 -0.1438 -0.2603 0.3731 303 VAL A CG1 2172 C CG2 . VAL A 303 ? 0.9514 1.0949 0.9584 -0.1108 -0.2334 0.3568 303 VAL A CG2 2173 N N . SER A 304 ? 1.0193 1.0552 1.0406 -0.1098 -0.2411 0.2750 304 SER A N 2174 C CA . SER A 304 ? 1.0319 1.0393 1.0622 -0.1157 -0.2455 0.2606 304 SER A CA 2175 C C . SER A 304 ? 1.1051 1.0606 1.1268 -0.1061 -0.2530 0.2346 304 SER A C 2176 O O . SER A 304 ? 1.1237 1.0459 1.1515 -0.1118 -0.2613 0.2261 304 SER A O 2177 C CB . SER A 304 ? 1.0633 1.1084 1.0968 -0.1091 -0.2309 0.2457 304 SER A CB 2178 O OG . SER A 304 ? 1.1321 1.2321 1.1714 -0.1139 -0.2222 0.2669 304 SER A OG 2179 N N . GLU A 305 ? 1.0967 1.0482 1.1045 -0.0906 -0.2500 0.2215 305 GLU A N 2180 C CA . GLU A 305 ? 1.0264 0.9346 1.0259 -0.0798 -0.2557 0.1973 305 GLU A CA 2181 C C . GLU A 305 ? 1.0258 0.9245 1.0289 -0.0757 -0.2510 0.1737 305 GLU A C 2182 O O . GLU A 305 ? 1.1784 1.0369 1.1810 -0.0755 -0.2602 0.1623 305 GLU A O 2183 C CB . GLU A 305 ? 0.9641 0.8251 0.9645 -0.0886 -0.2745 0.2082 305 GLU A CB 2184 C CG . GLU A 305 ? 1.0818 0.9489 1.0814 -0.0958 -0.2814 0.2365 305 GLU A CG 2185 C CD . GLU A 305 ? 1.1780 0.9932 1.1771 -0.1005 -0.3014 0.2426 305 GLU A CD 2186 O OE1 . GLU A 305 ? 1.0717 0.8738 1.0592 -0.0901 -0.3051 0.2395 305 GLU A OE1 2187 O OE2 . GLU A 305 ? 1.2627 1.0503 1.2732 -0.1139 -0.3144 0.2494 305 GLU A OE2 2188 N N . LEU A 306 ? 0.9360 0.8726 0.9426 -0.0716 -0.2372 0.1666 306 LEU A N 2189 C CA . LEU A 306 ? 0.9771 0.9082 0.9877 -0.0673 -0.2319 0.1457 306 LEU A CA 2190 C C . LEU A 306 ? 0.9572 0.8682 0.9778 -0.0809 -0.2403 0.1515 306 LEU A C 2191 O O . LEU A 306 ? 1.0695 0.9605 1.0903 -0.0765 -0.2404 0.1335 306 LEU A O 2192 C CB . LEU A 306 ? 0.9636 0.8657 0.9658 -0.0530 -0.2320 0.1205 306 LEU A CB 2193 C CG . LEU A 306 ? 0.8108 0.7328 0.8085 -0.0365 -0.2201 0.1005 306 LEU A CG 2194 C CD1 . LEU A 306 ? 0.6531 0.5459 0.6495 -0.0280 -0.2203 0.0781 306 LEU A CD1 2195 C CD2 . LEU A 306 ? 0.7998 0.7645 0.8043 -0.0352 -0.2085 0.0994 306 LEU A CD2 2196 N N . GLY A 307 ? 0.8824 0.7993 0.9120 -0.0973 -0.2476 0.1767 307 GLY A N 2197 C CA . GLY A 307 ? 0.8534 0.7546 0.8949 -0.1113 -0.2567 0.1834 307 GLY A CA 2198 C C . GLY A 307 ? 0.9419 0.7926 0.9808 -0.1096 -0.2694 0.1683 307 GLY A C 2199 O O . GLY A 307 ? 1.0019 0.8188 1.0343 -0.1075 -0.2808 0.1678 307 GLY A O 2200 N N . LYS A 308 ? 0.9959 0.8426 1.0394 -0.1095 -0.2680 0.1556 308 LYS A N 2201 C CA . LYS A 308 ? 0.9507 0.7542 0.9912 -0.1065 -0.2798 0.1408 308 LYS A CA 2202 C C . LYS A 308 ? 0.9093 0.7035 0.9377 -0.0878 -0.2713 0.1144 308 LYS A C 2203 O O . LYS A 308 ? 1.0127 0.7794 1.0377 -0.0826 -0.2776 0.0997 308 LYS A O 2204 C CB . LYS A 308 ? 0.8651 0.6674 0.9181 -0.1177 -0.2858 0.1438 308 LYS A CB 2205 C CG . LYS A 308 ? 0.8434 0.6327 0.9096 -0.1366 -0.3027 0.1664 308 LYS A CG 2206 C CD . LYS A 308 ? 0.9664 0.7777 1.0490 -0.1502 -0.3027 0.1764 308 LYS A CD 2207 C CE . LYS A 308 ? 1.0512 0.8518 1.1507 -0.1709 -0.3201 0.2016 308 LYS A CE 2208 N NZ . LYS A 308 ? 0.9999 0.8352 1.1182 -0.1860 -0.3171 0.2176 308 LYS A NZ 2209 N N . VAL A 309 ? 0.7610 0.5797 0.7838 -0.0777 -0.2576 0.1087 309 VAL A N 2210 C CA . VAL A 309 ? 0.8036 0.6167 0.8179 -0.0610 -0.2491 0.0859 309 VAL A CA 2211 C C . VAL A 309 ? 0.9251 0.7032 0.9291 -0.0530 -0.2584 0.0777 309 VAL A C 2212 O O . VAL A 309 ? 1.0072 0.7839 1.0061 -0.0510 -0.2608 0.0839 309 VAL A O 2213 C CB . VAL A 309 ? 0.7368 0.5858 0.7502 -0.0524 -0.2338 0.0813 309 VAL A CB 2214 C CG1 . VAL A 309 ? 0.6738 0.5122 0.6799 -0.0365 -0.2285 0.0609 309 VAL A CG1 2215 C CG2 . VAL A 309 ? 0.6991 0.5788 0.7213 -0.0544 -0.2238 0.0802 309 VAL A CG2 2216 N N . GLU A 310 ? 0.9145 0.6661 0.9151 -0.0473 -0.2637 0.0637 310 GLU A N 2217 C CA . GLU A 310 ? 0.9762 0.6942 0.9673 -0.0388 -0.2742 0.0548 310 GLU A CA 2218 C C . GLU A 310 ? 0.8422 0.5649 0.8268 -0.0226 -0.2632 0.0368 310 GLU A C 2219 O O . GLU A 310 ? 0.8541 0.5614 0.8309 -0.0140 -0.2675 0.0311 310 GLU A O 2220 C CB . GLU A 310 ? 1.2830 0.9711 1.2736 -0.0400 -0.2876 0.0490 310 GLU A CB 2221 C CG . GLU A 310 ? 1.5396 1.2198 1.5399 -0.0570 -0.3010 0.0658 310 GLU A CG 2222 C CD . GLU A 310 ? 1.7860 1.4466 1.7866 -0.0643 -0.3158 0.0808 310 GLU A CD 2223 O OE1 . GLU A 310 ? 1.9238 1.5775 1.9156 -0.0552 -0.3154 0.0775 310 GLU A OE1 2224 O OE2 . GLU A 310 ? 1.7844 1.4365 1.7952 -0.0793 -0.3285 0.0965 310 GLU A OE2 2225 N N . THR A 311 ? 0.7756 0.5200 0.7647 -0.0188 -0.2497 0.0284 311 THR A N 2226 C CA . THR A 311 ? 0.8050 0.5528 0.7914 -0.0047 -0.2399 0.0116 311 THR A CA 2227 C C . THR A 311 ? 0.7933 0.5735 0.7864 -0.0022 -0.2255 0.0094 311 THR A C 2228 O O . THR A 311 ? 0.9001 0.7014 0.9006 -0.0083 -0.2196 0.0142 311 THR A O 2229 C CB . THR A 311 ? 0.9663 0.7034 0.9522 0.0008 -0.2390 0.0002 311 THR A CB 2230 O OG1 . THR A 311 ? 1.0761 0.7828 1.0546 0.0015 -0.2538 -0.0011 311 THR A OG1 2231 C CG2 . THR A 311 ? 0.7855 0.5288 0.7712 0.0141 -0.2284 -0.0141 311 THR A CG2 2232 N N . VAL A 312 ? 0.6394 0.4236 0.6305 0.0077 -0.2209 0.0011 312 VAL A N 2233 C CA . VAL A 312 ? 0.7231 0.5358 0.7209 0.0121 -0.2095 -0.0037 312 VAL A CA 2234 C C . VAL A 312 ? 0.7050 0.5150 0.7060 0.0235 -0.2031 -0.0196 312 VAL A C 2235 O O . VAL A 312 ? 0.8090 0.6031 0.8044 0.0304 -0.2070 -0.0252 312 VAL A O 2236 C CB . VAL A 312 ? 0.7439 0.5677 0.7378 0.0127 -0.2112 0.0027 312 VAL A CB 2237 C CG1 . VAL A 312 ? 0.6356 0.4819 0.6350 0.0224 -0.2019 -0.0088 312 VAL A CG1 2238 C CG2 . VAL A 312 ? 0.7191 0.5576 0.7135 0.0012 -0.2139 0.0205 312 VAL A CG2 2239 N N . THR A 313 ? 0.5693 0.3953 0.5804 0.0256 -0.1938 -0.0262 313 THR A N 2240 C CA . THR A 313 ? 0.7437 0.5672 0.7607 0.0349 -0.1880 -0.0387 313 THR A CA 2241 C C . THR A 313 ? 0.8129 0.6591 0.8427 0.0395 -0.1797 -0.0467 313 THR A C 2242 O O . THR A 313 ? 0.8140 0.6760 0.8517 0.0368 -0.1751 -0.0464 313 THR A O 2243 C CB . THR A 313 ? 0.7840 0.5977 0.8027 0.0348 -0.1862 -0.0407 313 THR A CB 2244 O OG1 . THR A 313 ? 0.8918 0.6846 0.8993 0.0311 -0.1956 -0.0350 313 THR A OG1 2245 C CG2 . THR A 313 ? 0.5749 0.3860 0.5991 0.0443 -0.1808 -0.0505 313 THR A CG2 2246 N N . ILE A 314 ? 0.7200 0.5673 0.7528 0.0472 -0.1787 -0.0547 314 ILE A N 2247 C CA . ILE A 314 ? 0.7025 0.5691 0.7493 0.0524 -0.1730 -0.0642 314 ILE A CA 2248 C C . ILE A 314 ? 0.7105 0.5718 0.7686 0.0586 -0.1690 -0.0733 314 ILE A C 2249 O O . ILE A 314 ? 0.7490 0.6001 0.8030 0.0633 -0.1713 -0.0757 314 ILE A O 2250 C CB . ILE A 314 ? 0.6996 0.5785 0.7425 0.0557 -0.1760 -0.0653 314 ILE A CB 2251 C CG1 . ILE A 314 ? 0.5436 0.4328 0.5774 0.0488 -0.1787 -0.0535 314 ILE A CG1 2252 C CG2 . ILE A 314 ? 0.3358 0.2339 0.3940 0.0630 -0.1723 -0.0782 314 ILE A CG2 2253 C CD1 . ILE A 314 ? 0.6428 0.5320 0.6647 0.0493 -0.1846 -0.0469 314 ILE A CD1 2254 N N . ARG A 315 ? 0.6616 0.5306 0.7346 0.0588 -0.1633 -0.0772 315 ARG A N 2255 C CA . ARG A 315 ? 0.6791 0.5460 0.7666 0.0632 -0.1589 -0.0831 315 ARG A CA 2256 C C . ARG A 315 ? 0.6358 0.5182 0.7440 0.0662 -0.1565 -0.0922 315 ARG A C 2257 O O . ARG A 315 ? 0.7590 0.6515 0.8733 0.0644 -0.1556 -0.0933 315 ARG A O 2258 C CB . ARG A 315 ? 0.7105 0.5697 0.7995 0.0608 -0.1550 -0.0780 315 ARG A CB 2259 C CG . ARG A 315 ? 0.8764 0.7198 0.9469 0.0590 -0.1586 -0.0710 315 ARG A CG 2260 C CD . ARG A 315 ? 0.9420 0.7786 1.0143 0.0622 -0.1547 -0.0695 315 ARG A CD 2261 N NE . ARG A 315 ? 0.9641 0.7858 1.0192 0.0654 -0.1599 -0.0678 315 ARG A NE 2262 C CZ . ARG A 315 ? 1.0380 0.8478 1.0784 0.0623 -0.1655 -0.0631 315 ARG A CZ 2263 N NH1 . ARG A 315 ? 1.0339 0.8471 1.0754 0.0552 -0.1653 -0.0586 315 ARG A NH1 2264 N NH2 . ARG A 315 ? 0.9927 0.7876 1.0185 0.0667 -0.1721 -0.0637 315 ARG A NH2 2265 N N . ARG A 316 ? 0.6275 0.5120 0.7477 0.0711 -0.1562 -0.0992 316 ARG A N 2266 C CA . ARG A 316 ? 0.6715 0.5686 0.8149 0.0740 -0.1559 -0.1091 316 ARG A CA 2267 C C . ARG A 316 ? 0.7911 0.7031 0.9337 0.0756 -0.1595 -0.1152 316 ARG A C 2268 O O . ARG A 316 ? 0.7569 0.6769 0.9124 0.0757 -0.1591 -0.1195 316 ARG A O 2269 C CB . ARG A 316 ? 0.7557 0.6512 0.9179 0.0718 -0.1514 -0.1075 316 ARG A CB 2270 C CG . ARG A 316 ? 0.9966 0.8844 1.1653 0.0719 -0.1470 -0.1021 316 ARG A CG 2271 C CD . ARG A 316 ? 1.0248 0.9110 1.2083 0.0690 -0.1421 -0.0963 316 ARG A CD 2272 N NE . ARG A 316 ? 1.1455 1.0272 1.3150 0.0657 -0.1411 -0.0900 316 ARG A NE 2273 C CZ . ARG A 316 ? 1.0941 0.9668 1.2429 0.0645 -0.1401 -0.0822 316 ARG A CZ 2274 N NH1 . ARG A 316 ? 1.0864 0.9530 1.2244 0.0674 -0.1401 -0.0803 316 ARG A NH1 2275 N NH2 . ARG A 316 ? 0.8854 0.7556 1.0247 0.0611 -0.1401 -0.0774 316 ARG A NH2 2276 N N . LEU A 317 ? 0.8665 0.7831 0.9934 0.0776 -0.1633 -0.1150 317 LEU A N 2277 C CA . LEU A 317 ? 0.8345 0.7699 0.9593 0.0811 -0.1664 -0.1206 317 LEU A CA 2278 C C . LEU A 317 ? 0.7822 0.7283 0.9224 0.0890 -0.1701 -0.1351 317 LEU A C 2279 O O . LEU A 317 ? 0.7725 0.7158 0.9087 0.0921 -0.1725 -0.1370 317 LEU A O 2280 C CB . LEU A 317 ? 0.8090 0.7461 0.9102 0.0794 -0.1689 -0.1113 317 LEU A CB 2281 C CG . LEU A 317 ? 0.6371 0.5976 0.7328 0.0845 -0.1719 -0.1150 317 LEU A CG 2282 C CD1 . LEU A 317 ? 0.3455 0.3233 0.4476 0.0847 -0.1701 -0.1176 317 LEU A CD1 2283 C CD2 . LEU A 317 ? 0.6169 0.5761 0.6904 0.0812 -0.1743 -0.1018 317 LEU A CD2 2284 N N . HIS A 318 ? 0.8303 0.7878 0.9890 0.0927 -0.1717 -0.1460 318 HIS A N 2285 C CA . HIS A 318 ? 0.7175 0.6848 0.8945 0.1004 -0.1771 -0.1618 318 HIS A CA 2286 C C . HIS A 318 ? 0.7641 0.7523 0.9294 0.1084 -0.1820 -0.1690 318 HIS A C 2287 O O . HIS A 318 ? 0.7567 0.7596 0.9152 0.1106 -0.1821 -0.1694 318 HIS A O 2288 C CB . HIS A 318 ? 0.7926 0.7602 0.9974 0.1013 -0.1788 -0.1712 318 HIS A CB 2289 C CG . HIS A 318 ? 1.1957 1.1712 1.4231 0.1085 -0.1863 -0.1882 318 HIS A CG 2290 N ND1 . HIS A 318 ? 1.2362 1.2281 1.4725 0.1173 -0.1935 -0.2039 318 HIS A ND1 2291 C CD2 . HIS A 318 ? 1.2342 1.2045 1.4779 0.1088 -0.1885 -0.1928 318 HIS A CD2 2292 C CE1 . HIS A 318 ? 1.0665 1.0611 1.3241 0.1224 -0.2008 -0.2180 318 HIS A CE1 2293 N NE2 . HIS A 318 ? 1.0686 1.0506 1.3319 0.1167 -0.1976 -0.2109 318 HIS A NE2 2294 N N . ILE A 319 ? 0.7392 0.7306 0.9018 0.1136 -0.1858 -0.1742 319 ILE A N 2295 C CA . ILE A 319 ? 0.6114 0.6236 0.7611 0.1223 -0.1904 -0.1798 319 ILE A CA 2296 C C . ILE A 319 ? 0.6441 0.6647 0.8129 0.1315 -0.1976 -0.1986 319 ILE A C 2297 O O . ILE A 319 ? 0.5666 0.5799 0.7377 0.1323 -0.1993 -0.1999 319 ILE A O 2298 C CB . ILE A 319 ? 0.5549 0.5614 0.6797 0.1197 -0.1891 -0.1661 319 ILE A CB 2299 C CG1 . ILE A 319 ? 0.6476 0.6431 0.7570 0.1096 -0.1837 -0.1480 319 ILE A CG1 2300 C CG2 . ILE A 319 ? 0.6365 0.6658 0.7472 0.1287 -0.1935 -0.1693 319 ILE A CG2 2301 C CD1 . ILE A 319 ? 0.6911 0.6712 0.7810 0.1050 -0.1837 -0.1340 319 ILE A CD1 2302 N N . PRO A 320 ? 0.5699 0.6060 0.7534 0.1391 -0.2029 -0.2142 320 PRO A N 2303 C CA . PRO A 320 ? 0.4863 0.5296 0.6938 0.1478 -0.2120 -0.2348 320 PRO A CA 2304 C C . PRO A 320 ? 0.6241 0.6736 0.8258 0.1542 -0.2165 -0.2402 320 PRO A C 2305 O O . PRO A 320 ? 0.7500 0.7920 0.9729 0.1541 -0.2205 -0.2484 320 PRO A O 2306 C CB . PRO A 320 ? 0.4304 0.4964 0.6391 0.1586 -0.2176 -0.2487 320 PRO A CB 2307 C CG . PRO A 320 ? 0.5369 0.6007 0.7356 0.1519 -0.2104 -0.2359 320 PRO A CG 2308 C CD . PRO A 320 ? 0.6254 0.6753 0.8022 0.1408 -0.2015 -0.2134 320 PRO A CD 2309 N N . GLN A 321 ? 0.6340 0.6983 0.8091 0.1597 -0.2162 -0.2350 321 GLN A N 2310 C CA . GLN A 321 ? 0.7189 0.7895 0.8870 0.1667 -0.2210 -0.2396 321 GLN A CA 2311 C C . GLN A 321 ? 0.7281 0.7846 0.8732 0.1594 -0.2149 -0.2195 321 GLN A C 2312 O O . GLN A 321 ? 0.6670 0.7342 0.7897 0.1642 -0.2161 -0.2133 321 GLN A O 2313 C CB . GLN A 321 ? 0.8881 0.9888 1.0441 0.1812 -0.2273 -0.2505 321 GLN A CB 2314 C CG . GLN A 321 ? 1.0065 1.1222 1.1860 0.1926 -0.2373 -0.2759 321 GLN A CG 2315 C CD . GLN A 321 ? 1.1339 1.2832 1.2973 0.2081 -0.2422 -0.2853 321 GLN A CD 2316 O OE1 . GLN A 321 ? 1.1643 1.3269 1.3072 0.2078 -0.2364 -0.2733 321 GLN A OE1 2317 N NE2 . GLN A 321 ? 1.0544 1.2198 1.2275 0.2223 -0.2533 -0.3069 321 GLN A NE2 2318 N N . PHE A 322 ? 0.7547 0.7873 0.9059 0.1483 -0.2092 -0.2092 322 PHE A N 2319 C CA . PHE A 322 ? 0.5746 0.5905 0.7050 0.1412 -0.2044 -0.1908 322 PHE A CA 2320 C C . PHE A 322 ? 0.7078 0.7269 0.8229 0.1479 -0.2088 -0.1899 322 PHE A C 2321 O O . PHE A 322 ? 0.8059 0.8198 0.8974 0.1454 -0.2076 -0.1750 322 PHE A O 2322 C CB . PHE A 322 ? 0.4145 0.4077 0.5577 0.1323 -0.1995 -0.1855 322 PHE A CB 2323 C CG . PHE A 322 ? 0.5752 0.5638 0.7330 0.1354 -0.2022 -0.1930 322 PHE A CG 2324 C CD1 . PHE A 322 ? 0.6707 0.6487 0.8139 0.1358 -0.2021 -0.1854 322 PHE A CD1 2325 C CD2 . PHE A 322 ? 0.5931 0.5885 0.7806 0.1379 -0.2057 -0.2077 322 PHE A CD2 2326 C CE1 . PHE A 322 ? 0.6746 0.6516 0.8316 0.1395 -0.2043 -0.1925 322 PHE A CE1 2327 C CE2 . PHE A 322 ? 0.6784 0.6724 0.8815 0.1401 -0.2081 -0.2138 322 PHE A CE2 2328 C CZ . PHE A 322 ? 0.6359 0.6221 0.8233 0.1411 -0.2069 -0.2063 322 PHE A CZ 2329 N N . TYR A 323 ? 0.5587 0.5864 0.6884 0.1562 -0.2148 -0.2056 323 TYR A N 2330 C CA . TYR A 323 ? 0.6732 0.7035 0.7913 0.1635 -0.2196 -0.2063 323 TYR A CA 2331 C C . TYR A 323 ? 0.8242 0.8741 0.9189 0.1716 -0.2231 -0.2030 323 TYR A C 2332 O O . TYR A 323 ? 0.9218 0.9715 1.0006 0.1764 -0.2263 -0.1980 323 TYR A O 2333 C CB . TYR A 323 ? 0.6905 0.7266 0.8334 0.1701 -0.2256 -0.2247 323 TYR A CB 2334 C CG . TYR A 323 ? 0.6584 0.7172 0.8167 0.1794 -0.2326 -0.2441 323 TYR A CG 2335 C CD1 . TYR A 323 ? 0.8160 0.8940 0.9689 0.1923 -0.2408 -0.2559 323 TYR A CD1 2336 C CD2 . TYR A 323 ? 0.5163 0.5770 0.6938 0.1763 -0.2322 -0.2515 323 TYR A CD2 2337 C CE1 . TYR A 323 ? 0.7898 0.8893 0.9562 0.2027 -0.2488 -0.2759 323 TYR A CE1 2338 C CE2 . TYR A 323 ? 0.5668 0.6469 0.7583 0.1862 -0.2404 -0.2709 323 TYR A CE2 2339 C CZ . TYR A 323 ? 0.6963 0.7963 0.8823 0.1997 -0.2489 -0.2838 323 TYR A CZ 2340 O OH . TYR A 323 ? 0.7092 0.8293 0.9092 0.2112 -0.2586 -0.3055 323 TYR A OH 2341 N N . LEU A 324 ? 0.7928 0.8610 0.8851 0.1739 -0.2224 -0.2052 324 LEU A N 2342 C CA . LEU A 324 ? 0.7501 0.8431 0.8213 0.1826 -0.2249 -0.2017 324 LEU A CA 2343 C C . LEU A 324 ? 0.7759 0.8648 0.8248 0.1736 -0.2190 -0.1779 324 LEU A C 2344 O O . LEU A 324 ? 0.8443 0.9562 0.8771 0.1782 -0.2189 -0.1708 324 LEU A O 2345 C CB . LEU A 324 ? 0.6635 0.7843 0.7451 0.1929 -0.2285 -0.2194 324 LEU A CB 2346 C CG . LEU A 324 ? 0.6956 0.8252 0.8008 0.2037 -0.2373 -0.2454 324 LEU A CG 2347 C CD1 . LEU A 324 ? 0.3625 0.5205 0.4734 0.2155 -0.2423 -0.2623 324 LEU A CD1 2348 C CD2 . LEU A 324 ? 0.5319 0.6666 0.6292 0.2125 -0.2434 -0.2492 324 LEU A CD2 2349 N N . PHE A 325 ? 0.7680 0.8289 0.8167 0.1610 -0.2143 -0.1652 325 PHE A N 2350 C CA . PHE A 325 ? 0.8271 0.8820 0.8595 0.1507 -0.2096 -0.1439 325 PHE A CA 2351 C C . PHE A 325 ? 0.8606 0.9193 0.8693 0.1520 -0.2125 -0.1271 325 PHE A C 2352 O O . PHE A 325 ? 0.9329 0.9819 0.9362 0.1565 -0.2172 -0.1277 325 PHE A O 2353 C CB . PHE A 325 ? 0.6686 0.6918 0.7064 0.1382 -0.2056 -0.1360 325 PHE A CB 2354 C CG . PHE A 325 ? 0.5945 0.6165 0.6289 0.1282 -0.2003 -0.1237 325 PHE A CG 2355 C CD1 . PHE A 325 ? 0.5203 0.5511 0.5702 0.1275 -0.1967 -0.1332 325 PHE A CD1 2356 C CD2 . PHE A 325 ? 0.6939 0.7060 0.7107 0.1195 -0.1998 -0.1028 325 PHE A CD2 2357 C CE1 . PHE A 325 ? 0.5308 0.5620 0.5779 0.1190 -0.1921 -0.1225 325 PHE A CE1 2358 C CE2 . PHE A 325 ? 0.7787 0.7912 0.7940 0.1100 -0.1955 -0.0918 325 PHE A CE2 2359 C CZ . PHE A 325 ? 0.7017 0.7248 0.7316 0.1101 -0.1913 -0.1019 325 PHE A CZ 2360 N N . TYR A 326 ? 0.8428 0.9162 0.8384 0.1479 -0.2098 -0.1113 326 TYR A N 2361 C CA . TYR A 326 ? 0.8842 0.9642 0.8587 0.1479 -0.2124 -0.0920 326 TYR A CA 2362 C C . TYR A 326 ? 0.9399 0.9853 0.9052 0.1366 -0.2145 -0.0735 326 TYR A C 2363 O O . TYR A 326 ? 0.6097 0.6270 0.5830 0.1286 -0.2132 -0.0751 326 TYR A O 2364 C CB . TYR A 326 ? 0.8051 0.9170 0.7704 0.1472 -0.2087 -0.0793 326 TYR A CB 2365 C CG . TYR A 326 ? 0.8937 1.0464 0.8600 0.1630 -0.2093 -0.0949 326 TYR A CG 2366 C CD1 . TYR A 326 ? 1.0125 1.1826 0.9921 0.1669 -0.2064 -0.1105 326 TYR A CD1 2367 C CD2 . TYR A 326 ? 0.8760 1.0500 0.8295 0.1754 -0.2139 -0.0946 326 TYR A CD2 2368 C CE1 . TYR A 326 ? 0.8796 1.0866 0.8602 0.1832 -0.2087 -0.1269 326 TYR A CE1 2369 C CE2 . TYR A 326 ? 0.8481 1.0610 0.8016 0.1917 -0.2155 -0.1105 326 TYR A CE2 2370 C CZ . TYR A 326 ? 0.8199 1.0489 0.7871 0.1957 -0.2132 -0.1273 326 TYR A CZ 2371 O OH . TYR A 326 ? 0.9144 1.1818 0.8821 0.2135 -0.2163 -0.1454 326 TYR A OH 2372 N N . ASP A 327 ? 1.0850 1.1342 1.0331 0.1371 -0.2186 -0.0561 327 ASP A N 2373 C CA . ASP A 327 ? 0.9419 0.9605 0.8793 0.1284 -0.2236 -0.0372 327 ASP A CA 2374 C C . ASP A 327 ? 0.9323 0.9290 0.8731 0.1129 -0.2213 -0.0253 327 ASP A C 2375 O O . ASP A 327 ? 0.7139 0.6767 0.6518 0.1063 -0.2261 -0.0182 327 ASP A O 2376 C CB . ASP A 327 ? 0.9242 0.9610 0.8448 0.1295 -0.2269 -0.0161 327 ASP A CB 2377 C CG . ASP A 327 ? 1.1855 1.1927 1.0952 0.1266 -0.2354 -0.0017 327 ASP A CG 2378 O OD1 . ASP A 327 ? 1.3010 1.2727 1.2154 0.1219 -0.2386 -0.0062 327 ASP A OD1 2379 O OD2 . ASP A 327 ? 1.3496 1.3698 1.2461 0.1300 -0.2395 0.0139 327 ASP A OD2 2380 N N . LEU A 328 ? 0.9737 0.9916 0.9202 0.1084 -0.2146 -0.0237 328 LEU A N 2381 C CA . LEU A 328 ? 0.7882 0.7922 0.7380 0.0941 -0.2120 -0.0118 328 LEU A CA 2382 C C . LEU A 328 ? 0.8947 0.8882 0.8326 0.0836 -0.2175 0.0154 328 LEU A C 2383 O O . LEU A 328 ? 1.0713 1.0386 1.0107 0.0717 -0.2201 0.0253 328 LEU A O 2384 C CB . LEU A 328 ? 0.6029 0.5734 0.5624 0.0907 -0.2122 -0.0236 328 LEU A CB 2385 C CG . LEU A 328 ? 0.6267 0.5902 0.5949 0.0804 -0.2074 -0.0221 328 LEU A CG 2386 C CD1 . LEU A 328 ? 0.5307 0.5283 0.5068 0.0826 -0.2000 -0.0282 328 LEU A CD1 2387 C CD2 . LEU A 328 ? 0.7419 0.6786 0.7192 0.0812 -0.2070 -0.0362 328 LEU A CD2 2388 N N . SER A 329 ? 0.9441 0.9587 0.8710 0.0883 -0.2199 0.0276 329 SER A N 2389 C CA . SER A 329 ? 0.9503 0.9542 0.8670 0.0789 -0.2266 0.0552 329 SER A CA 2390 C C . SER A 329 ? 0.9728 1.0036 0.8895 0.0683 -0.2224 0.0774 329 SER A C 2391 O O . SER A 329 ? 0.9786 1.0014 0.8907 0.0572 -0.2278 0.1034 329 SER A O 2392 C CB . SER A 329 ? 0.8532 0.8662 0.7578 0.0896 -0.2318 0.0597 329 SER A CB 2393 O OG . SER A 329 ? 0.7953 0.8553 0.6951 0.0967 -0.2262 0.0640 329 SER A OG 2394 N N . THR A 330 ? 0.9204 0.9841 0.8434 0.0720 -0.2133 0.0673 330 THR A N 2395 C CA . THR A 330 ? 0.9003 0.9944 0.8249 0.0632 -0.2080 0.0860 330 THR A CA 2396 C C . THR A 330 ? 1.0074 1.0753 0.9413 0.0462 -0.2090 0.0948 330 THR A C 2397 O O . THR A 330 ? 1.1684 1.2553 1.1052 0.0355 -0.2064 0.1139 330 THR A O 2398 C CB . THR A 330 ? 0.8135 0.9511 0.7420 0.0749 -0.1990 0.0695 330 THR A CB 2399 O OG1 . THR A 330 ? 0.8518 0.9731 0.7900 0.0822 -0.1976 0.0401 330 THR A OG1 2400 C CG2 . THR A 330 ? 0.5831 0.7578 0.5003 0.0899 -0.1986 0.0696 330 THR A CG2 2401 N N . VAL A 331 ? 0.8947 0.9212 0.8332 0.0443 -0.2130 0.0809 331 VAL A N 2402 C CA . VAL A 331 ? 0.9112 0.9095 0.8572 0.0299 -0.2157 0.0872 331 VAL A CA 2403 C C . VAL A 331 ? 0.9200 0.8717 0.8622 0.0234 -0.2276 0.0947 331 VAL A C 2404 O O . VAL A 331 ? 1.0324 0.9551 0.9803 0.0155 -0.2312 0.0923 331 VAL A O 2405 C CB . VAL A 331 ? 0.7522 0.7444 0.7088 0.0326 -0.2094 0.0641 331 VAL A CB 2406 C CG1 . VAL A 331 ? 0.7007 0.7355 0.6629 0.0376 -0.1995 0.0576 331 VAL A CG1 2407 C CG2 . VAL A 331 ? 0.6062 0.5763 0.5634 0.0441 -0.2106 0.0406 331 VAL A CG2 2408 N N . TYR A 332 ? 0.8865 0.8311 0.8190 0.0278 -0.2346 0.1031 332 TYR A N 2409 C CA . TYR A 332 ? 0.9357 0.8353 0.8645 0.0241 -0.2475 0.1080 332 TYR A CA 2410 C C . TYR A 332 ? 1.0243 0.9072 0.9572 0.0064 -0.2557 0.1325 332 TYR A C 2411 O O . TYR A 332 ? 0.9904 0.8326 0.9245 0.0012 -0.2665 0.1323 332 TYR A O 2412 C CB . TYR A 332 ? 0.9119 0.8085 0.8296 0.0332 -0.2539 0.1127 332 TYR A CB 2413 C CG . TYR A 332 ? 0.9361 0.8368 0.8506 0.0505 -0.2503 0.0872 332 TYR A CG 2414 C CD1 . TYR A 332 ? 0.9137 0.8132 0.8364 0.0560 -0.2433 0.0626 332 TYR A CD1 2415 C CD2 . TYR A 332 ? 0.9093 0.8145 0.8138 0.0611 -0.2548 0.0887 332 TYR A CD2 2416 C CE1 . TYR A 332 ? 0.9926 0.8968 0.9155 0.0707 -0.2407 0.0405 332 TYR A CE1 2417 C CE2 . TYR A 332 ? 0.8510 0.7608 0.7545 0.0767 -0.2523 0.0651 332 TYR A CE2 2418 C CZ . TYR A 332 ? 0.8721 0.7818 0.7857 0.0809 -0.2453 0.0413 332 TYR A CZ 2419 O OH . TYR A 332 ? 0.8045 0.7196 0.7203 0.0950 -0.2435 0.0191 332 TYR A OH 2420 N N . SER A 333 ? 1.0164 0.9323 0.9521 -0.0024 -0.2513 0.1536 333 SER A N 2421 C CA . SER A 333 ? 1.0274 0.9328 0.9702 -0.0209 -0.2589 0.1797 333 SER A CA 2422 C C . SER A 333 ? 1.0649 0.9671 1.0192 -0.0301 -0.2554 0.1734 333 SER A C 2423 O O . SER A 333 ? 1.0830 0.9543 1.0438 -0.0422 -0.2656 0.1813 333 SER A O 2424 C CB . SER A 333 ? 0.9874 0.9335 0.9292 -0.0266 -0.2553 0.2076 333 SER A CB 2425 O OG . SER A 333 ? 0.9339 0.8843 0.8639 -0.0166 -0.2585 0.2127 333 SER A OG 2426 N N . LEU A 334 ? 1.1273 1.0613 1.0842 -0.0232 -0.2419 0.1581 334 LEU A N 2427 C CA . LEU A 334 ? 1.0434 0.9800 1.0106 -0.0294 -0.2367 0.1503 334 LEU A CA 2428 C C . LEU A 334 ? 1.1446 1.0354 1.1141 -0.0308 -0.2443 0.1357 334 LEU A C 2429 O O . LEU A 334 ? 1.1855 1.0681 1.1635 -0.0404 -0.2457 0.1371 334 LEU A O 2430 C CB . LEU A 334 ? 1.0338 1.0048 1.0016 -0.0165 -0.2227 0.1300 334 LEU A CB 2431 C CG . LEU A 334 ? 0.9825 0.9750 0.9604 -0.0204 -0.2142 0.1250 334 LEU A CG 2432 C CD1 . LEU A 334 ? 1.0377 1.0622 1.0203 -0.0326 -0.2127 0.1513 334 LEU A CD1 2433 C CD2 . LEU A 334 ? 0.8159 0.8352 0.7936 -0.0047 -0.2034 0.1020 334 LEU A CD2 2434 N N . LEU A 335 ? 1.1583 1.0217 1.1202 -0.0201 -0.2493 0.1213 335 LEU A N 2435 C CA . LEU A 335 ? 1.1126 0.9395 1.0751 -0.0168 -0.2541 0.1031 335 LEU A CA 2436 C C . LEU A 335 ? 1.1332 0.9160 1.0916 -0.0203 -0.2710 0.1092 335 LEU A C 2437 O O . LEU A 335 ? 0.9547 0.7085 0.9105 -0.0134 -0.2758 0.0924 335 LEU A O 2438 C CB . LEU A 335 ? 0.9352 0.7664 0.8942 -0.0002 -0.2459 0.0780 335 LEU A CB 2439 C CG . LEU A 335 ? 0.8755 0.7473 0.8391 0.0056 -0.2315 0.0693 335 LEU A CG 2440 C CD1 . LEU A 335 ? 0.8464 0.7199 0.8089 0.0210 -0.2262 0.0463 335 LEU A CD1 2441 C CD2 . LEU A 335 ? 0.8719 0.7522 0.8451 -0.0015 -0.2256 0.0672 335 LEU A CD2 2442 N N . GLU A 336 ? 1.2605 1.0393 1.2190 -0.0305 -0.2806 0.1332 336 GLU A N 2443 C CA . GLU A 336 ? 1.2760 1.0118 1.2317 -0.0333 -0.2989 0.1397 336 GLU A CA 2444 C C . GLU A 336 ? 1.1912 0.8954 1.1533 -0.0406 -0.3089 0.1348 336 GLU A C 2445 O O . GLU A 336 ? 1.0589 0.7238 1.0177 -0.0377 -0.3239 0.1296 336 GLU A O 2446 C CB . GLU A 336 ? 1.3758 1.1153 1.3329 -0.0445 -0.3074 0.1698 336 GLU A CB 2447 C CG . GLU A 336 ? 1.4968 1.2550 1.4436 -0.0342 -0.3034 0.1740 336 GLU A CG 2448 C CD . GLU A 336 ? 1.6263 1.3762 1.5731 -0.0437 -0.3159 0.2035 336 GLU A CD 2449 O OE1 . GLU A 336 ? 1.6833 1.4101 1.6398 -0.0590 -0.3288 0.2206 336 GLU A OE1 2450 O OE2 . GLU A 336 ? 1.5864 1.3528 1.5242 -0.0357 -0.3134 0.2100 336 GLU A OE2 2451 N N . LYS A 337 ? 1.3071 1.0299 1.2782 -0.0485 -0.3009 0.1350 337 LYS A N 2452 C CA . LYS A 337 ? 1.2405 0.9388 1.2190 -0.0570 -0.3105 0.1330 337 LYS A CA 2453 C C . LYS A 337 ? 1.1040 0.7952 1.0796 -0.0457 -0.3040 0.1062 337 LYS A C 2454 O O . LYS A 337 ? 1.1016 0.7633 1.0781 -0.0463 -0.3150 0.0984 337 LYS A O 2455 C CB . LYS A 337 ? 1.3232 1.0445 1.3152 -0.0751 -0.3090 0.1547 337 LYS A CB 2456 C CG . LYS A 337 ? 1.5936 1.3008 1.5950 -0.0834 -0.3148 0.1504 337 LYS A CG 2457 C CD . LYS A 337 ? 1.6068 1.3443 1.6107 -0.0796 -0.2977 0.1372 337 LYS A CD 2458 C CE . LYS A 337 ? 1.4942 1.2110 1.5029 -0.0820 -0.3040 0.1257 337 LYS A CE 2459 N NZ . LYS A 337 ? 1.3288 1.0247 1.3489 -0.0985 -0.3218 0.1420 337 LYS A NZ 2460 N N . VAL A 338 ? 0.9542 0.6718 0.9268 -0.0350 -0.2874 0.0921 338 VAL A N 2461 C CA . VAL A 338 ? 0.9375 0.6512 0.9089 -0.0249 -0.2803 0.0694 338 VAL A CA 2462 C C . VAL A 338 ? 0.9878 0.6663 0.9509 -0.0133 -0.2900 0.0533 338 VAL A C 2463 O O . VAL A 338 ? 1.1151 0.7791 1.0710 -0.0066 -0.2969 0.0528 338 VAL A O 2464 C CB . VAL A 338 ? 0.7980 0.5472 0.7709 -0.0165 -0.2615 0.0584 338 VAL A CB 2465 C CG1 . VAL A 338 ? 0.8398 0.6124 0.8100 -0.0146 -0.2569 0.0671 338 VAL A CG1 2466 C CG2 . VAL A 338 ? 0.8193 0.5595 0.7886 -0.0019 -0.2563 0.0358 338 VAL A CG2 2467 N N . LYS A 339 ? 1.0477 0.7147 1.0114 -0.0099 -0.2905 0.0404 339 LYS A N 2468 C CA . LYS A 339 ? 1.0086 0.6440 0.9643 0.0013 -0.3010 0.0257 339 LYS A CA 2469 C C . LYS A 339 ? 0.9739 0.6175 0.9258 0.0167 -0.2893 0.0055 339 LYS A C 2470 O O . LYS A 339 ? 0.9913 0.6175 0.9353 0.0293 -0.2950 -0.0061 339 LYS A O 2471 C CB . LYS A 339 ? 0.8997 0.5115 0.8579 -0.0053 -0.3149 0.0268 339 LYS A CB 2472 C CG . LYS A 339 ? 0.9275 0.5255 0.8921 -0.0212 -0.3299 0.0469 339 LYS A CG 2473 C CD . LYS A 339 ? 0.9723 0.5442 0.9407 -0.0265 -0.3461 0.0449 339 LYS A CD 2474 C CE . LYS A 339 ? 1.1215 0.6674 1.0958 -0.0388 -0.3669 0.0621 339 LYS A CE 2475 N NZ . LYS A 339 ? 1.1314 0.6643 1.0984 -0.0325 -0.3728 0.0658 339 LYS A NZ 2476 N N . ARG A 340 ? 0.8959 0.5660 0.8544 0.0159 -0.2738 0.0019 340 ARG A N 2477 C CA . ARG A 340 ? 0.8497 0.5305 0.8078 0.0289 -0.2618 -0.0142 340 ARG A CA 2478 C C . ARG A 340 ? 0.8257 0.5383 0.7914 0.0291 -0.2464 -0.0143 340 ARG A C 2479 O O . ARG A 340 ? 0.8176 0.5498 0.7908 0.0207 -0.2394 -0.0079 340 ARG A O 2480 C CB . ARG A 340 ? 0.8213 0.4994 0.7806 0.0312 -0.2594 -0.0222 340 ARG A CB 2481 C CG . ARG A 340 ? 1.0870 0.7425 1.0437 0.0246 -0.2740 -0.0180 340 ARG A CG 2482 C CD . ARG A 340 ? 1.1751 0.8160 1.1249 0.0364 -0.2781 -0.0322 340 ARG A CD 2483 N NE . ARG A 340 ? 1.2501 0.9110 1.2019 0.0459 -0.2622 -0.0418 340 ARG A NE 2484 C CZ . ARG A 340 ? 1.1899 0.8464 1.1353 0.0603 -0.2613 -0.0542 340 ARG A CZ 2485 N NH1 . ARG A 340 ? 1.0462 0.6787 0.9808 0.0688 -0.2761 -0.0609 340 ARG A NH1 2486 N NH2 . ARG A 340 ? 1.0943 0.7714 1.0446 0.0668 -0.2463 -0.0595 340 ARG A NH2 2487 N N . ILE A 341 ? 0.6202 0.3381 0.5844 0.0394 -0.2421 -0.0226 341 ILE A N 2488 C CA . ILE A 341 ? 0.7325 0.4784 0.7049 0.0419 -0.2292 -0.0265 341 ILE A CA 2489 C C . ILE A 341 ? 0.7875 0.5383 0.7651 0.0527 -0.2208 -0.0412 341 ILE A C 2490 O O . ILE A 341 ? 0.6387 0.3758 0.6109 0.0620 -0.2248 -0.0486 341 ILE A O 2491 C CB . ILE A 341 ? 0.7667 0.5200 0.7359 0.0438 -0.2314 -0.0222 341 ILE A CB 2492 C CG1 . ILE A 341 ? 0.7848 0.5406 0.7514 0.0321 -0.2375 -0.0044 341 ILE A CG1 2493 C CG2 . ILE A 341 ? 0.5542 0.3353 0.5322 0.0496 -0.2197 -0.0306 341 ILE A CG2 2494 C CD1 . ILE A 341 ? 0.7617 0.5283 0.7242 0.0342 -0.2391 0.0019 341 ILE A CD1 2495 N N . THR A 342 ? 0.8013 0.5726 0.7903 0.0517 -0.2095 -0.0447 342 THR A N 2496 C CA . THR A 342 ? 0.8083 0.5883 0.8064 0.0602 -0.2008 -0.0560 342 THR A CA 2497 C C . THR A 342 ? 0.8761 0.6799 0.8862 0.0612 -0.1932 -0.0599 342 THR A C 2498 O O . THR A 342 ? 0.9133 0.7320 0.9287 0.0553 -0.1897 -0.0561 342 THR A O 2499 C CB . THR A 342 ? 0.9387 0.7191 0.9422 0.0593 -0.1951 -0.0577 342 THR A CB 2500 O OG1 . THR A 342 ? 0.9625 0.7221 0.9547 0.0609 -0.2028 -0.0568 342 THR A OG1 2501 C CG2 . THR A 342 ? 0.8199 0.6120 0.8359 0.0667 -0.1858 -0.0664 342 THR A CG2 2502 N N . VAL A 343 ? 0.8832 0.6915 0.8981 0.0695 -0.1914 -0.0684 343 VAL A N 2503 C CA . VAL A 343 ? 0.7526 0.5823 0.7806 0.0719 -0.1858 -0.0748 343 VAL A CA 2504 C C . VAL A 343 ? 0.8092 0.6417 0.8496 0.0792 -0.1810 -0.0845 343 VAL A C 2505 O O . VAL A 343 ? 0.8201 0.6504 0.8592 0.0861 -0.1836 -0.0895 343 VAL A O 2506 C CB . VAL A 343 ? 0.6836 0.5190 0.7048 0.0741 -0.1909 -0.0737 343 VAL A CB 2507 C CG1 . VAL A 343 ? 0.6203 0.4811 0.6526 0.0748 -0.1865 -0.0784 343 VAL A CG1 2508 C CG2 . VAL A 343 ? 0.6486 0.4718 0.6538 0.0676 -0.1987 -0.0606 343 VAL A CG2 2509 N N . GLU A 344 ? 0.8910 0.7291 0.9442 0.0774 -0.1741 -0.0860 344 GLU A N 2510 C CA . GLU A 344 ? 0.9403 0.7815 1.0070 0.0825 -0.1688 -0.0914 344 GLU A CA 2511 C C . GLU A 344 ? 0.8192 0.6779 0.9088 0.0828 -0.1639 -0.0982 344 GLU A C 2512 O O . GLU A 344 ? 0.6694 0.5364 0.7659 0.0785 -0.1623 -0.0982 344 GLU A O 2513 C CB . GLU A 344 ? 0.9666 0.8001 1.0313 0.0807 -0.1652 -0.0864 344 GLU A CB 2514 C CG . GLU A 344 ? 1.0563 0.8985 1.1387 0.0841 -0.1577 -0.0886 344 GLU A CG 2515 C CD . GLU A 344 ? 1.1052 0.9467 1.1907 0.0805 -0.1527 -0.0829 344 GLU A CD 2516 O OE1 . GLU A 344 ? 1.1106 0.9624 1.2147 0.0775 -0.1476 -0.0831 344 GLU A OE1 2517 O OE2 . GLU A 344 ? 1.1192 0.9494 1.1888 0.0811 -0.1551 -0.0786 344 GLU A OE2 2518 N N . ASN A 345 ? 0.6521 0.5169 0.7545 0.0883 -0.1625 -0.1045 345 ASN A N 2519 C CA . ASN A 345 ? 0.7417 0.6212 0.8694 0.0885 -0.1596 -0.1115 345 ASN A CA 2520 C C . ASN A 345 ? 0.7485 0.6381 0.8790 0.0874 -0.1629 -0.1170 345 ASN A C 2521 O O . ASN A 345 ? 0.7989 0.6955 0.9433 0.0846 -0.1610 -0.1191 345 ASN A O 2522 C CB . ASN A 345 ? 0.7884 0.6690 0.9317 0.0849 -0.1530 -0.1073 345 ASN A CB 2523 C CG . ASN A 345 ? 0.8008 0.6933 0.9739 0.0853 -0.1509 -0.1131 345 ASN A CG 2524 O OD1 . ASN A 345 ? 0.8434 0.7438 1.0263 0.0888 -0.1545 -0.1216 345 ASN A OD1 2525 N ND2 . ASN A 345 ? 0.8744 0.7681 1.0634 0.0817 -0.1459 -0.1081 345 ASN A ND2 2526 N N . SER A 346 ? 0.6875 0.5791 0.8046 0.0906 -0.1684 -0.1192 346 SER A N 2527 C CA . SER A 346 ? 0.7020 0.6072 0.8186 0.0916 -0.1717 -0.1241 346 SER A CA 2528 C C . SER A 346 ? 0.8212 0.7356 0.9397 0.0990 -0.1767 -0.1331 346 SER A C 2529 O O . SER A 346 ? 0.8308 0.7583 0.9450 0.1022 -0.1803 -0.1373 346 SER A O 2530 C CB . SER A 346 ? 0.6270 0.5290 0.7216 0.0874 -0.1735 -0.1141 346 SER A CB 2531 O OG . SER A 346 ? 0.7688 0.6667 0.8641 0.0810 -0.1696 -0.1077 346 SER A OG 2532 N N . LYS A 347 ? 0.7359 0.6455 0.8605 0.1025 -0.1767 -0.1360 347 LYS A N 2533 C CA . LYS A 347 ? 0.6827 0.6015 0.8121 0.1100 -0.1816 -0.1455 347 LYS A CA 2534 C C . LYS A 347 ? 0.6190 0.5333 0.7234 0.1135 -0.1869 -0.1410 347 LYS A C 2535 O O . LYS A 347 ? 0.5723 0.4979 0.6755 0.1197 -0.1917 -0.1478 347 LYS A O 2536 C CB . LYS A 347 ? 0.6589 0.5959 0.8062 0.1130 -0.1843 -0.1578 347 LYS A CB 2537 C CG . LYS A 347 ? 0.5133 0.4537 0.6894 0.1096 -0.1813 -0.1630 347 LYS A CG 2538 C CD . LYS A 347 ? 0.6316 0.5863 0.8314 0.1153 -0.1870 -0.1787 347 LYS A CD 2539 C CE . LYS A 347 ? 0.6181 0.5755 0.8477 0.1118 -0.1865 -0.1841 347 LYS A CE 2540 N NZ . LYS A 347 ? 0.5376 0.5075 0.7911 0.1175 -0.1944 -0.2004 347 LYS A NZ 2541 N N . VAL A 348 ? 0.6355 0.5331 0.7207 0.1098 -0.1869 -0.1294 348 VAL A N 2542 C CA . VAL A 348 ? 0.7183 0.6078 0.7811 0.1124 -0.1933 -0.1232 348 VAL A CA 2543 C C . VAL A 348 ? 0.7102 0.5985 0.7740 0.1211 -0.1971 -0.1301 348 VAL A C 2544 O O . VAL A 348 ? 0.7171 0.5991 0.7880 0.1232 -0.1949 -0.1325 348 VAL A O 2545 C CB . VAL A 348 ? 0.6951 0.5636 0.7404 0.1066 -0.1944 -0.1105 348 VAL A CB 2546 C CG1 . VAL A 348 ? 0.5548 0.4137 0.5789 0.1077 -0.2026 -0.1021 348 VAL A CG1 2547 C CG2 . VAL A 348 ? 0.7223 0.5930 0.7697 0.0979 -0.1899 -0.1045 348 VAL A CG2 2548 N N . PHE A 349 ? 0.6999 0.5965 0.7566 0.1270 -0.2028 -0.1329 349 PHE A N 2549 C CA . PHE A 349 ? 0.7119 0.6089 0.7697 0.1362 -0.2071 -0.1401 349 PHE A CA 2550 C C . PHE A 349 ? 0.7996 0.6853 0.8340 0.1402 -0.2150 -0.1326 349 PHE A C 2551 O O . PHE A 349 ? 0.8403 0.7241 0.8727 0.1486 -0.2196 -0.1377 349 PHE A O 2552 C CB . PHE A 349 ? 0.6877 0.6069 0.7637 0.1421 -0.2080 -0.1540 349 PHE A CB 2553 C CG . PHE A 349 ? 0.6465 0.5807 0.7147 0.1444 -0.2116 -0.1547 349 PHE A CG 2554 C CD1 . PHE A 349 ? 0.6928 0.6288 0.7435 0.1511 -0.2183 -0.1520 349 PHE A CD1 2555 C CD2 . PHE A 349 ? 0.6472 0.5953 0.7252 0.1410 -0.2085 -0.1581 349 PHE A CD2 2556 C CE1 . PHE A 349 ? 0.6708 0.6247 0.7131 0.1544 -0.2211 -0.1515 349 PHE A CE1 2557 C CE2 . PHE A 349 ? 0.8198 0.7860 0.8896 0.1450 -0.2116 -0.1593 349 PHE A CE2 2558 C CZ . PHE A 349 ? 0.7519 0.7222 0.8035 0.1518 -0.2175 -0.1556 349 PHE A CZ 2559 N N . LEU A 350 ? 0.8748 0.7536 0.8930 0.1341 -0.2170 -0.1198 350 LEU A N 2560 C CA . LEU A 350 ? 0.8310 0.6958 0.8281 0.1360 -0.2255 -0.1094 350 LEU A CA 2561 C C . LEU A 350 ? 0.8461 0.7026 0.8301 0.1260 -0.2267 -0.0930 350 LEU A C 2562 O O . LEU A 350 ? 0.9867 0.8607 0.9734 0.1214 -0.2227 -0.0898 350 LEU A O 2563 C CB . LEU A 350 ? 0.7411 0.6221 0.7344 0.1447 -0.2302 -0.1134 350 LEU A CB 2564 C CG . LEU A 350 ? 0.7209 0.5897 0.6924 0.1454 -0.2389 -0.0990 350 LEU A CG 2565 C CD1 . LEU A 350 ? 0.6856 0.5328 0.6501 0.1524 -0.2463 -0.1009 350 LEU A CD1 2566 C CD2 . LEU A 350 ? 0.7046 0.5967 0.6708 0.1511 -0.2413 -0.0982 350 LEU A CD2 2567 N N . VAL A 351 ? 0.8501 0.6809 0.8210 0.1229 -0.2331 -0.0828 351 VAL A N 2568 C CA . VAL A 351 ? 0.9304 0.7531 0.8892 0.1133 -0.2371 -0.0651 351 VAL A CA 2569 C C . VAL A 351 ? 0.9058 0.7234 0.8506 0.1177 -0.2467 -0.0561 351 VAL A C 2570 O O . VAL A 351 ? 0.9116 0.7055 0.8481 0.1220 -0.2555 -0.0552 351 VAL A O 2571 C CB . VAL A 351 ? 0.9554 0.7507 0.9096 0.1059 -0.2405 -0.0581 351 VAL A CB 2572 C CG1 . VAL A 351 ? 0.8860 0.6754 0.8314 0.0945 -0.2452 -0.0388 351 VAL A CG1 2573 C CG2 . VAL A 351 ? 0.9154 0.7147 0.8826 0.1029 -0.2312 -0.0666 351 VAL A CG2 2574 N N . PRO A 352 ? 0.8843 0.7252 0.8259 0.1178 -0.2455 -0.0499 352 PRO A N 2575 C CA . PRO A 352 ? 0.8521 0.6928 0.7803 0.1226 -0.2539 -0.0397 352 PRO A CA 2576 C C . PRO A 352 ? 0.9619 0.7707 0.8781 0.1165 -0.2649 -0.0228 352 PRO A C 2577 O O . PRO A 352 ? 0.9344 0.7342 0.8500 0.1043 -0.2654 -0.0096 352 PRO A O 2578 C CB . PRO A 352 ? 0.6889 0.5613 0.6156 0.1196 -0.2490 -0.0308 352 PRO A CB 2579 C CG . PRO A 352 ? 0.7316 0.6249 0.6734 0.1206 -0.2388 -0.0467 352 PRO A CG 2580 C CD . PRO A 352 ? 0.8041 0.6746 0.7543 0.1145 -0.2364 -0.0519 352 PRO A CD 2581 N N . CYS A 353 ? 1.0161 0.8080 0.9241 0.1253 -0.2746 -0.0240 353 CYS A N 2582 C CA . CYS A 353 ? 0.9446 0.7033 0.8418 0.1219 -0.2879 -0.0097 353 CYS A CA 2583 C C . CYS A 353 ? 0.9703 0.7269 0.8632 0.1074 -0.2912 0.0151 353 CYS A C 2584 O O . CYS A 353 ? 0.9207 0.6501 0.8131 0.0984 -0.2985 0.0240 353 CYS A O 2585 C CB . CYS A 353 ? 0.8773 0.6290 0.7648 0.1342 -0.2976 -0.0104 353 CYS A CB 2586 S SG . CYS A 353 ? 1.4070 1.1180 1.2818 0.1300 -0.3166 0.0101 353 CYS A SG 2587 N N . SER A 354 ? 0.9353 0.7215 0.8257 0.1055 -0.2866 0.0266 354 SER A N 2588 C CA . SER A 354 ? 0.9109 0.7004 0.7988 0.0915 -0.2888 0.0524 354 SER A CA 2589 C C . SER A 354 ? 0.8475 0.6352 0.7450 0.0787 -0.2829 0.0535 354 SER A C 2590 O O . SER A 354 ? 0.9053 0.6730 0.8031 0.0663 -0.2903 0.0702 354 SER A O 2591 C CB . SER A 354 ? 0.9975 0.8265 0.8808 0.0934 -0.2830 0.0638 354 SER A CB 2592 O OG . SER A 354 ? 1.0143 0.8464 0.8951 0.0798 -0.2864 0.0923 354 SER A OG 2593 N N . PHE A 355 ? 0.7682 0.5760 0.6746 0.0817 -0.2707 0.0359 355 PHE A N 2594 C CA . PHE A 355 ? 0.7660 0.5706 0.6815 0.0715 -0.2652 0.0341 355 PHE A CA 2595 C C . PHE A 355 ? 0.8591 0.6230 0.7741 0.0675 -0.2750 0.0333 355 PHE A C 2596 O O . PHE A 355 ? 0.8182 0.5685 0.7351 0.0550 -0.2796 0.0467 355 PHE A O 2597 C CB . PHE A 355 ? 0.7124 0.5377 0.6381 0.0781 -0.2528 0.0124 355 PHE A CB 2598 C CG . PHE A 355 ? 0.8091 0.6430 0.7440 0.0683 -0.2450 0.0130 355 PHE A CG 2599 C CD1 . PHE A 355 ? 0.8487 0.6780 0.7828 0.0546 -0.2481 0.0323 355 PHE A CD1 2600 C CD2 . PHE A 355 ? 0.8724 0.7199 0.8183 0.0726 -0.2350 -0.0051 355 PHE A CD2 2601 C CE1 . PHE A 355 ? 0.9658 0.8042 0.9083 0.0463 -0.2412 0.0324 355 PHE A CE1 2602 C CE2 . PHE A 355 ? 0.9351 0.7903 0.8892 0.0645 -0.2284 -0.0045 355 PHE A CE2 2603 C CZ . PHE A 355 ? 0.9721 0.8234 0.9239 0.0518 -0.2312 0.0137 355 PHE A CZ 2604 N N . SER A 356 ? 0.8421 0.5884 0.7552 0.0791 -0.2786 0.0167 356 SER A N 2605 C CA . SER A 356 ? 0.8812 0.5908 0.7918 0.0796 -0.2888 0.0127 356 SER A CA 2606 C C . SER A 356 ? 0.9440 0.6260 0.8484 0.0711 -0.3045 0.0324 356 SER A C 2607 O O . SER A 356 ? 1.1285 0.7851 1.0342 0.0648 -0.3123 0.0345 356 SER A O 2608 C CB . SER A 356 ? 0.9144 0.6145 0.8221 0.0956 -0.2913 -0.0059 356 SER A CB 2609 O OG . SER A 356 ? 0.9642 0.6847 0.8814 0.1013 -0.2782 -0.0236 356 SER A OG 2610 N N . GLN A 357 ? 0.9679 0.6541 0.8659 0.0712 -0.3101 0.0473 357 GLN A N 2611 C CA . GLN A 357 ? 0.9804 0.6386 0.8744 0.0626 -0.3264 0.0681 357 GLN A CA 2612 C C . GLN A 357 ? 0.9839 0.6509 0.8851 0.0442 -0.3249 0.0890 357 GLN A C 2613 O O . GLN A 357 ? 1.0861 0.7290 0.9884 0.0336 -0.3387 0.1073 357 GLN A O 2614 C CB . GLN A 357 ? 0.9166 0.5781 0.8020 0.0680 -0.3328 0.0803 357 GLN A CB 2615 C CG . GLN A 357 ? 0.9691 0.6186 0.8472 0.0858 -0.3379 0.0629 357 GLN A CG 2616 C CD . GLN A 357 ? 1.0313 0.6846 0.9005 0.0904 -0.3448 0.0775 357 GLN A CD 2617 O OE1 . GLN A 357 ? 1.0015 0.6901 0.8686 0.0942 -0.3347 0.0796 357 GLN A OE1 2618 N NE2 . GLN A 357 ? 0.9639 0.5809 0.8279 0.0906 -0.3631 0.0879 357 GLN A NE2 2619 N N . HIS A 358 ? 0.9234 0.6258 0.8305 0.0405 -0.3089 0.0866 358 HIS A N 2620 C CA . HIS A 358 ? 1.0055 0.7235 0.9199 0.0240 -0.3056 0.1060 358 HIS A CA 2621 C C . HIS A 358 ? 1.0956 0.8026 1.0185 0.0171 -0.3037 0.0972 358 HIS A C 2622 O O . HIS A 358 ? 1.0835 0.7928 1.0137 0.0024 -0.3053 0.1129 358 HIS A O 2623 C CB . HIS A 358 ? 0.9332 0.6997 0.8485 0.0250 -0.2905 0.1104 358 HIS A CB 2624 C CG . HIS A 358 ? 1.0772 0.8599 0.9878 0.0202 -0.2941 0.1364 358 HIS A CG 2625 N ND1 . HIS A 358 ? 1.1307 0.9224 1.0313 0.0319 -0.2955 0.1367 358 HIS A ND1 2626 C CD2 . HIS A 358 ? 1.2055 0.9984 1.1205 0.0049 -0.2967 0.1643 358 HIS A CD2 2627 C CE1 . HIS A 358 ? 1.1612 0.9685 1.0592 0.0246 -0.2984 0.1641 358 HIS A CE1 2628 N NE2 . HIS A 358 ? 1.3109 1.1197 1.2181 0.0078 -0.2990 0.1820 358 HIS A NE2 2629 N N . LEU A 359 ? 1.0696 0.7667 0.9919 0.0280 -0.3002 0.0729 359 LEU A N 2630 C CA . LEU A 359 ? 0.9919 0.6755 0.9201 0.0244 -0.2996 0.0628 359 LEU A CA 2631 C C . LEU A 359 ? 1.1614 0.8017 1.0869 0.0221 -0.3185 0.0655 359 LEU A C 2632 O O . LEU A 359 ? 1.1442 0.7627 1.0661 0.0324 -0.3231 0.0476 359 LEU A O 2633 C CB . LEU A 359 ? 0.9227 0.6149 0.8516 0.0376 -0.2885 0.0378 359 LEU A CB 2634 C CG . LEU A 359 ? 0.8613 0.5937 0.7959 0.0395 -0.2716 0.0328 359 LEU A CG 2635 C CD1 . LEU A 359 ? 0.8617 0.6011 0.7982 0.0535 -0.2632 0.0101 359 LEU A CD1 2636 C CD2 . LEU A 359 ? 0.6479 0.3951 0.5910 0.0281 -0.2644 0.0384 359 LEU A CD2 2637 N N . LYS A 360 ? 1.2752 0.9043 1.2031 0.0089 -0.3300 0.0884 360 LYS A N 2638 C CA . LYS A 360 ? 1.3050 0.8911 1.2325 0.0055 -0.3511 0.0935 360 LYS A CA 2639 C C . LYS A 360 ? 1.2622 0.8290 1.1932 0.0053 -0.3553 0.0791 360 LYS A C 2640 O O . LYS A 360 ? 1.3364 0.8734 1.2616 0.0162 -0.3664 0.0637 360 LYS A O 2641 C CB . LYS A 360 ? 1.2447 0.8274 1.1794 -0.0126 -0.3612 0.1237 360 LYS A CB 2642 C CG . LYS A 360 ? 1.1786 0.7840 1.1097 -0.0136 -0.3574 0.1425 360 LYS A CG 2643 C CD . LYS A 360 ? 1.3587 0.9326 1.2820 -0.0064 -0.3742 0.1466 360 LYS A CD 2644 C CE . LYS A 360 ? 1.4937 1.0928 1.4124 -0.0067 -0.3699 0.1664 360 LYS A CE 2645 N NZ . LYS A 360 ? 1.4731 1.1052 1.4009 -0.0238 -0.3621 0.1926 360 LYS A NZ 2646 N N . SER A 361 ? 1.1796 0.7655 1.1195 -0.0059 -0.3464 0.0837 361 SER A N 2647 C CA . SER A 361 ? 1.1993 0.7677 1.1438 -0.0092 -0.3523 0.0750 361 SER A CA 2648 C C . SER A 361 ? 1.2504 0.8279 1.1907 0.0044 -0.3399 0.0502 361 SER A C 2649 O O . SER A 361 ? 1.3206 0.8931 1.2644 0.0024 -0.3402 0.0427 361 SER A O 2650 C CB . SER A 361 ? 1.1775 0.7628 1.1344 -0.0280 -0.3493 0.0928 361 SER A CB 2651 O OG . SER A 361 ? 1.2347 0.8215 1.1970 -0.0412 -0.3569 0.1190 361 SER A OG 2652 N N . LEU A 362 ? 1.1912 0.7828 1.1252 0.0180 -0.3294 0.0383 362 LEU A N 2653 C CA . LEU A 362 ? 1.1366 0.7425 1.0698 0.0292 -0.3156 0.0182 362 LEU A CA 2654 C C . LEU A 362 ? 1.2753 0.8546 1.2014 0.0427 -0.3249 0.0003 362 LEU A C 2655 O O . LEU A 362 ? 1.4608 1.0218 1.3792 0.0532 -0.3348 -0.0053 362 LEU A O 2656 C CB . LEU A 362 ? 0.9538 0.5872 0.8860 0.0377 -0.3013 0.0126 362 LEU A CB 2657 C CG . LEU A 362 ? 0.8285 0.4848 0.7654 0.0446 -0.2846 -0.0028 362 LEU A CG 2658 C CD1 . LEU A 362 ? 0.7247 0.3971 0.6702 0.0330 -0.2766 0.0031 362 LEU A CD1 2659 C CD2 . LEU A 362 ? 0.7446 0.4261 0.6829 0.0521 -0.2734 -0.0080 362 LEU A CD2 2660 N N . GLU A 363 ? 1.1351 0.7148 1.0633 0.0434 -0.3215 -0.0089 363 GLU A N 2661 C CA . GLU A 363 ? 1.1210 0.6793 1.0420 0.0565 -0.3303 -0.0255 363 GLU A CA 2662 C C . GLU A 363 ? 1.1465 0.7249 1.0663 0.0700 -0.3148 -0.0419 363 GLU A C 2663 O O . GLU A 363 ? 1.1648 0.7338 1.0770 0.0855 -0.3188 -0.0558 363 GLU A O 2664 C CB . GLU A 363 ? 1.1762 0.7182 1.1000 0.0485 -0.3408 -0.0234 363 GLU A CB 2665 C CG . GLU A 363 ? 1.3426 0.8515 1.2665 0.0409 -0.3637 -0.0134 363 GLU A CG 2666 C CD . GLU A 363 ? 1.3721 0.8719 1.3042 0.0269 -0.3725 -0.0057 363 GLU A CD 2667 O OE1 . GLU A 363 ? 1.3161 0.8253 1.2488 0.0294 -0.3659 -0.0152 363 GLU A OE1 2668 O OE2 . GLU A 363 ? 1.4527 0.9364 1.3916 0.0132 -0.3865 0.0108 363 GLU A OE2 2669 N N . PHE A 364 ? 1.0897 0.6965 1.0179 0.0641 -0.2975 -0.0396 364 PHE A N 2670 C CA . PHE A 364 ? 0.9160 0.5436 0.8466 0.0743 -0.2822 -0.0519 364 PHE A CA 2671 C C . PHE A 364 ? 1.0941 0.7486 1.0325 0.0727 -0.2680 -0.0494 364 PHE A C 2672 O O . PHE A 364 ? 1.1861 0.8535 1.1303 0.0611 -0.2639 -0.0383 364 PHE A O 2673 C CB . PHE A 364 ? 0.7545 0.3902 0.6897 0.0700 -0.2758 -0.0530 364 PHE A CB 2674 C CG . PHE A 364 ? 0.7967 0.4548 0.7369 0.0781 -0.2598 -0.0620 364 PHE A CG 2675 C CD1 . PHE A 364 ? 0.7746 0.4291 0.7089 0.0923 -0.2601 -0.0739 364 PHE A CD1 2676 C CD2 . PHE A 364 ? 0.8430 0.5266 0.7948 0.0717 -0.2449 -0.0582 364 PHE A CD2 2677 C CE1 . PHE A 364 ? 0.8676 0.5442 0.8085 0.0986 -0.2452 -0.0794 364 PHE A CE1 2678 C CE2 . PHE A 364 ? 0.8997 0.6021 0.8588 0.0781 -0.2314 -0.0651 364 PHE A CE2 2679 C CZ . PHE A 364 ? 0.9108 0.6099 0.8651 0.0908 -0.2312 -0.0745 364 PHE A CZ 2680 N N . LEU A 365 ? 1.0675 0.7318 1.0063 0.0850 -0.2615 -0.0601 365 LEU A N 2681 C CA . LEU A 365 ? 0.9603 0.6502 0.9083 0.0851 -0.2491 -0.0607 365 LEU A CA 2682 C C . LEU A 365 ? 0.9549 0.6613 0.9106 0.0946 -0.2372 -0.0724 365 LEU A C 2683 O O . LEU A 365 ? 0.9595 0.6605 0.9108 0.1068 -0.2397 -0.0814 365 LEU A O 2684 C CB . LEU A 365 ? 0.9671 0.6531 0.9101 0.0889 -0.2556 -0.0589 365 LEU A CB 2685 C CG . LEU A 365 ? 0.9144 0.6266 0.8663 0.0914 -0.2448 -0.0620 365 LEU A CG 2686 C CD1 . LEU A 365 ? 0.9039 0.6364 0.8643 0.0802 -0.2362 -0.0545 365 LEU A CD1 2687 C CD2 . LEU A 365 ? 0.9022 0.6097 0.8473 0.0966 -0.2526 -0.0604 365 LEU A CD2 2688 N N . ASP A 366 ? 0.9499 0.6777 0.9181 0.0892 -0.2247 -0.0716 366 ASP A N 2689 C CA . ASP A 366 ? 0.9153 0.6596 0.8946 0.0955 -0.2132 -0.0795 366 ASP A CA 2690 C C . ASP A 366 ? 0.8119 0.5785 0.8054 0.0947 -0.2045 -0.0820 366 ASP A C 2691 O O . ASP A 366 ? 0.8509 0.6300 0.8528 0.0868 -0.1991 -0.0783 366 ASP A O 2692 C CB . ASP A 366 ? 1.0481 0.7955 1.0313 0.0903 -0.2076 -0.0768 366 ASP A CB 2693 C CG . ASP A 366 ? 0.9648 0.7272 0.9590 0.0967 -0.1966 -0.0824 366 ASP A CG 2694 O OD1 . ASP A 366 ? 0.9264 0.6983 0.9270 0.1043 -0.1930 -0.0883 366 ASP A OD1 2695 O OD2 . ASP A 366 ? 0.8562 0.6217 0.8534 0.0938 -0.1919 -0.0799 366 ASP A OD2 2696 N N . LEU A 367 ? 0.7521 0.5243 0.7488 0.1039 -0.2040 -0.0894 367 LEU A N 2697 C CA . LEU A 367 ? 0.7911 0.5836 0.8023 0.1047 -0.1979 -0.0939 367 LEU A CA 2698 C C . LEU A 367 ? 0.8128 0.6200 0.8406 0.1102 -0.1890 -0.1008 367 LEU A C 2699 O O . LEU A 367 ? 0.7770 0.5950 0.8137 0.1162 -0.1878 -0.1074 367 LEU A O 2700 C CB . LEU A 367 ? 0.8416 0.6309 0.8454 0.1104 -0.2054 -0.0962 367 LEU A CB 2701 C CG . LEU A 367 ? 0.8560 0.6328 0.8452 0.1047 -0.2146 -0.0868 367 LEU A CG 2702 C CD1 . LEU A 367 ? 0.9296 0.7005 0.9101 0.1123 -0.2229 -0.0887 367 LEU A CD1 2703 C CD2 . LEU A 367 ? 0.7866 0.5798 0.7826 0.0957 -0.2096 -0.0816 367 LEU A CD2 2704 N N . SER A 368 ? 0.8517 0.6605 0.8845 0.1079 -0.1828 -0.0985 368 SER A N 2705 C CA . SER A 368 ? 0.8327 0.6558 0.8815 0.1125 -0.1743 -0.1018 368 SER A CA 2706 C C . SER A 368 ? 0.8448 0.6866 0.9173 0.1087 -0.1679 -0.1047 368 SER A C 2707 O O . SER A 368 ? 0.8950 0.7397 0.9719 0.1016 -0.1676 -0.1035 368 SER A O 2708 C CB . SER A 368 ? 0.8572 0.6779 0.9044 0.1110 -0.1696 -0.0967 368 SER A CB 2709 O OG . SER A 368 ? 0.9605 0.7641 0.9869 0.1159 -0.1769 -0.0961 368 SER A OG 2710 N N . GLU A 369 ? 0.8026 0.6580 0.8913 0.1139 -0.1636 -0.1090 369 GLU A N 2711 C CA . GLU A 369 ? 0.8776 0.7498 0.9931 0.1101 -0.1583 -0.1118 369 GLU A CA 2712 C C . GLU A 369 ? 0.9215 0.7983 1.0409 0.1090 -0.1635 -0.1186 369 GLU A C 2713 O O . GLU A 369 ? 1.0567 0.9423 1.1924 0.1043 -0.1620 -0.1213 369 GLU A O 2714 C CB . GLU A 369 ? 1.0332 0.9068 1.1584 0.1024 -0.1525 -0.1059 369 GLU A CB 2715 C CG . GLU A 369 ? 1.1309 1.0197 1.2862 0.1002 -0.1458 -0.1055 369 GLU A CG 2716 C CD . GLU A 369 ? 1.2044 1.0925 1.3650 0.0954 -0.1395 -0.0967 369 GLU A CD 2717 O OE1 . GLU A 369 ? 1.1987 1.0962 1.3849 0.0912 -0.1354 -0.0950 369 GLU A OE1 2718 O OE2 . GLU A 369 ? 1.1538 1.0313 1.2938 0.0960 -0.1396 -0.0915 369 GLU A OE2 2719 N N . ASN A 370 ? 0.7590 0.6303 0.8631 0.1146 -0.1703 -0.1219 370 ASN A N 2720 C CA . ASN A 370 ? 0.7621 0.6401 0.8679 0.1153 -0.1753 -0.1279 370 ASN A CA 2721 C C . ASN A 370 ? 0.7990 0.6870 0.9139 0.1233 -0.1780 -0.1365 370 ASN A C 2722 O O . ASN A 370 ? 0.7533 0.6497 0.8841 0.1260 -0.1739 -0.1386 370 ASN A O 2723 C CB . ASN A 370 ? 0.7878 0.6533 0.8687 0.1135 -0.1818 -0.1226 370 ASN A CB 2724 C CG . ASN A 370 ? 0.8348 0.6966 0.9117 0.1048 -0.1793 -0.1154 370 ASN A CG 2725 O OD1 . ASN A 370 ? 0.8735 0.7203 0.9350 0.1018 -0.1808 -0.1076 370 ASN A OD1 2726 N ND2 . ASN A 370 ? 0.8008 0.6763 0.8921 0.1013 -0.1765 -0.1188 370 ASN A ND2 2727 N N . LEU A 371 ? 0.7573 0.6466 0.8629 0.1270 -0.1849 -0.1407 371 LEU A N 2728 C CA . LEU A 371 ? 0.6066 0.5068 0.7210 0.1349 -0.1885 -0.1499 371 LEU A CA 2729 C C . LEU A 371 ? 0.7378 0.6271 0.8298 0.1428 -0.1957 -0.1491 371 LEU A C 2730 O O . LEU A 371 ? 0.8586 0.7562 0.9533 0.1500 -0.2003 -0.1564 371 LEU A O 2731 C CB . LEU A 371 ? 0.6013 0.5163 0.7272 0.1349 -0.1915 -0.1582 371 LEU A CB 2732 C CG . LEU A 371 ? 0.6066 0.5362 0.7632 0.1310 -0.1879 -0.1651 371 LEU A CG 2733 C CD1 . LEU A 371 ? 0.5880 0.5126 0.7550 0.1239 -0.1800 -0.1576 371 LEU A CD1 2734 C CD2 . LEU A 371 ? 0.4827 0.4207 0.6402 0.1299 -0.1913 -0.1703 371 LEU A CD2 2735 N N . MET A 372 ? 0.7230 0.5930 0.7938 0.1422 -0.1977 -0.1408 372 MET A N 2736 C CA . MET A 372 ? 0.8634 0.7197 0.9139 0.1501 -0.2063 -0.1400 372 MET A CA 2737 C C . MET A 372 ? 0.9642 0.8282 1.0226 0.1606 -0.2065 -0.1480 372 MET A C 2738 O O . MET A 372 ? 1.1179 0.9887 1.1882 0.1617 -0.2000 -0.1491 372 MET A O 2739 C CB . MET A 372 ? 0.8554 0.6879 0.8848 0.1477 -0.2101 -0.1309 372 MET A CB 2740 C CG . MET A 372 ? 0.9025 0.7284 0.9244 0.1368 -0.2102 -0.1216 372 MET A CG 2741 S SD . MET A 372 ? 1.6690 1.4982 1.6804 0.1357 -0.2172 -0.1175 372 MET A SD 2742 C CE . MET A 372 ? 0.9031 0.7065 0.8912 0.1421 -0.2300 -0.1121 372 MET A CE 2743 N N . VAL A 373 ? 0.9913 0.8564 1.0433 0.1687 -0.2139 -0.1528 373 VAL A N 2744 C CA . VAL A 373 ? 0.9883 0.8598 1.0441 0.1802 -0.2160 -0.1604 373 VAL A CA 2745 C C . VAL A 373 ? 0.9238 0.7763 0.9547 0.1886 -0.2277 -0.1589 373 VAL A C 2746 O O . VAL A 373 ? 0.8871 0.7291 0.9041 0.1850 -0.2336 -0.1530 373 VAL A O 2747 C CB . VAL A 373 ? 0.9272 0.8241 1.0072 0.1827 -0.2139 -0.1702 373 VAL A CB 2748 C CG1 . VAL A 373 ? 0.9708 0.8839 1.0781 0.1752 -0.2038 -0.1710 373 VAL A CG1 2749 C CG2 . VAL A 373 ? 0.8942 0.7948 0.9708 0.1808 -0.2191 -0.1720 373 VAL A CG2 2750 N N . GLU A 374 ? 0.8379 0.6863 0.8632 0.2000 -0.2314 -0.1635 374 GLU A N 2751 C CA . GLU A 374 ? 0.8578 0.6843 0.8596 0.2085 -0.2440 -0.1621 374 GLU A CA 2752 C C . GLU A 374 ? 0.8452 0.6696 0.8393 0.2076 -0.2511 -0.1594 374 GLU A C 2753 O O . GLU A 374 ? 0.7708 0.5730 0.7450 0.2071 -0.2607 -0.1512 374 GLU A O 2754 C CB . GLU A 374 ? 1.0527 0.8840 1.0545 0.2241 -0.2474 -0.1714 374 GLU A CB 2755 C CG . GLU A 374 ? 1.1344 0.9689 1.1394 0.2280 -0.2416 -0.1733 374 GLU A CG 2756 C CD . GLU A 374 ? 1.1659 1.0309 1.1984 0.2239 -0.2278 -0.1759 374 GLU A CD 2757 O OE1 . GLU A 374 ? 1.1567 1.0378 1.2067 0.2176 -0.2240 -0.1775 374 GLU A OE1 2758 O OE2 . GLU A 374 ? 1.1378 1.0112 1.1751 0.2274 -0.2215 -0.1761 374 GLU A OE2 2759 N N . GLU A 375 ? 0.8912 0.7397 0.9018 0.2075 -0.2471 -0.1657 375 GLU A N 2760 C CA . GLU A 375 ? 1.0267 0.8792 1.0305 0.2091 -0.2534 -0.1648 375 GLU A CA 2761 C C . GLU A 375 ? 0.9249 0.7669 0.9158 0.1984 -0.2546 -0.1520 375 GLU A C 2762 O O . GLU A 375 ? 0.9752 0.8064 0.9487 0.2003 -0.2631 -0.1442 375 GLU A O 2763 C CB . GLU A 375 ? 1.2649 1.1469 1.2912 0.2113 -0.2493 -0.1761 375 GLU A CB 2764 C CG . GLU A 375 ? 1.4832 1.3793 1.5248 0.2215 -0.2487 -0.1878 375 GLU A CG 2765 C CD . GLU A 375 ? 1.5463 1.4506 1.6068 0.2170 -0.2384 -0.1893 375 GLU A CD 2766 O OE1 . GLU A 375 ? 1.6177 1.5365 1.6990 0.2080 -0.2308 -0.1906 375 GLU A OE1 2767 O OE2 . GLU A 375 ? 1.4377 1.3350 1.4927 0.2233 -0.2384 -0.1891 375 GLU A OE2 2768 N N . TYR A 376 ? 0.8639 0.7103 0.8639 0.1872 -0.2459 -0.1487 376 TYR A N 2769 C CA . TYR A 376 ? 0.9135 0.7516 0.9023 0.1768 -0.2462 -0.1359 376 TYR A CA 2770 C C . TYR A 376 ? 0.8997 0.7086 0.8714 0.1732 -0.2518 -0.1250 376 TYR A C 2771 O O . TYR A 376 ? 0.9659 0.7613 0.9221 0.1692 -0.2588 -0.1128 376 TYR A O 2772 C CB . TYR A 376 ? 0.9547 0.8080 0.9600 0.1671 -0.2358 -0.1374 376 TYR A CB 2773 C CG . TYR A 376 ? 0.9394 0.8195 0.9624 0.1704 -0.2328 -0.1487 376 TYR A CG 2774 C CD1 . TYR A 376 ? 0.9474 0.8413 0.9944 0.1714 -0.2267 -0.1598 376 TYR A CD1 2775 C CD2 . TYR A 376 ? 0.8409 0.7333 0.8573 0.1730 -0.2370 -0.1481 376 TYR A CD2 2776 C CE1 . TYR A 376 ? 0.9877 0.9045 1.0535 0.1742 -0.2261 -0.1712 376 TYR A CE1 2777 C CE2 . TYR A 376 ? 0.7904 0.7075 0.8230 0.1776 -0.2361 -0.1607 376 TYR A CE2 2778 C CZ . TYR A 376 ? 0.7796 0.7074 0.8376 0.1779 -0.2313 -0.1728 376 TYR A CZ 2779 O OH . TYR A 376 ? 0.5921 0.5425 0.6690 0.1820 -0.2322 -0.1863 376 TYR A OH 2780 N N . LEU A 377 ? 0.9197 0.7201 0.8952 0.1748 -0.2491 -0.1292 377 LEU A N 2781 C CA . LEU A 377 ? 0.9898 0.7626 0.9504 0.1730 -0.2555 -0.1219 377 LEU A CA 2782 C C . LEU A 377 ? 1.0718 0.8229 1.0141 0.1796 -0.2700 -0.1171 377 LEU A C 2783 O O . LEU A 377 ? 0.9715 0.6980 0.9008 0.1746 -0.2784 -0.1068 377 LEU A O 2784 C CB . LEU A 377 ? 0.9651 0.7366 0.9314 0.1790 -0.2516 -0.1302 377 LEU A CB 2785 C CG . LEU A 377 ? 0.9936 0.7400 0.9472 0.1775 -0.2571 -0.1256 377 LEU A CG 2786 C CD1 . LEU A 377 ? 0.8554 0.6004 0.8113 0.1625 -0.2517 -0.1159 377 LEU A CD1 2787 C CD2 . LEU A 377 ? 1.0017 0.7531 0.9599 0.1875 -0.2532 -0.1355 377 LEU A CD2 2788 N N . LYS A 378 ? 1.1293 0.8890 1.0717 0.1907 -0.2738 -0.1242 378 LYS A N 2789 C CA . LYS A 378 ? 1.0695 0.8088 0.9952 0.1983 -0.2882 -0.1196 378 LYS A CA 2790 C C . LYS A 378 ? 0.9202 0.6543 0.8362 0.1889 -0.2929 -0.1034 378 LYS A C 2791 O O . LYS A 378 ? 0.8495 0.5588 0.7512 0.1891 -0.3054 -0.0929 378 LYS A O 2792 C CB . LYS A 378 ? 1.1296 0.8816 1.0582 0.2130 -0.2910 -0.1313 378 LYS A CB 2793 C CG . LYS A 378 ? 1.2665 0.9942 1.1776 0.2231 -0.3071 -0.1281 378 LYS A CG 2794 C CD . LYS A 378 ? 1.3574 1.0996 1.2718 0.2386 -0.3097 -0.1405 378 LYS A CD 2795 C CE . LYS A 378 ? 1.4399 1.1563 1.3396 0.2524 -0.3250 -0.1429 378 LYS A CE 2796 N NZ . LYS A 378 ? 1.5012 1.2358 1.4071 0.2685 -0.3258 -0.1576 378 LYS A NZ 2797 N N . ASN A 379 ? 0.9083 0.6665 0.8328 0.1811 -0.2833 -0.1008 379 ASN A N 2798 C CA . ASN A 379 ? 1.0394 0.7982 0.9551 0.1723 -0.2861 -0.0841 379 ASN A CA 2799 C C . ASN A 379 ? 1.1183 0.8641 1.0324 0.1580 -0.2845 -0.0719 379 ASN A C 2800 O O . ASN A 379 ? 1.1972 0.9277 1.1008 0.1508 -0.2925 -0.0550 379 ASN A O 2801 C CB . ASN A 379 ? 1.0397 0.8322 0.9632 0.1721 -0.2780 -0.0870 379 ASN A CB 2802 C CG . ASN A 379 ? 1.0400 0.8376 0.9516 0.1671 -0.2820 -0.0695 379 ASN A CG 2803 O OD1 . ASN A 379 ? 1.0145 0.8273 0.9288 0.1576 -0.2754 -0.0618 379 ASN A OD1 2804 N ND2 . ASN A 379 ? 0.9664 0.7520 0.8648 0.1739 -0.2932 -0.0621 379 ASN A ND2 2805 N N . SER A 380 ? 1.0373 0.7903 0.9632 0.1536 -0.2746 -0.0796 380 SER A N 2806 C CA . SER A 380 ? 0.9832 0.7277 0.9093 0.1404 -0.2720 -0.0696 380 SER A CA 2807 C C . SER A 380 ? 1.0857 0.7955 1.0010 0.1389 -0.2840 -0.0631 380 SER A C 2808 O O . SER A 380 ? 1.1572 0.8552 1.0691 0.1272 -0.2873 -0.0497 380 SER A O 2809 C CB . SER A 380 ? 0.8848 0.6451 0.8261 0.1374 -0.2591 -0.0797 380 SER A CB 2810 O OG . SER A 380 ? 0.8227 0.6129 0.7751 0.1380 -0.2505 -0.0853 380 SER A OG 2811 N N . ALA A 381 ? 1.1168 0.8110 1.0275 0.1512 -0.2915 -0.0731 381 ALA A N 2812 C CA . ALA A 381 ? 1.0323 0.6914 0.9316 0.1532 -0.3065 -0.0692 381 ALA A CA 2813 C C . ALA A 381 ? 1.0893 0.7338 0.9778 0.1614 -0.3202 -0.0647 381 ALA A C 2814 O O . ALA A 381 ? 1.0674 0.7001 0.9510 0.1756 -0.3279 -0.0758 381 ALA A O 2815 C CB . ALA A 381 ? 0.9652 0.6166 0.8661 0.1628 -0.3060 -0.0845 381 ALA A CB 2816 N N . CYS A 382 ? 1.0908 0.7386 0.9754 0.1529 -0.3229 -0.0478 382 CYS A N 2817 C CA . CYS A 382 ? 0.9891 0.6237 0.8633 0.1587 -0.3360 -0.0392 382 CYS A CA 2818 C C . CYS A 382 ? 1.0585 0.6519 0.9244 0.1561 -0.3543 -0.0297 382 CYS A C 2819 O O . CYS A 382 ? 1.0708 0.6488 0.9393 0.1500 -0.3562 -0.0310 382 CYS A O 2820 C CB . CYS A 382 ? 0.7582 0.4157 0.6315 0.1512 -0.3313 -0.0234 382 CYS A CB 2821 S SG . CYS A 382 ? 1.6591 1.3285 1.5373 0.1304 -0.3239 -0.0038 382 CYS A SG 2822 N N . LYS A 383 ? 1.1344 0.7093 0.9912 0.1610 -0.3689 -0.0204 383 LYS A N 2823 C CA . LYS A 383 ? 1.3136 0.8458 1.1642 0.1610 -0.3892 -0.0144 383 LYS A CA 2824 C C . LYS A 383 ? 1.5489 1.0650 1.4038 0.1425 -0.3934 0.0015 383 LYS A C 2825 O O . LYS A 383 ? 1.6793 1.1633 1.5333 0.1429 -0.4068 -0.0023 383 LYS A O 2826 C CB . LYS A 383 ? 1.2822 0.7963 1.1234 0.1677 -0.4051 -0.0035 383 LYS A CB 2827 C CG . LYS A 383 ? 1.3362 0.8030 1.1721 0.1719 -0.4285 -0.0027 383 LYS A CG 2828 C CD . LYS A 383 ? 1.4910 0.9379 1.3182 0.1799 -0.4453 0.0074 383 LYS A CD 2829 C CE . LYS A 383 ? 1.5913 0.9883 1.4146 0.1854 -0.4706 0.0055 383 LYS A CE 2830 N NZ . LYS A 383 ? 1.5793 0.9557 1.3937 0.1986 -0.4877 0.0090 383 LYS A NZ 2831 N N . GLY A 384 ? 1.4672 1.0067 1.3274 0.1272 -0.3828 0.0183 384 GLY A N 2832 C CA . GLY A 384 ? 1.4042 0.9313 1.2700 0.1089 -0.3871 0.0354 384 GLY A CA 2833 C C . GLY A 384 ? 1.2977 0.8471 1.1724 0.1000 -0.3709 0.0298 384 GLY A C 2834 O O . GLY A 384 ? 1.1804 0.7315 1.0612 0.0836 -0.3702 0.0457 384 GLY A O 2835 N N . ALA A 385 ? 1.2412 0.8083 1.1178 0.1107 -0.3582 0.0078 385 ALA A N 2836 C CA . ALA A 385 ? 1.1485 0.7401 1.0341 0.1038 -0.3416 0.0021 385 ALA A CA 2837 C C . ALA A 385 ? 1.2728 0.8434 1.1614 0.0982 -0.3465 -0.0017 385 ALA A C 2838 O O . ALA A 385 ? 1.2553 0.7949 1.1388 0.1055 -0.3610 -0.0091 385 ALA A O 2839 C CB . ALA A 385 ? 0.9809 0.5986 0.8699 0.1162 -0.3272 -0.0182 385 ALA A CB 2840 N N . TRP A 386 ? 1.2372 0.8260 1.1339 0.0862 -0.3352 0.0030 386 TRP A N 2841 C CA . TRP A 386 ? 1.2161 0.7942 1.1166 0.0821 -0.3354 -0.0034 386 TRP A CA 2842 C C . TRP A 386 ? 1.3307 0.8680 1.2266 0.0827 -0.3561 -0.0030 386 TRP A C 2843 O O . TRP A 386 ? 1.4868 1.0112 1.3801 0.0923 -0.3594 -0.0193 386 TRP A O 2844 C CB . TRP A 386 ? 1.1078 0.7018 1.0105 0.0942 -0.3225 -0.0247 386 TRP A CB 2845 C CG . TRP A 386 ? 1.0390 0.6705 0.9495 0.0924 -0.3038 -0.0264 386 TRP A CG 2846 C CD1 . TRP A 386 ? 0.9427 0.5958 0.8593 0.0798 -0.2954 -0.0138 386 TRP A CD1 2847 C CD2 . TRP A 386 ? 0.9903 0.6427 0.9049 0.1041 -0.2922 -0.0422 386 TRP A CD2 2848 N NE1 . TRP A 386 ? 0.9367 0.6210 0.8601 0.0839 -0.2803 -0.0223 386 TRP A NE1 2849 C CE2 . TRP A 386 ? 0.9665 0.6502 0.8900 0.0978 -0.2783 -0.0392 386 TRP A CE2 2850 C CE3 . TRP A 386 ? 0.8787 0.5278 0.7915 0.1193 -0.2927 -0.0584 386 TRP A CE3 2851 C CZ2 . TRP A 386 ? 0.8857 0.5940 0.8176 0.1055 -0.2663 -0.0521 386 TRP A CZ2 2852 C CZ3 . TRP A 386 ? 0.9019 0.5780 0.8237 0.1259 -0.2795 -0.0694 386 TRP A CZ3 2853 C CH2 . TRP A 386 ? 0.8827 0.5866 0.8146 0.1186 -0.2671 -0.0663 386 TRP A CH2 2854 N N . PRO A 387 ? 1.1806 0.6983 1.0762 0.0726 -0.3706 0.0162 387 PRO A N 2855 C CA . PRO A 387 ? 1.1645 0.6394 1.0568 0.0740 -0.3942 0.0171 387 PRO A CA 2856 C C . PRO A 387 ? 1.2526 0.7117 1.1476 0.0729 -0.3996 0.0065 387 PRO A C 2857 O O . PRO A 387 ? 1.3553 0.7838 1.2448 0.0836 -0.4161 -0.0057 387 PRO A O 2858 C CB . PRO A 387 ? 1.0252 0.4916 0.9227 0.0567 -0.4041 0.0451 387 PRO A CB 2859 C CG . PRO A 387 ? 1.0086 0.5138 0.9072 0.0523 -0.3866 0.0562 387 PRO A CG 2860 C CD . PRO A 387 ? 1.0899 0.6268 0.9905 0.0574 -0.3656 0.0396 387 PRO A CD 2861 N N . SER A 388 ? 1.2183 0.6987 1.1211 0.0615 -0.3866 0.0101 388 SER A N 2862 C CA . SER A 388 ? 1.1380 0.6047 1.0433 0.0599 -0.3922 0.0013 388 SER A CA 2863 C C . SER A 388 ? 1.2639 0.7507 1.1663 0.0724 -0.3765 -0.0194 388 SER A C 2864 O O . SER A 388 ? 1.4420 0.9250 1.3459 0.0720 -0.3773 -0.0269 388 SER A O 2865 C CB . SER A 388 ? 0.9765 0.4507 0.8933 0.0387 -0.3907 0.0195 388 SER A CB 2866 O OG . SER A 388 ? 1.0986 0.5601 1.0204 0.0254 -0.4030 0.0424 388 SER A OG 2867 N N . LEU A 389 ? 1.2290 0.7381 1.1283 0.0833 -0.3627 -0.0278 389 LEU A N 2868 C CA . LEU A 389 ? 1.1911 0.7224 1.0907 0.0934 -0.3468 -0.0442 389 LEU A CA 2869 C C . LEU A 389 ? 1.2034 0.7159 1.0950 0.1093 -0.3565 -0.0623 389 LEU A C 2870 O O . LEU A 389 ? 1.3293 0.8228 1.2128 0.1223 -0.3692 -0.0701 389 LEU A O 2871 C CB . LEU A 389 ? 1.1739 0.7317 1.0744 0.1014 -0.3321 -0.0492 389 LEU A CB 2872 C CG . LEU A 389 ? 1.0726 0.6612 0.9806 0.1026 -0.3120 -0.0572 389 LEU A CG 2873 C CD1 . LEU A 389 ? 0.9495 0.5534 0.8664 0.0854 -0.3034 -0.0442 389 LEU A CD1 2874 C CD2 . LEU A 389 ? 1.1361 0.7479 1.0470 0.1115 -0.3004 -0.0640 389 LEU A CD2 2875 N N . GLN A 390 ? 1.1926 0.7120 1.0860 0.1094 -0.3508 -0.0691 390 GLN A N 2876 C CA . GLN A 390 ? 1.1413 0.6484 1.0263 0.1257 -0.3586 -0.0866 390 GLN A CA 2877 C C . GLN A 390 ? 1.1153 0.6531 1.0011 0.1369 -0.3395 -0.0981 390 GLN A C 2878 O O . GLN A 390 ? 1.2457 0.7830 1.1238 0.1551 -0.3421 -0.1130 390 GLN A O 2879 C CB . GLN A 390 ? 1.1297 0.6194 1.0153 0.1186 -0.3697 -0.0855 390 GLN A CB 2880 C CG . GLN A 390 ? 1.2301 0.6857 1.1169 0.1082 -0.3922 -0.0748 390 GLN A CG 2881 C CD . GLN A 390 ? 1.2584 0.7035 1.1513 0.0952 -0.4001 -0.0692 390 GLN A CD 2882 O OE1 . GLN A 390 ? 1.3430 0.7845 1.2455 0.0760 -0.4033 -0.0509 390 GLN A OE1 2883 N NE2 . GLN A 390 ? 1.1056 0.5481 0.9932 0.1059 -0.4031 -0.0846 390 GLN A NE2 2884 N N . THR A 391 ? 0.9400 0.5055 0.8361 0.1264 -0.3206 -0.0907 391 THR A N 2885 C CA . THR A 391 ? 0.9409 0.5358 0.8415 0.1344 -0.3023 -0.0987 391 THR A CA 2886 C C . THR A 391 ? 1.0628 0.6824 0.9735 0.1297 -0.2875 -0.0937 391 THR A C 2887 O O . THR A 391 ? 1.1580 0.7859 1.0762 0.1152 -0.2819 -0.0823 391 THR A O 2888 C CB . THR A 391 ? 1.0013 0.6074 0.9065 0.1280 -0.2936 -0.0971 391 THR A CB 2889 O OG1 . THR A 391 ? 1.1014 0.6834 0.9981 0.1302 -0.3094 -0.1009 391 THR A OG1 2890 C CG2 . THR A 391 ? 0.8300 0.4632 0.7393 0.1386 -0.2772 -0.1053 391 THR A CG2 2891 N N . LEU A 392 ? 1.0017 0.6345 0.9130 0.1427 -0.2817 -0.1029 392 LEU A N 2892 C CA . LEU A 392 ? 0.8438 0.5019 0.7666 0.1400 -0.2679 -0.1010 392 LEU A CA 2893 C C . LEU A 392 ? 0.8540 0.5380 0.7869 0.1451 -0.2521 -0.1071 392 LEU A C 2894 O O . LEU A 392 ? 0.8157 0.5015 0.7440 0.1581 -0.2525 -0.1159 392 LEU A O 2895 C CB . LEU A 392 ? 0.8138 0.4682 0.7324 0.1498 -0.2743 -0.1055 392 LEU A CB 2896 C CG . LEU A 392 ? 0.9103 0.5895 0.8406 0.1482 -0.2630 -0.1049 392 LEU A CG 2897 C CD1 . LEU A 392 ? 0.8158 0.5091 0.7562 0.1326 -0.2535 -0.0951 392 LEU A CD1 2898 C CD2 . LEU A 392 ? 1.0521 0.7215 0.9756 0.1536 -0.2732 -0.1047 392 LEU A CD2 2899 N N . VAL A 393 ? 0.8052 0.5104 0.7523 0.1355 -0.2387 -0.1022 393 VAL A N 2900 C CA . VAL A 393 ? 0.8499 0.5796 0.8099 0.1394 -0.2243 -0.1063 393 VAL A CA 2901 C C . VAL A 393 ? 0.9439 0.6946 0.9192 0.1379 -0.2154 -0.1073 393 VAL A C 2902 O O . VAL A 393 ? 0.9955 0.7532 0.9790 0.1273 -0.2114 -0.1021 393 VAL A O 2903 C CB . VAL A 393 ? 0.8629 0.5987 0.8288 0.1303 -0.2165 -0.1007 393 VAL A CB 2904 C CG1 . VAL A 393 ? 0.8321 0.5907 0.8105 0.1357 -0.2033 -0.1035 393 VAL A CG1 2905 C CG2 . VAL A 393 ? 0.7213 0.4355 0.6726 0.1303 -0.2270 -0.0996 393 VAL A CG2 2906 N N . LEU A 394 ? 1.0006 0.7625 0.9802 0.1493 -0.2131 -0.1149 394 LEU A N 2907 C CA . LEU A 394 ? 0.9247 0.7076 0.9212 0.1491 -0.2057 -0.1176 394 LEU A CA 2908 C C . LEU A 394 ? 0.9097 0.7159 0.9231 0.1534 -0.1938 -0.1203 394 LEU A C 2909 O O . LEU A 394 ? 0.9306 0.7521 0.9544 0.1604 -0.1911 -0.1257 394 LEU A O 2910 C CB . LEU A 394 ? 0.8714 0.6500 0.8614 0.1584 -0.2141 -0.1234 394 LEU A CB 2911 C CG . LEU A 394 ? 0.9684 0.7237 0.9415 0.1564 -0.2275 -0.1197 394 LEU A CG 2912 C CD1 . LEU A 394 ? 0.9020 0.6522 0.8676 0.1696 -0.2361 -0.1268 394 LEU A CD1 2913 C CD2 . LEU A 394 ? 1.1651 0.9273 1.1446 0.1448 -0.2250 -0.1133 394 LEU A CD2 2914 N N . SER A 395 ? 0.7520 0.5618 0.7689 0.1494 -0.1871 -0.1157 395 SER A N 2915 C CA . SER A 395 ? 0.7012 0.5341 0.7358 0.1519 -0.1752 -0.1149 395 SER A CA 2916 C C . SER A 395 ? 0.7045 0.5547 0.7640 0.1440 -0.1680 -0.1142 395 SER A C 2917 O O . SER A 395 ? 0.7616 0.6066 0.8235 0.1350 -0.1701 -0.1132 395 SER A O 2918 C CB . SER A 395 ? 0.8709 0.7034 0.9035 0.1486 -0.1700 -0.1086 395 SER A CB 2919 O OG . SER A 395 ? 0.9780 0.8340 1.0276 0.1515 -0.1586 -0.1054 395 SER A OG 2920 N N . GLN A 396 ? 0.7144 0.5865 0.7932 0.1478 -0.1601 -0.1148 396 GLN A N 2921 C CA . GLN A 396 ? 0.7253 0.6141 0.8321 0.1402 -0.1539 -0.1142 396 GLN A CA 2922 C C . GLN A 396 ? 0.7832 0.6684 0.8922 0.1372 -0.1603 -0.1207 396 GLN A C 2923 O O . GLN A 396 ? 0.8703 0.7590 0.9931 0.1287 -0.1589 -0.1207 396 GLN A O 2924 C CB . GLN A 396 ? 0.8019 0.6919 0.9195 0.1300 -0.1473 -0.1066 396 GLN A CB 2925 C CG . GLN A 396 ? 1.0332 0.9427 1.1836 0.1244 -0.1397 -0.1042 396 GLN A CG 2926 C CD . GLN A 396 ? 1.2353 1.1462 1.3947 0.1172 -0.1329 -0.0949 396 GLN A CD 2927 O OE1 . GLN A 396 ? 1.2126 1.1132 1.3531 0.1182 -0.1326 -0.0903 396 GLN A OE1 2928 N NE2 . GLN A 396 ? 1.2334 1.1563 1.4226 0.1103 -0.1284 -0.0923 396 GLN A NE2 2929 N N . ASN A 397 ? 0.7879 0.6667 0.8826 0.1453 -0.1681 -0.1265 397 ASN A N 2930 C CA . ASN A 397 ? 0.9235 0.8053 1.0231 0.1453 -0.1734 -0.1329 397 ASN A CA 2931 C C . ASN A 397 ? 1.0262 0.9273 1.1430 0.1529 -0.1717 -0.1391 397 ASN A C 2932 O O . ASN A 397 ? 1.1139 1.0306 1.2474 0.1538 -0.1639 -0.1365 397 ASN A O 2933 C CB . ASN A 397 ? 0.8741 0.7357 0.9474 0.1478 -0.1840 -0.1335 397 ASN A CB 2934 C CG . ASN A 397 ? 0.8571 0.7055 0.9201 0.1378 -0.1854 -0.1267 397 ASN A CG 2935 O OD1 . ASN A 397 ? 1.0189 0.8574 1.0737 0.1347 -0.1837 -0.1209 397 ASN A OD1 2936 N ND2 . ASN A 397 ? 0.6817 0.5324 0.7455 0.1335 -0.1884 -0.1275 397 ASN A ND2 2937 N N . HIS A 398 ? 0.9476 0.8498 1.0617 0.1581 -0.1786 -0.1464 398 HIS A N 2938 C CA . HIS A 398 ? 1.0093 0.9322 1.1432 0.1644 -0.1772 -0.1529 398 HIS A CA 2939 C C . HIS A 398 ? 1.0595 0.9787 1.1765 0.1778 -0.1840 -0.1581 398 HIS A C 2940 O O . HIS A 398 ? 1.0367 0.9681 1.1629 0.1837 -0.1874 -0.1655 398 HIS A O 2941 C CB . HIS A 398 ? 1.0154 0.9503 1.1705 0.1595 -0.1789 -0.1592 398 HIS A CB 2942 C CG . HIS A 398 ? 1.0417 0.9852 1.2216 0.1486 -0.1722 -0.1560 398 HIS A CG 2943 N ND1 . HIS A 398 ? 1.1193 1.0798 1.3261 0.1459 -0.1645 -0.1524 398 HIS A ND1 2944 C CD2 . HIS A 398 ? 0.9812 0.9190 1.1636 0.1401 -0.1726 -0.1552 398 HIS A CD2 2945 C CE1 . HIS A 398 ? 1.1348 1.0969 1.3601 0.1359 -0.1612 -0.1495 398 HIS A CE1 2946 N NE2 . HIS A 398 ? 1.0688 1.0174 1.2792 0.1329 -0.1661 -0.1521 398 HIS A NE2 2947 N N . LEU A 399 ? 1.0302 0.9323 1.1229 0.1831 -0.1870 -0.1549 399 LEU A N 2948 C CA . LEU A 399 ? 1.1067 1.0021 1.1818 0.1972 -0.1950 -0.1603 399 LEU A CA 2949 C C . LEU A 399 ? 1.2434 1.1647 1.3344 0.2070 -0.1893 -0.1643 399 LEU A C 2950 O O . LEU A 399 ? 1.2393 1.1778 1.3464 0.2038 -0.1790 -0.1593 399 LEU A O 2951 C CB . LEU A 399 ? 0.9431 0.8133 0.9909 0.2006 -0.2008 -0.1569 399 LEU A CB 2952 C CG . LEU A 399 ? 0.8238 0.6699 0.8570 0.1900 -0.2064 -0.1509 399 LEU A CG 2953 C CD1 . LEU A 399 ? 0.7712 0.5941 0.7826 0.1920 -0.2121 -0.1473 399 LEU A CD1 2954 C CD2 . LEU A 399 ? 0.9299 0.7669 0.9546 0.1916 -0.2162 -0.1532 399 LEU A CD2 2955 N N . ARG A 400 ? 1.2187 1.1448 1.3060 0.2188 -0.1959 -0.1724 400 ARG A N 2956 C CA . ARG A 400 ? 1.0540 1.0075 1.1559 0.2294 -0.1911 -0.1763 400 ARG A CA 2957 C C . ARG A 400 ? 1.0831 1.0311 1.1636 0.2482 -0.1995 -0.1836 400 ARG A C 2958 O O . ARG A 400 ? 1.1523 1.1253 1.2427 0.2587 -0.1952 -0.1867 400 ARG A O 2959 C CB . ARG A 400 ? 0.8435 0.8219 0.9756 0.2256 -0.1881 -0.1802 400 ARG A CB 2960 C CG . ARG A 400 ? 0.9950 0.9933 1.1593 0.2120 -0.1766 -0.1733 400 ARG A CG 2961 C CD . ARG A 400 ? 1.2413 1.2726 1.4381 0.2140 -0.1730 -0.1770 400 ARG A CD 2962 N NE . ARG A 400 ? 1.2472 1.2911 1.4777 0.1998 -0.1687 -0.1747 400 ARG A NE 2963 C CZ . ARG A 400 ? 0.9799 1.0489 1.2423 0.1987 -0.1684 -0.1788 400 ARG A CZ 2964 N NH1 . ARG A 400 ? 0.9142 1.0002 1.1781 0.2109 -0.1708 -0.1849 400 ARG A NH1 2965 N NH2 . ARG A 400 ? 0.6991 0.7760 0.9926 0.1857 -0.1665 -0.1775 400 ARG A NH2 2966 N N . SER A 401 ? 1.0702 0.9867 1.1227 0.2526 -0.2119 -0.1859 401 SER A N 2967 C CA . SER A 401 ? 1.0568 0.9637 1.0882 0.2712 -0.2221 -0.1935 401 SER A CA 2968 C C . SER A 401 ? 1.0395 0.9113 1.0421 0.2739 -0.2324 -0.1922 401 SER A C 2969 O O . SER A 401 ? 1.1444 0.9880 1.1326 0.2687 -0.2427 -0.1898 401 SER A O 2970 C CB . SER A 401 ? 1.2058 1.1114 1.2345 0.2800 -0.2320 -0.2014 401 SER A CB 2971 O OG . SER A 401 ? 1.2773 1.1732 1.2864 0.2991 -0.2427 -0.2095 401 SER A OG 2972 N N . MET A 402 ? 1.0095 0.8849 1.0045 0.2828 -0.2303 -0.1935 402 MET A N 2973 C CA . MET A 402 ? 1.1485 0.9921 1.1173 0.2886 -0.2423 -0.1952 402 MET A CA 2974 C C . MET A 402 ? 1.0745 0.8900 1.0232 0.3001 -0.2609 -0.2024 402 MET A C 2975 O O . MET A 402 ? 1.0208 0.8020 0.9518 0.2970 -0.2731 -0.2001 402 MET A O 2976 C CB . MET A 402 ? 1.3064 1.1650 1.2702 0.3021 -0.2382 -0.1992 402 MET A CB 2977 C CG . MET A 402 ? 1.3555 1.2247 1.3280 0.2903 -0.2252 -0.1898 402 MET A CG 2978 S SD . MET A 402 ? 1.2605 1.1641 1.2339 0.3083 -0.2162 -0.1934 402 MET A SD 2979 C CE . MET A 402 ? 5.6633 5.6115 5.6669 0.3097 -0.2034 -0.1924 402 MET A CE 2980 N N . GLN A 403 ? 1.0855 0.9151 1.0377 0.3134 -0.2641 -0.2107 403 GLN A N 2981 C CA . GLN A 403 ? 1.1756 0.9772 1.1091 0.3245 -0.2826 -0.2169 403 GLN A CA 2982 C C . GLN A 403 ? 1.1820 0.9606 1.1129 0.3095 -0.2887 -0.2081 403 GLN A C 2983 O O . GLN A 403 ? 1.1557 0.8988 1.0686 0.3091 -0.3037 -0.2054 403 GLN A O 2984 C CB . GLN A 403 ? 1.2254 1.0482 1.1630 0.3431 -0.2851 -0.2281 403 GLN A CB 2985 C CG . GLN A 403 ? 1.2578 1.0491 1.1756 0.3553 -0.3056 -0.2341 403 GLN A CG 2986 C CD . GLN A 403 ? 1.3393 1.1512 1.2596 0.3758 -0.3092 -0.2464 403 GLN A CD 2987 O OE1 . GLN A 403 ? 1.2729 1.1216 1.2140 0.3752 -0.2968 -0.2477 403 GLN A OE1 2988 N NE2 . GLN A 403 ? 1.4232 1.2112 1.3236 0.3944 -0.3273 -0.2559 403 GLN A NE2 2989 N N . LYS A 404 ? 1.1826 0.9827 1.1323 0.2978 -0.2777 -0.2036 404 LYS A N 2990 C CA . LYS A 404 ? 1.1996 0.9845 1.1473 0.2845 -0.2818 -0.1952 404 LYS A CA 2991 C C . LYS A 404 ? 1.1633 0.9242 1.1022 0.2694 -0.2829 -0.1842 404 LYS A C 2992 O O . LYS A 404 ? 1.2442 0.9781 1.1695 0.2644 -0.2941 -0.1772 404 LYS A O 2993 C CB . LYS A 404 ? 1.2060 1.0211 1.1766 0.2762 -0.2702 -0.1948 404 LYS A CB 2994 C CG . LYS A 404 ? 1.2871 1.1176 1.2629 0.2891 -0.2747 -0.2039 404 LYS A CG 2995 C CD . LYS A 404 ? 1.3148 1.1730 1.3139 0.2806 -0.2657 -0.2045 404 LYS A CD 2996 C CE . LYS A 404 ? 1.3163 1.1937 1.3233 0.2942 -0.2696 -0.2148 404 LYS A CE 2997 N NZ . LYS A 404 ? 1.3398 1.2344 1.3518 0.3089 -0.2673 -0.2231 404 LYS A NZ 2998 N N . THR A 405 ? 1.0727 0.8445 1.0199 0.2623 -0.2715 -0.1817 405 THR A N 2999 C CA . THR A 405 ? 1.0682 0.8211 1.0092 0.2480 -0.2713 -0.1719 405 THR A CA 3000 C C . THR A 405 ? 1.0718 0.7881 0.9906 0.2529 -0.2880 -0.1712 405 THR A C 3001 O O . THR A 405 ? 0.9909 0.6830 0.9010 0.2428 -0.2966 -0.1619 405 THR A O 3002 C CB . THR A 405 ? 0.9756 0.7480 0.9292 0.2425 -0.2565 -0.1704 405 THR A CB 3003 O OG1 . THR A 405 ? 1.0030 0.8070 0.9800 0.2371 -0.2428 -0.1705 405 THR A OG1 3004 C CG2 . THR A 405 ? 0.8004 0.5556 0.7491 0.2271 -0.2559 -0.1603 405 THR A CG2 3005 N N . GLY A 406 ? 1.1190 0.8324 1.0295 0.2688 -0.2931 -0.1810 406 GLY A N 3006 C CA . GLY A 406 ? 1.1203 0.7987 1.0115 0.2751 -0.3107 -0.1830 406 GLY A CA 3007 C C . GLY A 406 ? 1.1008 0.7502 0.9806 0.2767 -0.3281 -0.1801 406 GLY A C 3008 O O . GLY A 406 ? 1.0465 0.6622 0.9146 0.2725 -0.3427 -0.1749 406 GLY A O 3009 N N . GLU A 407 ? 1.1584 0.8213 1.0429 0.2827 -0.3271 -0.1828 407 GLU A N 3010 C CA . GLU A 407 ? 1.3203 0.9583 1.1938 0.2868 -0.3438 -0.1801 407 GLU A CA 3011 C C . GLU A 407 ? 1.2668 0.8956 1.1417 0.2673 -0.3434 -0.1633 407 GLU A C 3012 O O . GLU A 407 ? 1.2345 0.8334 1.0985 0.2645 -0.3588 -0.1546 407 GLU A O 3013 C CB . GLU A 407 ? 1.3354 0.9934 1.2128 0.3021 -0.3433 -0.1901 407 GLU A CB 3014 C CG . GLU A 407 ? 1.4420 1.0774 1.3088 0.3067 -0.3594 -0.1864 407 GLU A CG 3015 C CD . GLU A 407 ? 1.5550 1.2098 1.4247 0.3245 -0.3604 -0.1984 407 GLU A CD 3016 O OE1 . GLU A 407 ? 1.5717 1.2345 1.4396 0.3422 -0.3623 -0.2125 407 GLU A OE1 3017 O OE2 . GLU A 407 ? 1.4632 1.1274 1.3368 0.3216 -0.3593 -0.1940 407 GLU A OE2 3018 N N . ILE A 408 ? 1.1445 0.8003 1.0338 0.2542 -0.3262 -0.1582 408 ILE A N 3019 C CA . ILE A 408 ? 1.0961 0.7493 0.9871 0.2365 -0.3238 -0.1430 408 ILE A CA 3020 C C . ILE A 408 ? 1.0995 0.7255 0.9828 0.2251 -0.3309 -0.1327 408 ILE A C 3021 O O . ILE A 408 ? 1.1839 0.7932 1.0618 0.2144 -0.3385 -0.1186 408 ILE A O 3022 C CB . ILE A 408 ? 1.0298 0.7168 0.9385 0.2261 -0.3047 -0.1421 408 ILE A CB 3023 C CG1 . ILE A 408 ? 0.8825 0.5967 0.8017 0.2351 -0.2990 -0.1511 408 ILE A CG1 3024 C CG2 . ILE A 408 ? 1.1400 0.8244 1.0489 0.2085 -0.3025 -0.1269 408 ILE A CG2 3025 C CD1 . ILE A 408 ? 0.8198 0.5675 0.7603 0.2303 -0.2815 -0.1563 408 ILE A CD1 3026 N N . LEU A 409 ? 1.0844 0.7080 0.9679 0.2277 -0.3285 -0.1394 409 LEU A N 3027 C CA . LEU A 409 ? 1.1206 0.7241 1.0003 0.2155 -0.3328 -0.1308 409 LEU A CA 3028 C C . LEU A 409 ? 1.1320 0.6954 0.9975 0.2201 -0.3552 -0.1290 409 LEU A C 3029 O O . LEU A 409 ? 1.1545 0.6973 1.0172 0.2101 -0.3623 -0.1217 409 LEU A O 3030 C CB . LEU A 409 ? 1.0969 0.7148 0.9822 0.2166 -0.3216 -0.1382 409 LEU A CB 3031 C CG . LEU A 409 ? 1.0034 0.6567 0.9054 0.2081 -0.3004 -0.1367 409 LEU A CG 3032 C CD1 . LEU A 409 ? 1.0219 0.6935 0.9298 0.2154 -0.2900 -0.1460 409 LEU A CD1 3033 C CD2 . LEU A 409 ? 0.9312 0.5839 0.8379 0.1882 -0.2954 -0.1225 409 LEU A CD2 3034 N N . LEU A 410 ? 1.1385 0.6903 0.9963 0.2352 -0.3675 -0.1358 410 LEU A N 3035 C CA . LEU A 410 ? 1.2431 0.7540 1.0885 0.2410 -0.3913 -0.1352 410 LEU A CA 3036 C C . LEU A 410 ? 1.2876 0.7762 1.1327 0.2218 -0.4000 -0.1140 410 LEU A C 3037 O O . LEU A 410 ? 1.2354 0.6889 1.0750 0.2194 -0.4185 -0.1096 410 LEU A O 3038 C CB . LEU A 410 ? 1.2213 0.7252 1.0593 0.2605 -0.4028 -0.1449 410 LEU A CB 3039 C CG . LEU A 410 ? 1.2024 0.7290 1.0406 0.2814 -0.3963 -0.1657 410 LEU A CG 3040 C CD1 . LEU A 410 ? 1.1632 0.6711 0.9907 0.3023 -0.4146 -0.1765 410 LEU A CD1 3041 C CD2 . LEU A 410 ? 1.3878 0.9159 1.2252 0.2845 -0.3933 -0.1746 410 LEU A CD2 3042 N N . THR A 411 ? 1.3381 0.8492 1.1903 0.2086 -0.3868 -0.1011 411 THR A N 3043 C CA . THR A 411 ? 1.3419 0.8425 1.1953 0.1898 -0.3909 -0.0790 411 THR A CA 3044 C C . THR A 411 ? 1.2610 0.7500 1.1182 0.1752 -0.3918 -0.0719 411 THR A C 3045 O O . THR A 411 ? 1.3276 0.7987 1.1855 0.1607 -0.4011 -0.0540 411 THR A O 3046 C CB . THR A 411 ? 1.2881 0.8240 1.1488 0.1809 -0.3731 -0.0705 411 THR A CB 3047 O OG1 . THR A 411 ? 1.1304 0.6975 1.0002 0.1833 -0.3543 -0.0835 411 THR A OG1 3048 C CG2 . THR A 411 ? 1.2823 0.8238 1.1384 0.1908 -0.3770 -0.0699 411 THR A CG2 3049 N N . LEU A 412 ? 1.0930 0.5944 0.9535 0.1788 -0.3819 -0.0851 412 LEU A N 3050 C CA . LEU A 412 ? 1.2552 0.7484 1.1192 0.1665 -0.3820 -0.0804 412 LEU A CA 3051 C C . LEU A 412 ? 1.2784 0.7361 1.1347 0.1757 -0.4026 -0.0895 412 LEU A C 3052 O O . LEU A 412 ? 1.2624 0.7232 1.1146 0.1908 -0.4017 -0.1077 412 LEU A O 3053 C CB . LEU A 412 ? 1.3072 0.8334 1.1792 0.1649 -0.3606 -0.0881 412 LEU A CB 3054 C CG . LEU A 412 ? 1.0821 0.6444 0.9630 0.1603 -0.3412 -0.0847 412 LEU A CG 3055 C CD1 . LEU A 412 ? 0.9916 0.5811 0.8820 0.1583 -0.3227 -0.0917 412 LEU A CD1 3056 C CD2 . LEU A 412 ? 0.9018 0.4668 0.7855 0.1437 -0.3409 -0.0648 412 LEU A CD2 3057 N N . LYS A 413 ? 1.2761 0.7011 1.1310 0.1665 -0.4216 -0.0764 413 LYS A N 3058 C CA . LYS A 413 ? 1.4086 0.7941 1.2573 0.1748 -0.4459 -0.0844 413 LYS A CA 3059 C C . LYS A 413 ? 1.4121 0.7926 1.2632 0.1709 -0.4470 -0.0908 413 LYS A C 3060 O O . LYS A 413 ? 1.2802 0.6430 1.1244 0.1860 -0.4598 -0.1083 413 LYS A O 3061 C CB . LYS A 413 ? 1.5698 0.9219 1.4199 0.1638 -0.4664 -0.0653 413 LYS A CB 3062 C CG . LYS A 413 ? 1.5618 0.9155 1.4077 0.1697 -0.4683 -0.0588 413 LYS A CG 3063 C CD . LYS A 413 ? 1.6505 0.9912 1.4860 0.1954 -0.4795 -0.0805 413 LYS A CD 3064 C CE . LYS A 413 ? 1.6952 1.0585 1.5273 0.2050 -0.4696 -0.0816 413 LYS A CE 3065 N NZ . LYS A 413 ? 1.7702 1.1238 1.5928 0.2309 -0.4802 -0.1032 413 LYS A NZ 3066 N N . ASN A 414 ? 1.4543 0.8521 1.3146 0.1517 -0.4337 -0.0774 414 ASN A N 3067 C CA . ASN A 414 ? 1.3694 0.7639 1.2329 0.1458 -0.4344 -0.0811 414 ASN A CA 3068 C C . ASN A 414 ? 1.3494 0.7775 1.2125 0.1539 -0.4132 -0.0948 414 ASN A C 3069 O O . ASN A 414 ? 1.3692 0.8008 1.2350 0.1488 -0.4101 -0.0969 414 ASN A O 3070 C CB . ASN A 414 ? 1.3055 0.6997 1.1801 0.1205 -0.4333 -0.0584 414 ASN A CB 3071 C CG . ASN A 414 ? 1.4245 0.7783 1.3020 0.1117 -0.4595 -0.0465 414 ASN A CG 3072 O OD1 . ASN A 414 ? 1.4363 0.7608 1.3115 0.1179 -0.4787 -0.0571 414 ASN A OD1 3073 N ND2 . ASN A 414 ? 1.7295 1.0822 1.6127 0.0972 -0.4612 -0.0238 414 ASN A ND2 3074 N N . LEU A 415 ? 1.3193 0.7722 1.1802 0.1661 -0.3992 -0.1033 415 LEU A N 3075 C CA . LEU A 415 ? 1.2730 0.7592 1.1360 0.1732 -0.3788 -0.1140 415 LEU A CA 3076 C C . LEU A 415 ? 1.2170 0.6960 1.0709 0.1921 -0.3865 -0.1331 415 LEU A C 3077 O O . LEU A 415 ? 1.3151 0.7801 1.1598 0.2100 -0.3995 -0.1454 415 LEU A O 3078 C CB . LEU A 415 ? 1.2125 0.7284 1.0790 0.1796 -0.3624 -0.1166 415 LEU A CB 3079 C CG . LEU A 415 ? 1.1603 0.7132 1.0349 0.1803 -0.3394 -0.1214 415 LEU A CG 3080 C CD1 . LEU A 415 ? 1.2252 0.7960 1.1116 0.1602 -0.3252 -0.1067 415 LEU A CD1 3081 C CD2 . LEU A 415 ? 1.0424 0.6191 0.9188 0.1953 -0.3295 -0.1320 415 LEU A CD2 3082 N N . THR A 416 ? 1.0495 0.5403 0.9054 0.1894 -0.3784 -0.1359 416 THR A N 3083 C CA . THR A 416 ? 1.1259 0.6112 0.9722 0.2068 -0.3864 -0.1528 416 THR A CA 3084 C C . THR A 416 ? 1.1792 0.7022 1.0276 0.2140 -0.3648 -0.1591 416 THR A C 3085 O O . THR A 416 ? 1.2405 0.7678 1.0805 0.2304 -0.3676 -0.1727 416 THR A O 3086 C CB . THR A 416 ? 1.2867 0.7435 1.1317 0.1981 -0.4036 -0.1507 416 THR A CB 3087 O OG1 . THR A 416 ? 1.2934 0.7692 1.1467 0.1832 -0.3885 -0.1418 416 THR A OG1 3088 C CG2 . THR A 416 ? 1.1787 0.6020 1.0273 0.1844 -0.4221 -0.1378 416 THR A CG2 3089 N N . SER A 417 ? 1.1710 0.7220 1.0311 0.2024 -0.3437 -0.1488 417 SER A N 3090 C CA . SER A 417 ? 1.0519 0.6378 0.9180 0.2055 -0.3229 -0.1509 417 SER A CA 3091 C C . SER A 417 ? 1.0227 0.6360 0.9029 0.1965 -0.3037 -0.1424 417 SER A C 3092 O O . SER A 417 ? 1.0952 0.7090 0.9840 0.1785 -0.2986 -0.1299 417 SER A O 3093 C CB . SER A 417 ? 1.0139 0.5992 0.8819 0.1948 -0.3204 -0.1458 417 SER A CB 3094 O OG . SER A 417 ? 1.0715 0.6878 0.9518 0.1863 -0.2985 -0.1385 417 SER A OG 3095 N N . LEU A 418 ? 1.0285 0.6657 0.9116 0.2095 -0.2937 -0.1497 418 LEU A N 3096 C CA . LEU A 418 ? 1.0046 0.6669 0.9025 0.2030 -0.2779 -0.1441 418 LEU A CA 3097 C C . LEU A 418 ? 1.0806 0.7776 0.9899 0.2065 -0.2588 -0.1451 418 LEU A C 3098 O O . LEU A 418 ? 1.0587 0.7657 0.9622 0.2212 -0.2578 -0.1530 418 LEU A O 3099 C CB . LEU A 418 ? 0.9031 0.5627 0.7984 0.2131 -0.2844 -0.1497 418 LEU A CB 3100 C CG . LEU A 418 ? 1.0760 0.7645 0.9871 0.2104 -0.2692 -0.1475 418 LEU A CG 3101 C CD1 . LEU A 418 ? 1.1563 0.8457 1.0771 0.1908 -0.2636 -0.1354 418 LEU A CD1 3102 C CD2 . LEU A 418 ? 1.0313 0.7200 0.9392 0.2236 -0.2759 -0.1552 418 LEU A CD2 3103 N N . ASP A 419 ? 1.0346 0.7505 0.9606 0.1933 -0.2444 -0.1367 419 ASP A N 3104 C CA . ASP A 419 ? 0.9108 0.6581 0.8518 0.1936 -0.2268 -0.1350 419 ASP A CA 3105 C C . ASP A 419 ? 1.0076 0.7747 0.9661 0.1898 -0.2175 -0.1335 419 ASP A C 3106 O O . ASP A 419 ? 1.0571 0.8248 1.0255 0.1759 -0.2138 -0.1271 419 ASP A O 3107 C CB . ASP A 419 ? 0.9119 0.6615 0.8589 0.1800 -0.2193 -0.1262 419 ASP A CB 3108 C CG . ASP A 419 ? 0.9760 0.7564 0.9402 0.1794 -0.2018 -0.1224 419 ASP A CG 3109 O OD1 . ASP A 419 ? 0.9001 0.6843 0.8691 0.1709 -0.1953 -0.1157 419 ASP A OD1 3110 O OD2 . ASP A 419 ? 0.9739 0.7750 0.9479 0.1873 -0.1950 -0.1254 419 ASP A OD2 3111 N N . ILE A 420 ? 1.0683 0.8531 1.0310 0.2029 -0.2143 -0.1401 420 ILE A N 3112 C CA . ILE A 420 ? 1.0685 0.8743 1.0501 0.2004 -0.2062 -0.1401 420 ILE A CA 3113 C C . ILE A 420 ? 1.0205 0.8588 1.0214 0.2023 -0.1908 -0.1376 420 ILE A C 3114 O O . ILE A 420 ? 1.0380 0.8979 1.0541 0.2064 -0.1853 -0.1400 420 ILE A O 3115 C CB . ILE A 420 ? 1.1125 0.9145 1.0873 0.2130 -0.2156 -0.1488 420 ILE A CB 3116 C CG1 . ILE A 420 ? 1.1489 0.9654 1.1187 0.2319 -0.2151 -0.1568 420 ILE A CG1 3117 C CG2 . ILE A 420 ? 1.1106 0.8783 1.0655 0.2122 -0.2323 -0.1495 420 ILE A CG2 3118 C CD1 . ILE A 420 ? 1.1252 0.9347 1.0846 0.2469 -0.2268 -0.1668 420 ILE A CD1 3119 N N . SER A 421 ? 0.8929 0.7350 0.8939 0.1988 -0.1844 -0.1318 421 SER A N 3120 C CA . SER A 421 ? 0.8448 0.7170 0.8635 0.1998 -0.1699 -0.1262 421 SER A CA 3121 C C . SER A 421 ? 0.8948 0.7837 0.9421 0.1866 -0.1598 -0.1202 421 SER A C 3122 O O . SER A 421 ? 0.9260 0.8038 0.9777 0.1771 -0.1637 -0.1211 421 SER A O 3123 C CB . SER A 421 ? 0.8589 0.7284 0.8698 0.1982 -0.1666 -0.1204 421 SER A CB 3124 O OG . SER A 421 ? 0.8919 0.7480 0.9073 0.1819 -0.1658 -0.1140 421 SER A OG 3125 N N . ARG A 422 ? 0.8669 0.7830 0.9339 0.1866 -0.1475 -0.1136 422 ARG A N 3126 C CA . ARG A 422 ? 0.8732 0.8065 0.9713 0.1752 -0.1390 -0.1082 422 ARG A CA 3127 C C . ARG A 422 ? 0.8848 0.8186 0.9931 0.1739 -0.1441 -0.1159 422 ARG A C 3128 O O . ARG A 422 ? 0.8753 0.8108 1.0026 0.1628 -0.1427 -0.1151 422 ARG A O 3129 C CB . ARG A 422 ? 0.8250 0.7499 0.9314 0.1605 -0.1352 -0.1005 422 ARG A CB 3130 C CG . ARG A 422 ? 0.9883 0.9175 1.0892 0.1616 -0.1287 -0.0916 422 ARG A CG 3131 C CD . ARG A 422 ? 1.2341 1.1656 1.3542 0.1477 -0.1218 -0.0820 422 ARG A CD 3132 N NE . ARG A 422 ? 1.3772 1.2999 1.4818 0.1475 -0.1207 -0.0764 422 ARG A NE 3133 C CZ . ARG A 422 ? 1.1526 1.0788 1.2697 0.1389 -0.1142 -0.0668 422 ARG A CZ 3134 N NH1 . ARG A 422 ? 0.9947 0.9318 1.1415 0.1293 -0.1085 -0.0615 422 ARG A NH1 3135 N NH2 . ARG A 422 ? 0.8752 0.7933 0.9756 0.1403 -0.1145 -0.0631 422 ARG A NH2 3136 N N . ASN A 423 ? 0.9623 0.8955 1.0578 0.1867 -0.1508 -0.1243 423 ASN A N 3137 C CA . ASN A 423 ? 0.9623 0.8996 1.0666 0.1883 -0.1556 -0.1319 423 ASN A CA 3138 C C . ASN A 423 ? 0.9031 0.8685 1.0198 0.2000 -0.1514 -0.1346 423 ASN A C 3139 O O . ASN A 423 ? 0.9899 0.9561 1.0885 0.2147 -0.1549 -0.1391 423 ASN A O 3140 C CB . ASN A 423 ? 1.0126 0.9221 1.0902 0.1931 -0.1694 -0.1395 423 ASN A CB 3141 C CG . ASN A 423 ? 1.0595 0.9467 1.1299 0.1803 -0.1736 -0.1363 423 ASN A CG 3142 O OD1 . ASN A 423 ? 1.1958 1.0811 1.2704 0.1709 -0.1680 -0.1294 423 ASN A OD1 3143 N ND2 . ASN A 423 ? 1.0077 0.8797 1.0670 0.1804 -0.1834 -0.1407 423 ASN A ND2 3144 N N . THR A 424 ? 0.7318 0.7207 0.8799 0.1939 -0.1449 -0.1324 424 THR A N 3145 C CA . THR A 424 ? 0.7183 0.7395 0.8843 0.2028 -0.1393 -0.1325 424 THR A CA 3146 C C . THR A 424 ? 0.6758 0.6987 0.8286 0.2182 -0.1477 -0.1442 424 THR A C 3147 O O . THR A 424 ? 0.7024 0.7403 0.8740 0.2185 -0.1490 -0.1490 424 THR A O 3148 C CB . THR A 424 ? 0.8073 0.8503 1.0135 0.1907 -0.1329 -0.1278 424 THR A CB 3149 O OG1 . THR A 424 ? 0.9918 1.0151 1.2033 0.1768 -0.1364 -0.1284 424 THR A OG1 3150 C CG2 . THR A 424 ? 0.7705 0.8398 0.9984 0.1871 -0.1201 -0.1136 424 THR A CG2 3151 N N . PHE A 425 ? 0.6971 0.7054 0.8188 0.2317 -0.1542 -0.1492 425 PHE A N 3152 C CA . PHE A 425 ? 0.7751 0.7768 0.8793 0.2472 -0.1652 -0.1612 425 PHE A CA 3153 C C . PHE A 425 ? 0.9109 0.9474 1.0312 0.2594 -0.1615 -0.1653 425 PHE A C 3154 O O . PHE A 425 ? 0.9029 0.9709 1.0385 0.2625 -0.1505 -0.1585 425 PHE A O 3155 C CB . PHE A 425 ? 0.8387 0.8174 0.9085 0.2597 -0.1737 -0.1656 425 PHE A CB 3156 C CG . PHE A 425 ? 1.0133 0.9520 1.0625 0.2515 -0.1842 -0.1661 425 PHE A CG 3157 C CD1 . PHE A 425 ? 0.9453 0.8682 0.9836 0.2448 -0.1829 -0.1599 425 PHE A CD1 3158 C CD2 . PHE A 425 ? 1.1108 1.0296 1.1523 0.2506 -0.1953 -0.1718 425 PHE A CD2 3159 C CE1 . PHE A 425 ? 0.9352 0.8240 0.9569 0.2364 -0.1924 -0.1590 425 PHE A CE1 3160 C CE2 . PHE A 425 ? 1.0378 0.9230 1.0619 0.2424 -0.2044 -0.1697 425 PHE A CE2 3161 C CZ . PHE A 425 ? 0.8887 0.7594 0.9037 0.2348 -0.2028 -0.1632 425 PHE A CZ 3162 N N . HIS A 426 ? 0.9607 0.9927 1.0774 0.2665 -0.1710 -0.1756 426 HIS A N 3163 C CA . HIS A 426 ? 1.0066 1.0668 1.1300 0.2826 -0.1710 -0.1823 426 HIS A CA 3164 C C . HIS A 426 ? 1.0086 1.0671 1.1048 0.3022 -0.1745 -0.1870 426 HIS A C 3165 O O . HIS A 426 ? 0.9191 0.9468 0.9893 0.3033 -0.1812 -0.1879 426 HIS A O 3166 C CB . HIS A 426 ? 1.2287 1.2798 1.3495 0.2876 -0.1826 -0.1934 426 HIS A CB 3167 C CG . HIS A 426 ? 1.2589 1.3136 1.4049 0.2719 -0.1813 -0.1922 426 HIS A CG 3168 N ND1 . HIS A 426 ? 1.3277 1.4095 1.5092 0.2592 -0.1701 -0.1845 426 HIS A ND1 3169 C CD2 . HIS A 426 ? 1.1167 1.1523 1.2577 0.2681 -0.1911 -0.1981 426 HIS A CD2 3170 C CE1 . HIS A 426 ? 1.1423 1.2201 1.3394 0.2488 -0.1738 -0.1877 426 HIS A CE1 3171 N NE2 . HIS A 426 ? 1.1015 1.1530 1.2737 0.2544 -0.1859 -0.1959 426 HIS A NE2 3172 N N . PRO A 427 ? 1.0630 1.1554 1.1655 0.3184 -0.1708 -0.1907 427 PRO A N 3173 C CA . PRO A 427 ? 1.1526 1.2495 1.2306 0.3402 -0.1742 -0.1970 427 PRO A CA 3174 C C . PRO A 427 ? 1.1217 1.1779 1.1653 0.3530 -0.1932 -0.2105 427 PRO A C 3175 O O . PRO A 427 ? 1.1361 1.1837 1.1775 0.3584 -0.2029 -0.2191 427 PRO A O 3176 C CB . PRO A 427 ? 1.1982 1.3417 1.2939 0.3544 -0.1681 -0.1999 427 PRO A CB 3177 C CG . PRO A 427 ? 1.1518 1.3203 1.2870 0.3356 -0.1568 -0.1894 427 PRO A CG 3178 C CD . PRO A 427 ? 1.0581 1.1892 1.1931 0.3176 -0.1637 -0.1897 427 PRO A CD 3179 N N . MET A 428 ? 1.0988 1.1305 1.1170 0.3580 -0.1991 -0.2120 428 MET A N 3180 C CA . MET A 428 ? 1.1392 1.1292 1.1268 0.3688 -0.2187 -0.2235 428 MET A CA 3181 C C . MET A 428 ? 1.1746 1.1773 1.1513 0.3952 -0.2276 -0.2380 428 MET A C 3182 O O . MET A 428 ? 1.1304 1.1731 1.1139 0.4092 -0.2186 -0.2395 428 MET A O 3183 C CB . MET A 428 ? 1.1230 1.0871 1.0889 0.3688 -0.2237 -0.2225 428 MET A CB 3184 C CG . MET A 428 ? 1.1380 1.1340 1.1020 0.3822 -0.2143 -0.2222 428 MET A CG 3185 S SD . MET A 428 ? 1.6546 1.6184 1.5904 0.3857 -0.2237 -0.2247 428 MET A SD 3186 C CE . MET A 428 ? 1.4222 1.3871 1.3766 0.3565 -0.2077 -0.2053 428 MET A CE 3187 N N . PRO A 429 ? 1.2989 1.2686 1.2588 0.4026 -0.2456 -0.2479 429 PRO A N 3188 C CA . PRO A 429 ? 1.3730 1.3491 1.3222 0.4278 -0.2569 -0.2629 429 PRO A CA 3189 C C . PRO A 429 ? 1.4505 1.4052 1.3705 0.4485 -0.2715 -0.2747 429 PRO A C 3190 O O . PRO A 429 ? 1.5017 1.4437 1.4123 0.4435 -0.2704 -0.2708 429 PRO A O 3191 C CB . PRO A 429 ? 1.3068 1.2511 1.2524 0.4219 -0.2702 -0.2651 429 PRO A CB 3192 C CG . PRO A 429 ? 1.3304 1.2478 1.2796 0.3951 -0.2674 -0.2519 429 PRO A CG 3193 C CD . PRO A 429 ? 1.3241 1.2477 1.2742 0.3870 -0.2567 -0.2442 429 PRO A CD 3194 N N . ASP A 430 ? 1.4250 1.3752 1.3313 0.4722 -0.2862 -0.2900 430 ASP A N 3195 C CA . ASP A 430 ? 1.5106 1.4376 1.3893 0.4945 -0.3038 -0.3043 430 ASP A CA 3196 C C . ASP A 430 ? 1.4588 1.3237 1.3192 0.4862 -0.3245 -0.3050 430 ASP A C 3197 O O . ASP A 430 ? 1.3024 1.1404 1.1448 0.4915 -0.3359 -0.3099 430 ASP A O 3198 C CB . ASP A 430 ? 1.6596 1.6072 1.5315 0.5250 -0.3125 -0.3215 430 ASP A CB 3199 C CG . ASP A 430 ? 1.7974 1.8058 1.6791 0.5406 -0.2957 -0.3234 430 ASP A CG 3200 O OD1 . ASP A 430 ? 1.7992 1.8418 1.6889 0.5572 -0.2935 -0.3309 430 ASP A OD1 3201 O OD2 . ASP A 430 ? 1.8406 1.8642 1.7222 0.5367 -0.2846 -0.3168 430 ASP A OD2 3202 N N . SER A 431 ? 1.5680 1.4117 1.4340 0.4730 -0.3295 -0.2992 431 SER A N 3203 C CA . SER A 431 ? 1.5128 1.3003 1.3630 0.4660 -0.3500 -0.2980 431 SER A CA 3204 C C . SER A 431 ? 1.4497 1.2193 1.3097 0.4349 -0.3430 -0.2798 431 SER A C 3205 O O . SER A 431 ? 1.4260 1.2095 1.3014 0.4232 -0.3343 -0.2725 431 SER A O 3206 C CB . SER A 431 ? 1.4279 1.2006 1.2705 0.4821 -0.3670 -0.3080 431 SER A CB 3207 O OG . SER A 431 ? 1.4650 1.1859 1.2865 0.4889 -0.3921 -0.3135 431 SER A OG 3208 N N . CYS A 432 ? 1.4246 1.1655 1.2761 0.4227 -0.3474 -0.2734 432 CYS A N 3209 C CA . CYS A 432 ? 1.4339 1.1550 1.2917 0.3949 -0.3433 -0.2568 432 CYS A CA 3210 C C . CYS A 432 ? 1.3914 1.0605 1.2314 0.3914 -0.3648 -0.2552 432 CYS A C 3211 O O . CYS A 432 ? 1.1870 0.8376 1.0116 0.4090 -0.3806 -0.2673 432 CYS A O 3212 C CB . CYS A 432 ? 1.3440 1.0892 1.2149 0.3789 -0.3230 -0.2471 432 CYS A CB 3213 S SG . CYS A 432 ? 1.8845 1.6916 1.7797 0.3814 -0.2976 -0.2465 432 CYS A SG 3214 N N . GLN A 433 ? 1.4948 1.1415 1.3377 0.3693 -0.3663 -0.2404 433 GLN A N 3215 C CA . GLN A 433 ? 1.4720 1.0730 1.3026 0.3611 -0.3840 -0.2348 433 GLN A CA 3216 C C . GLN A 433 ? 1.4458 1.0486 1.2848 0.3366 -0.3715 -0.2201 433 GLN A C 3217 O O . GLN A 433 ? 1.5052 1.1342 1.3589 0.3226 -0.3533 -0.2110 433 GLN A O 3218 C CB . GLN A 433 ? 1.4778 1.0472 1.3032 0.3569 -0.4002 -0.2276 433 GLN A CB 3219 C CG . GLN A 433 ? 1.5176 1.0970 1.3420 0.3738 -0.4046 -0.2361 433 GLN A CG 3220 C CD . GLN A 433 ? 1.6007 1.1470 1.4191 0.3682 -0.4209 -0.2263 433 GLN A CD 3221 O OE1 . GLN A 433 ? 1.5087 1.0140 1.3149 0.3730 -0.4432 -0.2268 433 GLN A OE1 3222 N NE2 . GLN A 433 ? 1.6833 1.2473 1.5109 0.3580 -0.4106 -0.2166 433 GLN A NE2 3223 N N . TRP A 434 ? 1.3273 0.9021 1.1578 0.3318 -0.3823 -0.2185 434 TRP A N 3224 C CA . TRP A 434 ? 1.2545 0.8275 1.0919 0.3088 -0.3730 -0.2044 434 TRP A CA 3225 C C . TRP A 434 ? 1.3047 0.8329 1.1334 0.2995 -0.3933 -0.1975 434 TRP A C 3226 O O . TRP A 434 ? 1.4364 0.9341 1.2541 0.3120 -0.4151 -0.2049 434 TRP A O 3227 C CB . TRP A 434 ? 1.1873 0.7849 1.0276 0.3117 -0.3595 -0.2096 434 TRP A CB 3228 C CG . TRP A 434 ? 1.2477 0.8898 1.0980 0.3217 -0.3408 -0.2155 434 TRP A CG 3229 C CD1 . TRP A 434 ? 1.3789 1.0377 1.2243 0.3454 -0.3430 -0.2302 434 TRP A CD1 3230 C CD2 . TRP A 434 ? 1.2273 0.9040 1.0959 0.3082 -0.3178 -0.2064 434 TRP A CD2 3231 N NE1 . TRP A 434 ? 1.4370 1.1401 1.2977 0.3464 -0.3220 -0.2293 434 TRP A NE1 3232 C CE2 . TRP A 434 ? 1.2727 0.9857 1.1483 0.3234 -0.3070 -0.2149 434 TRP A CE2 3233 C CE3 . TRP A 434 ? 1.1750 0.8558 1.0555 0.2852 -0.3060 -0.1922 434 TRP A CE3 3234 C CZ2 . TRP A 434 ? 1.1067 0.8575 1.0026 0.3150 -0.2857 -0.2087 434 TRP A CZ2 3235 C CZ3 . TRP A 434 ? 1.1712 0.8882 1.0702 0.2784 -0.2856 -0.1879 434 TRP A CZ3 3236 C CH2 . TRP A 434 ? 1.0868 0.8372 0.9942 0.2926 -0.2761 -0.1957 434 TRP A CH2 3237 N N . PRO A 435 ? 1.2677 0.7919 1.1030 0.2772 -0.3870 -0.1828 435 PRO A N 3238 C CA . PRO A 435 ? 1.3520 0.8369 1.1821 0.2665 -0.4054 -0.1750 435 PRO A CA 3239 C C . PRO A 435 ? 1.3909 0.8536 1.2094 0.2837 -0.4234 -0.1911 435 PRO A C 3240 O O . PRO A 435 ? 1.3819 0.8649 1.1986 0.2933 -0.4147 -0.2018 435 PRO A O 3241 C CB . PRO A 435 ? 1.3153 0.8142 1.1554 0.2448 -0.3898 -0.1619 435 PRO A CB 3242 C CG . PRO A 435 ? 1.2815 0.8160 1.1327 0.2387 -0.3683 -0.1561 435 PRO A CG 3243 C CD . PRO A 435 ? 1.2216 0.7768 1.0711 0.2600 -0.3639 -0.1716 435 PRO A CD 3244 N N . GLU A 436 ? 1.4279 0.8498 1.2388 0.2881 -0.4491 -0.1926 436 GLU A N 3245 C CA . GLU A 436 ? 1.5698 0.9689 1.3690 0.3084 -0.4696 -0.2113 436 GLU A CA 3246 C C . GLU A 436 ? 1.5486 0.9410 1.3479 0.3015 -0.4719 -0.2127 436 GLU A C 3247 O O . GLU A 436 ? 1.5974 0.9783 1.3870 0.3196 -0.4860 -0.2304 436 GLU A O 3248 C CB . GLU A 436 ? 1.8103 1.1636 1.6037 0.3139 -0.4989 -0.2120 436 GLU A CB 3249 C CG . GLU A 436 ? 1.9854 1.3302 1.7661 0.3453 -0.5153 -0.2357 436 GLU A CG 3250 C CD . GLU A 436 ? 2.0757 1.4413 1.8557 0.3569 -0.5070 -0.2382 436 GLU A CD 3251 O OE1 . GLU A 436 ? 2.0804 1.4216 1.8527 0.3735 -0.5275 -0.2472 436 GLU A OE1 3252 O OE2 . GLU A 436 ? 2.0584 1.4642 1.8464 0.3495 -0.4810 -0.2314 436 GLU A OE2 3253 N N . LYS A 437 ? 1.4691 0.8699 1.2790 0.2768 -0.4585 -0.1950 437 LYS A N 3254 C CA . LYS A 437 ? 1.3025 0.6997 1.1137 0.2685 -0.4591 -0.1948 437 LYS A CA 3255 C C . LYS A 437 ? 1.2265 0.6673 1.0425 0.2658 -0.4315 -0.1942 437 LYS A C 3256 O O . LYS A 437 ? 1.0945 0.5378 0.9136 0.2556 -0.4275 -0.1905 437 LYS A O 3257 C CB . LYS A 437 ? 1.2476 0.6191 1.0680 0.2422 -0.4677 -0.1748 437 LYS A CB 3258 C CG . LYS A 437 ? 1.4624 0.7881 1.2809 0.2420 -0.4965 -0.1719 437 LYS A CG 3259 C CD . LYS A 437 ? 1.6727 0.9697 1.4995 0.2215 -0.5112 -0.1588 437 LYS A CD 3260 C CE . LYS A 437 ? 1.7341 1.0408 1.5737 0.1937 -0.4985 -0.1315 437 LYS A CE 3261 N NZ . LYS A 437 ? 1.7602 1.0303 1.6087 0.1757 -0.5203 -0.1163 437 LYS A NZ 3262 N N . MET A 438 ? 1.3163 0.7909 1.1344 0.2744 -0.4132 -0.1973 438 MET A N 3263 C CA . MET A 438 ? 1.2318 0.7480 1.0573 0.2713 -0.3871 -0.1951 438 MET A CA 3264 C C . MET A 438 ? 1.2809 0.8079 1.0971 0.2897 -0.3881 -0.2106 438 MET A C 3265 O O . MET A 438 ? 1.2655 0.8038 1.0733 0.3130 -0.3908 -0.2258 438 MET A O 3266 C CB . MET A 438 ? 1.1404 0.6883 0.9730 0.2757 -0.3699 -0.1943 438 MET A CB 3267 C CG . MET A 438 ? 1.1580 0.7466 1.0033 0.2679 -0.3434 -0.1882 438 MET A CG 3268 S SD . MET A 438 ? 1.2267 0.8541 1.0831 0.2750 -0.3252 -0.1898 438 MET A SD 3269 C CE . MET A 438 ? 3.8810 3.4977 3.7466 0.2544 -0.3246 -0.1747 438 MET A CE 3270 N N . ARG A 439 ? 1.2543 0.7792 1.0715 0.2800 -0.3865 -0.2068 439 ARG A N 3271 C CA . ARG A 439 ? 1.2928 0.8286 1.1003 0.2968 -0.3878 -0.2204 439 ARG A CA 3272 C C . ARG A 439 ? 1.3727 0.9532 1.1878 0.2950 -0.3605 -0.2150 439 ARG A C 3273 O O . ARG A 439 ? 1.4356 1.0374 1.2431 0.3123 -0.3561 -0.2252 439 ARG A O 3274 C CB . ARG A 439 ? 1.3380 0.8441 1.1417 0.2893 -0.4047 -0.2210 439 ARG A CB 3275 C CG . ARG A 439 ? 1.3676 0.8254 1.1687 0.2849 -0.4330 -0.2218 439 ARG A CG 3276 C CD . ARG A 439 ? 1.5098 0.9444 1.3135 0.2707 -0.4452 -0.2174 439 ARG A CD 3277 N NE . ARG A 439 ? 1.6243 1.0739 1.4417 0.2447 -0.4268 -0.1973 439 ARG A NE 3278 C CZ . ARG A 439 ? 1.5455 1.0244 1.3657 0.2411 -0.4081 -0.1946 439 ARG A CZ 3279 N NH1 . ARG A 439 ? 1.5365 1.0352 1.3466 0.2614 -0.4040 -0.2090 439 ARG A NH1 3280 N NH2 . ARG A 439 ? 1.3878 0.8775 1.2207 0.2180 -0.3936 -0.1770 439 ARG A NH2 3281 N N . PHE A 440 ? 1.3888 0.9838 1.2190 0.2745 -0.3428 -0.1987 440 PHE A N 3282 C CA . PHE A 440 ? 1.2359 0.8694 1.0764 0.2699 -0.3182 -0.1916 440 PHE A CA 3283 C C . PHE A 440 ? 1.1155 0.7736 0.9698 0.2653 -0.3018 -0.1850 440 PHE A C 3284 O O . PHE A 440 ? 1.2550 0.9025 1.1174 0.2499 -0.3017 -0.1758 440 PHE A O 3285 C CB . PHE A 440 ? 1.1035 0.7320 0.9514 0.2484 -0.3128 -0.1789 440 PHE A CB 3286 C CG . PHE A 440 ? 1.1811 0.8454 1.0413 0.2420 -0.2889 -0.1702 440 PHE A CG 3287 C CD1 . PHE A 440 ? 1.3113 0.9856 1.1683 0.2438 -0.2844 -0.1701 440 PHE A CD1 3288 C CD2 . PHE A 440 ? 1.1875 0.8745 1.0632 0.2341 -0.2722 -0.1620 440 PHE A CD2 3289 C CE1 . PHE A 440 ? 1.2364 0.9418 1.1055 0.2376 -0.2634 -0.1607 440 PHE A CE1 3290 C CE2 . PHE A 440 ? 1.1207 0.8378 1.0098 0.2278 -0.2522 -0.1537 440 PHE A CE2 3291 C CZ . PHE A 440 ? 1.1951 0.9210 1.0810 0.2294 -0.2477 -0.1523 440 PHE A CZ 3292 N N . LEU A 441 ? 0.9453 0.6378 0.8029 0.2790 -0.2883 -0.1894 441 LEU A N 3293 C CA . LEU A 441 ? 0.9554 0.6750 0.8295 0.2744 -0.2720 -0.1832 441 LEU A CA 3294 C C . LEU A 441 ? 1.0473 0.8049 0.9346 0.2721 -0.2504 -0.1761 441 LEU A C 3295 O O . LEU A 441 ? 1.1110 0.8885 0.9921 0.2879 -0.2467 -0.1816 441 LEU A O 3296 C CB . LEU A 441 ? 0.9511 0.6773 0.8204 0.2936 -0.2777 -0.1946 441 LEU A CB 3297 C CG . LEU A 441 ? 1.0839 0.8372 0.9715 0.2893 -0.2632 -0.1895 441 LEU A CG 3298 C CD1 . LEU A 441 ? 1.1994 0.9363 1.0964 0.2681 -0.2633 -0.1792 441 LEU A CD1 3299 C CD2 . LEU A 441 ? 1.0622 0.8241 0.9450 0.3095 -0.2694 -0.2015 441 LEU A CD2 3300 N N . ASN A 442 ? 0.8954 0.6638 0.8013 0.2533 -0.2368 -0.1637 442 ASN A N 3301 C CA . ASN A 442 ? 0.8284 0.6304 0.7501 0.2494 -0.2173 -0.1553 442 ASN A CA 3302 C C . ASN A 442 ? 0.9399 0.7677 0.8809 0.2485 -0.2060 -0.1529 442 ASN A C 3303 O O . ASN A 442 ? 1.0319 0.8528 0.9837 0.2356 -0.2055 -0.1490 442 ASN A O 3304 C CB . ASN A 442 ? 0.9104 0.7049 0.8400 0.2293 -0.2117 -0.1440 442 ASN A CB 3305 C CG . ASN A 442 ? 1.0943 0.9192 1.0387 0.2258 -0.1938 -0.1347 442 ASN A CG 3306 O OD1 . ASN A 442 ? 1.0207 0.8756 0.9764 0.2334 -0.1827 -0.1333 442 ASN A OD1 3307 N ND2 . ASN A 442 ? 1.1986 1.0163 1.1443 0.2136 -0.1911 -0.1272 442 ASN A ND2 3308 N N . LEU A 443 ? 1.0756 0.9345 1.0209 0.2632 -0.1978 -0.1555 443 LEU A N 3309 C CA . LEU A 443 ? 0.9400 0.8272 0.9058 0.2638 -0.1875 -0.1534 443 LEU A CA 3310 C C . LEU A 443 ? 0.9208 0.8441 0.9073 0.2596 -0.1688 -0.1418 443 LEU A C 3311 O O . LEU A 443 ? 0.9233 0.8781 0.9264 0.2648 -0.1594 -0.1397 443 LEU A O 3312 C CB . LEU A 443 ? 0.9347 0.8315 0.8907 0.2856 -0.1943 -0.1657 443 LEU A CB 3313 C CG . LEU A 443 ? 1.0239 0.8875 0.9625 0.2918 -0.2133 -0.1770 443 LEU A CG 3314 C CD1 . LEU A 443 ? 0.9316 0.8105 0.8658 0.3131 -0.2180 -0.1886 443 LEU A CD1 3315 C CD2 . LEU A 443 ? 1.1033 0.9508 1.0532 0.2730 -0.2142 -0.1712 443 LEU A CD2 3316 N N . SER A 444 ? 0.9004 0.8193 0.8869 0.2499 -0.1640 -0.1334 444 SER A N 3317 C CA . SER A 444 ? 1.0478 0.9979 1.0528 0.2457 -0.1474 -0.1205 444 SER A CA 3318 C C . SER A 444 ? 1.0769 1.0431 1.1138 0.2308 -0.1368 -0.1117 444 SER A C 3319 O O . SER A 444 ? 1.1612 1.1102 1.2046 0.2202 -0.1420 -0.1147 444 SER A O 3320 C CB . SER A 444 ? 1.1246 1.0621 1.1222 0.2377 -0.1463 -0.1139 444 SER A CB 3321 O OG . SER A 444 ? 1.1571 1.1213 1.1749 0.2310 -0.1308 -0.0995 444 SER A OG 3322 N N . SER A 445 ? 1.0472 1.0475 1.1047 0.2306 -0.1227 -0.1005 445 SER A N 3323 C CA . SER A 445 ? 1.0812 1.0966 1.1726 0.2154 -0.1133 -0.0909 445 SER A CA 3324 C C . SER A 445 ? 1.0142 1.0267 1.1157 0.2140 -0.1189 -0.0998 445 SER A C 3325 O O . SER A 445 ? 0.8046 0.8150 0.9284 0.1999 -0.1174 -0.0973 445 SER A O 3326 C CB . SER A 445 ? 1.1191 1.1157 1.2180 0.1975 -0.1120 -0.0837 445 SER A CB 3327 O OG . SER A 445 ? 1.1509 1.1445 1.2343 0.2005 -0.1099 -0.0783 445 SER A OG 3328 N N . THR A 446 ? 1.0506 1.0643 1.1355 0.2302 -0.1260 -0.1108 446 THR A N 3329 C CA . THR A 446 ? 0.9383 0.9433 1.0249 0.2315 -0.1344 -0.1212 446 THR A CA 3330 C C . THR A 446 ? 0.8965 0.9371 1.0061 0.2376 -0.1278 -0.1208 446 THR A C 3331 O O . THR A 446 ? 0.8199 0.8580 0.9306 0.2418 -0.1346 -0.1302 446 THR A O 3332 C CB . THR A 446 ? 0.9731 0.9509 1.0262 0.2450 -0.1495 -0.1344 446 THR A CB 3333 O OG1 . THR A 446 ? 1.1686 1.1211 1.2186 0.2380 -0.1597 -0.1408 446 THR A OG1 3334 C CG2 . THR A 446 ? 0.8465 0.8451 0.8907 0.2667 -0.1511 -0.1423 446 THR A CG2 3335 N N . GLY A 447 ? 0.9799 1.0547 1.1086 0.2379 -0.1145 -0.1088 447 GLY A N 3336 C CA . GLY A 447 ? 1.0237 1.1364 1.1797 0.2411 -0.1068 -0.1052 447 GLY A CA 3337 C C . GLY A 447 ? 1.0554 1.1901 1.1992 0.2631 -0.1089 -0.1138 447 GLY A C 3338 O O . GLY A 447 ? 0.9901 1.1612 1.1577 0.2663 -0.1016 -0.1096 447 GLY A O 3339 N N . ILE A 448 ? 1.0228 1.1366 1.1312 0.2787 -0.1195 -0.1261 448 ILE A N 3340 C CA . ILE A 448 ? 1.0308 1.1609 1.1254 0.3015 -0.1244 -0.1376 448 ILE A CA 3341 C C . ILE A 448 ? 1.1518 1.3271 1.2493 0.3164 -0.1128 -0.1304 448 ILE A C 3342 O O . ILE A 448 ? 1.1867 1.3748 1.2889 0.3113 -0.1026 -0.1170 448 ILE A O 3343 C CB . ILE A 448 ? 1.0410 1.1326 1.0980 0.3144 -0.1418 -0.1537 448 ILE A CB 3344 C CG1 . ILE A 448 ? 1.0379 1.1143 1.0722 0.3175 -0.1432 -0.1518 448 ILE A CG1 3345 C CG2 . ILE A 448 ? 1.0839 1.1370 1.1387 0.3016 -0.1530 -0.1596 448 ILE A CG2 3346 C CD1 . ILE A 448 ? 0.9936 1.0306 0.9935 0.3294 -0.1619 -0.1674 448 ILE A CD1 3347 N N . ARG A 449 ? 1.1569 1.3580 1.2514 0.3359 -0.1145 -0.1391 449 ARG A N 3348 C CA . ARG A 449 ? 1.0936 1.3444 1.1912 0.3527 -0.1033 -0.1327 449 ARG A CA 3349 C C . ARG A 449 ? 1.1372 1.3953 1.2061 0.3825 -0.1131 -0.1507 449 ARG A C 3350 O O . ARG A 449 ? 1.2300 1.5353 1.3040 0.3994 -0.1050 -0.1486 449 ARG A O 3351 C CB . ARG A 449 ? 0.9638 1.2601 1.1031 0.3433 -0.0889 -0.1182 449 ARG A CB 3352 C CG . ARG A 449 ? 0.9847 1.2661 1.1465 0.3282 -0.0941 -0.1223 449 ARG A CG 3353 C CD . ARG A 449 ? 1.1802 1.4957 1.3882 0.3099 -0.0803 -0.1038 449 ARG A CD 3354 N NE . ARG A 449 ? 1.3985 1.7626 1.6270 0.3208 -0.0743 -0.1023 449 ARG A NE 3355 C CZ . ARG A 449 ? 1.4147 1.8139 1.6867 0.3073 -0.0638 -0.0874 449 ARG A CZ 3356 N NH1 . ARG A 449 ? 1.3693 1.7581 1.6681 0.2831 -0.0590 -0.0734 449 ARG A NH1 3357 N NH2 . ARG A 449 ? 1.3552 1.8001 1.6448 0.3183 -0.0590 -0.0865 449 ARG A NH2 3358 N N . VAL A 450 ? 1.0238 1.2357 1.0633 0.3892 -0.1312 -0.1678 450 VAL A N 3359 C CA . VAL A 450 ? 1.1136 1.3229 1.1251 0.4173 -0.1445 -0.1873 450 VAL A CA 3360 C C . VAL A 450 ? 1.1882 1.3380 1.1708 0.4158 -0.1633 -0.1993 450 VAL A C 3361 O O . VAL A 450 ? 1.2153 1.3312 1.2043 0.3936 -0.1661 -0.1943 450 VAL A O 3362 C CB . VAL A 450 ? 1.0326 1.2552 1.0555 0.4251 -0.1489 -0.1965 450 VAL A CB 3363 C CG1 . VAL A 450 ? 1.0198 1.2143 1.0111 0.4483 -0.1697 -0.2193 450 VAL A CG1 3364 C CG2 . VAL A 450 ? 0.8877 1.1753 0.9354 0.4338 -0.1326 -0.1875 450 VAL A CG2 3365 N N . VAL A 451 ? 1.2178 1.3553 1.1696 0.4391 -0.1767 -0.2149 451 VAL A N 3366 C CA . VAL A 451 ? 1.2200 1.2993 1.1472 0.4381 -0.1976 -0.2272 451 VAL A CA 3367 C C . VAL A 451 ? 1.2563 1.3223 1.1633 0.4630 -0.2164 -0.2482 451 VAL A C 3368 O O . VAL A 451 ? 1.3274 1.4138 1.2182 0.4896 -0.2205 -0.2599 451 VAL A O 3369 C CB . VAL A 451 ? 1.1343 1.1933 1.0423 0.4375 -0.2014 -0.2265 451 VAL A CB 3370 C CG1 . VAL A 451 ? 1.1283 1.1276 1.0146 0.4351 -0.2241 -0.2382 451 VAL A CG1 3371 C CG2 . VAL A 451 ? 0.9326 1.0007 0.8606 0.4124 -0.1842 -0.2058 451 VAL A CG2 3372 N N . LYS A 452 ? 1.1739 1.2069 1.0819 0.4551 -0.2281 -0.2529 452 LYS A N 3373 C CA . LYS A 452 ? 1.2754 1.2914 1.1662 0.4768 -0.2472 -0.2716 452 LYS A CA 3374 C C . LYS A 452 ? 1.3407 1.2975 1.2059 0.4781 -0.2706 -0.2817 452 LYS A C 3375 O O . LYS A 452 ? 1.2622 1.1947 1.1230 0.4626 -0.2710 -0.2743 452 LYS A O 3376 C CB . LYS A 452 ? 1.2299 1.2493 1.1383 0.4697 -0.2465 -0.2705 452 LYS A CB 3377 C CG . LYS A 452 ? 1.2719 1.3492 1.2078 0.4704 -0.2270 -0.2629 452 LYS A CG 3378 C CD . LYS A 452 ? 1.4507 1.5589 1.3795 0.5012 -0.2318 -0.2779 452 LYS A CD 3379 C CE . LYS A 452 ? 1.4622 1.5978 1.4148 0.4995 -0.2261 -0.2768 452 LYS A CE 3380 N NZ . LYS A 452 ? 1.4133 1.5840 1.4010 0.4767 -0.2045 -0.2578 452 LYS A NZ 3381 N N . THR A 453 ? 1.3439 1.2782 1.1938 0.4964 -0.2904 -0.2979 453 THR A N 3382 C CA . THR A 453 ? 1.3354 1.2125 1.1629 0.4993 -0.3155 -0.3078 453 THR A CA 3383 C C . THR A 453 ? 1.3857 1.2212 1.2196 0.4724 -0.3210 -0.2965 453 THR A C 3384 O O . THR A 453 ? 1.3262 1.1147 1.1459 0.4732 -0.3426 -0.3024 453 THR A O 3385 C CB . THR A 453 ? 1.3971 1.2643 1.2071 0.5295 -0.3362 -0.3291 453 THR A CB 3386 O OG1 . THR A 453 ? 1.2927 1.1975 1.1164 0.5384 -0.3269 -0.3306 453 THR A OG1 3387 C CG2 . THR A 453 ? 1.3944 1.2747 1.1853 0.5571 -0.3432 -0.3447 453 THR A CG2 3388 N N . CYS A 454 ? 1.4075 1.2620 1.2636 0.4491 -0.3019 -0.2800 454 CYS A N 3389 C CA . CYS A 454 ? 1.2572 1.0797 1.1201 0.4229 -0.3037 -0.2677 454 CYS A CA 3390 C C . CYS A 454 ? 1.3453 1.1319 1.1956 0.4123 -0.3124 -0.2640 454 CYS A C 3391 O O . CYS A 454 ? 1.4384 1.1807 1.2774 0.4075 -0.3306 -0.2650 454 CYS A O 3392 C CB . CYS A 454 ? 1.1516 1.0065 1.0412 0.4025 -0.2809 -0.2527 454 CYS A CB 3393 S SG . CYS A 454 ? 1.4448 1.2703 1.3443 0.3724 -0.2808 -0.2385 454 CYS A SG 3394 N N . ILE A 455 ? 1.2946 1.1017 1.1478 0.4089 -0.2995 -0.2591 455 ILE A N 3395 C CA . ILE A 455 ? 1.3012 1.0809 1.1431 0.4011 -0.3064 -0.2568 455 ILE A CA 3396 C C . ILE A 455 ? 1.4461 1.1864 1.2649 0.4179 -0.3332 -0.2721 455 ILE A C 3397 O O . ILE A 455 ? 1.4054 1.1571 1.2123 0.4445 -0.3410 -0.2881 455 ILE A O 3398 C CB . ILE A 455 ? 1.2984 1.1126 1.1422 0.4059 -0.2911 -0.2543 455 ILE A CB 3399 C CG1 . ILE A 455 ? 1.2021 1.0468 1.0704 0.3848 -0.2668 -0.2365 455 ILE A CG1 3400 C CG2 . ILE A 455 ? 1.4113 1.1973 1.2398 0.4040 -0.3021 -0.2564 455 ILE A CG2 3401 C CD1 . ILE A 455 ? 1.2073 1.0854 1.0941 0.3865 -0.2550 -0.2342 455 ILE A CD1 3402 N N . PRO A 456 ? 1.5816 1.2763 1.3950 0.4025 -0.3478 -0.2672 456 PRO A N 3403 C CA . PRO A 456 ? 1.6418 1.2908 1.4374 0.4135 -0.3762 -0.2791 456 PRO A CA 3404 C C . PRO A 456 ? 1.8024 1.4451 1.5826 0.4293 -0.3869 -0.2920 456 PRO A C 3405 O O . PRO A 456 ? 1.8976 1.5535 1.6807 0.4200 -0.3753 -0.2854 456 PRO A O 3406 C CB . PRO A 456 ? 1.5264 1.1373 1.3270 0.3861 -0.3829 -0.2638 456 PRO A CB 3407 C CG . PRO A 456 ? 1.5760 1.2144 1.3956 0.3643 -0.3585 -0.2466 456 PRO A CG 3408 C CD . PRO A 456 ? 1.5554 1.2414 1.3820 0.3724 -0.3376 -0.2485 456 PRO A CD 3409 N N . GLN A 457 ? 1.7768 1.3988 1.5409 0.4536 -0.4099 -0.3110 457 GLN A N 3410 C CA . GLN A 457 ? 1.7392 1.3528 1.4875 0.4716 -0.4239 -0.3266 457 GLN A CA 3411 C C . GLN A 457 ? 1.8363 1.4170 1.5847 0.4511 -0.4317 -0.3183 457 GLN A C 3412 O O . GLN A 457 ? 2.0237 1.6094 1.7636 0.4595 -0.4344 -0.3260 457 GLN A O 3413 C CB . GLN A 457 ? 1.7531 1.3396 1.4851 0.4993 -0.4525 -0.3490 457 GLN A CB 3414 C CG . GLN A 457 ? 1.7729 1.4003 1.4980 0.5309 -0.4474 -0.3653 457 GLN A CG 3415 C CD . GLN A 457 ? 1.8122 1.4140 1.5181 0.5623 -0.4775 -0.3914 457 GLN A CD 3416 O OE1 . GLN A 457 ? 1.8396 1.4633 1.5395 0.5885 -0.4800 -0.4059 457 GLN A OE1 3417 N NE2 . GLN A 457 ? 1.7641 1.3196 1.4615 0.5603 -0.5016 -0.3980 457 GLN A NE2 3418 N N . THR A 458 ? 1.6769 1.2267 1.4351 0.4249 -0.4353 -0.3024 458 THR A N 3419 C CA . THR A 458 ? 1.5901 1.1060 1.3501 0.4044 -0.4453 -0.2935 458 THR A CA 3420 C C . THR A 458 ? 1.5415 1.0846 1.3084 0.3901 -0.4240 -0.2827 458 THR A C 3421 O O . THR A 458 ? 1.4976 1.0187 1.2663 0.3743 -0.4303 -0.2761 458 THR A O 3422 C CB . THR A 458 ? 1.4909 0.9756 1.2614 0.3792 -0.4507 -0.2759 458 THR A CB 3423 O OG1 . THR A 458 ? 1.4446 0.9609 1.2283 0.3657 -0.4257 -0.2614 458 THR A OG1 3424 C CG2 . THR A 458 ? 1.4362 0.8839 1.1992 0.3916 -0.4770 -0.2852 458 THR A CG2 3425 N N . LEU A 459 ? 1.4945 1.0857 1.2661 0.3962 -0.3995 -0.2808 459 LEU A N 3426 C CA . LEU A 459 ? 1.4354 1.0552 1.2173 0.3802 -0.3763 -0.2668 459 LEU A CA 3427 C C . LEU A 459 ? 1.4947 1.1223 1.2664 0.3901 -0.3781 -0.2744 459 LEU A C 3428 O O . LEU A 459 ? 1.5514 1.2099 1.3142 0.4133 -0.3731 -0.2857 459 LEU A O 3429 C CB . LEU A 459 ? 1.3059 0.9733 1.0998 0.3820 -0.3506 -0.2603 459 LEU A CB 3430 C CG . LEU A 459 ? 1.2889 0.9719 1.1025 0.3546 -0.3287 -0.2396 459 LEU A CG 3431 C CD1 . LEU A 459 ? 1.2155 0.8607 1.0342 0.3316 -0.3383 -0.2291 459 LEU A CD1 3432 C CD2 . LEU A 459 ? 1.3298 1.0518 1.1572 0.3570 -0.3095 -0.2352 459 LEU A CD2 3433 N N . GLU A 460 ? 1.4944 1.0967 1.2676 0.3725 -0.3849 -0.2676 460 GLU A N 3434 C CA . GLU A 460 ? 1.4880 1.0979 1.2533 0.3782 -0.3855 -0.2725 460 GLU A CA 3435 C C . GLU A 460 ? 1.4104 1.0645 1.1850 0.3706 -0.3566 -0.2592 460 GLU A C 3436 O O . GLU A 460 ? 1.4482 1.1234 1.2144 0.3833 -0.3524 -0.2646 460 GLU A O 3437 C CB . GLU A 460 ? 1.4695 1.0383 1.2358 0.3604 -0.4027 -0.2686 460 GLU A CB 3438 C CG . GLU A 460 ? 1.6091 1.1300 1.3678 0.3665 -0.4344 -0.2806 460 GLU A CG 3439 C CD . GLU A 460 ? 1.6967 1.1813 1.4595 0.3476 -0.4505 -0.2751 460 GLU A CD 3440 O OE1 . GLU A 460 ? 1.6005 1.0995 1.3709 0.3311 -0.4360 -0.2628 460 GLU A OE1 3441 O OE2 . GLU A 460 ? 1.7951 1.2374 1.5550 0.3493 -0.4781 -0.2825 460 GLU A OE2 3442 N N . VAL A 461 ? 1.3366 1.0038 1.1288 0.3500 -0.3377 -0.2417 461 VAL A N 3443 C CA . VAL A 461 ? 1.2734 0.9802 1.0777 0.3417 -0.3114 -0.2282 461 VAL A CA 3444 C C . VAL A 461 ? 1.3015 1.0359 1.1208 0.3384 -0.2936 -0.2202 461 VAL A C 3445 O O . VAL A 461 ? 1.3962 1.1144 1.2241 0.3258 -0.2959 -0.2151 461 VAL A O 3446 C CB . VAL A 461 ? 1.1223 0.8179 0.9374 0.3150 -0.3051 -0.2127 461 VAL A CB 3447 C CG1 . VAL A 461 ? 1.0259 0.7616 0.8543 0.3081 -0.2790 -0.1992 461 VAL A CG1 3448 C CG2 . VAL A 461 ? 0.9538 0.6228 0.7565 0.3165 -0.3229 -0.2199 461 VAL A CG2 3449 N N . LEU A 462 ? 1.2100 0.9876 1.0332 0.3500 -0.2762 -0.2185 462 LEU A N 3450 C CA . LEU A 462 ? 1.1412 0.9485 0.9820 0.3463 -0.2589 -0.2103 462 LEU A CA 3451 C C . LEU A 462 ? 1.2173 1.0609 1.0733 0.3373 -0.2357 -0.1951 462 LEU A C 3452 O O . LEU A 462 ? 1.2212 1.0837 1.0692 0.3480 -0.2314 -0.1956 462 LEU A O 3453 C CB . LEU A 462 ? 1.1740 1.0011 1.0069 0.3724 -0.2625 -0.2238 462 LEU A CB 3454 C CG . LEU A 462 ? 1.2691 1.1254 1.1204 0.3708 -0.2482 -0.2179 462 LEU A CG 3455 C CD1 . LEU A 462 ? 1.2955 1.1258 1.1586 0.3503 -0.2514 -0.2118 462 LEU A CD1 3456 C CD2 . LEU A 462 ? 1.3482 1.2227 1.1892 0.3988 -0.2544 -0.2332 462 LEU A CD2 3457 N N . ASP A 463 ? 1.2411 1.0933 1.1193 0.3175 -0.2220 -0.1814 463 ASP A N 3458 C CA . ASP A 463 ? 1.0970 0.9828 0.9933 0.3085 -0.2007 -0.1663 463 ASP A CA 3459 C C . ASP A 463 ? 1.0623 0.9753 0.9785 0.3079 -0.1891 -0.1619 463 ASP A C 3460 O O . ASP A 463 ? 1.1356 1.0347 1.0631 0.2947 -0.1907 -0.1601 463 ASP A O 3461 C CB . ASP A 463 ? 0.9104 0.7795 0.8178 0.2836 -0.1963 -0.1539 463 ASP A CB 3462 C CG . ASP A 463 ? 0.9879 0.8889 0.9137 0.2754 -0.1763 -0.1384 463 ASP A CG 3463 O OD1 . ASP A 463 ? 0.8959 0.8326 0.8328 0.2838 -0.1640 -0.1342 463 ASP A OD1 3464 O OD2 . ASP A 463 ? 1.0928 0.9839 1.0229 0.2605 -0.1731 -0.1298 463 ASP A OD2 3465 N N . VAL A 464 ? 0.9760 0.9292 0.8961 0.3230 -0.1782 -0.1605 464 VAL A N 3466 C CA . VAL A 464 ? 1.0107 0.9941 0.9521 0.3230 -0.1670 -0.1558 464 VAL A CA 3467 C C . VAL A 464 ? 1.0784 1.1039 1.0395 0.3194 -0.1467 -0.1392 464 VAL A C 3468 O O . VAL A 464 ? 1.1328 1.1970 1.1062 0.3289 -0.1366 -0.1356 464 VAL A O 3469 C CB . VAL A 464 ? 0.9984 0.9935 0.9275 0.3475 -0.1751 -0.1708 464 VAL A CB 3470 C CG1 . VAL A 464 ? 0.9431 0.9400 0.8887 0.3419 -0.1749 -0.1720 464 VAL A CG1 3471 C CG2 . VAL A 464 ? 1.0385 0.9963 0.9379 0.3606 -0.1969 -0.1879 464 VAL A CG2 3472 N N . SER A 465 ? 1.1192 1.1374 1.0843 0.3052 -0.1411 -0.1282 465 SER A N 3473 C CA . SER A 465 ? 1.1595 1.2136 1.1425 0.3007 -0.1230 -0.1105 465 SER A CA 3474 C C . SER A 465 ? 1.2350 1.3032 1.2534 0.2814 -0.1107 -0.0966 465 SER A C 3475 O O . SER A 465 ? 1.3581 1.4079 1.3860 0.2712 -0.1161 -0.1016 465 SER A O 3476 C CB . SER A 465 ? 1.0245 1.0651 0.9973 0.2947 -0.1228 -0.1045 465 SER A CB 3477 O OG . SER A 465 ? 0.9918 0.9999 0.9727 0.2726 -0.1262 -0.1012 465 SER A OG 3478 N N . ASN A 466 ? 1.1583 1.2598 1.1965 0.2771 -0.0949 -0.0791 466 ASN A N 3479 C CA . ASN A 466 ? 1.1999 1.3160 1.2750 0.2589 -0.0839 -0.0650 466 ASN A CA 3480 C C . ASN A 466 ? 1.2653 1.3892 1.3556 0.2594 -0.0860 -0.0718 466 ASN A C 3481 O O . ASN A 466 ? 1.3201 1.4284 1.4290 0.2432 -0.0881 -0.0721 466 ASN A O 3482 C CB . ASN A 466 ? 1.2470 1.3314 1.3311 0.2370 -0.0861 -0.0606 466 ASN A CB 3483 C CG . ASN A 466 ? 1.2985 1.3990 1.4216 0.2191 -0.0751 -0.0449 466 ASN A CG 3484 O OD1 . ASN A 466 ? 1.3051 1.4421 1.4500 0.2215 -0.0644 -0.0336 466 ASN A OD1 3485 N ND2 . ASN A 466 ? 1.2786 1.3526 1.4117 0.2014 -0.0783 -0.0439 466 ASN A ND2 3486 N N . ASN A 467 ? 1.2397 1.3894 1.3217 0.2791 -0.0859 -0.0782 467 ASN A N 3487 C CA . ASN A 467 ? 1.2570 1.4179 1.3530 0.2817 -0.0878 -0.0850 467 ASN A CA 3488 C C . ASN A 467 ? 1.2080 1.4228 1.3241 0.2912 -0.0746 -0.0745 467 ASN A C 3489 O O . ASN A 467 ? 1.1955 1.4387 1.3291 0.2859 -0.0611 -0.0558 467 ASN A O 3490 C CB . ASN A 467 ? 1.2938 1.4289 1.3601 0.2972 -0.1043 -0.1066 467 ASN A CB 3491 C CG . ASN A 467 ? 1.3214 1.4059 1.3748 0.2847 -0.1175 -0.1149 467 ASN A CG 3492 O OD1 . ASN A 467 ? 1.3515 1.4077 1.3763 0.2948 -0.1314 -0.1285 467 ASN A OD1 3493 N ND2 . ASN A 467 ? 1.3309 1.4047 1.4065 0.2629 -0.1136 -0.1065 467 ASN A ND2 3494 N N . ASN A 468 ? 1.1635 1.3930 1.2777 0.3052 -0.0787 -0.0857 468 ASN A N 3495 C CA . ASN A 468 ? 1.1500 1.4338 1.2810 0.3170 -0.0671 -0.0774 468 ASN A CA 3496 C C . ASN A 468 ? 1.1748 1.4730 1.2765 0.3467 -0.0737 -0.0935 468 ASN A C 3497 O O . ASN A 468 ? 1.0344 1.3711 1.1473 0.3589 -0.0691 -0.0942 468 ASN A O 3498 C CB . ASN A 468 ? 1.0763 1.3761 1.2457 0.3034 -0.0629 -0.0720 468 ASN A CB 3499 C CG . ASN A 468 ? 1.0917 1.3926 1.2961 0.2777 -0.0536 -0.0527 468 ASN A CG 3500 O OD1 . ASN A 468 ? 1.0304 1.2945 1.2297 0.2636 -0.0579 -0.0524 468 ASN A OD1 3501 N ND2 . ASN A 468 ? 1.1392 1.4830 1.3806 0.2716 -0.0414 -0.0361 468 ASN A ND2 3502 N N . LEU A 469 ? 1.2255 1.4927 1.2906 0.3585 -0.0855 -0.1070 469 LEU A N 3503 C CA . LEU A 469 ? 1.2708 1.5454 1.3049 0.3880 -0.0948 -0.1246 469 LEU A CA 3504 C C . LEU A 469 ? 1.3787 1.7125 1.4139 0.4072 -0.0812 -0.1154 469 LEU A C 3505 O O . LEU A 469 ? 1.3197 1.6710 1.3568 0.4038 -0.0703 -0.0999 469 LEU A O 3506 C CB . LEU A 469 ? 1.1967 1.4256 1.1955 0.3937 -0.1101 -0.1381 469 LEU A CB 3507 C CG . LEU A 469 ? 1.1121 1.2892 1.0924 0.3942 -0.1307 -0.1578 469 LEU A CG 3508 C CD1 . LEU A 469 ? 1.0500 1.2137 1.0548 0.3745 -0.1306 -0.1549 469 LEU A CD1 3509 C CD2 . LEU A 469 ? 1.1007 1.2330 1.0592 0.3876 -0.1415 -0.1618 469 LEU A CD2 3510 N N . ASP A 470 ? 1.4489 1.8150 1.4823 0.4281 -0.0819 -0.1245 470 ASP A N 3511 C CA . ASP A 470 ? 1.5088 1.9353 1.5401 0.4502 -0.0700 -0.1177 470 ASP A CA 3512 C C . ASP A 470 ? 1.5209 1.9406 1.5097 0.4815 -0.0835 -0.1394 470 ASP A C 3513 O O . ASP A 470 ? 1.4340 1.8924 1.4104 0.5002 -0.0760 -0.1351 470 ASP A O 3514 C CB . ASP A 470 ? 1.5191 1.9938 1.5767 0.4558 -0.0613 -0.1134 470 ASP A CB 3515 C CG . ASP A 470 ? 1.5080 2.0309 1.6062 0.4385 -0.0394 -0.0833 470 ASP A CG 3516 O OD1 . ASP A 470 ? 1.4698 2.0511 1.5714 0.4545 -0.0265 -0.0719 470 ASP A OD1 3517 O OD2 . ASP A 470 ? 1.4916 1.9949 1.6188 0.4095 -0.0357 -0.0705 470 ASP A OD2 3518 N N . SER A 471 ? 1.5712 1.9411 1.5379 0.4872 -0.1043 -0.1627 471 SER A N 3519 C CA . SER A 471 ? 1.5502 1.9082 1.4785 0.5173 -0.1210 -0.1864 471 SER A CA 3520 C C . SER A 471 ? 1.4793 1.7662 1.3875 0.5110 -0.1438 -0.2043 471 SER A C 3521 O O . SER A 471 ? 1.5060 1.7645 1.4239 0.4991 -0.1513 -0.2091 471 SER A O 3522 C CB . SER A 471 ? 1.5003 1.8973 1.4250 0.5454 -0.1230 -0.1994 471 SER A CB 3523 O OG . SER A 471 ? 1.4434 1.8341 1.3905 0.5332 -0.1238 -0.1997 471 SER A OG 3524 N N . PHE A 472 ? 1.3448 1.6043 1.2261 0.5186 -0.1550 -0.2134 472 PHE A N 3525 C CA . PHE A 472 ? 1.3406 1.5363 1.2008 0.5175 -0.1791 -0.2320 472 PHE A CA 3526 C C . PHE A 472 ? 1.4049 1.5991 1.2349 0.5531 -0.1980 -0.2582 472 PHE A C 3527 O O . PHE A 472 ? 1.4966 1.7064 1.3060 0.5738 -0.2008 -0.2656 472 PHE A O 3528 C CB . PHE A 472 ? 1.3811 1.5404 1.2340 0.4998 -0.1823 -0.2258 472 PHE A CB 3529 C CG . PHE A 472 ? 1.4826 1.5766 1.3203 0.4925 -0.2055 -0.2399 472 PHE A CG 3530 C CD1 . PHE A 472 ? 1.4893 1.5485 1.3433 0.4633 -0.2058 -0.2307 472 PHE A CD1 3531 C CD2 . PHE A 472 ? 1.5478 1.6163 1.3559 0.5152 -0.2277 -0.2622 472 PHE A CD2 3532 C CE1 . PHE A 472 ? 1.5511 1.5534 1.3923 0.4559 -0.2264 -0.2410 472 PHE A CE1 3533 C CE2 . PHE A 472 ? 1.6421 1.6504 1.4390 0.5071 -0.2498 -0.2730 472 PHE A CE2 3534 C CZ . PHE A 472 ? 1.6765 1.6527 1.4902 0.4769 -0.2484 -0.2611 472 PHE A CZ 3535 N N . SER A 473 ? 1.3789 1.5549 1.2063 0.5613 -0.2116 -0.2730 473 SER A N 3536 C CA . SER A 473 ? 1.4917 1.6688 1.2936 0.5966 -0.2299 -0.2986 473 SER A CA 3537 C C . SER A 473 ? 1.5447 1.6567 1.3335 0.5950 -0.2566 -0.3159 473 SER A C 3538 O O . SER A 473 ? 1.5194 1.6273 1.3102 0.6040 -0.2649 -0.3258 473 SER A O 3539 C CB . SER A 473 ? 1.4639 1.6979 1.2773 0.6148 -0.2187 -0.2993 473 SER A CB 3540 O OG . SER A 473 ? 1.3114 1.5490 1.1544 0.5911 -0.2075 -0.2849 473 SER A OG 3541 N N . LEU A 474 ? 1.5621 1.6244 1.3381 0.5841 -0.2706 -0.3189 474 LEU A N 3542 C CA . LEU A 474 ? 1.4951 1.4937 1.2665 0.5716 -0.2919 -0.3262 474 LEU A CA 3543 C C . LEU A 474 ? 1.5768 1.5276 1.3232 0.5817 -0.3180 -0.3434 474 LEU A C 3544 O O . LEU A 474 ? 1.6105 1.5503 1.3526 0.5714 -0.3168 -0.3376 474 LEU A O 3545 C CB . LEU A 474 ? 1.2704 1.2499 1.0638 0.5332 -0.2797 -0.3039 474 LEU A CB 3546 C CG . LEU A 474 ? 0.9878 0.9271 0.7886 0.5177 -0.2906 -0.3037 474 LEU A CG 3547 C CD1 . LEU A 474 ? 0.8816 0.8488 0.6885 0.5342 -0.2888 -0.3109 474 LEU A CD1 3548 C CD2 . LEU A 474 ? 0.9110 0.8446 0.7342 0.4828 -0.2748 -0.2814 474 LEU A CD2 3549 N N . PHE A 475 ? 1.5986 1.5192 1.3300 0.6009 -0.3428 -0.3643 475 PHE A N 3550 C CA . PHE A 475 ? 1.6324 1.5019 1.3429 0.6098 -0.3714 -0.3815 475 PHE A CA 3551 C C . PHE A 475 ? 1.6405 1.4554 1.3591 0.5760 -0.3787 -0.3686 475 PHE A C 3552 O O . PHE A 475 ? 1.6371 1.4259 1.3659 0.5601 -0.3826 -0.3620 475 PHE A O 3553 C CB . PHE A 475 ? 1.6609 1.5107 1.3562 0.6385 -0.3970 -0.4064 475 PHE A CB 3554 C CG . PHE A 475 ? 1.7365 1.5413 1.4099 0.6550 -0.4282 -0.4281 475 PHE A CG 3555 C CD1 . PHE A 475 ? 1.8084 1.5667 1.4724 0.6674 -0.4579 -0.4457 475 PHE A CD1 3556 C CD2 . PHE A 475 ? 1.6531 1.4613 1.3162 0.6581 -0.4292 -0.4309 475 PHE A CD2 3557 C CE1 . PHE A 475 ? 1.8036 1.5183 1.4500 0.6821 -0.4888 -0.4661 475 PHE A CE1 3558 C CE2 . PHE A 475 ? 1.6707 1.4370 1.3153 0.6733 -0.4596 -0.4521 475 PHE A CE2 3559 C CZ . PHE A 475 ? 1.7364 1.4552 1.3736 0.6849 -0.4899 -0.4698 475 PHE A CZ 3560 N N . LEU A 476 ? 1.5702 1.3711 1.2843 0.5657 -0.3801 -0.3645 476 LEU A N 3561 C CA . LEU A 476 ? 1.5718 1.3233 1.2925 0.5354 -0.3882 -0.3530 476 LEU A CA 3562 C C . LEU A 476 ? 1.6791 1.4008 1.3831 0.5435 -0.4091 -0.3660 476 LEU A C 3563 O O . LEU A 476 ? 1.7511 1.4845 1.4559 0.5341 -0.3988 -0.3577 476 LEU A O 3564 C CB . LEU A 476 ? 1.4559 1.2279 1.1969 0.5045 -0.3608 -0.3268 476 LEU A CB 3565 C CG . LEU A 476 ? 1.3046 1.1075 1.0661 0.4928 -0.3388 -0.3122 476 LEU A CG 3566 C CD1 . LEU A 476 ? 1.2306 1.0629 1.0106 0.4698 -0.3119 -0.2900 476 LEU A CD1 3567 C CD2 . LEU A 476 ? 1.1070 0.8715 0.8754 0.4779 -0.3500 -0.3091 476 LEU A CD2 3568 N N . PRO A 477 ? 1.6243 1.3066 1.3139 0.5614 -0.4398 -0.3870 477 PRO A N 3569 C CA . PRO A 477 ? 1.5104 1.1630 1.1841 0.5737 -0.4645 -0.4041 477 PRO A CA 3570 C C . PRO A 477 ? 1.5958 1.2288 1.2765 0.5458 -0.4613 -0.3892 477 PRO A C 3571 O O . PRO A 477 ? 1.6996 1.3580 1.3743 0.5516 -0.4527 -0.3902 477 PRO A O 3572 C CB . PRO A 477 ? 1.4125 1.0103 1.0807 0.5808 -0.4974 -0.4188 477 PRO A CB 3573 C CG . PRO A 477 ? 1.4745 1.0930 1.1456 0.5926 -0.4904 -0.4207 477 PRO A CG 3574 C CD . PRO A 477 ? 1.5346 1.1969 1.2236 0.5711 -0.4543 -0.3959 477 PRO A CD 3575 N N . ARG A 478 ? 1.6131 1.2042 1.3066 0.5165 -0.4680 -0.3751 478 ARG A N 3576 C CA . ARG A 478 ? 1.7006 1.2687 1.4013 0.4903 -0.4689 -0.3622 478 ARG A CA 3577 C C . ARG A 478 ? 1.6221 1.2331 1.3307 0.4770 -0.4383 -0.3452 478 ARG A C 3578 O O . ARG A 478 ? 1.5827 1.1837 1.2930 0.4631 -0.4389 -0.3391 478 ARG A O 3579 C CB . ARG A 478 ? 1.7626 1.2878 1.4777 0.4606 -0.4766 -0.3463 478 ARG A CB 3580 C CG . ARG A 478 ? 1.7836 1.2716 1.4942 0.4720 -0.5022 -0.3581 478 ARG A CG 3581 C CD . ARG A 478 ? 1.8221 1.2600 1.5442 0.4445 -0.5174 -0.3438 478 ARG A CD 3582 N NE . ARG A 478 ? 1.9360 1.3408 1.6554 0.4541 -0.5396 -0.3517 478 ARG A NE 3583 C CZ . ARG A 478 ? 2.0785 1.4365 1.7913 0.4646 -0.5736 -0.3663 478 ARG A CZ 3584 N NH1 . ARG A 478 ? 2.0954 1.4341 1.8039 0.4667 -0.5903 -0.3759 478 ARG A NH1 3585 N NH2 . ARG A 478 ? 2.1192 1.4488 1.8305 0.4730 -0.5922 -0.3716 478 ARG A NH2 3586 N N . LEU A 479 ? 1.5488 1.2072 1.2629 0.4818 -0.4128 -0.3377 479 LEU A N 3587 C CA . LEU A 479 ? 1.5188 1.2172 1.2451 0.4662 -0.3826 -0.3180 479 LEU A CA 3588 C C . LEU A 479 ? 1.5408 1.2527 1.2589 0.4702 -0.3796 -0.3191 479 LEU A C 3589 O O . LEU A 479 ? 1.5739 1.3161 1.2777 0.4971 -0.3789 -0.3319 479 LEU A O 3590 C CB . LEU A 479 ? 1.4926 1.2429 1.2249 0.4776 -0.3597 -0.3137 479 LEU A CB 3591 C CG . LEU A 479 ? 1.4907 1.2797 1.2405 0.4588 -0.3289 -0.2910 479 LEU A CG 3592 C CD1 . LEU A 479 ? 1.5475 1.3135 1.3167 0.4251 -0.3222 -0.2725 479 LEU A CD1 3593 C CD2 . LEU A 479 ? 1.5383 1.3803 1.2943 0.4733 -0.3091 -0.2882 479 LEU A CD2 3594 N N . GLN A 480 ? 1.5283 1.2209 1.2558 0.4438 -0.3770 -0.3051 480 GLN A N 3595 C CA . GLN A 480 ? 1.5272 1.2326 1.2494 0.4438 -0.3725 -0.3033 480 GLN A CA 3596 C C . GLN A 480 ? 1.5025 1.2575 1.2355 0.4368 -0.3404 -0.2847 480 GLN A C 3597 O O . GLN A 480 ? 1.3970 1.1914 1.1206 0.4575 -0.3309 -0.2888 480 GLN A O 3598 C CB . GLN A 480 ? 1.4427 1.1057 1.1711 0.4189 -0.3851 -0.2968 480 GLN A CB 3599 C CG . GLN A 480 ? 1.4219 1.0342 1.1422 0.4243 -0.4187 -0.3134 480 GLN A CG 3600 C CD . GLN A 480 ? 1.3896 0.9619 1.1210 0.3956 -0.4296 -0.3026 480 GLN A CD 3601 O OE1 . GLN A 480 ? 1.3976 0.9810 1.1391 0.3754 -0.4139 -0.2863 480 GLN A OE1 3602 N NE2 . GLN A 480 ? 1.3107 0.8368 1.0412 0.3939 -0.4569 -0.3109 480 GLN A NE2 3603 N N . GLU A 481 ? 1.5666 1.3204 1.3199 0.4082 -0.3244 -0.2640 481 GLU A N 3604 C CA . GLU A 481 ? 1.5861 1.3821 1.3534 0.3989 -0.2957 -0.2453 481 GLU A CA 3605 C C . GLU A 481 ? 1.3996 1.2257 1.1787 0.4022 -0.2799 -0.2396 481 GLU A C 3606 O O . GLU A 481 ? 1.2817 1.0889 1.0639 0.4005 -0.2883 -0.2443 481 GLU A O 3607 C CB . GLU A 481 ? 1.7263 1.5068 1.5100 0.3670 -0.2873 -0.2269 481 GLU A CB 3608 C CG . GLU A 481 ? 1.8736 1.6224 1.6486 0.3609 -0.3040 -0.2318 481 GLU A CG 3609 C CD . GLU A 481 ? 1.9247 1.6723 1.7144 0.3344 -0.2915 -0.2133 481 GLU A CD 3610 O OE1 . GLU A 481 ? 1.9375 1.7090 1.7441 0.3217 -0.2698 -0.1973 481 GLU A OE1 3611 O OE2 . GLU A 481 ? 1.9146 1.6375 1.7002 0.3266 -0.3042 -0.2154 481 GLU A OE2 3612 N N . LEU A 482 ? 1.3563 1.2300 1.1428 0.4072 -0.2577 -0.2289 482 LEU A N 3613 C CA . LEU A 482 ? 1.3450 1.2509 1.1473 0.4076 -0.2411 -0.2209 482 LEU A CA 3614 C C . LEU A 482 ? 1.4679 1.4116 1.2901 0.3943 -0.2151 -0.1990 482 LEU A C 3615 O O . LEU A 482 ? 1.4526 1.4403 1.2743 0.4097 -0.2021 -0.1949 482 LEU A O 3616 C CB . LEU A 482 ? 1.3028 1.2366 1.0917 0.4394 -0.2448 -0.2360 482 LEU A CB 3617 C CG . LEU A 482 ? 1.2344 1.2031 1.0424 0.4383 -0.2277 -0.2268 482 LEU A CG 3618 C CD1 . LEU A 482 ? 1.2685 1.2064 1.0796 0.4341 -0.2406 -0.2352 482 LEU A CD1 3619 C CD2 . LEU A 482 ? 1.1457 1.1658 0.9465 0.4668 -0.2193 -0.2316 482 LEU A CD2 3620 N N . TYR A 483 ? 1.6328 1.5602 1.4734 0.3663 -0.2080 -0.1845 483 TYR A N 3621 C CA . TYR A 483 ? 1.6869 1.6450 1.5501 0.3515 -0.1851 -0.1636 483 TYR A CA 3622 C C . TYR A 483 ? 1.6104 1.6009 1.4917 0.3541 -0.1722 -0.1580 483 TYR A C 3623 O O . TYR A 483 ? 1.7339 1.7088 1.6247 0.3456 -0.1762 -0.1607 483 TYR A O 3624 C CB . TYR A 483 ? 1.8141 1.7444 1.6915 0.3226 -0.1833 -0.1523 483 TYR A CB 3625 C CG . TYR A 483 ? 2.0659 1.9773 1.9310 0.3184 -0.1901 -0.1524 483 TYR A CG 3626 C CD1 . TYR A 483 ? 2.1563 2.0302 2.0022 0.3224 -0.2117 -0.1671 483 TYR A CD1 3627 C CD2 . TYR A 483 ? 2.1450 2.0762 2.0189 0.3106 -0.1757 -0.1375 483 TYR A CD2 3628 C CE1 . TYR A 483 ? 2.1645 2.0226 2.0008 0.3184 -0.2185 -0.1675 483 TYR A CE1 3629 C CE2 . TYR A 483 ? 2.1262 2.0419 1.9889 0.3076 -0.1820 -0.1379 483 TYR A CE2 3630 C CZ . TYR A 483 ? 2.0802 1.9602 1.9244 0.3114 -0.2033 -0.1532 483 TYR A CZ 3631 O OH . TYR A 483 ? 1.9175 1.7836 1.7526 0.3080 -0.2100 -0.1537 483 TYR A OH 3632 N N . ILE A 484 ? 1.4673 1.5047 1.3535 0.3666 -0.1572 -0.1500 484 ILE A N 3633 C CA . ILE A 484 ? 1.4236 1.4974 1.3288 0.3702 -0.1447 -0.1438 484 ILE A CA 3634 C C . ILE A 484 ? 1.3903 1.5115 1.3153 0.3669 -0.1224 -0.1223 484 ILE A C 3635 O O . ILE A 484 ? 1.4029 1.5677 1.3352 0.3805 -0.1122 -0.1179 484 ILE A O 3636 C CB . ILE A 484 ? 1.3866 1.4730 1.2740 0.3986 -0.1546 -0.1623 484 ILE A CB 3637 C CG1 . ILE A 484 ? 1.3429 1.4665 1.2521 0.4009 -0.1423 -0.1561 484 ILE A CG1 3638 C CG2 . ILE A 484 ? 1.3947 1.5045 1.2581 0.4249 -0.1567 -0.1696 484 ILE A CG2 3639 C CD1 . ILE A 484 ? 1.2757 1.4324 1.1700 0.4322 -0.1451 -0.1690 484 ILE A CD1 3640 N N . SER A 485 ? 1.2933 1.4064 1.2281 0.3484 -0.1153 -0.1078 485 SER A N 3641 C CA . SER A 485 ? 1.2162 1.3689 1.1714 0.3426 -0.0954 -0.0850 485 SER A CA 3642 C C . SER A 485 ? 1.1067 1.2813 1.0980 0.3276 -0.0820 -0.0704 485 SER A C 3643 O O . SER A 485 ? 1.0520 1.2201 1.0505 0.3266 -0.0869 -0.0791 485 SER A O 3644 C CB . SER A 485 ? 1.2992 1.4329 1.2554 0.3268 -0.0934 -0.0747 485 SER A CB 3645 O OG . SER A 485 ? 1.3308 1.4582 1.2570 0.3429 -0.1022 -0.0842 485 SER A OG 3646 N N . ARG A 486 ? 1.1517 1.3521 1.1662 0.3161 -0.0661 -0.0478 486 ARG A N 3647 C CA . ARG A 486 ? 1.1951 1.4183 1.2480 0.3008 -0.0536 -0.0316 486 ARG A CA 3648 C C . ARG A 486 ? 1.2532 1.4909 1.3144 0.3084 -0.0555 -0.0409 486 ARG A C 3649 O O . ARG A 486 ? 1.2448 1.4647 1.3247 0.2936 -0.0589 -0.0440 486 ARG A O 3650 C CB . ARG A 486 ? 1.1802 1.3704 1.2540 0.2735 -0.0545 -0.0252 486 ARG A CB 3651 C CG . ARG A 486 ? 1.2213 1.3974 1.2891 0.2653 -0.0527 -0.0158 486 ARG A CG 3652 C CD . ARG A 486 ? 1.3583 1.4980 1.4419 0.2413 -0.0569 -0.0149 486 ARG A CD 3653 N NE . ARG A 486 ? 1.5694 1.7212 1.6911 0.2258 -0.0495 -0.0041 486 ARG A NE 3654 C CZ . ARG A 486 ? 1.7250 1.8502 1.8641 0.2071 -0.0539 -0.0064 486 ARG A CZ 3655 N NH1 . ARG A 486 ? 1.7736 1.8605 1.8953 0.2012 -0.0644 -0.0174 486 ARG A NH1 3656 N NH2 . ARG A 486 ? 1.7647 1.9030 1.9394 0.1948 -0.0483 0.0022 486 ARG A NH2 3657 N N . ASN A 487 ? 1.3512 1.6233 1.3982 0.3327 -0.0535 -0.0458 487 ASN A N 3658 C CA . ASN A 487 ? 1.4441 1.7374 1.4992 0.3427 -0.0542 -0.0537 487 ASN A CA 3659 C C . ASN A 487 ? 1.4636 1.8209 1.5354 0.3540 -0.0376 -0.0372 487 ASN A C 3660 O O . ASN A 487 ? 1.3997 1.7845 1.4791 0.3521 -0.0248 -0.0173 487 ASN A O 3661 C CB . ASN A 487 ? 1.4812 1.7521 1.5011 0.3644 -0.0718 -0.0807 487 ASN A CB 3662 C CG . ASN A 487 ? 1.4076 1.6216 1.4208 0.3513 -0.0879 -0.0956 487 ASN A CG 3663 O OD1 . ASN A 487 ? 1.4072 1.5838 1.3940 0.3546 -0.1013 -0.1080 487 ASN A OD1 3664 N ND2 . ASN A 487 ? 1.2689 1.4778 1.3066 0.3367 -0.0870 -0.0940 487 ASN A ND2 3665 N N . LYS A 488 ? 1.4838 1.8661 1.5619 0.3659 -0.0377 -0.0444 488 LYS A N 3666 C CA . LYS A 488 ? 1.4878 1.9349 1.5815 0.3786 -0.0225 -0.0298 488 LYS A CA 3667 C C . LYS A 488 ? 1.5911 2.0619 1.6503 0.4131 -0.0278 -0.0468 488 LYS A C 3668 O O . LYS A 488 ? 1.6417 2.1595 1.7090 0.4284 -0.0212 -0.0454 488 LYS A O 3669 C CB . LYS A 488 ? 1.4623 1.9290 1.5926 0.3675 -0.0176 -0.0244 488 LYS A CB 3670 C CG . LYS A 488 ? 1.4888 1.9649 1.6639 0.3388 -0.0053 0.0013 488 LYS A CG 3671 C CD . LYS A 488 ? 1.5086 2.0051 1.7190 0.3306 -0.0029 0.0034 488 LYS A CD 3672 C CE . LYS A 488 ? 1.4082 1.9258 1.6676 0.3052 0.0098 0.0309 488 LYS A CE 3673 N NZ . LYS A 488 ? 1.2766 1.8207 1.5716 0.2995 0.0120 0.0329 488 LYS A NZ 3674 N N . LEU A 489 ? 1.6229 2.0620 1.6447 0.4259 -0.0405 -0.0632 489 LEU A N 3675 C CA . LEU A 489 ? 1.6596 2.1110 1.6457 0.4599 -0.0504 -0.0846 489 LEU A CA 3676 C C . LEU A 489 ? 1.7509 2.2655 1.7302 0.4816 -0.0362 -0.0719 489 LEU A C 3677 O O . LEU A 489 ? 1.8044 2.3197 1.7693 0.4841 -0.0335 -0.0650 489 LEU A O 3678 C CB . LEU A 489 ? 1.5824 1.9756 1.5336 0.4646 -0.0708 -0.1066 489 LEU A CB 3679 C CG . LEU A 489 ? 1.5250 1.8931 1.4460 0.4882 -0.0921 -0.1375 489 LEU A CG 3680 C CD1 . LEU A 489 ? 1.4180 1.7518 1.3521 0.4744 -0.1014 -0.1466 489 LEU A CD1 3681 C CD2 . LEU A 489 ? 1.5424 1.8668 1.4302 0.4956 -0.1095 -0.1539 489 LEU A CD2 3682 N N . LYS A 490 ? 1.7177 2.2874 1.7074 0.4979 -0.0272 -0.0686 490 LYS A N 3683 C CA . LYS A 490 ? 1.5514 2.1879 1.5328 0.5226 -0.0139 -0.0578 490 LYS A CA 3684 C C . LYS A 490 ? 1.5900 2.2176 1.5243 0.5549 -0.0288 -0.0833 490 LYS A C 3685 O O . LYS A 490 ? 1.4626 2.1121 1.3804 0.5665 -0.0234 -0.0759 490 LYS A O 3686 C CB . LYS A 490 ? 1.2597 1.9546 1.2595 0.5359 -0.0044 -0.0540 490 LYS A CB 3687 C CG . LYS A 490 ? 1.0300 1.7678 1.0781 0.5126 0.0170 -0.0203 490 LYS A CG 3688 C CD . LYS A 490 ? 0.9673 1.7573 1.0309 0.5275 0.0226 -0.0219 490 LYS A CD 3689 C CE . LYS A 490 ? 0.9660 1.7935 1.0826 0.5020 0.0406 0.0091 490 LYS A CE 3690 N NZ . LYS A 490 ? 0.9061 1.7747 1.0395 0.5136 0.0426 0.0035 490 LYS A NZ 3691 N N . THR A 491 ? 1.6636 2.2584 1.5771 0.5697 -0.0487 -0.1136 491 THR A N 3692 C CA . THR A 491 ? 1.6118 2.1962 1.4826 0.6028 -0.0667 -0.1421 491 THR A CA 3693 C C . THR A 491 ? 1.5504 2.0572 1.4005 0.5928 -0.0885 -0.1608 491 THR A C 3694 O O . THR A 491 ? 1.5981 2.0565 1.4635 0.5661 -0.0943 -0.1604 491 THR A O 3695 C CB . THR A 491 ? 1.6164 2.2164 1.4779 0.6290 -0.0767 -0.1647 491 THR A CB 3696 O OG1 . THR A 491 ? 1.6609 2.2243 1.4832 0.6544 -0.1016 -0.1975 491 THR A OG1 3697 C CG2 . THR A 491 ? 1.5350 2.1062 1.4234 0.6059 -0.0793 -0.1647 491 THR A CG2 3698 N N . LEU A 492 ? 1.3790 1.8759 1.1949 0.6146 -0.1011 -0.1772 492 LEU A N 3699 C CA . LEU A 492 ? 1.3638 1.7895 1.1596 0.6076 -0.1238 -0.1962 492 LEU A CA 3700 C C . LEU A 492 ? 1.5197 1.9091 1.2960 0.6256 -0.1490 -0.2283 492 LEU A C 3701 O O . LEU A 492 ? 1.5389 1.9629 1.3035 0.6559 -0.1523 -0.2425 492 LEU A O 3702 C CB . LEU A 492 ? 1.2794 1.7073 1.0500 0.6204 -0.1274 -0.1989 492 LEU A CB 3703 C CG . LEU A 492 ? 1.2434 1.6025 0.9957 0.6114 -0.1495 -0.2151 492 LEU A CG 3704 C CD1 . LEU A 492 ? 1.1387 1.5000 0.8883 0.6010 -0.1413 -0.1996 492 LEU A CD1 3705 C CD2 . LEU A 492 ? 1.3175 1.6549 1.0360 0.6433 -0.1764 -0.2500 492 LEU A CD2 3706 N N . PRO A 493 ? 1.6063 1.9267 1.3803 0.6069 -0.1668 -0.2386 493 PRO A N 3707 C CA . PRO A 493 ? 1.6666 1.9427 1.4242 0.6194 -0.1927 -0.2666 493 PRO A CA 3708 C C . PRO A 493 ? 1.6938 1.9624 1.4154 0.6550 -0.2150 -0.2954 493 PRO A C 3709 O O . PRO A 493 ? 1.4936 1.7621 1.1990 0.6618 -0.2179 -0.2973 493 PRO A O 3710 C CB . PRO A 493 ? 1.6048 1.8135 1.3706 0.5863 -0.2028 -0.2633 493 PRO A CB 3711 C CG . PRO A 493 ? 1.5153 1.7313 1.2915 0.5648 -0.1867 -0.2405 493 PRO A CG 3712 C CD . PRO A 493 ? 1.5146 1.7988 1.3089 0.5685 -0.1606 -0.2199 493 PRO A CD 3713 N N . ASP A 494 ? 1.8427 2.1038 1.5524 0.6780 -0.2319 -0.3187 494 ASP A N 3714 C CA . ASP A 494 ? 1.9651 2.2149 1.6419 0.7138 -0.2568 -0.3498 494 ASP A CA 3715 C C . ASP A 494 ? 1.9283 2.1103 1.5907 0.7038 -0.2806 -0.3622 494 ASP A C 3716 O O . ASP A 494 ? 1.8955 2.0235 1.5694 0.6761 -0.2890 -0.3580 494 ASP A O 3717 C CB . ASP A 494 ? 2.1210 2.3671 1.7919 0.7360 -0.2719 -0.3715 494 ASP A CB 3718 C CG . ASP A 494 ? 2.3045 2.5244 1.9431 0.7705 -0.3031 -0.4064 494 ASP A CG 3719 O OD1 . ASP A 494 ? 2.3822 2.6235 2.0005 0.7922 -0.3063 -0.4153 494 ASP A OD1 3720 O OD2 . ASP A 494 ? 2.3692 2.5469 2.0029 0.7764 -0.3255 -0.4251 494 ASP A OD2 3721 N N . ALA A 495 ? 1.9717 2.1588 1.6092 0.7274 -0.2922 -0.3775 495 ALA A N 3722 C CA . ALA A 495 ? 2.0695 2.1977 1.6947 0.7188 -0.3146 -0.3887 495 ALA A CA 3723 C C . ALA A 495 ? 2.1448 2.2129 1.7574 0.7290 -0.3490 -0.4167 495 ALA A C 3724 O O . ALA A 495 ? 2.2257 2.2437 1.8282 0.7247 -0.3715 -0.4286 495 ALA A O 3725 C CB . ALA A 495 ? 2.1228 2.2783 1.7266 0.7406 -0.3156 -0.3956 495 ALA A CB 3726 N N . SER A 496 ? 2.1165 2.1892 1.7310 0.7422 -0.3540 -0.4267 496 SER A N 3727 C CA . SER A 496 ? 2.1291 2.1431 1.7342 0.7505 -0.3867 -0.4510 496 SER A CA 3728 C C . SER A 496 ? 2.1213 2.0875 1.7485 0.7123 -0.3863 -0.4346 496 SER A C 3729 O O . SER A 496 ? 2.1844 2.0892 1.8082 0.7056 -0.4124 -0.4460 496 SER A O 3730 C CB . SER A 496 ? 2.1021 2.1430 1.6959 0.7873 -0.3954 -0.4726 496 SER A CB 3731 O OG . SER A 496 ? 2.0862 2.1188 1.6981 0.7733 -0.3901 -0.4641 496 SER A OG 3732 N N . LEU A 497 ? 1.9915 1.9875 1.6420 0.6875 -0.3570 -0.4072 497 LEU A N 3733 C CA . LEU A 497 ? 1.8578 1.8192 1.5302 0.6534 -0.3532 -0.3909 497 LEU A CA 3734 C C . LEU A 497 ? 1.9084 1.8093 1.5826 0.6261 -0.3669 -0.3860 497 LEU A C 3735 O O . LEU A 497 ? 1.9721 1.8349 1.6597 0.6010 -0.3707 -0.3768 497 LEU A O 3736 C CB . LEU A 497 ? 1.6315 1.6389 1.3292 0.6322 -0.3192 -0.3627 497 LEU A CB 3737 C CG . LEU A 497 ? 1.4216 1.4916 1.1254 0.6523 -0.3022 -0.3615 497 LEU A CG 3738 C CD1 . LEU A 497 ? 1.3355 1.4490 1.0667 0.6286 -0.2696 -0.3315 497 LEU A CD1 3739 C CD2 . LEU A 497 ? 1.2498 1.3025 0.9550 0.6611 -0.3157 -0.3746 497 LEU A CD2 3740 N N . PHE A 498 ? 1.8707 1.7654 1.5314 0.6317 -0.3743 -0.3920 498 PHE A N 3741 C CA . PHE A 498 ? 1.8979 1.7420 1.5618 0.6055 -0.3853 -0.3858 498 PHE A CA 3742 C C . PHE A 498 ? 1.8251 1.6562 1.4680 0.6241 -0.4050 -0.4043 498 PHE A C 3743 O O . PHE A 498 ? 1.7784 1.6302 1.4199 0.6192 -0.3928 -0.3953 498 PHE A O 3744 C CB . PHE A 498 ? 2.0188 1.8797 1.7036 0.5722 -0.3574 -0.3560 498 PHE A CB 3745 C CG . PHE A 498 ? 2.0721 1.9991 1.7659 0.5779 -0.3272 -0.3417 498 PHE A CG 3746 C CD1 . PHE A 498 ? 2.0842 2.0543 1.7664 0.5970 -0.3176 -0.3428 498 PHE A CD1 3747 C CD2 . PHE A 498 ? 2.0115 1.9583 1.7264 0.5641 -0.3089 -0.3263 498 PHE A CD2 3748 C CE1 . PHE A 498 ? 2.0560 2.0883 1.7486 0.6010 -0.2898 -0.3268 498 PHE A CE1 3749 C CE2 . PHE A 498 ? 1.9908 1.9981 1.7174 0.5678 -0.2821 -0.3118 498 PHE A CE2 3750 C CZ . PHE A 498 ? 2.0168 2.0671 1.7328 0.5857 -0.2722 -0.3109 498 PHE A CZ 3751 N N . PRO A 499 ? 1.8570 1.6526 1.4840 0.6460 -0.4367 -0.4310 499 PRO A N 3752 C CA . PRO A 499 ? 1.9238 1.7045 1.5296 0.6696 -0.4613 -0.4550 499 PRO A CA 3753 C C . PRO A 499 ? 2.0205 1.7645 1.6297 0.6461 -0.4700 -0.4483 499 PRO A C 3754 O O . PRO A 499 ? 2.0712 1.8193 1.6646 0.6642 -0.4818 -0.4635 499 PRO A O 3755 C CB . PRO A 499 ? 1.8857 1.6248 1.4816 0.6899 -0.4947 -0.4811 499 PRO A CB 3756 C CG . PRO A 499 ? 1.8524 1.6128 1.4573 0.6917 -0.4811 -0.4745 499 PRO A CG 3757 C CD . PRO A 499 ? 1.8416 1.6140 1.4700 0.6534 -0.4511 -0.4412 499 PRO A CD 3758 N N . VAL A 500 ? 1.9728 1.6841 1.6019 0.6080 -0.4646 -0.4269 500 VAL A N 3759 C CA . VAL A 500 ? 1.8150 1.4938 1.4495 0.5842 -0.4720 -0.4191 500 VAL A CA 3760 C C . VAL A 500 ? 1.5898 1.2981 1.2390 0.5573 -0.4401 -0.3907 500 VAL A C 3761 O O . VAL A 500 ? 1.4299 1.1136 1.0874 0.5329 -0.4421 -0.3799 500 VAL A O 3762 C CB . VAL A 500 ? 1.7417 1.3551 1.3869 0.5618 -0.4958 -0.4179 500 VAL A CB 3763 C CG1 . VAL A 500 ? 1.7151 1.2875 1.3457 0.5832 -0.5345 -0.4464 500 VAL A CG1 3764 C CG2 . VAL A 500 ? 1.7202 1.3272 1.3762 0.5536 -0.4902 -0.4096 500 VAL A CG2 3765 N N . LEU A 501 ? 1.5371 1.2986 1.1903 0.5627 -0.4118 -0.3790 501 LEU A N 3766 C CA . LEU A 501 ? 1.5395 1.3355 1.2072 0.5414 -0.3807 -0.3527 501 LEU A CA 3767 C C . LEU A 501 ? 1.6039 1.3905 1.2692 0.5302 -0.3824 -0.3479 501 LEU A C 3768 O O . LEU A 501 ? 1.6088 1.3878 1.2563 0.5503 -0.4012 -0.3669 501 LEU A O 3769 C CB . LEU A 501 ? 1.5087 1.3697 1.1727 0.5631 -0.3576 -0.3494 501 LEU A CB 3770 C CG . LEU A 501 ? 1.5856 1.4888 1.2706 0.5446 -0.3234 -0.3216 501 LEU A CG 3771 C CD1 . LEU A 501 ? 1.6728 1.5956 1.3612 0.5327 -0.3075 -0.3052 501 LEU A CD1 3772 C CD2 . LEU A 501 ? 1.4916 1.3696 1.1993 0.5144 -0.3174 -0.3067 501 LEU A CD2 3773 N N . LEU A 502 ? 1.6966 1.4829 1.3803 0.4986 -0.3642 -0.3236 502 LEU A N 3774 C CA . LEU A 502 ? 1.6835 1.4663 1.3671 0.4867 -0.3623 -0.3164 502 LEU A CA 3775 C C . LEU A 502 ? 1.6333 1.4627 1.3276 0.4772 -0.3304 -0.2933 502 LEU A C 3776 O O . LEU A 502 ? 1.5248 1.3726 1.2126 0.4811 -0.3248 -0.2901 502 LEU A O 3777 C CB . LEU A 502 ? 1.5759 1.3093 1.2732 0.4551 -0.3733 -0.3081 502 LEU A CB 3778 C CG . LEU A 502 ? 1.5490 1.2291 1.2395 0.4575 -0.4072 -0.3265 502 LEU A CG 3779 C CD1 . LEU A 502 ? 1.4449 1.0896 1.1498 0.4254 -0.4128 -0.3135 502 LEU A CD1 3780 C CD2 . LEU A 502 ? 1.5200 1.2017 1.1879 0.4895 -0.4280 -0.3524 502 LEU A CD2 3781 N N . VAL A 503 ? 1.6104 1.4573 1.3222 0.4640 -0.3103 -0.2770 503 VAL A N 3782 C CA . VAL A 503 ? 1.4841 1.3698 1.2114 0.4508 -0.2812 -0.2531 503 VAL A CA 3783 C C . VAL A 503 ? 1.3935 1.3163 1.1313 0.4569 -0.2632 -0.2455 503 VAL A C 3784 O O . VAL A 503 ? 1.3926 1.3022 1.1313 0.4613 -0.2717 -0.2546 503 VAL A O 3785 C CB . VAL A 503 ? 1.4532 1.3129 1.2006 0.4150 -0.2747 -0.2349 503 VAL A CB 3786 C CG1 . VAL A 503 ? 1.4281 1.3254 1.1935 0.4015 -0.2461 -0.2108 503 VAL A CG1 3787 C CG2 . VAL A 503 ? 1.4345 1.2608 1.1734 0.4082 -0.2920 -0.2412 503 VAL A CG2 3788 N N . MET A 504 ? 1.3805 1.3504 1.1271 0.4574 -0.2390 -0.2282 504 MET A N 3789 C CA . MET A 504 ? 1.4572 1.4648 1.2197 0.4584 -0.2199 -0.2169 504 MET A CA 3790 C C . MET A 504 ? 1.4299 1.4723 1.2133 0.4421 -0.1934 -0.1899 504 MET A C 3791 O O . MET A 504 ? 1.2285 1.3145 1.0073 0.4568 -0.1808 -0.1825 504 MET A O 3792 C CB . MET A 504 ? 1.4295 1.4733 1.1753 0.4933 -0.2222 -0.2314 504 MET A CB 3793 C CG . MET A 504 ? 1.3869 1.4720 1.1507 0.4948 -0.2032 -0.2198 504 MET A CG 3794 S SD . MET A 504 ? 1.8364 1.9703 1.5808 0.5372 -0.2049 -0.2363 504 MET A SD 3795 C CE . MET A 504 ? 1.4813 1.5608 1.2008 0.5544 -0.2404 -0.2705 504 MET A CE 3796 N N . LYS A 505 ? 1.5548 1.5779 1.3613 0.4122 -0.1857 -0.1751 505 LYS A N 3797 C CA . LYS A 505 ? 1.5417 1.5939 1.3721 0.3954 -0.1622 -0.1499 505 LYS A CA 3798 C C . LYS A 505 ? 1.5356 1.6268 1.3830 0.4002 -0.1474 -0.1418 505 LYS A C 3799 O O . LYS A 505 ? 1.6315 1.7106 1.4964 0.3861 -0.1462 -0.1398 505 LYS A O 3800 C CB . LYS A 505 ? 1.4470 1.4647 1.2957 0.3635 -0.1612 -0.1394 505 LYS A CB 3801 C CG . LYS A 505 ? 1.4699 1.5121 1.3484 0.3442 -0.1391 -0.1151 505 LYS A CG 3802 C CD . LYS A 505 ? 1.4918 1.5093 1.3808 0.3198 -0.1374 -0.1044 505 LYS A CD 3803 C CE . LYS A 505 ? 1.3727 1.4128 1.2925 0.3021 -0.1176 -0.0817 505 LYS A CE 3804 N NZ . LYS A 505 ? 1.2484 1.2856 1.1722 0.2907 -0.1121 -0.0690 505 LYS A NZ 3805 N N . ILE A 506 ? 1.4292 1.5693 1.2716 0.4208 -0.1363 -0.1369 506 ILE A N 3806 C CA . ILE A 506 ? 1.3626 1.5447 1.2207 0.4280 -0.1230 -0.1297 506 ILE A CA 3807 C C . ILE A 506 ? 1.2524 1.4868 1.1285 0.4258 -0.0993 -0.1036 506 ILE A C 3808 O O . ILE A 506 ? 1.1461 1.4287 1.0165 0.4478 -0.0909 -0.1009 506 ILE A O 3809 C CB . ILE A 506 ? 1.3137 1.5088 1.1487 0.4600 -0.1350 -0.1523 506 ILE A CB 3810 C CG1 . ILE A 506 ? 1.3192 1.5652 1.1707 0.4695 -0.1200 -0.1439 506 ILE A CG1 3811 C CG2 . ILE A 506 ? 1.1845 1.3914 0.9886 0.4868 -0.1434 -0.1646 506 ILE A CG2 3812 C CD1 . ILE A 506 ? 1.2691 1.5415 1.0966 0.5054 -0.1284 -0.1636 506 ILE A CD1 3813 N N . ALA A 507 ? 1.3094 1.3854 1.1966 0.3101 -0.1064 -0.0501 507 ALA A N 3814 C CA . ALA A 507 ? 1.2648 1.3697 1.1693 0.3062 -0.0913 -0.0329 507 ALA A CA 3815 C C . ALA A 507 ? 1.3830 1.5041 1.3127 0.2941 -0.0797 -0.0229 507 ALA A C 3816 O O . ALA A 507 ? 1.4228 1.5412 1.3543 0.2934 -0.0824 -0.0300 507 ALA A O 3817 C CB . ALA A 507 ? 1.0342 1.1252 0.9440 0.2952 -0.0890 -0.0253 507 ALA A CB 3818 N N . SER A 508 ? 1.3434 1.4808 1.2925 0.2848 -0.0675 -0.0065 508 SER A N 3819 C CA . SER A 508 ? 1.3771 1.5326 1.3526 0.2734 -0.0563 0.0051 508 SER A CA 3820 C C . SER A 508 ? 1.4737 1.6471 1.4506 0.2806 -0.0561 -0.0001 508 SER A C 3821 O O . SER A 508 ? 1.4334 1.6029 1.4274 0.2688 -0.0538 0.0001 508 SER A O 3822 C CB . SER A 508 ? 1.3220 1.4515 1.3153 0.2523 -0.0557 0.0069 508 SER A CB 3823 O OG . SER A 508 ? 1.3025 1.4493 1.3224 0.2408 -0.0440 0.0233 508 SER A OG 3824 N N . ASN A 509 ? 1.5607 1.9525 1.5653 0.3830 -0.0223 -0.0068 509 ASN A N 3825 C CA . ASN A 509 ? 1.6098 2.0284 1.6159 0.3987 -0.0228 -0.0168 509 ASN A CA 3826 C C . ASN A 509 ? 1.6098 2.0990 1.6318 0.4106 -0.0040 0.0041 509 ASN A C 3827 O O . ASN A 509 ? 1.6504 2.1666 1.6904 0.4010 0.0108 0.0308 509 ASN A O 3828 C CB . ASN A 509 ? 1.6141 2.0128 1.5801 0.4246 -0.0412 -0.0478 509 ASN A CB 3829 C CG . ASN A 509 ? 1.5160 1.8589 1.4784 0.4143 -0.0588 -0.0688 509 ASN A CG 3830 O OD1 . ASN A 509 ? 1.4565 1.7978 1.4424 0.4023 -0.0568 -0.0671 509 ASN A OD1 3831 N ND2 . ASN A 509 ? 1.4768 1.7750 1.4101 0.4195 -0.0764 -0.0882 509 ASN A ND2 3832 N N . GLN A 510 ? 1.5320 2.0519 1.5482 0.4315 -0.0050 -0.0071 510 GLN A N 3833 C CA . GLN A 510 ? 1.4652 2.0571 1.4960 0.4450 0.0125 0.0117 510 GLN A CA 3834 C C . GLN A 510 ? 1.5161 2.1440 1.5098 0.4827 0.0101 -0.0017 510 GLN A C 3835 O O . GLN A 510 ? 1.5216 2.2063 1.5195 0.5015 0.0191 0.0026 510 GLN A O 3836 C CB . GLN A 510 ? 1.3058 1.9175 1.3672 0.4385 0.0165 0.0135 510 GLN A CB 3837 C CG . GLN A 510 ? 1.2725 1.8806 1.3810 0.4045 0.0267 0.0380 510 GLN A CG 3838 C CD . GLN A 510 ? 1.3360 1.9572 1.4581 0.3908 0.0398 0.0670 510 GLN A CD 3839 O OE1 . GLN A 510 ? 1.2916 1.8675 1.4175 0.3703 0.0352 0.0694 510 GLN A OE1 3840 N NE2 . GLN A 510 ? 1.3228 2.0078 1.4521 0.4029 0.0562 0.0895 510 GLN A NE2 3841 N N . LEU A 511 ? 1.5040 2.1004 1.4618 0.4944 -0.0027 -0.0183 511 LEU A N 3842 C CA . LEU A 511 ? 1.5454 2.1709 1.4657 0.5317 -0.0081 -0.0347 511 LEU A CA 3843 C C . LEU A 511 ? 1.6397 2.3346 1.5632 0.5442 0.0120 -0.0085 511 LEU A C 3844 O O . LEU A 511 ? 1.6575 2.3513 1.5865 0.5308 0.0203 0.0118 511 LEU A O 3845 C CB . LEU A 511 ? 1.4060 1.9772 1.2900 0.5391 -0.0286 -0.0592 511 LEU A CB 3846 C CG . LEU A 511 ? 1.2402 1.7465 1.1134 0.5342 -0.0514 -0.0881 511 LEU A CG 3847 C CD1 . LEU A 511 ? 1.2396 1.7030 1.0767 0.5460 -0.0715 -0.1110 511 LEU A CD1 3848 C CD2 . LEU A 511 ? 1.0761 1.6001 0.9457 0.5544 -0.0575 -0.1060 511 LEU A CD2 3849 N N . LYS A 512 ? 1.6104 2.3673 1.5308 0.5702 0.0199 -0.0081 512 LYS A N 3850 C CA . LYS A 512 ? 1.4329 2.2612 1.3478 0.5898 0.0371 0.0130 512 LYS A CA 3851 C C . LYS A 512 ? 1.4983 2.3234 1.3647 0.6222 0.0239 -0.0106 512 LYS A C 3852 O O . LYS A 512 ? 1.5583 2.3803 1.4142 0.6198 0.0269 0.0004 512 LYS A O 3853 C CB . LYS A 512 ? 1.2845 2.1857 1.2156 0.6058 0.0513 0.0234 512 LYS A CB 3854 C CG . LYS A 512 ? 1.2163 2.1420 1.2004 0.5746 0.0702 0.0581 512 LYS A CG 3855 C CD . LYS A 512 ? 1.2587 2.2740 1.2588 0.5917 0.0896 0.0790 512 LYS A CD 3856 C CE . LYS A 512 ? 1.2607 2.2963 1.2460 0.6198 0.0807 0.0509 512 LYS A CE 3857 N NZ . LYS A 512 ? 1.1194 2.2494 1.1111 0.6444 0.0988 0.0681 512 LYS A NZ 3858 N N . SER A 513 ? 1.5676 2.3920 1.4051 0.6528 0.0079 -0.0437 513 SER A N 3859 C CA . SER A 513 ? 1.6981 2.5112 1.4895 0.6842 -0.0094 -0.0716 513 SER A CA 3860 C C . SER A 513 ? 1.6583 2.4321 1.4238 0.7051 -0.0357 -0.1137 513 SER A C 3861 O O . SER A 513 ? 1.4794 2.2787 1.2490 0.7198 -0.0360 -0.1234 513 SER A O 3862 C CB . SER A 513 ? 1.8204 2.7136 1.5945 0.7169 0.0043 -0.0603 513 SER A CB 3863 O OG . SER A 513 ? 1.8885 2.8407 1.6629 0.7428 0.0103 -0.0651 513 SER A OG 3864 N N . VAL A 514 ? 1.8278 2.5396 1.5678 0.7062 -0.0580 -0.1379 514 VAL A N 3865 C CA . VAL A 514 ? 1.9922 2.6551 1.7090 0.7220 -0.0861 -0.1769 514 VAL A CA 3866 C C . VAL A 514 ? 2.1110 2.8081 1.7898 0.7699 -0.0985 -0.2042 514 VAL A C 3867 O O . VAL A 514 ? 2.0957 2.8281 1.7554 0.7887 -0.0936 -0.2001 514 VAL A O 3868 C CB . VAL A 514 ? 1.9317 2.5116 1.6404 0.7007 -0.1062 -0.1903 514 VAL A CB 3869 C CG1 . VAL A 514 ? 1.8759 2.4310 1.6184 0.6565 -0.0918 -0.1609 514 VAL A CG1 3870 C CG2 . VAL A 514 ? 1.9044 2.4797 1.5798 0.7213 -0.1181 -0.2039 514 VAL A CG2 3871 N N . PRO A 515 ? 2.2094 2.8957 1.8765 0.7911 -0.1157 -0.2329 515 PRO A N 3872 C CA . PRO A 515 ? 2.3469 3.0668 1.9791 0.8393 -0.1292 -0.2618 515 PRO A CA 3873 C C . PRO A 515 ? 2.4863 3.1809 2.0847 0.8567 -0.1479 -0.2819 515 PRO A C 3874 O O . PRO A 515 ? 2.4574 3.0802 2.0527 0.8369 -0.1657 -0.2922 515 PRO A O 3875 C CB . PRO A 515 ? 2.3013 2.9814 1.9297 0.8478 -0.1512 -0.2914 515 PRO A CB 3876 C CG . PRO A 515 ? 2.2217 2.8846 1.8883 0.8097 -0.1379 -0.2692 515 PRO A CG 3877 C CD . PRO A 515 ? 2.1720 2.8122 1.8577 0.7714 -0.1246 -0.2407 515 PRO A CD 3878 N N . ASP A 516 ? 2.6170 3.3727 2.1910 0.8937 -0.1438 -0.2868 516 ASP A N 3879 C CA . ASP A 516 ? 2.6554 3.3944 2.1947 0.9166 -0.1633 -0.3095 516 ASP A CA 3880 C C . ASP A 516 ? 2.6675 3.3490 2.1834 0.9371 -0.1999 -0.3545 516 ASP A C 3881 O O . ASP A 516 ? 2.5944 3.2937 2.1032 0.9631 -0.2083 -0.3745 516 ASP A O 3882 C CB . ASP A 516 ? 2.6301 3.4550 2.1476 0.9554 -0.1503 -0.3054 516 ASP A CB 3883 C CG . ASP A 516 ? 2.5524 3.4225 2.0875 0.9350 -0.1193 -0.2618 516 ASP A CG 3884 O OD1 . ASP A 516 ? 2.5082 3.3358 2.0681 0.8926 -0.1117 -0.2393 516 ASP A OD1 3885 O OD2 . ASP A 516 ? 2.5251 3.4743 2.0489 0.9621 -0.1030 -0.2498 516 ASP A OD2 3886 N N . GLY A 517 ? 2.7158 3.3283 2.2217 0.9249 -0.2223 -0.3697 517 GLY A N 3887 C CA . GLY A 517 ? 2.7646 3.3141 2.2526 0.9389 -0.2588 -0.4095 517 GLY A CA 3888 C C . GLY A 517 ? 2.7364 3.2212 2.2492 0.9038 -0.2657 -0.4067 517 GLY A C 3889 O O . GLY A 517 ? 2.7791 3.2444 2.2889 0.9170 -0.2823 -0.4286 517 GLY A O 3890 N N . ILE A 518 ? 2.6298 3.0826 2.1668 0.8600 -0.2531 -0.3797 518 ILE A N 3891 C CA . ILE A 518 ? 2.5050 2.9002 2.0666 0.8246 -0.2571 -0.3737 518 ILE A CA 3892 C C . ILE A 518 ? 2.3410 2.6565 1.9006 0.8016 -0.2799 -0.3833 518 ILE A C 3893 O O . ILE A 518 ? 2.3545 2.6130 1.9206 0.7883 -0.2979 -0.3949 518 ILE A O 3894 C CB . ILE A 518 ? 1.7585 2.1814 1.3554 0.7905 -0.2241 -0.3343 518 ILE A CB 3895 C CG1 . ILE A 518 ? 1.5843 1.9515 1.2045 0.7582 -0.2295 -0.3311 518 ILE A CG1 3896 C CG2 . ILE A 518 ? 1.7339 2.1683 1.3390 0.7690 -0.2060 -0.3071 518 ILE A CG2 3897 C CD1 . ILE A 518 ? 1.5004 1.8530 1.1131 0.7785 -0.2482 -0.3571 518 ILE A CD1 3898 N N . PHE A 519 ? 2.1473 2.4603 1.6983 0.7972 -0.2792 -0.3778 519 PHE A N 3899 C CA . PHE A 519 ? 2.0675 2.3097 1.6156 0.7784 -0.3020 -0.3883 519 PHE A CA 3900 C C . PHE A 519 ? 2.1781 2.3965 1.6960 0.8129 -0.3364 -0.4274 519 PHE A C 3901 O O . PHE A 519 ? 2.1498 2.3367 1.6567 0.8114 -0.3530 -0.4376 519 PHE A O 3902 C CB . PHE A 519 ? 1.9723 2.2181 1.5269 0.7559 -0.2873 -0.3651 519 PHE A CB 3903 C CG . PHE A 519 ? 1.9091 2.1970 1.4894 0.7323 -0.2517 -0.3271 519 PHE A CG 3904 C CD1 . PHE A 519 ? 1.9156 2.2406 1.4960 0.7291 -0.2328 -0.3057 519 PHE A CD1 3905 C CD2 . PHE A 519 ? 1.8249 2.1154 1.4300 0.7140 -0.2383 -0.3128 519 PHE A CD2 3906 C CE1 . PHE A 519 ? 1.8402 2.2017 1.4464 0.7070 -0.2017 -0.2701 519 PHE A CE1 3907 C CE2 . PHE A 519 ? 1.7451 2.0729 1.3762 0.6922 -0.2075 -0.2786 519 PHE A CE2 3908 C CZ . PHE A 519 ? 1.7544 2.1169 1.3867 0.6884 -0.1895 -0.2570 519 PHE A CZ 3909 N N . ASP A 520 ? 2.3301 2.5642 1.8355 0.8447 -0.3478 -0.4500 520 ASP A N 3910 C CA . ASP A 520 ? 2.4862 2.6959 1.9642 0.8800 -0.3832 -0.4902 520 ASP A CA 3911 C C . ASP A 520 ? 2.5227 2.6488 2.0078 0.8623 -0.4131 -0.5061 520 ASP A C 3912 O O . ASP A 520 ? 2.5540 2.6326 2.0284 0.8644 -0.4409 -0.5255 520 ASP A O 3913 C CB . ASP A 520 ? 2.5745 2.8375 2.0359 0.9236 -0.3838 -0.5087 520 ASP A CB 3914 C CG . ASP A 520 ? 2.5978 2.9440 2.0447 0.9506 -0.3616 -0.5000 520 ASP A CG 3915 O OD1 . ASP A 520 ? 2.5842 2.9433 2.0325 0.9364 -0.3476 -0.4808 520 ASP A OD1 3916 O OD2 . ASP A 520 ? 2.6013 3.0014 2.0353 0.9865 -0.3583 -0.5118 520 ASP A OD2 3917 N N . ARG A 521 ? 2.5004 2.6097 2.0042 0.8449 -0.4079 -0.4972 521 ARG A N 3918 C CA . ARG A 521 ? 2.4898 2.5231 2.0021 0.8267 -0.4342 -0.5082 521 ARG A CA 3919 C C . ARG A 521 ? 2.3451 2.3371 1.8814 0.7777 -0.4248 -0.4812 521 ARG A C 3920 O O . ARG A 521 ? 2.3561 2.2862 1.9021 0.7573 -0.4436 -0.4846 521 ARG A O 3921 C CB . ARG A 521 ? 2.5751 2.6074 2.0929 0.8358 -0.4375 -0.5155 521 ARG A CB 3922 C CG . ARG A 521 ? 2.6331 2.7274 2.1662 0.8308 -0.4018 -0.4907 521 ARG A CG 3923 C CD . ARG A 521 ? 2.6910 2.8631 2.2064 0.8705 -0.3890 -0.4978 521 ARG A CD 3924 N NE . ARG A 521 ? 2.6639 2.8943 2.1961 0.8674 -0.3582 -0.4758 521 ARG A NE 3925 C CZ . ARG A 521 ? 2.6073 2.9153 2.1328 0.8921 -0.3374 -0.4695 521 ARG A CZ 3926 N NH1 . ARG A 521 ? 2.5595 2.8980 2.0594 0.9234 -0.3435 -0.4842 521 ARG A NH1 3927 N NH2 . ARG A 521 ? 2.5895 2.9464 2.1348 0.8854 -0.3106 -0.4480 521 ARG A NH2 3928 N N . LEU A 522 ? 2.2214 2.2492 1.7674 0.7599 -0.3960 -0.4540 522 LEU A N 3929 C CA . LEU A 522 ? 2.0983 2.0910 1.6637 0.7176 -0.3883 -0.4309 522 LEU A CA 3930 C C . LEU A 522 ? 2.0976 2.0639 1.6495 0.7201 -0.4073 -0.4429 522 LEU A C 3931 O O . LEU A 522 ? 1.9550 1.9362 1.5115 0.7048 -0.3917 -0.4249 522 LEU A O 3932 C CB . LEU A 522 ? 1.9303 1.9700 1.5146 0.6962 -0.3502 -0.3961 522 LEU A CB 3933 C CG . LEU A 522 ? 1.7692 1.8319 1.3731 0.6864 -0.3302 -0.3804 522 LEU A CG 3934 C CD1 . LEU A 522 ? 1.5521 1.6424 1.1804 0.6560 -0.2976 -0.3451 522 LEU A CD1 3935 C CD2 . LEU A 522 ? 1.8097 1.8151 1.4228 0.6714 -0.3486 -0.3886 522 LEU A CD2 3936 N N . THR A 523 ? 2.2116 2.1382 1.7477 0.7403 -0.4424 -0.4742 523 THR A N 3937 C CA . THR A 523 ? 2.2417 2.1388 1.7649 0.7463 -0.4666 -0.4912 523 THR A CA 3938 C C . THR A 523 ? 2.0808 1.9267 1.6242 0.7036 -0.4695 -0.4740 523 THR A C 3939 O O . THR A 523 ? 2.0163 1.8238 1.5551 0.7011 -0.4936 -0.4871 523 THR A O 3940 C CB . THR A 523 ? 2.4943 2.3548 1.9998 0.7767 -0.5069 -0.5298 523 THR A CB 3941 O OG1 . THR A 523 ? 2.4838 2.2932 2.0038 0.7598 -0.5211 -0.5308 523 THR A OG1 3942 C CG2 . THR A 523 ? 2.4826 2.3965 1.9649 0.8239 -0.5068 -0.5509 523 THR A CG2 3943 N N . SER A 524 ? 1.9366 1.7842 1.5030 0.6706 -0.4448 -0.4447 524 SER A N 3944 C CA . SER A 524 ? 1.7192 1.5178 1.3061 0.6305 -0.4479 -0.4287 524 SER A CA 3945 C C . SER A 524 ? 1.6013 1.4283 1.2049 0.6024 -0.4145 -0.3960 524 SER A C 3946 O O . SER A 524 ? 1.4722 1.2736 1.0870 0.5753 -0.4148 -0.3838 524 SER A O 3947 C CB . SER A 524 ? 1.6231 1.3845 1.2229 0.6172 -0.4568 -0.4281 524 SER A CB 3948 O OG . SER A 524 ? 1.5922 1.3563 1.1766 0.6508 -0.4741 -0.4535 524 SER A OG 3949 N N . LEU A 525 ? 1.6506 1.5314 1.2572 0.6092 -0.3864 -0.3819 525 LEU A N 3950 C CA . LEU A 525 ? 1.6253 1.5372 1.2489 0.5854 -0.3543 -0.3508 525 LEU A CA 3951 C C . LEU A 525 ? 1.6254 1.5355 1.2452 0.5776 -0.3542 -0.3454 525 LEU A C 3952 O O . LEU A 525 ? 1.8231 1.7530 1.4222 0.6041 -0.3624 -0.3601 525 LEU A O 3953 C CB . LEU A 525 ? 1.5547 1.5324 1.1774 0.6034 -0.3284 -0.3408 525 LEU A CB 3954 C CG . LEU A 525 ? 1.4901 1.5194 1.1174 0.6000 -0.2999 -0.3172 525 LEU A CG 3955 C CD1 . LEU A 525 ? 1.4278 1.4394 1.0786 0.5608 -0.2851 -0.2911 525 LEU A CD1 3956 C CD2 . LEU A 525 ? 1.4830 1.5713 1.1148 0.6143 -0.2768 -0.3063 525 LEU A CD2 3957 N N . GLN A 526 ? 1.4487 1.3363 1.0881 0.5425 -0.3454 -0.3251 526 GLN A N 3958 C CA . GLN A 526 ? 1.5516 1.4340 1.1894 0.5326 -0.3461 -0.3195 526 GLN A CA 3959 C C . GLN A 526 ? 1.5955 1.5068 1.2509 0.5099 -0.3154 -0.2887 526 GLN A C 3960 O O . GLN A 526 ? 1.6488 1.5578 1.3050 0.4997 -0.3133 -0.2811 526 GLN A O 3961 C CB . GLN A 526 ? 1.6634 1.4849 1.3063 0.5135 -0.3717 -0.3282 526 GLN A CB 3962 C CG . GLN A 526 ? 1.7695 1.5588 1.4360 0.4801 -0.3674 -0.3126 526 GLN A CG 3963 C CD . GLN A 526 ? 1.8091 1.5397 1.4786 0.4678 -0.3968 -0.3245 526 GLN A CD 3964 O OE1 . GLN A 526 ? 1.8031 1.5071 1.4905 0.4370 -0.3951 -0.3096 526 GLN A OE1 3965 N NE2 . GLN A 526 ? 1.7870 1.4981 1.4398 0.4924 -0.4246 -0.3513 526 GLN A NE2 3966 N N . LYS A 527 ? 1.6479 1.5861 1.3180 0.5028 -0.2927 -0.2717 527 LYS A N 3967 C CA . LYS A 527 ? 1.6053 1.5714 1.2947 0.4821 -0.2641 -0.2424 527 LYS A CA 3968 C C . LYS A 527 ? 1.4439 1.4433 1.1474 0.4822 -0.2436 -0.2295 527 LYS A C 3969 O O . LYS A 527 ? 1.2106 1.1947 0.9175 0.4832 -0.2509 -0.2384 527 LYS A O 3970 C CB . LYS A 527 ? 1.6032 1.5305 1.3117 0.4465 -0.2644 -0.2297 527 LYS A CB 3971 C CG . LYS A 527 ? 1.6113 1.5621 1.3363 0.4276 -0.2401 -0.2032 527 LYS A CG 3972 C CD . LYS A 527 ? 1.5982 1.5111 1.3353 0.3989 -0.2456 -0.1963 527 LYS A CD 3973 C CE . LYS A 527 ? 1.5604 1.4963 1.3101 0.3850 -0.2250 -0.1734 527 LYS A CE 3974 N NZ . LYS A 527 ? 1.4634 1.3685 1.2177 0.3653 -0.2334 -0.1711 527 LYS A NZ 3975 N N . ILE A 528 ? 1.4516 1.4969 1.1644 0.4812 -0.2186 -0.2081 528 ILE A N 3976 C CA . ILE A 528 ? 1.4882 1.5719 1.2145 0.4846 -0.1998 -0.1962 528 ILE A CA 3977 C C . ILE A 528 ? 1.5721 1.6883 1.3214 0.4666 -0.1727 -0.1656 528 ILE A C 3978 O O . ILE A 528 ? 1.6514 1.7740 1.3994 0.4614 -0.1668 -0.1545 528 ILE A O 3979 C CB . ILE A 528 ? 1.6027 1.7277 1.3076 0.5224 -0.2019 -0.2104 528 ILE A CB 3980 C CG1 . ILE A 528 ? 1.4641 1.6184 1.1829 0.5263 -0.1891 -0.2045 528 ILE A CG1 3981 C CG2 . ILE A 528 ? 1.5491 1.7207 1.2425 0.5389 -0.1896 -0.2006 528 ILE A CG2 3982 C CD1 . ILE A 528 ? 1.2894 1.4829 0.9870 0.5646 -0.1933 -0.2213 528 ILE A CD1 3983 N N . TRP A 529 ? 1.4930 1.6282 1.2643 0.4573 -0.1575 -0.1523 529 TRP A N 3984 C CA . TRP A 529 ? 1.3564 1.5212 1.1544 0.4393 -0.1329 -0.1231 529 TRP A CA 3985 C C . TRP A 529 ? 1.3478 1.5684 1.1517 0.4563 -0.1173 -0.1143 529 TRP A C 3986 O O . TRP A 529 ? 1.4252 1.6489 1.2269 0.4675 -0.1228 -0.1272 529 TRP A O 3987 C CB . TRP A 529 ? 1.2735 1.4057 1.0987 0.4074 -0.1302 -0.1143 529 TRP A CB 3988 C CG . TRP A 529 ? 1.3043 1.3989 1.1345 0.3844 -0.1348 -0.1096 529 TRP A CG 3989 C CD1 . TRP A 529 ? 1.4048 1.5061 1.2548 0.3646 -0.1203 -0.0875 529 TRP A CD1 3990 C CD2 . TRP A 529 ? 1.2788 1.3245 1.0952 0.3788 -0.1558 -0.1267 529 TRP A CD2 3991 N NE1 . TRP A 529 ? 1.4375 1.4992 1.2857 0.3483 -0.1303 -0.0909 529 TRP A NE1 3992 C CE2 . TRP A 529 ? 1.3314 1.3595 1.1598 0.3559 -0.1517 -0.1139 529 TRP A CE2 3993 C CE3 . TRP A 529 ? 1.1591 1.1743 0.9557 0.3908 -0.1783 -0.1510 529 TRP A CE3 3994 C CZ2 . TRP A 529 ? 1.1856 1.1702 1.0070 0.3445 -0.1682 -0.1239 529 TRP A CZ2 3995 C CZ3 . TRP A 529 ? 1.1499 1.1194 0.9409 0.3783 -0.1954 -0.1599 529 TRP A CZ3 3996 C CH2 . TRP A 529 ? 1.1068 1.0631 0.9102 0.3552 -0.1896 -0.1460 529 TRP A CH2 3997 N N . LEU A 530 ? 1.3417 1.6077 1.1537 0.4586 -0.0980 -0.0917 530 LEU A N 3998 C CA . LEU A 530 ? 1.3414 1.6655 1.1642 0.4716 -0.0807 -0.0783 530 LEU A CA 3999 C C . LEU A 530 ? 1.3300 1.6868 1.1832 0.4531 -0.0570 -0.0436 530 LEU A C 4000 O O . LEU A 530 ? 1.3392 1.7422 1.2100 0.4568 -0.0412 -0.0278 530 LEU A O 4001 C CB . LEU A 530 ? 1.3079 1.6724 1.1002 0.5093 -0.0839 -0.0905 530 LEU A CB 4002 C CG . LEU A 530 ? 1.2045 1.5625 0.9736 0.5356 -0.1019 -0.1213 530 LEU A CG 4003 C CD1 . LEU A 530 ? 1.1249 1.4209 0.8733 0.5352 -0.1286 -0.1484 530 LEU A CD1 4004 C CD2 . LEU A 530 ? 1.1521 1.5677 0.8983 0.5726 -0.0980 -0.1259 530 LEU A CD2 4005 N N . HIS A 531 ? 1.2783 1.6111 1.1389 0.4331 -0.0552 -0.0318 531 HIS A N 4006 C CA . HIS A 531 ? 1.4185 1.7775 1.3073 0.4158 -0.0351 0.0009 531 HIS A CA 4007 C C . HIS A 531 ? 1.4563 1.8335 1.3827 0.3990 -0.0213 0.0185 531 HIS A C 4008 O O . HIS A 531 ? 1.2920 1.6674 1.2217 0.4028 -0.0259 0.0056 531 HIS A O 4009 C CB . HIS A 531 ? 1.5126 1.8334 1.4063 0.3941 -0.0382 0.0075 531 HIS A CB 4010 C CG . HIS A 531 ? 1.6321 1.8951 1.5324 0.3730 -0.0519 -0.0072 531 HIS A CG 4011 N ND1 . HIS A 531 ? 1.6552 1.9045 1.5875 0.3488 -0.0464 0.0021 531 HIS A ND1 4012 C CD2 . HIS A 531 ? 1.6629 1.8802 1.5426 0.3725 -0.0709 -0.0296 531 HIS A CD2 4013 C CE1 . HIS A 531 ? 1.6250 1.8247 1.5542 0.3354 -0.0606 -0.0138 531 HIS A CE1 4014 N NE2 . HIS A 531 ? 1.6416 1.8211 1.5402 0.3485 -0.0754 -0.0321 531 HIS A NE2 4015 N N . THR A 532 ? 1.6513 2.0463 1.6068 0.3810 -0.0055 0.0479 532 THR A N 4016 C CA . THR A 532 ? 1.7306 2.1487 1.7253 0.3653 0.0081 0.0678 532 THR A CA 4017 C C . THR A 532 ? 1.7576 2.2057 1.7504 0.3824 0.0088 0.0576 532 THR A C 4018 O O . THR A 532 ? 1.6586 2.0799 1.6556 0.3768 -0.0006 0.0404 532 THR A O 4019 C CB . THR A 532 ? 1.7562 2.1275 1.7777 0.3346 0.0035 0.0678 532 THR A CB 4020 O OG1 . THR A 532 ? 1.7625 2.1089 1.7855 0.3204 0.0029 0.0770 532 THR A OG1 4021 C CG2 . THR A 532 ? 1.7490 2.1448 1.8136 0.3183 0.0164 0.0885 532 THR A CG2 4022 N N . ASN A 533 ? 1.8995 2.4058 1.8856 0.4042 0.0203 0.0689 533 ASN A N 4023 C CA . ASN A 533 ? 1.9194 2.4600 1.8985 0.4258 0.0205 0.0575 533 ASN A CA 4024 C C . ASN A 533 ? 1.9266 2.5415 1.9139 0.4411 0.0399 0.0827 533 ASN A C 4025 O O . ASN A 533 ? 1.9402 2.5804 1.9091 0.4552 0.0451 0.0922 533 ASN A O 4026 C CB . ASN A 533 ? 1.9182 2.4369 1.8530 0.4521 0.0014 0.0227 533 ASN A CB 4027 C CG . ASN A 533 ? 1.9102 2.4270 1.8409 0.4639 -0.0076 0.0006 533 ASN A CG 4028 O OD1 . ASN A 533 ? 1.9774 2.5343 1.9299 0.4653 0.0039 0.0116 533 ASN A OD1 4029 N ND2 . ASN A 533 ? 1.8230 2.2932 1.7264 0.4725 -0.0288 -0.0303 533 ASN A ND2 4030 N N . PRO A 534 ? 1.9275 2.5797 1.9435 0.4379 0.0507 0.0950 534 PRO A N 4031 C CA . PRO A 534 ? 1.9190 2.6475 1.9436 0.4537 0.0693 0.1194 534 PRO A CA 4032 C C . PRO A 534 ? 1.9222 2.6838 1.9067 0.4932 0.0639 0.0972 534 PRO A C 4033 O O . PRO A 534 ? 1.9238 2.6978 1.9076 0.5053 0.0599 0.0813 534 PRO A O 4034 C CB . PRO A 534 ? 1.8754 2.6252 1.9434 0.4370 0.0785 0.1334 534 PRO A CB 4035 C CG . PRO A 534 ? 1.8616 2.5452 1.9481 0.4077 0.0672 0.1231 534 PRO A CG 4036 C CD . PRO A 534 ? 1.9033 2.5312 1.9491 0.4171 0.0474 0.0904 534 PRO A CD 4037 N N . TRP A 535 ? 1.9273 2.7028 1.8791 0.5141 0.0628 0.0950 535 TRP A N 4038 C CA . TRP A 535 ? 1.9518 2.7557 1.8625 0.5542 0.0550 0.0705 535 TRP A CA 4039 C C . TRP A 535 ? 1.9771 2.8691 1.8909 0.5769 0.0744 0.0925 535 TRP A C 4040 O O . TRP A 535 ? 1.9963 2.9273 1.9469 0.5642 0.0906 0.1179 535 TRP A O 4041 C CB . TRP A 535 ? 1.9816 2.7548 1.8525 0.5683 0.0410 0.0523 535 TRP A CB 4042 C CG . TRP A 535 ? 1.9867 2.6785 1.8448 0.5557 0.0180 0.0228 535 TRP A CG 4043 C CD1 . TRP A 535 ? 1.9791 2.6170 1.8473 0.5273 0.0134 0.0279 535 TRP A CD1 4044 C CD2 . TRP A 535 ? 1.9956 2.6528 1.8293 0.5717 -0.0037 -0.0152 535 TRP A CD2 4045 N NE1 . TRP A 535 ? 1.9599 2.5346 1.8121 0.5239 -0.0088 -0.0032 535 TRP A NE1 4046 C CE2 . TRP A 535 ? 2.0135 2.5972 1.8448 0.5503 -0.0200 -0.0294 535 TRP A CE2 4047 C CE3 . TRP A 535 ? 1.9827 2.6645 1.7971 0.6024 -0.0114 -0.0381 535 TRP A CE3 4048 C CZ2 . TRP A 535 ? 2.0505 2.5844 1.8621 0.5571 -0.0433 -0.0634 535 TRP A CZ2 4049 C CZ3 . TRP A 535 ? 2.0022 2.6317 1.7963 0.6100 -0.0356 -0.0736 535 TRP A CZ3 4050 C CH2 . TRP A 535 ? 2.0413 2.5974 1.8347 0.5868 -0.0512 -0.0849 535 TRP A CH2 4051 N N . ASP A 536 ? 1.9525 2.8769 1.8279 0.6110 0.0720 0.0825 536 ASP A N 4052 C CA . ASP A 536 ? 1.8815 2.8938 1.7523 0.6388 0.0890 0.0997 536 ASP A CA 4053 C C . ASP A 536 ? 1.8488 2.8818 1.6734 0.6733 0.0829 0.0864 536 ASP A C 4054 O O . ASP A 536 ? 1.7955 2.8365 1.5849 0.7075 0.0691 0.0536 536 ASP A O 4055 C CB . ASP A 536 ? 1.7948 2.8381 1.6667 0.6577 0.0873 0.0830 536 ASP A CB 4056 C CG . ASP A 536 ? 1.7015 2.8419 1.5757 0.6832 0.1074 0.1049 536 ASP A CG 4057 O OD1 . ASP A 536 ? 1.6684 2.8524 1.5487 0.6819 0.1245 0.1377 536 ASP A OD1 4058 O OD2 . ASP A 536 ? 1.6369 2.8115 1.5071 0.7048 0.1062 0.0900 536 ASP A OD2 4059 N N . CYS A 537 ? 1.8946 2.9355 1.7195 0.6651 0.0922 0.1112 537 CYS A N 4060 C CA . CYS A 537 ? 2.0350 3.0885 1.8165 0.6951 0.0850 0.0983 537 CYS A CA 4061 C C . CYS A 537 ? 2.1213 3.2694 1.8889 0.7293 0.1018 0.1155 537 CYS A C 4062 O O . CYS A 537 ? 2.0127 3.1947 1.7731 0.7348 0.1131 0.1395 537 CYS A O 4063 C CB . CYS A 537 ? 2.0257 3.0386 1.8102 0.6720 0.0844 0.1131 537 CYS A CB 4064 S SG . CYS A 537 ? 1.9165 2.8212 1.7098 0.6375 0.0626 0.0887 537 CYS A SG 4065 N N . SER A 538 ? 2.2467 3.4384 2.0101 0.7531 0.1031 0.1031 538 SER A N 4066 C CA . SER A 538 ? 2.3207 3.6064 2.0679 0.7902 0.1176 0.1145 538 SER A CA 4067 C C . SER A 538 ? 2.3447 3.6324 2.0366 0.8350 0.0977 0.0736 538 SER A C 4068 O O . SER A 538 ? 2.3557 3.6056 2.0279 0.8498 0.0758 0.0320 538 SER A O 4069 C CB . SER A 538 ? 2.3544 3.6894 2.1245 0.7958 0.1282 0.1198 538 SER A CB 4070 O OG . SER A 538 ? 2.3623 3.6693 2.1821 0.7528 0.1366 0.1421 538 SER A OG 4071 N N . CYS A 539 ? 2.2945 3.6271 1.9622 0.8569 0.1048 0.0857 539 CYS A N 4072 C CA . CYS A 539 ? 2.2039 3.5369 1.8191 0.8987 0.0849 0.0478 539 CYS A CA 4073 C C . CYS A 539 ? 2.0477 3.4047 1.6380 0.9380 0.0713 0.0094 539 CYS A C 4074 O O . CYS A 539 ? 1.9789 3.2920 1.5349 0.9599 0.0439 -0.0354 539 CYS A O 4075 C CB . CYS A 539 ? 2.3065 3.7071 1.9023 0.9208 0.0997 0.0725 539 CYS A CB 4076 S SG . CYS A 539 ? 4.1352 5.4865 3.6880 0.9344 0.0770 0.0459 539 CYS A SG 4077 N N . PRO A 540 ? 1.9984 3.4253 1.6070 0.9474 0.0897 0.0269 540 PRO A N 4078 C CA . PRO A 540 ? 2.0097 3.4642 1.5960 0.9860 0.0777 -0.0087 540 PRO A CA 4079 C C . PRO A 540 ? 1.9418 3.3177 1.5337 0.9734 0.0543 -0.0448 540 PRO A C 4080 O O . PRO A 540 ? 1.9326 3.3168 1.4998 1.0079 0.0380 -0.0816 540 PRO A O 4081 C CB . PRO A 540 ? 1.9761 3.5255 1.5897 0.9905 0.1070 0.0277 540 PRO A CB 4082 C CG . PRO A 540 ? 1.9486 3.5368 1.5830 0.9698 0.1326 0.0792 540 PRO A CG 4083 C CD . PRO A 540 ? 1.9223 3.4184 1.5687 0.9293 0.1226 0.0814 540 PRO A CD 4084 N N . ARG A 541 ? 1.8424 3.1455 1.4654 0.9267 0.0523 -0.0348 541 ARG A N 4085 C CA . ARG A 541 ? 1.7906 3.0200 1.4201 0.9131 0.0311 -0.0659 541 ARG A CA 4086 C C . ARG A 541 ? 1.6305 2.7600 1.2521 0.8897 0.0081 -0.0866 541 ARG A C 4087 O O . ARG A 541 ? 1.4937 2.5664 1.0990 0.8973 -0.0179 -0.1253 541 ARG A O 4088 C CB . ARG A 541 ? 1.7793 3.0159 1.4564 0.8814 0.0475 -0.0410 541 ARG A CB 4089 C CG . ARG A 541 ? 1.7264 2.9959 1.4443 0.8474 0.0765 0.0121 541 ARG A CG 4090 C CD . ARG A 541 ? 1.6752 3.0527 1.3998 0.8699 0.1019 0.0416 541 ARG A CD 4091 N NE . ARG A 541 ? 1.6143 3.0306 1.3540 0.8807 0.1062 0.0359 541 ARG A NE 4092 C CZ . ARG A 541 ? 1.5207 3.0329 1.2665 0.9035 0.1261 0.0560 541 ARG A CZ 4093 N NH1 . ARG A 541 ? 1.5156 3.0953 1.2529 0.9181 0.1439 0.0842 541 ARG A NH1 4094 N NH2 . ARG A 541 ? 1.3856 2.9285 1.1460 0.9123 0.1283 0.0486 541 ARG A NH2 4095 N N . ILE A 542 ? 1.5933 2.7026 1.2274 0.8615 0.0172 -0.0603 542 ILE A N 4096 C CA . ILE A 542 ? 1.6546 2.6730 1.2872 0.8347 -0.0016 -0.0746 542 ILE A CA 4097 C C . ILE A 542 ? 1.8210 2.8141 1.4088 0.8633 -0.0257 -0.1088 542 ILE A C 4098 O O . ILE A 542 ? 1.7127 2.6712 1.2949 0.8492 -0.0302 -0.1043 542 ILE A O 4099 C CB . ILE A 542 ? 1.4767 2.4786 1.1427 0.7916 0.0163 -0.0344 542 ILE A CB 4100 C CG1 . ILE A 542 ? 1.5031 2.4102 1.1780 0.7581 -0.0014 -0.0483 542 ILE A CG1 4101 C CG2 . ILE A 542 ? 1.4513 2.4958 1.1024 0.8033 0.0280 -0.0130 542 ILE A CG2 4102 C CD1 . ILE A 542 ? 1.5143 2.4008 1.2187 0.7186 0.0129 -0.0136 542 ILE A CD1 4103 N N . ASP A 543 ? 2.0764 3.0860 1.6332 0.9039 -0.0426 -0.1443 543 ASP A N 4104 C CA . ASP A 543 ? 2.2569 3.2479 1.7708 0.9364 -0.0680 -0.1806 543 ASP A CA 4105 C C . ASP A 543 ? 2.3235 3.2158 1.8339 0.9146 -0.0954 -0.2059 543 ASP A C 4106 O O . ASP A 543 ? 2.1933 3.0546 1.7006 0.8988 -0.0985 -0.1992 543 ASP A O 4107 C CB . ASP A 543 ? 2.2760 3.3042 1.7610 0.9848 -0.0818 -0.2151 543 ASP A CB 4108 C CG . ASP A 543 ? 2.2061 3.3400 1.6847 1.0158 -0.0577 -0.1946 543 ASP A CG 4109 O OD1 . ASP A 543 ? 2.2137 3.3901 1.6768 1.0292 -0.0476 -0.1794 543 ASP A OD1 4110 O OD2 . ASP A 543 ? 2.1122 3.2882 1.6011 1.0276 -0.0490 -0.1935 543 ASP A OD2 4111 N N . TYR A 544 ? 2.4563 3.3018 1.9677 0.9143 -0.1152 -0.2341 544 TYR A N 4112 C CA . TYR A 544 ? 2.5037 3.2591 2.0089 0.8997 -0.1446 -0.2623 544 TYR A CA 4113 C C . TYR A 544 ? 2.4239 3.1280 1.9541 0.8526 -0.1379 -0.2384 544 TYR A C 4114 O O . TYR A 544 ? 2.4509 3.1277 1.9681 0.8490 -0.1478 -0.2429 544 TYR A O 4115 C CB . TYR A 544 ? 2.5499 3.2676 2.0608 0.9001 -0.1612 -0.2866 544 TYR A CB 4116 C CG . TYR A 544 ? 2.6278 3.2547 2.1328 0.8864 -0.1926 -0.3149 544 TYR A CG 4117 C CD1 . TYR A 544 ? 2.6934 3.2882 2.1753 0.8947 -0.2128 -0.3332 544 TYR A CD1 4118 C CD2 . TYR A 544 ? 2.6403 3.2156 2.1632 0.8656 -0.2025 -0.3228 544 TYR A CD2 4119 C CE1 . TYR A 544 ? 2.7190 3.2327 2.1980 0.8811 -0.2417 -0.3571 544 TYR A CE1 4120 C CE2 . TYR A 544 ? 2.6860 3.1807 2.2045 0.8527 -0.2309 -0.3460 544 TYR A CE2 4121 C CZ . TYR A 544 ? 2.7225 3.1869 2.2201 0.8599 -0.2503 -0.3625 544 TYR A CZ 4122 O OH . TYR A 544 ? 2.7522 3.1382 2.2481 0.8459 -0.2787 -0.3837 544 TYR A OH 4123 N N . LEU A 545 ? 2.2814 2.9734 1.8475 0.8177 -0.1222 -0.2144 545 LEU A N 4124 C CA . LEU A 545 ? 2.2044 2.8517 1.7972 0.7730 -0.1144 -0.1908 545 LEU A CA 4125 C C . LEU A 545 ? 2.2034 2.8618 1.7860 0.7717 -0.1084 -0.1762 545 LEU A C 4126 O O . LEU A 545 ? 2.1381 2.7408 1.7201 0.7520 -0.1207 -0.1812 545 LEU A O 4127 C CB . LEU A 545 ? 2.1227 2.7950 1.7553 0.7448 -0.0877 -0.1558 545 LEU A CB 4128 C CG . LEU A 545 ? 2.0114 2.6410 1.6755 0.6985 -0.0786 -0.1306 545 LEU A CG 4129 C CD1 . LEU A 545 ? 1.9241 2.4724 1.5913 0.6777 -0.1009 -0.1528 545 LEU A CD1 4130 C CD2 . LEU A 545 ? 1.9412 2.6089 1.6437 0.6768 -0.0515 -0.0951 545 LEU A CD2 4131 N N . SER A 546 ? 2.2490 2.9820 1.8238 0.7937 -0.0896 -0.1578 546 SER A N 4132 C CA . SER A 546 ? 2.2017 2.9562 1.7684 0.7937 -0.0799 -0.1385 546 SER A CA 4133 C C . SER A 546 ? 2.1970 2.9121 1.7313 0.8090 -0.1062 -0.1689 546 SER A C 4134 O O . SER A 546 ? 2.1140 2.8053 1.6509 0.7908 -0.1055 -0.1573 546 SER A O 4135 C CB . SER A 546 ? 2.1430 2.9902 1.7019 0.8218 -0.0576 -0.1173 546 SER A CB 4136 O OG . SER A 546 ? 2.0527 2.9365 1.6480 0.8003 -0.0305 -0.0805 546 SER A OG 4137 N N . ARG A 547 ? 2.2538 2.9618 1.7589 0.8426 -0.1303 -0.2082 547 ARG A N 4138 C CA . ARG A 547 ? 2.3032 2.9775 1.7775 0.8607 -0.1575 -0.2394 547 ARG A CA 4139 C C . ARG A 547 ? 2.2632 2.8476 1.7426 0.8385 -0.1850 -0.2644 547 ARG A C 4140 O O . ARG A 547 ? 2.1663 2.7116 1.6326 0.8370 -0.2038 -0.2795 547 ARG A O 4141 C CB . ARG A 547 ? 2.3831 3.1024 1.8199 0.9137 -0.1711 -0.2697 547 ARG A CB 4142 C CG . ARG A 547 ? 2.3302 3.1436 1.7636 0.9392 -0.1445 -0.2480 547 ARG A CG 4143 C CD . ARG A 547 ? 2.2382 3.1025 1.6301 0.9908 -0.1550 -0.2713 547 ARG A CD 4144 N NE . ARG A 547 ? 2.2189 3.1351 1.5970 1.0282 -0.1554 -0.2878 547 ARG A NE 4145 C CZ . ARG A 547 ? 2.1698 3.1522 1.5641 1.0303 -0.1275 -0.2599 547 ARG A CZ 4146 N NH1 . ARG A 547 ? 2.1539 3.1563 1.5803 0.9960 -0.0976 -0.2135 547 ARG A NH1 4147 N NH2 . ARG A 547 ? 2.0989 3.1275 1.4787 1.0669 -0.1305 -0.2786 547 ARG A NH2 4148 N N . TRP A 548 ? 2.3050 2.8583 1.8042 0.8213 -0.1875 -0.2679 548 TRP A N 4149 C CA . TRP A 548 ? 2.1888 2.6595 1.6948 0.7987 -0.2121 -0.2879 548 TRP A CA 4150 C C . TRP A 548 ? 1.8761 2.3074 1.4069 0.7548 -0.2031 -0.2631 548 TRP A C 4151 O O . TRP A 548 ? 1.7285 2.1013 1.2569 0.7406 -0.2234 -0.2772 548 TRP A O 4152 C CB . TRP A 548 ? 2.2707 2.7204 1.7897 0.7939 -0.2176 -0.2981 548 TRP A CB 4153 C CG . TRP A 548 ? 2.3838 2.7527 1.9038 0.7785 -0.2467 -0.3224 548 TRP A CG 4154 C CD1 . TRP A 548 ? 2.4607 2.7978 1.9590 0.8032 -0.2785 -0.3605 548 TRP A CD1 4155 C CD2 . TRP A 548 ? 2.4204 2.7311 1.9651 0.7354 -0.2474 -0.3093 548 TRP A CD2 4156 N NE1 . TRP A 548 ? 2.4694 2.7319 1.9788 0.7765 -0.2985 -0.3699 548 TRP A NE1 4157 C CE2 . TRP A 548 ? 2.4700 2.7170 2.0069 0.7352 -0.2793 -0.3389 548 TRP A CE2 4158 C CE3 . TRP A 548 ? 2.3522 2.6592 1.9252 0.6975 -0.2247 -0.2756 548 TRP A CE3 4159 C CZ2 . TRP A 548 ? 2.4473 2.6311 2.0035 0.6984 -0.2876 -0.3340 548 TRP A CZ2 4160 C CZ3 . TRP A 548 ? 2.2730 2.5170 1.8637 0.6627 -0.2337 -0.2734 548 TRP A CZ3 4161 C CH2 . TRP A 548 ? 2.3216 2.5066 1.9036 0.6633 -0.2640 -0.3016 548 TRP A CH2 4162 N N . LEU A 549 ? 1.7823 2.2468 1.3380 0.7335 -0.1731 -0.2260 549 LEU A N 4163 C CA . LEU A 549 ? 1.8471 2.2807 1.4274 0.6937 -0.1626 -0.2009 549 LEU A CA 4164 C C . LEU A 549 ? 1.8284 2.2554 1.3923 0.6971 -0.1693 -0.2019 549 LEU A C 4165 O O . LEU A 549 ? 1.6983 2.0867 1.2769 0.6671 -0.1692 -0.1907 549 LEU A O 4166 C CB . LEU A 549 ? 1.8959 2.3723 1.5058 0.6746 -0.1302 -0.1614 549 LEU A CB 4167 C CG . LEU A 549 ? 1.8246 2.2945 1.4600 0.6588 -0.1231 -0.1561 549 LEU A CG 4168 C CD1 . LEU A 549 ? 1.7735 2.2915 1.4387 0.6430 -0.0921 -0.1173 549 LEU A CD1 4169 C CD2 . LEU A 549 ? 1.6901 2.0860 1.3406 0.6274 -0.1377 -0.1654 549 LEU A CD2 4170 N N . ASN A 550 ? 1.9169 2.3833 1.4500 0.7352 -0.1757 -0.2165 550 ASN A N 4171 C CA . ASN A 550 ? 1.9395 2.4083 1.4537 0.7444 -0.1822 -0.2190 550 ASN A CA 4172 C C . ASN A 550 ? 1.7950 2.2095 1.2886 0.7544 -0.2175 -0.2576 550 ASN A C 4173 O O . ASN A 550 ? 1.5884 1.9640 1.0848 0.7360 -0.2269 -0.2579 550 ASN A O 4174 C CB . ASN A 550 ? 2.0814 2.6274 1.5727 0.7815 -0.1695 -0.2123 550 ASN A CB 4175 C CG . ASN A 550 ? 2.0973 2.7030 1.6096 0.7745 -0.1355 -0.1738 550 ASN A CG 4176 O OD1 . ASN A 550 ? 2.1696 2.7596 1.7132 0.7447 -0.1230 -0.1556 550 ASN A OD1 4177 N ND2 . ASN A 550 ? 1.9694 2.6455 1.4651 0.8026 -0.1211 -0.1609 550 ASN A ND2 4178 N N . LYS A 551 ? 1.8349 2.2479 1.3090 0.7840 -0.2375 -0.2899 551 LYS A N 4179 C CA . LYS A 551 ? 1.8811 2.2430 1.3367 0.7963 -0.2737 -0.3285 551 LYS A CA 4180 C C . LYS A 551 ? 2.0489 2.3381 1.5270 0.7552 -0.2846 -0.3261 551 LYS A C 4181 O O . LYS A 551 ? 2.0882 2.3419 1.5594 0.7510 -0.3039 -0.3394 551 LYS A O 4182 C CB . LYS A 551 ? 1.8024 2.1609 1.2443 0.8244 -0.2927 -0.3600 551 LYS A CB 4183 C CG . LYS A 551 ? 1.8253 2.2564 1.2416 0.8702 -0.2860 -0.3683 551 LYS A CG 4184 C CD . LYS A 551 ? 1.8271 2.2440 1.2224 0.9043 -0.3157 -0.4104 551 LYS A CD 4185 C CE . LYS A 551 ? 1.8115 2.3040 1.1776 0.9546 -0.3113 -0.4222 551 LYS A CE 4186 N NZ . LYS A 551 ? 1.6814 2.2109 1.0218 0.9796 -0.3127 -0.4258 551 LYS A NZ 4187 N N . ASN A 552 ? 2.0814 2.3522 1.5872 0.7255 -0.2715 -0.3084 552 ASN A N 4188 C CA . ASN A 552 ? 1.9413 2.1466 1.4696 0.6871 -0.2804 -0.3055 552 ASN A CA 4189 C C . ASN A 552 ? 1.9383 2.1467 1.4961 0.6498 -0.2530 -0.2682 552 ASN A C 4190 O O . ASN A 552 ? 1.9345 2.1136 1.5155 0.6226 -0.2486 -0.2590 552 ASN A O 4191 C CB . ASN A 552 ? 1.8193 1.9910 1.3544 0.6847 -0.2941 -0.3217 552 ASN A CB 4192 C CG . ASN A 552 ? 1.8246 1.9901 1.3328 0.7218 -0.3228 -0.3596 552 ASN A CG 4193 O OD1 . ASN A 552 ? 1.9281 2.0547 1.4247 0.7270 -0.3504 -0.3828 552 ASN A OD1 4194 N ND2 . ASN A 552 ? 1.7386 1.9425 1.2378 0.7482 -0.3174 -0.3667 552 ASN A ND2 4195 N N . SER A 553 ? 2.0115 2.2549 1.5684 0.6491 -0.2355 -0.2470 553 SER A N 4196 C CA . SER A 553 ? 2.0637 2.3082 1.6491 0.6147 -0.2114 -0.2126 553 SER A CA 4197 C C . SER A 553 ? 2.0283 2.2079 1.6323 0.5801 -0.2233 -0.2148 553 SER A C 4198 O O . SER A 553 ? 1.9464 2.1160 1.5771 0.5495 -0.2074 -0.1916 553 SER A O 4199 C CB . SER A 553 ? 2.1590 2.4387 1.7384 0.6190 -0.1976 -0.1935 553 SER A CB 4200 O OG . SER A 553 ? 2.1708 2.4444 1.7787 0.5850 -0.1778 -0.1623 553 SER A OG 4201 N N . GLN A 554 ? 2.0789 2.2162 1.6690 0.5860 -0.2522 -0.2429 554 GLN A N 4202 C CA . GLN A 554 ? 2.0480 2.1242 1.6539 0.5561 -0.2669 -0.2477 554 GLN A CA 4203 C C . GLN A 554 ? 2.0799 2.1369 1.7058 0.5380 -0.2619 -0.2424 554 GLN A C 4204 O O . GLN A 554 ? 2.0724 2.1084 1.7226 0.5059 -0.2518 -0.2244 554 GLN A O 4205 C CB . GLN A 554 ? 1.9966 2.0355 1.5837 0.5710 -0.3011 -0.2809 554 GLN A CB 4206 C CG . GLN A 554 ? 1.9392 1.9951 1.5027 0.6087 -0.3153 -0.3072 554 GLN A CG 4207 C CD . GLN A 554 ? 1.8606 1.8654 1.4146 0.6160 -0.3515 -0.3396 554 GLN A CD 4208 O OE1 . GLN A 554 ? 1.8045 1.7587 1.3744 0.5885 -0.3638 -0.3395 554 GLN A OE1 4209 N NE2 . GLN A 554 ? 1.7964 1.8152 1.3253 0.6535 -0.3692 -0.3672 554 GLN A NE2 4210 N N . LYS A 555 ? 2.0874 2.1526 1.7022 0.5604 -0.2700 -0.2596 555 LYS A N 4211 C CA . LYS A 555 ? 2.0709 2.1205 1.7012 0.5486 -0.2675 -0.2581 555 LYS A CA 4212 C C . LYS A 555 ? 2.0358 2.1282 1.6849 0.5395 -0.2362 -0.2300 555 LYS A C 4213 O O . LYS A 555 ? 2.1078 2.2371 1.7519 0.5597 -0.2282 -0.2316 555 LYS A O 4214 C CB . LYS A 555 ? 2.0809 2.1297 1.6916 0.5795 -0.2869 -0.2866 555 LYS A CB 4215 C CG . LYS A 555 ? 2.0173 2.0179 1.6127 0.5884 -0.3218 -0.3166 555 LYS A CG 4216 C CD . LYS A 555 ? 1.9189 1.9251 1.4932 0.6242 -0.3409 -0.3457 555 LYS A CD 4217 C CE . LYS A 555 ? 1.8537 1.7971 1.4250 0.6220 -0.3756 -0.3712 555 LYS A CE 4218 N NZ . LYS A 555 ? 1.8082 1.7159 1.3790 0.6092 -0.3929 -0.3764 555 LYS A NZ 4219 N N . GLU A 556 ? 1.9639 2.0520 1.6356 0.5095 -0.2194 -0.2047 556 GLU A N 4220 C CA . GLU A 556 ? 1.9743 2.1025 1.6664 0.5001 -0.1909 -0.1771 556 GLU A CA 4221 C C . GLU A 556 ? 2.1284 2.2526 1.8420 0.4711 -0.1752 -0.1512 556 GLU A C 4222 O O . GLU A 556 ? 2.1134 2.2432 1.8184 0.4734 -0.1752 -0.1469 556 GLU A O 4223 C CB . GLU A 556 ? 1.8338 2.0234 1.5105 0.5311 -0.1790 -0.1736 556 GLU A CB 4224 C CG . GLU A 556 ? 1.7464 1.9800 1.4406 0.5314 -0.1561 -0.1544 556 GLU A CG 4225 C CD . GLU A 556 ? 1.6874 1.9567 1.4010 0.5173 -0.1301 -0.1205 556 GLU A CD 4226 O OE1 . GLU A 556 ? 1.6633 1.9068 1.3897 0.4928 -0.1277 -0.1083 556 GLU A OE1 4227 O OE2 . GLU A 556 ? 1.6510 1.9749 1.3680 0.5309 -0.1123 -0.1054 556 GLU A OE2 4228 N N . GLN A 557 ? 2.1742 2.2885 1.9155 0.4449 -0.1630 -0.1350 557 GLN A N 4229 C CA . GLN A 557 ? 2.1443 2.2671 1.9092 0.4211 -0.1441 -0.1076 557 GLN A CA 4230 C C . GLN A 557 ? 1.9403 2.0993 1.7287 0.4153 -0.1217 -0.0860 557 GLN A C 4231 O O . GLN A 557 ? 1.7374 1.8956 1.5333 0.4156 -0.1221 -0.0916 557 GLN A O 4232 C CB . GLN A 557 ? 2.1627 2.2366 1.9419 0.3914 -0.1516 -0.1068 557 GLN A CB 4233 C CG . GLN A 557 ? 2.1972 2.2520 1.9641 0.3894 -0.1623 -0.1114 557 GLN A CG 4234 C CD . GLN A 557 ? 1.8283 1.9122 1.6013 0.3864 -0.1455 -0.0889 557 GLN A CD 4235 O OE1 . GLN A 557 ? 1.6235 1.7334 1.3773 0.4074 -0.1456 -0.0904 557 GLN A OE1 4236 N NE2 . GLN A 557 ? 1.6730 1.7522 1.4727 0.3612 -0.1319 -0.0685 557 GLN A NE2 4237 N N . GLY A 558 ? 1.9390 2.1298 1.7398 0.4103 -0.1031 -0.0609 558 GLY A N 4238 C CA . GLY A 558 ? 1.8958 2.1281 1.7193 0.4073 -0.0818 -0.0378 558 GLY A CA 4239 C C . GLY A 558 ? 1.9125 2.2005 1.7194 0.4368 -0.0731 -0.0330 558 GLY A C 4240 O O . GLY A 558 ? 1.9704 2.2665 1.7519 0.4626 -0.0845 -0.0546 558 GLY A O 4241 N N . SER A 559 ? 1.8432 2.1707 1.6644 0.4339 -0.0535 -0.0044 559 SER A N 4242 C CA . SER A 559 ? 1.7658 2.1522 1.5717 0.4618 -0.0432 0.0042 559 SER A CA 4243 C C . SER A 559 ? 1.6983 2.1312 1.5240 0.4655 -0.0264 0.0205 559 SER A C 4244 O O . SER A 559 ? 1.6311 2.0741 1.4909 0.4434 -0.0109 0.0465 559 SER A O 4245 C CB . SER A 559 ? 1.7259 2.1326 1.5301 0.4614 -0.0333 0.0261 559 SER A CB 4246 O OG . SER A 559 ? 1.6802 2.0681 1.5164 0.4300 -0.0238 0.0490 559 SER A OG 4247 N N . ALA A 560 ? 1.6870 2.1489 1.4922 0.4940 -0.0304 0.0043 560 ALA A N 4248 C CA . ALA A 560 ? 1.7169 2.2257 1.5384 0.5008 -0.0161 0.0162 560 ALA A CA 4249 C C . ALA A 560 ? 1.9544 2.5208 1.7955 0.4987 0.0082 0.0540 560 ALA A C 4250 O O . ALA A 560 ? 2.0017 2.6017 1.8239 0.5170 0.0131 0.0623 560 ALA A O 4251 C CB . ALA A 560 ? 1.5837 2.1158 1.3749 0.5361 -0.0261 -0.0098 560 ALA A CB 4252 N N . LYS A 561 ? 2.0969 2.6750 1.9770 0.4764 0.0225 0.0771 561 LYS A N 4253 C CA . LYS A 561 ? 2.1297 2.7594 2.0360 0.4696 0.0452 0.1163 561 LYS A CA 4254 C C . LYS A 561 ? 2.1837 2.8809 2.0923 0.4912 0.0579 0.1251 561 LYS A C 4255 O O . LYS A 561 ? 2.2054 2.9043 2.1282 0.4887 0.0571 0.1169 561 LYS A O 4256 C CB . LYS A 561 ? 2.0210 2.6247 1.9724 0.4319 0.0523 0.1373 561 LYS A CB 4257 C CG . LYS A 561 ? 1.8422 2.4794 1.8224 0.4182 0.0712 0.1785 561 LYS A CG 4258 C CD . LYS A 561 ? 1.6212 2.2298 1.6475 0.3824 0.0750 0.1947 561 LYS A CD 4259 C CE . LYS A 561 ? 1.4377 2.0519 1.4874 0.3648 0.0859 0.2286 561 LYS A CE 4260 N NZ . LYS A 561 ? 1.2384 1.8110 1.2659 0.3625 0.0755 0.2188 561 LYS A NZ 4261 N N . CYS A 562 ? 2.1978 2.9527 2.0923 0.5132 0.0696 0.1421 562 CYS A N 4262 C CA . CYS A 562 ? 2.1830 3.0102 2.0794 0.5353 0.0833 0.1533 562 CYS A CA 4263 C C . CYS A 562 ? 2.0728 2.9280 2.0194 0.5103 0.1020 0.1882 562 CYS A C 4264 O O . CYS A 562 ? 2.0314 2.8784 2.0071 0.4843 0.1113 0.2174 562 CYS A O 4265 C CB . CYS A 562 ? 2.2755 3.1608 2.1445 0.5649 0.0921 0.1654 562 CYS A CB 4266 S SG . CYS A 562 ? 2.3136 3.1879 2.1214 0.6059 0.0700 0.1207 562 CYS A SG 4267 N N . SER A 563 ? 2.0281 2.9164 1.9855 0.5188 0.1064 0.1846 563 SER A N 4268 C CA . SER A 563 ? 2.0090 2.9230 2.0160 0.4953 0.1218 0.2142 563 SER A CA 4269 C C . SER A 563 ? 2.0653 3.0421 2.0949 0.4923 0.1443 0.2600 563 SER A C 4270 O O . SER A 563 ? 2.1358 3.1840 2.1602 0.5155 0.1571 0.2730 563 SER A O 4271 C CB . SER A 563 ? 1.9859 2.9290 1.9960 0.5098 0.1215 0.1992 563 SER A CB 4272 O OG . SER A 563 ? 2.0085 3.0063 1.9833 0.5495 0.1234 0.1889 563 SER A OG 4273 N N . GLY A 564 ? 2.0169 2.9679 2.0718 0.4642 0.1486 0.2849 564 GLY A N 4274 C CA . GLY A 564 ? 1.9652 2.9686 2.0479 0.4561 0.1689 0.3318 564 GLY A CA 4275 C C . GLY A 564 ? 1.8707 2.8817 1.9279 0.4668 0.1717 0.3444 564 GLY A C 4276 O O . GLY A 564 ? 1.8370 2.8713 1.9200 0.4526 0.1853 0.3839 564 GLY A O 4277 N N . SER A 565 ? 1.7948 2.7859 1.8021 0.4919 0.1579 0.3112 565 SER A N 4278 C CA . SER A 565 ? 1.6737 2.6729 1.6522 0.5058 0.1586 0.3188 565 SER A CA 4279 C C . SER A 565 ? 1.7067 2.6288 1.6814 0.4850 0.1439 0.3054 565 SER A C 4280 O O . SER A 565 ? 1.6371 2.5563 1.6165 0.4760 0.1489 0.3284 565 SER A O 4281 C CB . SER A 565 ? 1.5239 2.5542 1.4497 0.5489 0.1517 0.2908 565 SER A CB 4282 O OG . SER A 565 ? 1.4512 2.5550 1.3787 0.5706 0.1648 0.3004 565 SER A OG 4283 N N . GLY A 566 ? 1.8017 2.6632 1.7685 0.4779 0.1257 0.2689 566 GLY A N 4284 C CA . GLY A 566 ? 1.8542 2.6439 1.8138 0.4609 0.1102 0.2519 566 GLY A CA 4285 C C . GLY A 566 ? 1.8837 2.6611 1.7928 0.4878 0.0961 0.2234 566 GLY A C 4286 O O . GLY A 566 ? 1.8772 2.5956 1.7738 0.4787 0.0803 0.2021 566 GLY A O 4287 N N . LYS A 567 ? 1.8598 2.6953 1.7407 0.5217 0.1015 0.2232 567 LYS A N 4288 C CA . LYS A 567 ? 1.7759 2.6087 1.6079 0.5522 0.0876 0.1952 567 LYS A CA 4289 C C . LYS A 567 ? 1.7692 2.5512 1.5798 0.5590 0.0647 0.1493 567 LYS A C 4290 O O . LYS A 567 ? 1.8106 2.5988 1.6287 0.5621 0.0636 0.1377 567 LYS A O 4291 C CB . LYS A 567 ? 1.6938 2.6072 1.5034 0.5888 0.0992 0.2046 567 LYS A CB 4292 C CG . LYS A 567 ? 1.6152 2.5372 1.3746 0.6236 0.0866 0.1803 567 LYS A CG 4293 C CD . LYS A 567 ? 1.5234 2.5331 1.2634 0.6599 0.1006 0.1938 567 LYS A CD 4294 C CE . LYS A 567 ? 1.3492 2.3750 1.0443 0.6914 0.0921 0.1806 567 LYS A CE 4295 N NZ . LYS A 567 ? 1.0887 2.2052 0.7689 0.7233 0.1096 0.2031 567 LYS A NZ 4296 N N . PRO A 568 ? 1.7147 2.4465 1.4999 0.5609 0.0458 0.1239 568 PRO A N 4297 C CA . PRO A 568 ? 1.7693 2.4512 1.5337 0.5675 0.0222 0.0812 568 PRO A CA 4298 C C . PRO A 568 ? 1.9343 2.6531 1.6690 0.6054 0.0157 0.0570 568 PRO A C 4299 O O . PRO A 568 ? 2.0186 2.7973 1.7348 0.6333 0.0247 0.0660 568 PRO A O 4300 C CB . PRO A 568 ? 1.6558 2.2950 1.3971 0.5675 0.0061 0.0655 568 PRO A CB 4301 C CG . PRO A 568 ? 1.5975 2.2428 1.3605 0.5463 0.0212 0.1009 568 PRO A CG 4302 C CD . PRO A 568 ? 1.6203 2.3367 1.3990 0.5538 0.0452 0.1355 568 PRO A CD 4303 N N . VAL A 569 ? 1.9571 2.6416 1.6871 0.6073 -0.0001 0.0268 569 VAL A N 4304 C CA . VAL A 569 ? 1.9576 2.6709 1.6604 0.6433 -0.0091 0.0004 569 VAL A CA 4305 C C . VAL A 569 ? 1.9534 2.6511 1.6131 0.6721 -0.0311 -0.0322 569 VAL A C 4306 O O . VAL A 569 ? 1.8776 2.6037 1.5094 0.7077 -0.0401 -0.0554 569 VAL A O 4307 C CB . VAL A 569 ? 2.2507 2.9318 1.9658 0.6349 -0.0188 -0.0194 569 VAL A CB 4308 C CG1 . VAL A 569 ? 2.2627 2.9686 1.9480 0.6737 -0.0309 -0.0497 569 VAL A CG1 4309 C CG2 . VAL A 569 ? 2.2343 2.9377 1.9916 0.6103 0.0024 0.0112 569 VAL A CG2 4310 N N . ARG A 570 ? 2.0204 2.6733 1.6758 0.6569 -0.0405 -0.0346 570 ARG A N 4311 C CA . ARG A 570 ? 2.0584 2.6957 1.6765 0.6809 -0.0615 -0.0627 570 ARG A CA 4312 C C . ARG A 570 ? 1.9792 2.6806 1.5776 0.7072 -0.0492 -0.0467 570 ARG A C 4313 O O . ARG A 570 ? 1.8654 2.5627 1.4336 0.7280 -0.0638 -0.0653 570 ARG A O 4314 C CB . ARG A 570 ? 2.0926 2.6598 1.7155 0.6537 -0.0760 -0.0702 570 ARG A CB 4315 C CG . ARG A 570 ? 2.1434 2.6478 1.7850 0.6273 -0.0883 -0.0846 570 ARG A CG 4316 C CD . ARG A 570 ? 2.1744 2.6129 1.8144 0.6071 -0.1066 -0.0978 570 ARG A CD 4317 N NE . ARG A 570 ? 2.1289 2.5568 1.7935 0.5761 -0.0922 -0.0685 570 ARG A NE 4318 C CZ . ARG A 570 ? 2.0642 2.4371 1.7376 0.5507 -0.1027 -0.0727 570 ARG A CZ 4319 N NH1 . ARG A 570 ? 2.0594 2.3832 1.7203 0.5511 -0.1273 -0.1031 570 ARG A NH1 4320 N NH2 . ARG A 570 ? 1.9846 2.3522 1.6803 0.5251 -0.0892 -0.0462 570 ARG A NH2 4321 N N . SER A 571 ? 2.0129 2.7747 1.6296 0.7062 -0.0226 -0.0117 571 SER A N 4322 C CA . SER A 571 ? 2.0299 2.8583 1.6328 0.7279 -0.0070 0.0112 571 SER A CA 4323 C C . SER A 571 ? 2.1598 3.0589 1.7385 0.7706 -0.0030 0.0025 571 SER A C 4324 O O . SER A 571 ? 2.0554 2.9475 1.6238 0.7866 -0.0159 -0.0267 571 SER A O 4325 C CB . SER A 571 ? 1.8349 2.6881 1.4749 0.6990 0.0202 0.0605 571 SER A CB 4326 O OG . SER A 571 ? 1.6237 2.4189 1.2812 0.6652 0.0163 0.0686 571 SER A OG 4327 N N . ILE A 572 ? 2.3761 3.3442 1.9461 0.7889 0.0150 0.0290 572 ILE A N 4328 C CA . ILE A 572 ? 2.6023 3.6469 2.1440 0.8340 0.0197 0.0227 572 ILE A CA 4329 C C . ILE A 572 ? 2.7193 3.7649 2.2477 0.8575 0.0055 -0.0131 572 ILE A C 4330 O O . ILE A 572 ? 2.6689 3.6966 2.2244 0.8377 0.0090 -0.0112 572 ILE A O 4331 C CB . ILE A 572 ? 1.7815 2.9088 1.3432 0.8342 0.0525 0.0720 572 ILE A CB 4332 C CG1 . ILE A 572 ? 1.7394 2.8778 1.3040 0.8230 0.0644 0.1050 572 ILE A CG1 4333 C CG2 . ILE A 572 ? 1.7693 2.9788 1.3038 0.8808 0.0579 0.0646 572 ILE A CG2 4334 C CD1 . ILE A 572 ? 1.5892 2.7608 1.1082 0.8624 0.0559 0.0906 572 ILE A CD1 4335 N N . ILE A 573 ? 2.8186 3.8854 2.3049 0.9009 -0.0114 -0.0466 573 ILE A N 4336 C CA . ILE A 573 ? 2.8206 3.8972 2.2891 0.9311 -0.0259 -0.0821 573 ILE A CA 4337 C C . ILE A 573 ? 2.8329 4.0103 2.2865 0.9703 -0.0082 -0.0700 573 ILE A C 4338 O O . ILE A 573 ? 2.8082 4.0446 2.2643 0.9733 0.0142 -0.0341 573 ILE A O 4339 C CB . ILE A 573 ? 2.7647 3.7866 2.1981 0.9528 -0.0621 -0.1339 573 ILE A CB 4340 C CG1 . ILE A 573 ? 2.6793 3.6992 2.0889 0.9624 -0.0689 -0.1350 573 ILE A CG1 4341 C CG2 . ILE A 573 ? 2.6960 3.6250 2.1488 0.9181 -0.0806 -0.1519 573 ILE A CG2 4342 C CD1 . ILE A 573 ? 2.6383 3.7486 2.0226 1.0012 -0.0543 -0.1214 573 ILE A CD1 4343 N N . CYS A 574 ? 2.8407 4.0393 2.2792 1.0006 -0.0182 -0.0989 574 CYS A N 4344 C CA . CYS A 574 ? 2.8039 4.1009 2.2348 1.0344 0.0010 -0.0851 574 CYS A CA 4345 C C . CYS A 574 ? 2.7549 4.0843 2.1394 1.0910 -0.0196 -0.1293 574 CYS A C 4346 O O . CYS A 574 ? 2.7179 3.9919 2.0878 1.1012 -0.0485 -0.1736 574 CYS A O 4347 C CB . CYS A 574 ? 2.8236 4.1357 2.2923 1.0136 0.0177 -0.0659 574 CYS A CB 4348 S SG . CYS A 574 ? 2.8355 4.0893 2.3600 0.9460 0.0332 -0.0262 574 CYS A SG 4349 N N . PRO A 575 ? 2.7747 4.1958 2.1367 1.1286 -0.0050 -0.1165 575 PRO A N 4350 C CA . PRO A 575 ? 2.7835 4.2518 2.0986 1.1877 -0.0214 -0.1543 575 PRO A CA 4351 C C . PRO A 575 ? 2.7253 4.2089 2.0339 1.2146 -0.0321 -0.1856 575 PRO A C 4352 O O . PRO A 575 ? 2.6429 4.1669 1.9136 1.2656 -0.0467 -0.2193 575 PRO A O 4353 C CB . PRO A 575 ? 2.7739 4.3479 2.0806 1.2098 0.0080 -0.1156 575 PRO A CB 4354 C CG . PRO A 575 ? 2.7590 4.3500 2.1151 1.1646 0.0408 -0.0593 575 PRO A CG 4355 C CD . PRO A 575 ? 2.7544 4.2405 2.1359 1.1146 0.0293 -0.0606 575 PRO A CD 4356 N N . GLU B 33 ? 1.1915 1.6294 1.2483 -0.0805 0.0427 0.0174 33 GLU B N 4357 C CA . GLU B 33 ? 1.2083 1.6665 1.2856 -0.0810 0.0353 0.0143 33 GLU B CA 4358 C C . GLU B 33 ? 1.3171 1.8053 1.4069 -0.0629 0.0384 0.0122 33 GLU B C 4359 O O . GLU B 33 ? 1.4219 1.9262 1.5270 -0.0586 0.0318 0.0099 33 GLU B O 4360 C CB . GLU B 33 ? 1.0949 1.5229 1.1648 -0.0789 0.0229 0.0086 33 GLU B CB 4361 C CG . GLU B 33 ? 1.0865 1.4893 1.1404 -0.0602 0.0208 0.0038 33 GLU B CG 4362 C CD . GLU B 33 ? 1.1982 1.5699 1.2442 -0.0598 0.0100 -0.0007 33 GLU B CD 4363 O OE1 . GLU B 33 ? 1.1911 1.5713 1.2487 -0.0631 0.0029 -0.0021 33 GLU B OE1 4364 O OE2 . GLU B 33 ? 1.1846 1.5246 1.2126 -0.0557 0.0087 -0.0030 33 GLU B OE2 4365 N N . SER B 34 ? 1.1844 1.6794 1.2665 -0.0516 0.0483 0.0130 34 SER B N 4366 C CA . SER B 34 ? 0.9886 1.5108 1.0813 -0.0327 0.0527 0.0102 34 SER B CA 4367 C C . SER B 34 ? 0.9706 1.4777 1.0633 -0.0159 0.0429 0.0034 34 SER B C 4368 O O . SER B 34 ? 0.9585 1.4871 1.0697 -0.0111 0.0382 0.0030 34 SER B O 4369 C CB . SER B 34 ? 0.8645 1.4341 0.9843 -0.0395 0.0573 0.0147 34 SER B CB 4370 O OG . SER B 34 ? 0.7547 1.3535 0.8841 -0.0217 0.0646 0.0130 34 SER B OG 4371 N N . MET B 35 ? 0.8959 1.3665 0.9681 -0.0070 0.0396 -0.0015 35 MET B N 4372 C CA . MET B 35 ? 0.6745 1.1249 0.7456 0.0067 0.0302 -0.0071 35 MET B CA 4373 C C . MET B 35 ? 0.7578 1.2016 0.8219 0.0284 0.0334 -0.0136 35 MET B C 4374 O O . MET B 35 ? 0.7838 1.2269 0.8352 0.0325 0.0415 -0.0153 35 MET B O 4375 C CB . MET B 35 ? 0.4295 0.8408 0.4857 -0.0019 0.0217 -0.0085 35 MET B CB 4376 C CG . MET B 35 ? 0.3397 0.7227 0.3892 0.0123 0.0141 -0.0144 35 MET B CG 4377 S SD . MET B 35 ? 1.0230 1.4057 1.0866 0.0124 0.0031 -0.0132 35 MET B SD 4378 C CE . MET B 35 ? 1.7466 2.1037 1.7990 -0.0072 -0.0028 -0.0121 35 MET B CE 4379 N N . VAL B 36 ? 0.6634 1.1023 0.7357 0.0423 0.0269 -0.0171 36 VAL B N 4380 C CA . VAL B 36 ? 0.6494 1.0743 0.7159 0.0626 0.0271 -0.0247 36 VAL B CA 4381 C C . VAL B 36 ? 0.7796 1.1736 0.8448 0.0668 0.0160 -0.0271 36 VAL B C 4382 O O . VAL B 36 ? 0.7750 1.1767 0.8545 0.0670 0.0102 -0.0233 36 VAL B O 4383 C CB . VAL B 36 ? 0.6149 1.0719 0.6991 0.0788 0.0320 -0.0258 36 VAL B CB 4384 C CG1 . VAL B 36 ? 0.3784 0.8165 0.4570 0.1006 0.0312 -0.0352 36 VAL B CG1 4385 C CG2 . VAL B 36 ? 0.6205 1.1138 0.7096 0.0741 0.0439 -0.0225 36 VAL B CG2 4386 N N . ASP B 37 ? 0.7987 1.1587 0.8467 0.0699 0.0131 -0.0329 37 ASP B N 4387 C CA . ASP B 37 ? 0.6812 1.0116 0.7284 0.0727 0.0034 -0.0349 37 ASP B CA 4388 C C . ASP B 37 ? 0.7658 1.0837 0.8152 0.0926 0.0019 -0.0424 37 ASP B C 4389 O O . ASP B 37 ? 0.8941 1.1974 0.9304 0.1000 0.0040 -0.0504 37 ASP B O 4390 C CB . ASP B 37 ? 0.6837 0.9841 0.7131 0.0616 -0.0002 -0.0364 37 ASP B CB 4391 C CG . ASP B 37 ? 0.8013 1.0730 0.8311 0.0631 -0.0095 -0.0380 37 ASP B CG 4392 O OD1 . ASP B 37 ? 0.7854 1.0352 0.8039 0.0530 -0.0134 -0.0383 37 ASP B OD1 4393 O OD2 . ASP B 37 ? 0.7766 1.0481 0.8185 0.0745 -0.0127 -0.0384 37 ASP B OD2 4394 N N . TYR B 38 ? 0.8113 1.1345 0.8772 0.1014 -0.0021 -0.0398 38 TYR B N 4395 C CA . TYR B 38 ? 0.7824 1.0918 0.8532 0.1202 -0.0042 -0.0462 38 TYR B CA 4396 C C . TYR B 38 ? 0.7280 1.0100 0.8034 0.1209 -0.0134 -0.0442 38 TYR B C 4397 O O . TYR B 38 ? 0.7756 1.0551 0.8640 0.1338 -0.0161 -0.0434 38 TYR B O 4398 C CB . TYR B 38 ? 0.7371 1.0765 0.8256 0.1339 -0.0001 -0.0445 38 TYR B CB 4399 C CG . TYR B 38 ? 0.7139 1.0748 0.7991 0.1421 0.0097 -0.0504 38 TYR B CG 4400 C CD1 . TYR B 38 ? 0.6480 0.9948 0.7136 0.1419 0.0136 -0.0587 38 TYR B CD1 4401 C CD2 . TYR B 38 ? 0.6276 1.0244 0.7293 0.1511 0.0152 -0.0477 38 TYR B CD2 4402 C CE1 . TYR B 38 ? 0.6664 1.0343 0.7275 0.1500 0.0234 -0.0638 38 TYR B CE1 4403 C CE2 . TYR B 38 ? 0.6061 1.0248 0.7055 0.1591 0.0252 -0.0530 38 TYR B CE2 4404 C CZ . TYR B 38 ? 0.7017 1.1058 0.7800 0.1586 0.0297 -0.0610 38 TYR B CZ 4405 O OH . TYR B 38 ? 0.7601 1.1875 0.8344 0.1672 0.0405 -0.0660 38 TYR B OH 4406 N N . SER B 39 ? 0.5231 0.7849 0.5885 0.1073 -0.0179 -0.0427 39 SER B N 4407 C CA . SER B 39 ? 0.6898 0.9263 0.7595 0.1076 -0.0256 -0.0406 39 SER B CA 4408 C C . SER B 39 ? 0.8161 1.0222 0.8814 0.1180 -0.0285 -0.0505 39 SER B C 4409 O O . SER B 39 ? 0.9741 1.1752 1.0274 0.1214 -0.0256 -0.0597 39 SER B O 4410 C CB . SER B 39 ? 0.6607 0.8884 0.7231 0.0901 -0.0291 -0.0359 39 SER B CB 4411 O OG . SER B 39 ? 0.6281 0.8492 0.6743 0.0814 -0.0267 -0.0407 39 SER B OG 4412 N N . ASN B 40 ? 0.7010 0.8877 0.7761 0.1229 -0.0343 -0.0485 40 ASN B N 4413 C CA . ASN B 40 ? 0.8865 1.0429 0.9609 0.1317 -0.0383 -0.0579 40 ASN B CA 4414 C C . ASN B 40 ? 0.9932 1.1516 1.0680 0.1482 -0.0350 -0.0686 40 ASN B C 4415 O O . ASN B 40 ? 1.0365 1.1706 1.1089 0.1556 -0.0383 -0.0792 40 ASN B O 4416 C CB . ASN B 40 ? 0.9022 1.0373 0.9616 0.1214 -0.0414 -0.0640 40 ASN B CB 4417 C CG . ASN B 40 ? 1.0529 1.1826 1.1126 0.1068 -0.0449 -0.0552 40 ASN B CG 4418 O OD1 . ASN B 40 ? 0.9669 1.0837 1.0374 0.1070 -0.0491 -0.0501 40 ASN B OD1 4419 N ND2 . ASN B 40 ? 1.1926 1.3321 1.2405 0.0942 -0.0428 -0.0531 40 ASN B ND2 4420 N N . ARG B 41 ? 0.9364 1.1248 1.0148 0.1540 -0.0285 -0.0665 41 ARG B N 4421 C CA . ARG B 41 ? 0.8759 1.0709 0.9560 0.1710 -0.0242 -0.0762 41 ARG B CA 4422 C C . ARG B 41 ? 1.0000 1.1856 1.0987 0.1871 -0.0274 -0.0758 41 ARG B C 4423 O O . ARG B 41 ? 1.0815 1.2779 1.1861 0.2030 -0.0235 -0.0818 41 ARG B O 4424 C CB . ARG B 41 ? 0.8618 1.0953 0.9406 0.1710 -0.0153 -0.0734 41 ARG B CB 4425 C CG . ARG B 41 ? 0.8890 1.1290 0.9475 0.1636 -0.0096 -0.0792 41 ARG B CG 4426 C CD . ARG B 41 ? 1.1596 1.4087 1.2117 0.1796 -0.0029 -0.0914 41 ARG B CD 4427 N NE . ARG B 41 ? 1.2181 1.5035 1.2830 0.1882 0.0049 -0.0877 41 ARG B NE 4428 C CZ . ARG B 41 ? 1.1415 1.4333 1.2167 0.2080 0.0074 -0.0946 41 ARG B CZ 4429 N NH1 . ARG B 41 ? 1.2316 1.4936 1.3050 0.2208 0.0024 -0.1064 41 ARG B NH1 4430 N NH2 . ARG B 41 ? 0.7275 1.0557 0.8157 0.2151 0.0147 -0.0904 41 ARG B NH2 4431 N N . ASN B 42 ? 0.9973 1.1632 1.1057 0.1834 -0.0341 -0.0682 42 ASN B N 4432 C CA . ASN B 42 ? 0.9090 1.0616 1.0354 0.1975 -0.0376 -0.0658 42 ASN B CA 4433 C C . ASN B 42 ? 0.8383 1.0192 0.9792 0.2101 -0.0339 -0.0587 42 ASN B C 4434 O O . ASN B 42 ? 0.6325 0.8040 0.7869 0.2264 -0.0353 -0.0602 42 ASN B O 4435 C CB . ASN B 42 ? 0.8795 1.0034 1.0048 0.2097 -0.0401 -0.0817 42 ASN B CB 4436 C CG . ASN B 42 ? 1.0919 1.1792 1.2220 0.2047 -0.0479 -0.0817 42 ASN B CG 4437 O OD1 . ASN B 42 ? 1.1681 1.2457 1.3139 0.2069 -0.0512 -0.0711 42 ASN B OD1 4438 N ND2 . ASN B 42 ? 1.1119 1.1796 1.2291 0.1980 -0.0509 -0.0931 42 ASN B ND2 4439 N N . LEU B 43 ? 0.8728 1.0880 1.0120 0.2024 -0.0296 -0.0511 43 LEU B N 4440 C CA . LEU B 43 ? 0.8579 1.1070 1.0095 0.2137 -0.0251 -0.0469 43 LEU B CA 4441 C C . LEU B 43 ? 0.9734 1.2259 1.1436 0.2222 -0.0294 -0.0341 43 LEU B C 4442 O O . LEU B 43 ? 1.1004 1.3318 1.2731 0.2167 -0.0354 -0.0260 43 LEU B O 4443 C CB . LEU B 43 ? 0.8277 1.1123 0.9732 0.2006 -0.0199 -0.0426 43 LEU B CB 4444 C CG . LEU B 43 ? 0.8570 1.1527 0.9893 0.2003 -0.0122 -0.0539 43 LEU B CG 4445 C CD1 . LEU B 43 ? 0.8857 1.1950 1.0058 0.1795 -0.0099 -0.0497 43 LEU B CD1 4446 C CD2 . LEU B 43 ? 0.9026 1.2300 1.0464 0.2162 -0.0054 -0.0564 43 LEU B CD2 4447 N N . THR B 44 ? 0.9492 1.2301 1.1326 0.2360 -0.0262 -0.0315 44 THR B N 4448 C CA . THR B 44 ? 0.9283 1.2138 1.1299 0.2475 -0.0305 -0.0192 44 THR B CA 4449 C C . THR B 44 ? 0.9757 1.3074 1.1882 0.2499 -0.0281 -0.0105 44 THR B C 4450 O O . THR B 44 ? 0.9912 1.3338 1.2138 0.2510 -0.0328 0.0034 44 THR B O 4451 C CB . THR B 44 ? 0.8301 1.0917 1.0426 0.2693 -0.0315 -0.0260 44 THR B CB 4452 O OG1 . THR B 44 ? 0.7602 0.9831 0.9750 0.2674 -0.0382 -0.0211 44 THR B OG1 4453 C CG2 . THR B 44 ? 0.7866 1.0747 1.0183 0.2879 -0.0306 -0.0193 44 THR B CG2 4454 N N . HIS B 45 ? 1.0450 1.4048 1.2552 0.2506 -0.0208 -0.0184 45 HIS B N 4455 C CA . HIS B 45 ? 1.0884 1.4953 1.3104 0.2518 -0.0178 -0.0119 45 HIS B CA 4456 C C . HIS B 45 ? 1.0394 1.4661 1.2487 0.2324 -0.0125 -0.0154 45 HIS B C 4457 O O . HIS B 45 ? 1.0330 1.4358 1.2249 0.2217 -0.0111 -0.0227 45 HIS B O 4458 C CB . HIS B 45 ? 1.2813 1.7052 1.5170 0.2748 -0.0126 -0.0187 45 HIS B CB 4459 C CG . HIS B 45 ? 1.5056 1.9173 1.7300 0.2804 -0.0054 -0.0355 45 HIS B CG 4460 N ND1 . HIS B 45 ? 1.5796 1.9481 1.7894 0.2785 -0.0075 -0.0449 45 HIS B ND1 4461 C CD2 . HIS B 45 ? 1.5323 1.9708 1.7574 0.2883 0.0040 -0.0448 45 HIS B CD2 4462 C CE1 . HIS B 45 ? 1.5623 1.9311 1.7628 0.2852 -0.0005 -0.0596 45 HIS B CE1 4463 N NE2 . HIS B 45 ? 1.5616 1.9725 1.7706 0.2914 0.0071 -0.0595 45 HIS B NE2 4464 N N . VAL B 46 ? 1.0305 1.5003 1.2492 0.2276 -0.0098 -0.0099 46 VAL B N 4465 C CA . VAL B 46 ? 1.0629 1.5520 1.2718 0.2085 -0.0043 -0.0122 46 VAL B CA 4466 C C . VAL B 46 ? 0.9564 1.4647 1.1648 0.2158 0.0065 -0.0221 46 VAL B C 4467 O O . VAL B 46 ? 1.0334 1.5800 1.2583 0.2247 0.0110 -0.0205 46 VAL B O 4468 C CB . VAL B 46 ? 1.1514 1.6775 1.3709 0.1961 -0.0072 -0.0017 46 VAL B CB 4469 C CG1 . VAL B 46 ? 1.1509 1.6863 1.3586 0.1730 -0.0033 -0.0034 46 VAL B CG1 4470 C CG2 . VAL B 46 ? 1.1325 1.6452 1.3541 0.1938 -0.0176 0.0085 46 VAL B CG2 4471 N N . PRO B 47 ? 0.7805 1.2643 0.9697 0.2120 0.0109 -0.0321 47 PRO B N 4472 C CA . PRO B 47 ? 0.5834 1.0786 0.7667 0.2201 0.0214 -0.0427 47 PRO B CA 4473 C C . PRO B 47 ? 0.5646 1.1112 0.7628 0.2208 0.0297 -0.0393 47 PRO B C 4474 O O . PRO B 47 ? 0.6413 1.2083 0.8368 0.2021 0.0330 -0.0343 47 PRO B O 4475 C CB . PRO B 47 ? 0.4050 0.8799 0.5646 0.2023 0.0233 -0.0465 47 PRO B CB 4476 C CG . PRO B 47 ? 0.5089 0.9450 0.6611 0.1951 0.0131 -0.0440 47 PRO B CG 4477 C CD . PRO B 47 ? 0.6694 1.1158 0.8399 0.1968 0.0057 -0.0328 47 PRO B CD 4478 N N . LYS B 48 ? 0.6325 1.1993 0.8473 0.2422 0.0330 -0.0420 48 LYS B N 4479 C CA . LYS B 48 ? 0.8248 1.4443 1.0587 0.2455 0.0404 -0.0384 48 LYS B CA 4480 C C . LYS B 48 ? 0.8070 1.4486 1.0314 0.2393 0.0538 -0.0441 48 LYS B C 4481 O O . LYS B 48 ? 0.5653 1.2530 0.8052 0.2386 0.0616 -0.0407 48 LYS B O 4482 C CB . LYS B 48 ? 0.9627 1.5956 1.2174 0.2726 0.0399 -0.0402 48 LYS B CB 4483 C CG . LYS B 48 ? 1.1588 1.7626 1.4052 0.2945 0.0430 -0.0542 48 LYS B CG 4484 C CD . LYS B 48 ? 0.9266 1.4734 1.1563 0.2926 0.0340 -0.0579 48 LYS B CD 4485 C CE . LYS B 48 ? 0.7493 1.2694 0.9607 0.3026 0.0391 -0.0745 48 LYS B CE 4486 N NZ . LYS B 48 ? 0.6128 1.0881 0.8019 0.2888 0.0332 -0.0779 48 LYS B NZ 4487 N N . ASP B 49 ? 0.8125 1.4215 1.0117 0.2344 0.0561 -0.0519 49 ASP B N 4488 C CA . ASP B 49 ? 0.6129 1.2349 0.7977 0.2304 0.0686 -0.0575 49 ASP B CA 4489 C C . ASP B 49 ? 0.6888 1.3187 0.8640 0.2028 0.0712 -0.0493 49 ASP B C 4490 O O . ASP B 49 ? 0.7424 1.3964 0.9126 0.1972 0.0827 -0.0492 49 ASP B O 4491 C CB . ASP B 49 ? 0.5402 1.1241 0.7019 0.2423 0.0695 -0.0713 49 ASP B CB 4492 C CG . ASP B 49 ? 1.1144 1.6494 1.2569 0.2297 0.0591 -0.0718 49 ASP B CG 4493 O OD1 . ASP B 49 ? 1.0946 1.6263 1.2296 0.2073 0.0568 -0.0636 49 ASP B OD1 4494 O OD2 . ASP B 49 ? 1.0149 1.5143 1.1502 0.2423 0.0532 -0.0811 49 ASP B OD2 4495 N N . LEU B 50 ? 0.5942 1.2034 0.7667 0.1861 0.0608 -0.0423 50 LEU B N 4496 C CA . LEU B 50 ? 0.5055 1.1154 0.6684 0.1602 0.0616 -0.0353 50 LEU B CA 4497 C C . LEU B 50 ? 0.6655 1.3223 0.8404 0.1496 0.0723 -0.0292 50 LEU B C 4498 O O . LEU B 50 ? 0.5626 1.2590 0.7609 0.1583 0.0759 -0.0270 50 LEU B O 4499 C CB . LEU B 50 ? 0.4577 1.0528 0.6251 0.1462 0.0491 -0.0279 50 LEU B CB 4500 C CG . LEU B 50 ? 0.5469 1.0931 0.7000 0.1483 0.0386 -0.0311 50 LEU B CG 4501 C CD1 . LEU B 50 ? 0.3468 0.8928 0.5145 0.1479 0.0278 -0.0242 50 LEU B CD1 4502 C CD2 . LEU B 50 ? 0.4350 0.9510 0.5649 0.1304 0.0373 -0.0317 50 LEU B CD2 4503 N N . PRO B 51 ? 0.6785 1.3309 0.8382 0.1307 0.0776 -0.0261 51 PRO B N 4504 C CA . PRO B 51 ? 0.6860 1.3777 0.8556 0.1155 0.0877 -0.0187 51 PRO B CA 4505 C C . PRO B 51 ? 0.6884 1.4079 0.8837 0.1036 0.0812 -0.0106 51 PRO B C 4506 O O . PRO B 51 ? 0.5253 1.2239 0.7186 0.0915 0.0699 -0.0076 51 PRO B O 4507 C CB . PRO B 51 ? 0.6365 1.3012 0.7818 0.0963 0.0893 -0.0161 51 PRO B CB 4508 C CG . PRO B 51 ? 0.5684 1.1890 0.6890 0.1087 0.0852 -0.0252 51 PRO B CG 4509 C CD . PRO B 51 ? 0.5250 1.1326 0.6564 0.1241 0.0744 -0.0298 51 PRO B CD 4510 N N . PRO B 52 ? 0.6565 1.4248 0.8763 0.1075 0.0881 -0.0077 52 PRO B N 4511 C CA . PRO B 52 ? 0.6344 1.4351 0.8816 0.1001 0.0813 -0.0014 52 PRO B CA 4512 C C . PRO B 52 ? 0.7634 1.5588 1.0102 0.0720 0.0749 0.0051 52 PRO B C 4513 O O . PRO B 52 ? 0.9654 1.7621 1.2228 0.0673 0.0629 0.0075 52 PRO B O 4514 C CB . PRO B 52 ? 0.5700 1.4251 0.8398 0.1051 0.0938 0.0006 52 PRO B CB 4515 C CG . PRO B 52 ? 0.5565 1.4046 0.8135 0.1269 0.1039 -0.0073 52 PRO B CG 4516 C CD . PRO B 52 ? 0.5949 1.3921 0.8181 0.1215 0.1028 -0.0110 52 PRO B CD 4517 N N . ARG B 53 ? 0.6487 1.4373 0.8827 0.0541 0.0825 0.0079 53 ARG B N 4518 C CA . ARG B 53 ? 0.5155 1.2999 0.7508 0.0271 0.0773 0.0135 53 ARG B CA 4519 C C . ARG B 53 ? 0.5153 1.2465 0.7253 0.0194 0.0680 0.0114 53 ARG B C 4520 O O . ARG B 53 ? 0.5013 1.2206 0.7053 -0.0024 0.0665 0.0150 53 ARG B O 4521 C CB . ARG B 53 ? 0.4886 1.2956 0.7272 0.0095 0.0904 0.0195 53 ARG B CB 4522 C CG . ARG B 53 ? 0.5524 1.4187 0.8236 0.0061 0.0975 0.0240 53 ARG B CG 4523 C CD . ARG B 53 ? 0.8196 1.6991 1.0985 -0.0230 0.1021 0.0317 53 ARG B CD 4524 N NE . ARG B 53 ? 1.0856 1.9247 1.3354 -0.0336 0.1067 0.0337 53 ARG B NE 4525 C CZ . ARG B 53 ? 1.0980 1.9194 1.3431 -0.0583 0.1039 0.0384 53 ARG B CZ 4526 N NH1 . ARG B 53 ? 1.1771 2.0171 1.4444 -0.0762 0.0962 0.0405 53 ARG B NH1 4527 N NH2 . ARG B 53 ? 0.8542 1.6387 1.0721 -0.0646 0.1081 0.0407 53 ARG B NH2 4528 N N . THR B 54 ? 0.5900 1.2897 0.7863 0.0371 0.0620 0.0056 54 THR B N 4529 C CA . THR B 54 ? 0.6237 1.2745 0.7979 0.0319 0.0530 0.0033 54 THR B CA 4530 C C . THR B 54 ? 0.7205 1.3707 0.9030 0.0158 0.0418 0.0065 54 THR B C 4531 O O . THR B 54 ? 0.8584 1.5395 1.0624 0.0172 0.0373 0.0087 54 THR B O 4532 C CB . THR B 54 ? 0.5583 1.1810 0.7236 0.0536 0.0468 -0.0029 54 THR B CB 4533 O OG1 . THR B 54 ? 0.6805 1.3106 0.8433 0.0727 0.0559 -0.0079 54 THR B OG1 4534 C CG2 . THR B 54 ? 0.5240 1.0977 0.6652 0.0483 0.0405 -0.0057 54 THR B CG2 4535 N N . LYS B 55 ? 0.7249 1.3404 0.8903 0.0017 0.0367 0.0064 55 LYS B N 4536 C CA . LYS B 55 ? 0.7457 1.3603 0.9173 -0.0145 0.0266 0.0082 55 LYS B CA 4537 C C . LYS B 55 ? 0.7504 1.3281 0.9086 -0.0106 0.0155 0.0053 55 LYS B C 4538 O O . LYS B 55 ? 0.9561 1.5418 1.1235 -0.0122 0.0063 0.0060 55 LYS B O 4539 C CB . LYS B 55 ? 0.6970 1.3124 0.8670 -0.0388 0.0302 0.0114 55 LYS B CB 4540 C CG . LYS B 55 ? 0.6589 1.3189 0.8491 -0.0455 0.0399 0.0159 55 LYS B CG 4541 C CD . LYS B 55 ? 0.6329 1.2945 0.8248 -0.0709 0.0434 0.0201 55 LYS B CD 4542 C CE . LYS B 55 ? 0.6803 1.3922 0.8985 -0.0784 0.0514 0.0248 55 LYS B CE 4543 N NZ . LYS B 55 ? 0.8348 1.5479 1.0552 -0.1029 0.0574 0.0303 55 LYS B NZ 4544 N N . ALA B 56 ? 0.6268 1.1660 0.7636 -0.0054 0.0163 0.0021 56 ALA B N 4545 C CA . ALA B 56 ? 0.6147 1.1200 0.7403 -0.0003 0.0069 -0.0005 56 ALA B CA 4546 C C . ALA B 56 ? 0.6834 1.1716 0.8026 0.0214 0.0078 -0.0043 56 ALA B C 4547 O O . ALA B 56 ? 0.7371 1.2090 0.8427 0.0261 0.0137 -0.0076 56 ALA B O 4548 C CB . ALA B 56 ? 0.5625 1.0339 0.6699 -0.0150 0.0046 -0.0017 56 ALA B CB 4549 N N . LEU B 57 ? 0.6567 1.1483 0.7855 0.0344 0.0017 -0.0037 57 LEU B N 4550 C CA . LEU B 57 ? 0.6803 1.1537 0.8055 0.0547 0.0015 -0.0073 57 LEU B CA 4551 C C . LEU B 57 ? 0.7178 1.1580 0.8355 0.0571 -0.0076 -0.0074 57 LEU B C 4552 O O . LEU B 57 ? 0.7906 1.2372 0.9155 0.0535 -0.0145 -0.0029 57 LEU B O 4553 C CB . LEU B 57 ? 0.6243 1.1291 0.7689 0.0713 0.0034 -0.0058 57 LEU B CB 4554 C CG . LEU B 57 ? 0.5875 1.0754 0.7338 0.0933 0.0012 -0.0086 57 LEU B CG 4555 C CD1 . LEU B 57 ? 0.6431 1.0985 0.7718 0.0995 0.0047 -0.0166 57 LEU B CD1 4556 C CD2 . LEU B 57 ? 0.3886 0.9108 0.5544 0.1095 0.0048 -0.0075 57 LEU B CD2 4557 N N . SER B 58 ? 0.7060 1.1121 0.8094 0.0630 -0.0076 -0.0126 58 SER B N 4558 C CA . SER B 58 ? 0.6570 1.0324 0.7556 0.0666 -0.0152 -0.0127 58 SER B CA 4559 C C . SER B 58 ? 0.6871 1.0496 0.7894 0.0866 -0.0154 -0.0162 58 SER B C 4560 O O . SER B 58 ? 0.7916 1.1445 0.8866 0.0943 -0.0108 -0.0233 58 SER B O 4561 C CB . SER B 58 ? 0.5741 0.9175 0.6547 0.0552 -0.0170 -0.0161 58 SER B CB 4562 O OG . SER B 58 ? 0.4958 0.8104 0.5734 0.0602 -0.0234 -0.0167 58 SER B OG 4563 N N . LEU B 59 ? 0.6265 0.9888 0.7399 0.0952 -0.0209 -0.0113 59 LEU B N 4564 C CA . LEU B 59 ? 0.6168 0.9620 0.7353 0.1135 -0.0223 -0.0138 59 LEU B CA 4565 C C . LEU B 59 ? 0.7268 1.0411 0.8418 0.1113 -0.0294 -0.0108 59 LEU B C 4566 O O . LEU B 59 ? 0.7716 1.0721 0.8944 0.1240 -0.0324 -0.0090 59 LEU B O 4567 C CB . LEU B 59 ? 0.3397 0.7128 0.4767 0.1277 -0.0217 -0.0090 59 LEU B CB 4568 C CG . LEU B 59 ? 0.4436 0.8484 0.5849 0.1301 -0.0136 -0.0126 59 LEU B CG 4569 C CD1 . LEU B 59 ? 0.4941 0.9380 0.6549 0.1363 -0.0137 -0.0057 59 LEU B CD1 4570 C CD2 . LEU B 59 ? 0.5343 0.9252 0.6711 0.1450 -0.0085 -0.0226 59 LEU B CD2 4571 N N . SER B 60 ? 0.7413 1.0449 0.8452 0.0951 -0.0315 -0.0102 60 SER B N 4572 C CA . SER B 60 ? 0.7256 1.0036 0.8257 0.0906 -0.0373 -0.0071 60 SER B CA 4573 C C . SER B 60 ? 0.7171 0.9638 0.8166 0.1014 -0.0387 -0.0124 60 SER B C 4574 O O . SER B 60 ? 0.9050 1.1456 1.0009 0.1085 -0.0354 -0.0210 60 SER B O 4575 C CB . SER B 60 ? 0.8171 1.0866 0.9037 0.0728 -0.0380 -0.0090 60 SER B CB 4576 O OG . SER B 60 ? 0.9195 1.1607 1.0011 0.0697 -0.0423 -0.0088 60 SER B OG 4577 N N . GLN B 61 ? 0.6056 0.8333 0.7089 0.1025 -0.0435 -0.0073 61 GLN B N 4578 C CA . GLN B 61 ? 0.6419 0.8378 0.7469 0.1105 -0.0457 -0.0120 61 GLN B CA 4579 C C . GLN B 61 ? 0.7489 0.9423 0.8622 0.1279 -0.0440 -0.0175 61 GLN B C 4580 O O . GLN B 61 ? 0.8562 1.0296 0.9645 0.1326 -0.0438 -0.0283 61 GLN B O 4581 C CB . GLN B 61 ? 0.7400 0.9134 0.8313 0.1011 -0.0465 -0.0207 61 GLN B CB 4582 C CG . GLN B 61 ? 1.0002 1.1505 1.0919 0.0945 -0.0510 -0.0172 61 GLN B CG 4583 C CD . GLN B 61 ? 1.1975 1.3575 1.2826 0.0799 -0.0516 -0.0115 61 GLN B CD 4584 O OE1 . GLN B 61 ? 1.2986 1.4793 1.3775 0.0729 -0.0491 -0.0116 61 GLN B OE1 4585 N NE2 . GLN B 61 ? 1.1287 1.2739 1.2155 0.0748 -0.0546 -0.0067 61 GLN B NE2 4586 N N . ASN B 62 ? 0.7272 0.9412 0.8530 0.1382 -0.0431 -0.0108 62 ASN B N 4587 C CA . ASN B 62 ? 0.7622 0.9732 0.8985 0.1567 -0.0419 -0.0150 62 ASN B CA 4588 C C . ASN B 62 ? 0.8268 1.0322 0.9788 0.1670 -0.0458 -0.0038 62 ASN B C 4589 O O . ASN B 62 ? 0.7588 0.9532 0.9115 0.1597 -0.0496 0.0056 62 ASN B O 4590 C CB . ASN B 62 ? 0.6958 0.9391 0.8338 0.1629 -0.0361 -0.0187 62 ASN B CB 4591 C CG . ASN B 62 ? 0.7788 1.0238 0.9013 0.1557 -0.0313 -0.0297 62 ASN B CG 4592 O OD1 . ASN B 62 ? 0.9021 1.1746 1.0211 0.1484 -0.0269 -0.0285 62 ASN B OD1 4593 N ND2 . ASN B 62 ? 0.7485 0.9642 0.8619 0.1574 -0.0325 -0.0400 62 ASN B ND2 4594 N N . SER B 63 ? 0.7328 0.9460 0.8970 0.1844 -0.0445 -0.0042 63 SER B N 4595 C CA . SER B 63 ? 0.7242 0.9309 0.9038 0.1961 -0.0481 0.0071 63 SER B CA 4596 C C . SER B 63 ? 0.7974 1.0391 0.9884 0.2075 -0.0467 0.0141 63 SER B C 4597 O O . SER B 63 ? 0.8836 1.1214 1.0888 0.2243 -0.0481 0.0187 63 SER B O 4598 C CB . SER B 63 ? 0.8791 1.0507 1.0661 0.2090 -0.0498 0.0000 63 SER B CB 4599 O OG . SER B 63 ? 0.9410 1.0812 1.1199 0.1985 -0.0522 -0.0062 63 SER B OG 4600 N N . ILE B 64 ? 0.7478 1.0237 0.9340 0.1984 -0.0441 0.0148 64 ILE B N 4601 C CA . ILE B 64 ? 0.7338 1.0478 0.9317 0.2060 -0.0438 0.0227 64 ILE B CA 4602 C C . ILE B 64 ? 0.7899 1.1059 0.9947 0.2073 -0.0498 0.0393 64 ILE B C 4603 O O . ILE B 64 ? 0.5810 0.8830 0.7771 0.1945 -0.0528 0.0449 64 ILE B O 4604 C CB . ILE B 64 ? 0.7425 1.0909 0.9340 0.1922 -0.0405 0.0203 64 ILE B CB 4605 C CG1 . ILE B 64 ? 0.8608 1.2084 1.0445 0.1915 -0.0336 0.0056 64 ILE B CG1 4606 C CG2 . ILE B 64 ? 0.6802 1.0702 0.8860 0.1989 -0.0413 0.0288 64 ILE B CG2 4607 C CD1 . ILE B 64 ? 0.9476 1.3183 1.1219 0.1739 -0.0300 0.0032 64 ILE B CD1 4608 N N . SER B 65 ? 0.9506 1.2847 1.1707 0.2235 -0.0515 0.0475 65 SER B N 4609 C CA . SER B 65 ? 0.8986 1.2325 1.1253 0.2282 -0.0574 0.0646 65 SER B CA 4610 C C . SER B 65 ? 0.9213 1.2999 1.1562 0.2317 -0.0601 0.0743 65 SER B C 4611 O O . SER B 65 ? 1.0777 1.4659 1.3106 0.2272 -0.0651 0.0875 65 SER B O 4612 C CB . SER B 65 ? 0.9441 1.2481 1.1827 0.2468 -0.0589 0.0686 65 SER B CB 4613 O OG . SER B 65 ? 1.0180 1.2796 1.2499 0.2411 -0.0584 0.0621 65 SER B OG 4614 N N . GLU B 66 ? 0.8445 1.2519 1.0887 0.2400 -0.0567 0.0676 66 GLU B N 4615 C CA . GLU B 66 ? 0.7679 1.2219 1.0216 0.2420 -0.0593 0.0748 66 GLU B CA 4616 C C . GLU B 66 ? 0.8150 1.2993 1.0678 0.2321 -0.0538 0.0631 66 GLU B C 4617 O O . GLU B 66 ? 0.9902 1.4626 1.2392 0.2325 -0.0471 0.0504 66 GLU B O 4618 C CB . GLU B 66 ? 0.7257 1.1910 0.9986 0.2665 -0.0615 0.0824 66 GLU B CB 4619 C CG . GLU B 66 ? 0.9874 1.4385 1.2689 0.2832 -0.0556 0.0709 66 GLU B CG 4620 C CD . GLU B 66 ? 1.2093 1.6756 1.5113 0.3082 -0.0577 0.0779 66 GLU B CD 4621 O OE1 . GLU B 66 ? 1.2052 1.6897 1.5141 0.3128 -0.0644 0.0934 66 GLU B OE1 4622 O OE2 . GLU B 66 ? 1.2954 1.7558 1.6062 0.3241 -0.0529 0.0678 66 GLU B OE2 4623 N N . LEU B 67 ? 0.6922 1.2153 0.9477 0.2226 -0.0567 0.0676 67 LEU B N 4624 C CA . LEU B 67 ? 0.7293 1.2826 0.9859 0.2112 -0.0515 0.0582 67 LEU B CA 4625 C C . LEU B 67 ? 0.8027 1.4055 1.0790 0.2201 -0.0534 0.0631 67 LEU B C 4626 O O . LEU B 67 ? 0.7476 1.3783 1.0262 0.2111 -0.0597 0.0697 67 LEU B O 4627 C CB . LEU B 67 ? 0.7053 1.2572 0.9461 0.1860 -0.0529 0.0563 67 LEU B CB 4628 C CG . LEU B 67 ? 0.6762 1.2567 0.9173 0.1703 -0.0481 0.0481 67 LEU B CG 4629 C CD1 . LEU B 67 ? 0.5048 1.0727 0.7426 0.1731 -0.0383 0.0369 67 LEU B CD1 4630 C CD2 . LEU B 67 ? 0.7336 1.3085 0.9598 0.1468 -0.0511 0.0472 67 LEU B CD2 4631 N N . ARG B 68 ? 0.8519 1.4659 1.1428 0.2386 -0.0485 0.0592 68 ARG B N 4632 C CA . ARG B 68 ? 0.8792 1.5417 1.1918 0.2498 -0.0497 0.0632 68 ARG B CA 4633 C C . ARG B 68 ? 0.7898 1.4899 1.1069 0.2351 -0.0438 0.0555 68 ARG B C 4634 O O . ARG B 68 ? 0.7829 1.4683 1.0873 0.2216 -0.0367 0.0460 68 ARG B O 4635 C CB . ARG B 68 ? 0.9975 1.6569 1.3249 0.2769 -0.0461 0.0615 68 ARG B CB 4636 C CG . ARG B 68 ? 1.2280 1.8563 1.5568 0.2938 -0.0527 0.0716 68 ARG B CG 4637 C CD . ARG B 68 ? 1.3842 2.0264 1.7131 0.2893 -0.0633 0.0872 68 ARG B CD 4638 N NE . ARG B 68 ? 1.5102 2.1334 1.8458 0.3094 -0.0692 0.0998 68 ARG B NE 4639 C CZ . ARG B 68 ? 1.5991 2.2087 1.9264 0.3062 -0.0770 0.1136 68 ARG B CZ 4640 N NH1 . ARG B 68 ? 1.5847 2.1974 1.8964 0.2841 -0.0800 0.1150 68 ARG B NH1 4641 N NH2 . ARG B 68 ? 1.6371 2.2291 1.9716 0.3254 -0.0814 0.1261 68 ARG B NH2 4642 N N . MET B 69 ? 0.6065 1.3558 0.9426 0.2375 -0.0469 0.0601 69 MET B N 4643 C CA . MET B 69 ? 0.6600 1.4485 1.0042 0.2227 -0.0414 0.0539 69 MET B CA 4644 C C . MET B 69 ? 0.8153 1.6020 1.1608 0.2278 -0.0282 0.0430 69 MET B C 4645 O O . MET B 69 ? 0.7828 1.5660 1.1177 0.2098 -0.0214 0.0361 69 MET B O 4646 C CB . MET B 69 ? 0.6412 1.4854 1.0097 0.2277 -0.0472 0.0604 69 MET B CB 4647 C CG . MET B 69 ? 0.5811 1.4671 0.9590 0.2069 -0.0441 0.0558 69 MET B CG 4648 S SD . MET B 69 ? 1.0765 2.0292 1.4842 0.2113 -0.0532 0.0630 69 MET B SD 4649 C CE . MET B 69 ? 0.7404 1.7128 1.1712 0.2436 -0.0462 0.0629 69 MET B CE 4650 N N . PRO B 70 ? 0.8687 1.6565 1.2261 0.2531 -0.0244 0.0414 70 PRO B N 4651 C CA . PRO B 70 ? 0.7231 1.5141 1.0815 0.2595 -0.0114 0.0302 70 PRO B CA 4652 C C . PRO B 70 ? 0.5801 1.3241 0.9124 0.2491 -0.0063 0.0218 70 PRO B C 4653 O O . PRO B 70 ? 0.5179 1.2632 0.8461 0.2507 0.0045 0.0123 70 PRO B O 4654 C CB . PRO B 70 ? 0.7217 1.5111 1.0944 0.2904 -0.0108 0.0299 70 PRO B CB 4655 C CG . PRO B 70 ? 0.7581 1.5607 1.1440 0.2991 -0.0229 0.0429 70 PRO B CG 4656 C CD . PRO B 70 ? 0.8690 1.6518 1.2377 0.2773 -0.0314 0.0493 70 PRO B CD 4657 N N . ASP B 71 ? 0.5587 1.2640 0.8739 0.2393 -0.0137 0.0254 71 ASP B N 4658 C CA . ASP B 71 ? 0.7761 1.4376 1.0671 0.2282 -0.0104 0.0180 71 ASP B CA 4659 C C . ASP B 71 ? 0.7209 1.3926 1.0012 0.2027 -0.0059 0.0149 71 ASP B C 4660 O O . ASP B 71 ? 0.7508 1.3983 1.0142 0.1962 0.0005 0.0069 71 ASP B O 4661 C CB . ASP B 71 ? 0.9531 1.5719 1.2313 0.2259 -0.0196 0.0234 71 ASP B CB 4662 C CG . ASP B 71 ? 0.9811 1.5723 1.2639 0.2494 -0.0219 0.0239 71 ASP B CG 4663 O OD1 . ASP B 71 ? 1.0047 1.6169 1.3048 0.2694 -0.0194 0.0232 71 ASP B OD1 4664 O OD2 . ASP B 71 ? 0.8918 1.4404 1.1622 0.2478 -0.0261 0.0250 71 ASP B OD2 4665 N N . ILE B 72 ? 0.6189 1.3249 0.9087 0.1883 -0.0098 0.0211 72 ILE B N 4666 C CA . ILE B 72 ? 0.5669 1.2826 0.8490 0.1630 -0.0064 0.0189 72 ILE B CA 4667 C C . ILE B 72 ? 0.5126 1.2831 0.8154 0.1551 -0.0031 0.0209 72 ILE B C 4668 O O . ILE B 72 ? 0.4624 1.2426 0.7616 0.1333 -0.0005 0.0199 72 ILE B O 4669 C CB . ILE B 72 ? 0.6341 1.3269 0.9016 0.1441 -0.0154 0.0227 72 ILE B CB 4670 C CG1 . ILE B 72 ? 0.5573 1.2619 0.8348 0.1507 -0.0269 0.0317 72 ILE B CG1 4671 C CG2 . ILE B 72 ? 0.3059 0.9451 0.5494 0.1417 -0.0151 0.0183 72 ILE B CG2 4672 C CD1 . ILE B 72 ? 0.5633 1.2592 0.8296 0.1312 -0.0350 0.0348 72 ILE B CD1 4673 N N . SER B 73 ? 0.4915 1.2974 0.8171 0.1727 -0.0034 0.0237 73 SER B N 4674 C CA . SER B 73 ? 0.5326 1.3946 0.8818 0.1673 -0.0001 0.0254 73 SER B CA 4675 C C . SER B 73 ? 0.6078 1.4821 0.9544 0.1522 0.0126 0.0202 73 SER B C 4676 O O . SER B 73 ? 0.5606 1.4647 0.9170 0.1325 0.0130 0.0222 73 SER B O 4677 C CB . SER B 73 ? 0.6293 1.5230 1.0020 0.1934 0.0017 0.0267 73 SER B CB 4678 O OG . SER B 73 ? 0.7227 1.6056 1.0991 0.2100 -0.0093 0.0330 73 SER B OG 4679 N N . PHE B 74 ? 0.7361 1.5876 1.0697 0.1619 0.0228 0.0137 74 PHE B N 4680 C CA . PHE B 74 ? 0.7438 1.6094 1.0747 0.1528 0.0368 0.0095 74 PHE B CA 4681 C C . PHE B 74 ? 0.8245 1.6697 1.1369 0.1252 0.0381 0.0097 74 PHE B C 4682 O O . PHE B 74 ? 0.9780 1.8453 1.2937 0.1116 0.0478 0.0100 74 PHE B O 4683 C CB . PHE B 74 ? 0.6638 1.5102 0.9839 0.1734 0.0465 0.0015 74 PHE B CB 4684 C CG . PHE B 74 ? 0.7000 1.4878 0.9930 0.1765 0.0422 -0.0030 74 PHE B CG 4685 C CD1 . PHE B 74 ? 0.6545 1.4141 0.9235 0.1646 0.0482 -0.0075 74 PHE B CD1 4686 C CD2 . PHE B 74 ? 0.7282 1.4897 1.0207 0.1910 0.0317 -0.0019 74 PHE B CD2 4687 C CE1 . PHE B 74 ? 0.7323 1.4405 0.9784 0.1671 0.0434 -0.0120 74 PHE B CE1 4688 C CE2 . PHE B 74 ? 0.7718 1.4812 1.0421 0.1927 0.0277 -0.0058 74 PHE B CE2 4689 C CZ . PHE B 74 ? 0.8048 1.4882 1.0524 0.1807 0.0333 -0.0115 74 PHE B CZ 4690 N N . LEU B 75 ? 0.6369 1.4402 0.9304 0.1173 0.0287 0.0101 75 LEU B N 4691 C CA . LEU B 75 ? 0.5764 1.3562 0.8516 0.0931 0.0291 0.0098 75 LEU B CA 4692 C C . LEU B 75 ? 0.5779 1.3853 0.8667 0.0714 0.0233 0.0147 75 LEU B C 4693 O O . LEU B 75 ? 0.6495 1.4362 0.9292 0.0592 0.0134 0.0159 75 LEU B O 4694 C CB . LEU B 75 ? 0.5523 1.2787 0.8037 0.0938 0.0214 0.0078 75 LEU B CB 4695 C CG . LEU B 75 ? 0.6478 1.3437 0.8860 0.1141 0.0255 0.0018 75 LEU B CG 4696 C CD1 . LEU B 75 ? 0.6371 1.2942 0.8655 0.1223 0.0150 0.0019 75 LEU B CD1 4697 C CD2 . LEU B 75 ? 0.7778 1.4532 0.9955 0.1060 0.0348 -0.0031 75 LEU B CD2 4698 N N . SER B 76 ? 0.5434 1.3981 0.8544 0.0664 0.0296 0.0168 76 SER B N 4699 C CA . SER B 76 ? 0.5382 1.4263 0.8677 0.0475 0.0234 0.0204 76 SER B CA 4700 C C . SER B 76 ? 0.6042 1.4705 0.9202 0.0201 0.0211 0.0203 76 SER B C 4701 O O . SER B 76 ? 0.8949 1.7782 1.2218 0.0040 0.0126 0.0216 76 SER B O 4702 C CB . SER B 76 ? 0.6039 1.5480 0.9615 0.0469 0.0325 0.0224 76 SER B CB 4703 O OG . SER B 76 ? 0.5986 1.5464 0.9531 0.0274 0.0435 0.0231 76 SER B OG 4704 N N . GLU B 77 ? 0.4975 1.3264 0.7899 0.0153 0.0281 0.0182 77 GLU B N 4705 C CA . GLU B 77 ? 0.5439 1.3520 0.8241 -0.0099 0.0277 0.0185 77 GLU B CA 4706 C C . GLU B 77 ? 0.5032 1.2624 0.7597 -0.0123 0.0180 0.0159 77 GLU B C 4707 O O . GLU B 77 ? 0.5089 1.2462 0.7538 -0.0315 0.0163 0.0154 77 GLU B O 4708 C CB . GLU B 77 ? 0.7969 1.5974 1.0664 -0.0153 0.0423 0.0193 77 GLU B CB 4709 C CG . GLU B 77 ? 0.9002 1.7170 1.1784 -0.0415 0.0470 0.0231 77 GLU B CG 4710 C CD . GLU B 77 ? 0.9519 1.8232 1.2578 -0.0421 0.0567 0.0268 77 GLU B CD 4711 O OE1 . GLU B 77 ? 1.1450 2.0226 1.4474 -0.0449 0.0708 0.0298 77 GLU B OE1 4712 O OE2 . GLU B 77 ? 0.7227 1.6317 1.0536 -0.0390 0.0504 0.0270 77 GLU B OE2 4713 N N . LEU B 78 ? 0.6285 1.3707 0.8786 0.0074 0.0121 0.0145 78 LEU B N 4714 C CA . LEU B 78 ? 0.7253 1.4213 0.9534 0.0084 0.0043 0.0125 78 LEU B CA 4715 C C . LEU B 78 ? 0.7564 1.4459 0.9820 -0.0110 -0.0057 0.0125 78 LEU B C 4716 O O . LEU B 78 ? 0.8769 1.5961 1.1187 -0.0144 -0.0131 0.0141 78 LEU B O 4717 C CB . LEU B 78 ? 0.6713 1.3593 0.9001 0.0318 -0.0013 0.0128 78 LEU B CB 4718 C CG . LEU B 78 ? 0.7037 1.3424 0.9101 0.0359 -0.0065 0.0108 78 LEU B CG 4719 C CD1 . LEU B 78 ? 0.8264 1.4349 1.0138 0.0313 0.0015 0.0068 78 LEU B CD1 4720 C CD2 . LEU B 78 ? 0.6662 1.2962 0.8750 0.0594 -0.0097 0.0118 78 LEU B CD2 4721 N N . ARG B 79 ? 0.6084 1.2601 0.8138 -0.0229 -0.0062 0.0101 79 ARG B N 4722 C CA . ARG B 79 ? 0.5987 1.2384 0.7987 -0.0394 -0.0155 0.0086 79 ARG B CA 4723 C C . ARG B 79 ? 0.5497 1.1520 0.7318 -0.0304 -0.0224 0.0071 79 ARG B C 4724 O O . ARG B 79 ? 0.7638 1.3655 0.9453 -0.0331 -0.0321 0.0069 79 ARG B O 4725 C CB . ARG B 79 ? 0.6902 1.3139 0.8816 -0.0607 -0.0113 0.0071 79 ARG B CB 4726 C CG . ARG B 79 ? 0.9286 1.5866 1.1380 -0.0751 -0.0045 0.0094 79 ARG B CG 4727 C CD . ARG B 79 ? 1.3059 1.9402 1.5046 -0.0964 -0.0014 0.0089 79 ARG B CD 4728 N NE . ARG B 79 ? 1.6230 2.2213 1.7996 -0.0911 0.0061 0.0096 79 ARG B NE 4729 C CZ . ARG B 79 ? 1.6228 2.1783 1.7777 -0.0897 0.0018 0.0067 79 ARG B CZ 4730 N NH1 . ARG B 79 ? 1.6308 2.1732 1.7822 -0.0930 -0.0091 0.0030 79 ARG B NH1 4731 N NH2 . ARG B 79 ? 1.4369 1.9644 1.5735 -0.0845 0.0084 0.0073 79 ARG B NH2 4732 N N . VAL B 80 ? 0.3476 0.9196 0.5151 -0.0196 -0.0173 0.0061 80 VAL B N 4733 C CA . VAL B 80 ? 0.4362 0.9703 0.5872 -0.0127 -0.0226 0.0047 80 VAL B CA 4734 C C . VAL B 80 ? 0.5336 1.0606 0.6852 0.0101 -0.0213 0.0056 80 VAL B C 4735 O O . VAL B 80 ? 0.4707 1.0014 0.6237 0.0195 -0.0134 0.0044 80 VAL B O 4736 C CB . VAL B 80 ? 0.4517 0.9490 0.5831 -0.0227 -0.0195 0.0013 80 VAL B CB 4737 C CG1 . VAL B 80 ? 0.2751 0.7345 0.3913 -0.0140 -0.0240 -0.0004 80 VAL B CG1 4738 C CG2 . VAL B 80 ? 0.4034 0.9029 0.5342 -0.0451 -0.0219 0.0002 80 VAL B CG2 4739 N N . LEU B 81 ? 0.5771 1.0945 0.7280 0.0190 -0.0289 0.0079 81 LEU B N 4740 C CA . LEU B 81 ? 0.5998 1.1045 0.7513 0.0398 -0.0286 0.0091 81 LEU B CA 4741 C C . LEU B 81 ? 0.5341 1.0031 0.6725 0.0409 -0.0346 0.0096 81 LEU B C 4742 O O . LEU B 81 ? 0.6006 1.0734 0.7395 0.0371 -0.0416 0.0134 81 LEU B O 4743 C CB . LEU B 81 ? 0.5650 1.1033 0.7357 0.0531 -0.0314 0.0144 81 LEU B CB 4744 C CG . LEU B 81 ? 0.5211 1.0463 0.6949 0.0749 -0.0331 0.0172 81 LEU B CG 4745 C CD1 . LEU B 81 ? 0.3996 0.9155 0.5732 0.0881 -0.0250 0.0121 81 LEU B CD1 4746 C CD2 . LEU B 81 ? 0.5234 1.0820 0.7150 0.0850 -0.0385 0.0244 81 LEU B CD2 4747 N N . ARG B 82 ? 0.5332 0.9687 0.6594 0.0456 -0.0316 0.0057 82 ARG B N 4748 C CA . ARG B 82 ? 0.6229 1.0249 0.7384 0.0463 -0.0365 0.0060 82 ARG B CA 4749 C C . ARG B 82 ? 0.7445 1.1340 0.8653 0.0656 -0.0372 0.0079 82 ARG B C 4750 O O . ARG B 82 ? 0.7680 1.1496 0.8888 0.0756 -0.0325 0.0034 82 ARG B O 4751 C CB . ARG B 82 ? 0.5162 0.8882 0.6151 0.0359 -0.0344 0.0001 82 ARG B CB 4752 C CG . ARG B 82 ? 0.7315 1.1148 0.8265 0.0175 -0.0326 -0.0018 82 ARG B CG 4753 C CD . ARG B 82 ? 0.9590 1.3111 1.0374 0.0060 -0.0331 -0.0058 82 ARG B CD 4754 N NE . ARG B 82 ? 1.1821 1.5160 1.2507 0.0093 -0.0277 -0.0101 82 ARG B NE 4755 C CZ . ARG B 82 ? 1.3473 1.6522 1.4074 0.0178 -0.0287 -0.0133 82 ARG B CZ 4756 N NH1 . ARG B 82 ? 1.4666 1.7564 1.5282 0.0231 -0.0343 -0.0120 82 ARG B NH1 4757 N NH2 . ARG B 82 ? 1.1990 1.4907 1.2492 0.0206 -0.0243 -0.0178 82 ARG B NH2 4758 N N . LEU B 83 ? 0.7776 1.1657 0.9028 0.0709 -0.0431 0.0148 83 LEU B N 4759 C CA . LEU B 83 ? 0.7154 1.0926 0.8482 0.0889 -0.0443 0.0185 83 LEU B CA 4760 C C . LEU B 83 ? 0.7223 1.0700 0.8485 0.0881 -0.0487 0.0224 83 LEU B C 4761 O O . LEU B 83 ? 0.6784 1.0158 0.8114 0.1007 -0.0509 0.0283 83 LEU B O 4762 C CB . LEU B 83 ? 0.6874 1.0974 0.8360 0.0992 -0.0465 0.0261 83 LEU B CB 4763 C CG . LEU B 83 ? 0.6720 1.1032 0.8321 0.1105 -0.0411 0.0226 83 LEU B CG 4764 C CD1 . LEU B 83 ? 0.5527 1.0256 0.7287 0.1152 -0.0436 0.0293 83 LEU B CD1 4765 C CD2 . LEU B 83 ? 0.6878 1.0939 0.8506 0.1285 -0.0395 0.0205 83 LEU B CD2 4766 N N . SER B 84 ? 0.6909 1.0254 0.8045 0.0730 -0.0497 0.0195 84 SER B N 4767 C CA . SER B 84 ? 0.7626 1.0686 0.8694 0.0708 -0.0526 0.0217 84 SER B CA 4768 C C . SER B 84 ? 0.7410 1.0199 0.8517 0.0837 -0.0518 0.0208 84 SER B C 4769 O O . SER B 84 ? 0.8148 1.0892 0.9275 0.0911 -0.0485 0.0142 84 SER B O 4770 C CB . SER B 84 ? 0.9534 1.2446 1.0464 0.0552 -0.0520 0.0149 84 SER B CB 4771 O OG . SER B 84 ? 1.1813 1.4819 1.2709 0.0492 -0.0480 0.0079 84 SER B OG 4772 N N . HIS B 85 ? 0.7000 0.9616 0.8122 0.0863 -0.0548 0.0275 85 HIS B N 4773 C CA . HIS B 85 ? 0.5754 0.8098 0.6940 0.0975 -0.0550 0.0279 85 HIS B CA 4774 C C . HIS B 85 ? 0.6021 0.8409 0.7325 0.1141 -0.0537 0.0275 85 HIS B C 4775 O O . HIS B 85 ? 0.5968 0.8189 0.7274 0.1200 -0.0518 0.0183 85 HIS B O 4776 C CB . HIS B 85 ? 0.4353 0.6407 0.5454 0.0917 -0.0541 0.0177 85 HIS B CB 4777 C CG . HIS B 85 ? 0.5940 0.7887 0.6954 0.0785 -0.0558 0.0190 85 HIS B CG 4778 N ND1 . HIS B 85 ? 0.7703 0.9454 0.8752 0.0788 -0.0576 0.0248 85 HIS B ND1 4779 C CD2 . HIS B 85 ? 0.6079 0.8091 0.6981 0.0649 -0.0555 0.0152 85 HIS B CD2 4780 C CE1 . HIS B 85 ? 0.8317 1.0031 0.9276 0.0666 -0.0581 0.0240 85 HIS B CE1 4781 N NE2 . HIS B 85 ? 0.7660 0.9520 0.8527 0.0583 -0.0572 0.0179 85 HIS B NE2 4782 N N . ASN B 86 ? 0.6992 0.9607 0.8394 0.1224 -0.0552 0.0372 86 ASN B N 4783 C CA . ASN B 86 ? 0.7128 0.9744 0.8665 0.1406 -0.0547 0.0390 86 ASN B CA 4784 C C . ASN B 86 ? 0.7510 1.0081 0.9144 0.1499 -0.0584 0.0536 86 ASN B C 4785 O O . ASN B 86 ? 0.7996 1.0410 0.9592 0.1434 -0.0603 0.0605 86 ASN B O 4786 C CB . ASN B 86 ? 0.7328 1.0279 0.8920 0.1462 -0.0522 0.0360 86 ASN B CB 4787 C CG . ASN B 86 ? 0.7456 1.0381 0.8988 0.1444 -0.0471 0.0219 86 ASN B CG 4788 O OD1 . ASN B 86 ? 0.8170 1.1084 0.9579 0.1298 -0.0455 0.0161 86 ASN B OD1 4789 N ND2 . ASN B 86 ? 0.6462 0.9376 0.8075 0.1598 -0.0444 0.0165 86 ASN B ND2 4790 N N . ARG B 87 ? 0.8371 1.1086 1.0134 0.1655 -0.0589 0.0588 87 ARG B N 4791 C CA . ARG B 87 ? 1.0351 1.2971 1.2218 0.1773 -0.0621 0.0730 87 ARG B CA 4792 C C . ARG B 87 ? 0.8625 1.1597 1.0580 0.1872 -0.0646 0.0837 87 ARG B C 4793 O O . ARG B 87 ? 0.7602 1.0534 0.9675 0.2024 -0.0668 0.0945 87 ARG B O 4794 C CB . ARG B 87 ? 1.3665 1.5968 1.5633 0.1911 -0.0612 0.0682 87 ARG B CB 4795 C CG . ARG B 87 ? 1.5243 1.7247 1.7135 0.1835 -0.0590 0.0530 87 ARG B CG 4796 C CD . ARG B 87 ? 1.6595 1.8277 1.8471 0.1756 -0.0610 0.0580 87 ARG B CD 4797 N NE . ARG B 87 ? 1.7846 1.9257 1.9666 0.1694 -0.0602 0.0432 87 ARG B NE 4798 C CZ . ARG B 87 ? 1.8857 2.0021 2.0750 0.1794 -0.0605 0.0335 87 ARG B CZ 4799 N NH1 . ARG B 87 ? 1.9319 2.0452 2.1351 0.1965 -0.0610 0.0370 87 ARG B NH1 4800 N NH2 . ARG B 87 ? 1.8637 1.9581 2.0464 0.1728 -0.0607 0.0198 87 ARG B NH2 4801 N N . ILE B 88 ? 0.7284 1.0599 0.9191 0.1785 -0.0646 0.0808 88 ILE B N 4802 C CA . ILE B 88 ? 0.7564 1.1263 0.9557 0.1859 -0.0678 0.0895 88 ILE B CA 4803 C C . ILE B 88 ? 0.8676 1.2428 1.0646 0.1860 -0.0732 0.1063 88 ILE B C 4804 O O . ILE B 88 ? 0.8140 1.1831 0.9978 0.1717 -0.0743 0.1081 88 ILE B O 4805 C CB . ILE B 88 ? 0.6412 1.0456 0.8363 0.1735 -0.0669 0.0815 88 ILE B CB 4806 C CG1 . ILE B 88 ? 0.6760 1.0756 0.8707 0.1718 -0.0605 0.0661 88 ILE B CG1 4807 C CG2 . ILE B 88 ? 0.5773 1.0239 0.7840 0.1816 -0.0707 0.0891 88 ILE B CG2 4808 C CD1 . ILE B 88 ? 0.8179 1.2457 1.0076 0.1566 -0.0586 0.0587 88 ILE B CD1 4809 N N . ARG B 89 ? 0.9180 1.3054 1.1271 0.2028 -0.0766 0.1186 89 ARG B N 4810 C CA . ARG B 89 ? 0.9633 1.3567 1.1698 0.2054 -0.0818 0.1366 89 ARG B CA 4811 C C . ARG B 89 ? 0.8612 1.3010 1.0670 0.2035 -0.0871 0.1414 89 ARG B C 4812 O O . ARG B 89 ? 0.7763 1.2269 0.9701 0.1934 -0.0906 0.1475 89 ARG B O 4813 C CB . ARG B 89 ? 1.0232 1.3965 1.2423 0.2249 -0.0830 0.1501 89 ARG B CB 4814 C CG . ARG B 89 ? 1.1455 1.4713 1.3628 0.2225 -0.0797 0.1501 89 ARG B CG 4815 C CD . ARG B 89 ? 1.2833 1.5854 1.5144 0.2407 -0.0808 0.1634 89 ARG B CD 4816 N NE . ARG B 89 ? 1.4288 1.6858 1.6602 0.2363 -0.0776 0.1606 89 ARG B NE 4817 C CZ . ARG B 89 ? 1.4585 1.6874 1.6999 0.2442 -0.0753 0.1498 89 ARG B CZ 4818 N NH1 . ARG B 89 ? 1.4585 1.6997 1.7100 0.2581 -0.0750 0.1411 89 ARG B NH1 4819 N NH2 . ARG B 89 ? 1.4024 1.5921 1.6445 0.2385 -0.0735 0.1472 89 ARG B NH2 4820 N N . SER B 90 ? 0.8407 1.3092 1.0598 0.2131 -0.0878 0.1376 90 SER B N 4821 C CA . SER B 90 ? 0.7254 1.2407 0.9465 0.2100 -0.0931 0.1394 90 SER B CA 4822 C C . SER B 90 ? 0.8489 1.3845 1.0712 0.1974 -0.0896 0.1225 90 SER B C 4823 O O . SER B 90 ? 0.8135 1.3344 1.0402 0.1990 -0.0830 0.1115 90 SER B O 4824 C CB . SER B 90 ? 0.7010 1.2400 0.9392 0.2315 -0.0976 0.1508 90 SER B CB 4825 O OG . SER B 90 ? 0.8860 1.4675 1.1236 0.2290 -0.1052 0.1572 90 SER B OG 4826 N N . LEU B 91 ? 0.8889 1.4581 1.1070 0.1847 -0.0939 0.1204 91 LEU B N 4827 C CA . LEU B 91 ? 0.7980 1.3902 1.0197 0.1722 -0.0909 0.1064 91 LEU B CA 4828 C C . LEU B 91 ? 0.6770 1.3206 0.9099 0.1725 -0.0976 0.1090 91 LEU B C 4829 O O . LEU B 91 ? 0.6348 1.2954 0.8596 0.1636 -0.1046 0.1127 91 LEU B O 4830 C CB . LEU B 91 ? 0.7630 1.3383 0.9671 0.1497 -0.0886 0.0967 91 LEU B CB 4831 C CG . LEU B 91 ? 0.7039 1.2801 0.9095 0.1385 -0.0816 0.0820 91 LEU B CG 4832 C CD1 . LEU B 91 ? 0.7060 1.2883 0.8995 0.1156 -0.0830 0.0743 91 LEU B CD1 4833 C CD2 . LEU B 91 ? 0.6301 1.2423 0.8555 0.1478 -0.0800 0.0799 91 LEU B CD2 4834 N N . ASP B 92 ? 0.4964 1.1656 0.7483 0.1828 -0.0954 0.1062 92 ASP B N 4835 C CA . ASP B 92 ? 0.5343 1.2553 0.8007 0.1833 -0.1015 0.1076 92 ASP B CA 4836 C C . ASP B 92 ? 0.6079 1.3503 0.8766 0.1630 -0.0981 0.0940 92 ASP B C 4837 O O . ASP B 92 ? 0.6595 1.4014 0.9363 0.1632 -0.0896 0.0857 92 ASP B O 4838 C CB . ASP B 92 ? 0.3416 1.0815 0.6298 0.2072 -0.1010 0.1132 92 ASP B CB 4839 C CG . ASP B 92 ? 0.7210 1.5171 1.0267 0.2107 -0.1087 0.1168 92 ASP B CG 4840 O OD1 . ASP B 92 ? 0.6584 1.4802 0.9607 0.1926 -0.1136 0.1122 92 ASP B OD1 4841 O OD2 . ASP B 92 ? 0.5285 1.3431 0.8521 0.2319 -0.1103 0.1236 92 ASP B OD2 4842 N N . PHE B 93 ? 0.5951 1.3557 0.8564 0.1456 -0.1046 0.0918 93 PHE B N 4843 C CA . PHE B 93 ? 0.5449 1.3228 0.8084 0.1244 -0.1020 0.0795 93 PHE B CA 4844 C C . PHE B 93 ? 0.5951 1.4188 0.8836 0.1268 -0.1006 0.0764 93 PHE B C 4845 O O . PHE B 93 ? 0.6420 1.4810 0.9353 0.1094 -0.0973 0.0672 93 PHE B O 4846 C CB . PHE B 93 ? 0.4956 1.2832 0.7469 0.1059 -0.1105 0.0770 93 PHE B CB 4847 C CG . PHE B 93 ? 0.5109 1.2549 0.7379 0.0957 -0.1087 0.0747 93 PHE B CG 4848 C CD1 . PHE B 93 ? 0.5760 1.3132 0.7880 0.0964 -0.1162 0.0813 93 PHE B CD1 4849 C CD2 . PHE B 93 ? 0.5248 1.2360 0.7436 0.0860 -0.0994 0.0662 93 PHE B CD2 4850 C CE1 . PHE B 93 ? 0.5768 1.2758 0.7676 0.0874 -0.1139 0.0791 93 PHE B CE1 4851 C CE2 . PHE B 93 ? 0.5944 1.2669 0.7922 0.0773 -0.0981 0.0640 93 PHE B CE2 4852 C CZ . PHE B 93 ? 0.5183 1.1852 0.7030 0.0780 -0.1050 0.0703 93 PHE B CZ 4853 N N . HIS B 94 ? 0.6621 1.5086 0.9676 0.1481 -0.1031 0.0844 94 HIS B N 4854 C CA . HIS B 94 ? 0.7034 1.5954 1.0347 0.1522 -0.1010 0.0816 94 HIS B CA 4855 C C . HIS B 94 ? 0.7198 1.5946 1.0559 0.1583 -0.0874 0.0754 94 HIS B C 4856 O O . HIS B 94 ? 0.8026 1.7058 1.1546 0.1539 -0.0810 0.0692 94 HIS B O 4857 C CB . HIS B 94 ? 0.7368 1.6625 1.0854 0.1738 -0.1095 0.0925 94 HIS B CB 4858 C CG . HIS B 94 ? 0.9418 1.9196 1.3192 0.1779 -0.1085 0.0898 94 HIS B CG 4859 N ND1 . HIS B 94 ? 1.0377 2.0588 1.4268 0.1605 -0.1139 0.0848 94 HIS B ND1 4860 C CD2 . HIS B 94 ? 1.0005 1.9951 1.3984 0.1975 -0.1024 0.0909 94 HIS B CD2 4861 C CE1 . HIS B 94 ? 1.0150 2.0788 1.4317 0.1685 -0.1110 0.0838 94 HIS B CE1 4862 N NE2 . HIS B 94 ? 1.0040 2.0531 1.4260 0.1915 -0.1038 0.0874 94 HIS B NE2 4863 N N . VAL B 95 ? 0.6309 1.4591 0.9526 0.1684 -0.0830 0.0770 95 VAL B N 4864 C CA . VAL B 95 ? 0.6503 1.4541 0.9705 0.1736 -0.0709 0.0697 95 VAL B CA 4865 C C . VAL B 95 ? 0.6023 1.4136 0.9208 0.1527 -0.0627 0.0589 95 VAL B C 4866 O O . VAL B 95 ? 0.4906 1.3087 0.8173 0.1578 -0.0528 0.0534 95 VAL B O 4867 C CB . VAL B 95 ? 0.6558 1.4033 0.9557 0.1788 -0.0696 0.0713 95 VAL B CB 4868 C CG1 . VAL B 95 ? 0.5806 1.2962 0.8660 0.1666 -0.0600 0.0605 95 VAL B CG1 4869 C CG2 . VAL B 95 ? 0.5572 1.2937 0.8662 0.2061 -0.0701 0.0784 95 VAL B CG2 4870 N N . PHE B 96 ? 0.6246 1.4353 0.9323 0.1297 -0.0668 0.0563 96 PHE B N 4871 C CA . PHE B 96 ? 0.5610 1.3771 0.8671 0.1083 -0.0599 0.0476 96 PHE B CA 4872 C C . PHE B 96 ? 0.6045 1.4754 0.9342 0.1000 -0.0604 0.0462 96 PHE B C 4873 O O . PHE B 96 ? 0.4761 1.3556 0.8056 0.0779 -0.0582 0.0408 96 PHE B O 4874 C CB . PHE B 96 ? 0.3991 1.1877 0.6840 0.0869 -0.0639 0.0445 96 PHE B CB 4875 C CG . PHE B 96 ? 0.4770 1.2139 0.7397 0.0917 -0.0632 0.0452 96 PHE B CG 4876 C CD1 . PHE B 96 ? 0.6152 1.3369 0.8668 0.0937 -0.0721 0.0509 96 PHE B CD1 4877 C CD2 . PHE B 96 ? 0.6681 1.3728 0.9211 0.0940 -0.0536 0.0401 96 PHE B CD2 4878 C CE1 . PHE B 96 ? 0.7200 1.3959 0.9534 0.0971 -0.0710 0.0520 96 PHE B CE1 4879 C CE2 . PHE B 96 ? 0.8158 1.4743 1.0504 0.0978 -0.0535 0.0403 96 PHE B CE2 4880 C CZ . PHE B 96 ? 0.8297 1.4740 1.0556 0.0990 -0.0620 0.0465 96 PHE B CZ 4881 N N . LEU B 97 ? 0.6367 1.5446 0.9882 0.1173 -0.0633 0.0513 97 LEU B N 4882 C CA . LEU B 97 ? 0.6102 1.5739 0.9866 0.1096 -0.0658 0.0507 97 LEU B CA 4883 C C . LEU B 97 ? 0.6682 1.6458 1.0524 0.0933 -0.0541 0.0436 97 LEU B C 4884 O O . LEU B 97 ? 0.6491 1.6566 1.0447 0.0736 -0.0568 0.0410 97 LEU B O 4885 C CB . LEU B 97 ? 0.6195 1.6207 1.0197 0.1338 -0.0690 0.0570 97 LEU B CB 4886 C CG . LEU B 97 ? 0.6223 1.6859 1.0536 0.1299 -0.0693 0.0560 97 LEU B CG 4887 C CD1 . LEU B 97 ? 0.5244 1.6127 0.9594 0.1038 -0.0781 0.0531 97 LEU B CD1 4888 C CD2 . LEU B 97 ? 0.5881 1.6857 1.0408 0.1557 -0.0754 0.0635 97 LEU B CD2 4889 N N . PHE B 98 ? 0.6960 1.6513 1.0738 0.1010 -0.0414 0.0406 98 PHE B N 4890 C CA . PHE B 98 ? 0.6714 1.6443 1.0578 0.0892 -0.0287 0.0359 98 PHE B CA 4891 C C . PHE B 98 ? 0.6171 1.5531 0.9811 0.0675 -0.0230 0.0311 98 PHE B C 4892 O O . PHE B 98 ? 0.6172 1.5657 0.9862 0.0546 -0.0128 0.0285 98 PHE B O 4893 C CB . PHE B 98 ? 0.6070 1.5903 1.0038 0.1115 -0.0172 0.0351 98 PHE B CB 4894 C CG . PHE B 98 ? 0.5506 1.5817 0.9760 0.1301 -0.0210 0.0393 98 PHE B CG 4895 C CD1 . PHE B 98 ? 0.6380 1.6582 1.0639 0.1561 -0.0266 0.0434 98 PHE B CD1 4896 C CD2 . PHE B 98 ? 0.5413 1.6283 0.9943 0.1215 -0.0191 0.0396 98 PHE B CD2 4897 C CE1 . PHE B 98 ? 0.6760 1.7398 1.1285 0.1746 -0.0305 0.0479 98 PHE B CE1 4898 C CE2 . PHE B 98 ? 0.5994 1.7326 1.0802 0.1394 -0.0230 0.0434 98 PHE B CE2 4899 C CZ . PHE B 98 ? 0.6393 1.7606 1.1193 0.1667 -0.0289 0.0477 98 PHE B CZ 4900 N N . ASN B 99 ? 0.5497 1.4416 0.8897 0.0637 -0.0294 0.0307 99 ASN B N 4901 C CA . ASN B 99 ? 0.6319 1.4896 0.9512 0.0428 -0.0266 0.0265 99 ASN B CA 4902 C C . ASN B 99 ? 0.6562 1.5266 0.9780 0.0200 -0.0363 0.0255 99 ASN B C 4903 O O . ASN B 99 ? 0.6306 1.4728 0.9352 0.0136 -0.0446 0.0247 99 ASN B O 4904 C CB . ASN B 99 ? 0.7005 1.5036 0.9933 0.0508 -0.0275 0.0257 99 ASN B CB 4905 C CG . ASN B 99 ? 0.6715 1.4639 0.9647 0.0773 -0.0233 0.0268 99 ASN B CG 4906 O OD1 . ASN B 99 ? 0.6393 1.4483 0.9447 0.0945 -0.0289 0.0314 99 ASN B OD1 4907 N ND2 . ASN B 99 ? 0.7976 1.5611 1.0769 0.0810 -0.0138 0.0225 99 ASN B ND2 4908 N N . GLN B 100 ? 0.6137 1.5282 0.9583 0.0080 -0.0351 0.0251 100 GLN B N 4909 C CA . GLN B 100 ? 0.5834 1.5152 0.9347 -0.0151 -0.0438 0.0225 100 GLN B CA 4910 C C . GLN B 100 ? 0.5957 1.4887 0.9264 -0.0371 -0.0426 0.0178 100 GLN B C 4911 O O . GLN B 100 ? 0.7342 1.6352 1.0682 -0.0569 -0.0500 0.0142 100 GLN B O 4912 C CB . GLN B 100 ? 0.6971 1.6824 1.0791 -0.0250 -0.0400 0.0226 100 GLN B CB 4913 C CG . GLN B 100 ? 0.9375 1.9676 1.3441 -0.0042 -0.0406 0.0268 100 GLN B CG 4914 C CD . GLN B 100 ? 1.2647 2.3139 1.6773 0.0035 -0.0569 0.0287 100 GLN B CD 4915 O OE1 . GLN B 100 ? 1.2478 2.2781 1.6454 -0.0072 -0.0675 0.0264 100 GLN B OE1 4916 N NE2 . GLN B 100 ? 1.4141 2.5020 1.8481 0.0230 -0.0590 0.0331 100 GLN B NE2 4917 N N . ASP B 101 ? 0.4724 1.3242 0.7826 -0.0338 -0.0337 0.0174 101 ASP B N 4918 C CA . ASP B 101 ? 0.5285 1.3471 0.8220 -0.0543 -0.0311 0.0137 101 ASP B CA 4919 C C . ASP B 101 ? 0.6255 1.3936 0.8911 -0.0491 -0.0352 0.0121 101 ASP B C 4920 O O . ASP B 101 ? 0.6769 1.4126 0.9262 -0.0635 -0.0342 0.0089 101 ASP B O 4921 C CB . ASP B 101 ? 0.7940 1.6098 1.0876 -0.0589 -0.0161 0.0149 101 ASP B CB 4922 C CG . ASP B 101 ? 0.9453 1.8069 1.2656 -0.0733 -0.0112 0.0164 101 ASP B CG 4923 O OD1 . ASP B 101 ? 0.9999 1.8926 1.3382 -0.0828 -0.0207 0.0150 101 ASP B OD1 4924 O OD2 . ASP B 101 ? 0.9362 1.8040 1.2597 -0.0752 0.0021 0.0189 101 ASP B OD2 4925 N N . LEU B 102 ? 0.5447 1.3064 0.8059 -0.0284 -0.0397 0.0147 102 LEU B N 4926 C CA . LEU B 102 ? 0.4202 1.1358 0.6573 -0.0214 -0.0424 0.0141 102 LEU B CA 4927 C C . LEU B 102 ? 0.5497 1.2496 0.7751 -0.0368 -0.0520 0.0107 102 LEU B C 4928 O O . LEU B 102 ? 0.5805 1.3029 0.8130 -0.0380 -0.0621 0.0111 102 LEU B O 4929 C CB . LEU B 102 ? 0.4097 1.1253 0.6483 0.0032 -0.0456 0.0189 102 LEU B CB 4930 C CG . LEU B 102 ? 0.5402 1.2098 0.7573 0.0126 -0.0473 0.0194 102 LEU B CG 4931 C CD1 . LEU B 102 ? 0.4520 1.0890 0.6564 0.0158 -0.0373 0.0164 102 LEU B CD1 4932 C CD2 . LEU B 102 ? 0.7026 1.3786 0.9254 0.0340 -0.0525 0.0257 102 LEU B CD2 4933 N N . GLU B 103 ? 0.5297 1.1920 0.7369 -0.0480 -0.0491 0.0069 103 GLU B N 4934 C CA . GLU B 103 ? 0.6751 1.3192 0.8698 -0.0613 -0.0573 0.0025 103 GLU B CA 4935 C C . GLU B 103 ? 0.6948 1.2959 0.8672 -0.0539 -0.0591 0.0021 103 GLU B C 4936 O O . GLU B 103 ? 0.7545 1.3451 0.9172 -0.0598 -0.0667 -0.0007 103 GLU B O 4937 C CB . GLU B 103 ? 0.6605 1.3014 0.8560 -0.0848 -0.0552 -0.0027 103 GLU B CB 4938 C CG . GLU B 103 ? 0.7073 1.3337 0.8999 -0.0888 -0.0434 -0.0015 103 GLU B CG 4939 C CD . GLU B 103 ? 0.9045 1.5417 1.1064 -0.1119 -0.0412 -0.0039 103 GLU B CD 4940 O OE1 . GLU B 103 ? 0.9879 1.5930 1.1762 -0.1238 -0.0386 -0.0062 103 GLU B OE1 4941 O OE2 . GLU B 103 ? 0.9024 1.5803 1.1263 -0.1184 -0.0425 -0.0033 103 GLU B OE2 4942 N N . TYR B 104 ? 0.6047 1.1826 0.7695 -0.0408 -0.0522 0.0045 104 TYR B N 4943 C CA . TYR B 104 ? 0.5078 1.0466 0.6542 -0.0336 -0.0537 0.0044 104 TYR B CA 4944 C C . TYR B 104 ? 0.5494 1.0855 0.6984 -0.0116 -0.0525 0.0097 104 TYR B C 4945 O O . TYR B 104 ? 0.5919 1.1284 0.7452 -0.0021 -0.0454 0.0104 104 TYR B O 4946 C CB . TYR B 104 ? 0.3845 0.8885 0.5161 -0.0425 -0.0478 0.0003 104 TYR B CB 4947 C CG . TYR B 104 ? 0.4544 0.9182 0.5687 -0.0358 -0.0486 -0.0005 104 TYR B CG 4948 C CD1 . TYR B 104 ? 0.2668 0.7031 0.3671 -0.0478 -0.0503 -0.0050 104 TYR B CD1 4949 C CD2 . TYR B 104 ? 0.6356 1.0886 0.7490 -0.0176 -0.0474 0.0029 104 TYR B CD2 4950 C CE1 . TYR B 104 ? 0.4448 0.8465 0.5312 -0.0418 -0.0508 -0.0058 104 TYR B CE1 4951 C CE2 . TYR B 104 ? 0.6479 1.0653 0.7479 -0.0125 -0.0481 0.0021 104 TYR B CE2 4952 C CZ . TYR B 104 ? 0.6051 0.9982 0.6919 -0.0246 -0.0497 -0.0022 104 TYR B CZ 4953 O OH . TYR B 104 ? 0.5907 0.9511 0.6663 -0.0193 -0.0503 -0.0029 104 TYR B OH 4954 N N . LEU B 105 ? 0.5711 1.1046 0.7173 -0.0033 -0.0595 0.0136 105 LEU B N 4955 C CA . LEU B 105 ? 0.6232 1.1507 0.7722 0.0171 -0.0594 0.0197 105 LEU B CA 4956 C C . LEU B 105 ? 0.6037 1.0968 0.7375 0.0199 -0.0624 0.0214 105 LEU B C 4957 O O . LEU B 105 ? 0.5838 1.0785 0.7114 0.0134 -0.0686 0.0223 105 LEU B O 4958 C CB . LEU B 105 ? 0.6683 1.2337 0.8330 0.0265 -0.0649 0.0261 105 LEU B CB 4959 C CG . LEU B 105 ? 0.6212 1.1821 0.7897 0.0477 -0.0668 0.0344 105 LEU B CG 4960 C CD1 . LEU B 105 ? 0.6138 1.1502 0.7817 0.0598 -0.0593 0.0330 105 LEU B CD1 4961 C CD2 . LEU B 105 ? 0.5486 1.1518 0.7352 0.0572 -0.0713 0.0403 105 LEU B CD2 4962 N N . ASP B 106 ? 0.6116 1.0745 0.7396 0.0291 -0.0580 0.0211 106 ASP B N 4963 C CA . ASP B 106 ? 0.7501 1.1800 0.8662 0.0317 -0.0599 0.0228 106 ASP B CA 4964 C C . ASP B 106 ? 0.7629 1.1829 0.8850 0.0508 -0.0597 0.0294 106 ASP B C 4965 O O . ASP B 106 ? 0.8403 1.2430 0.9634 0.0589 -0.0550 0.0265 106 ASP B O 4966 C CB . ASP B 106 ? 0.7507 1.1482 0.8536 0.0228 -0.0559 0.0154 106 ASP B CB 4967 C CG . ASP B 106 ? 0.7577 1.1220 0.8511 0.0263 -0.0574 0.0168 106 ASP B CG 4968 O OD1 . ASP B 106 ? 0.8264 1.1927 0.9192 0.0289 -0.0618 0.0228 106 ASP B OD1 4969 O OD2 . ASP B 106 ? 0.7392 1.0764 0.8259 0.0264 -0.0541 0.0121 106 ASP B OD2 4970 N N . VAL B 107 ? 0.6715 1.1023 0.7974 0.0579 -0.0650 0.0382 107 VAL B N 4971 C CA . VAL B 107 ? 0.6179 1.0379 0.7504 0.0756 -0.0653 0.0460 107 VAL B CA 4972 C C . VAL B 107 ? 0.6994 1.0929 0.8224 0.0752 -0.0675 0.0514 107 VAL B C 4973 O O . VAL B 107 ? 0.7501 1.1408 0.8778 0.0869 -0.0698 0.0617 107 VAL B O 4974 C CB . VAL B 107 ? 0.5784 1.0319 0.7249 0.0875 -0.0690 0.0546 107 VAL B CB 4975 C CG1 . VAL B 107 ? 0.6008 1.0418 0.7571 0.1070 -0.0674 0.0603 107 VAL B CG1 4976 C CG2 . VAL B 107 ? 0.5184 1.0062 0.6744 0.0828 -0.0678 0.0494 107 VAL B CG2 4977 N N . SER B 108 ? 0.6616 1.0360 0.7719 0.0618 -0.0665 0.0450 108 SER B N 4978 C CA . SER B 108 ? 0.6474 0.9970 0.7493 0.0604 -0.0675 0.0489 108 SER B CA 4979 C C . SER B 108 ? 0.6250 0.9477 0.7328 0.0729 -0.0652 0.0527 108 SER B C 4980 O O . SER B 108 ? 0.7042 1.0260 0.8209 0.0827 -0.0631 0.0507 108 SER B O 4981 C CB . SER B 108 ? 0.6681 1.0002 0.7574 0.0454 -0.0660 0.0395 108 SER B CB 4982 O OG . SER B 108 ? 0.7135 1.0271 0.8026 0.0451 -0.0619 0.0313 108 SER B OG 4983 N N . HIS B 109 ? 0.6187 0.9199 0.7223 0.0725 -0.0656 0.0578 109 HIS B N 4984 C CA . HIS B 109 ? 0.6087 0.8805 0.7185 0.0815 -0.0638 0.0602 109 HIS B CA 4985 C C . HIS B 109 ? 0.6074 0.8815 0.7310 0.0977 -0.0637 0.0644 109 HIS B C 4986 O O . HIS B 109 ? 0.7020 0.9543 0.8307 0.1040 -0.0617 0.0591 109 HIS B O 4987 C CB . HIS B 109 ? 0.4937 0.7397 0.5978 0.0744 -0.0612 0.0479 109 HIS B CB 4988 C CG . HIS B 109 ? 0.6545 0.8926 0.7468 0.0606 -0.0614 0.0446 109 HIS B CG 4989 N ND1 . HIS B 109 ? 0.6970 0.9169 0.7881 0.0590 -0.0614 0.0497 109 HIS B ND1 4990 C CD2 . HIS B 109 ? 0.7027 0.9491 0.7848 0.0481 -0.0614 0.0367 109 HIS B CD2 4991 C CE1 . HIS B 109 ? 0.6836 0.9017 0.7640 0.0470 -0.0613 0.0444 109 HIS B CE1 4992 N NE2 . HIS B 109 ? 0.6908 0.9235 0.7654 0.0403 -0.0616 0.0364 109 HIS B NE2 4993 N N . ASN B 110 ? 0.5822 0.8832 0.7119 0.1052 -0.0662 0.0733 110 ASN B N 4994 C CA . ASN B 110 ? 0.6974 0.9988 0.8411 0.1225 -0.0665 0.0797 110 ASN B CA 4995 C C . ASN B 110 ? 0.7998 1.0944 0.9473 0.1301 -0.0690 0.0961 110 ASN B C 4996 O O . ASN B 110 ? 0.7549 1.0302 0.8964 0.1236 -0.0684 0.1002 110 ASN B O 4997 C CB . ASN B 110 ? 0.7156 1.0525 0.8667 0.1285 -0.0675 0.0790 110 ASN B CB 4998 C CG . ASN B 110 ? 0.7223 1.0630 0.8736 0.1253 -0.0634 0.0646 110 ASN B CG 4999 O OD1 . ASN B 110 ? 0.7139 1.0528 0.8547 0.1109 -0.0618 0.0558 110 ASN B OD1 5000 N ND2 . ASN B 110 ? 0.7710 1.1175 0.9341 0.1394 -0.0615 0.0626 110 ASN B ND2 5001 N N . ARG B 111 ? 0.8402 1.1517 0.9983 0.1443 -0.0714 0.1062 111 ARG B N 5002 C CA . ARG B 111 ? 0.9304 1.2383 1.0921 0.1529 -0.0738 0.1241 111 ARG B CA 5003 C C . ARG B 111 ? 0.9977 1.3444 1.1611 0.1592 -0.0786 0.1340 111 ARG B C 5004 O O . ARG B 111 ? 1.1034 1.4538 1.2745 0.1729 -0.0812 0.1490 111 ARG B O 5005 C CB . ARG B 111 ? 0.9462 1.2258 1.1221 0.1677 -0.0726 0.1287 111 ARG B CB 5006 C CG . ARG B 111 ? 1.0401 1.2808 1.2155 0.1617 -0.0693 0.1207 111 ARG B CG 5007 C CD . ARG B 111 ? 1.3421 1.5539 1.5314 0.1748 -0.0693 0.1298 111 ARG B CD 5008 N NE . ARG B 111 ? 1.5392 1.7187 1.7337 0.1748 -0.0672 0.1162 111 ARG B NE 5009 C CZ . ARG B 111 ? 1.5562 1.7282 1.7607 0.1872 -0.0669 0.1071 111 ARG B CZ 5010 N NH1 . ARG B 111 ? 1.5014 1.6967 1.7132 0.2008 -0.0680 0.1108 111 ARG B NH1 5011 N NH2 . ARG B 111 ? 1.5358 1.6783 1.7429 0.1864 -0.0656 0.0938 111 ARG B NH2 5012 N N . LEU B 112 ? 0.8744 1.2499 1.0309 0.1489 -0.0801 0.1254 112 LEU B N 5013 C CA . LEU B 112 ? 0.8163 1.2321 0.9745 0.1525 -0.0856 0.1318 112 LEU B CA 5014 C C . LEU B 112 ? 0.8738 1.2968 1.0254 0.1560 -0.0898 0.1491 112 LEU B C 5015 O O . LEU B 112 ? 0.9375 1.3418 1.0777 0.1482 -0.0881 0.1528 112 LEU B O 5016 C CB . LEU B 112 ? 0.7619 1.2023 0.9125 0.1366 -0.0865 0.1186 112 LEU B CB 5017 C CG . LEU B 112 ? 0.5815 1.0268 0.7396 0.1341 -0.0828 0.1041 112 LEU B CG 5018 C CD1 . LEU B 112 ? 0.4616 0.9290 0.6122 0.1165 -0.0838 0.0932 112 LEU B CD1 5019 C CD2 . LEU B 112 ? 0.5609 1.0274 0.7364 0.1510 -0.0839 0.1082 112 LEU B CD2 5020 N N . GLN B 113 ? 0.8288 1.2805 0.9873 0.1683 -0.0952 0.1599 113 GLN B N 5021 C CA . GLN B 113 ? 0.7714 1.2358 0.9224 0.1730 -0.1000 0.1774 113 GLN B CA 5022 C C . GLN B 113 ? 0.8889 1.3995 1.0435 0.1792 -0.1078 0.1814 113 GLN B C 5023 O O . GLN B 113 ? 1.0909 1.6224 1.2344 0.1781 -0.1132 0.1906 113 GLN B O 5024 C CB . GLN B 113 ? 0.8185 1.2549 0.9766 0.1877 -0.0981 0.1945 113 GLN B CB 5025 C CG . GLN B 113 ? 1.0326 1.4697 1.2105 0.2067 -0.0991 0.1985 113 GLN B CG 5026 C CD . GLN B 113 ? 1.1539 1.5557 1.3401 0.2197 -0.0967 0.2133 113 GLN B CD 5027 O OE1 . GLN B 113 ? 1.1233 1.4958 1.3025 0.2124 -0.0929 0.2179 113 GLN B OE1 5028 N NE2 . GLN B 113 ? 1.1160 1.5204 1.3188 0.2390 -0.0989 0.2208 113 GLN B NE2 5029 N N . ASN B 114 ? 0.7098 1.2377 0.8801 0.1860 -0.1085 0.1741 114 ASN B N 5030 C CA . ASN B 114 ? 0.7013 1.2761 0.8785 0.1904 -0.1160 0.1752 114 ASN B CA 5031 C C . ASN B 114 ? 0.7734 1.3668 0.9556 0.1775 -0.1143 0.1556 114 ASN B C 5032 O O . ASN B 114 ? 0.8789 1.4487 1.0638 0.1724 -0.1071 0.1442 114 ASN B O 5033 C CB . ASN B 114 ? 0.6904 1.2742 0.8855 0.2138 -0.1186 0.1881 114 ASN B CB 5034 C CG . ASN B 114 ? 1.1124 1.7465 1.3131 0.2213 -0.1285 0.1951 114 ASN B CG 5035 O OD1 . ASN B 114 ? 1.0650 1.7254 1.2538 0.2096 -0.1342 0.1926 114 ASN B OD1 5036 N ND2 . ASN B 114 ? 1.0419 1.6891 1.2611 0.2415 -0.1309 0.2032 114 ASN B ND2 5037 N N . ILE B 115 ? 0.7129 1.3486 0.8964 0.1719 -0.1211 0.1523 115 ILE B N 5038 C CA . ILE B 115 ? 0.5663 1.2215 0.7541 0.1566 -0.1200 0.1350 115 ILE B CA 5039 C C . ILE B 115 ? 0.5863 1.2941 0.7846 0.1573 -0.1288 0.1348 115 ILE B C 5040 O O . ILE B 115 ? 0.4902 1.2196 0.6806 0.1577 -0.1374 0.1422 115 ILE B O 5041 C CB . ILE B 115 ? 0.4073 1.0452 0.5759 0.1349 -0.1180 0.1244 115 ILE B CB 5042 C CG1 . ILE B 115 ? 0.5601 1.1560 0.7254 0.1295 -0.1083 0.1162 115 ILE B CG1 5043 C CG2 . ILE B 115 ? 0.3587 1.0277 0.5285 0.1183 -0.1215 0.1112 115 ILE B CG2 5044 C CD1 . ILE B 115 ? 0.6757 1.2623 0.8274 0.1082 -0.1064 0.1028 115 ILE B CD1 5045 N N . SER B 116 ? 0.7399 1.4704 0.9566 0.1576 -0.1268 0.1264 116 SER B N 5046 C CA . SER B 116 ? 0.7894 1.5715 1.0183 0.1550 -0.1350 0.1241 116 SER B CA 5047 C C . SER B 116 ? 0.8818 1.6750 1.0949 0.1347 -0.1411 0.1168 116 SER B C 5048 O O . SER B 116 ? 0.8201 1.5856 1.0190 0.1188 -0.1361 0.1076 116 SER B O 5049 C CB . SER B 116 ? 0.7112 1.5132 0.9605 0.1519 -0.1296 0.1131 116 SER B CB 5050 O OG . SER B 116 ? 0.6831 1.5338 0.9438 0.1431 -0.1371 0.1081 116 SER B OG 5051 N N . CYS B 117 ? 0.9724 1.8061 1.1877 0.1357 -0.1524 0.1204 117 CYS B N 5052 C CA . CYS B 117 ? 0.9449 1.7898 1.1440 0.1180 -0.1594 0.1129 117 CYS B CA 5053 C C . CYS B 117 ? 0.9735 1.8341 1.1802 0.0962 -0.1588 0.0950 117 CYS B C 5054 O O . CYS B 117 ? 0.9656 1.8223 1.1578 0.0786 -0.1617 0.0852 117 CYS B O 5055 C CB . CYS B 117 ? 0.8594 1.7416 1.0557 0.1269 -0.1727 0.1227 117 CYS B CB 5056 S SG . CYS B 117 ? 1.8157 2.6736 1.9849 0.1379 -0.1752 0.1396 117 CYS B SG 5057 N N . CYS B 118 ? 0.9482 1.8257 1.1777 0.0973 -0.1544 0.0907 118 CYS B N 5058 C CA . CYS B 118 ? 0.8328 1.7274 1.0719 0.0764 -0.1533 0.0756 118 CYS B CA 5059 C C . CYS B 118 ? 0.8537 1.7199 1.0967 0.0690 -0.1398 0.0680 118 CYS B C 5060 O O . CYS B 118 ? 0.8781 1.7575 1.1405 0.0767 -0.1339 0.0687 118 CYS B O 5061 C CB . CYS B 118 ? 0.7374 1.6878 1.0012 0.0783 -0.1611 0.0749 118 CYS B CB 5062 S SG . CYS B 118 ? 1.2912 2.2680 1.5629 0.0489 -0.1652 0.0573 118 CYS B SG 5063 N N . PRO B 119 ? 0.7156 1.5438 0.9394 0.0545 -0.1349 0.0608 119 PRO B N 5064 C CA . PRO B 119 ? 0.5793 1.3792 0.8023 0.0441 -0.1235 0.0525 119 PRO B CA 5065 C C . PRO B 119 ? 0.6433 1.4723 0.8833 0.0277 -0.1224 0.0428 119 PRO B C 5066 O O . PRO B 119 ? 0.5010 1.3616 0.7466 0.0167 -0.1315 0.0382 119 PRO B O 5067 C CB . PRO B 119 ? 0.5075 1.2703 0.7058 0.0312 -0.1232 0.0472 119 PRO B CB 5068 C CG . PRO B 119 ? 0.5289 1.2895 0.7144 0.0422 -0.1303 0.0564 119 PRO B CG 5069 C CD . PRO B 119 ? 0.6667 1.4758 0.8667 0.0497 -0.1403 0.0613 119 PRO B CD 5070 N N . MET B 120 ? 0.7607 1.5789 1.0084 0.0258 -0.1113 0.0396 120 MET B N 5071 C CA . MET B 120 ? 0.5569 1.4018 0.8222 0.0106 -0.1080 0.0322 120 MET B CA 5072 C C . MET B 120 ? 0.4682 1.3084 0.7254 -0.0148 -0.1119 0.0220 120 MET B C 5073 O O . MET B 120 ? 0.3348 1.1357 0.5710 -0.0227 -0.1100 0.0181 120 MET B O 5074 C CB . MET B 120 ? 0.4875 1.3171 0.7580 0.0141 -0.0941 0.0315 120 MET B CB 5075 C CG . MET B 120 ? 0.7546 1.5301 1.0023 0.0157 -0.0868 0.0307 120 MET B CG 5076 S SD . MET B 120 ? 0.9672 1.7198 1.2124 0.0436 -0.0815 0.0390 120 MET B SD 5077 C CE . MET B 120 ? 0.4118 1.2127 0.6783 0.0607 -0.0902 0.0475 120 MET B CE 5078 N N . ALA B 121 ? 0.5367 1.4176 0.8119 -0.0273 -0.1179 0.0172 121 ALA B N 5079 C CA . ALA B 121 ? 0.5783 1.4581 0.8489 -0.0515 -0.1232 0.0065 121 ALA B CA 5080 C C . ALA B 121 ? 0.5861 1.4338 0.8509 -0.0676 -0.1123 0.0007 121 ALA B C 5081 O O . ALA B 121 ? 0.4948 1.3282 0.7515 -0.0868 -0.1152 -0.0080 121 ALA B O 5082 C CB . ALA B 121 ? 0.5421 1.4748 0.8371 -0.0614 -0.1320 0.0026 121 ALA B CB 5083 N N . SER B 122 ? 0.6734 1.5095 0.9420 -0.0590 -0.1001 0.0055 122 SER B N 5084 C CA . SER B 122 ? 0.6287 1.4361 0.8913 -0.0719 -0.0892 0.0018 122 SER B CA 5085 C C . SER B 122 ? 0.5839 1.3380 0.8186 -0.0720 -0.0869 0.0000 122 SER B C 5086 O O . SER B 122 ? 0.3944 1.1214 0.6210 -0.0839 -0.0799 -0.0035 122 SER B O 5087 C CB . SER B 122 ? 0.5733 1.3892 0.8481 -0.0612 -0.0771 0.0071 122 SER B CB 5088 O OG . SER B 122 ? 0.7941 1.5965 1.0684 -0.0776 -0.0677 0.0038 122 SER B OG 5089 N N . LEU B 123 ? 0.6216 1.3622 0.8424 -0.0587 -0.0929 0.0031 123 LEU B N 5090 C CA . LEU B 123 ? 0.6668 1.3602 0.8633 -0.0559 -0.0908 0.0026 123 LEU B CA 5091 C C . LEU B 123 ? 0.6933 1.3644 0.8765 -0.0758 -0.0936 -0.0066 123 LEU B C 5092 O O . LEU B 123 ? 0.8128 1.5037 0.9997 -0.0877 -0.1023 -0.0124 123 LEU B O 5093 C CB . LEU B 123 ? 0.6061 1.2957 0.7935 -0.0382 -0.0968 0.0092 123 LEU B CB 5094 C CG . LEU B 123 ? 0.5945 1.2695 0.7816 -0.0169 -0.0905 0.0178 123 LEU B CG 5095 C CD1 . LEU B 123 ? 0.7257 1.3997 0.9227 -0.0160 -0.0796 0.0169 123 LEU B CD1 5096 C CD2 . LEU B 123 ? 0.4214 1.1244 0.6184 0.0010 -0.0967 0.0266 123 LEU B CD2 5097 N N . ARG B 124 ? 0.5751 1.2054 0.7435 -0.0788 -0.0865 -0.0083 124 ARG B N 5098 C CA . ARG B 124 ? 0.5690 1.1712 0.7225 -0.0942 -0.0886 -0.0164 124 ARG B CA 5099 C C . ARG B 124 ? 0.6114 1.1754 0.7445 -0.0838 -0.0871 -0.0146 124 ARG B C 5100 O O . ARG B 124 ? 0.7352 1.2780 0.8540 -0.0908 -0.0907 -0.0203 124 ARG B O 5101 C CB . ARG B 124 ? 0.5880 1.1776 0.7446 -0.1104 -0.0814 -0.0203 124 ARG B CB 5102 C CG . ARG B 124 ? 0.7105 1.3383 0.8899 -0.1215 -0.0810 -0.0209 124 ARG B CG 5103 C CD . ARG B 124 ? 0.8441 1.4596 1.0259 -0.1426 -0.0767 -0.0257 124 ARG B CD 5104 N NE . ARG B 124 ? 1.0754 1.7309 1.2811 -0.1556 -0.0785 -0.0269 124 ARG B NE 5105 C CZ . ARG B 124 ? 1.2340 1.8888 1.4471 -0.1775 -0.0787 -0.0323 124 ARG B CZ 5106 N NH1 . ARG B 124 ? 1.3021 1.9169 1.4995 -0.1878 -0.0774 -0.0368 124 ARG B NH1 5107 N NH2 . ARG B 124 ? 1.2102 1.9044 1.4478 -0.1891 -0.0805 -0.0331 124 ARG B NH2 5108 N N . HIS B 125 ? 0.4791 1.0349 0.6121 -0.0668 -0.0817 -0.0070 125 HIS B N 5109 C CA . HIS B 125 ? 0.4960 1.0175 0.6129 -0.0563 -0.0802 -0.0044 125 HIS B CA 5110 C C . HIS B 125 ? 0.5610 1.0913 0.6831 -0.0359 -0.0802 0.0049 125 HIS B C 5111 O O . HIS B 125 ? 0.5991 1.1338 0.7303 -0.0263 -0.0745 0.0086 125 HIS B O 5112 C CB . HIS B 125 ? 0.4946 0.9813 0.6028 -0.0599 -0.0721 -0.0070 125 HIS B CB 5113 C CG . HIS B 125 ? 0.5906 1.0437 0.6855 -0.0489 -0.0702 -0.0046 125 HIS B CG 5114 N ND1 . HIS B 125 ? 0.6957 1.1160 0.7759 -0.0558 -0.0696 -0.0094 125 HIS B ND1 5115 C CD2 . HIS B 125 ? 0.6397 1.0867 0.7354 -0.0318 -0.0688 0.0021 125 HIS B CD2 5116 C CE1 . HIS B 125 ? 0.7450 1.1424 0.8182 -0.0440 -0.0679 -0.0059 125 HIS B CE1 5117 N NE2 . HIS B 125 ? 0.6882 1.1001 0.7705 -0.0297 -0.0675 0.0011 125 HIS B NE2 5118 N N . LEU B 126 ? 0.5765 1.1098 0.6926 -0.0289 -0.0865 0.0088 126 LEU B N 5119 C CA . LEU B 126 ? 0.5538 1.0937 0.6746 -0.0098 -0.0873 0.0190 126 LEU B CA 5120 C C . LEU B 126 ? 0.5769 1.0845 0.6828 -0.0028 -0.0868 0.0229 126 LEU B C 5121 O O . LEU B 126 ? 0.5480 1.0536 0.6430 -0.0072 -0.0916 0.0223 126 LEU B O 5122 C CB . LEU B 126 ? 0.5672 1.1471 0.6969 -0.0064 -0.0957 0.0231 126 LEU B CB 5123 C CG . LEU B 126 ? 0.6344 1.2228 0.7676 0.0135 -0.0984 0.0353 126 LEU B CG 5124 C CD1 . LEU B 126 ? 0.7251 1.3026 0.8678 0.0277 -0.0913 0.0402 126 LEU B CD1 5125 C CD2 . LEU B 126 ? 0.6660 1.2989 0.8103 0.0159 -0.1069 0.0385 126 LEU B CD2 5126 N N . ASP B 127 ? 0.6663 1.1492 0.7723 0.0078 -0.0809 0.0265 127 ASP B N 5127 C CA . ASP B 127 ? 0.6782 1.1296 0.7730 0.0134 -0.0798 0.0302 127 ASP B CA 5128 C C . ASP B 127 ? 0.6932 1.1448 0.7945 0.0318 -0.0802 0.0418 127 ASP B C 5129 O O . ASP B 127 ? 0.5625 1.0087 0.6730 0.0421 -0.0762 0.0436 127 ASP B O 5130 C CB . ASP B 127 ? 0.6616 1.0786 0.7500 0.0093 -0.0735 0.0239 127 ASP B CB 5131 C CG . ASP B 127 ? 0.6618 1.0483 0.7389 0.0105 -0.0731 0.0254 127 ASP B CG 5132 O OD1 . ASP B 127 ? 0.6201 1.0095 0.6961 0.0182 -0.0758 0.0337 127 ASP B OD1 5133 O OD2 . ASP B 127 ? 0.7551 1.1155 0.8247 0.0041 -0.0698 0.0189 127 ASP B OD2 5134 N N . LEU B 128 ? 0.6753 1.1330 0.7713 0.0358 -0.0849 0.0496 128 LEU B N 5135 C CA . LEU B 128 ? 0.5659 1.0200 0.6664 0.0525 -0.0855 0.0627 128 LEU B CA 5136 C C . LEU B 128 ? 0.5120 0.9383 0.6010 0.0528 -0.0842 0.0676 128 LEU B C 5137 O O . LEU B 128 ? 0.5365 0.9632 0.6258 0.0632 -0.0857 0.0800 128 LEU B O 5138 C CB . LEU B 128 ? 0.4896 0.9803 0.5954 0.0594 -0.0924 0.0713 128 LEU B CB 5139 C CG . LEU B 128 ? 0.5820 1.1080 0.6989 0.0553 -0.0954 0.0656 128 LEU B CG 5140 C CD1 . LEU B 128 ? 0.5068 1.0686 0.6260 0.0605 -0.1038 0.0732 128 LEU B CD1 5141 C CD2 . LEU B 128 ? 0.7613 1.2879 0.8937 0.0650 -0.0905 0.0653 128 LEU B CD2 5142 N N . SER B 129 ? 0.5502 0.9531 0.6295 0.0414 -0.0810 0.0585 129 SER B N 5143 C CA . SER B 129 ? 0.5940 0.9727 0.6639 0.0408 -0.0792 0.0622 129 SER B CA 5144 C C . SER B 129 ? 0.5360 0.8887 0.6137 0.0521 -0.0753 0.0691 129 SER B C 5145 O O . SER B 129 ? 0.5660 0.9151 0.6540 0.0589 -0.0736 0.0675 129 SER B O 5146 C CB . SER B 129 ? 0.6089 0.9708 0.6678 0.0263 -0.0774 0.0500 129 SER B CB 5147 O OG . SER B 129 ? 0.8076 1.1505 0.8703 0.0238 -0.0735 0.0419 129 SER B OG 5148 N N . PHE B 130 ? 0.4886 0.8242 0.5620 0.0541 -0.0739 0.0765 130 PHE B N 5149 C CA . PHE B 130 ? 0.5510 0.8600 0.6328 0.0633 -0.0706 0.0833 130 PHE B CA 5150 C C . PHE B 130 ? 0.6267 0.9425 0.7221 0.0780 -0.0717 0.0916 130 PHE B C 5151 O O . PHE B 130 ? 0.7850 1.0861 0.8894 0.0835 -0.0696 0.0869 130 PHE B O 5152 C CB . PHE B 130 ? 0.4315 0.7121 0.5134 0.0574 -0.0671 0.0716 130 PHE B CB 5153 C CG . PHE B 130 ? 0.5546 0.8275 0.6243 0.0443 -0.0662 0.0636 130 PHE B CG 5154 C CD1 . PHE B 130 ? 0.5436 0.8283 0.6056 0.0337 -0.0675 0.0524 130 PHE B CD1 5155 C CD2 . PHE B 130 ? 0.6296 0.8840 0.6966 0.0425 -0.0640 0.0676 130 PHE B CD2 5156 C CE1 . PHE B 130 ? 0.5851 0.8613 0.6363 0.0225 -0.0669 0.0448 130 PHE B CE1 5157 C CE2 . PHE B 130 ? 0.7152 0.9638 0.7717 0.0315 -0.0630 0.0598 130 PHE B CE2 5158 C CZ . PHE B 130 ? 0.6649 0.9234 0.7131 0.0221 -0.0647 0.0481 130 PHE B CZ 5159 N N . ASN B 131 ? 0.5854 0.9243 0.6818 0.0852 -0.0752 0.1037 131 ASN B N 5160 C CA . ASN B 131 ? 0.6833 1.0270 0.7931 0.1011 -0.0765 0.1143 131 ASN B CA 5161 C C . ASN B 131 ? 0.8181 1.1608 0.9267 0.1086 -0.0775 0.1325 131 ASN B C 5162 O O . ASN B 131 ? 0.8547 1.1870 0.9536 0.1016 -0.0756 0.1359 131 ASN B O 5163 C CB . ASN B 131 ? 0.5903 0.9687 0.7053 0.1049 -0.0804 0.1120 131 ASN B CB 5164 C CG . ASN B 131 ? 0.6188 0.9998 0.7356 0.0971 -0.0784 0.0957 131 ASN B CG 5165 O OD1 . ASN B 131 ? 0.7116 1.0993 0.8187 0.0829 -0.0787 0.0860 131 ASN B OD1 5166 N ND2 . ASN B 131 ? 0.5049 0.8799 0.6336 0.1066 -0.0760 0.0927 131 ASN B ND2 5167 N N . ASP B 132 ? 0.8437 1.1976 0.9621 0.1233 -0.0802 0.1448 132 ASP B N 5168 C CA . ASP B 132 ? 0.9807 1.3318 1.0986 0.1317 -0.0808 0.1645 132 ASP B CA 5169 C C . ASP B 132 ? 0.9260 1.3147 1.0381 0.1369 -0.0869 0.1748 132 ASP B C 5170 O O . ASP B 132 ? 0.8610 1.2552 0.9790 0.1507 -0.0892 0.1916 132 ASP B O 5171 C CB . ASP B 132 ? 1.1145 1.4398 1.2486 0.1457 -0.0789 0.1738 132 ASP B CB 5172 C CG . ASP B 132 ? 1.3418 1.6407 1.4754 0.1456 -0.0753 0.1877 132 ASP B CG 5173 O OD1 . ASP B 132 ? 1.4813 1.7494 1.6188 0.1396 -0.0711 0.1805 132 ASP B OD1 5174 O OD2 . ASP B 132 ? 1.2843 1.5945 1.4135 0.1511 -0.0767 0.2059 132 ASP B OD2 5175 N N . PHE B 133 ? 0.9181 1.3324 1.0188 0.1259 -0.0900 0.1645 133 PHE B N 5176 C CA . PHE B 133 ? 0.8130 1.2647 0.9067 0.1292 -0.0968 0.1720 133 PHE B CA 5177 C C . PHE B 133 ? 0.9862 1.4374 1.0660 0.1300 -0.0965 0.1869 133 PHE B C 5178 O O . PHE B 133 ? 1.0884 1.5234 1.1572 0.1193 -0.0920 0.1830 133 PHE B O 5179 C CB . PHE B 133 ? 0.6230 1.1004 0.7093 0.1158 -0.1005 0.1551 133 PHE B CB 5180 C CG . PHE B 133 ? 0.6795 1.1684 0.7799 0.1163 -0.1016 0.1438 133 PHE B CG 5181 C CD1 . PHE B 133 ? 0.7289 1.2043 0.8300 0.1041 -0.0975 0.1266 133 PHE B CD1 5182 C CD2 . PHE B 133 ? 0.6467 1.1607 0.7601 0.1298 -0.1063 0.1511 133 PHE B CD2 5183 C CE1 . PHE B 133 ? 0.8342 1.3217 0.9479 0.1045 -0.0974 0.1173 133 PHE B CE1 5184 C CE2 . PHE B 133 ? 0.7005 1.2278 0.8280 0.1306 -0.1063 0.1410 133 PHE B CE2 5185 C CZ . PHE B 133 ? 0.8782 1.3924 1.0055 0.1177 -0.1015 0.1242 133 PHE B CZ 5186 N N . ASP B 134 ? 1.0495 1.5191 1.1303 0.1434 -0.1009 0.2048 134 ASP B N 5187 C CA . ASP B 134 ? 1.0851 1.5629 1.1508 0.1458 -0.1016 0.2211 134 ASP B CA 5188 C C . ASP B 134 ? 1.0240 1.5273 1.0705 0.1328 -0.1051 0.2090 134 ASP B C 5189 O O . ASP B 134 ? 0.8479 1.3399 0.8807 0.1229 -0.1005 0.2058 134 ASP B O 5190 C CB . ASP B 134 ? 1.2203 1.7195 1.2907 0.1635 -0.1077 0.2408 134 ASP B CB 5191 C CG . ASP B 134 ? 1.3762 1.8682 1.4370 0.1707 -0.1052 0.2646 134 ASP B CG 5192 O OD1 . ASP B 134 ? 1.3760 1.8811 1.4405 0.1862 -0.1097 0.2834 134 ASP B OD1 5193 O OD2 . ASP B 134 ? 1.4666 1.9406 1.5168 0.1613 -0.0986 0.2653 134 ASP B OD2 5194 N N . VAL B 135 ? 1.0170 1.5550 1.0638 0.1328 -0.1133 0.2013 135 VAL B N 5195 C CA . VAL B 135 ? 0.9026 1.4658 0.9329 0.1204 -0.1181 0.1880 135 VAL B CA 5196 C C . VAL B 135 ? 0.8786 1.4522 0.9175 0.1096 -0.1209 0.1663 135 VAL B C 5197 O O . VAL B 135 ? 0.9779 1.5578 1.0345 0.1156 -0.1226 0.1650 135 VAL B O 5198 C CB . VAL B 135 ? 0.8251 1.4265 0.8438 0.1288 -0.1270 0.1999 135 VAL B CB 5199 C CG1 . VAL B 135 ? 0.4791 1.1156 0.5094 0.1322 -0.1366 0.1938 135 VAL B CG1 5200 C CG2 . VAL B 135 ? 0.9877 1.6010 0.9820 0.1181 -0.1281 0.1929 135 VAL B CG2 5201 N N . LEU B 136 ? 0.8207 1.3952 0.8473 0.0938 -0.1209 0.1496 136 LEU B N 5202 C CA . LEU B 136 ? 0.7679 1.3520 0.8010 0.0812 -0.1235 0.1294 136 LEU B CA 5203 C C . LEU B 136 ? 0.7613 1.3776 0.8104 0.0872 -0.1307 0.1294 136 LEU B C 5204 O O . LEU B 136 ? 0.8890 1.5400 0.9339 0.0911 -0.1395 0.1334 136 LEU B O 5205 C CB . LEU B 136 ? 0.7671 1.3635 0.7822 0.0671 -0.1271 0.1156 136 LEU B CB 5206 C CG . LEU B 136 ? 0.8208 1.3894 0.8294 0.0520 -0.1210 0.0996 136 LEU B CG 5207 C CD1 . LEU B 136 ? 0.8762 1.4054 0.8938 0.0543 -0.1113 0.1029 136 LEU B CD1 5208 C CD2 . LEU B 136 ? 0.6936 1.2646 0.6797 0.0461 -0.1216 0.0959 136 LEU B CD2 5209 N N . PRO B 137 ? 0.7875 1.3943 0.8549 0.0880 -0.1271 0.1241 137 PRO B N 5210 C CA . PRO B 137 ? 0.7156 1.3503 0.8020 0.0958 -0.1317 0.1252 137 PRO B CA 5211 C C . PRO B 137 ? 0.7248 1.3948 0.8150 0.0837 -0.1389 0.1109 137 PRO B C 5212 O O . PRO B 137 ? 0.7414 1.4335 0.8498 0.0876 -0.1411 0.1093 137 PRO B O 5213 C CB . PRO B 137 ? 0.6033 1.2105 0.7043 0.0976 -0.1232 0.1211 137 PRO B CB 5214 C CG . PRO B 137 ? 0.5815 1.1471 0.6714 0.0918 -0.1154 0.1193 137 PRO B CG 5215 C CD . PRO B 137 ? 0.6639 1.2336 0.7342 0.0804 -0.1180 0.1150 137 PRO B CD 5216 N N . VAL B 138 ? 0.7535 1.4285 0.8281 0.0694 -0.1422 0.1002 138 VAL B N 5217 C CA . VAL B 138 ? 0.6859 1.3917 0.7642 0.0560 -0.1495 0.0855 138 VAL B CA 5218 C C . VAL B 138 ? 0.7171 1.4682 0.7988 0.0644 -0.1611 0.0923 138 VAL B C 5219 O O . VAL B 138 ? 0.7689 1.5320 0.8334 0.0667 -0.1672 0.0966 138 VAL B O 5220 C CB . VAL B 138 ? 0.6319 1.3277 0.6912 0.0393 -0.1503 0.0717 138 VAL B CB 5221 C CG1 . VAL B 138 ? 0.5597 1.2861 0.6240 0.0245 -0.1587 0.0558 138 VAL B CG1 5222 C CG2 . VAL B 138 ? 0.6041 1.2562 0.6597 0.0314 -0.1396 0.0652 138 VAL B CG2 5223 N N . CYS B 139 ? 0.6700 1.4477 0.7736 0.0694 -0.1642 0.0931 139 CYS B N 5224 C CA . CYS B 139 ? 0.6536 1.4779 0.7638 0.0776 -0.1762 0.0988 139 CYS B CA 5225 C C . CYS B 139 ? 0.6802 1.5357 0.7911 0.0599 -0.1853 0.0815 139 CYS B C 5226 O O . CYS B 139 ? 0.7385 1.5786 0.8481 0.0420 -0.1814 0.0660 139 CYS B O 5227 C CB . CYS B 139 ? 0.7274 1.5697 0.8631 0.0921 -0.1759 0.1073 139 CYS B CB 5228 S SG . CYS B 139 ? 1.1289 1.9382 1.2700 0.1148 -0.1667 0.1265 139 CYS B SG 5229 N N . LYS B 140 ? 0.7067 1.6063 0.8210 0.0650 -0.1979 0.0842 140 LYS B N 5230 C CA . LYS B 140 ? 0.7281 1.6595 0.8433 0.0484 -0.2083 0.0675 140 LYS B CA 5231 C C . LYS B 140 ? 0.6453 1.5863 0.7852 0.0336 -0.2059 0.0538 140 LYS B C 5232 O O . LYS B 140 ? 0.5688 1.5188 0.7088 0.0143 -0.2104 0.0369 140 LYS B O 5233 C CB . LYS B 140 ? 0.7024 1.6819 0.8173 0.0586 -0.2234 0.0740 140 LYS B CB 5234 C CG . LYS B 140 ? 0.5564 1.5715 0.6996 0.0708 -0.2277 0.0821 140 LYS B CG 5235 C CD . LYS B 140 ? 0.4812 1.5490 0.6256 0.0746 -0.2448 0.0822 140 LYS B CD 5236 C CE . LYS B 140 ? 0.4927 1.5896 0.6558 0.0971 -0.2492 0.0997 140 LYS B CE 5237 N NZ . LYS B 140 ? 0.5150 1.6649 0.6777 0.1026 -0.2671 0.1013 140 LYS B NZ 5238 N N . GLU B 141 ? 0.6152 1.5538 0.7760 0.0428 -0.1985 0.0611 141 GLU B N 5239 C CA . GLU B 141 ? 0.6160 1.5690 0.8015 0.0307 -0.1955 0.0506 141 GLU B CA 5240 C C . GLU B 141 ? 0.6575 1.5720 0.8372 0.0124 -0.1852 0.0382 141 GLU B C 5241 O O . GLU B 141 ? 0.6400 1.5648 0.8357 -0.0030 -0.1834 0.0272 141 GLU B O 5242 C CB . GLU B 141 ? 0.5980 1.5619 0.8069 0.0475 -0.1901 0.0618 141 GLU B CB 5243 C CG . GLU B 141 ? 0.5867 1.5995 0.8106 0.0626 -0.2015 0.0709 141 GLU B CG 5244 C CD . GLU B 141 ? 0.7931 1.7980 1.0022 0.0849 -0.2045 0.0889 141 GLU B CD 5245 O OE1 . GLU B 141 ? 0.8353 1.7976 1.0235 0.0871 -0.1975 0.0937 141 GLU B OE1 5246 O OE2 . GLU B 141 ? 0.8572 1.8989 1.0766 0.1001 -0.2139 0.0989 141 GLU B OE2 5247 N N . PHE B 142 ? 0.6671 1.5382 0.8247 0.0142 -0.1783 0.0408 142 PHE B N 5248 C CA . PHE B 142 ? 0.6459 1.4780 0.7955 -0.0014 -0.1691 0.0300 142 PHE B CA 5249 C C . PHE B 142 ? 0.5063 1.3495 0.6550 -0.0241 -0.1752 0.0125 142 PHE B C 5250 O O . PHE B 142 ? 0.5234 1.3390 0.6687 -0.0388 -0.1688 0.0025 142 PHE B O 5251 C CB . PHE B 142 ? 0.7166 1.5067 0.8417 0.0041 -0.1635 0.0351 142 PHE B CB 5252 C CG . PHE B 142 ? 0.7111 1.4755 0.8388 0.0209 -0.1541 0.0486 142 PHE B CG 5253 C CD1 . PHE B 142 ? 0.5677 1.2868 0.6845 0.0186 -0.1440 0.0476 142 PHE B CD1 5254 C CD2 . PHE B 142 ? 0.6813 1.4666 0.8232 0.0393 -0.1557 0.0618 142 PHE B CD2 5255 C CE1 . PHE B 142 ? 0.5148 1.2098 0.6348 0.0334 -0.1361 0.0587 142 PHE B CE1 5256 C CE2 . PHE B 142 ? 0.6610 1.4204 0.8059 0.0547 -0.1474 0.0731 142 PHE B CE2 5257 C CZ . PHE B 142 ? 0.5732 1.2873 0.7071 0.0513 -0.1378 0.0711 142 PHE B CZ 5258 N N . GLY B 143 ? 0.5385 1.4218 0.6903 -0.0266 -0.1882 0.0086 143 GLY B N 5259 C CA . GLY B 143 ? 0.5907 1.4870 0.7438 -0.0481 -0.1956 -0.0090 143 GLY B CA 5260 C C . GLY B 143 ? 0.7079 1.6173 0.8875 -0.0620 -0.1921 -0.0159 143 GLY B C 5261 O O . GLY B 143 ? 0.7709 1.6729 0.9519 -0.0826 -0.1929 -0.0303 143 GLY B O 5262 N N . ASN B 144 ? 0.7350 1.6634 0.9359 -0.0505 -0.1879 -0.0055 144 ASN B N 5263 C CA . ASN B 144 ? 0.6736 1.6205 0.9021 -0.0613 -0.1834 -0.0096 144 ASN B CA 5264 C C . ASN B 144 ? 0.5499 1.4547 0.7756 -0.0710 -0.1690 -0.0127 144 ASN B C 5265 O O . ASN B 144 ? 0.4972 1.4102 0.7410 -0.0853 -0.1644 -0.0183 144 ASN B O 5266 C CB . ASN B 144 ? 0.7321 1.7133 0.9833 -0.0434 -0.1827 0.0026 144 ASN B CB 5267 C CG . ASN B 144 ? 0.7426 1.7551 1.0250 -0.0549 -0.1798 -0.0020 144 ASN B CG 5268 O OD1 . ASN B 144 ? 0.6461 1.6736 0.9373 -0.0761 -0.1850 -0.0142 144 ASN B OD1 5269 N ND2 . ASN B 144 ? 0.8769 1.8993 1.1767 -0.0407 -0.1712 0.0076 144 ASN B ND2 5270 N N . LEU B 145 ? 0.4993 1.3604 0.7026 -0.0630 -0.1621 -0.0083 145 LEU B N 5271 C CA . LEU B 145 ? 0.5265 1.3451 0.7233 -0.0704 -0.1496 -0.0109 145 LEU B CA 5272 C C . LEU B 145 ? 0.5801 1.3811 0.7685 -0.0931 -0.1516 -0.0254 145 LEU B C 5273 O O . LEU B 145 ? 0.6395 1.4005 0.8076 -0.0957 -0.1476 -0.0284 145 LEU B O 5274 C CB . LEU B 145 ? 0.4944 1.2737 0.6711 -0.0548 -0.1431 -0.0024 145 LEU B CB 5275 C CG . LEU B 145 ? 0.5695 1.3564 0.7511 -0.0309 -0.1411 0.0123 145 LEU B CG 5276 C CD1 . LEU B 145 ? 0.5448 1.2857 0.7107 -0.0211 -0.1318 0.0182 145 LEU B CD1 5277 C CD2 . LEU B 145 ? 0.6175 1.4328 0.8250 -0.0264 -0.1372 0.0157 145 LEU B CD2 5278 N N . THR B 146 ? 0.5016 1.3324 0.7070 -0.1096 -0.1578 -0.0343 146 THR B N 5279 C CA . THR B 146 ? 0.5634 1.3795 0.7636 -0.1320 -0.1609 -0.0489 146 THR B CA 5280 C C . THR B 146 ? 0.6220 1.3927 0.8149 -0.1407 -0.1486 -0.0505 146 THR B C 5281 O O . THR B 146 ? 0.6298 1.3709 0.8074 -0.1518 -0.1496 -0.0600 146 THR B O 5282 C CB . THR B 146 ? 0.6247 1.4814 0.8501 -0.1493 -0.1685 -0.0573 146 THR B CB 5283 O OG1 . THR B 146 ? 0.7789 1.6206 1.0163 -0.1667 -0.1595 -0.0609 146 THR B OG1 5284 C CG2 . THR B 146 ? 0.3974 1.3029 0.6451 -0.1367 -0.1719 -0.0482 146 THR B CG2 5285 N N . LYS B 147 ? 0.7165 1.4822 0.9196 -0.1347 -0.1372 -0.0416 147 LYS B N 5286 C CA . LYS B 147 ? 0.7069 1.4329 0.9036 -0.1422 -0.1255 -0.0420 147 LYS B CA 5287 C C . LYS B 147 ? 0.6760 1.3583 0.8477 -0.1298 -0.1205 -0.0384 147 LYS B C 5288 O O . LYS B 147 ? 0.5602 1.2068 0.7233 -0.1349 -0.1123 -0.0394 147 LYS B O 5289 C CB . LYS B 147 ? 0.7254 1.4642 0.9412 -0.1405 -0.1149 -0.0345 147 LYS B CB 5290 C CG . LYS B 147 ? 0.3381 1.1042 0.5780 -0.1609 -0.1146 -0.0392 147 LYS B CG 5291 C CD . LYS B 147 ? 1.7597 2.5436 2.0180 -0.1554 -0.1029 -0.0300 147 LYS B CD 5292 C CE . LYS B 147 ? 0.8019 1.6311 1.0909 -0.1702 -0.1040 -0.0317 147 LYS B CE 5293 N NZ . LYS B 147 ? 0.7143 1.5955 1.0235 -0.1588 -0.1113 -0.0284 147 LYS B NZ 5294 N N . LEU B 148 ? 0.6888 1.3746 0.8496 -0.1140 -0.1257 -0.0338 148 LEU B N 5295 C CA . LEU B 148 ? 0.6927 1.3421 0.8337 -0.1005 -0.1205 -0.0283 148 LEU B CA 5296 C C . LEU B 148 ? 0.7096 1.3214 0.8312 -0.1105 -0.1202 -0.0371 148 LEU B C 5297 O O . LEU B 148 ? 0.7713 1.3883 0.8864 -0.1201 -0.1283 -0.0465 148 LEU B O 5298 C CB . LEU B 148 ? 0.6380 1.3016 0.7729 -0.0823 -0.1262 -0.0201 148 LEU B CB 5299 C CG . LEU B 148 ? 0.6015 1.2294 0.7205 -0.0681 -0.1198 -0.0125 148 LEU B CG 5300 C CD1 . LEU B 148 ? 0.3884 1.0052 0.5168 -0.0597 -0.1098 -0.0057 148 LEU B CD1 5301 C CD2 . LEU B 148 ? 0.6514 1.2901 0.7623 -0.0520 -0.1254 -0.0037 148 LEU B CD2 5302 N N . THR B 149 ? 0.6753 1.2498 0.7875 -0.1071 -0.1111 -0.0344 149 THR B N 5303 C CA . THR B 149 ? 0.7165 1.2542 0.8116 -0.1152 -0.1100 -0.0421 149 THR B CA 5304 C C . THR B 149 ? 0.6773 1.1845 0.7563 -0.1011 -0.1057 -0.0364 149 THR B C 5305 O O . THR B 149 ? 0.6196 1.1064 0.6831 -0.1029 -0.1077 -0.0418 149 THR B O 5306 C CB . THR B 149 ? 0.6999 1.2189 0.7996 -0.1304 -0.1042 -0.0470 149 THR B CB 5307 O OG1 . THR B 149 ? 0.8754 1.3779 0.9661 -0.1447 -0.1087 -0.0588 149 THR B OG1 5308 C CG2 . THR B 149 ? 0.6063 1.0927 0.6993 -0.1227 -0.0941 -0.0409 149 THR B CG2 5309 N N . PHE B 150 ? 0.5415 1.0462 0.6250 -0.0871 -0.0999 -0.0261 150 PHE B N 5310 C CA . PHE B 150 ? 0.5921 1.0712 0.6637 -0.0737 -0.0965 -0.0201 150 PHE B CA 5311 C C . PHE B 150 ? 0.6683 1.1680 0.7442 -0.0571 -0.0989 -0.0094 150 PHE B C 5312 O O . PHE B 150 ? 0.6839 1.2046 0.7740 -0.0502 -0.0978 -0.0036 150 PHE B O 5313 C CB . PHE B 150 ? 0.6584 1.1095 0.7299 -0.0707 -0.0876 -0.0178 150 PHE B CB 5314 C CG . PHE B 150 ? 0.6166 1.0432 0.6796 -0.0570 -0.0843 -0.0116 150 PHE B CG 5315 C CD1 . PHE B 150 ? 0.5044 0.8968 0.5550 -0.0600 -0.0815 -0.0156 150 PHE B CD1 5316 C CD2 . PHE B 150 ? 0.6736 1.1111 0.7425 -0.0412 -0.0841 -0.0017 150 PHE B CD2 5317 C CE1 . PHE B 150 ? 0.5736 0.9448 0.6187 -0.0485 -0.0788 -0.0101 150 PHE B CE1 5318 C CE2 . PHE B 150 ? 0.7905 1.2044 0.8536 -0.0298 -0.0812 0.0041 150 PHE B CE2 5319 C CZ . PHE B 150 ? 0.7192 1.1006 0.7708 -0.0340 -0.0785 -0.0003 150 PHE B CZ 5320 N N . LEU B 151 ? 0.6013 1.0946 0.6649 -0.0503 -0.1018 -0.0063 151 LEU B N 5321 C CA . LEU B 151 ? 0.4890 0.9977 0.5547 -0.0342 -0.1040 0.0056 151 LEU B CA 5322 C C . LEU B 151 ? 0.5007 0.9794 0.5561 -0.0241 -0.0995 0.0125 151 LEU B C 5323 O O . LEU B 151 ? 0.5217 0.9824 0.5635 -0.0290 -0.0992 0.0081 151 LEU B O 5324 C CB . LEU B 151 ? 0.5010 1.0410 0.5631 -0.0356 -0.1134 0.0048 151 LEU B CB 5325 C CG . LEU B 151 ? 0.5548 1.1135 0.6185 -0.0186 -0.1166 0.0187 151 LEU B CG 5326 C CD1 . LEU B 151 ? 0.5964 1.1621 0.6774 -0.0074 -0.1129 0.0272 151 LEU B CD1 5327 C CD2 . LEU B 151 ? 0.4577 1.0535 0.5195 -0.0207 -0.1269 0.0169 151 LEU B CD2 5328 N N . GLY B 152 ? 0.5266 1.0000 0.5897 -0.0102 -0.0957 0.0228 152 GLY B N 5329 C CA . GLY B 152 ? 0.5781 1.0229 0.6352 -0.0011 -0.0913 0.0297 152 GLY B CA 5330 C C . GLY B 152 ? 0.7603 1.2184 0.8206 0.0141 -0.0937 0.0439 152 GLY B C 5331 O O . GLY B 152 ? 0.8667 1.3425 0.9397 0.0232 -0.0948 0.0499 152 GLY B O 5332 N N . LEU B 153 ? 0.7529 1.2030 0.8021 0.0172 -0.0941 0.0498 153 LEU B N 5333 C CA . LEU B 153 ? 0.6604 1.1243 0.7105 0.0307 -0.0967 0.0648 153 LEU B CA 5334 C C . LEU B 153 ? 0.7202 1.1570 0.7650 0.0375 -0.0918 0.0746 153 LEU B C 5335 O O . LEU B 153 ? 0.5649 0.9773 0.6022 0.0303 -0.0877 0.0685 153 LEU B O 5336 C CB . LEU B 153 ? 0.6904 1.1855 0.7310 0.0274 -0.1042 0.0644 153 LEU B CB 5337 C CG . LEU B 153 ? 0.6766 1.2013 0.7249 0.0198 -0.1100 0.0549 153 LEU B CG 5338 C CD1 . LEU B 153 ? 0.6344 1.1843 0.6709 0.0127 -0.1177 0.0493 153 LEU B CD1 5339 C CD2 . LEU B 153 ? 0.7252 1.2713 0.7901 0.0322 -0.1121 0.0643 153 LEU B CD2 5340 N N . SER B 154 ? 0.7860 1.2274 0.8361 0.0515 -0.0923 0.0902 154 SER B N 5341 C CA . SER B 154 ? 0.7245 1.1447 0.7706 0.0577 -0.0881 0.1021 154 SER B CA 5342 C C . SER B 154 ? 0.7758 1.2150 0.8216 0.0703 -0.0915 0.1199 154 SER B C 5343 O O . SER B 154 ? 0.7774 1.2390 0.8318 0.0785 -0.0962 0.1248 154 SER B O 5344 C CB . SER B 154 ? 0.7010 1.0886 0.7586 0.0623 -0.0823 0.1034 154 SER B CB 5345 O OG . SER B 154 ? 0.8450 1.2364 0.9163 0.0762 -0.0833 0.1137 154 SER B OG 5346 N N . ALA B 155 ? 0.8098 1.2406 0.8461 0.0724 -0.0888 0.1305 155 ALA B N 5347 C CA . ALA B 155 ? 0.7571 1.2053 0.7902 0.0840 -0.0915 0.1492 155 ALA B CA 5348 C C . ALA B 155 ? 0.7587 1.1883 0.7844 0.0855 -0.0854 0.1617 155 ALA B C 5349 O O . ALA B 155 ? 0.8021 1.2096 0.8245 0.0766 -0.0798 0.1539 155 ALA B O 5350 C CB . ALA B 155 ? 0.7331 1.2191 0.7540 0.0814 -0.0993 0.1458 155 ALA B CB 5351 N N . ALA B 156 ? 0.8085 1.2481 0.8323 0.0970 -0.0864 0.1819 156 ALA B N 5352 C CA . ALA B 156 ? 0.8531 1.2788 0.8707 0.0992 -0.0801 0.1974 156 ALA B CA 5353 C C . ALA B 156 ? 0.9197 1.3750 0.9164 0.1006 -0.0827 0.2061 156 ALA B C 5354 O O . ALA B 156 ? 0.9932 1.4426 0.9804 0.1003 -0.0768 0.2171 156 ALA B O 5355 C CB . ALA B 156 ? 0.8263 1.2331 0.8600 0.1118 -0.0776 0.2164 156 ALA B CB 5356 N N . LYS B 157 ? 0.7712 1.2595 0.7611 0.1020 -0.0916 0.2007 157 LYS B N 5357 C CA . LYS B 157 ? 0.7836 1.3035 0.7525 0.1038 -0.0959 0.2063 157 LYS B CA 5358 C C . LYS B 157 ? 0.7705 1.3144 0.7301 0.0935 -0.1033 0.1841 157 LYS B C 5359 O O . LYS B 157 ? 0.8201 1.3692 0.7922 0.0908 -0.1081 0.1723 157 LYS B O 5360 C CB . LYS B 157 ? 0.8192 1.3613 0.7900 0.1194 -0.1021 0.2265 157 LYS B CB 5361 C CG . LYS B 157 ? 0.8268 1.3491 0.8056 0.1314 -0.0964 0.2521 157 LYS B CG 5362 C CD . LYS B 157 ? 0.9771 1.5281 0.9524 0.1466 -0.1041 0.2711 157 LYS B CD 5363 C CE . LYS B 157 ? 1.0703 1.6012 1.0629 0.1610 -0.1015 0.2937 157 LYS B CE 5364 N NZ . LYS B 157 ? 1.0546 1.6159 1.0443 0.1766 -0.1104 0.3108 157 LYS B NZ 5365 N N . PHE B 158 ? 0.7086 1.2686 0.6466 0.0881 -0.1042 0.1787 158 PHE B N 5366 C CA . PHE B 158 ? 0.7369 1.3204 0.6655 0.0783 -0.1122 0.1574 158 PHE B CA 5367 C C . PHE B 158 ? 0.8059 1.4270 0.7127 0.0821 -0.1198 0.1604 158 PHE B C 5368 O O . PHE B 158 ? 0.9888 1.6125 0.8780 0.0858 -0.1154 0.1707 158 PHE B O 5369 C CB . PHE B 158 ? 0.7079 1.2693 0.6330 0.0637 -0.1067 0.1370 158 PHE B CB 5370 C CG . PHE B 158 ? 0.7540 1.2816 0.6989 0.0598 -0.1007 0.1324 158 PHE B CG 5371 C CD1 . PHE B 158 ? 0.8055 1.3024 0.7552 0.0614 -0.0909 0.1414 158 PHE B CD1 5372 C CD2 . PHE B 158 ? 0.7458 1.2739 0.7050 0.0546 -0.1050 0.1196 158 PHE B CD2 5373 C CE1 . PHE B 158 ? 0.7622 1.2290 0.7293 0.0583 -0.0864 0.1362 158 PHE B CE1 5374 C CE2 . PHE B 158 ? 0.6835 1.1817 0.6587 0.0519 -0.0995 0.1154 158 PHE B CE2 5375 C CZ . PHE B 158 ? 0.6348 1.1024 0.6135 0.0540 -0.0907 0.1233 158 PHE B CZ 5376 N N . ARG B 159 ? 0.7178 1.3695 0.6261 0.0814 -0.1313 0.1517 159 ARG B N 5377 C CA . ARG B 159 ? 0.7611 1.4499 0.6479 0.0827 -0.1404 0.1489 159 ARG B CA 5378 C C . ARG B 159 ? 0.7304 1.4300 0.6127 0.0675 -0.1469 0.1207 159 ARG B C 5379 O O . ARG B 159 ? 0.7476 1.4348 0.6472 0.0582 -0.1471 0.1069 159 ARG B O 5380 C CB . ARG B 159 ? 0.7509 1.4721 0.6411 0.0964 -0.1502 0.1646 159 ARG B CB 5381 C CG . ARG B 159 ? 0.9159 1.6339 0.8010 0.1125 -0.1455 0.1940 159 ARG B CG 5382 C CD . ARG B 159 ? 1.1949 1.8796 1.1036 0.1182 -0.1374 0.2071 159 ARG B CD 5383 N NE . ARG B 159 ? 1.4812 2.1698 1.4136 0.1179 -0.1430 0.1985 159 ARG B NE 5384 C CZ . ARG B 159 ? 1.6050 2.3213 1.5464 0.1289 -0.1524 0.2071 159 ARG B CZ 5385 N NH1 . ARG B 159 ? 1.6644 2.4066 1.5921 0.1414 -0.1582 0.2250 159 ARG B NH1 5386 N NH2 . ARG B 159 ? 1.4463 2.1658 1.4103 0.1278 -0.1559 0.1981 159 ARG B NH2 5387 N N . GLN B 160 ? 0.8701 1.5923 0.7290 0.0649 -0.1521 0.1121 160 GLN B N 5388 C CA . GLN B 160 ? 0.9668 1.6914 0.8198 0.0494 -0.1564 0.0843 160 GLN B CA 5389 C C . GLN B 160 ? 0.9741 1.7086 0.8479 0.0409 -0.1649 0.0704 160 GLN B C 5390 O O . GLN B 160 ? 0.9916 1.7096 0.8729 0.0270 -0.1637 0.0511 160 GLN B O 5391 C CB . GLN B 160 ? 0.9919 1.7466 0.8171 0.0498 -0.1638 0.0763 160 GLN B CB 5392 C CG . GLN B 160 ? 1.0910 1.8384 0.9077 0.0343 -0.1652 0.0477 160 GLN B CG 5393 C CD . GLN B 160 ? 1.0871 1.8703 0.8820 0.0326 -0.1773 0.0335 160 GLN B CD 5394 O OE1 . GLN B 160 ? 0.7880 1.6058 0.5773 0.0414 -0.1871 0.0429 160 GLN B OE1 5395 N NE2 . GLN B 160 ? 1.2090 1.9839 0.9917 0.0215 -0.1773 0.0098 160 GLN B NE2 5396 N N . LEU B 161 ? 0.9762 1.7379 0.8602 0.0499 -0.1731 0.0816 161 LEU B N 5397 C CA . LEU B 161 ? 0.8117 1.5946 0.7136 0.0424 -0.1831 0.0686 161 LEU B CA 5398 C C . LEU B 161 ? 0.6901 1.4573 0.6208 0.0429 -0.1786 0.0734 161 LEU B C 5399 O O . LEU B 161 ? 0.6507 1.4389 0.5985 0.0387 -0.1860 0.0662 161 LEU B O 5400 C CB . LEU B 161 ? 0.6933 1.5227 0.5896 0.0515 -0.1968 0.0750 161 LEU B CB 5401 C CG . LEU B 161 ? 0.6983 1.5534 0.5697 0.0464 -0.2061 0.0607 161 LEU B CG 5402 C CD1 . LEU B 161 ? 0.5183 1.4215 0.3915 0.0526 -0.2219 0.0629 161 LEU B CD1 5403 C CD2 . LEU B 161 ? 0.4968 1.3384 0.3694 0.0268 -0.2066 0.0327 161 LEU B CD2 5404 N N . ASP B 162 ? 0.7361 1.4678 0.6724 0.0478 -0.1665 0.0848 162 ASP B N 5405 C CA . ASP B 162 ? 0.8000 1.5186 0.7614 0.0522 -0.1623 0.0920 162 ASP B CA 5406 C C . ASP B 162 ? 0.7397 1.4559 0.7186 0.0379 -0.1634 0.0732 162 ASP B C 5407 O O . ASP B 162 ? 0.6963 1.4248 0.6956 0.0414 -0.1656 0.0761 162 ASP B O 5408 C CB . ASP B 162 ? 0.8365 1.5156 0.8002 0.0590 -0.1496 0.1055 162 ASP B CB 5409 C CG . ASP B 162 ? 1.0024 1.6866 0.9616 0.0770 -0.1487 0.1308 162 ASP B CG 5410 O OD1 . ASP B 162 ? 0.8564 1.5751 0.8104 0.0857 -0.1580 0.1390 162 ASP B OD1 5411 O OD2 . ASP B 162 ? 1.1710 1.8242 1.1324 0.0825 -0.1390 0.1429 162 ASP B OD2 5412 N N . LEU B 163 ? 0.7432 1.4446 0.7141 0.0222 -0.1617 0.0546 163 LEU B N 5413 C CA . LEU B 163 ? 0.6389 1.3351 0.6254 0.0075 -0.1618 0.0379 163 LEU B CA 5414 C C . LEU B 163 ? 0.6906 1.4205 0.6782 -0.0040 -0.1738 0.0218 163 LEU B C 5415 O O . LEU B 163 ? 0.6464 1.3685 0.6398 -0.0199 -0.1740 0.0047 163 LEU B O 5416 C CB . LEU B 163 ? 0.3869 1.0426 0.3679 -0.0031 -0.1524 0.0274 163 LEU B CB 5417 C CG . LEU B 163 ? 0.5337 1.1547 0.5179 0.0057 -0.1409 0.0404 163 LEU B CG 5418 C CD1 . LEU B 163 ? 0.3589 0.9431 0.3353 -0.0041 -0.1330 0.0299 163 LEU B CD1 5419 C CD2 . LEU B 163 ? 0.5433 1.1637 0.5501 0.0104 -0.1387 0.0466 163 LEU B CD2 5420 N N . LEU B 164 ? 0.7233 1.4907 0.7060 0.0040 -0.1841 0.0275 164 LEU B N 5421 C CA . LEU B 164 ? 0.7651 1.5670 0.7476 -0.0066 -0.1970 0.0117 164 LEU B CA 5422 C C . LEU B 164 ? 0.7546 1.5729 0.7649 -0.0155 -0.2005 0.0046 164 LEU B C 5423 O O . LEU B 164 ? 0.7417 1.5674 0.7570 -0.0324 -0.2057 -0.0140 164 LEU B O 5424 C CB . LEU B 164 ? 0.7454 1.5855 0.7150 0.0057 -0.2079 0.0207 164 LEU B CB 5425 C CG . LEU B 164 ? 0.7509 1.6105 0.6997 -0.0028 -0.2181 0.0040 164 LEU B CG 5426 C CD1 . LEU B 164 ? 0.5628 1.4733 0.5115 0.0034 -0.2337 0.0060 164 LEU B CD1 5427 C CD2 . LEU B 164 ? 0.8596 1.7057 0.8144 -0.0243 -0.2188 -0.0207 164 LEU B CD2 5428 N N . PRO B 165 ? 0.7158 1.5400 0.7452 -0.0042 -0.1972 0.0192 165 PRO B N 5429 C CA . PRO B 165 ? 0.7612 1.6030 0.8177 -0.0119 -0.1991 0.0132 165 PRO B CA 5430 C C . PRO B 165 ? 0.7361 1.5496 0.8005 -0.0302 -0.1915 -0.0014 165 PRO B C 5431 O O . PRO B 165 ? 0.6758 1.5081 0.7590 -0.0424 -0.1951 -0.0112 165 PRO B O 5432 C CB . PRO B 165 ? 0.7666 1.6095 0.8381 0.0062 -0.1937 0.0324 165 PRO B CB 5433 C CG . PRO B 165 ? 0.7462 1.5935 0.7998 0.0237 -0.1965 0.0485 165 PRO B CG 5434 C CD . PRO B 165 ? 0.6712 1.4927 0.6987 0.0169 -0.1934 0.0418 165 PRO B CD 5435 N N . VAL B 166 ? 0.6812 1.4516 0.7326 -0.0324 -0.1813 -0.0024 166 VAL B N 5436 C CA . VAL B 166 ? 0.7376 1.4812 0.7951 -0.0491 -0.1748 -0.0155 166 VAL B CA 5437 C C . VAL B 166 ? 0.8034 1.5325 0.8441 -0.0642 -0.1777 -0.0330 166 VAL B C 5438 O O . VAL B 166 ? 0.8223 1.5211 0.8634 -0.0761 -0.1714 -0.0422 166 VAL B O 5439 C CB . VAL B 166 ? 0.6085 1.3134 0.6694 -0.0433 -0.1610 -0.0068 166 VAL B CB 5440 C CG1 . VAL B 166 ? 0.7274 1.4472 0.8078 -0.0301 -0.1583 0.0068 166 VAL B CG1 5441 C CG2 . VAL B 166 ? 0.4319 1.1061 0.4720 -0.0341 -0.1552 0.0002 166 VAL B CG2 5442 N N . ALA B 167 ? 0.7695 1.5210 0.7956 -0.0633 -0.1878 -0.0380 167 ALA B N 5443 C CA . ALA B 167 ? 0.7899 1.5289 0.7980 -0.0752 -0.1911 -0.0553 167 ALA B CA 5444 C C . ALA B 167 ? 0.7922 1.5388 0.8128 -0.0959 -0.1973 -0.0747 167 ALA B C 5445 O O . ALA B 167 ? 0.7671 1.4978 0.7759 -0.1074 -0.1993 -0.0909 167 ALA B O 5446 C CB . ALA B 167 ? 0.8640 1.6260 0.8510 -0.0664 -0.1996 -0.0546 167 ALA B CB 5447 N N . HIS B 168 ? 0.8366 1.6072 0.8819 -0.1006 -0.2002 -0.0729 168 HIS B N 5448 C CA . HIS B 168 ? 0.9462 1.7265 1.0066 -0.1213 -0.2061 -0.0899 168 HIS B CA 5449 C C . HIS B 168 ? 1.0916 1.8528 1.1725 -0.1310 -0.1963 -0.0884 168 HIS B C 5450 O O . HIS B 168 ? 1.2212 2.0000 1.3224 -0.1460 -0.2003 -0.0964 168 HIS B O 5451 C CB . HIS B 168 ? 0.9041 1.7361 0.9781 -0.1228 -0.2200 -0.0927 168 HIS B CB 5452 C CG . HIS B 168 ? 0.9174 1.7715 0.9705 -0.1169 -0.2319 -0.0982 168 HIS B CG 5453 N ND1 . HIS B 168 ? 0.8940 1.7612 0.9422 -0.1315 -0.2437 -0.1189 168 HIS B ND1 5454 C CD2 . HIS B 168 ? 0.9615 1.8270 0.9965 -0.0979 -0.2338 -0.0856 168 HIS B CD2 5455 C CE1 . HIS B 168 ? 1.0002 1.8874 1.0270 -0.1210 -0.2525 -0.1194 168 HIS B CE1 5456 N NE2 . HIS B 168 ? 1.0308 1.9176 1.0491 -0.1007 -0.2464 -0.0985 168 HIS B NE2 5457 N N . LEU B 169 ? 1.0469 1.7735 1.1229 -0.1228 -0.1835 -0.0780 169 LEU B N 5458 C CA . LEU B 169 ? 0.9387 1.6442 1.0300 -0.1308 -0.1734 -0.0762 169 LEU B CA 5459 C C . LEU B 169 ? 1.0914 1.7523 1.1692 -0.1408 -0.1675 -0.0857 169 LEU B C 5460 O O . LEU B 169 ? 1.2618 1.9038 1.3182 -0.1354 -0.1676 -0.0885 169 LEU B O 5461 C CB . LEU B 169 ? 0.7028 1.4019 0.7993 -0.1139 -0.1637 -0.0584 169 LEU B CB 5462 C CG . LEU B 169 ? 0.6369 1.3750 0.7426 -0.0985 -0.1691 -0.0465 169 LEU B CG 5463 C CD1 . LEU B 169 ? 0.5523 1.2741 0.6557 -0.0792 -0.1599 -0.0298 169 LEU B CD1 5464 C CD2 . LEU B 169 ? 0.3365 1.1117 0.4691 -0.1067 -0.1731 -0.0486 169 LEU B CD2 5465 N N . HIS B 170 ? 1.0098 1.6546 1.1001 -0.1547 -0.1620 -0.0899 170 HIS B N 5466 C CA . HIS B 170 ? 1.0987 1.7005 1.1774 -0.1638 -0.1567 -0.0982 170 HIS B CA 5467 C C . HIS B 170 ? 0.9753 1.5439 1.0475 -0.1525 -0.1443 -0.0863 170 HIS B C 5468 O O . HIS B 170 ? 0.8863 1.4353 0.9663 -0.1585 -0.1363 -0.0840 170 HIS B O 5469 C CB . HIS B 170 ? 1.2742 1.8729 1.3673 -0.1859 -0.1583 -0.1097 170 HIS B CB 5470 C CG . HIS B 170 ? 1.3975 2.0216 1.4938 -0.1982 -0.1716 -0.1248 170 HIS B CG 5471 N ND1 . HIS B 170 ? 1.3901 2.0600 1.5040 -0.2006 -0.1799 -0.1245 170 HIS B ND1 5472 C CD2 . HIS B 170 ? 1.4552 2.0662 1.5393 -0.2079 -0.1786 -0.1416 170 HIS B CD2 5473 C CE1 . HIS B 170 ? 1.3842 2.0683 1.4965 -0.2121 -0.1919 -0.1407 170 HIS B CE1 5474 N NE2 . HIS B 170 ? 1.4161 2.0643 1.5101 -0.2166 -0.1912 -0.1517 170 HIS B NE2 5475 N N . LEU B 171 ? 0.7553 1.3190 0.8128 -0.1359 -0.1431 -0.0788 171 LEU B N 5476 C CA . LEU B 171 ? 0.7541 1.2903 0.8058 -0.1235 -0.1330 -0.0675 171 LEU B CA 5477 C C . LEU B 171 ? 0.8312 1.3245 0.8720 -0.1298 -0.1270 -0.0739 171 LEU B C 5478 O O . LEU B 171 ? 0.7805 1.2628 0.8111 -0.1386 -0.1311 -0.0864 171 LEU B O 5479 C CB . LEU B 171 ? 0.7294 1.2722 0.7690 -0.1059 -0.1340 -0.0582 171 LEU B CB 5480 C CG . LEU B 171 ? 0.7457 1.3252 0.7957 -0.0944 -0.1380 -0.0470 171 LEU B CG 5481 C CD1 . LEU B 171 ? 0.7578 1.3414 0.7926 -0.0796 -0.1400 -0.0390 171 LEU B CD1 5482 C CD2 . LEU B 171 ? 0.7966 1.3736 0.8619 -0.0871 -0.1302 -0.0358 171 LEU B CD2 5483 N N . SER B 172 ? 0.7777 1.2475 0.8204 -0.1243 -0.1178 -0.0657 172 SER B N 5484 C CA . SER B 172 ? 0.7239 1.1533 0.7568 -0.1275 -0.1119 -0.0695 172 SER B CA 5485 C C . SER B 172 ? 0.8157 1.2246 0.8376 -0.1122 -0.1066 -0.0612 172 SER B C 5486 O O . SER B 172 ? 0.7958 1.1787 0.8053 -0.1123 -0.1049 -0.0662 172 SER B O 5487 C CB . SER B 172 ? 0.6925 1.1086 0.7357 -0.1362 -0.1059 -0.0684 172 SER B CB 5488 O OG . SER B 172 ? 0.8124 1.2268 0.8596 -0.1540 -0.1096 -0.0795 172 SER B OG 5489 N N . CYS B 173 ? 0.7348 1.1554 0.7627 -0.0990 -0.1039 -0.0489 173 CYS B N 5490 C CA . CYS B 173 ? 0.6473 1.0518 0.6666 -0.0850 -0.1000 -0.0407 173 CYS B CA 5491 C C . CYS B 173 ? 0.6228 1.0527 0.6446 -0.0718 -0.1026 -0.0300 173 CYS B C 5492 O O . CYS B 173 ? 0.6436 1.0961 0.6780 -0.0679 -0.1036 -0.0240 173 CYS B O 5493 C CB . CYS B 173 ? 0.5836 0.9605 0.6055 -0.0804 -0.0920 -0.0357 173 CYS B CB 5494 S SG . CYS B 173 ? 0.8546 1.2044 0.8661 -0.0677 -0.0876 -0.0295 173 CYS B SG 5495 N N . ILE B 174 ? 0.6089 1.0354 0.6186 -0.0648 -0.1034 -0.0273 174 ILE B N 5496 C CA . ILE B 174 ? 0.6067 1.0481 0.6165 -0.0503 -0.1040 -0.0140 174 ILE B CA 5497 C C . ILE B 174 ? 0.6674 1.0796 0.6732 -0.0413 -0.0969 -0.0065 174 ILE B C 5498 O O . ILE B 174 ? 0.6873 1.0828 0.6816 -0.0425 -0.0950 -0.0098 174 ILE B O 5499 C CB . ILE B 174 ? 0.5666 1.0316 0.5651 -0.0490 -0.1108 -0.0151 174 ILE B CB 5500 C CG1 . ILE B 174 ? 0.6112 1.1083 0.6158 -0.0576 -0.1192 -0.0227 174 ILE B CG1 5501 C CG2 . ILE B 174 ? 0.4343 0.9101 0.4311 -0.0332 -0.1103 0.0011 174 ILE B CG2 5502 C CD1 . ILE B 174 ? 0.6296 1.1586 0.6270 -0.0516 -0.1269 -0.0192 174 ILE B CD1 5503 N N . LEU B 175 ? 0.7134 1.1196 0.7299 -0.0325 -0.0930 0.0027 175 LEU B N 5504 C CA . LEU B 175 ? 0.7182 1.0988 0.7336 -0.0237 -0.0872 0.0103 175 LEU B CA 5505 C C . LEU B 175 ? 0.7706 1.1655 0.7870 -0.0107 -0.0884 0.0245 175 LEU B C 5506 O O . LEU B 175 ? 0.8312 1.2478 0.8567 -0.0041 -0.0912 0.0312 175 LEU B O 5507 C CB . LEU B 175 ? 0.5586 0.9213 0.5843 -0.0214 -0.0825 0.0108 175 LEU B CB 5508 C CG . LEU B 175 ? 0.4824 0.8207 0.5093 -0.0116 -0.0778 0.0186 175 LEU B CG 5509 C CD1 . LEU B 175 ? 0.5230 0.8374 0.5399 -0.0170 -0.0754 0.0131 175 LEU B CD1 5510 C CD2 . LEU B 175 ? 0.4957 0.8213 0.5326 -0.0066 -0.0743 0.0196 175 LEU B CD2 5511 N N . LEU B 176 ? 0.6936 1.0772 0.7013 -0.0068 -0.0860 0.0297 176 LEU B N 5512 C CA . LEU B 176 ? 0.5580 0.9541 0.5646 0.0049 -0.0866 0.0447 176 LEU B CA 5513 C C . LEU B 176 ? 0.6501 1.0204 0.6570 0.0109 -0.0803 0.0535 176 LEU B C 5514 O O . LEU B 176 ? 0.6296 0.9827 0.6291 0.0053 -0.0769 0.0476 176 LEU B O 5515 C CB . LEU B 176 ? 0.5651 0.9852 0.5578 0.0021 -0.0915 0.0430 176 LEU B CB 5516 C CG . LEU B 176 ? 0.6378 1.0755 0.6247 0.0131 -0.0929 0.0584 176 LEU B CG 5517 C CD1 . LEU B 176 ? 0.7265 1.1758 0.7270 0.0248 -0.0947 0.0719 176 LEU B CD1 5518 C CD2 . LEU B 176 ? 0.6178 1.0838 0.5905 0.0083 -0.0996 0.0516 176 LEU B CD2 5519 N N . ASP B 177 ? 0.6280 0.9953 0.6448 0.0224 -0.0787 0.0674 177 ASP B N 5520 C CA . ASP B 177 ? 0.6410 0.9828 0.6609 0.0271 -0.0729 0.0756 177 ASP B CA 5521 C C . ASP B 177 ? 0.7210 1.0712 0.7403 0.0373 -0.0721 0.0939 177 ASP B C 5522 O O . ASP B 177 ? 0.7421 1.1092 0.7663 0.0463 -0.0754 0.1042 177 ASP B O 5523 C CB . ASP B 177 ? 0.6369 0.9556 0.6709 0.0304 -0.0703 0.0744 177 ASP B CB 5524 C CG . ASP B 177 ? 0.7813 1.1057 0.8272 0.0431 -0.0713 0.0870 177 ASP B CG 5525 O OD1 . ASP B 177 ? 0.9854 1.3274 1.0362 0.0454 -0.0748 0.0844 177 ASP B OD1 5526 O OD2 . ASP B 177 ? 0.7053 1.0165 0.7567 0.0508 -0.0685 0.0995 177 ASP B OD2 5527 N N . LEU B 178 ? 0.7174 1.0548 0.7313 0.0360 -0.0672 0.0984 178 LEU B N 5528 C CA . LEU B 178 ? 0.6514 0.9955 0.6620 0.0436 -0.0649 0.1162 178 LEU B CA 5529 C C . LEU B 178 ? 0.7212 1.0367 0.7457 0.0478 -0.0592 0.1258 178 LEU B C 5530 O O . LEU B 178 ? 0.6973 1.0063 0.7199 0.0485 -0.0540 0.1360 178 LEU B O 5531 C CB . LEU B 178 ? 0.6753 1.0281 0.6691 0.0376 -0.0626 0.1129 178 LEU B CB 5532 C CG . LEU B 178 ? 0.5735 0.9521 0.5502 0.0317 -0.0676 0.1015 178 LEU B CG 5533 C CD1 . LEU B 178 ? 0.4085 0.8123 0.3725 0.0386 -0.0687 0.1154 178 LEU B CD1 5534 C CD2 . LEU B 178 ? 0.5951 0.9858 0.5749 0.0276 -0.0748 0.0889 178 LEU B CD2 5535 N N . VAL B 179 ? 0.8012 1.0995 0.8398 0.0500 -0.0598 0.1215 179 VAL B N 5536 C CA . VAL B 179 ? 0.8123 1.0831 0.8654 0.0541 -0.0556 0.1292 179 VAL B CA 5537 C C . VAL B 179 ? 0.9678 1.2441 1.0264 0.0655 -0.0553 0.1504 179 VAL B C 5538 O O . VAL B 179 ? 1.0158 1.2779 1.0801 0.0673 -0.0506 0.1630 179 VAL B O 5539 C CB . VAL B 179 ? 0.6196 0.8718 0.6850 0.0549 -0.0569 0.1185 179 VAL B CB 5540 C CG1 . VAL B 179 ? 0.6909 0.9136 0.7707 0.0580 -0.0534 0.1239 179 VAL B CG1 5541 C CG2 . VAL B 179 ? 0.5992 0.8481 0.6576 0.0443 -0.0577 0.0993 179 VAL B CG2 5542 N N . SER B 180 ? 0.9196 1.2178 0.9770 0.0728 -0.0604 0.1547 180 SER B N 5543 C CA . SER B 180 ? 0.9300 1.2350 0.9929 0.0853 -0.0614 0.1752 180 SER B CA 5544 C C . SER B 180 ? 0.9427 1.2641 0.9921 0.0863 -0.0594 0.1905 180 SER B C 5545 O O . SER B 180 ? 0.8938 1.2201 0.9459 0.0965 -0.0596 0.2101 180 SER B O 5546 C CB . SER B 180 ? 0.9488 1.2759 1.0147 0.0933 -0.0680 0.1743 180 SER B CB 5547 O OG . SER B 180 ? 0.9241 1.2338 1.0064 0.0989 -0.0684 0.1695 180 SER B OG 5548 N N . TYR B 181 ? 0.9356 1.2650 0.9701 0.0763 -0.0574 0.1818 181 TYR B N 5549 C CA . TYR B 181 ? 0.9062 1.2582 0.9233 0.0770 -0.0563 0.1923 181 TYR B CA 5550 C C . TYR B 181 ? 0.9413 1.2802 0.9585 0.0765 -0.0478 0.2070 181 TYR B C 5551 O O . TYR B 181 ? 0.8860 1.2049 0.9081 0.0686 -0.0423 0.1995 181 TYR B O 5552 C CB . TYR B 181 ? 0.8772 1.2483 0.8769 0.0673 -0.0591 0.1739 181 TYR B CB 5553 C CG . TYR B 181 ? 0.8668 1.2556 0.8472 0.0658 -0.0561 0.1797 181 TYR B CG 5554 C CD1 . TYR B 181 ? 0.9247 1.3466 0.8888 0.0699 -0.0618 0.1834 181 TYR B CD1 5555 C CD2 . TYR B 181 ? 0.8438 1.2181 0.8222 0.0606 -0.0476 0.1809 181 TYR B CD2 5556 C CE1 . TYR B 181 ? 0.9763 1.4156 0.9205 0.0693 -0.0590 0.1878 181 TYR B CE1 5557 C CE2 . TYR B 181 ? 0.9149 1.3073 0.8750 0.0600 -0.0439 0.1859 181 TYR B CE2 5558 C CZ . TYR B 181 ? 0.9728 1.3974 0.9148 0.0646 -0.0496 0.1891 181 TYR B CZ 5559 O OH . TYR B 181 ? 1.0439 1.4878 0.9656 0.0648 -0.0459 0.1933 181 TYR B OH 5560 N N . HIS B 182 ? 1.0770 1.4290 1.0888 0.0850 -0.0467 0.2288 182 HIS B N 5561 C CA . HIS B 182 ? 1.0550 1.4002 1.0650 0.0847 -0.0379 0.2456 182 HIS B CA 5562 C C . HIS B 182 ? 0.9841 1.3625 0.9693 0.0863 -0.0381 0.2519 182 HIS B C 5563 O O . HIS B 182 ? 0.9664 1.3702 0.9402 0.0904 -0.0462 0.2482 182 HIS B O 5564 C CB . HIS B 182 ? 1.1392 1.4666 1.1663 0.0940 -0.0356 0.2688 182 HIS B CB 5565 C CG . HIS B 182 ? 1.3531 1.6515 1.4032 0.0950 -0.0377 0.2611 182 HIS B CG 5566 N ND1 . HIS B 182 ? 1.4269 1.6962 1.4914 0.0870 -0.0329 0.2524 182 HIS B ND1 5567 C CD2 . HIS B 182 ? 1.4362 1.7316 1.4967 0.1034 -0.0442 0.2599 182 HIS B CD2 5568 C CE1 . HIS B 182 ? 1.4309 1.6800 1.5124 0.0906 -0.0366 0.2458 182 HIS B CE1 5569 N NE2 . HIS B 182 ? 1.4249 1.6893 1.5045 0.1007 -0.0430 0.2502 182 HIS B NE2 5570 N N . ILE B 183 ? 1.0319 1.4114 1.0090 0.0828 -0.0294 0.2601 183 ILE B N 5571 C CA . ILE B 183 ? 0.9848 1.3956 0.9367 0.0852 -0.0282 0.2673 183 ILE B CA 5572 C C . ILE B 183 ? 1.0870 1.5117 1.0350 0.0979 -0.0302 0.2937 183 ILE B C 5573 O O . ILE B 183 ? 1.1465 1.5507 1.1129 0.1034 -0.0281 0.3109 183 ILE B O 5574 C CB . ILE B 183 ? 0.9884 1.3959 0.9351 0.0796 -0.0164 0.2726 183 ILE B CB 5575 C CG1 . ILE B 183 ? 0.9901 1.3939 0.9328 0.0685 -0.0150 0.2459 183 ILE B CG1 5576 C CG2 . ILE B 183 ? 1.1518 1.5901 1.0741 0.0855 -0.0135 0.2882 183 ILE B CG2 5577 C CD1 . ILE B 183 ? 1.0674 1.4995 0.9859 0.0672 -0.0216 0.2287 183 ILE B CD1 5578 N N . LYS B 184 ? 1.2651 1.7239 1.1896 0.1029 -0.0349 0.2968 184 LYS B N 5579 C CA . LYS B 184 ? 1.4799 1.9545 1.3980 0.1159 -0.0370 0.3237 184 LYS B CA 5580 C C . LYS B 184 ? 1.5542 2.0545 1.4464 0.1190 -0.0315 0.3387 184 LYS B C 5581 O O . LYS B 184 ? 1.5833 2.0797 1.4698 0.1120 -0.0214 0.3371 184 LYS B O 5582 C CB . LYS B 184 ? 1.5106 2.0039 1.4279 0.1237 -0.0504 0.3194 184 LYS B CB 5583 C CG . LYS B 184 ? 1.4868 1.9557 1.4314 0.1295 -0.0535 0.3247 184 LYS B CG 5584 C CD . LYS B 184 ? 1.4730 1.9214 1.4298 0.1377 -0.0464 0.3546 184 LYS B CD 5585 C CE . LYS B 184 ? 1.3263 1.8010 1.2657 0.1501 -0.0482 0.3810 184 LYS B CE 5586 N NZ . LYS B 184 ? 1.2043 1.6569 1.1566 0.1577 -0.0410 0.4117 184 LYS B NZ 5587 N N . GLY B 185 ? 1.6245 2.1524 1.5012 0.1302 -0.0381 0.3536 185 GLY B N 5588 C CA . GLY B 185 ? 1.7473 2.3000 1.5992 0.1360 -0.0331 0.3731 185 GLY B CA 5589 C C . GLY B 185 ? 1.8414 2.4201 1.6656 0.1300 -0.0316 0.3556 185 GLY B C 5590 O O . GLY B 185 ? 1.6950 2.3062 1.4926 0.1370 -0.0342 0.3643 185 GLY B O 5591 N N . GLY B 186 ? 2.0233 2.5880 1.8531 0.1177 -0.0279 0.3307 186 GLY B N 5592 C CA . GLY B 186 ? 2.1493 2.7336 1.9554 0.1118 -0.0252 0.3127 186 GLY B CA 5593 C C . GLY B 186 ? 2.2571 2.8723 2.0423 0.1127 -0.0385 0.2925 186 GLY B C 5594 O O . GLY B 186 ? 2.2972 2.9209 2.0692 0.1053 -0.0389 0.2683 186 GLY B O 5595 N N . GLU B 187 ? 2.2742 2.9064 2.0575 0.1218 -0.0497 0.3021 187 GLU B N 5596 C CA . GLU B 187 ? 2.2054 2.8695 1.9717 0.1229 -0.0639 0.2845 187 GLU B CA 5597 C C . GLU B 187 ? 2.0757 2.7272 1.8564 0.1114 -0.0706 0.2532 187 GLU B C 5598 O O . GLU B 187 ? 2.0303 2.6823 1.8257 0.1125 -0.0806 0.2487 187 GLU B O 5599 C CB . GLU B 187 ? 2.2390 2.9216 2.0062 0.1358 -0.0742 0.3037 187 GLU B CB 5600 C CG . GLU B 187 ? 2.3178 3.0024 2.0788 0.1477 -0.0667 0.3398 187 GLU B CG 5601 C CD . GLU B 187 ? 2.3670 3.0580 2.1385 0.1608 -0.0758 0.3603 187 GLU B CD 5602 O OE1 . GLU B 187 ? 2.3733 3.0576 2.1648 0.1596 -0.0848 0.3478 187 GLU B OE1 5603 O OE2 . GLU B 187 ? 2.3811 3.0841 2.1409 0.1726 -0.0736 0.3893 187 GLU B OE2 5604 N N . THR B 188 ? 1.9666 2.6078 1.7428 0.1007 -0.0648 0.2324 188 THR B N 5605 C CA . THR B 188 ? 1.7694 2.3909 1.5609 0.0888 -0.0680 0.2051 188 THR B CA 5606 C C . THR B 188 ? 1.4833 2.1145 1.2845 0.0876 -0.0822 0.1928 188 THR B C 5607 O O . THR B 188 ? 1.4546 2.1177 1.2407 0.0906 -0.0930 0.1877 188 THR B O 5608 C CB . THR B 188 ? 1.6464 2.2696 1.4222 0.0796 -0.0645 0.1807 188 THR B CB 5609 O OG1 . THR B 188 ? 1.6103 2.2048 1.3974 0.0750 -0.0512 0.1829 188 THR B OG1 5610 C CG2 . THR B 188 ? 1.5958 2.2176 1.3762 0.0695 -0.0747 0.1508 188 THR B CG2 5611 N N . GLU B 189 ? 1.1991 1.8033 1.0264 0.0832 -0.0819 0.1885 189 GLU B N 5612 C CA . GLU B 189 ? 0.9917 1.6019 0.8320 0.0808 -0.0931 0.1762 189 GLU B CA 5613 C C . GLU B 189 ? 0.8960 1.5105 0.7293 0.0679 -0.0981 0.1457 189 GLU B C 5614 O O . GLU B 189 ? 0.8927 1.4902 0.7217 0.0600 -0.0911 0.1332 189 GLU B O 5615 C CB . GLU B 189 ? 0.8880 1.4671 0.7570 0.0811 -0.0896 0.1822 189 GLU B CB 5616 C CG . GLU B 189 ? 0.6506 1.2144 0.5280 0.0915 -0.0816 0.2109 189 GLU B CG 5617 C CD . GLU B 189 ? 0.8864 1.4185 0.7922 0.0926 -0.0788 0.2153 189 GLU B CD 5618 O OE1 . GLU B 189 ? 0.7904 1.3213 0.7093 0.0900 -0.0852 0.2025 189 GLU B OE1 5619 O OE2 . GLU B 189 ? 1.0124 1.5214 0.9276 0.0960 -0.0699 0.2319 189 GLU B OE2 5620 N N . SER B 190 ? 0.7257 1.3638 0.5586 0.0659 -0.1105 0.1338 190 SER B N 5621 C CA . SER B 190 ? 0.7209 1.3613 0.5502 0.0529 -0.1160 0.1053 190 SER B CA 5622 C C . SER B 190 ? 0.8394 1.4708 0.6930 0.0470 -0.1210 0.0968 190 SER B C 5623 O O . SER B 190 ? 0.8411 1.4704 0.7111 0.0546 -0.1215 0.1119 190 SER B O 5624 C CB . SER B 190 ? 0.8924 1.5712 0.6999 0.0533 -0.1269 0.0957 190 SER B CB 5625 O OG . SER B 190 ? 1.1950 1.8889 0.9787 0.0622 -0.1229 0.1087 190 SER B OG 5626 N N . LEU B 191 ? 0.8456 1.4714 0.7015 0.0339 -0.1244 0.0726 191 LEU B N 5627 C CA . LEU B 191 ? 0.7139 1.3360 0.5909 0.0273 -0.1295 0.0635 191 LEU B CA 5628 C C . LEU B 191 ? 0.7484 1.3700 0.6227 0.0122 -0.1344 0.0369 191 LEU B C 5629 O O . LEU B 191 ? 0.7837 1.3809 0.6537 0.0046 -0.1283 0.0251 191 LEU B O 5630 C CB . LEU B 191 ? 0.7232 1.3109 0.6201 0.0281 -0.1204 0.0713 191 LEU B CB 5631 C CG . LEU B 191 ? 0.6265 1.2118 0.5444 0.0222 -0.1245 0.0629 191 LEU B CG 5632 C CD1 . LEU B 191 ? 0.4875 1.1037 0.4133 0.0317 -0.1327 0.0747 191 LEU B CD1 5633 C CD2 . LEU B 191 ? 0.5126 1.0613 0.4468 0.0213 -0.1153 0.0658 191 LEU B CD2 5634 N N . GLN B 192 ? 0.7699 1.4189 0.6477 0.0079 -0.1459 0.0275 192 GLN B N 5635 C CA . GLN B 192 ? 0.8155 1.4651 0.6932 -0.0072 -0.1517 0.0027 192 GLN B CA 5636 C C . GLN B 192 ? 0.7930 1.4205 0.6942 -0.0156 -0.1486 -0.0020 192 GLN B C 5637 O O . GLN B 192 ? 0.8192 1.4573 0.7377 -0.0117 -0.1509 0.0072 192 GLN B O 5638 C CB . GLN B 192 ? 1.0093 1.6999 0.8828 -0.0089 -0.1659 -0.0049 192 GLN B CB 5639 C CG . GLN B 192 ? 1.1803 1.8731 1.0570 -0.0258 -0.1732 -0.0307 192 GLN B CG 5640 C CD . GLN B 192 ? 1.3201 2.0117 1.1731 -0.0305 -0.1748 -0.0476 192 GLN B CD 5641 O OE1 . GLN B 192 ? 1.3822 2.1035 1.2171 -0.0255 -0.1825 -0.0495 192 GLN B OE1 5642 N NE2 . GLN B 192 ? 1.2623 1.9204 1.1148 -0.0393 -0.1676 -0.0604 192 GLN B NE2 5643 N N . ILE B 193 ? 0.7796 1.3772 0.6811 -0.0260 -0.1431 -0.0159 193 ILE B N 5644 C CA . ILE B 193 ? 0.7881 1.3645 0.7091 -0.0353 -0.1403 -0.0220 193 ILE B CA 5645 C C . ILE B 193 ? 0.7762 1.3652 0.7036 -0.0501 -0.1491 -0.0411 193 ILE B C 5646 O O . ILE B 193 ? 0.8534 1.4395 0.7692 -0.0591 -0.1524 -0.0582 193 ILE B O 5647 C CB . ILE B 193 ? 0.7832 1.3192 0.7029 -0.0388 -0.1300 -0.0259 193 ILE B CB 5648 C CG1 . ILE B 193 ? 0.8605 1.3788 0.7858 -0.0270 -0.1208 -0.0066 193 ILE B CG1 5649 C CG2 . ILE B 193 ? 0.7644 1.2823 0.6981 -0.0517 -0.1296 -0.0382 193 ILE B CG2 5650 C CD1 . ILE B 193 ? 0.9452 1.4664 0.8548 -0.0167 -0.1167 0.0046 193 ILE B CD1 5651 N N . PRO B 194 ? 0.7651 1.3679 0.7122 -0.0528 -0.1526 -0.0384 194 PRO B N 5652 C CA . PRO B 194 ? 0.7875 1.4036 0.7450 -0.0680 -0.1604 -0.0546 194 PRO B CA 5653 C C . PRO B 194 ? 0.7789 1.3617 0.7355 -0.0817 -0.1561 -0.0701 194 PRO B C 5654 O O . PRO B 194 ? 0.6998 1.2502 0.6539 -0.0785 -0.1464 -0.0655 194 PRO B O 5655 C CB . PRO B 194 ? 0.7585 1.3852 0.7396 -0.0661 -0.1596 -0.0447 194 PRO B CB 5656 C CG . PRO B 194 ? 0.7449 1.3771 0.7251 -0.0476 -0.1560 -0.0239 194 PRO B CG 5657 C CD . PRO B 194 ? 0.7761 1.3808 0.7382 -0.0417 -0.1485 -0.0200 194 PRO B CD 5658 N N . ASN B 195 ? 0.8332 1.4230 0.7925 -0.0967 -0.1634 -0.0880 195 ASN B N 5659 C CA . ASN B 195 ? 0.9251 1.4815 0.8849 -0.1098 -0.1595 -0.1019 195 ASN B CA 5660 C C . ASN B 195 ? 0.8321 1.3648 0.8081 -0.1117 -0.1505 -0.0936 195 ASN B C 5661 O O . ASN B 195 ? 0.8185 1.3671 0.8126 -0.1147 -0.1517 -0.0886 195 ASN B O 5662 C CB . ASN B 195 ? 1.1208 1.6891 1.0847 -0.1267 -0.1695 -0.1217 195 ASN B CB 5663 C CG . ASN B 195 ? 1.4565 2.0599 1.4087 -0.1243 -0.1810 -0.1288 195 ASN B CG 5664 O OD1 . ASN B 195 ? 1.4894 2.1256 1.4454 -0.1157 -0.1857 -0.1180 195 ASN B OD1 5665 N ND2 . ASN B 195 ? 1.8344 2.4310 1.7715 -0.1310 -0.1858 -0.1474 195 ASN B ND2 5666 N N . THR B 196 ? 0.9141 1.4108 0.8834 -0.1091 -0.1416 -0.0920 196 THR B N 5667 C CA . THR B 196 ? 0.8751 1.3467 0.8565 -0.1106 -0.1332 -0.0855 196 THR B CA 5668 C C . THR B 196 ? 0.8050 1.2407 0.7805 -0.1193 -0.1294 -0.0967 196 THR B C 5669 O O . THR B 196 ? 0.8705 1.2951 0.8308 -0.1178 -0.1297 -0.1044 196 THR B O 5670 C CB . THR B 196 ? 0.9572 1.4180 0.9374 -0.0949 -0.1252 -0.0686 196 THR B CB 5671 O OG1 . THR B 196 ? 1.2266 1.7166 1.2052 -0.0832 -0.1287 -0.0577 196 THR B OG1 5672 C CG2 . THR B 196 ? 0.9424 1.3915 0.9379 -0.0952 -0.1192 -0.0612 196 THR B CG2 5673 N N . THR B 197 ? 0.6964 1.1140 0.6833 -0.1277 -0.1254 -0.0972 197 THR B N 5674 C CA . THR B 197 ? 0.7655 1.1451 0.7467 -0.1326 -0.1205 -0.1038 197 THR B CA 5675 C C . THR B 197 ? 0.7990 1.1581 0.7710 -0.1187 -0.1132 -0.0949 197 THR B C 5676 O O . THR B 197 ? 0.8072 1.1495 0.7668 -0.1167 -0.1120 -0.1016 197 THR B O 5677 C CB . THR B 197 ? 0.6663 1.0305 0.6606 -0.1429 -0.1169 -0.1032 197 THR B CB 5678 O OG1 . THR B 197 ? 0.6678 1.0490 0.6717 -0.1577 -0.1235 -0.1124 197 THR B OG1 5679 C CG2 . THR B 197 ? 0.4800 0.8039 0.4672 -0.1459 -0.1121 -0.1083 197 THR B CG2 5680 N N . VAL B 198 ? 0.6539 1.0154 0.6330 -0.1091 -0.1083 -0.0804 198 VAL B N 5681 C CA . VAL B 198 ? 0.6720 1.0149 0.6452 -0.0970 -0.1019 -0.0718 198 VAL B CA 5682 C C . VAL B 198 ? 0.7783 1.1429 0.7505 -0.0839 -0.1020 -0.0593 198 VAL B C 5683 O O . VAL B 198 ? 0.8821 1.2705 0.8634 -0.0811 -0.1046 -0.0523 198 VAL B O 5684 C CB . VAL B 198 ? 0.6736 0.9931 0.6549 -0.0959 -0.0954 -0.0657 198 VAL B CB 5685 C CG1 . VAL B 198 ? 0.5631 0.8647 0.5406 -0.0840 -0.0898 -0.0575 198 VAL B CG1 5686 C CG2 . VAL B 198 ? 0.6547 0.9507 0.6358 -0.1080 -0.0949 -0.0760 198 VAL B CG2 5687 N N . LEU B 199 ? 0.7479 1.1050 0.7097 -0.0756 -0.0992 -0.0561 199 LEU B N 5688 C CA . LEU B 199 ? 0.7413 1.1119 0.7029 -0.0625 -0.0975 -0.0414 199 LEU B CA 5689 C C . LEU B 199 ? 0.7315 1.0759 0.6948 -0.0550 -0.0898 -0.0333 199 LEU B C 5690 O O . LEU B 199 ? 0.8020 1.1291 0.7573 -0.0552 -0.0866 -0.0379 199 LEU B O 5691 C CB . LEU B 199 ? 0.7688 1.1593 0.7165 -0.0588 -0.1008 -0.0422 199 LEU B CB 5692 C CG . LEU B 199 ? 0.7306 1.1338 0.6778 -0.0451 -0.0985 -0.0247 199 LEU B CG 5693 C CD1 . LEU B 199 ? 0.7403 1.1594 0.7013 -0.0405 -0.1009 -0.0143 199 LEU B CD1 5694 C CD2 . LEU B 199 ? 0.8151 1.2414 0.7470 -0.0416 -0.1022 -0.0249 199 LEU B CD2 5695 N N . HIS B 200 ? 0.7254 1.0676 0.6999 -0.0481 -0.0872 -0.0219 200 HIS B N 5696 C CA . HIS B 200 ? 0.7276 1.0454 0.7059 -0.0411 -0.0808 -0.0146 200 HIS B CA 5697 C C . HIS B 200 ? 0.7837 1.1117 0.7646 -0.0289 -0.0792 0.0009 200 HIS B C 5698 O O . HIS B 200 ? 0.7925 1.1376 0.7808 -0.0234 -0.0814 0.0091 200 HIS B O 5699 C CB . HIS B 200 ? 0.7926 1.0949 0.7816 -0.0426 -0.0787 -0.0151 200 HIS B CB 5700 C CG . HIS B 200 ? 0.8583 1.1333 0.8504 -0.0374 -0.0735 -0.0113 200 HIS B CG 5701 N ND1 . HIS B 200 ? 0.9636 1.2316 0.9537 -0.0307 -0.0705 -0.0047 200 HIS B ND1 5702 C CD2 . HIS B 200 ? 0.6296 0.8841 0.6273 -0.0380 -0.0710 -0.0132 200 HIS B CD2 5703 C CE1 . HIS B 200 ? 0.7654 1.0094 0.7610 -0.0280 -0.0669 -0.0035 200 HIS B CE1 5704 N NE2 . HIS B 200 ? 0.5886 0.8240 0.5879 -0.0319 -0.0675 -0.0090 200 HIS B NE2 5705 N N . LEU B 201 ? 0.6288 0.9462 0.6044 -0.0247 -0.0751 0.0053 201 LEU B N 5706 C CA . LEU B 201 ? 0.6054 0.9300 0.5831 -0.0140 -0.0728 0.0212 201 LEU B CA 5707 C C . LEU B 201 ? 0.6182 0.9164 0.6053 -0.0093 -0.0669 0.0277 201 LEU B C 5708 O O . LEU B 201 ? 0.5607 0.8397 0.5460 -0.0130 -0.0636 0.0214 201 LEU B O 5709 C CB . LEU B 201 ? 0.5605 0.9001 0.5242 -0.0127 -0.0726 0.0229 201 LEU B CB 5710 C CG . LEU B 201 ? 0.6046 0.9706 0.5578 -0.0176 -0.0795 0.0143 201 LEU B CG 5711 C CD1 . LEU B 201 ? 0.6191 0.9953 0.5557 -0.0176 -0.0787 0.0112 201 LEU B CD1 5712 C CD2 . LEU B 201 ? 0.6641 1.0551 0.6225 -0.0115 -0.0843 0.0246 201 LEU B CD2 5713 N N . VAL B 202 ? 0.6743 0.9717 0.6724 -0.0009 -0.0662 0.0398 202 VAL B N 5714 C CA . VAL B 202 ? 0.7796 1.0523 0.7881 0.0036 -0.0616 0.0456 202 VAL B CA 5715 C C . VAL B 202 ? 0.7462 1.0235 0.7578 0.0124 -0.0589 0.0628 202 VAL B C 5716 O O . VAL B 202 ? 0.7689 1.0647 0.7811 0.0189 -0.0614 0.0728 202 VAL B O 5717 C CB . VAL B 202 ? 0.5694 0.8312 0.5900 0.0062 -0.0626 0.0440 202 VAL B CB 5718 C CG1 . VAL B 202 ? 0.3660 0.5999 0.3956 0.0085 -0.0590 0.0450 202 VAL B CG1 5719 C CG2 . VAL B 202 ? 0.5230 0.7873 0.5400 -0.0022 -0.0654 0.0302 202 VAL B CG2 5720 N N . PHE B 203 ? 0.6478 0.9088 0.6622 0.0126 -0.0538 0.0668 203 PHE B N 5721 C CA . PHE B 203 ? 0.6466 0.9101 0.6645 0.0196 -0.0500 0.0842 203 PHE B CA 5722 C C . PHE B 203 ? 0.7690 1.0091 0.8044 0.0243 -0.0475 0.0919 203 PHE B C 5723 O O . PHE B 203 ? 0.8220 1.0437 0.8652 0.0223 -0.0486 0.0823 203 PHE B O 5724 C CB . PHE B 203 ? 0.6420 0.9090 0.6505 0.0161 -0.0453 0.0846 203 PHE B CB 5725 C CG . PHE B 203 ? 0.7153 1.0032 0.7060 0.0114 -0.0480 0.0746 203 PHE B CG 5726 C CD1 . PHE B 203 ? 0.6456 0.9259 0.6304 0.0033 -0.0485 0.0572 203 PHE B CD1 5727 C CD2 . PHE B 203 ? 0.7737 1.0884 0.7537 0.0155 -0.0507 0.0822 203 PHE B CD2 5728 C CE1 . PHE B 203 ? 0.6840 0.9813 0.6532 -0.0012 -0.0515 0.0466 203 PHE B CE1 5729 C CE2 . PHE B 203 ? 0.8581 1.1921 0.8219 0.0110 -0.0542 0.0712 203 PHE B CE2 5730 C CZ . PHE B 203 ? 0.8027 1.1271 0.7615 0.0023 -0.0545 0.0528 203 PHE B CZ 5731 N N . HIS B 204 ? 0.8411 1.0815 0.8823 0.0307 -0.0443 0.1092 204 HIS B N 5732 C CA . HIS B 204 ? 0.8958 1.1124 0.9548 0.0344 -0.0419 0.1167 204 HIS B CA 5733 C C . HIS B 204 ? 0.9921 1.1885 1.0563 0.0271 -0.0391 0.1063 204 HIS B C 5734 O O . HIS B 204 ? 1.0985 1.3002 1.1555 0.0220 -0.0355 0.1044 204 HIS B O 5735 C CB . HIS B 204 ? 0.9287 1.1489 0.9922 0.0404 -0.0379 0.1378 204 HIS B CB 5736 C CG . HIS B 204 ? 0.8633 1.0595 0.9467 0.0451 -0.0364 0.1470 204 HIS B CG 5737 N ND1 . HIS B 204 ? 0.8328 1.0263 0.9249 0.0545 -0.0397 0.1551 204 HIS B ND1 5738 C CD2 . HIS B 204 ? 0.7259 0.9000 0.8236 0.0418 -0.0324 0.1492 204 HIS B CD2 5739 C CE1 . HIS B 204 ? 0.8047 0.9735 0.9147 0.0568 -0.0378 0.1613 204 HIS B CE1 5740 N NE2 . HIS B 204 ? 0.8078 0.9647 0.9219 0.0486 -0.0336 0.1579 204 HIS B NE2 5741 N N . PRO B 205 ? 0.9564 1.1307 1.0332 0.0274 -0.0409 0.0993 205 PRO B N 5742 C CA . PRO B 205 ? 0.9233 1.0791 1.0044 0.0208 -0.0404 0.0864 205 PRO B CA 5743 C C . PRO B 205 ? 0.9233 1.0632 1.0197 0.0200 -0.0362 0.0942 205 PRO B C 5744 O O . PRO B 205 ? 0.9290 1.0530 1.0322 0.0154 -0.0365 0.0844 205 PRO B O 5745 C CB . PRO B 205 ? 0.7037 0.8460 0.7901 0.0231 -0.0450 0.0764 205 PRO B CB 5746 C CG . PRO B 205 ? 0.6406 0.7926 0.7294 0.0318 -0.0469 0.0858 205 PRO B CG 5747 C CD . PRO B 205 ? 0.8303 0.9962 0.9179 0.0350 -0.0439 0.1030 205 PRO B CD 5748 N N . ASN B 206 ? 0.8324 0.9766 0.9348 0.0241 -0.0326 0.1120 206 ASN B N 5749 C CA . ASN B 206 ? 0.8877 1.0158 1.0081 0.0230 -0.0285 0.1212 206 ASN B CA 5750 C C . ASN B 206 ? 0.9024 1.0439 1.0216 0.0231 -0.0216 0.1392 206 ASN B C 5751 O O . ASN B 206 ? 0.9561 1.0895 1.0891 0.0261 -0.0188 0.1554 206 ASN B O 5752 C CB . ASN B 206 ? 0.9325 1.0414 1.0693 0.0290 -0.0314 0.1262 206 ASN B CB 5753 C CG . ASN B 206 ? 1.0038 1.0917 1.1492 0.0270 -0.0360 0.1096 206 ASN B CG 5754 O OD1 . ASN B 206 ? 1.0866 1.1661 1.2368 0.0203 -0.0353 0.1010 206 ASN B OD1 5755 N ND2 . ASN B 206 ? 1.0232 1.1036 1.1704 0.0333 -0.0408 0.1046 206 ASN B ND2 5756 N N . SER B 207 ? 0.8380 0.9997 0.9407 0.0199 -0.0188 0.1367 207 SER B N 5757 C CA . SER B 207 ? 0.8810 1.0587 0.9794 0.0205 -0.0116 0.1534 207 SER B CA 5758 C C . SER B 207 ? 0.9779 1.1759 1.0574 0.0167 -0.0090 0.1448 207 SER B C 5759 O O . SER B 207 ? 0.9714 1.1716 1.0403 0.0140 -0.0136 0.1269 207 SER B O 5760 C CB . SER B 207 ? 0.6508 0.8403 0.7441 0.0287 -0.0122 0.1711 207 SER B CB 5761 O OG . SER B 207 ? 0.5998 0.8004 0.6799 0.0323 -0.0193 0.1621 207 SER B OG 5762 N N . LEU B 208 ? 0.9324 1.1447 1.0080 0.0167 -0.0013 0.1580 208 LEU B N 5763 C CA . LEU B 208 ? 0.7781 1.0118 0.8346 0.0147 0.0019 0.1511 208 LEU B CA 5764 C C . LEU B 208 ? 0.7775 1.0294 0.8132 0.0186 -0.0043 0.1469 208 LEU B C 5765 O O . LEU B 208 ? 0.7759 1.0320 0.8111 0.0245 -0.0074 0.1590 208 LEU B O 5766 C CB . LEU B 208 ? 0.7274 0.9744 0.7840 0.0152 0.0122 0.1688 208 LEU B CB 5767 C CG . LEU B 208 ? 0.6122 0.8433 0.6915 0.0097 0.0183 0.1701 208 LEU B CG 5768 C CD1 . LEU B 208 ? 0.4076 0.6521 0.4902 0.0095 0.0298 0.1894 208 LEU B CD1 5769 C CD2 . LEU B 208 ? 0.6421 0.8690 0.7197 0.0046 0.0164 0.1470 208 LEU B CD2 5770 N N . PHE B 209 ? 0.8140 1.0754 0.8343 0.0152 -0.0069 0.1291 209 PHE B N 5771 C CA . PHE B 209 ? 0.7856 1.0656 0.7869 0.0172 -0.0133 0.1227 209 PHE B CA 5772 C C . PHE B 209 ? 0.8226 1.1280 0.8097 0.0226 -0.0099 0.1387 209 PHE B C 5773 O O . PHE B 209 ? 0.7730 1.0894 0.7525 0.0221 -0.0026 0.1421 209 PHE B O 5774 C CB . PHE B 209 ? 0.8047 1.0878 0.7936 0.0115 -0.0158 0.1005 209 PHE B CB 5775 C CG . PHE B 209 ? 0.8146 1.1205 0.7829 0.0122 -0.0213 0.0935 209 PHE B CG 5776 C CD1 . PHE B 209 ? 0.7654 1.0706 0.7325 0.0106 -0.0299 0.0838 209 PHE B CD1 5777 C CD2 . PHE B 209 ? 0.6816 1.0110 0.6319 0.0143 -0.0179 0.0963 209 PHE B CD2 5778 C CE1 . PHE B 209 ? 0.7784 1.1056 0.7288 0.0102 -0.0357 0.0767 209 PHE B CE1 5779 C CE2 . PHE B 209 ? 0.6631 1.0141 0.5948 0.0146 -0.0241 0.0884 209 PHE B CE2 5780 C CZ . PHE B 209 ? 0.6988 1.0485 0.6314 0.0122 -0.0333 0.0785 209 PHE B CZ 5781 N N . SER B 210 ? 0.8509 1.1670 0.8340 0.0286 -0.0149 0.1488 210 SER B N 5782 C CA . SER B 210 ? 0.8811 1.2213 0.8506 0.0349 -0.0121 0.1665 210 SER B CA 5783 C C . SER B 210 ? 0.8428 1.2059 0.7969 0.0393 -0.0209 0.1647 210 SER B C 5784 O O . SER B 210 ? 0.9532 1.3265 0.9064 0.0470 -0.0225 0.1825 210 SER B O 5785 C CB . SER B 210 ? 0.8037 1.1339 0.7886 0.0400 -0.0066 0.1915 210 SER B CB 5786 O OG . SER B 210 ? 0.8317 1.1540 0.8268 0.0455 -0.0132 0.1981 210 SER B OG 5787 N N . VAL B 211 ? 0.7452 1.1165 0.6880 0.0344 -0.0268 0.1436 211 VAL B N 5788 C CA . VAL B 211 ? 0.7964 1.1915 0.7258 0.0374 -0.0358 0.1406 211 VAL B CA 5789 C C . VAL B 211 ? 0.8298 1.2542 0.7343 0.0389 -0.0355 0.1391 211 VAL B C 5790 O O . VAL B 211 ? 0.7489 1.1746 0.6431 0.0336 -0.0324 0.1248 211 VAL B O 5791 C CB . VAL B 211 ? 0.7188 1.1078 0.6525 0.0313 -0.0439 0.1200 211 VAL B CB 5792 C CG1 . VAL B 211 ? 0.7849 1.2009 0.7078 0.0339 -0.0533 0.1177 211 VAL B CG1 5793 C CG2 . VAL B 211 ? 0.6737 1.0374 0.6293 0.0316 -0.0441 0.1226 211 VAL B CG2 5794 N N . GLN B 212 ? 0.7811 1.2290 0.6756 0.0469 -0.0391 0.1539 212 GLN B N 5795 C CA . GLN B 212 ? 0.8558 1.3346 0.7247 0.0500 -0.0400 0.1542 212 GLN B CA 5796 C C . GLN B 212 ? 0.8521 1.3555 0.7097 0.0506 -0.0527 0.1436 212 GLN B C 5797 O O . GLN B 212 ? 1.0318 1.5634 0.8676 0.0539 -0.0557 0.1435 212 GLN B O 5798 C CB . GLN B 212 ? 1.0122 1.5023 0.8754 0.0594 -0.0334 0.1822 212 GLN B CB 5799 C CG . GLN B 212 ? 1.0918 1.5722 0.9558 0.0579 -0.0200 0.1904 212 GLN B CG 5800 C CD . GLN B 212 ? 1.1620 1.6520 1.0226 0.0667 -0.0130 0.2208 212 GLN B CD 5801 O OE1 . GLN B 212 ? 1.0310 1.5017 0.9084 0.0663 -0.0038 0.2360 212 GLN B OE1 5802 N NE2 . GLN B 212 ? 1.2803 1.8006 1.1197 0.0745 -0.0176 0.2302 212 GLN B NE2 5803 N N . VAL B 213 ? 0.7416 1.2358 0.6141 0.0474 -0.0600 0.1349 213 VAL B N 5804 C CA . VAL B 213 ? 0.6892 1.2064 0.5553 0.0461 -0.0719 0.1231 213 VAL B CA 5805 C C . VAL B 213 ? 0.7603 1.2868 0.6102 0.0372 -0.0753 0.0985 213 VAL B C 5806 O O . VAL B 213 ? 0.7147 1.2196 0.5692 0.0289 -0.0715 0.0829 213 VAL B O 5807 C CB . VAL B 213 ? 0.8649 1.3683 0.7528 0.0432 -0.0772 0.1176 213 VAL B CB 5808 C CG1 . VAL B 213 ? 0.7565 1.2803 0.6402 0.0374 -0.0884 0.0995 213 VAL B CG1 5809 C CG2 . VAL B 213 ? 0.8713 1.3732 0.7730 0.0539 -0.0773 0.1402 213 VAL B CG2 5810 N N . ASN B 214 ? 0.9028 1.4613 0.7338 0.0397 -0.0829 0.0948 214 ASN B N 5811 C CA . ASN B 214 ? 1.0611 1.6311 0.8766 0.0316 -0.0884 0.0700 214 ASN B CA 5812 C C . ASN B 214 ? 1.0683 1.6369 0.8964 0.0226 -0.0984 0.0525 214 ASN B C 5813 O O . ASN B 214 ? 1.1611 1.7524 0.9914 0.0250 -0.1080 0.0554 214 ASN B O 5814 C CB . ASN B 214 ? 1.1604 1.7667 0.9499 0.0383 -0.0931 0.0731 214 ASN B CB 5815 C CG . ASN B 214 ? 1.3871 2.0032 1.1570 0.0315 -0.0964 0.0476 214 ASN B CG 5816 O OD1 . ASN B 214 ? 1.1699 1.7635 0.9450 0.0225 -0.0935 0.0294 214 ASN B OD1 5817 N ND2 . ASN B 214 ? 1.8271 2.4772 1.5735 0.0366 -0.1028 0.0463 214 ASN B ND2 5818 N N . MET B 215 ? 0.8916 1.4345 0.7289 0.0124 -0.0961 0.0354 215 MET B N 5819 C CA . MET B 215 ? 0.9106 1.4496 0.7615 0.0029 -0.1040 0.0207 215 MET B CA 5820 C C . MET B 215 ? 0.8761 1.4213 0.7167 -0.0077 -0.1108 -0.0048 215 MET B C 5821 O O . MET B 215 ? 0.9314 1.4555 0.7691 -0.0140 -0.1063 -0.0186 215 MET B O 5822 C CB . MET B 215 ? 0.9572 1.4616 0.8285 -0.0014 -0.0978 0.0207 215 MET B CB 5823 C CG . MET B 215 ? 1.0438 1.5403 0.9295 0.0077 -0.0933 0.0426 215 MET B CG 5824 S SD . MET B 215 ? 0.8182 1.2896 0.7286 0.0023 -0.0930 0.0388 215 MET B SD 5825 C CE . MET B 215 ? 0.6320 1.0977 0.5551 0.0158 -0.0881 0.0652 215 MET B CE 5826 N N . SER B 216 ? 0.8139 1.3876 0.6508 -0.0099 -0.1221 -0.0114 216 SER B N 5827 C CA . SER B 216 ? 0.9089 1.4875 0.7396 -0.0215 -0.1299 -0.0366 216 SER B CA 5828 C C . SER B 216 ? 0.9288 1.4915 0.7804 -0.0336 -0.1332 -0.0475 216 SER B C 5829 O O . SER B 216 ? 0.9083 1.4705 0.7779 -0.0321 -0.1333 -0.0362 216 SER B O 5830 C CB . SER B 216 ? 0.9113 1.5295 0.7273 -0.0193 -0.1415 -0.0408 216 SER B CB 5831 O OG . SER B 216 ? 1.0613 1.6937 0.8549 -0.0086 -0.1378 -0.0322 216 SER B OG 5832 N N . VAL B 217 ? 0.8603 1.4095 0.7091 -0.0451 -0.1352 -0.0693 217 VAL B N 5833 C CA . VAL B 217 ? 0.9467 1.4853 0.8127 -0.0582 -0.1396 -0.0813 217 VAL B CA 5834 C C . VAL B 217 ? 0.9449 1.4896 0.8014 -0.0692 -0.1480 -0.1057 217 VAL B C 5835 O O . VAL B 217 ? 0.8736 1.4136 0.7122 -0.0676 -0.1463 -0.1159 217 VAL B O 5836 C CB . VAL B 217 ? 1.0484 1.5474 0.9265 -0.0619 -0.1302 -0.0806 217 VAL B CB 5837 C CG1 . VAL B 217 ? 0.9511 1.4392 0.8444 -0.0762 -0.1343 -0.0933 217 VAL B CG1 5838 C CG2 . VAL B 217 ? 1.2048 1.6965 1.0938 -0.0518 -0.1227 -0.0584 217 VAL B CG2 5839 N N . ASN B 218 ? 1.0372 1.5927 0.9065 -0.0805 -0.1569 -0.1155 218 ASN B N 5840 C CA . ASN B 218 ? 1.2226 1.7792 1.0869 -0.0934 -0.1653 -0.1401 218 ASN B CA 5841 C C . ASN B 218 ? 1.1396 1.6585 1.0153 -0.1054 -0.1608 -0.1509 218 ASN B C 5842 O O . ASN B 218 ? 1.0922 1.5864 0.9577 -0.1063 -0.1564 -0.1617 218 ASN B O 5843 C CB . ASN B 218 ? 1.4476 2.0385 1.3209 -0.1006 -0.1783 -0.1457 218 ASN B CB 5844 C CG . ASN B 218 ? 1.5810 2.2010 1.4611 -0.0895 -0.1799 -0.1245 218 ASN B CG 5845 O OD1 . ASN B 218 ? 1.6274 2.2827 1.4984 -0.0843 -0.1889 -0.1236 218 ASN B OD1 5846 N ND2 . ASN B 218 ? 1.4976 2.1027 1.3934 -0.0852 -0.1715 -0.1074 218 ASN B ND2 5847 N N . ALA B 219 ? 1.0103 1.5261 0.9076 -0.1139 -0.1618 -0.1473 219 ALA B N 5848 C CA . ALA B 219 ? 0.9131 1.3952 0.8219 -0.1258 -0.1581 -0.1556 219 ALA B CA 5849 C C . ALA B 219 ? 0.9271 1.3844 0.8445 -0.1193 -0.1467 -0.1388 219 ALA B C 5850 O O . ALA B 219 ? 1.0312 1.5002 0.9610 -0.1149 -0.1449 -0.1235 219 ALA B O 5851 C CB . ALA B 219 ? 0.8214 1.3157 0.7482 -0.1411 -0.1661 -0.1634 219 ALA B CB 5852 N N . LEU B 220 ? 0.7254 1.1492 0.6365 -0.1181 -0.1394 -0.1424 220 LEU B N 5853 C CA . LEU B 220 ? 0.5393 0.9388 0.4569 -0.1115 -0.1292 -0.1282 220 LEU B CA 5854 C C . LEU B 220 ? 0.6644 1.0260 0.5839 -0.1187 -0.1250 -0.1375 220 LEU B C 5855 O O . LEU B 220 ? 0.8214 1.1702 0.7298 -0.1206 -0.1258 -0.1515 220 LEU B O 5856 C CB . LEU B 220 ? 0.5540 0.9564 0.4601 -0.0962 -0.1232 -0.1164 220 LEU B CB 5857 C CG . LEU B 220 ? 0.6774 1.0627 0.5930 -0.0884 -0.1144 -0.0993 220 LEU B CG 5858 C CD1 . LEU B 220 ? 0.7824 1.1804 0.7144 -0.0900 -0.1163 -0.0894 220 LEU B CD1 5859 C CD2 . LEU B 220 ? 0.6469 1.0382 0.5536 -0.0746 -0.1091 -0.0863 220 LEU B CD2 5860 N N . GLY B 221 ? 0.6098 0.9538 0.5428 -0.1219 -0.1206 -0.1300 221 GLY B N 5861 C CA . GLY B 221 ? 0.6534 0.9620 0.5882 -0.1284 -0.1171 -0.1372 221 GLY B CA 5862 C C . GLY B 221 ? 0.8183 1.1042 0.7498 -0.1175 -0.1085 -0.1282 221 GLY B C 5863 O O . GLY B 221 ? 0.8812 1.1414 0.8071 -0.1176 -0.1059 -0.1359 221 GLY B O 5864 N N . HIS B 222 ? 0.7905 1.0863 0.7265 -0.1079 -0.1046 -0.1120 222 HIS B N 5865 C CA . HIS B 222 ? 0.7469 1.0223 0.6833 -0.0985 -0.0970 -0.1025 222 HIS B CA 5866 C C . HIS B 222 ? 0.7901 1.0848 0.7261 -0.0865 -0.0946 -0.0879 222 HIS B C 5867 O O . HIS B 222 ? 0.8141 1.1272 0.7580 -0.0846 -0.0961 -0.0785 222 HIS B O 5868 C CB . HIS B 222 ? 0.8970 1.1528 0.8448 -0.1023 -0.0940 -0.0975 222 HIS B CB 5869 C CG . HIS B 222 ? 1.0277 1.2587 0.9761 -0.0946 -0.0876 -0.0912 222 HIS B CG 5870 N ND1 . HIS B 222 ? 1.0883 1.3027 1.0291 -0.0909 -0.0851 -0.0968 222 HIS B ND1 5871 C CD2 . HIS B 222 ? 0.9423 1.1632 0.8986 -0.0901 -0.0836 -0.0808 222 HIS B CD2 5872 C CE1 . HIS B 222 ? 0.9518 1.1478 0.8969 -0.0848 -0.0802 -0.0896 222 HIS B CE1 5873 N NE2 . HIS B 222 ? 0.8704 1.0693 0.8242 -0.0842 -0.0795 -0.0802 222 HIS B NE2 5874 N N . LEU B 223 ? 0.8173 1.1086 0.7446 -0.0783 -0.0906 -0.0859 223 LEU B N 5875 C CA . LEU B 223 ? 0.8420 1.1457 0.7699 -0.0669 -0.0870 -0.0703 223 LEU B CA 5876 C C . LEU B 223 ? 0.9073 1.1862 0.8436 -0.0622 -0.0805 -0.0624 223 LEU B C 5877 O O . LEU B 223 ? 1.0880 1.3435 1.0232 -0.0645 -0.0780 -0.0698 223 LEU B O 5878 C CB . LEU B 223 ? 0.8033 1.1190 0.7172 -0.0610 -0.0855 -0.0716 223 LEU B CB 5879 C CG . LEU B 223 ? 0.6653 0.9892 0.5804 -0.0495 -0.0802 -0.0537 223 LEU B CG 5880 C CD1 . LEU B 223 ? 0.6245 0.9741 0.5433 -0.0459 -0.0844 -0.0424 223 LEU B CD1 5881 C CD2 . LEU B 223 ? 0.5675 0.8990 0.4688 -0.0444 -0.0768 -0.0553 223 LEU B CD2 5882 N N . GLN B 224 ? 0.8332 1.1166 0.7783 -0.0553 -0.0783 -0.0479 224 GLN B N 5883 C CA . GLN B 224 ? 0.7635 1.0239 0.7169 -0.0507 -0.0729 -0.0412 224 GLN B CA 5884 C C . GLN B 224 ? 0.6938 0.9605 0.6526 -0.0403 -0.0694 -0.0251 224 GLN B C 5885 O O . GLN B 224 ? 0.6247 0.9071 0.5886 -0.0365 -0.0713 -0.0162 224 GLN B O 5886 C CB . GLN B 224 ? 0.7964 1.0433 0.7586 -0.0555 -0.0739 -0.0432 224 GLN B CB 5887 C CG . GLN B 224 ? 0.9458 1.1655 0.9131 -0.0530 -0.0698 -0.0420 224 GLN B CG 5888 C CD . GLN B 224 ? 0.8959 1.1076 0.8720 -0.0537 -0.0698 -0.0390 224 GLN B CD 5889 O OE1 . GLN B 224 ? 0.9267 1.1471 0.9040 -0.0599 -0.0726 -0.0423 224 GLN B OE1 5890 N NE2 . GLN B 224 ? 0.6742 0.8703 0.6568 -0.0473 -0.0667 -0.0328 224 GLN B NE2 5891 N N . LEU B 225 ? 0.6547 0.9090 0.6137 -0.0357 -0.0642 -0.0215 225 LEU B N 5892 C CA . LEU B 225 ? 0.7089 0.9670 0.6737 -0.0268 -0.0602 -0.0059 225 LEU B CA 5893 C C . LEU B 225 ? 0.6997 0.9332 0.6769 -0.0244 -0.0568 -0.0022 225 LEU B C 5894 O O . LEU B 225 ? 0.6126 0.8277 0.5903 -0.0278 -0.0555 -0.0108 225 LEU B O 5895 C CB . LEU B 225 ? 0.6865 0.9541 0.6425 -0.0233 -0.0561 -0.0025 225 LEU B CB 5896 C CG . LEU B 225 ? 0.7141 1.0009 0.6539 -0.0258 -0.0582 -0.0110 225 LEU B CG 5897 C CD1 . LEU B 225 ? 0.5815 0.8805 0.5150 -0.0191 -0.0525 -0.0007 225 LEU B CD1 5898 C CD2 . LEU B 225 ? 0.7083 1.0171 0.6431 -0.0280 -0.0652 -0.0128 225 LEU B CD2 5899 N N . SER B 226 ? 0.7190 0.9525 0.7065 -0.0181 -0.0559 0.0102 226 SER B N 5900 C CA . SER B 226 ? 0.7195 0.9307 0.7195 -0.0153 -0.0537 0.0133 226 SER B CA 5901 C C . SER B 226 ? 0.8139 1.0244 0.8228 -0.0080 -0.0498 0.0282 226 SER B C 5902 O O . SER B 226 ? 0.8370 1.0637 0.8456 -0.0029 -0.0500 0.0394 226 SER B O 5903 C CB . SER B 226 ? 0.7125 0.9190 0.7184 -0.0154 -0.0569 0.0112 226 SER B CB 5904 O OG . SER B 226 ? 0.8815 1.0870 0.8806 -0.0232 -0.0598 -0.0012 226 SER B OG 5905 N N . ASN B 227 ? 0.8320 1.0236 0.8499 -0.0075 -0.0466 0.0287 227 ASN B N 5906 C CA . ASN B 227 ? 0.6845 0.8722 0.7134 -0.0023 -0.0424 0.0424 227 ASN B CA 5907 C C . ASN B 227 ? 0.8209 1.0242 0.8431 -0.0017 -0.0376 0.0498 227 ASN B C 5908 O O . ASN B 227 ? 0.8727 1.0917 0.8923 0.0029 -0.0364 0.0627 227 ASN B O 5909 C CB . ASN B 227 ? 0.6513 0.8415 0.6885 0.0043 -0.0440 0.0539 227 ASN B CB 5910 C CG . ASN B 227 ? 0.7170 0.8928 0.7609 0.0050 -0.0478 0.0467 227 ASN B CG 5911 O OD1 . ASN B 227 ? 0.6263 0.7878 0.6699 0.0006 -0.0491 0.0349 227 ASN B OD1 5912 N ND2 . ASN B 227 ? 0.6760 0.8563 0.7257 0.0114 -0.0495 0.0543 227 ASN B ND2 5913 N N . ILE B 228 ? 0.7627 0.9623 0.7816 -0.0055 -0.0347 0.0419 228 ILE B N 5914 C CA . ILE B 228 ? 0.6201 0.8351 0.6315 -0.0048 -0.0292 0.0469 228 ILE B CA 5915 C C . ILE B 228 ? 0.6720 0.8764 0.6969 -0.0046 -0.0229 0.0523 228 ILE B C 5916 O O . ILE B 228 ? 0.6908 0.8823 0.7203 -0.0079 -0.0227 0.0415 228 ILE B O 5917 C CB . ILE B 228 ? 0.4925 0.7152 0.4881 -0.0090 -0.0304 0.0315 228 ILE B CB 5918 C CG1 . ILE B 228 ? 0.4802 0.7095 0.4660 -0.0115 -0.0376 0.0234 228 ILE B CG1 5919 C CG2 . ILE B 228 ? 0.4904 0.7334 0.4748 -0.0069 -0.0248 0.0361 228 ILE B CG2 5920 C CD1 . ILE B 228 ? 0.5913 0.8208 0.5651 -0.0171 -0.0401 0.0060 228 ILE B CD1 5921 N N . LYS B 229 ? 0.6018 0.8121 0.6340 -0.0010 -0.0180 0.0697 229 LYS B N 5922 C CA . LYS B 229 ? 0.5186 0.7212 0.5663 -0.0017 -0.0114 0.0769 229 LYS B CA 5923 C C . LYS B 229 ? 0.6618 0.8854 0.7014 -0.0003 -0.0032 0.0862 229 LYS B C 5924 O O . LYS B 229 ? 0.6783 0.9164 0.7118 0.0036 -0.0010 0.1010 229 LYS B O 5925 C CB . LYS B 229 ? 0.4238 0.6130 0.4902 0.0007 -0.0115 0.0905 229 LYS B CB 5926 C CG . LYS B 229 ? 0.5935 0.7742 0.6794 -0.0012 -0.0051 0.0992 229 LYS B CG 5927 C CD . LYS B 229 ? 0.7865 0.9524 0.8903 0.0012 -0.0063 0.1122 229 LYS B CD 5928 C CE . LYS B 229 ? 0.8598 1.0120 0.9876 -0.0025 -0.0022 0.1174 229 LYS B CE 5929 N NZ . LYS B 229 ? 0.8887 1.0189 1.0343 -0.0010 -0.0069 0.1208 229 LYS B NZ 5930 N N . LEU B 230 ? 0.6533 0.8791 0.6925 -0.0028 0.0013 0.0778 230 LEU B N 5931 C CA . LEU B 230 ? 0.6045 0.8523 0.6338 -0.0011 0.0098 0.0841 230 LEU B CA 5932 C C . LEU B 230 ? 0.6159 0.8616 0.6620 -0.0028 0.0183 0.0888 230 LEU B C 5933 O O . LEU B 230 ? 0.7788 1.0095 0.8378 -0.0058 0.0167 0.0778 230 LEU B O 5934 C CB . LEU B 230 ? 0.5626 0.8221 0.5705 -0.0014 0.0078 0.0668 230 LEU B CB 5935 C CG . LEU B 230 ? 0.6823 0.9420 0.6761 -0.0019 -0.0017 0.0570 230 LEU B CG 5936 C CD1 . LEU B 230 ? 0.6076 0.8677 0.5880 -0.0045 -0.0048 0.0359 230 LEU B CD1 5937 C CD2 . LEU B 230 ? 0.8344 1.1156 0.8146 0.0022 -0.0019 0.0697 230 LEU B CD2 5938 N N . ASN B 231 ? 0.5422 0.8045 0.5886 -0.0008 0.0275 0.1059 231 ASN B N 5939 C CA . ASN B 231 ? 0.7142 0.9846 0.7704 -0.0021 0.0375 0.1084 231 ASN B CA 5940 C C . ASN B 231 ? 0.6700 0.9670 0.7026 0.0015 0.0436 0.1052 231 ASN B C 5941 O O . ASN B 231 ? 0.7126 1.0163 0.7233 0.0035 0.0377 0.0940 231 ASN B O 5942 C CB . ASN B 231 ? 0.9043 1.1727 0.9823 -0.0036 0.0450 0.1305 231 ASN B CB 5943 C CG . ASN B 231 ? 0.8498 1.1217 0.9224 -0.0003 0.0444 0.1499 231 ASN B CG 5944 O OD1 . ASN B 231 ? 0.8788 1.1715 0.9298 0.0041 0.0469 0.1564 231 ASN B OD1 5945 N ND2 . ASN B 231 ? 0.6753 0.9270 0.7678 -0.0018 0.0409 0.1592 231 ASN B ND2 5946 N N . ASP B 232 ? 0.5709 0.8837 0.6080 0.0021 0.0552 0.1140 232 ASP B N 5947 C CA . ASP B 232 ? 0.7430 1.0822 0.7562 0.0065 0.0615 0.1099 232 ASP B CA 5948 C C . ASP B 232 ? 0.9291 1.2875 0.9238 0.0108 0.0638 0.1276 232 ASP B C 5949 O O . ASP B 232 ? 0.9492 1.3273 0.9176 0.0149 0.0635 0.1210 232 ASP B O 5950 C CB . ASP B 232 ? 0.8237 1.1756 0.8478 0.0065 0.0740 0.1117 232 ASP B CB 5951 C CG . ASP B 232 ? 0.9272 1.2605 0.9740 0.0027 0.0715 0.0975 232 ASP B CG 5952 O OD1 . ASP B 232 ? 0.8534 1.1728 0.8938 0.0025 0.0620 0.0772 232 ASP B OD1 5953 O OD2 . ASP B 232 ? 0.9764 1.3092 1.0478 -0.0003 0.0788 0.1071 232 ASP B OD2 5954 N N . GLU B 233 ? 1.0018 1.3536 1.0105 0.0100 0.0652 0.1495 233 GLU B N 5955 C CA . GLU B 233 ? 0.9496 1.3179 0.9442 0.0147 0.0677 0.1705 233 GLU B CA 5956 C C . GLU B 233 ? 0.9294 1.2993 0.9043 0.0181 0.0558 0.1651 233 GLU B C 5957 O O . GLU B 233 ? 0.9733 1.3631 0.9297 0.0234 0.0567 0.1778 233 GLU B O 5958 C CB . GLU B 233 ? 0.9715 1.3285 0.9898 0.0128 0.0725 0.1958 233 GLU B CB 5959 C CG . GLU B 233 ? 1.1853 1.5496 1.2208 0.0097 0.0866 0.2082 233 GLU B CG 5960 C CD . GLU B 233 ? 1.4328 1.7953 1.4826 0.0092 0.0935 0.2388 233 GLU B CD 5961 O OE1 . GLU B 233 ? 1.5093 1.8538 1.5665 0.0099 0.0858 0.2471 233 GLU B OE1 5962 O OE2 . GLU B 233 ? 1.4672 1.8463 1.5213 0.0084 0.1070 0.2548 233 GLU B OE2 5963 N N . ASN B 234 ? 0.7909 1.1415 0.7704 0.0152 0.0449 0.1471 234 ASN B N 5964 C CA . ASN B 234 ? 0.7338 1.0867 0.6976 0.0174 0.0336 0.1404 234 ASN B CA 5965 C C . ASN B 234 ? 0.8014 1.1519 0.7534 0.0148 0.0263 0.1131 234 ASN B C 5966 O O . ASN B 234 ? 0.6751 1.0250 0.6180 0.0147 0.0163 0.1046 234 ASN B O 5967 C CB . ASN B 234 ? 0.6863 1.0186 0.6670 0.0171 0.0266 0.1489 234 ASN B CB 5968 C CG . ASN B 234 ? 0.7620 1.0673 0.7596 0.0118 0.0206 0.1321 234 ASN B CG 5969 O OD1 . ASN B 234 ? 0.8837 1.1804 0.8910 0.0079 0.0244 0.1225 234 ASN B OD1 5970 N ND2 . ASN B 234 ? 0.6153 0.9086 0.6161 0.0121 0.0113 0.1288 234 ASN B ND2 5971 N N . CYS B 235 ? 0.8814 1.2307 0.8350 0.0126 0.0314 0.1000 235 CYS B N 5972 C CA . CYS B 235 ? 0.8768 1.2228 0.8192 0.0105 0.0255 0.0744 235 CYS B CA 5973 C C . CYS B 235 ? 0.8484 1.2156 0.7635 0.0132 0.0205 0.0677 235 CYS B C 5974 O O . CYS B 235 ? 0.6652 1.0263 0.5741 0.0106 0.0103 0.0538 235 CYS B O 5975 C CB . CYS B 235 ? 0.9405 1.2878 0.8861 0.0102 0.0336 0.0640 235 CYS B CB 5976 S SG . CYS B 235 ? 0.9603 1.2926 0.9005 0.0072 0.0261 0.0329 235 CYS B SG 5977 N N . GLN B 236 ? 0.8501 1.2433 0.7493 0.0183 0.0275 0.0780 236 GLN B N 5978 C CA . GLN B 236 ? 0.6911 1.1078 0.5627 0.0216 0.0227 0.0707 236 GLN B CA 5979 C C . GLN B 236 ? 0.6849 1.1050 0.5523 0.0221 0.0123 0.0773 236 GLN B C 5980 O O . GLN B 236 ? 0.7095 1.1390 0.5610 0.0213 0.0033 0.0629 236 GLN B O 5981 C CB . GLN B 236 ? 0.7254 1.1706 0.5800 0.0279 0.0332 0.0820 236 GLN B CB 5982 C CG . GLN B 236 ? 0.7203 1.1927 0.5444 0.0321 0.0279 0.0752 236 GLN B CG 5983 C CD . GLN B 236 ? 0.7256 1.1988 0.5353 0.0302 0.0231 0.0451 236 GLN B CD 5984 O OE1 . GLN B 236 ? 0.7087 1.1794 0.5193 0.0306 0.0305 0.0340 236 GLN B OE1 5985 N NE2 . GLN B 236 ? 0.6073 1.0847 0.4045 0.0282 0.0105 0.0319 236 GLN B NE2 5986 N N . ARG B 237 ? 0.7094 1.1220 0.5920 0.0235 0.0132 0.0985 237 ARG B N 5987 C CA . ARG B 237 ? 0.8105 1.2244 0.6931 0.0249 0.0034 0.1051 237 ARG B CA 5988 C C . ARG B 237 ? 0.7485 1.1498 0.6328 0.0192 -0.0077 0.0833 237 ARG B C 5989 O O . ARG B 237 ? 0.7287 1.1440 0.6012 0.0198 -0.0167 0.0784 237 ARG B O 5990 C CB . ARG B 237 ? 0.8765 1.2746 0.7812 0.0265 0.0058 0.1267 237 ARG B CB 5991 C CG . ARG B 237 ? 0.8766 1.2842 0.7786 0.0320 -0.0007 0.1420 237 ARG B CG 5992 C CD . ARG B 237 ? 1.1871 1.6102 1.0843 0.0390 0.0072 0.1689 237 ARG B CD 5993 N NE . ARG B 237 ? 1.4297 1.8420 1.3426 0.0431 0.0050 0.1889 237 ARG B NE 5994 C CZ . ARG B 237 ? 1.4914 1.8827 1.4267 0.0424 0.0114 0.2038 237 ARG B CZ 5995 N NH1 . ARG B 237 ? 1.5300 1.9109 1.4757 0.0373 0.0206 0.2019 237 ARG B NH1 5996 N NH2 . ARG B 237 ? 1.3855 1.7666 1.3340 0.0469 0.0084 0.2204 237 ARG B NH2 5997 N N . LEU B 238 ? 0.5699 0.9462 0.4695 0.0137 -0.0071 0.0711 238 LEU B N 5998 C CA . LEU B 238 ? 0.5286 0.8908 0.4305 0.0077 -0.0163 0.0514 238 LEU B CA 5999 C C . LEU B 238 ? 0.7112 1.0852 0.5935 0.0051 -0.0204 0.0306 238 LEU B C 6000 O O . LEU B 238 ? 0.8054 1.1813 0.6827 0.0013 -0.0297 0.0192 238 LEU B O 6001 C CB . LEU B 238 ? 0.4717 0.8045 0.3930 0.0031 -0.0145 0.0444 238 LEU B CB 6002 C CG . LEU B 238 ? 0.5266 0.8453 0.4483 -0.0031 -0.0233 0.0248 238 LEU B CG 6003 C CD1 . LEU B 238 ? 0.4722 0.7931 0.3970 -0.0035 -0.0312 0.0297 238 LEU B CD1 6004 C CD2 . LEU B 238 ? 0.4219 0.7133 0.3590 -0.0068 -0.0219 0.0167 238 LEU B CD2 6005 N N . MET B 239 ? 0.7466 1.1283 0.6191 0.0069 -0.0133 0.0248 239 MET B N 6006 C CA . MET B 239 ? 0.7276 1.1193 0.5811 0.0053 -0.0168 0.0034 239 MET B CA 6007 C C . MET B 239 ? 0.7639 1.1834 0.5971 0.0076 -0.0234 0.0037 239 MET B C 6008 O O . MET B 239 ? 0.7980 1.2215 0.6205 0.0035 -0.0319 -0.0150 239 MET B O 6009 C CB . MET B 239 ? 0.7851 1.1807 0.6326 0.0084 -0.0068 -0.0022 239 MET B CB 6010 C CG . MET B 239 ? 0.7046 1.0735 0.5668 0.0046 -0.0047 -0.0157 239 MET B CG 6011 S SD . MET B 239 ? 0.8957 1.2715 0.7572 0.0100 0.0089 -0.0170 239 MET B SD 6012 C CE . MET B 239 ? 1.6610 2.0603 1.4918 0.0134 0.0074 -0.0363 239 MET B CE 6013 N N . THR B 240 ? 0.7409 1.1791 0.5696 0.0141 -0.0201 0.0251 240 THR B N 6014 C CA . THR B 240 ? 0.6569 1.1232 0.4672 0.0177 -0.0271 0.0287 240 THR B CA 6015 C C . THR B 240 ? 0.7819 1.2448 0.6006 0.0136 -0.0389 0.0264 240 THR B C 6016 O O . THR B 240 ? 0.6640 1.1430 0.4701 0.0115 -0.0486 0.0139 240 THR B O 6017 C CB . THR B 240 ? 0.6388 1.1229 0.4450 0.0262 -0.0206 0.0558 240 THR B CB 6018 O OG1 . THR B 240 ? 0.6950 1.1871 0.4923 0.0301 -0.0086 0.0596 240 THR B OG1 6019 C CG2 . THR B 240 ? 0.4950 1.0083 0.2828 0.0306 -0.0291 0.0599 240 THR B CG2 6020 N N . PHE B 241 ? 0.8328 1.2762 0.6734 0.0128 -0.0381 0.0384 241 PHE B N 6021 C CA . PHE B 241 ? 0.7488 1.1893 0.5995 0.0101 -0.0476 0.0380 241 PHE B CA 6022 C C . PHE B 241 ? 0.7864 1.2173 0.6371 0.0007 -0.0550 0.0133 241 PHE B C 6023 O O . PHE B 241 ? 0.8668 1.3082 0.7170 -0.0026 -0.0646 0.0071 241 PHE B O 6024 C CB . PHE B 241 ? 0.6872 1.1056 0.5612 0.0114 -0.0442 0.0531 241 PHE B CB 6025 C CG . PHE B 241 ? 0.7568 1.1681 0.6433 0.0080 -0.0526 0.0495 241 PHE B CG 6026 C CD1 . PHE B 241 ? 0.8403 1.2680 0.7286 0.0135 -0.0580 0.0625 241 PHE B CD1 6027 C CD2 . PHE B 241 ? 0.7084 1.0975 0.6051 0.0001 -0.0548 0.0337 241 PHE B CD2 6028 C CE1 . PHE B 241 ? 0.8502 1.2737 0.7512 0.0110 -0.0649 0.0590 241 PHE B CE1 6029 C CE2 . PHE B 241 ? 0.7296 1.1141 0.6374 -0.0030 -0.0614 0.0310 241 PHE B CE2 6030 C CZ . PHE B 241 ? 0.7005 1.1027 0.6109 0.0025 -0.0662 0.0432 241 PHE B CZ 6031 N N . LEU B 242 ? 0.7734 1.1852 0.6257 -0.0036 -0.0505 -0.0003 242 LEU B N 6032 C CA . LEU B 242 ? 0.8597 1.2570 0.7136 -0.0126 -0.0564 -0.0227 242 LEU B CA 6033 C C . LEU B 242 ? 0.8200 1.2364 0.6536 -0.0147 -0.0620 -0.0398 242 LEU B C 6034 O O . LEU B 242 ? 0.7054 1.1197 0.5385 -0.0225 -0.0704 -0.0560 242 LEU B O 6035 C CB . LEU B 242 ? 0.7627 1.1322 0.6254 -0.0150 -0.0499 -0.0305 242 LEU B CB 6036 C CG . LEU B 242 ? 0.5479 0.8904 0.4319 -0.0167 -0.0472 -0.0235 242 LEU B CG 6037 C CD1 . LEU B 242 ? 0.5438 0.8668 0.4328 -0.0167 -0.0402 -0.0300 242 LEU B CD1 6038 C CD2 . LEU B 242 ? 0.5639 0.8948 0.4554 -0.0241 -0.0552 -0.0328 242 LEU B CD2 6039 N N . SER B 243 ? 0.8755 1.3107 0.6925 -0.0079 -0.0570 -0.0364 243 SER B N 6040 C CA . SER B 243 ? 0.9748 1.4281 0.7701 -0.0084 -0.0611 -0.0542 243 SER B CA 6041 C C . SER B 243 ? 0.9399 1.4092 0.7299 -0.0139 -0.0743 -0.0645 243 SER B C 6042 O O . SER B 243 ? 1.0339 1.5022 0.8159 -0.0201 -0.0805 -0.0868 243 SER B O 6043 C CB . SER B 243 ? 1.0322 1.5107 0.8089 0.0014 -0.0543 -0.0437 243 SER B CB 6044 O OG . SER B 243 ? 1.2194 1.7206 0.9730 0.0017 -0.0606 -0.0601 243 SER B OG 6045 N N . GLU B 244 ? 0.8337 1.3175 0.6294 -0.0116 -0.0789 -0.0486 244 GLU B N 6046 C CA . GLU B 244 ? 0.8208 1.3255 0.6126 -0.0158 -0.0916 -0.0565 244 GLU B CA 6047 C C . GLU B 244 ? 0.8947 1.3831 0.7062 -0.0263 -0.0982 -0.0645 244 GLU B C 6048 O O . GLU B 244 ? 1.0168 1.5176 0.8266 -0.0334 -0.1085 -0.0782 244 GLU B O 6049 C CB . GLU B 244 ? 0.8561 1.3906 0.6419 -0.0067 -0.0941 -0.0362 244 GLU B CB 6050 C CG . GLU B 244 ? 1.0901 1.6565 0.8625 -0.0082 -0.1069 -0.0462 244 GLU B CG 6051 C CD . GLU B 244 ? 1.2884 1.8673 1.0367 -0.0087 -0.1088 -0.0658 244 GLU B CD 6052 O OE1 . GLU B 244 ? 1.3405 1.9186 1.0755 -0.0017 -0.0989 -0.0616 244 GLU B OE1 6053 O OE2 . GLU B 244 ? 1.3226 1.9125 1.0658 -0.0162 -0.1200 -0.0859 244 GLU B OE2 6054 N N . LEU B 245 ? 0.8577 1.3196 0.6879 -0.0274 -0.0922 -0.0560 245 LEU B N 6055 C CA . LEU B 245 ? 0.9125 1.3572 0.7597 -0.0372 -0.0968 -0.0637 245 LEU B CA 6056 C C . LEU B 245 ? 0.9310 1.3551 0.7753 -0.0462 -0.0974 -0.0861 245 LEU B C 6057 O O . LEU B 245 ? 0.8964 1.3091 0.7502 -0.0562 -0.1026 -0.0972 245 LEU B O 6058 C CB . LEU B 245 ? 0.8807 1.3038 0.7467 -0.0345 -0.0903 -0.0482 245 LEU B CB 6059 C CG . LEU B 245 ? 0.8793 1.3172 0.7517 -0.0253 -0.0895 -0.0258 245 LEU B CG 6060 C CD1 . LEU B 245 ? 0.8208 1.2342 0.7083 -0.0212 -0.0812 -0.0121 245 LEU B CD1 6061 C CD2 . LEU B 245 ? 0.9310 1.3864 0.8117 -0.0284 -0.0986 -0.0256 245 LEU B CD2 6062 N N . THR B 246 ? 0.9616 1.3818 0.7927 -0.0421 -0.0919 -0.0923 246 THR B N 6063 C CA . THR B 246 ? 0.9547 1.3517 0.7837 -0.0479 -0.0907 -0.1118 246 THR B CA 6064 C C . THR B 246 ? 1.0937 1.5039 0.9048 -0.0510 -0.0970 -0.1332 246 THR B C 6065 O O . THR B 246 ? 1.0340 1.4246 0.8450 -0.0577 -0.0988 -0.1521 246 THR B O 6066 C CB . THR B 246 ? 0.8949 1.2750 0.7246 -0.0409 -0.0794 -0.1059 246 THR B CB 6067 O OG1 . THR B 246 ? 0.7803 1.1338 0.6291 -0.0433 -0.0760 -0.0984 246 THR B OG1 6068 C CG2 . THR B 246 ? 0.9042 1.2746 0.7225 -0.0419 -0.0779 -0.1264 246 THR B CG2 6069 N N . ARG B 247 ? 1.1963 1.6389 0.9917 -0.0457 -0.1005 -0.1304 247 ARG B N 6070 C CA . ARG B 247 ? 1.0304 1.4888 0.8081 -0.0487 -0.1084 -0.1518 247 ARG B CA 6071 C C . ARG B 247 ? 1.0163 1.4633 0.8058 -0.0627 -0.1184 -0.1678 247 ARG B C 6072 O O . ARG B 247 ? 0.9536 1.4009 0.7596 -0.0679 -0.1219 -0.1584 247 ARG B O 6073 C CB . ARG B 247 ? 0.9464 1.4445 0.7074 -0.0416 -0.1131 -0.1444 247 ARG B CB 6074 C CG . ARG B 247 ? 1.1625 1.6734 0.9054 -0.0286 -0.1032 -0.1345 247 ARG B CG 6075 C CD . ARG B 247 ? 1.2697 1.8206 0.9928 -0.0212 -0.1084 -0.1278 247 ARG B CD 6076 N NE . ARG B 247 ? 1.4860 2.0536 1.1963 -0.0273 -0.1213 -0.1514 247 ARG B NE 6077 C CZ . ARG B 247 ? 1.6995 2.3033 1.3913 -0.0226 -0.1291 -0.1514 247 ARG B CZ 6078 N NH1 . ARG B 247 ? 1.7622 2.3888 1.4452 -0.0111 -0.1249 -0.1275 247 ARG B NH1 6079 N NH2 . ARG B 247 ? 1.7460 2.3629 1.4282 -0.0294 -0.1417 -0.1753 247 ARG B NH2 6080 N N . GLY B 248 ? 1.0276 1.4639 0.8096 -0.0688 -0.1223 -0.1919 248 GLY B N 6081 C CA . GLY B 248 ? 1.1864 1.6024 0.9824 -0.0829 -0.1292 -0.2062 248 GLY B CA 6082 C C . GLY B 248 ? 1.3977 1.8297 1.1906 -0.0935 -0.1427 -0.2251 248 GLY B C 6083 O O . GLY B 248 ? 1.2567 1.6947 1.0332 -0.0936 -0.1472 -0.2453 248 GLY B O 6084 N N . PRO B 249 ? 1.5407 1.9812 1.3500 -0.1024 -0.1493 -0.2192 249 PRO B N 6085 C CA . PRO B 249 ? 1.5995 2.0330 1.4162 -0.1178 -0.1594 -0.2400 249 PRO B CA 6086 C C . PRO B 249 ? 1.5012 1.8911 1.3251 -0.1235 -0.1540 -0.2494 249 PRO B C 6087 O O . PRO B 249 ? 1.4298 1.8043 1.2413 -0.1164 -0.1483 -0.2575 249 PRO B O 6088 C CB . PRO B 249 ? 1.5034 1.9501 1.3404 -0.1255 -0.1641 -0.2275 249 PRO B CB 6089 C CG . PRO B 249 ? 1.4738 1.9515 1.3050 -0.1126 -0.1622 -0.2072 249 PRO B CG 6090 C CD . PRO B 249 ? 1.4832 1.9482 1.3012 -0.0986 -0.1504 -0.1977 249 PRO B CD 6091 N N . THR B 250 ? 1.3542 1.7254 1.1982 -0.1354 -0.1552 -0.2475 250 THR B N 6092 C CA . THR B 250 ? 1.4659 1.7958 1.3169 -0.1409 -0.1509 -0.2554 250 THR B CA 6093 C C . THR B 250 ? 1.4168 1.7259 1.2691 -0.1298 -0.1385 -0.2390 250 THR B C 6094 O O . THR B 250 ? 1.4118 1.7346 1.2534 -0.1166 -0.1327 -0.2292 250 THR B O 6095 C CB . THR B 250 ? 1.5505 1.8670 1.4219 -0.1577 -0.1558 -0.2575 250 THR B CB 6096 O OG1 . THR B 250 ? 1.6173 1.9415 1.5029 -0.1569 -0.1517 -0.2354 250 THR B OG1 6097 C CG2 . THR B 250 ? 1.4302 1.7687 1.3026 -0.1699 -0.1688 -0.2745 250 THR B CG2 6098 N N . LEU B 251 ? 1.2926 1.5693 1.1583 -0.1354 -0.1347 -0.2360 251 LEU B N 6099 C CA . LEU B 251 ? 1.1114 1.3672 0.9801 -0.1260 -0.1243 -0.2221 251 LEU B CA 6100 C C . LEU B 251 ? 1.0743 1.3390 0.9553 -0.1242 -0.1207 -0.1999 251 LEU B C 6101 O O . LEU B 251 ? 1.1859 1.4657 1.0763 -0.1323 -0.1258 -0.1961 251 LEU B O 6102 C CB . LEU B 251 ? 0.9260 1.1414 0.8012 -0.1314 -0.1223 -0.2302 251 LEU B CB 6103 C CG . LEU B 251 ? 0.9328 1.1309 0.7971 -0.1300 -0.1235 -0.2514 251 LEU B CG 6104 C CD1 . LEU B 251 ? 0.9073 1.1167 0.7573 -0.1145 -0.1170 -0.2502 251 LEU B CD1 6105 C CD2 . LEU B 251 ? 1.0394 1.2480 0.8993 -0.1408 -0.1341 -0.2717 251 LEU B CD2 6106 N N . LEU B 252 ? 0.9005 1.1564 0.7821 -0.1134 -0.1121 -0.1859 252 LEU B N 6107 C CA . LEU B 252 ? 0.8581 1.1168 0.7516 -0.1108 -0.1082 -0.1660 252 LEU B CA 6108 C C . LEU B 252 ? 0.9596 1.1927 0.8564 -0.1032 -0.0998 -0.1578 252 LEU B C 6109 O O . LEU B 252 ? 0.9942 1.2162 0.8832 -0.0971 -0.0961 -0.1640 252 LEU B O 6110 C CB . LEU B 252 ? 0.8236 1.1161 0.7139 -0.1029 -0.1084 -0.1531 252 LEU B CB 6111 C CG . LEU B 252 ? 0.8498 1.1485 0.7321 -0.0888 -0.1012 -0.1422 252 LEU B CG 6112 C CD1 . LEU B 252 ? 0.8379 1.1614 0.7238 -0.0822 -0.1006 -0.1238 252 LEU B CD1 6113 C CD2 . LEU B 252 ? 0.8009 1.1097 0.6655 -0.0846 -0.1017 -0.1546 252 LEU B CD2 6114 N N . ASN B 253 ? 1.0052 1.2302 0.9140 -0.1035 -0.0970 -0.1444 253 ASN B N 6115 C CA . ASN B 253 ? 0.9370 1.1409 0.8500 -0.0962 -0.0901 -0.1355 253 ASN B CA 6116 C C . ASN B 253 ? 0.8912 1.1124 0.8048 -0.0851 -0.0855 -0.1199 253 ASN B C 6117 O O . ASN B 253 ? 0.8522 1.0982 0.7666 -0.0841 -0.0878 -0.1124 253 ASN B O 6118 C CB . ASN B 253 ? 0.8599 1.0441 0.7843 -0.1023 -0.0897 -0.1306 253 ASN B CB 6119 C CG . ASN B 253 ? 1.0284 1.1926 0.9532 -0.1137 -0.0936 -0.1441 253 ASN B CG 6120 O OD1 . ASN B 253 ? 0.9758 1.1307 0.8930 -0.1148 -0.0953 -0.1578 253 ASN B OD1 6121 N ND2 . ASN B 253 ? 1.3151 1.4721 1.2490 -0.1221 -0.0947 -0.1398 253 ASN B ND2 6122 N N . VAL B 254 ? 0.8552 1.0637 0.7692 -0.0769 -0.0793 -0.1150 254 VAL B N 6123 C CA . VAL B 254 ? 0.7476 0.9676 0.6649 -0.0673 -0.0745 -0.0992 254 VAL B CA 6124 C C . VAL B 254 ? 0.8534 1.0510 0.7818 -0.0639 -0.0701 -0.0908 254 VAL B C 6125 O O . VAL B 254 ? 0.8091 0.9841 0.7387 -0.0644 -0.0687 -0.0974 254 VAL B O 6126 C CB . VAL B 254 ? 0.6388 0.8729 0.5458 -0.0598 -0.0707 -0.0995 254 VAL B CB 6127 C CG1 . VAL B 254 ? 0.5900 0.8291 0.5030 -0.0507 -0.0644 -0.0823 254 VAL B CG1 6128 C CG2 . VAL B 254 ? 0.6655 0.9270 0.5611 -0.0614 -0.0755 -0.1041 254 VAL B CG2 6129 N N . THR B 255 ? 0.7714 0.9756 0.7080 -0.0601 -0.0688 -0.0768 255 THR B N 6130 C CA . THR B 255 ? 0.6255 0.8110 0.5724 -0.0563 -0.0655 -0.0693 255 THR B CA 6131 C C . THR B 255 ? 0.7005 0.8948 0.6530 -0.0475 -0.0612 -0.0550 255 THR B C 6132 O O . THR B 255 ? 0.7083 0.9204 0.6625 -0.0449 -0.0620 -0.0456 255 THR B O 6133 C CB . THR B 255 ? 0.7194 0.8974 0.6730 -0.0609 -0.0681 -0.0674 255 THR B CB 6134 O OG1 . THR B 255 ? 0.9984 1.1637 0.9482 -0.0696 -0.0712 -0.0794 255 THR B OG1 6135 C CG2 . THR B 255 ? 0.6930 0.8536 0.6558 -0.0560 -0.0653 -0.0601 255 THR B CG2 6136 N N . LEU B 256 ? 0.6174 0.7992 0.5740 -0.0430 -0.0567 -0.0533 256 LEU B N 6137 C CA . LEU B 256 ? 0.5379 0.7233 0.5028 -0.0358 -0.0522 -0.0398 256 LEU B CA 6138 C C . LEU B 256 ? 0.5853 0.7510 0.5630 -0.0344 -0.0522 -0.0356 256 LEU B C 6139 O O . LEU B 256 ? 0.6494 0.7962 0.6293 -0.0361 -0.0527 -0.0428 256 LEU B O 6140 C CB . LEU B 256 ? 0.5115 0.6991 0.4742 -0.0323 -0.0469 -0.0409 256 LEU B CB 6141 C CG . LEU B 256 ? 0.6249 0.8374 0.5769 -0.0294 -0.0443 -0.0373 256 LEU B CG 6142 C CD1 . LEU B 256 ? 0.4823 0.7115 0.4230 -0.0332 -0.0500 -0.0420 256 LEU B CD1 6143 C CD2 . LEU B 256 ? 0.6638 0.8777 0.6098 -0.0275 -0.0395 -0.0449 256 LEU B CD2 6144 N N . GLN B 257 ? 0.6272 0.7971 0.6127 -0.0308 -0.0522 -0.0244 257 GLN B N 6145 C CA . GLN B 257 ? 0.5976 0.7498 0.5943 -0.0288 -0.0527 -0.0214 257 GLN B CA 6146 C C . GLN B 257 ? 0.6558 0.8069 0.6640 -0.0226 -0.0492 -0.0096 257 GLN B C 6147 O O . GLN B 257 ? 0.7404 0.9067 0.7494 -0.0190 -0.0474 0.0008 257 GLN B O 6148 C CB . GLN B 257 ? 0.6419 0.7967 0.6393 -0.0298 -0.0561 -0.0202 257 GLN B CB 6149 C CG . GLN B 257 ? 0.8343 0.9738 0.8296 -0.0346 -0.0588 -0.0293 257 GLN B CG 6150 C CD . GLN B 257 ? 1.0221 1.1680 1.0188 -0.0353 -0.0608 -0.0272 257 GLN B CD 6151 O OE1 . GLN B 257 ? 1.1434 1.2969 1.1344 -0.0415 -0.0629 -0.0323 257 GLN B OE1 6152 N NE2 . GLN B 257 ? 0.9470 1.0906 0.9526 -0.0289 -0.0601 -0.0199 257 GLN B NE2 6153 N N . HIS B 258 ? 0.6845 0.8177 0.7023 -0.0214 -0.0485 -0.0110 258 HIS B N 6154 C CA . HIS B 258 ? 0.7092 0.8390 0.7407 -0.0169 -0.0455 -0.0006 258 HIS B CA 6155 C C . HIS B 258 ? 0.7531 0.8963 0.7856 -0.0153 -0.0398 0.0075 258 HIS B C 6156 O O . HIS B 258 ? 0.8550 1.0039 0.8951 -0.0116 -0.0371 0.0203 258 HIS B O 6157 C CB . HIS B 258 ? 0.6151 0.7461 0.6525 -0.0130 -0.0472 0.0077 258 HIS B CB 6158 C CG . HIS B 258 ? 0.7796 0.9030 0.8136 -0.0143 -0.0516 0.0003 258 HIS B CG 6159 N ND1 . HIS B 258 ? 0.8404 0.9769 0.8680 -0.0145 -0.0535 0.0011 258 HIS B ND1 6160 C CD2 . HIS B 258 ? 0.7235 0.8293 0.7592 -0.0154 -0.0543 -0.0078 258 HIS B CD2 6161 C CE1 . HIS B 258 ? 0.6258 0.7531 0.6519 -0.0160 -0.0563 -0.0057 258 HIS B CE1 6162 N NE2 . HIS B 258 ? 0.6532 0.7615 0.6831 -0.0163 -0.0568 -0.0110 258 HIS B NE2 6163 N N . ILE B 259 ? 0.7029 0.8507 0.7278 -0.0175 -0.0377 0.0002 259 ILE B N 6164 C CA . ILE B 259 ? 0.7385 0.9006 0.7627 -0.0158 -0.0313 0.0066 259 ILE B CA 6165 C C . ILE B 259 ? 0.7852 0.9378 0.8257 -0.0148 -0.0274 0.0098 259 ILE B C 6166 O O . ILE B 259 ? 0.9593 1.1003 1.0033 -0.0163 -0.0286 -0.0003 259 ILE B O 6167 C CB . ILE B 259 ? 0.6833 0.8545 0.6927 -0.0178 -0.0304 -0.0046 259 ILE B CB 6168 C CG1 . ILE B 259 ? 0.9471 1.1175 0.9439 -0.0215 -0.0366 -0.0151 259 ILE B CG1 6169 C CG2 . ILE B 259 ? 0.3601 0.5538 0.3619 -0.0152 -0.0245 0.0031 259 ILE B CG2 6170 C CD1 . ILE B 259 ? 1.0382 1.1871 1.0380 -0.0246 -0.0409 -0.0260 259 ILE B CD1 6171 N N . GLU B 260 ? 0.6284 0.7862 0.6798 -0.0125 -0.0228 0.0244 260 GLU B N 6172 C CA . GLU B 260 ? 0.6078 0.7616 0.6757 -0.0126 -0.0179 0.0286 260 GLU B CA 6173 C C . GLU B 260 ? 0.7265 0.9012 0.7883 -0.0114 -0.0097 0.0356 260 GLU B C 6174 O O . GLU B 260 ? 0.8482 1.0369 0.9038 -0.0092 -0.0069 0.0479 260 GLU B O 6175 C CB . GLU B 260 ? 0.7277 0.8720 0.8141 -0.0117 -0.0177 0.0410 260 GLU B CB 6176 C CG . GLU B 260 ? 0.8049 0.9538 0.9076 -0.0123 -0.0102 0.0514 260 GLU B CG 6177 C CD . GLU B 260 ? 0.9622 1.1054 1.0807 -0.0114 -0.0088 0.0673 260 GLU B CD 6178 O OE1 . GLU B 260 ? 1.1355 1.2901 1.2602 -0.0113 -0.0010 0.0820 260 GLU B OE1 6179 O OE2 . GLU B 260 ? 0.8714 0.9986 0.9957 -0.0105 -0.0152 0.0652 260 GLU B OE2 6180 N N . THR B 261 ? 0.7554 0.9334 0.8184 -0.0121 -0.0059 0.0280 261 THR B N 6181 C CA . THR B 261 ? 0.7633 0.9633 0.8162 -0.0102 0.0021 0.0315 261 THR B CA 6182 C C . THR B 261 ? 0.6676 0.8707 0.7332 -0.0101 0.0088 0.0294 261 THR B C 6183 O O . THR B 261 ? 0.9002 1.0886 0.9779 -0.0115 0.0054 0.0201 261 THR B O 6184 C CB . THR B 261 ? 0.5769 0.7857 0.6057 -0.0097 -0.0010 0.0185 261 THR B CB 6185 O OG1 . THR B 261 ? 0.5808 0.8038 0.6026 -0.0078 0.0056 0.0130 261 THR B OG1 6186 C CG2 . THR B 261 ? 0.6549 0.8446 0.6814 -0.0123 -0.0095 0.0024 261 THR B CG2 6187 N N . THR B 262 ? 0.5565 0.7803 0.6197 -0.0082 0.0183 0.0387 262 THR B N 6188 C CA . THR B 262 ? 0.6594 0.8921 0.7309 -0.0073 0.0259 0.0348 262 THR B CA 6189 C C . THR B 262 ? 0.7004 0.9295 0.7603 -0.0057 0.0224 0.0137 262 THR B C 6190 O O . THR B 262 ? 0.7231 0.9477 0.7648 -0.0057 0.0158 0.0038 262 THR B O 6191 C CB . THR B 262 ? 0.6889 0.9484 0.7526 -0.0045 0.0374 0.0472 262 THR B CB 6192 O OG1 . THR B 262 ? 0.8090 1.0703 0.8893 -0.0064 0.0424 0.0681 262 THR B OG1 6193 C CG2 . THR B 262 ? 0.8000 1.0724 0.8676 -0.0023 0.0456 0.0397 262 THR B CG2 6194 N N . TRP B 263 ? 0.8138 1.0448 0.8856 -0.0043 0.0266 0.0070 263 TRP B N 6195 C CA . TRP B 263 ? 0.8558 1.0857 0.9157 -0.0013 0.0249 -0.0119 263 TRP B CA 6196 C C . TRP B 263 ? 0.8124 1.0651 0.8501 0.0025 0.0315 -0.0138 263 TRP B C 6197 O O . TRP B 263 ? 0.6595 0.9097 0.6774 0.0034 0.0265 -0.0274 263 TRP B O 6198 C CB . TRP B 263 ? 0.8010 1.0273 0.8802 0.0006 0.0270 -0.0193 263 TRP B CB 6199 C CG . TRP B 263 ? 0.7311 0.9525 0.7982 0.0046 0.0242 -0.0390 263 TRP B CG 6200 C CD1 . TRP B 263 ? 0.6778 0.9128 0.7446 0.0101 0.0314 -0.0474 263 TRP B CD1 6201 C CD2 . TRP B 263 ? 0.6313 0.8326 0.6846 0.0035 0.0138 -0.0525 263 TRP B CD2 6202 N NE1 . TRP B 263 ? 0.6386 0.8611 0.6925 0.0129 0.0254 -0.0658 263 TRP B NE1 6203 C CE2 . TRP B 263 ? 0.6185 0.8199 0.6644 0.0084 0.0147 -0.0686 263 TRP B CE2 6204 C CE3 . TRP B 263 ? 0.4925 0.6761 0.5397 -0.0009 0.0043 -0.0522 263 TRP B CE3 6205 C CZ2 . TRP B 263 ? 0.5606 0.7429 0.5939 0.0082 0.0061 -0.0836 263 TRP B CZ2 6206 C CZ3 . TRP B 263 ? 0.4571 0.6241 0.4917 -0.0015 -0.0036 -0.0666 263 TRP B CZ3 6207 C CH2 . TRP B 263 ? 0.4619 0.6274 0.4899 0.0026 -0.0028 -0.0818 263 TRP B CH2 6208 N N . LYS B 264 ? 0.8706 1.1456 0.9117 0.0043 0.0426 -0.0003 264 LYS B N 6209 C CA . LYS B 264 ? 0.8359 1.1356 0.8543 0.0085 0.0496 -0.0001 264 LYS B CA 6210 C C . LYS B 264 ? 0.8508 1.1492 0.8456 0.0076 0.0415 -0.0033 264 LYS B C 6211 O O . LYS B 264 ? 0.8210 1.1278 0.7943 0.0103 0.0402 -0.0168 264 LYS B O 6212 C CB . LYS B 264 ? 0.6789 1.0009 0.7043 0.0093 0.0617 0.0215 264 LYS B CB 6213 C CG . LYS B 264 ? 0.7121 1.0633 0.7149 0.0148 0.0710 0.0229 264 LYS B CG 6214 C CD . LYS B 264 ? 0.7893 1.1616 0.8032 0.0152 0.0847 0.0457 264 LYS B CD 6215 C CE . LYS B 264 ? 0.9165 1.3183 0.9178 0.0216 0.0976 0.0428 264 LYS B CE 6216 N NZ . LYS B 264 ? 1.0260 1.4522 0.9989 0.0257 0.1022 0.0519 264 LYS B NZ 6217 N N . CYS B 265 ? 0.7841 1.0722 0.7843 0.0038 0.0358 0.0084 265 CYS B N 6218 C CA . CYS B 265 ? 0.7276 1.0172 0.7090 0.0028 0.0284 0.0080 265 CYS B CA 6219 C C . CYS B 265 ? 0.6681 0.9396 0.6419 0.0002 0.0176 -0.0117 265 CYS B C 6220 O O . CYS B 265 ? 0.6634 0.9401 0.6187 -0.0005 0.0121 -0.0185 265 CYS B O 6221 C CB . CYS B 265 ? 0.6344 0.9194 0.6256 0.0008 0.0262 0.0270 265 CYS B CB 6222 S SG . CYS B 265 ? 1.2610 1.5548 1.2306 0.0011 0.0183 0.0300 265 CYS B SG 6223 N N . SER B 266 ? 0.6622 0.9127 0.6508 -0.0015 0.0145 -0.0204 266 SER B N 6224 C CA . SER B 266 ? 0.6549 0.8865 0.6371 -0.0042 0.0050 -0.0373 266 SER B CA 6225 C C . SER B 266 ? 0.7514 0.9892 0.7176 -0.0016 0.0059 -0.0548 266 SER B C 6226 O O . SER B 266 ? 0.7644 0.9983 0.7154 -0.0040 -0.0008 -0.0664 266 SER B O 6227 C CB . SER B 266 ? 0.6288 0.8365 0.6301 -0.0060 0.0010 -0.0403 266 SER B CB 6228 O OG . SER B 266 ? 0.6801 0.8791 0.6926 -0.0088 -0.0024 -0.0278 266 SER B OG 6229 N N . VAL B 267 ? 0.7461 0.9943 0.7166 0.0032 0.0145 -0.0569 267 VAL B N 6230 C CA . VAL B 267 ? 0.7041 0.9605 0.6596 0.0075 0.0169 -0.0735 267 VAL B CA 6231 C C . VAL B 267 ? 0.7799 1.0584 0.7113 0.0085 0.0178 -0.0740 267 VAL B C 6232 O O . VAL B 267 ? 0.7173 0.9973 0.6317 0.0096 0.0146 -0.0911 267 VAL B O 6233 C CB . VAL B 267 ? 0.5550 0.8215 0.5224 0.0134 0.0273 -0.0737 267 VAL B CB 6234 C CG1 . VAL B 267 ? 0.6321 0.9032 0.5856 0.0190 0.0292 -0.0937 267 VAL B CG1 6235 C CG2 . VAL B 267 ? 0.4398 0.6868 0.4321 0.0121 0.0251 -0.0719 267 VAL B CG2 6236 N N . LYS B 268 ? 0.7397 1.0348 0.6699 0.0084 0.0214 -0.0553 268 LYS B N 6237 C CA . LYS B 268 ? 0.6653 0.9809 0.5730 0.0092 0.0201 -0.0535 268 LYS B CA 6238 C C . LYS B 268 ? 0.7334 1.0372 0.6331 0.0034 0.0075 -0.0610 268 LYS B C 6239 O O . LYS B 268 ? 0.8194 1.1300 0.7007 0.0029 0.0027 -0.0750 268 LYS B O 6240 C CB . LYS B 268 ? 0.5885 0.9233 0.4984 0.0110 0.0270 -0.0293 268 LYS B CB 6241 C CG . LYS B 268 ? 0.6815 1.0347 0.5951 0.0164 0.0405 -0.0215 268 LYS B CG 6242 C CD . LYS B 268 ? 0.8136 1.1853 0.7282 0.0179 0.0475 0.0040 268 LYS B CD 6243 C CE . LYS B 268 ? 0.8182 1.2132 0.7318 0.0232 0.0621 0.0111 268 LYS B CE 6244 N NZ . LYS B 268 ? 0.9134 1.3228 0.8330 0.0237 0.0702 0.0387 268 LYS B NZ 6245 N N . LEU B 269 ? 0.7015 0.9885 0.6159 -0.0011 0.0024 -0.0521 269 LEU B N 6246 C CA . LEU B 269 ? 0.6911 0.9673 0.6012 -0.0068 -0.0084 -0.0582 269 LEU B CA 6247 C C . LEU B 269 ? 0.8075 1.0711 0.7086 -0.0097 -0.0144 -0.0811 269 LEU B C 6248 O O . LEU B 269 ? 0.7292 0.9990 0.6163 -0.0130 -0.0210 -0.0899 269 LEU B O 6249 C CB . LEU B 269 ? 0.6232 0.8794 0.5524 -0.0102 -0.0118 -0.0483 269 LEU B CB 6250 C CG . LEU B 269 ? 0.5372 0.8025 0.4728 -0.0092 -0.0105 -0.0274 269 LEU B CG 6251 C CD1 . LEU B 269 ? 0.6107 0.8594 0.5545 -0.0136 -0.0184 -0.0264 269 LEU B CD1 6252 C CD2 . LEU B 269 ? 0.6765 0.9683 0.5943 -0.0067 -0.0103 -0.0220 269 LEU B CD2 6253 N N . PHE B 270 ? 0.9497 1.1955 0.8600 -0.0086 -0.0126 -0.0907 270 PHE B N 6254 C CA . PHE B 270 ? 0.8974 1.1289 0.7999 -0.0105 -0.0177 -0.1121 270 PHE B CA 6255 C C . PHE B 270 ? 0.8098 1.0607 0.6916 -0.0076 -0.0165 -0.1245 270 PHE B C 6256 O O . PHE B 270 ? 0.8861 1.1342 0.7563 -0.0122 -0.0241 -0.1378 270 PHE B O 6257 C CB . PHE B 270 ? 0.8422 1.0544 0.7577 -0.0073 -0.0149 -0.1193 270 PHE B CB 6258 C CG . PHE B 270 ? 0.7256 0.9164 0.6594 -0.0103 -0.0180 -0.1110 270 PHE B CG 6259 C CD1 . PHE B 270 ? 0.7462 0.9336 0.6972 -0.0062 -0.0125 -0.1035 270 PHE B CD1 6260 C CD2 . PHE B 270 ? 0.6584 0.8342 0.5925 -0.0171 -0.0264 -0.1109 270 PHE B CD2 6261 C CE1 . PHE B 270 ? 0.7122 0.8809 0.6791 -0.0085 -0.0162 -0.0969 270 PHE B CE1 6262 C CE2 . PHE B 270 ? 0.7454 0.9027 0.6945 -0.0190 -0.0290 -0.1037 270 PHE B CE2 6263 C CZ . PHE B 270 ? 0.6603 0.8138 0.6251 -0.0145 -0.0244 -0.0972 270 PHE B CZ 6264 N N . GLN B 271 ? 0.7365 1.0077 0.6141 -0.0003 -0.0069 -0.1203 271 GLN B N 6265 C CA . GLN B 271 ? 0.7858 1.0776 0.6422 0.0042 -0.0046 -0.1326 271 GLN B CA 6266 C C . GLN B 271 ? 0.8960 1.2058 0.7352 0.0008 -0.0110 -0.1312 271 GLN B C 6267 O O . GLN B 271 ? 0.8718 1.1892 0.6932 0.0007 -0.0153 -0.1481 271 GLN B O 6268 C CB . GLN B 271 ? 0.7588 1.0730 0.6143 0.0128 0.0083 -0.1239 271 GLN B CB 6269 C CG . GLN B 271 ? 0.7869 1.0897 0.6579 0.0174 0.0152 -0.1284 271 GLN B CG 6270 C CD . GLN B 271 ? 0.8241 1.1218 0.6845 0.0219 0.0147 -0.1530 271 GLN B CD 6271 O OE1 . GLN B 271 ? 0.7564 1.0760 0.6017 0.0286 0.0213 -0.1598 271 GLN B OE1 6272 N NE2 . GLN B 271 ? 0.9229 1.1913 0.7911 0.0186 0.0072 -0.1664 271 GLN B NE2 6273 N N . PHE B 272 ? 0.9416 1.2586 0.7867 -0.0014 -0.0119 -0.1113 272 PHE B N 6274 C CA . PHE B 272 ? 0.9352 1.2704 0.7671 -0.0039 -0.0185 -0.1073 272 PHE B CA 6275 C C . PHE B 272 ? 0.8661 1.1873 0.6953 -0.0123 -0.0305 -0.1236 272 PHE B C 6276 O O . PHE B 272 ? 1.0213 1.3581 0.8350 -0.0144 -0.0371 -0.1320 272 PHE B O 6277 C CB . PHE B 272 ? 0.9637 1.3037 0.8070 -0.0042 -0.0173 -0.0825 272 PHE B CB 6278 C CG . PHE B 272 ? 0.8935 1.2465 0.7291 -0.0075 -0.0262 -0.0782 272 PHE B CG 6279 C CD1 . PHE B 272 ? 0.8857 1.2689 0.7039 -0.0029 -0.0257 -0.0711 272 PHE B CD1 6280 C CD2 . PHE B 272 ? 0.8302 1.1667 0.6759 -0.0150 -0.0350 -0.0809 272 PHE B CD2 6281 C CE1 . PHE B 272 ? 0.8418 1.2388 0.6539 -0.0053 -0.0346 -0.0672 272 PHE B CE1 6282 C CE2 . PHE B 272 ? 0.9013 1.2522 0.7419 -0.0178 -0.0430 -0.0772 272 PHE B CE2 6283 C CZ . PHE B 272 ? 0.8822 1.2635 0.7065 -0.0128 -0.0432 -0.0705 272 PHE B CZ 6284 N N . PHE B 273 ? 0.7481 1.0405 0.5929 -0.0173 -0.0334 -0.1278 273 PHE B N 6285 C CA . PHE B 273 ? 0.7335 1.0104 0.5792 -0.0263 -0.0437 -0.1399 273 PHE B CA 6286 C C . PHE B 273 ? 0.8286 1.0960 0.6641 -0.0280 -0.0472 -0.1644 273 PHE B C 6287 O O . PHE B 273 ? 0.9016 1.1669 0.7313 -0.0353 -0.0561 -0.1768 273 PHE B O 6288 C CB . PHE B 273 ? 0.5342 0.7840 0.3994 -0.0306 -0.0450 -0.1333 273 PHE B CB 6289 C CG . PHE B 273 ? 0.7074 0.9631 0.5820 -0.0321 -0.0461 -0.1142 273 PHE B CG 6290 C CD1 . PHE B 273 ? 0.8195 1.0677 0.7088 -0.0284 -0.0404 -0.0985 273 PHE B CD1 6291 C CD2 . PHE B 273 ? 0.7802 1.0489 0.6502 -0.0371 -0.0533 -0.1125 273 PHE B CD2 6292 C CE1 . PHE B 273 ? 0.7718 1.0236 0.6699 -0.0290 -0.0416 -0.0821 273 PHE B CE1 6293 C CE2 . PHE B 273 ? 0.8693 1.1434 0.7485 -0.0371 -0.0541 -0.0955 273 PHE B CE2 6294 C CZ . PHE B 273 ? 0.8069 1.0716 0.6997 -0.0328 -0.0482 -0.0805 273 PHE B CZ 6295 N N . TRP B 274 ? 0.8038 1.0657 0.6384 -0.0211 -0.0402 -0.1717 274 TRP B N 6296 C CA . TRP B 274 ? 0.8760 1.1209 0.7052 -0.0217 -0.0431 -0.1951 274 TRP B CA 6297 C C . TRP B 274 ? 0.8657 1.1247 0.6756 -0.0246 -0.0500 -0.2129 274 TRP B C 6298 O O . TRP B 274 ? 0.8248 1.0657 0.6337 -0.0316 -0.0580 -0.2301 274 TRP B O 6299 C CB . TRP B 274 ? 0.8806 1.1227 0.7124 -0.0117 -0.0334 -0.1988 274 TRP B CB 6300 C CG . TRP B 274 ? 0.8529 1.0622 0.6968 -0.0123 -0.0350 -0.2093 274 TRP B CG 6301 C CD1 . TRP B 274 ? 0.9087 1.1038 0.7470 -0.0098 -0.0365 -0.2309 274 TRP B CD1 6302 C CD2 . TRP B 274 ? 0.8248 1.0111 0.6878 -0.0149 -0.0355 -0.1986 274 TRP B CD2 6303 N NE1 . TRP B 274 ? 0.9074 1.0719 0.7605 -0.0104 -0.0380 -0.2330 274 TRP B NE1 6304 C CE2 . TRP B 274 ? 0.8391 0.9985 0.7068 -0.0136 -0.0376 -0.2134 274 TRP B CE2 6305 C CE3 . TRP B 274 ? 0.8716 1.0572 0.7476 -0.0176 -0.0349 -0.1784 274 TRP B CE3 6306 C CZ2 . TRP B 274 ? 0.9244 1.0580 0.8083 -0.0149 -0.0391 -0.2078 274 TRP B CZ2 6307 C CZ3 . TRP B 274 ? 0.8588 1.0190 0.7507 -0.0191 -0.0364 -0.1744 274 TRP B CZ3 6308 C CH2 . TRP B 274 ? 0.9319 1.0671 0.8271 -0.0178 -0.0386 -0.1886 274 TRP B CH2 6309 N N . PRO B 275 ? 0.8279 1.1191 0.6222 -0.0194 -0.0473 -0.2087 275 PRO B N 6310 C CA . PRO B 275 ? 0.8864 1.1938 0.6610 -0.0215 -0.0546 -0.2261 275 PRO B CA 6311 C C . PRO B 275 ? 0.9903 1.3008 0.7671 -0.0326 -0.0662 -0.2246 275 PRO B C 6312 O O . PRO B 275 ? 1.1525 1.4669 0.9190 -0.0383 -0.0752 -0.2427 275 PRO B O 6313 C CB . PRO B 275 ? 0.8784 1.2215 0.6367 -0.0117 -0.0474 -0.2167 275 PRO B CB 6314 C CG . PRO B 275 ? 0.7905 1.1317 0.5609 -0.0044 -0.0349 -0.1984 275 PRO B CG 6315 C CD . PRO B 275 ? 0.7926 1.1069 0.5860 -0.0112 -0.0374 -0.1882 275 PRO B CD 6316 N N . ARG B 276 ? 0.9291 1.2381 0.7202 -0.0357 -0.0659 -0.2038 276 ARG B N 6317 C CA . ARG B 276 ? 0.8776 1.1961 0.6717 -0.0442 -0.0751 -0.1987 276 ARG B CA 6318 C C . ARG B 276 ? 1.0226 1.3141 0.8291 -0.0563 -0.0831 -0.2094 276 ARG B C 6319 O O . ARG B 276 ? 1.0386 1.3009 0.8529 -0.0574 -0.0809 -0.2172 276 ARG B O 6320 C CB . ARG B 276 ? 0.7635 1.0938 0.5668 -0.0407 -0.0708 -0.1719 276 ARG B CB 6321 C CG . ARG B 276 ? 0.8207 1.1742 0.6129 -0.0292 -0.0617 -0.1601 276 ARG B CG 6322 C CD . ARG B 276 ? 0.8842 1.2537 0.6824 -0.0257 -0.0591 -0.1344 276 ARG B CD 6323 N NE . ARG B 276 ? 0.8628 1.2643 0.6433 -0.0173 -0.0554 -0.1263 276 ARG B NE 6324 C CZ . ARG B 276 ? 0.9218 1.3494 0.6917 -0.0170 -0.0622 -0.1213 276 ARG B CZ 6325 N NH1 . ARG B 276 ? 0.9598 1.3863 0.7372 -0.0250 -0.0726 -0.1238 276 ARG B NH1 6326 N NH2 . ARG B 276 ? 0.9838 1.4403 0.7361 -0.0085 -0.0585 -0.1129 276 ARG B NH2 6327 N N . PRO B 277 ? 1.0334 1.3360 0.8418 -0.0652 -0.0924 -0.2098 277 PRO B N 6328 C CA . PRO B 277 ? 0.9454 1.2280 0.7656 -0.0783 -0.1002 -0.2185 277 PRO B CA 6329 C C . PRO B 277 ? 0.9972 1.2604 0.8365 -0.0815 -0.0972 -0.2024 277 PRO B C 6330 O O . PRO B 277 ? 1.1508 1.4195 0.9993 -0.0893 -0.1024 -0.1962 277 PRO B O 6331 C CB . PRO B 277 ? 0.8529 1.1639 0.6690 -0.0848 -0.1099 -0.2206 277 PRO B CB 6332 C CG . PRO B 277 ? 0.9111 1.2535 0.7078 -0.0747 -0.1085 -0.2200 277 PRO B CG 6333 C CD . PRO B 277 ? 0.9470 1.2861 0.7440 -0.0629 -0.0964 -0.2038 277 PRO B CD 6334 N N . VAL B 278 ? 0.9562 1.1985 0.8016 -0.0753 -0.0893 -0.1963 278 VAL B N 6335 C CA . VAL B 278 ? 0.9075 1.1304 0.7694 -0.0778 -0.0870 -0.1827 278 VAL B CA 6336 C C . VAL B 278 ? 0.9435 1.1312 0.8116 -0.0822 -0.0873 -0.1935 278 VAL B C 6337 O O . VAL B 278 ? 0.8089 0.9832 0.6739 -0.0755 -0.0828 -0.2003 278 VAL B O 6338 C CB . VAL B 278 ? 0.7904 1.0184 0.6570 -0.0675 -0.0784 -0.1636 278 VAL B CB 6339 C CG1 . VAL B 278 ? 0.8505 1.0578 0.7331 -0.0697 -0.0768 -0.1520 278 VAL B CG1 6340 C CG2 . VAL B 278 ? 0.6434 0.9044 0.5044 -0.0632 -0.0783 -0.1511 278 VAL B CG2 6341 N N . GLU B 279 ? 1.0518 1.2256 0.9290 -0.0931 -0.0925 -0.1945 279 GLU B N 6342 C CA . GLU B 279 ? 1.0523 1.1919 0.9352 -0.0986 -0.0937 -0.2034 279 GLU B CA 6343 C C . GLU B 279 ? 0.9989 1.1181 0.8921 -0.0940 -0.0883 -0.1899 279 GLU B C 6344 O O . GLU B 279 ? 1.0577 1.1537 0.9519 -0.0896 -0.0856 -0.1948 279 GLU B O 6345 C CB . GLU B 279 ? 1.0491 1.1835 0.9374 -0.1133 -0.1013 -0.2097 279 GLU B CB 6346 C CG . GLU B 279 ? 1.0461 1.1462 0.9371 -0.1199 -0.1039 -0.2229 279 GLU B CG 6347 C CD . GLU B 279 ? 1.1025 1.1961 1.0020 -0.1358 -0.1102 -0.2258 279 GLU B CD 6348 O OE1 . GLU B 279 ? 0.9934 1.1044 0.9000 -0.1409 -0.1110 -0.2136 279 GLU B OE1 6349 O OE2 . GLU B 279 ? 1.1582 1.2289 1.0581 -0.1431 -0.1142 -0.2402 279 GLU B OE2 6350 N N . TYR B 280 ? 0.9334 1.0615 0.8345 -0.0947 -0.0870 -0.1736 280 TYR B N 6351 C CA . TYR B 280 ? 0.8303 0.9425 0.7401 -0.0896 -0.0823 -0.1609 280 TYR B CA 6352 C C . TYR B 280 ? 0.7675 0.8992 0.6793 -0.0803 -0.0773 -0.1462 280 TYR B C 6353 O O . TYR B 280 ? 0.8117 0.9658 0.7240 -0.0812 -0.0783 -0.1380 280 TYR B O 6354 C CB . TYR B 280 ? 0.7611 0.8607 0.6796 -0.0982 -0.0848 -0.1547 280 TYR B CB 6355 C CG . TYR B 280 ? 0.9496 1.0236 0.8683 -0.1071 -0.0885 -0.1660 280 TYR B CG 6356 C CD1 . TYR B 280 ? 1.0579 1.1367 0.9732 -0.1168 -0.0940 -0.1788 280 TYR B CD1 6357 C CD2 . TYR B 280 ? 0.9742 1.0189 0.8970 -0.1059 -0.0870 -0.1637 280 TYR B CD2 6358 C CE1 . TYR B 280 ? 1.1016 1.1549 1.0186 -0.1257 -0.0975 -0.1888 280 TYR B CE1 6359 C CE2 . TYR B 280 ? 1.0190 1.0385 0.9422 -0.1139 -0.0903 -0.1726 280 TYR B CE2 6360 C CZ . TYR B 280 ? 1.1420 1.1651 1.0628 -0.1242 -0.0953 -0.1850 280 TYR B CZ 6361 O OH . TYR B 280 ? 1.2044 1.2010 1.1269 -0.1331 -0.0988 -0.1938 280 TYR B OH 6362 N N . LEU B 281 ? 0.7174 0.8403 0.6314 -0.0714 -0.0720 -0.1429 281 LEU B N 6363 C CA . LEU B 281 ? 0.7449 0.8817 0.6635 -0.0632 -0.0667 -0.1284 281 LEU B CA 6364 C C . LEU B 281 ? 0.7658 0.8843 0.6960 -0.0610 -0.0650 -0.1187 281 LEU B C 6365 O O . LEU B 281 ? 0.9304 1.0270 0.8634 -0.0597 -0.0646 -0.1238 281 LEU B O 6366 C CB . LEU B 281 ? 0.7657 0.9105 0.6792 -0.0548 -0.0614 -0.1319 281 LEU B CB 6367 C CG . LEU B 281 ? 0.7147 0.8742 0.6336 -0.0472 -0.0554 -0.1164 281 LEU B CG 6368 C CD1 . LEU B 281 ? 0.7473 0.9274 0.6652 -0.0489 -0.0573 -0.1054 281 LEU B CD1 6369 C CD2 . LEU B 281 ? 0.7422 0.9148 0.6542 -0.0403 -0.0498 -0.1204 281 LEU B CD2 6370 N N . ASN B 282 ? 0.7413 0.8687 0.6778 -0.0601 -0.0644 -0.1054 282 ASN B N 6371 C CA . ASN B 282 ? 0.7110 0.8226 0.6577 -0.0579 -0.0634 -0.0970 282 ASN B CA 6372 C C . ASN B 282 ? 0.7661 0.8882 0.7203 -0.0506 -0.0592 -0.0840 282 ASN B C 6373 O O . ASN B 282 ? 0.8335 0.9760 0.7867 -0.0492 -0.0584 -0.0765 282 ASN B O 6374 C CB . ASN B 282 ? 0.5473 0.6546 0.4962 -0.0645 -0.0670 -0.0941 282 ASN B CB 6375 C CG . ASN B 282 ? 0.7063 0.8058 0.6493 -0.0737 -0.0711 -0.1053 282 ASN B CG 6376 O OD1 . ASN B 282 ? 0.9281 1.0052 0.8704 -0.0755 -0.0721 -0.1120 282 ASN B OD1 6377 N ND2 . ASN B 282 ? 0.7258 0.8436 0.6655 -0.0796 -0.0739 -0.1073 282 ASN B ND2 6378 N N . ILE B 283 ? 0.7350 0.8428 0.6975 -0.0459 -0.0570 -0.0811 283 ILE B N 6379 C CA . ILE B 283 ? 0.7035 0.8178 0.6758 -0.0399 -0.0534 -0.0692 283 ILE B CA 6380 C C . ILE B 283 ? 0.6867 0.7836 0.6686 -0.0388 -0.0552 -0.0650 283 ILE B C 6381 O O . ILE B 283 ? 0.6689 0.7475 0.6519 -0.0392 -0.0571 -0.0712 283 ILE B O 6382 C CB . ILE B 283 ? 0.5352 0.6543 0.5102 -0.0346 -0.0482 -0.0697 283 ILE B CB 6383 C CG1 . ILE B 283 ? 0.4721 0.6110 0.4354 -0.0347 -0.0461 -0.0735 283 ILE B CG1 6384 C CG2 . ILE B 283 ? 0.4606 0.5837 0.4485 -0.0298 -0.0444 -0.0569 283 ILE B CG2 6385 C CD1 . ILE B 283 ? 0.5777 0.7204 0.5404 -0.0300 -0.0408 -0.0782 283 ILE B CD1 6386 N N . TYR B 284 ? 0.7512 0.8542 0.7394 -0.0369 -0.0549 -0.0548 284 TYR B N 6387 C CA . TYR B 284 ? 0.6963 0.7850 0.6922 -0.0354 -0.0570 -0.0516 284 TYR B CA 6388 C C . TYR B 284 ? 0.6171 0.7075 0.6256 -0.0298 -0.0544 -0.0422 284 TYR B C 6389 O O . TYR B 284 ? 0.6696 0.7748 0.6805 -0.0278 -0.0520 -0.0336 284 TYR B O 6390 C CB . TYR B 284 ? 0.9258 1.0187 0.9183 -0.0383 -0.0594 -0.0492 284 TYR B CB 6391 C CG . TYR B 284 ? 1.2406 1.3257 1.2244 -0.0449 -0.0624 -0.0574 284 TYR B CG 6392 C CD1 . TYR B 284 ? 1.4174 1.4829 1.4009 -0.0456 -0.0646 -0.0606 284 TYR B CD1 6393 C CD2 . TYR B 284 ? 1.2702 1.3677 1.2462 -0.0507 -0.0634 -0.0614 284 TYR B CD2 6394 C CE1 . TYR B 284 ? 1.4660 1.5232 1.4419 -0.0521 -0.0667 -0.0663 284 TYR B CE1 6395 C CE2 . TYR B 284 ? 1.3435 1.4325 1.3135 -0.0580 -0.0661 -0.0684 284 TYR B CE2 6396 C CZ . TYR B 284 ? 1.3765 1.4448 1.3466 -0.0588 -0.0673 -0.0701 284 TYR B CZ 6397 O OH . TYR B 284 ? 1.2794 1.3380 1.2440 -0.0663 -0.0693 -0.0752 284 TYR B OH 6398 N N . ASN B 285 ? 0.7049 0.7803 0.7222 -0.0274 -0.0554 -0.0436 285 ASN B N 6399 C CA . ASN B 285 ? 0.6393 0.7142 0.6710 -0.0233 -0.0537 -0.0356 285 ASN B CA 6400 C C . ASN B 285 ? 0.5503 0.6400 0.5866 -0.0218 -0.0480 -0.0295 285 ASN B C 6401 O O . ASN B 285 ? 0.6351 0.7355 0.6758 -0.0199 -0.0452 -0.0191 285 ASN B O 6402 C CB . ASN B 285 ? 0.6357 0.7112 0.6705 -0.0215 -0.0553 -0.0291 285 ASN B CB 6403 C CG . ASN B 285 ? 0.7344 0.8080 0.7848 -0.0175 -0.0539 -0.0207 285 ASN B CG 6404 O OD1 . ASN B 285 ? 0.8052 0.8722 0.8666 -0.0167 -0.0532 -0.0212 285 ASN B OD1 6405 N ND2 . ASN B 285 ? 0.8007 0.8800 0.8535 -0.0150 -0.0536 -0.0130 285 ASN B ND2 6406 N N . LEU B 286 ? 0.4787 0.5688 0.5134 -0.0221 -0.0460 -0.0357 286 LEU B N 6407 C CA . LEU B 286 ? 0.6228 0.7265 0.6624 -0.0203 -0.0396 -0.0311 286 LEU B CA 6408 C C . LEU B 286 ? 0.6642 0.7628 0.7232 -0.0182 -0.0377 -0.0259 286 LEU B C 6409 O O . LEU B 286 ? 0.5894 0.6731 0.6561 -0.0179 -0.0418 -0.0317 286 LEU B O 6410 C CB . LEU B 286 ? 0.5972 0.7038 0.6271 -0.0207 -0.0382 -0.0417 286 LEU B CB 6411 C CG . LEU B 286 ? 0.5150 0.6350 0.5493 -0.0180 -0.0310 -0.0402 286 LEU B CG 6412 C CD1 . LEU B 286 ? 0.5374 0.6785 0.5647 -0.0174 -0.0260 -0.0308 286 LEU B CD1 6413 C CD2 . LEU B 286 ? 0.4583 0.5752 0.4844 -0.0174 -0.0312 -0.0538 286 LEU B CD2 6414 N N . THR B 287 ? 0.7446 0.8563 0.8119 -0.0170 -0.0315 -0.0146 287 THR B N 6415 C CA . THR B 287 ? 0.7564 0.8658 0.8446 -0.0164 -0.0287 -0.0086 287 THR B CA 6416 C C . THR B 287 ? 0.7659 0.8930 0.8581 -0.0155 -0.0199 -0.0036 287 THR B C 6417 O O . THR B 287 ? 0.9039 1.0452 0.9947 -0.0150 -0.0142 0.0083 287 THR B O 6418 C CB . THR B 287 ? 0.5351 0.6404 0.6351 -0.0161 -0.0293 0.0033 287 THR B CB 6419 O OG1 . THR B 287 ? 0.6451 0.7371 0.7398 -0.0159 -0.0365 -0.0013 287 THR B OG1 6420 C CG2 . THR B 287 ? 0.4834 0.5828 0.6070 -0.0169 -0.0281 0.0073 287 THR B CG2 6421 N N . ILE B 288 ? 0.7062 0.8333 0.8031 -0.0148 -0.0185 -0.0122 288 ILE B N 6422 C CA . ILE B 288 ? 0.5959 0.7410 0.6982 -0.0133 -0.0094 -0.0087 288 ILE B CA 6423 C C . ILE B 288 ? 0.5683 0.7186 0.6931 -0.0148 -0.0041 0.0056 288 ILE B C 6424 O O . ILE B 288 ? 0.4834 0.6204 0.6262 -0.0165 -0.0086 0.0058 288 ILE B O 6425 C CB . ILE B 288 ? 0.6514 0.7937 0.7572 -0.0112 -0.0098 -0.0219 288 ILE B CB 6426 C CG1 . ILE B 288 ? 0.7460 0.8753 0.8339 -0.0106 -0.0171 -0.0363 288 ILE B CG1 6427 C CG2 . ILE B 288 ? 0.6498 0.8133 0.7564 -0.0087 0.0003 -0.0202 288 ILE B CG2 6428 C CD1 . ILE B 288 ? 0.8038 0.9424 0.8689 -0.0107 -0.0155 -0.0390 288 ILE B CD1 6429 N N . THR B 289 ? 0.7134 0.8830 0.8378 -0.0143 0.0054 0.0176 289 THR B N 6430 C CA . THR B 289 ? 0.6613 0.8324 0.8034 -0.0166 0.0093 0.0346 289 THR B CA 6431 C C . THR B 289 ? 0.6840 0.8657 0.8498 -0.0186 0.0180 0.0447 289 THR B C 6432 O O . THR B 289 ? 1.0438 1.2137 1.2327 -0.0219 0.0150 0.0469 289 THR B O 6433 C CB . THR B 289 ? 0.7365 0.9127 0.8655 -0.0157 0.0103 0.0470 289 THR B CB 6434 O OG1 . THR B 289 ? 0.7931 0.9498 0.9253 -0.0165 0.0014 0.0459 289 THR B OG1 6435 C CG2 . THR B 289 ? 0.7222 0.9114 0.8626 -0.0165 0.0198 0.0669 289 THR B CG2 6436 N N . GLU B 290 ? 0.4299 0.6340 0.5917 -0.0172 0.0287 0.0511 290 GLU B N 6437 C CA . GLU B 290 ? 0.4972 0.7116 0.6843 -0.0204 0.0378 0.0649 290 GLU B CA 6438 C C . GLU B 290 ? 0.5905 0.8162 0.7901 -0.0197 0.0426 0.0563 290 GLU B C 6439 O O . GLU B 290 ? 0.5697 0.7970 0.7973 -0.0235 0.0455 0.0613 290 GLU B O 6440 C CB . GLU B 290 ? 0.5646 0.7983 0.7447 -0.0198 0.0487 0.0845 290 GLU B CB 6441 C CG . GLU B 290 ? 0.7739 0.9989 0.9476 -0.0202 0.0456 0.0981 290 GLU B CG 6442 C CD . GLU B 290 ? 1.0002 1.2473 1.1573 -0.0173 0.0553 0.1146 290 GLU B CD 6443 O OE1 . GLU B 290 ? 1.1415 1.4109 1.2924 -0.0154 0.0651 0.1154 290 GLU B OE1 6444 O OE2 . GLU B 290 ? 0.9975 1.2406 1.1472 -0.0161 0.0531 0.1266 290 GLU B OE2 6445 N N . ARG B 291 ? 0.6093 0.8437 0.7892 -0.0146 0.0436 0.0431 291 ARG B N 6446 C CA . ARG B 291 ? 0.5480 0.7953 0.7367 -0.0119 0.0489 0.0338 291 ARG B CA 6447 C C . ARG B 291 ? 0.7075 0.9526 0.8710 -0.0062 0.0447 0.0155 291 ARG B C 6448 O O . ARG B 291 ? 0.8299 1.0710 0.9689 -0.0051 0.0411 0.0134 291 ARG B O 6449 C CB . ARG B 291 ? 0.4026 0.6781 0.5977 -0.0115 0.0643 0.0476 291 ARG B CB 6450 C CG . ARG B 291 ? 0.7101 0.9981 0.8833 -0.0106 0.0706 0.0616 291 ARG B CG 6451 C CD . ARG B 291 ? 0.6561 0.9686 0.8406 -0.0120 0.0857 0.0812 291 ARG B CD 6452 N NE . ARG B 291 ? 0.9707 1.3051 1.1596 -0.0082 0.0954 0.0741 291 ARG B NE 6453 C CZ . ARG B 291 ? 1.2606 1.5998 1.4797 -0.0106 0.0990 0.0731 291 ARG B CZ 6454 N NH1 . ARG B 291 ? 1.3973 1.7200 1.6444 -0.0176 0.0930 0.0784 291 ARG B NH1 6455 N NH2 . ARG B 291 ? 1.2468 1.6082 1.4685 -0.0057 0.1084 0.0662 291 ARG B NH2 6456 N N . ILE B 292 ? 0.7166 0.9637 0.8877 -0.0026 0.0446 0.0022 292 ILE B N 6457 C CA . ILE B 292 ? 0.5794 0.8245 0.7288 0.0033 0.0419 -0.0153 292 ILE B CA 6458 C C . ILE B 292 ? 0.6479 0.9162 0.8015 0.0090 0.0529 -0.0200 292 ILE B C 6459 O O . ILE B 292 ? 0.7222 0.9930 0.8978 0.0108 0.0537 -0.0246 292 ILE B O 6460 C CB . ILE B 292 ? 0.5144 0.7341 0.6660 0.0038 0.0290 -0.0298 292 ILE B CB 6461 C CG1 . ILE B 292 ? 0.5796 0.7782 0.7273 -0.0014 0.0190 -0.0253 292 ILE B CG1 6462 C CG2 . ILE B 292 ? 0.4850 0.7004 0.6153 0.0094 0.0263 -0.0470 292 ILE B CG2 6463 C CD1 . ILE B 292 ? 0.2965 0.4702 0.4443 -0.0009 0.0065 -0.0381 292 ILE B CD1 6464 N N . ASP B 293 ? 0.6493 0.9364 0.7819 0.0125 0.0613 -0.0188 293 ASP B N 6465 C CA . ASP B 293 ? 0.5941 0.9056 0.7273 0.0190 0.0730 -0.0236 293 ASP B CA 6466 C C . ASP B 293 ? 0.6663 0.9758 0.7723 0.0258 0.0705 -0.0428 293 ASP B C 6467 O O . ASP B 293 ? 0.8342 1.1243 0.9221 0.0241 0.0601 -0.0505 293 ASP B O 6468 C CB . ASP B 293 ? 0.5631 0.9025 0.6960 0.0180 0.0871 -0.0052 293 ASP B CB 6469 C CG . ASP B 293 ? 0.7738 1.1133 0.9349 0.0104 0.0898 0.0146 293 ASP B CG 6470 O OD1 . ASP B 293 ? 0.8875 1.2254 1.0428 0.0058 0.0900 0.0303 293 ASP B OD1 6471 O OD2 . ASP B 293 ? 0.8035 1.1443 0.9937 0.0090 0.0910 0.0143 293 ASP B OD2 6472 N N . ARG B 294 ? 0.5575 0.8868 0.6621 0.0333 0.0800 -0.0510 294 ARG B N 6473 C CA . ARG B 294 ? 0.8069 1.1348 0.8863 0.0403 0.0783 -0.0705 294 ARG B CA 6474 C C . ARG B 294 ? 0.9779 1.3184 1.0282 0.0396 0.0813 -0.0662 294 ARG B C 6475 O O . ARG B 294 ? 1.0352 1.4028 1.0823 0.0411 0.0934 -0.0540 294 ARG B O 6476 C CB . ARG B 294 ? 0.8499 1.1959 0.9366 0.0499 0.0878 -0.0817 294 ARG B CB 6477 C CG . ARG B 294 ? 1.0826 1.4076 1.1789 0.0549 0.0792 -0.1000 294 ARG B CG 6478 C CD . ARG B 294 ? 1.2894 1.6346 1.3970 0.0655 0.0893 -0.1098 294 ARG B CD 6479 N NE . ARG B 294 ? 1.3977 1.7566 1.5398 0.0643 0.0951 -0.0985 294 ARG B NE 6480 C CZ . ARG B 294 ? 1.3086 1.6525 1.4746 0.0648 0.0871 -0.1027 294 ARG B CZ 6481 N NH1 . ARG B 294 ? 1.2194 1.5332 1.3771 0.0667 0.0735 -0.1166 294 ARG B NH1 6482 N NH2 . ARG B 294 ? 1.1783 1.5379 1.3768 0.0631 0.0923 -0.0926 294 ARG B NH2 6483 N N . GLU B 295 ? 0.9528 1.2747 0.9824 0.0373 0.0703 -0.0754 295 GLU B N 6484 C CA . GLU B 295 ? 0.8455 1.1790 0.8479 0.0364 0.0708 -0.0723 295 GLU B CA 6485 C C . GLU B 295 ? 0.8654 1.2023 0.8427 0.0426 0.0697 -0.0938 295 GLU B C 6486 O O . GLU B 295 ? 0.9195 1.2366 0.8971 0.0449 0.0627 -0.1122 295 GLU B O 6487 C CB . GLU B 295 ? 0.8240 1.1383 0.8222 0.0283 0.0594 -0.0649 295 GLU B CB 6488 C CG . GLU B 295 ? 0.9433 1.2532 0.9647 0.0225 0.0599 -0.0443 295 GLU B CG 6489 C CD . GLU B 295 ? 1.0401 1.3757 1.0620 0.0223 0.0713 -0.0235 295 GLU B CD 6490 O OE1 . GLU B 295 ? 1.2136 1.5651 1.2116 0.0242 0.0737 -0.0212 295 GLU B OE1 6491 O OE2 . GLU B 295 ? 0.9419 1.2817 0.9882 0.0199 0.0775 -0.0091 295 GLU B OE2 6492 N N . GLU B 296 ? 0.8506 1.2121 0.8058 0.0456 0.0763 -0.0915 296 GLU B N 6493 C CA . GLU B 296 ? 0.9204 1.2870 0.8499 0.0514 0.0749 -0.1127 296 GLU B CA 6494 C C . GLU B 296 ? 0.9060 1.2497 0.8207 0.0456 0.0601 -0.1236 296 GLU B C 6495 O O . GLU B 296 ? 0.9454 1.2852 0.8576 0.0386 0.0541 -0.1109 296 GLU B O 6496 C CB . GLU B 296 ? 1.1307 1.5322 1.0391 0.0563 0.0856 -0.1065 296 GLU B CB 6497 C CG . GLU B 296 ? 1.3969 1.8243 1.3184 0.0624 0.1021 -0.0964 296 GLU B CG 6498 C CD . GLU B 296 ? 1.6085 2.0280 1.5481 0.0684 0.1048 -0.1118 296 GLU B CD 6499 O OE1 . GLU B 296 ? 1.6911 2.1003 1.6180 0.0738 0.0998 -0.1357 296 GLU B OE1 6500 O OE2 . GLU B 296 ? 1.6281 2.0516 1.5956 0.0678 0.1116 -0.1001 296 GLU B OE2 6501 N N . PHE B 297 ? 0.8651 1.1937 0.7713 0.0486 0.0542 -0.1470 297 PHE B N 6502 C CA . PHE B 297 ? 0.8921 1.1998 0.7846 0.0427 0.0408 -0.1591 297 PHE B CA 6503 C C . PHE B 297 ? 1.0032 1.2997 0.8844 0.0478 0.0373 -0.1860 297 PHE B C 6504 O O . PHE B 297 ? 1.0635 1.3547 0.9558 0.0550 0.0418 -0.1953 297 PHE B O 6505 C CB . PHE B 297 ? 0.8018 1.0810 0.7121 0.0344 0.0312 -0.1516 297 PHE B CB 6506 C CG . PHE B 297 ? 0.8705 1.1290 0.8014 0.0373 0.0304 -0.1578 297 PHE B CG 6507 C CD1 . PHE B 297 ? 0.9088 1.1400 0.8377 0.0369 0.0214 -0.1756 297 PHE B CD1 6508 C CD2 . PHE B 297 ? 0.8521 1.1188 0.8053 0.0403 0.0385 -0.1453 297 PHE B CD2 6509 C CE1 . PHE B 297 ? 0.9538 1.1663 0.9011 0.0407 0.0202 -0.1804 297 PHE B CE1 6510 C CE2 . PHE B 297 ? 0.8146 1.0645 0.7872 0.0436 0.0369 -0.1511 297 PHE B CE2 6511 C CZ . PHE B 297 ? 0.9148 1.1377 0.8838 0.0443 0.0276 -0.1684 297 PHE B CZ 6512 N N . THR B 298 ? 1.0267 1.3202 0.8866 0.0444 0.0292 -0.1988 298 THR B N 6513 C CA . THR B 298 ? 1.0773 1.3527 0.9275 0.0467 0.0229 -0.2249 298 THR B CA 6514 C C . THR B 298 ? 1.1183 1.3727 0.9621 0.0357 0.0090 -0.2297 298 THR B C 6515 O O . THR B 298 ? 1.2086 1.4764 1.0421 0.0296 0.0055 -0.2206 298 THR B O 6516 C CB . THR B 298 ? 1.0588 1.3578 0.8857 0.0553 0.0286 -0.2417 298 THR B CB 6517 O OG1 . THR B 298 ? 0.9203 1.2527 0.7328 0.0555 0.0343 -0.2275 298 THR B OG1 6518 C CG2 . THR B 298 ? 1.1035 1.4082 0.9386 0.0676 0.0393 -0.2506 298 THR B CG2 6519 N N . TYR B 299 ? 1.0244 1.2468 0.8753 0.0332 0.0012 -0.2432 299 TYR B N 6520 C CA . TYR B 299 ? 0.8897 1.0915 0.7355 0.0224 -0.0114 -0.2493 299 TYR B CA 6521 C C . TYR B 299 ? 0.9445 1.1412 0.7724 0.0227 -0.0170 -0.2748 299 TYR B C 6522 O O . TYR B 299 ? 0.7962 0.9730 0.6264 0.0277 -0.0178 -0.2921 299 TYR B O 6523 C CB . TYR B 299 ? 0.8216 0.9899 0.6862 0.0179 -0.0171 -0.2459 299 TYR B CB 6524 C CG . TYR B 299 ? 0.8923 1.0641 0.7737 0.0161 -0.0139 -0.2224 299 TYR B CG 6525 C CD1 . TYR B 299 ? 0.7843 0.9495 0.6838 0.0225 -0.0086 -0.2167 299 TYR B CD1 6526 C CD2 . TYR B 299 ? 0.9442 1.1268 0.8240 0.0085 -0.0163 -0.2065 299 TYR B CD2 6527 C CE1 . TYR B 299 ? 0.7748 0.9429 0.6902 0.0204 -0.0064 -0.1967 299 TYR B CE1 6528 C CE2 . TYR B 299 ? 1.0503 1.2346 0.9456 0.0072 -0.0137 -0.1863 299 TYR B CE2 6529 C CZ . TYR B 299 ? 0.9902 1.1667 0.9032 0.0128 -0.0089 -0.1818 299 TYR B CZ 6530 O OH . TYR B 299 ? 1.0536 1.2311 0.9827 0.0109 -0.0070 -0.1630 299 TYR B OH 6531 N N . SER B 300 ? 1.0295 1.2439 0.8399 0.0175 -0.0213 -0.2774 300 SER B N 6532 C CA . SER B 300 ? 1.0539 1.2656 0.8467 0.0164 -0.0280 -0.3022 300 SER B CA 6533 C C . SER B 300 ? 1.0708 1.2602 0.8666 0.0025 -0.0410 -0.3060 300 SER B C 6534 O O . SER B 300 ? 1.0382 1.2186 0.8474 -0.0050 -0.0436 -0.2886 300 SER B O 6535 C CB . SER B 300 ? 1.1330 1.3821 0.9034 0.0199 -0.0252 -0.3040 300 SER B CB 6536 O OG . SER B 300 ? 1.2580 1.5331 1.0283 0.0301 -0.0120 -0.2901 300 SER B OG 6537 N N . GLU B 301 ? 1.1022 1.2833 0.8858 -0.0010 -0.0488 -0.3292 301 GLU B N 6538 C CA . GLU B 301 ? 1.0898 1.2542 0.8753 -0.0154 -0.0611 -0.3343 301 GLU B CA 6539 C C . GLU B 301 ? 0.9641 1.1437 0.7552 -0.0235 -0.0630 -0.3108 301 GLU B C 6540 O O . GLU B 301 ? 0.9870 1.1992 0.7686 -0.0201 -0.0593 -0.3000 301 GLU B O 6541 C CB . GLU B 301 ? 1.2969 1.4711 1.0634 -0.0181 -0.0685 -0.3582 301 GLU B CB 6542 C CG . GLU B 301 ? 1.5300 1.7470 1.2761 -0.0117 -0.0647 -0.3563 301 GLU B CG 6543 C CD . GLU B 301 ? 1.6323 1.8620 1.3642 0.0033 -0.0559 -0.3711 301 GLU B CD 6544 O OE1 . GLU B 301 ? 1.6960 1.9091 1.4381 0.0117 -0.0485 -0.3728 301 GLU B OE1 6545 O OE2 . GLU B 301 ? 1.5623 1.8204 1.2725 0.0072 -0.0565 -0.3812 301 GLU B OE2 6546 N N . THR B 302 ? 0.8376 0.9937 0.6440 -0.0335 -0.0684 -0.3024 302 THR B N 6547 C CA . THR B 302 ? 0.8999 1.0678 0.7136 -0.0405 -0.0700 -0.2807 302 THR B CA 6548 C C . THR B 302 ? 0.9747 1.1245 0.7959 -0.0550 -0.0801 -0.2830 302 THR B C 6549 O O . THR B 302 ? 1.1050 1.2255 0.9308 -0.0597 -0.0845 -0.2965 302 THR B O 6550 C CB . THR B 302 ? 0.8684 1.0303 0.6974 -0.0354 -0.0622 -0.2594 302 THR B CB 6551 O OG1 . THR B 302 ? 0.8597 1.0284 0.6966 -0.0425 -0.0646 -0.2404 302 THR B OG1 6552 C CG2 . THR B 302 ? 0.8552 0.9809 0.6971 -0.0350 -0.0625 -0.2644 302 THR B CG2 6553 N N . ALA B 303 ? 0.8793 1.0470 0.7026 -0.0619 -0.0835 -0.2694 303 ALA B N 6554 C CA . ALA B 303 ? 0.8825 1.0366 0.7154 -0.0758 -0.0917 -0.2686 303 ALA B CA 6555 C C . ALA B 303 ? 0.9200 1.0497 0.7698 -0.0776 -0.0889 -0.2531 303 ALA B C 6556 O O . ALA B 303 ? 0.9305 1.0397 0.7893 -0.0882 -0.0941 -0.2542 303 ALA B O 6557 C CB . ALA B 303 ? 0.8178 1.0027 0.6472 -0.0815 -0.0966 -0.2609 303 ALA B CB 6558 N N . LEU B 304 ? 0.7706 0.9033 0.6247 -0.0676 -0.0806 -0.2389 304 LEU B N 6559 C CA . LEU B 304 ? 0.7395 0.8523 0.6084 -0.0675 -0.0779 -0.2244 304 LEU B CA 6560 C C . LEU B 304 ? 0.8407 0.9171 0.7164 -0.0720 -0.0811 -0.2331 304 LEU B C 6561 O O . LEU B 304 ? 0.9041 0.9648 0.7771 -0.0667 -0.0800 -0.2465 304 LEU B O 6562 C CB . LEU B 304 ? 0.7708 0.8896 0.6433 -0.0553 -0.0689 -0.2135 304 LEU B CB 6563 C CG . LEU B 304 ? 0.8605 0.9995 0.7382 -0.0530 -0.0650 -0.1924 304 LEU B CG 6564 C CD1 . LEU B 304 ? 0.9776 1.1095 0.8654 -0.0442 -0.0577 -0.1823 304 LEU B CD1 6565 C CD2 . LEU B 304 ? 0.8051 0.9394 0.6905 -0.0623 -0.0701 -0.1827 304 LEU B CD2 6566 N N . LYS B 305 ? 0.9095 0.9729 0.7942 -0.0812 -0.0846 -0.2245 305 LYS B N 6567 C CA . LYS B 305 ? 0.9999 1.0284 0.8919 -0.0849 -0.0868 -0.2275 305 LYS B CA 6568 C C . LYS B 305 ? 0.9957 1.0135 0.8970 -0.0782 -0.0821 -0.2118 305 LYS B C 6569 O O . LYS B 305 ? 0.9961 0.9876 0.9016 -0.0746 -0.0818 -0.2144 305 LYS B O 6570 C CB . LYS B 305 ? 1.0989 1.1192 0.9947 -0.0998 -0.0933 -0.2280 305 LYS B CB 6571 C CG . LYS B 305 ? 1.2403 1.2242 1.1431 -0.1049 -0.0953 -0.2285 305 LYS B CG 6572 C CD . LYS B 305 ? 1.3417 1.3200 1.2480 -0.1210 -0.1014 -0.2313 305 LYS B CD 6573 C CE . LYS B 305 ? 1.2224 1.1664 1.1362 -0.1270 -0.1024 -0.2266 305 LYS B CE 6574 N NZ . LYS B 305 ? 1.1152 1.0581 1.0345 -0.1437 -0.1071 -0.2266 305 LYS B NZ 6575 N N . SER B 306 ? 0.9037 0.9418 0.8085 -0.0759 -0.0789 -0.1960 306 SER B N 6576 C CA . SER B 306 ? 0.9281 0.9563 0.8425 -0.0718 -0.0760 -0.1813 306 SER B CA 6577 C C . SER B 306 ? 0.8220 0.8721 0.7400 -0.0645 -0.0708 -0.1675 306 SER B C 6578 O O . SER B 306 ? 0.9257 0.9963 0.8430 -0.0675 -0.0710 -0.1593 306 SER B O 6579 C CB . SER B 306 ? 0.9435 0.9602 0.8629 -0.0815 -0.0797 -0.1734 306 SER B CB 6580 O OG . SER B 306 ? 0.8560 0.8793 0.7820 -0.0781 -0.0769 -0.1574 306 SER B OG 6581 N N . LEU B 307 ? 0.7289 0.7738 0.6524 -0.0551 -0.0665 -0.1644 307 LEU B N 6582 C CA . LEU B 307 ? 0.6431 0.7012 0.5743 -0.0495 -0.0621 -0.1495 307 LEU B CA 6583 C C . LEU B 307 ? 0.7635 0.8031 0.7039 -0.0503 -0.0639 -0.1404 307 LEU B C 6584 O O . LEU B 307 ? 0.8532 0.8693 0.7956 -0.0498 -0.0662 -0.1451 307 LEU B O 6585 C CB . LEU B 307 ? 0.7033 0.7697 0.6372 -0.0395 -0.0560 -0.1506 307 LEU B CB 6586 C CG . LEU B 307 ? 0.7659 0.8483 0.7085 -0.0349 -0.0511 -0.1352 307 LEU B CG 6587 C CD1 . LEU B 307 ? 0.7404 0.8448 0.6777 -0.0387 -0.0512 -0.1271 307 LEU B CD1 6588 C CD2 . LEU B 307 ? 0.7798 0.8732 0.7257 -0.0262 -0.0442 -0.1365 307 LEU B CD2 6589 N N . MET B 308 ? 0.7538 0.8039 0.6991 -0.0510 -0.0631 -0.1274 308 MET B N 6590 C CA . MET B 308 ? 0.7113 0.7464 0.6638 -0.0512 -0.0649 -0.1193 308 MET B CA 6591 C C . MET B 308 ? 0.8284 0.8760 0.7896 -0.0461 -0.0617 -0.1070 308 MET B C 6592 O O . MET B 308 ? 0.9065 0.9714 0.8674 -0.0477 -0.0608 -0.0997 308 MET B O 6593 C CB . MET B 308 ? 0.7389 0.7695 0.6879 -0.0602 -0.0688 -0.1177 308 MET B CB 6594 C CG . MET B 308 ? 0.8524 0.8627 0.8050 -0.0608 -0.0709 -0.1127 308 MET B CG 6595 S SD . MET B 308 ? 1.9943 2.0143 1.9503 -0.0635 -0.0710 -0.1003 308 MET B SD 6596 C CE . MET B 308 ? 0.3212 0.3535 0.2860 -0.0538 -0.0675 -0.0922 308 MET B CE 6597 N N . ILE B 309 ? 0.7270 0.7657 0.6970 -0.0398 -0.0605 -0.1048 309 ILE B N 6598 C CA . ILE B 309 ? 0.6465 0.6941 0.6271 -0.0354 -0.0579 -0.0940 309 ILE B CA 6599 C C . ILE B 309 ? 0.7941 0.8250 0.7809 -0.0346 -0.0615 -0.0899 309 ILE B C 6600 O O . ILE B 309 ? 0.8574 0.8705 0.8443 -0.0332 -0.0644 -0.0952 309 ILE B O 6601 C CB . ILE B 309 ? 0.5705 0.6262 0.5587 -0.0289 -0.0530 -0.0944 309 ILE B CB 6602 C CG1 . ILE B 309 ? 0.8133 0.8840 0.7923 -0.0288 -0.0494 -0.1008 309 ILE B CG1 6603 C CG2 . ILE B 309 ? 0.5394 0.6065 0.5391 -0.0261 -0.0498 -0.0824 309 ILE B CG2 6604 C CD1 . ILE B 309 ? 0.8734 0.9599 0.8590 -0.0228 -0.0426 -0.0978 309 ILE B CD1 6605 N N . GLU B 310 ? 0.7591 0.7958 0.7504 -0.0348 -0.0616 -0.0808 310 GLU B N 6606 C CA . GLU B 310 ? 0.7303 0.7530 0.7257 -0.0336 -0.0651 -0.0777 310 GLU B CA 6607 C C . GLU B 310 ? 0.7276 0.7572 0.7343 -0.0299 -0.0639 -0.0692 310 GLU B C 6608 O O . GLU B 310 ? 0.7558 0.7993 0.7633 -0.0306 -0.0616 -0.0628 310 GLU B O 6609 C CB . GLU B 310 ? 0.7427 0.7599 0.7289 -0.0391 -0.0679 -0.0775 310 GLU B CB 6610 C CG . GLU B 310 ? 0.9126 0.9121 0.8987 -0.0376 -0.0717 -0.0769 310 GLU B CG 6611 C CD . GLU B 310 ? 1.0262 1.0229 1.0039 -0.0428 -0.0730 -0.0749 310 GLU B CD 6612 O OE1 . GLU B 310 ? 1.0718 1.0714 1.0426 -0.0494 -0.0725 -0.0776 310 GLU B OE1 6613 O OE2 . GLU B 310 ? 0.9001 0.8922 0.8786 -0.0405 -0.0745 -0.0710 310 GLU B OE2 6614 N N . HIS B 311 ? 0.7448 0.7640 0.7606 -0.0258 -0.0661 -0.0695 311 HIS B N 6615 C CA . HIS B 311 ? 0.7233 0.7456 0.7520 -0.0226 -0.0658 -0.0629 311 HIS B CA 6616 C C . HIS B 311 ? 0.7748 0.8114 0.8140 -0.0210 -0.0605 -0.0584 311 HIS B C 6617 O O . HIS B 311 ? 0.8128 0.8633 0.8506 -0.0220 -0.0567 -0.0521 311 HIS B O 6618 C CB . HIS B 311 ? 0.6382 0.6642 0.6641 -0.0237 -0.0663 -0.0571 311 HIS B CB 6619 C CG . HIS B 311 ? 0.7761 0.7995 0.8147 -0.0201 -0.0675 -0.0524 311 HIS B CG 6620 N ND1 . HIS B 311 ? 0.8044 0.8150 0.8502 -0.0173 -0.0719 -0.0561 311 HIS B ND1 6621 C CD2 . HIS B 311 ? 0.9251 0.9564 0.9710 -0.0186 -0.0655 -0.0449 311 HIS B CD2 6622 C CE1 . HIS B 311 ? 0.8501 0.8604 0.9074 -0.0149 -0.0726 -0.0520 311 HIS B CE1 6623 N NE2 . HIS B 311 ? 0.8829 0.9046 0.9407 -0.0155 -0.0686 -0.0449 311 HIS B NE2 6624 N N . VAL B 312 ? 0.6916 0.7257 0.7415 -0.0182 -0.0602 -0.0609 312 VAL B N 6625 C CA . VAL B 312 ? 0.6970 0.7458 0.7572 -0.0170 -0.0540 -0.0564 312 VAL B CA 6626 C C . VAL B 312 ? 0.7013 0.7479 0.7814 -0.0150 -0.0547 -0.0524 312 VAL B C 6627 O O . VAL B 312 ? 0.7941 0.8311 0.8816 -0.0131 -0.0590 -0.0581 312 VAL B O 6628 C CB . VAL B 312 ? 0.7267 0.7790 0.7837 -0.0155 -0.0513 -0.0639 312 VAL B CB 6629 C CG1 . VAL B 312 ? 0.7147 0.7847 0.7823 -0.0139 -0.0437 -0.0585 312 VAL B CG1 6630 C CG2 . VAL B 312 ? 0.7778 0.8306 0.8159 -0.0182 -0.0514 -0.0695 312 VAL B CG2 6631 N N . LYS B 313 ? 0.6209 0.6760 0.7101 -0.0157 -0.0512 -0.0424 313 LYS B N 6632 C CA . LYS B 313 ? 0.6001 0.6541 0.7108 -0.0151 -0.0512 -0.0379 313 LYS B CA 6633 C C . LYS B 313 ? 0.7790 0.8495 0.8993 -0.0150 -0.0431 -0.0335 313 LYS B C 6634 O O . LYS B 313 ? 0.7470 0.8311 0.8576 -0.0153 -0.0369 -0.0289 313 LYS B O 6635 C CB . LYS B 313 ? 0.5102 0.5606 0.6268 -0.0156 -0.0525 -0.0296 313 LYS B CB 6636 C CG . LYS B 313 ? 0.7485 0.7907 0.8489 -0.0152 -0.0571 -0.0317 313 LYS B CG 6637 C CD . LYS B 313 ? 1.7583 1.7927 1.8668 -0.0137 -0.0601 -0.0269 313 LYS B CD 6638 C CE . LYS B 313 ? 1.7939 1.8235 1.8866 -0.0125 -0.0635 -0.0294 313 LYS B CE 6639 N NZ . LYS B 313 ? 0.2650 0.2852 0.3619 -0.0094 -0.0674 -0.0288 313 LYS B NZ 6640 N N . ASN B 314 ? 0.7797 0.8509 0.9180 -0.0143 -0.0430 -0.0356 314 ASN B N 6641 C CA . ASN B 314 ? 0.6859 0.7750 0.8352 -0.0142 -0.0341 -0.0306 314 ASN B CA 6642 C C . ASN B 314 ? 0.6225 0.7155 0.7991 -0.0164 -0.0319 -0.0225 314 ASN B C 6643 O O . ASN B 314 ? 0.7392 0.8234 0.9312 -0.0165 -0.0381 -0.0277 314 ASN B O 6644 C CB . ASN B 314 ? 0.5888 0.6816 0.7349 -0.0109 -0.0332 -0.0412 314 ASN B CB 6645 C CG . ASN B 314 ? 0.6023 0.7154 0.7614 -0.0099 -0.0234 -0.0369 314 ASN B CG 6646 O OD1 . ASN B 314 ? 0.6535 0.7786 0.8223 -0.0123 -0.0165 -0.0248 314 ASN B OD1 6647 N ND2 . ASN B 314 ? 0.5536 0.6706 0.7129 -0.0059 -0.0224 -0.0465 314 ASN B ND2 6648 N N . GLN B 315 ? 0.5986 0.7050 0.7812 -0.0183 -0.0234 -0.0096 315 GLN B N 6649 C CA . GLN B 315 ? 0.6455 0.7542 0.8544 -0.0218 -0.0207 0.0004 315 GLN B CA 6650 C C . GLN B 315 ? 0.6383 0.7648 0.8658 -0.0227 -0.0126 0.0035 315 GLN B C 6651 O O . GLN B 315 ? 0.6718 0.8010 0.9244 -0.0267 -0.0102 0.0114 315 GLN B O 6652 C CB . GLN B 315 ? 0.6804 0.7915 0.8875 -0.0236 -0.0162 0.0154 315 GLN B CB 6653 C CG . GLN B 315 ? 0.7632 0.8599 0.9543 -0.0222 -0.0232 0.0134 315 GLN B CG 6654 C CD . GLN B 315 ? 0.8413 0.9404 1.0330 -0.0227 -0.0192 0.0286 315 GLN B CD 6655 O OE1 . GLN B 315 ? 0.8445 0.9571 1.0445 -0.0241 -0.0104 0.0418 315 GLN B OE1 6656 N NE2 . GLN B 315 ? 0.7253 0.8119 0.9081 -0.0210 -0.0253 0.0276 315 GLN B NE2 6657 N N . VAL B 316 ? 0.5831 0.7219 0.7990 -0.0191 -0.0079 -0.0027 316 VAL B N 6658 C CA . VAL B 316 ? 0.6696 0.8268 0.9027 -0.0186 0.0000 -0.0018 316 VAL B CA 6659 C C . VAL B 316 ? 0.6730 0.8229 0.9174 -0.0161 -0.0079 -0.0159 316 VAL B C 6660 O O . VAL B 316 ? 0.4806 0.6171 0.7081 -0.0125 -0.0158 -0.0277 316 VAL B O 6661 C CB . VAL B 316 ? 0.6059 0.7818 0.8201 -0.0146 0.0097 -0.0020 316 VAL B CB 6662 C CG1 . VAL B 316 ? 0.5435 0.7420 0.7765 -0.0140 0.0204 0.0020 316 VAL B CG1 6663 C CG2 . VAL B 316 ? 0.6295 0.8104 0.8266 -0.0158 0.0144 0.0097 316 VAL B CG2 6664 N N . PHE B 317 ? 0.6354 0.7947 0.9089 -0.0181 -0.0060 -0.0141 317 PHE B N 6665 C CA . PHE B 317 ? 0.5821 0.7360 0.8686 -0.0152 -0.0146 -0.0269 317 PHE B CA 6666 C C . PHE B 317 ? 0.5957 0.7697 0.8932 -0.0109 -0.0078 -0.0314 317 PHE B C 6667 O O . PHE B 317 ? 0.6882 0.8577 0.9825 -0.0049 -0.0139 -0.0442 317 PHE B O 6668 C CB . PHE B 317 ? 0.5434 0.6879 0.8557 -0.0203 -0.0229 -0.0259 317 PHE B CB 6669 C CG . PHE B 317 ? 0.6316 0.7532 0.9310 -0.0220 -0.0323 -0.0267 317 PHE B CG 6670 C CD1 . PHE B 317 ? 0.5845 0.7019 0.8893 -0.0274 -0.0298 -0.0150 317 PHE B CD1 6671 C CD2 . PHE B 317 ? 0.7365 0.8412 1.0172 -0.0176 -0.0427 -0.0385 317 PHE B CD2 6672 C CE1 . PHE B 317 ? 0.5931 0.6907 0.8859 -0.0278 -0.0378 -0.0164 317 PHE B CE1 6673 C CE2 . PHE B 317 ? 0.7737 0.8596 1.0418 -0.0187 -0.0502 -0.0392 317 PHE B CE2 6674 C CZ . PHE B 317 ? 0.6021 0.6849 0.8763 -0.0234 -0.0477 -0.0288 317 PHE B CZ 6675 N N . LEU B 318 ? 0.5336 0.7300 0.8439 -0.0133 0.0052 -0.0204 318 LEU B N 6676 C CA . LEU B 318 ? 0.5587 0.7785 0.8782 -0.0086 0.0144 -0.0236 318 LEU B CA 6677 C C . LEU B 318 ? 0.6618 0.8935 0.9542 -0.0039 0.0249 -0.0228 318 LEU B C 6678 O O . LEU B 318 ? 0.6883 0.9293 0.9732 -0.0072 0.0337 -0.0099 318 LEU B O 6679 C CB . LEU B 318 ? 0.5318 0.7724 0.8863 -0.0143 0.0228 -0.0123 318 LEU B CB 6680 C CG . LEU B 318 ? 0.5139 0.7445 0.8972 -0.0221 0.0143 -0.0088 318 LEU B CG 6681 C CD1 . LEU B 318 ? 0.5556 0.8105 0.9754 -0.0280 0.0243 0.0019 318 LEU B CD1 6682 C CD2 . LEU B 318 ? 0.4409 0.6565 0.8277 -0.0181 -0.0008 -0.0245 318 LEU B CD2 6683 N N . PHE B 319 ? 0.6823 0.9135 0.9603 0.0043 0.0234 -0.0369 319 PHE B N 6684 C CA . PHE B 319 ? 0.7213 0.9639 0.9743 0.0093 0.0323 -0.0395 319 PHE B CA 6685 C C . PHE B 319 ? 0.8016 1.0412 1.0464 0.0187 0.0292 -0.0571 319 PHE B C 6686 O O . PHE B 319 ? 0.9417 1.1639 1.1919 0.0208 0.0180 -0.0663 319 PHE B O 6687 C CB . PHE B 319 ? 0.5660 0.7944 0.7900 0.0066 0.0290 -0.0365 319 PHE B CB 6688 C CG . PHE B 319 ? 0.5610 0.7614 0.7715 0.0071 0.0149 -0.0470 319 PHE B CG 6689 C CD1 . PHE B 319 ? 0.6183 0.8097 0.8068 0.0128 0.0114 -0.0609 319 PHE B CD1 6690 C CD2 . PHE B 319 ? 0.5589 0.7415 0.7783 0.0018 0.0055 -0.0430 319 PHE B CD2 6691 C CE1 . PHE B 319 ? 0.6202 0.7858 0.7962 0.0126 -0.0008 -0.0691 319 PHE B CE1 6692 C CE2 . PHE B 319 ? 0.6136 0.7720 0.8191 0.0025 -0.0066 -0.0519 319 PHE B CE2 6693 C CZ . PHE B 319 ? 0.5623 0.7124 0.7462 0.0076 -0.0095 -0.0641 319 PHE B CZ 6694 N N . SER B 320 ? 0.7907 1.0466 1.0218 0.0248 0.0390 -0.0618 320 SER B N 6695 C CA . SER B 320 ? 0.7977 1.0481 1.0202 0.0343 0.0359 -0.0793 320 SER B CA 6696 C C . SER B 320 ? 0.8447 1.0669 1.0396 0.0345 0.0249 -0.0887 320 SER B C 6697 O O . SER B 320 ? 0.8260 1.0471 0.9967 0.0324 0.0271 -0.0875 320 SER B O 6698 C CB . SER B 320 ? 0.7434 1.0189 0.9585 0.0416 0.0494 -0.0837 320 SER B CB 6699 O OG . SER B 320 ? 0.7775 1.0430 0.9810 0.0511 0.0454 -0.1019 320 SER B OG 6700 N N . LYS B 321 ? 0.8068 1.0073 1.0057 0.0369 0.0130 -0.0976 321 LYS B N 6701 C CA . LYS B 321 ? 0.7150 0.8881 0.8900 0.0359 0.0027 -0.1046 321 LYS B CA 6702 C C . LYS B 321 ? 0.7595 0.9308 0.9094 0.0410 0.0058 -0.1162 321 LYS B C 6703 O O . LYS B 321 ? 0.7567 0.9114 0.8843 0.0375 0.0005 -0.1192 321 LYS B O 6704 C CB . LYS B 321 ? 0.6873 0.8383 0.8711 0.0381 -0.0102 -0.1107 321 LYS B CB 6705 C CG . LYS B 321 ? 0.7202 0.8662 0.9212 0.0315 -0.0167 -0.1009 321 LYS B CG 6706 C CD . LYS B 321 ? 0.8237 0.9933 1.0558 0.0310 -0.0103 -0.0942 321 LYS B CD 6707 C CE . LYS B 321 ? 0.6337 0.7990 0.8820 0.0229 -0.0157 -0.0842 321 LYS B CE 6708 N NZ . LYS B 321 ? 0.6268 0.7741 0.8532 0.0172 -0.0202 -0.0800 321 LYS B NZ 6709 N N . GLU B 322 ? 0.7438 0.9330 0.8979 0.0490 0.0145 -0.1234 322 GLU B N 6710 C CA . GLU B 322 ? 0.7717 0.9624 0.9021 0.0539 0.0187 -0.1350 322 GLU B CA 6711 C C . GLU B 322 ? 0.7352 0.9338 0.8452 0.0470 0.0229 -0.1274 322 GLU B C 6712 O O . GLU B 322 ? 0.5595 0.7441 0.6462 0.0449 0.0179 -0.1343 322 GLU B O 6713 C CB . GLU B 322 ? 0.7790 0.9936 0.9183 0.0638 0.0297 -0.1421 322 GLU B CB 6714 C CG . GLU B 322 ? 1.0877 1.2912 1.2379 0.0740 0.0248 -0.1558 322 GLU B CG 6715 C CD . GLU B 322 ? 1.3759 1.6066 1.5532 0.0815 0.0340 -0.1550 322 GLU B CD 6716 O OE1 . GLU B 322 ? 1.4086 1.6420 1.5882 0.0930 0.0362 -0.1687 322 GLU B OE1 6717 O OE2 . GLU B 322 ? 1.4276 1.6769 1.6252 0.0758 0.0389 -0.1408 322 GLU B OE2 6718 N N . ALA B 323 ? 0.8473 1.0685 0.9674 0.0431 0.0316 -0.1125 323 ALA B N 6719 C CA . ALA B 323 ? 0.7589 0.9926 0.8619 0.0379 0.0370 -0.1028 323 ALA B CA 6720 C C . ALA B 323 ? 0.7233 0.9357 0.8098 0.0308 0.0267 -0.1009 323 ALA B C 6721 O O . ALA B 323 ? 0.8317 1.0499 0.8972 0.0284 0.0282 -0.0995 323 ALA B O 6722 C CB . ALA B 323 ? 0.6305 0.8860 0.7519 0.0339 0.0461 -0.0841 323 ALA B CB 6723 N N . LEU B 324 ? 0.6837 0.8731 0.7799 0.0277 0.0164 -0.1010 324 LEU B N 6724 C CA . LEU B 324 ? 0.6283 0.7976 0.7117 0.0211 0.0068 -0.0990 324 LEU B CA 6725 C C . LEU B 324 ? 0.7020 0.8495 0.7694 0.0230 -0.0013 -0.1146 324 LEU B C 6726 O O . LEU B 324 ? 0.8280 0.9707 0.8752 0.0195 -0.0039 -0.1178 324 LEU B O 6727 C CB . LEU B 324 ? 0.7132 0.8708 0.8150 0.0165 0.0006 -0.0892 324 LEU B CB 6728 C CG . LEU B 324 ? 0.7807 0.9143 0.8730 0.0114 -0.0104 -0.0893 324 LEU B CG 6729 C CD1 . LEU B 324 ? 0.8970 1.0356 0.9755 0.0057 -0.0093 -0.0802 324 LEU B CD1 6730 C CD2 . LEU B 324 ? 0.5152 0.6375 0.6272 0.0099 -0.0167 -0.0846 324 LEU B CD2 6731 N N . TYR B 325 ? 0.6903 0.8249 0.7674 0.0284 -0.0054 -0.1239 325 TYR B N 6732 C CA . TYR B 325 ? 0.8517 0.9613 0.9155 0.0296 -0.0139 -0.1368 325 TYR B CA 6733 C C . TYR B 325 ? 0.8792 0.9912 0.9245 0.0333 -0.0107 -0.1505 325 TYR B C 6734 O O . TYR B 325 ? 0.8311 0.9242 0.8606 0.0306 -0.0171 -0.1589 325 TYR B O 6735 C CB . TYR B 325 ? 0.8291 0.9222 0.9077 0.0351 -0.0203 -0.1418 325 TYR B CB 6736 C CG . TYR B 325 ? 0.7970 0.8825 0.8903 0.0313 -0.0266 -0.1314 325 TYR B CG 6737 C CD1 . TYR B 325 ? 0.7485 0.8368 0.8642 0.0363 -0.0281 -0.1306 325 TYR B CD1 6738 C CD2 . TYR B 325 ? 0.7718 0.8486 0.8571 0.0230 -0.0312 -0.1231 325 TYR B CD2 6739 C CE1 . TYR B 325 ? 0.6815 0.7633 0.8102 0.0329 -0.0347 -0.1228 325 TYR B CE1 6740 C CE2 . TYR B 325 ? 0.7217 0.7914 0.8195 0.0203 -0.0370 -0.1152 325 TYR B CE2 6741 C CZ . TYR B 325 ? 0.6942 0.7661 0.8133 0.0250 -0.0390 -0.1154 325 TYR B CZ 6742 O OH . TYR B 325 ? 0.6569 0.7223 0.7881 0.0223 -0.0456 -0.1091 325 TYR B OH 6743 N N . SER B 326 ? 0.8550 0.9904 0.9022 0.0393 -0.0007 -0.1534 326 SER B N 6744 C CA . SER B 326 ? 0.8818 1.0197 0.9112 0.0440 0.0022 -0.1686 326 SER B CA 6745 C C . SER B 326 ? 0.9228 1.0645 0.9296 0.0368 0.0011 -0.1681 326 SER B C 6746 O O . SER B 326 ? 0.8269 0.9571 0.8169 0.0364 -0.0029 -0.1817 326 SER B O 6747 C CB . SER B 326 ? 0.7030 0.8672 0.7394 0.0532 0.0139 -0.1722 326 SER B CB 6748 O OG . SER B 326 ? 0.8511 1.0422 0.8912 0.0499 0.0226 -0.1570 326 SER B OG 6749 N N . VAL B 327 ? 0.9377 1.0950 0.9454 0.0310 0.0042 -0.1524 327 VAL B N 6750 C CA . VAL B 327 ? 0.8136 0.9763 0.8023 0.0242 0.0023 -0.1493 327 VAL B CA 6751 C C . VAL B 327 ? 0.8114 0.9480 0.7894 0.0178 -0.0089 -0.1568 327 VAL B C 6752 O O . VAL B 327 ? 0.7939 0.9333 0.7541 0.0138 -0.0113 -0.1623 327 VAL B O 6753 C CB . VAL B 327 ? 0.7560 0.9328 0.7520 0.0192 0.0053 -0.1290 327 VAL B CB 6754 C CG1 . VAL B 327 ? 0.6452 0.8222 0.6249 0.0119 0.0003 -0.1248 327 VAL B CG1 6755 C CG2 . VAL B 327 ? 0.8108 1.0172 0.8119 0.0240 0.0176 -0.1210 327 VAL B CG2 6756 N N . PHE B 328 ? 0.7964 0.9089 0.7853 0.0167 -0.0157 -0.1566 328 PHE B N 6757 C CA . PHE B 328 ? 0.7039 0.7905 0.6841 0.0110 -0.0254 -0.1633 328 PHE B CA 6758 C C . PHE B 328 ? 0.7201 0.7880 0.6968 0.0162 -0.0283 -0.1805 328 PHE B C 6759 O O . PHE B 328 ? 0.6317 0.6859 0.5952 0.0120 -0.0334 -0.1906 328 PHE B O 6760 C CB . PHE B 328 ? 0.7085 0.7783 0.6998 0.0070 -0.0316 -0.1528 328 PHE B CB 6761 C CG . PHE B 328 ? 0.7034 0.7868 0.6992 0.0022 -0.0299 -0.1368 328 PHE B CG 6762 C CD1 . PHE B 328 ? 0.6615 0.7538 0.6749 0.0050 -0.0262 -0.1261 328 PHE B CD1 6763 C CD2 . PHE B 328 ? 0.6606 0.7479 0.6446 -0.0050 -0.0323 -0.1327 328 PHE B CD2 6764 C CE1 . PHE B 328 ? 0.6188 0.7212 0.6372 0.0009 -0.0249 -0.1117 328 PHE B CE1 6765 C CE2 . PHE B 328 ? 0.6586 0.7575 0.6474 -0.0081 -0.0309 -0.1180 328 PHE B CE2 6766 C CZ . PHE B 328 ? 0.5984 0.7035 0.6041 -0.0051 -0.0271 -0.1076 328 PHE B CZ 6767 N N . ALA B 329 ? 0.7552 0.8220 0.7451 0.0252 -0.0254 -0.1837 329 ALA B N 6768 C CA . ALA B 329 ? 0.7760 0.8216 0.7649 0.0313 -0.0289 -0.1988 329 ALA B CA 6769 C C . ALA B 329 ? 0.8551 0.9046 0.8275 0.0332 -0.0267 -0.2152 329 ALA B C 6770 O O . ALA B 329 ? 0.9131 0.9391 0.8770 0.0319 -0.0328 -0.2274 329 ALA B O 6771 C CB . ALA B 329 ? 0.7911 0.8403 0.7986 0.0419 -0.0255 -0.1991 329 ALA B CB 6772 N N . GLU B 330 ? 0.8960 0.9750 0.8633 0.0361 -0.0180 -0.2150 330 GLU B N 6773 C CA . GLU B 330 ? 0.8796 0.9673 0.8295 0.0388 -0.0153 -0.2310 330 GLU B CA 6774 C C . GLU B 330 ? 0.8825 0.9713 0.8141 0.0283 -0.0203 -0.2324 330 GLU B C 6775 O O . GLU B 330 ? 1.0102 1.1154 0.9266 0.0296 -0.0173 -0.2422 330 GLU B O 6776 C CB . GLU B 330 ? 0.7692 0.8911 0.7193 0.0471 -0.0032 -0.2300 330 GLU B CB 6777 C CG . GLU B 330 ? 0.8918 1.0226 0.8635 0.0560 0.0035 -0.2239 330 GLU B CG 6778 C CD . GLU B 330 ? 0.9205 1.0843 0.8906 0.0649 0.0163 -0.2266 330 GLU B CD 6779 O OE1 . GLU B 330 ? 0.8767 1.0614 0.8627 0.0672 0.0244 -0.2130 330 GLU B OE1 6780 O OE2 . GLU B 330 ? 0.7695 0.9385 0.7223 0.0694 0.0185 -0.2428 330 GLU B OE2 6781 N N . MET B 331 ? 0.8538 0.9274 0.7870 0.0182 -0.0277 -0.2231 331 MET B N 6782 C CA . MET B 331 ? 0.9115 0.9873 0.8301 0.0079 -0.0329 -0.2243 331 MET B CA 6783 C C . MET B 331 ? 0.9793 1.0307 0.8889 0.0045 -0.0402 -0.2425 331 MET B C 6784 O O . MET B 331 ? 1.0775 1.1010 0.9946 0.0062 -0.0442 -0.2473 331 MET B O 6785 C CB . MET B 331 ? 0.8430 0.9151 0.7675 -0.0014 -0.0372 -0.2070 331 MET B CB 6786 C CG . MET B 331 ? 0.7831 0.8808 0.7134 -0.0004 -0.0310 -0.1892 331 MET B CG 6787 S SD . MET B 331 ? 0.8327 0.9251 0.7696 -0.0098 -0.0361 -0.1710 331 MET B SD 6788 C CE . MET B 331 ? 0.6132 0.7403 0.5502 -0.0077 -0.0280 -0.1556 331 MET B CE 6789 N N . ASN B 332 ? 0.9266 0.9884 0.8203 -0.0002 -0.0424 -0.2526 332 ASN B N 6790 C CA . ASN B 332 ? 0.9077 0.9478 0.7929 -0.0044 -0.0495 -0.2717 332 ASN B CA 6791 C C . ASN B 332 ? 0.8872 0.9173 0.7693 -0.0189 -0.0581 -0.2687 332 ASN B C 6792 O O . ASN B 332 ? 0.8162 0.8496 0.6867 -0.0252 -0.0628 -0.2813 332 ASN B O 6793 C CB . ASN B 332 ? 0.8572 0.9138 0.7271 0.0014 -0.0467 -0.2904 332 ASN B CB 6794 C CG . ASN B 332 ? 0.9040 0.9945 0.7607 -0.0023 -0.0451 -0.2855 332 ASN B CG 6795 O OD1 . ASN B 332 ? 0.9707 1.0763 0.8319 -0.0060 -0.0434 -0.2661 332 ASN B OD1 6796 N ND2 . ASN B 332 ? 0.7632 0.8656 0.6032 -0.0005 -0.0460 -0.3035 332 ASN B ND2 6797 N N . ILE B 333 ? 0.8367 0.8553 0.7298 -0.0241 -0.0602 -0.2526 333 ILE B N 6798 C CA . ILE B 333 ? 0.9165 0.9250 0.8094 -0.0375 -0.0673 -0.2480 333 ILE B CA 6799 C C . ILE B 333 ? 1.0059 0.9774 0.9067 -0.0404 -0.0721 -0.2493 333 ILE B C 6800 O O . ILE B 333 ? 1.0918 1.0480 0.9989 -0.0312 -0.0701 -0.2517 333 ILE B O 6801 C CB . ILE B 333 ? 0.8856 0.9127 0.7833 -0.0410 -0.0656 -0.2275 333 ILE B CB 6802 C CG1 . ILE B 333 ? 0.8382 0.8592 0.7489 -0.0336 -0.0613 -0.2141 333 ILE B CG1 6803 C CG2 . ILE B 333 ? 0.8014 0.8639 0.6903 -0.0387 -0.0616 -0.2252 333 ILE B CG2 6804 C CD1 . ILE B 333 ? 0.8209 0.8661 0.7361 -0.0325 -0.0569 -0.1965 333 ILE B CD1 6805 N N . LYS B 334 ? 0.9936 0.9518 0.8946 -0.0529 -0.0783 -0.2473 334 LYS B N 6806 C CA . LYS B 334 ? 0.8659 0.7889 0.7732 -0.0567 -0.0826 -0.2464 334 LYS B CA 6807 C C . LYS B 334 ? 0.9436 0.8607 0.8601 -0.0558 -0.0814 -0.2272 334 LYS B C 6808 O O . LYS B 334 ? 0.9744 0.8660 0.8963 -0.0519 -0.0828 -0.2251 334 LYS B O 6809 C CB . LYS B 334 ? 0.8355 0.7451 0.7398 -0.0713 -0.0893 -0.2534 334 LYS B CB 6810 C CG . LYS B 334 ? 1.0675 0.9625 0.9659 -0.0712 -0.0926 -0.2758 334 LYS B CG 6811 C CD . LYS B 334 ? 1.1572 1.0404 1.0544 -0.0872 -0.0997 -0.2837 334 LYS B CD 6812 C CE . LYS B 334 ? 1.1760 1.0584 1.0648 -0.0869 -0.1029 -0.3081 334 LYS B CE 6813 N NZ . LYS B 334 ? 1.1837 1.0680 1.0708 -0.1033 -0.1101 -0.3169 334 LYS B NZ 6814 N N . MET B 335 ? 0.9177 0.8579 0.8355 -0.0586 -0.0794 -0.2136 335 MET B N 6815 C CA . MET B 335 ? 0.8876 0.8228 0.8132 -0.0579 -0.0787 -0.1968 335 MET B CA 6816 C C . MET B 335 ? 0.9049 0.8643 0.8351 -0.0504 -0.0735 -0.1858 335 MET B C 6817 O O . MET B 335 ? 1.0059 0.9911 0.9329 -0.0521 -0.0712 -0.1827 335 MET B O 6818 C CB . MET B 335 ? 0.9318 0.8648 0.8570 -0.0705 -0.0822 -0.1887 335 MET B CB 6819 C CG . MET B 335 ? 0.9422 0.8540 0.8644 -0.0805 -0.0871 -0.1984 335 MET B CG 6820 S SD . MET B 335 ? 1.0044 0.9267 0.9273 -0.0959 -0.0896 -0.1896 335 MET B SD 6821 C CE . MET B 335 ? 1.0002 0.9148 0.9289 -0.0927 -0.0875 -0.1702 335 MET B CE 6822 N N . LEU B 336 ? 0.8665 0.8169 0.8049 -0.0421 -0.0720 -0.1797 336 LEU B N 6823 C CA . LEU B 336 ? 0.7802 0.7492 0.7262 -0.0360 -0.0677 -0.1683 336 LEU B CA 6824 C C . LEU B 336 ? 0.8789 0.8349 0.8319 -0.0362 -0.0702 -0.1565 336 LEU B C 6825 O O . LEU B 336 ? 0.8950 0.8293 0.8510 -0.0325 -0.0731 -0.1581 336 LEU B O 6826 C CB . LEU B 336 ? 0.6966 0.6718 0.6480 -0.0247 -0.0632 -0.1736 336 LEU B CB 6827 C CG . LEU B 336 ? 0.7929 0.7871 0.7547 -0.0194 -0.0584 -0.1617 336 LEU B CG 6828 C CD1 . LEU B 336 ? 0.7739 0.7936 0.7316 -0.0237 -0.0553 -0.1543 336 LEU B CD1 6829 C CD2 . LEU B 336 ? 0.8205 0.8219 0.7897 -0.0088 -0.0534 -0.1668 336 LEU B CD2 6830 N N . SER B 337 ? 0.8289 0.7985 0.7838 -0.0398 -0.0695 -0.1450 337 SER B N 6831 C CA . SER B 337 ? 0.8257 0.7879 0.7872 -0.0382 -0.0712 -0.1341 337 SER B CA 6832 C C . SER B 337 ? 0.8406 0.8221 0.8114 -0.0326 -0.0672 -0.1261 337 SER B C 6833 O O . SER B 337 ? 0.7948 0.7969 0.7646 -0.0345 -0.0640 -0.1223 337 SER B O 6834 C CB . SER B 337 ? 0.8654 0.8248 0.8222 -0.0471 -0.0737 -0.1274 337 SER B CB 6835 O OG . SER B 337 ? 0.7839 0.7247 0.7339 -0.0538 -0.0771 -0.1329 337 SER B OG 6836 N N . ILE B 338 ? 0.8471 0.8218 0.8276 -0.0259 -0.0679 -0.1233 338 ILE B N 6837 C CA . ILE B 338 ? 0.7742 0.7636 0.7659 -0.0222 -0.0652 -0.1146 338 ILE B CA 6838 C C . ILE B 338 ? 0.7654 0.7422 0.7634 -0.0203 -0.0697 -0.1088 338 ILE B C 6839 O O . ILE B 338 ? 0.7343 0.6989 0.7374 -0.0149 -0.0726 -0.1120 338 ILE B O 6840 C CB . ILE B 338 ? 0.7324 0.7324 0.7339 -0.0150 -0.0607 -0.1177 338 ILE B CB 6841 C CG1 . ILE B 338 ? 0.6537 0.6715 0.6484 -0.0157 -0.0552 -0.1223 338 ILE B CG1 6842 C CG2 . ILE B 338 ? 0.6918 0.7020 0.7080 -0.0121 -0.0592 -0.1081 338 ILE B CG2 6843 C CD1 . ILE B 338 ? 0.5945 0.6240 0.5974 -0.0082 -0.0495 -0.1262 338 ILE B CD1 6844 N N . SER B 339 ? 0.8496 0.8303 0.8471 -0.0238 -0.0706 -0.1008 339 SER B N 6845 C CA . SER B 339 ? 0.8079 0.7759 0.8072 -0.0225 -0.0754 -0.0965 339 SER B CA 6846 C C . SER B 339 ? 0.7245 0.7023 0.7341 -0.0207 -0.0750 -0.0890 339 SER B C 6847 O O . SER B 339 ? 0.7291 0.7227 0.7415 -0.0224 -0.0709 -0.0843 339 SER B O 6848 C CB . SER B 339 ? 0.7662 0.7238 0.7527 -0.0287 -0.0779 -0.0954 339 SER B CB 6849 O OG . SER B 339 ? 0.8682 0.8131 0.8467 -0.0311 -0.0790 -0.1021 339 SER B OG 6850 N N . ASP B 340 ? 0.7507 0.7184 0.7654 -0.0169 -0.0797 -0.0879 340 ASP B N 6851 C CA . ASP B 340 ? 0.7649 0.7385 0.7896 -0.0152 -0.0805 -0.0825 340 ASP B CA 6852 C C . ASP B 340 ? 0.7611 0.7503 0.8012 -0.0136 -0.0759 -0.0798 340 ASP B C 6853 O O . ASP B 340 ? 0.6596 0.6599 0.7035 -0.0153 -0.0725 -0.0737 340 ASP B O 6854 C CB . ASP B 340 ? 0.8002 0.7770 0.8170 -0.0192 -0.0797 -0.0775 340 ASP B CB 6855 C CG . ASP B 340 ? 0.7972 0.7756 0.8227 -0.0166 -0.0816 -0.0733 340 ASP B CG 6856 O OD1 . ASP B 340 ? 0.8841 0.8592 0.9214 -0.0126 -0.0847 -0.0747 340 ASP B OD1 6857 O OD2 . ASP B 340 ? 0.6310 0.6144 0.6523 -0.0185 -0.0803 -0.0692 340 ASP B OD2 6858 N N . THR B 341 ? 0.7739 0.7639 0.8235 -0.0098 -0.0756 -0.0838 341 THR B N 6859 C CA . THR B 341 ? 0.7905 0.7962 0.8553 -0.0085 -0.0702 -0.0809 341 THR B CA 6860 C C . THR B 341 ? 0.7926 0.7954 0.8740 -0.0039 -0.0740 -0.0836 341 THR B C 6861 O O . THR B 341 ? 0.8398 0.8287 0.9180 -0.0011 -0.0807 -0.0884 341 THR B O 6862 C CB . THR B 341 ? 0.9391 0.9539 0.9990 -0.0081 -0.0644 -0.0848 341 THR B CB 6863 O OG1 . THR B 341 ? 0.9865 0.9946 1.0511 -0.0032 -0.0665 -0.0923 341 THR B OG1 6864 C CG2 . THR B 341 ? 1.0158 1.0269 1.0564 -0.0123 -0.0642 -0.0872 341 THR B CG2 6865 N N . PRO B 342 ? 0.7344 0.7511 0.8341 -0.0033 -0.0696 -0.0800 342 PRO B N 6866 C CA . PRO B 342 ? 0.6463 0.6641 0.7651 0.0005 -0.0729 -0.0829 342 PRO B CA 6867 C C . PRO B 342 ? 0.7976 0.8192 0.9186 0.0052 -0.0706 -0.0895 342 PRO B C 6868 O O . PRO B 342 ? 0.7994 0.8264 0.9387 0.0088 -0.0721 -0.0916 342 PRO B O 6869 C CB . PRO B 342 ? 0.5003 0.5334 0.6387 -0.0020 -0.0674 -0.0751 342 PRO B CB 6870 C CG . PRO B 342 ? 0.6081 0.6472 0.7356 -0.0061 -0.0615 -0.0676 342 PRO B CG 6871 C CD . PRO B 342 ? 0.6387 0.6720 0.7429 -0.0062 -0.0615 -0.0721 342 PRO B CD 6872 N N . PHE B 343 ? 0.8623 0.8819 0.9664 0.0054 -0.0673 -0.0934 343 PHE B N 6873 C CA . PHE B 343 ? 0.9489 0.9731 1.0552 0.0106 -0.0641 -0.1005 343 PHE B CA 6874 C C . PHE B 343 ? 1.0012 1.0124 1.1130 0.0170 -0.0720 -0.1071 343 PHE B C 6875 O O . PHE B 343 ? 1.0971 1.0907 1.1997 0.0169 -0.0800 -0.1079 343 PHE B O 6876 C CB . PHE B 343 ? 1.0017 1.0240 1.0879 0.0094 -0.0601 -0.1050 343 PHE B CB 6877 C CG . PHE B 343 ? 1.0185 1.0563 1.0987 0.0043 -0.0528 -0.0989 343 PHE B CG 6878 C CD1 . PHE B 343 ? 0.9754 1.0297 1.0698 0.0027 -0.0478 -0.0898 343 PHE B CD1 6879 C CD2 . PHE B 343 ? 0.9782 1.0140 1.0389 0.0011 -0.0514 -0.1019 343 PHE B CD2 6880 C CE1 . PHE B 343 ? 0.8463 0.9145 0.9343 -0.0010 -0.0414 -0.0827 343 PHE B CE1 6881 C CE2 . PHE B 343 ? 0.9194 0.9711 0.9742 -0.0027 -0.0456 -0.0961 343 PHE B CE2 6882 C CZ . PHE B 343 ? 0.7792 0.8469 0.8469 -0.0033 -0.0405 -0.0859 343 PHE B CZ 6883 N N . ILE B 344 ? 0.8749 0.8963 1.0018 0.0229 -0.0696 -0.1113 344 ILE B N 6884 C CA . ILE B 344 ? 0.6856 0.6983 0.8213 0.0303 -0.0772 -0.1170 344 ILE B CA 6885 C C . ILE B 344 ? 0.7172 0.7215 0.8439 0.0369 -0.0766 -0.1259 344 ILE B C 6886 O O . ILE B 344 ? 0.7021 0.6976 0.8344 0.0444 -0.0830 -0.1307 344 ILE B O 6887 C CB . ILE B 344 ? 0.5565 0.5878 0.7204 0.0332 -0.0760 -0.1159 344 ILE B CB 6888 C CG1 . ILE B 344 ? 0.6161 0.6693 0.7885 0.0343 -0.0640 -0.1162 344 ILE B CG1 6889 C CG2 . ILE B 344 ? 0.5187 0.5546 0.6941 0.0269 -0.0784 -0.1083 344 ILE B CG2 6890 C CD1 . ILE B 344 ? 0.6825 0.7567 0.8847 0.0366 -0.0612 -0.1144 344 ILE B CD1 6891 N N . HIS B 345 ? 0.7517 0.7584 0.8644 0.0346 -0.0694 -0.1284 345 HIS B N 6892 C CA . HIS B 345 ? 0.6617 0.6639 0.7685 0.0412 -0.0670 -0.1383 345 HIS B CA 6893 C C . HIS B 345 ? 0.8085 0.8119 0.8966 0.0367 -0.0607 -0.1416 345 HIS B C 6894 O O . HIS B 345 ? 0.9818 0.9954 1.0642 0.0293 -0.0565 -0.1353 345 HIS B O 6895 C CB . HIS B 345 ? 0.5018 0.5245 0.6297 0.0489 -0.0615 -0.1418 345 HIS B CB 6896 C CG . HIS B 345 ? 0.6266 0.6416 0.7534 0.0590 -0.0619 -0.1530 345 HIS B CG 6897 N ND1 . HIS B 345 ? 0.7317 0.7283 0.8614 0.0661 -0.0713 -0.1565 345 HIS B ND1 6898 C CD2 . HIS B 345 ? 0.5922 0.6149 0.7148 0.0639 -0.0543 -0.1617 345 HIS B CD2 6899 C CE1 . HIS B 345 ? 0.6020 0.5941 0.7306 0.0750 -0.0695 -0.1667 345 HIS B CE1 6900 N NE2 . HIS B 345 ? 0.5485 0.5561 0.6726 0.0739 -0.0591 -0.1708 345 HIS B NE2 6901 N N . MET B 346 ? 0.6969 0.6897 0.7761 0.0417 -0.0605 -0.1520 346 MET B N 6902 C CA . MET B 346 ? 0.7196 0.7176 0.7841 0.0393 -0.0541 -0.1584 346 MET B CA 6903 C C . MET B 346 ? 0.8735 0.8735 0.9418 0.0496 -0.0506 -0.1707 346 MET B C 6904 O O . MET B 346 ? 1.0155 0.9983 1.0879 0.0569 -0.0562 -0.1763 346 MET B O 6905 C CB . MET B 346 ? 0.6807 0.6578 0.7247 0.0317 -0.0590 -0.1598 346 MET B CB 6906 C CG . MET B 346 ? 0.7018 0.6837 0.7303 0.0286 -0.0540 -0.1680 346 MET B CG 6907 S SD . MET B 346 ? 0.7370 0.7533 0.7652 0.0249 -0.0440 -0.1623 346 MET B SD 6908 C CE . MET B 346 ? 0.3650 0.3842 0.3984 0.0168 -0.0469 -0.1456 346 MET B CE 6909 N N . VAL B 347 ? 0.8027 0.8245 0.8693 0.0510 -0.0411 -0.1746 347 VAL B N 6910 C CA . VAL B 347 ? 0.7273 0.7559 0.7973 0.0615 -0.0358 -0.1870 347 VAL B CA 6911 C C . VAL B 347 ? 0.6967 0.7014 0.7491 0.0629 -0.0397 -0.2004 347 VAL B C 6912 O O . VAL B 347 ? 0.7815 0.7743 0.8172 0.0539 -0.0429 -0.2002 347 VAL B O 6913 C CB . VAL B 347 ? 0.7096 0.7708 0.7806 0.0621 -0.0237 -0.1862 347 VAL B CB 6914 C CG1 . VAL B 347 ? 0.8096 0.8759 0.8743 0.0713 -0.0180 -0.2017 347 VAL B CG1 6915 C CG2 . VAL B 347 ? 0.7430 0.8269 0.8378 0.0640 -0.0190 -0.1757 347 VAL B CG2 6916 N N . CYS B 348 ? 0.6451 0.6423 0.7025 0.0743 -0.0398 -0.2123 348 CYS B N 6917 C CA . CYS B 348 ? 0.7076 0.6823 0.7496 0.0763 -0.0426 -0.2268 348 CYS B CA 6918 C C . CYS B 348 ? 0.8186 0.8119 0.8473 0.0757 -0.0341 -0.2368 348 CYS B C 6919 O O . CYS B 348 ? 0.7996 0.8214 0.8353 0.0819 -0.0246 -0.2381 348 CYS B O 6920 C CB . CYS B 348 ? 0.4942 0.4515 0.5464 0.0898 -0.0464 -0.2359 348 CYS B CB 6921 S SG . CYS B 348 ? 1.8319 1.7607 1.8701 0.0960 -0.0489 -0.2563 348 CYS B SG 6922 N N . PRO B 349 ? 0.7584 0.7376 0.7679 0.0676 -0.0374 -0.2431 349 PRO B N 6923 C CA . PRO B 349 ? 0.7736 0.7697 0.7686 0.0673 -0.0309 -0.2541 349 PRO B CA 6924 C C . PRO B 349 ? 0.8866 0.8925 0.8861 0.0820 -0.0242 -0.2692 349 PRO B C 6925 O O . PRO B 349 ? 0.8482 0.8325 0.8545 0.0909 -0.0281 -0.2780 349 PRO B O 6926 C CB . PRO B 349 ? 0.6906 0.6597 0.6687 0.0587 -0.0387 -0.2629 349 PRO B CB 6927 C CG . PRO B 349 ? 0.5780 0.5248 0.5601 0.0504 -0.0471 -0.2496 349 PRO B CG 6928 C CD . PRO B 349 ? 0.6012 0.5503 0.6021 0.0578 -0.0471 -0.2396 349 PRO B CD 6929 N N . PRO B 350 ? 0.9504 0.9889 0.9456 0.0853 -0.0138 -0.2719 350 PRO B N 6930 C CA . PRO B 350 ? 0.9209 0.9743 0.9211 0.1001 -0.0055 -0.2853 350 PRO B CA 6931 C C . PRO B 350 ? 0.9853 1.0186 0.9703 0.1052 -0.0085 -0.3081 350 PRO B C 6932 O O . PRO B 350 ? 0.8306 0.8604 0.8223 0.1190 -0.0059 -0.3217 350 PRO B O 6933 C CB . PRO B 350 ? 0.7665 0.8606 0.7619 0.0994 0.0063 -0.2794 350 PRO B CB 6934 C CG . PRO B 350 ? 0.8882 0.9862 0.8773 0.0847 0.0033 -0.2626 350 PRO B CG 6935 C CD . PRO B 350 ? 0.9714 1.0336 0.9541 0.0759 -0.0095 -0.2638 350 PRO B CD 6936 N N . SER B 351 ? 1.0514 1.0724 1.0174 0.0942 -0.0141 -0.3126 351 SER B N 6937 C CA . SER B 351 ? 1.0127 1.0123 0.9638 0.0958 -0.0186 -0.3343 351 SER B CA 6938 C C . SER B 351 ? 0.9885 0.9527 0.9355 0.0829 -0.0307 -0.3309 351 SER B C 6939 O O . SER B 351 ? 0.9571 0.9226 0.9071 0.0721 -0.0337 -0.3128 351 SER B O 6940 C CB . SER B 351 ? 0.9403 0.9650 0.8710 0.0936 -0.0132 -0.3444 351 SER B CB 6941 O OG . SER B 351 ? 0.8928 0.9522 0.8255 0.1055 -0.0008 -0.3471 351 SER B OG 6942 N N . PRO B 352 ? 0.9215 0.8536 0.8623 0.0841 -0.0374 -0.3479 352 PRO B N 6943 C CA . PRO B 352 ? 0.9372 0.8350 0.8743 0.0711 -0.0483 -0.3449 352 PRO B CA 6944 C C . PRO B 352 ? 0.9616 0.8734 0.8885 0.0547 -0.0501 -0.3340 352 PRO B C 6945 O O . PRO B 352 ? 0.9523 0.8816 0.8649 0.0511 -0.0481 -0.3439 352 PRO B O 6946 C CB . PRO B 352 ? 0.8125 0.6858 0.7399 0.0739 -0.0523 -0.3692 352 PRO B CB 6947 C CG . PRO B 352 ? 0.7889 0.6701 0.7228 0.0929 -0.0456 -0.3818 352 PRO B CG 6948 C CD . PRO B 352 ? 0.7522 0.6772 0.6911 0.0983 -0.0349 -0.3705 352 PRO B CD 6949 N N . SER B 353 ? 0.8282 0.7337 0.7618 0.0456 -0.0539 -0.3146 353 SER B N 6950 C CA . SER B 353 ? 0.9218 0.8415 0.8473 0.0311 -0.0554 -0.3038 353 SER B CA 6951 C C . SER B 353 ? 0.9478 0.8400 0.8660 0.0181 -0.0644 -0.3088 353 SER B C 6952 O O . SER B 353 ? 0.8940 0.7557 0.8123 0.0200 -0.0692 -0.3214 353 SER B O 6953 C CB . SER B 353 ? 1.0238 0.9548 0.9599 0.0280 -0.0541 -0.2808 353 SER B CB 6954 O OG . SER B 353 ? 1.1770 1.0784 1.1197 0.0233 -0.0612 -0.2724 353 SER B OG 6955 N N . SER B 354 ? 1.0283 0.9317 0.9412 0.0048 -0.0666 -0.2987 354 SER B N 6956 C CA . SER B 354 ? 1.1834 1.0664 1.0906 -0.0092 -0.0744 -0.3027 354 SER B CA 6957 C C . SER B 354 ? 1.1997 1.0769 1.1130 -0.0190 -0.0773 -0.2823 354 SER B C 6958 O O . SER B 354 ? 1.2700 1.1341 1.1808 -0.0321 -0.0829 -0.2809 354 SER B O 6959 C CB . SER B 354 ? 1.2945 1.1988 1.1881 -0.0165 -0.0751 -0.3137 354 SER B CB 6960 O OG . SER B 354 ? 1.3372 1.2776 1.2282 -0.0171 -0.0701 -0.3011 354 SER B OG 6961 N N . PHE B 355 ? 1.1739 1.0620 1.0961 -0.0126 -0.0734 -0.2669 355 PHE B N 6962 C CA . PHE B 355 ? 1.0464 0.9262 0.9747 -0.0191 -0.0761 -0.2486 355 PHE B CA 6963 C C . PHE B 355 ? 1.0223 0.8648 0.9516 -0.0243 -0.0827 -0.2507 355 PHE B C 6964 O O . PHE B 355 ? 1.1499 0.9697 1.0825 -0.0159 -0.0841 -0.2587 355 PHE B O 6965 C CB . PHE B 355 ? 1.0256 0.9124 0.9652 -0.0088 -0.0725 -0.2367 355 PHE B CB 6966 C CG . PHE B 355 ? 0.9413 0.8636 0.8828 -0.0055 -0.0657 -0.2298 355 PHE B CG 6967 C CD1 . PHE B 355 ? 0.9435 0.8785 0.8941 0.0067 -0.0602 -0.2292 355 PHE B CD1 6968 C CD2 . PHE B 355 ? 0.9173 0.8603 0.8525 -0.0146 -0.0648 -0.2231 355 PHE B CD2 6969 C CE1 . PHE B 355 ? 1.0360 1.0026 0.9894 0.0089 -0.0535 -0.2216 355 PHE B CE1 6970 C CE2 . PHE B 355 ? 1.0354 1.0091 0.9724 -0.0113 -0.0586 -0.2152 355 PHE B CE2 6971 C CZ . PHE B 355 ? 1.1168 1.1017 1.0630 0.0000 -0.0527 -0.2141 355 PHE B CZ 6972 N N . THR B 356 ? 0.9685 0.8047 0.8952 -0.0379 -0.0864 -0.2429 356 THR B N 6973 C CA . THR B 356 ? 1.0350 0.8366 0.9634 -0.0439 -0.0918 -0.2402 356 THR B CA 6974 C C . THR B 356 ? 1.0095 0.8114 0.9413 -0.0486 -0.0923 -0.2201 356 THR B C 6975 O O . THR B 356 ? 1.0453 0.8211 0.9781 -0.0530 -0.0959 -0.2134 356 THR B O 6976 C CB . THR B 356 ? 1.0127 0.8020 0.9356 -0.0573 -0.0961 -0.2512 356 THR B CB 6977 O OG1 . THR B 356 ? 0.9066 0.7190 0.8268 -0.0696 -0.0960 -0.2443 356 THR B OG1 6978 C CG2 . THR B 356 ? 1.0484 0.8399 0.9664 -0.0519 -0.0958 -0.2729 356 THR B CG2 6979 N N . PHE B 357 ? 0.9192 0.7505 0.8524 -0.0472 -0.0885 -0.2106 357 PHE B N 6980 C CA . PHE B 357 ? 0.7790 0.6141 0.7151 -0.0502 -0.0885 -0.1930 357 PHE B CA 6981 C C . PHE B 357 ? 0.8472 0.7050 0.7892 -0.0406 -0.0845 -0.1854 357 PHE B C 6982 O O . PHE B 357 ? 0.8916 0.7755 0.8332 -0.0390 -0.0805 -0.1878 357 PHE B O 6983 C CB . PHE B 357 ? 0.8768 0.7241 0.8090 -0.0641 -0.0891 -0.1879 357 PHE B CB 6984 C CG . PHE B 357 ? 0.9592 0.8128 0.8937 -0.0667 -0.0885 -0.1711 357 PHE B CG 6985 C CD1 . PHE B 357 ? 0.8887 0.7205 0.8226 -0.0719 -0.0911 -0.1626 357 PHE B CD1 6986 C CD2 . PHE B 357 ? 0.9768 0.8580 0.9138 -0.0636 -0.0851 -0.1636 357 PHE B CD2 6987 C CE1 . PHE B 357 ? 0.9737 0.8126 0.9083 -0.0734 -0.0903 -0.1483 357 PHE B CE1 6988 C CE2 . PHE B 357 ? 0.9968 0.8831 0.9359 -0.0652 -0.0847 -0.1497 357 PHE B CE2 6989 C CZ . PHE B 357 ? 0.9900 0.8558 0.9273 -0.0698 -0.0873 -0.1426 357 PHE B CZ 6990 N N . LEU B 358 ? 0.9396 0.7870 0.8871 -0.0344 -0.0859 -0.1761 358 LEU B N 6991 C CA . LEU B 358 ? 0.8824 0.7485 0.8378 -0.0260 -0.0830 -0.1688 358 LEU B CA 6992 C C . LEU B 358 ? 0.9916 0.8532 0.9487 -0.0278 -0.0855 -0.1546 358 LEU B C 6993 O O . LEU B 358 ? 1.1318 0.9701 1.0868 -0.0278 -0.0897 -0.1511 358 LEU B O 6994 C CB . LEU B 358 ? 0.7761 0.6373 0.7390 -0.0130 -0.0824 -0.1758 358 LEU B CB 6995 C CG . LEU B 358 ? 0.7925 0.6665 0.7541 -0.0090 -0.0780 -0.1895 358 LEU B CG 6996 C CD1 . LEU B 358 ? 0.9041 0.7737 0.8744 0.0045 -0.0770 -0.1962 358 LEU B CD1 6997 C CD2 . LEU B 358 ? 0.6476 0.5546 0.6089 -0.0113 -0.0723 -0.1861 358 LEU B CD2 6998 N N . ASN B 359 ? 0.9555 0.8393 0.9156 -0.0292 -0.0828 -0.1465 359 ASN B N 6999 C CA . ASN B 359 ? 0.8960 0.7790 0.8570 -0.0309 -0.0848 -0.1343 359 ASN B CA 7000 C C . ASN B 359 ? 0.8650 0.7676 0.8359 -0.0246 -0.0824 -0.1292 359 ASN B C 7001 O O . ASN B 359 ? 0.8145 0.7379 0.7867 -0.0275 -0.0788 -0.1262 359 ASN B O 7002 C CB . ASN B 359 ? 0.9262 0.8146 0.8800 -0.0423 -0.0843 -0.1294 359 ASN B CB 7003 C CG . ASN B 359 ? 0.9961 0.8865 0.9500 -0.0435 -0.0854 -0.1176 359 ASN B CG 7004 O OD1 . ASN B 359 ? 0.9180 0.8072 0.8771 -0.0361 -0.0868 -0.1133 359 ASN B OD1 7005 N ND2 . ASN B 359 ? 1.1244 1.0191 1.0729 -0.0528 -0.0847 -0.1130 359 ASN B ND2 7006 N N . PHE B 360 ? 0.8680 0.7638 0.8468 -0.0159 -0.0849 -0.1283 360 PHE B N 7007 C CA . PHE B 360 ? 0.8206 0.7329 0.8114 -0.0105 -0.0835 -0.1236 360 PHE B CA 7008 C C . PHE B 360 ? 0.8676 0.7726 0.8593 -0.0096 -0.0883 -0.1155 360 PHE B C 7009 O O . PHE B 360 ? 0.9023 0.8017 0.9016 -0.0023 -0.0922 -0.1153 360 PHE B O 7010 C CB . PHE B 360 ? 0.7688 0.6840 0.7708 -0.0010 -0.0826 -0.1298 360 PHE B CB 7011 C CG . PHE B 360 ? 0.8865 0.8101 0.8867 -0.0003 -0.0773 -0.1390 360 PHE B CG 7012 C CD1 . PHE B 360 ? 0.9022 0.8093 0.8979 0.0030 -0.0789 -0.1487 360 PHE B CD1 7013 C CD2 . PHE B 360 ? 0.9280 0.8756 0.9299 -0.0026 -0.0710 -0.1380 360 PHE B CD2 7014 C CE1 . PHE B 360 ? 0.9396 0.8547 0.9326 0.0042 -0.0742 -0.1589 360 PHE B CE1 7015 C CE2 . PHE B 360 ? 0.9562 0.9132 0.9543 -0.0013 -0.0662 -0.1469 360 PHE B CE2 7016 C CZ . PHE B 360 ? 0.9349 0.8759 0.9283 0.0021 -0.0678 -0.1582 360 PHE B CZ 7017 N N . THR B 361 ? 0.8517 0.7581 0.8357 -0.0166 -0.0883 -0.1094 361 THR B N 7018 C CA . THR B 361 ? 0.8637 0.7637 0.8456 -0.0159 -0.0924 -0.1024 361 THR B CA 7019 C C . THR B 361 ? 0.8124 0.7269 0.8061 -0.0120 -0.0924 -0.0989 361 THR B C 7020 O O . THR B 361 ? 0.7787 0.7107 0.7790 -0.0137 -0.0877 -0.0978 361 THR B O 7021 C CB . THR B 361 ? 0.8643 0.7628 0.8345 -0.0243 -0.0914 -0.0973 361 THR B CB 7022 O OG1 . THR B 361 ? 0.8970 0.7753 0.8567 -0.0273 -0.0938 -0.0976 361 THR B OG1 7023 C CG2 . THR B 361 ? 0.8105 0.7128 0.7808 -0.0229 -0.0933 -0.0906 361 THR B CG2 7024 N N . GLN B 362 ? 0.7416 0.6483 0.7380 -0.0067 -0.0980 -0.0971 362 GLN B N 7025 C CA . GLN B 362 ? 0.6798 0.5970 0.6869 -0.0041 -0.0994 -0.0942 362 GLN B CA 7026 C C . GLN B 362 ? 0.7374 0.6710 0.7616 -0.0020 -0.0956 -0.0959 362 GLN B C 7027 O O . GLN B 362 ? 0.6360 0.5832 0.6663 -0.0047 -0.0918 -0.0922 362 GLN B O 7028 C CB . GLN B 362 ? 0.7041 0.6268 0.7046 -0.0091 -0.0976 -0.0889 362 GLN B CB 7029 C CG . GLN B 362 ? 0.8990 0.8271 0.9085 -0.0058 -0.1006 -0.0868 362 GLN B CG 7030 C CD . GLN B 362 ? 1.0910 1.0226 1.0929 -0.0092 -0.0991 -0.0824 362 GLN B CD 7031 O OE1 . GLN B 362 ? 1.3089 1.2338 1.2963 -0.0122 -0.0989 -0.0805 362 GLN B OE1 7032 N NE2 . GLN B 362 ? 1.0258 0.9682 1.0383 -0.0087 -0.0977 -0.0805 362 GLN B NE2 7033 N N . ASN B 363 ? 0.7599 0.6925 0.7925 0.0032 -0.0964 -0.1007 363 ASN B N 7034 C CA . ASN B 363 ? 0.7342 0.6831 0.7851 0.0059 -0.0929 -0.1016 363 ASN B CA 7035 C C . ASN B 363 ? 0.7363 0.6822 0.8004 0.0126 -0.0995 -0.1038 363 ASN B C 7036 O O . ASN B 363 ? 0.8078 0.7436 0.8678 0.0142 -0.1067 -0.1027 363 ASN B O 7037 C CB . ASN B 363 ? 0.7829 0.7385 0.8340 0.0066 -0.0866 -0.1063 363 ASN B CB 7038 C CG . ASN B 363 ? 0.7801 0.7393 0.8175 -0.0001 -0.0814 -0.1055 363 ASN B CG 7039 O OD1 . ASN B 363 ? 0.9269 0.8776 0.9534 -0.0011 -0.0809 -0.1107 363 ASN B OD1 7040 N ND2 . ASN B 363 ? 0.5743 0.5456 0.6127 -0.0046 -0.0782 -0.0991 363 ASN B ND2 7041 N N . VAL B 364 ? 0.7194 0.6756 0.7992 0.0170 -0.0972 -0.1072 364 VAL B N 7042 C CA . VAL B 364 ? 0.5737 0.5295 0.6682 0.0239 -0.1039 -0.1102 364 VAL B CA 7043 C C . VAL B 364 ? 0.5921 0.5476 0.6908 0.0305 -0.1024 -0.1164 364 VAL B C 7044 O O . VAL B 364 ? 0.6790 0.6469 0.7973 0.0355 -0.1020 -0.1190 364 VAL B O 7045 C CB . VAL B 364 ? 0.5978 0.5705 0.7148 0.0227 -0.1032 -0.1075 364 VAL B CB 7046 C CG1 . VAL B 364 ? 0.6283 0.5984 0.7583 0.0284 -0.1133 -0.1105 364 VAL B CG1 7047 C CG2 . VAL B 364 ? 0.4705 0.4452 0.5831 0.0157 -0.1012 -0.1014 364 VAL B CG2 7048 N N . PHE B 365 ? 0.5513 0.4924 0.6324 0.0306 -0.1015 -0.1193 365 PHE B N 7049 C CA . PHE B 365 ? 0.6396 0.5763 0.7222 0.0376 -0.1004 -0.1264 365 PHE B CA 7050 C C . PHE B 365 ? 0.6822 0.6085 0.7716 0.0470 -0.1096 -0.1288 365 PHE B C 7051 O O . PHE B 365 ? 0.6289 0.5456 0.7142 0.0475 -0.1177 -0.1250 365 PHE B O 7052 C CB . PHE B 365 ? 0.6429 0.5636 0.7050 0.0342 -0.0983 -0.1292 365 PHE B CB 7053 C CG . PHE B 365 ? 0.8641 0.7976 0.9213 0.0280 -0.0891 -0.1304 365 PHE B CG 7054 C CD1 . PHE B 365 ? 0.8128 0.7679 0.8790 0.0239 -0.0835 -0.1256 365 PHE B CD1 7055 C CD2 . PHE B 365 ? 0.7849 0.7084 0.8282 0.0260 -0.0865 -0.1363 365 PHE B CD2 7056 C CE1 . PHE B 365 ? 0.7444 0.7121 0.8046 0.0190 -0.0756 -0.1259 365 PHE B CE1 7057 C CE2 . PHE B 365 ? 0.6005 0.5371 0.6380 0.0206 -0.0791 -0.1382 365 PHE B CE2 7058 C CZ . PHE B 365 ? 0.6696 0.6291 0.7149 0.0175 -0.0737 -0.1326 365 PHE B CZ 7059 N N . THR B 366 ? 0.7184 0.6472 0.8174 0.0553 -0.1083 -0.1353 366 THR B N 7060 C CA . THR B 366 ? 0.7071 0.6272 0.8135 0.0657 -0.1173 -0.1376 366 THR B CA 7061 C C . THR B 366 ? 0.8606 0.7609 0.9565 0.0721 -0.1181 -0.1430 366 THR B C 7062 O O . THR B 366 ? 0.9622 0.8567 1.0465 0.0681 -0.1116 -0.1464 366 THR B O 7063 C CB . THR B 366 ? 0.6631 0.6065 0.7971 0.0720 -0.1169 -0.1402 366 THR B CB 7064 O OG1 . THR B 366 ? 0.7226 0.6800 0.8650 0.0748 -0.1070 -0.1461 366 THR B OG1 7065 C CG2 . THR B 366 ? 0.4235 0.3836 0.5691 0.0647 -0.1167 -0.1347 366 THR B CG2 7066 N N . ASP B 367 ? 0.9539 0.8432 1.0541 0.0823 -0.1267 -0.1440 367 ASP B N 7067 C CA . ASP B 367 ? 1.0301 0.8973 1.1218 0.0899 -0.1288 -0.1485 367 ASP B CA 7068 C C . ASP B 367 ? 0.9613 0.8391 1.0646 0.0965 -0.1212 -0.1585 367 ASP B C 7069 O O . ASP B 367 ? 1.0691 0.9286 1.1658 0.1025 -0.1214 -0.1644 367 ASP B O 7070 C CB . ASP B 367 ? 1.1329 0.9866 1.2267 0.1004 -0.1408 -0.1456 367 ASP B CB 7071 C CG . ASP B 367 ? 1.1712 1.0483 1.2893 0.1075 -0.1453 -0.1465 367 ASP B CG 7072 O OD1 . ASP B 367 ? 1.1909 1.0675 1.3089 0.1083 -0.1546 -0.1411 367 ASP B OD1 7073 O OD2 . ASP B 367 ? 1.1118 1.0090 1.2494 0.1121 -0.1394 -0.1530 367 ASP B OD2 7074 N N . SER B 368 ? 0.8159 0.7228 0.9366 0.0955 -0.1143 -0.1605 368 SER B N 7075 C CA . SER B 368 ? 0.8666 0.7874 0.9971 0.1015 -0.1054 -0.1699 368 SER B CA 7076 C C . SER B 368 ? 0.8090 0.7288 0.9231 0.0929 -0.0961 -0.1733 368 SER B C 7077 O O . SER B 368 ? 0.7987 0.7258 0.9147 0.0976 -0.0887 -0.1825 368 SER B O 7078 C CB . SER B 368 ? 0.8474 0.8015 1.0043 0.1045 -0.1010 -0.1698 368 SER B CB 7079 O OG . SER B 368 ? 0.8485 0.8183 1.0069 0.0928 -0.0969 -0.1625 368 SER B OG 7080 N N . VAL B 369 ? 0.7389 0.6507 0.8369 0.0809 -0.0966 -0.1667 369 VAL B N 7081 C CA . VAL B 369 ? 0.8502 0.7609 0.9324 0.0724 -0.0895 -0.1697 369 VAL B CA 7082 C C . VAL B 369 ? 0.9307 0.8203 1.0027 0.0777 -0.0898 -0.1802 369 VAL B C 7083 O O . VAL B 369 ? 0.8444 0.7078 0.9108 0.0817 -0.0975 -0.1798 369 VAL B O 7084 C CB . VAL B 369 ? 0.8983 0.8003 0.9648 0.0597 -0.0918 -0.1610 369 VAL B CB 7085 C CG1 . VAL B 369 ? 0.9198 0.7900 0.9703 0.0584 -0.0990 -0.1600 369 VAL B CG1 7086 C CG2 . VAL B 369 ? 0.8339 0.7492 0.8912 0.0506 -0.0832 -0.1623 369 VAL B CG2 7087 N N . PHE B 370 ? 0.8691 0.7703 0.9388 0.0781 -0.0813 -0.1894 370 PHE B N 7088 C CA . PHE B 370 ? 0.9036 0.7866 0.9639 0.0827 -0.0806 -0.2019 370 PHE B CA 7089 C C . PHE B 370 ? 0.9199 0.7866 0.9898 0.0974 -0.0859 -0.2078 370 PHE B C 7090 O O . PHE B 370 ? 0.8413 0.6803 0.9017 0.1002 -0.0895 -0.2146 370 PHE B O 7091 C CB . PHE B 370 ? 0.8728 0.7311 0.9125 0.0715 -0.0840 -0.2010 370 PHE B CB 7092 C CG . PHE B 370 ? 0.8751 0.7490 0.9053 0.0583 -0.0794 -0.1963 370 PHE B CG 7093 C CD1 . PHE B 370 ? 0.9083 0.7680 0.9259 0.0467 -0.0836 -0.1886 370 PHE B CD1 7094 C CD2 . PHE B 370 ? 0.9549 0.8587 0.9891 0.0578 -0.0707 -0.1987 370 PHE B CD2 7095 C CE1 . PHE B 370 ? 0.9182 0.7933 0.9282 0.0355 -0.0797 -0.1841 370 PHE B CE1 7096 C CE2 . PHE B 370 ? 0.9394 0.8575 0.9646 0.0465 -0.0670 -0.1935 370 PHE B CE2 7097 C CZ . PHE B 370 ? 0.8906 0.7943 0.9042 0.0357 -0.0718 -0.1865 370 PHE B CZ 7098 N N . GLN B 371 ? 0.8371 0.7207 0.9268 0.1067 -0.0867 -0.2053 371 GLN B N 7099 C CA . GLN B 371 ? 0.9398 0.8109 1.0401 0.1219 -0.0919 -0.2109 371 GLN B CA 7100 C C . GLN B 371 ? 0.9544 0.8236 1.0537 0.1306 -0.0857 -0.2266 371 GLN B C 7101 O O . GLN B 371 ? 0.9332 0.8290 1.0374 0.1315 -0.0757 -0.2328 371 GLN B O 7102 C CB . GLN B 371 ? 1.1431 1.0372 1.2676 0.1304 -0.0939 -0.2062 371 GLN B CB 7103 C CG . GLN B 371 ? 1.3548 1.2357 1.4805 0.1299 -0.1057 -0.1949 371 GLN B CG 7104 C CD . GLN B 371 ? 1.4037 1.2455 1.5120 0.1314 -0.1142 -0.1936 371 GLN B CD 7105 O OE1 . GLN B 371 ? 1.3818 1.2068 1.4928 0.1436 -0.1174 -0.2002 371 GLN B OE1 7106 N NE2 . GLN B 371 ? 1.3097 1.1367 1.4007 0.1190 -0.1175 -0.1846 371 GLN B NE2 7107 N N . GLY B 372 ? 1.0604 0.8970 1.1524 0.1372 -0.0915 -0.2327 372 GLY B N 7108 C CA . GLY B 372 ? 1.0376 0.8666 1.1275 0.1463 -0.0870 -0.2494 372 GLY B CA 7109 C C . GLY B 372 ? 1.1091 0.9513 1.1863 0.1373 -0.0777 -0.2578 372 GLY B C 7110 O O . GLY B 372 ? 1.1262 0.9850 1.2073 0.1454 -0.0697 -0.2707 372 GLY B O 7111 N N . CYS B 373 ? 1.2334 1.0699 1.2951 0.1210 -0.0787 -0.2507 373 CYS B N 7112 C CA . CYS B 373 ? 1.2784 1.1279 1.3268 0.1117 -0.0713 -0.2576 373 CYS B CA 7113 C C . CYS B 373 ? 1.2696 1.0884 1.3026 0.1096 -0.0742 -0.2704 373 CYS B C 7114 O O . CYS B 373 ? 1.2610 1.0506 1.2847 0.1012 -0.0815 -0.2651 373 CYS B O 7115 C CB . CYS B 373 ? 1.2783 1.1406 1.3197 0.0959 -0.0708 -0.2438 373 CYS B CB 7116 S SG . CYS B 373 ? 1.3705 1.2518 1.3957 0.0847 -0.0628 -0.2503 373 CYS B SG 7117 N N . SER B 374 ? 1.2683 1.0943 1.2993 0.1172 -0.0681 -0.2877 374 SER B N 7118 C CA . SER B 374 ? 1.3597 1.1557 1.3790 0.1180 -0.0711 -0.3035 374 SER B CA 7119 C C . SER B 374 ? 1.2733 1.0792 1.2757 0.1058 -0.0671 -0.3117 374 SER B C 7120 O O . SER B 374 ? 1.2778 1.0729 1.2715 0.1084 -0.0663 -0.3298 374 SER B O 7121 C CB . SER B 374 ? 1.4439 1.2381 1.4725 0.1371 -0.0682 -0.3199 374 SER B CB 7122 O OG . SER B 374 ? 1.4872 1.3223 1.5252 0.1451 -0.0581 -0.3225 374 SER B OG 7123 N N . THR B 375 ? 1.1964 1.0224 1.1942 0.0928 -0.0654 -0.2987 375 THR B N 7124 C CA . THR B 375 ? 1.0246 0.8715 1.0088 0.0838 -0.0602 -0.3046 375 THR B CA 7125 C C . THR B 375 ? 1.1221 0.9625 1.0969 0.0657 -0.0651 -0.2922 375 THR B C 7126 O O . THR B 375 ? 0.9886 0.8508 0.9543 0.0563 -0.0618 -0.2903 375 THR B O 7127 C CB . THR B 375 ? 0.8448 0.7345 0.8360 0.0900 -0.0500 -0.3014 375 THR B CB 7128 O OG1 . THR B 375 ? 0.9185 0.8257 0.8985 0.0928 -0.0433 -0.3173 375 THR B OG1 7129 C CG2 . THR B 375 ? 0.5678 0.4782 0.5609 0.0791 -0.0487 -0.2818 375 THR B CG2 7130 N N . LEU B 376 ? 1.2045 1.0151 1.1816 0.0616 -0.0729 -0.2832 376 LEU B N 7131 C CA . LEU B 376 ? 1.1447 0.9448 1.1136 0.0452 -0.0777 -0.2723 376 LEU B CA 7132 C C . LEU B 376 ? 1.1636 0.9228 1.1273 0.0409 -0.0851 -0.2782 376 LEU B C 7133 O O . LEU B 376 ? 1.1688 0.9080 1.1317 0.0330 -0.0905 -0.2658 376 LEU B O 7134 C CB . LEU B 376 ? 1.1033 0.9100 1.0799 0.0430 -0.0793 -0.2519 376 LEU B CB 7135 C CG . LEU B 376 ? 1.0848 0.9295 1.0676 0.0440 -0.0728 -0.2432 376 LEU B CG 7136 C CD1 . LEU B 376 ? 0.9958 0.8413 0.9889 0.0451 -0.0758 -0.2266 376 LEU B CD1 7137 C CD2 . LEU B 376 ? 1.0709 0.9363 1.0430 0.0316 -0.0695 -0.2411 376 LEU B CD2 7138 N N . LYS B 377 ? 1.1702 0.9167 1.1303 0.0461 -0.0850 -0.2975 377 LYS B N 7139 C CA . LYS B 377 ? 1.0972 0.8024 1.0543 0.0431 -0.0918 -0.3047 377 LYS B CA 7140 C C . LYS B 377 ? 1.1146 0.8108 1.0615 0.0237 -0.0953 -0.3042 377 LYS B C 7141 O O . LYS B 377 ? 1.0590 0.7207 1.0042 0.0176 -0.1010 -0.3077 377 LYS B O 7142 C CB . LYS B 377 ? 1.0095 0.7029 0.9670 0.0557 -0.0908 -0.3272 377 LYS B CB 7143 C CG . LYS B 377 ? 1.0674 0.7572 1.0376 0.0755 -0.0896 -0.3281 377 LYS B CG 7144 C CD . LYS B 377 ? 1.2358 0.9169 1.2055 0.0883 -0.0877 -0.3522 377 LYS B CD 7145 C CE . LYS B 377 ? 1.2920 0.9751 1.2759 0.1093 -0.0856 -0.3543 377 LYS B CE 7146 N NZ . LYS B 377 ? 1.4244 1.0686 1.4156 0.1144 -0.0936 -0.3464 377 LYS B NZ 7147 N N . ARG B 378 ? 1.1961 0.9235 1.1373 0.0141 -0.0920 -0.2996 378 ARG B N 7148 C CA . ARG B 378 ? 1.1696 0.8928 1.1032 -0.0044 -0.0955 -0.2977 378 ARG B CA 7149 C C . ARG B 378 ? 1.0814 0.8071 1.0174 -0.0133 -0.0967 -0.2749 378 ARG B C 7150 O O . ARG B 378 ? 1.1352 0.8485 1.0681 -0.0279 -0.1004 -0.2695 378 ARG B O 7151 C CB . ARG B 378 ? 0.9309 0.6852 0.8554 -0.0100 -0.0924 -0.3087 378 ARG B CB 7152 C CG . ARG B 378 ? 0.9728 0.7170 0.8910 -0.0072 -0.0938 -0.3337 378 ARG B CG 7153 C CD . ARG B 378 ? 1.3240 1.1047 1.2319 -0.0093 -0.0901 -0.3439 378 ARG B CD 7154 N NE . ARG B 378 ? 1.5283 1.2999 1.4277 -0.0097 -0.0929 -0.3690 378 ARG B NE 7155 C CZ . ARG B 378 ? 1.5547 1.3543 1.4426 -0.0119 -0.0914 -0.3813 378 ARG B CZ 7156 N NH1 . ARG B 378 ? 1.4785 1.3164 1.3622 -0.0139 -0.0867 -0.3694 378 ARG B NH1 7157 N NH2 . ARG B 378 ? 1.5131 1.3018 1.3932 -0.0119 -0.0950 -0.4056 378 ARG B NH2 7158 N N . LEU B 379 ? 0.8943 0.6361 0.8367 -0.0044 -0.0936 -0.2623 379 LEU B N 7159 C CA . LEU B 379 ? 0.9806 0.7273 0.9252 -0.0103 -0.0945 -0.2417 379 LEU B CA 7160 C C . LEU B 379 ? 1.0136 0.7266 0.9575 -0.0170 -0.1002 -0.2323 379 LEU B C 7161 O O . LEU B 379 ? 1.1214 0.8082 1.0691 -0.0082 -0.1033 -0.2323 379 LEU B O 7162 C CB . LEU B 379 ? 0.9046 0.6674 0.8582 0.0025 -0.0917 -0.2329 379 LEU B CB 7163 C CG . LEU B 379 ? 0.8538 0.6236 0.8095 -0.0017 -0.0927 -0.2136 379 LEU B CG 7164 C CD1 . LEU B 379 ? 0.8821 0.6723 0.8318 -0.0151 -0.0907 -0.2082 379 LEU B CD1 7165 C CD2 . LEU B 379 ? 0.8971 0.6861 0.8632 0.0103 -0.0901 -0.2081 379 LEU B CD2 7166 N N . GLN B 380 ? 0.8969 0.6120 0.8362 -0.0321 -0.1012 -0.2233 380 GLN B N 7167 C CA . GLN B 380 ? 0.8946 0.5798 0.8323 -0.0408 -0.1054 -0.2138 380 GLN B CA 7168 C C . GLN B 380 ? 1.0121 0.7022 0.9503 -0.0409 -0.1054 -0.1938 380 GLN B C 7169 O O . GLN B 380 ? 1.0792 0.7443 1.0171 -0.0388 -0.1087 -0.1842 380 GLN B O 7170 C CB . GLN B 380 ? 0.8618 0.5459 0.7953 -0.0586 -0.1064 -0.2172 380 GLN B CB 7171 C CG . GLN B 380 ? 1.1609 0.8398 1.0928 -0.0606 -0.1076 -0.2381 380 GLN B CG 7172 C CD . GLN B 380 ? 1.1973 0.8641 1.1276 -0.0788 -0.1107 -0.2410 380 GLN B CD 7173 O OE1 . GLN B 380 ? 1.0735 0.7386 1.0043 -0.0901 -0.1110 -0.2261 380 GLN B OE1 7174 N NE2 . GLN B 380 ? 1.1333 0.7922 1.0623 -0.0819 -0.1131 -0.2607 380 GLN B NE2 7175 N N . THR B 381 ? 0.9648 0.6869 0.9029 -0.0432 -0.1019 -0.1875 381 THR B N 7176 C CA . THR B 381 ? 0.9202 0.6492 0.8582 -0.0436 -0.1019 -0.1704 381 THR B CA 7177 C C . THR B 381 ? 0.9512 0.7074 0.8946 -0.0333 -0.0991 -0.1685 381 THR B C 7178 O O . THR B 381 ? 1.1107 0.8931 1.0552 -0.0347 -0.0952 -0.1732 381 THR B O 7179 C CB . THR B 381 ? 0.9447 0.6846 0.8784 -0.0589 -0.1006 -0.1625 381 THR B CB 7180 O OG1 . THR B 381 ? 0.9121 0.6278 0.8429 -0.0701 -0.1029 -0.1648 381 THR B OG1 7181 C CG2 . THR B 381 ? 0.9135 0.6590 0.8460 -0.0582 -0.1004 -0.1457 381 THR B CG2 7182 N N . LEU B 382 ? 0.9400 0.6899 0.8874 -0.0230 -0.1012 -0.1613 382 LEU B N 7183 C CA . LEU B 382 ? 0.9918 0.7659 0.9467 -0.0142 -0.0992 -0.1585 382 LEU B CA 7184 C C . LEU B 382 ? 0.9720 0.7483 0.9258 -0.0149 -0.1013 -0.1438 382 LEU B C 7185 O O . LEU B 382 ? 0.9169 0.6715 0.8663 -0.0143 -0.1056 -0.1367 382 LEU B O 7186 C CB . LEU B 382 ? 1.0381 0.8071 1.0016 0.0004 -0.1003 -0.1660 382 LEU B CB 7187 C CG . LEU B 382 ? 1.0157 0.8052 0.9900 0.0102 -0.0995 -0.1615 382 LEU B CG 7188 C CD1 . LEU B 382 ? 0.9367 0.7572 0.9160 0.0097 -0.0929 -0.1663 382 LEU B CD1 7189 C CD2 . LEU B 382 ? 1.1047 0.8815 1.0872 0.0242 -0.1029 -0.1658 382 LEU B CD2 7190 N N . ILE B 383 ? 1.0203 0.8225 0.9776 -0.0160 -0.0984 -0.1392 383 ILE B N 7191 C CA . ILE B 383 ? 0.9129 0.7195 0.8688 -0.0170 -0.1002 -0.1270 383 ILE B CA 7192 C C . ILE B 383 ? 0.9438 0.7690 0.9105 -0.0082 -0.1000 -0.1255 383 ILE B C 7193 O O . ILE B 383 ? 0.9425 0.7902 0.9154 -0.0087 -0.0955 -0.1280 383 ILE B O 7194 C CB . ILE B 383 ? 0.8006 0.6192 0.7502 -0.0290 -0.0971 -0.1216 383 ILE B CB 7195 C CG1 . ILE B 383 ? 0.8377 0.6401 0.7793 -0.0393 -0.0972 -0.1239 383 ILE B CG1 7196 C CG2 . ILE B 383 ? 0.8144 0.6355 0.7611 -0.0291 -0.0988 -0.1101 383 ILE B CG2 7197 C CD1 . ILE B 383 ? 0.8793 0.6927 0.8160 -0.0510 -0.0948 -0.1176 383 ILE B CD1 7198 N N . LEU B 384 ? 0.9371 0.7531 0.9063 -0.0004 -0.1052 -0.1209 384 LEU B N 7199 C CA . LEU B 384 ? 0.8529 0.6847 0.8346 0.0077 -0.1064 -0.1200 384 LEU B CA 7200 C C . LEU B 384 ? 0.9126 0.7450 0.8912 0.0077 -0.1106 -0.1107 384 LEU B C 7201 O O . LEU B 384 ? 0.9592 0.7981 0.9471 0.0150 -0.1144 -0.1097 384 LEU B O 7202 C CB . LEU B 384 ? 0.7262 0.5504 0.7171 0.0193 -0.1096 -0.1261 384 LEU B CB 7203 C CG . LEU B 384 ? 0.7831 0.6130 0.7786 0.0205 -0.1041 -0.1368 384 LEU B CG 7204 C CD1 . LEU B 384 ? 0.8308 0.6446 0.8305 0.0309 -0.1072 -0.1437 384 LEU B CD1 7205 C CD2 . LEU B 384 ? 0.8052 0.6643 0.8131 0.0218 -0.0984 -0.1389 384 LEU B CD2 7206 N N . GLN B 385 ? 0.7817 0.6086 0.7476 -0.0006 -0.1098 -0.1046 385 GLN B N 7207 C CA . GLN B 385 ? 0.7678 0.5954 0.7280 -0.0007 -0.1130 -0.0965 385 GLN B CA 7208 C C . GLN B 385 ? 0.7768 0.6255 0.7474 0.0014 -0.1125 -0.0960 385 GLN B C 7209 O O . GLN B 385 ? 0.9278 0.7932 0.9047 -0.0027 -0.1072 -0.0977 385 GLN B O 7210 C CB . GLN B 385 ? 0.7410 0.5644 0.6877 -0.0109 -0.1100 -0.0906 385 GLN B CB 7211 C CG . GLN B 385 ? 0.7986 0.6331 0.7415 -0.0125 -0.1098 -0.0843 385 GLN B CG 7212 C CD . GLN B 385 ? 0.9730 0.8012 0.9021 -0.0209 -0.1074 -0.0774 385 GLN B CD 7213 O OE1 . GLN B 385 ? 1.0673 0.9038 0.9914 -0.0221 -0.1066 -0.0723 385 GLN B OE1 7214 N NE2 . GLN B 385 ? 0.8006 0.6141 0.7243 -0.0267 -0.1060 -0.0775 385 GLN B NE2 7215 N N . ARG B 386 ? 0.8437 0.6908 0.8160 0.0079 -0.1186 -0.0936 386 ARG B N 7216 C CA . ARG B 386 ? 0.9315 0.7951 0.9141 0.0098 -0.1196 -0.0934 386 ARG B CA 7217 C C . ARG B 386 ? 0.9216 0.7988 0.9240 0.0142 -0.1187 -0.0989 386 ARG B C 7218 O O . ARG B 386 ? 0.8691 0.7627 0.8815 0.0113 -0.1144 -0.0989 386 ARG B O 7219 C CB . ARG B 386 ? 0.8831 0.7578 0.8612 0.0022 -0.1143 -0.0898 386 ARG B CB 7220 C CG . ARG B 386 ? 0.8573 0.7296 0.8256 0.0027 -0.1178 -0.0852 386 ARG B CG 7221 C CD . ARG B 386 ? 0.9250 0.8057 0.8866 -0.0047 -0.1118 -0.0815 386 ARG B CD 7222 N NE . ARG B 386 ? 1.2167 1.0902 1.1676 -0.0117 -0.1077 -0.0792 386 ARG B NE 7223 C CZ . ARG B 386 ? 1.4240 1.3075 1.3739 -0.0194 -0.1016 -0.0780 386 ARG B CZ 7224 N NH1 . ARG B 386 ? 1.3700 1.2705 1.3279 -0.0201 -0.0986 -0.0779 386 ARG B NH1 7225 N NH2 . ARG B 386 ? 1.5023 1.3786 1.4439 -0.0264 -0.0989 -0.0768 386 ARG B NH2 7226 N N . ASN B 387 ? 0.9241 0.7946 0.9328 0.0215 -0.1226 -0.1027 387 ASN B N 7227 C CA . ASN B 387 ? 0.8865 0.7711 0.9157 0.0266 -0.1220 -0.1076 387 ASN B CA 7228 C C . ASN B 387 ? 0.8750 0.7569 0.9135 0.0360 -0.1312 -0.1092 387 ASN B C 7229 O O . ASN B 387 ? 0.9888 0.8615 1.0179 0.0382 -0.1384 -0.1061 387 ASN B O 7230 C CB . ASN B 387 ? 0.9082 0.7934 0.9398 0.0270 -0.1159 -0.1128 387 ASN B CB 7231 C CG . ASN B 387 ? 0.9551 0.8494 0.9812 0.0181 -0.1074 -0.1123 387 ASN B CG 7232 O OD1 . ASN B 387 ? 0.9819 0.8656 0.9932 0.0126 -0.1056 -0.1117 387 ASN B OD1 7233 N ND2 . ASN B 387 ? 0.8606 0.7753 0.8994 0.0165 -0.1023 -0.1120 387 ASN B ND2 7234 N N . GLY B 388 ? 0.7489 0.6405 0.8056 0.0420 -0.1310 -0.1142 388 GLY B N 7235 C CA . GLY B 388 ? 0.6056 0.4987 0.6746 0.0510 -0.1400 -0.1163 388 GLY B CA 7236 C C . GLY B 388 ? 0.6933 0.5756 0.7634 0.0604 -0.1434 -0.1197 388 GLY B C 7237 O O . GLY B 388 ? 0.8579 0.7496 0.9461 0.0683 -0.1476 -0.1235 388 GLY B O 7238 N N . LEU B 389 ? 0.7158 0.5784 0.7682 0.0597 -0.1418 -0.1187 389 LEU B N 7239 C CA . LEU B 389 ? 0.8507 0.6999 0.9039 0.0691 -0.1449 -0.1221 389 LEU B CA 7240 C C . LEU B 389 ? 0.9249 0.7658 0.9784 0.0789 -0.1569 -0.1195 389 LEU B C 7241 O O . LEU B 389 ? 1.0064 0.8332 1.0424 0.0776 -0.1622 -0.1130 389 LEU B O 7242 C CB . LEU B 389 ? 0.8632 0.6900 0.8972 0.0650 -0.1413 -0.1211 389 LEU B CB 7243 C CG . LEU B 389 ? 0.8418 0.6741 0.8726 0.0559 -0.1308 -0.1248 389 LEU B CG 7244 C CD1 . LEU B 389 ? 0.8309 0.6399 0.8492 0.0553 -0.1294 -0.1273 389 LEU B CD1 7245 C CD2 . LEU B 389 ? 0.8562 0.7118 0.9065 0.0588 -0.1251 -0.1315 389 LEU B CD2 7246 N N . LYS B 390 ? 0.9683 0.8192 1.0412 0.0892 -0.1611 -0.1243 390 LYS B N 7247 C CA . LYS B 390 ? 0.9642 0.8116 1.0398 0.0993 -0.1737 -0.1222 390 LYS B CA 7248 C C . LYS B 390 ? 0.8824 0.7056 0.9474 0.1091 -0.1790 -0.1203 390 LYS B C 7249 O O . LYS B 390 ? 0.9237 0.7290 0.9701 0.1106 -0.1859 -0.1130 390 LYS B O 7250 C CB . LYS B 390 ? 0.9288 0.8012 1.0333 0.1057 -0.1770 -0.1280 390 LYS B CB 7251 C CG . LYS B 390 ? 0.8271 0.7107 0.9379 0.1065 -0.1873 -0.1266 390 LYS B CG 7252 C CD . LYS B 390 ? 0.8479 0.7486 0.9664 0.0949 -0.1815 -0.1270 390 LYS B CD 7253 C CE . LYS B 390 ? 1.0050 0.9238 1.1432 0.0969 -0.1908 -0.1298 390 LYS B CE 7254 N NZ . LYS B 390 ? 0.9949 0.9030 1.1197 0.1038 -0.2050 -0.1277 390 LYS B NZ 7255 N N . ASN B 391 ? 0.6596 0.4821 0.7363 0.1160 -0.1755 -0.1266 391 ASN B N 7256 C CA . ASN B 391 ? 0.6704 0.4726 0.7439 0.1284 -0.1817 -0.1261 391 ASN B CA 7257 C C . ASN B 391 ? 0.9101 0.6821 0.9637 0.1253 -0.1775 -0.1239 391 ASN B C 7258 O O . ASN B 391 ? 1.0403 0.8089 1.0985 0.1257 -0.1701 -0.1312 391 ASN B O 7259 C CB . ASN B 391 ? 0.7049 0.5231 0.8043 0.1401 -0.1814 -0.1350 391 ASN B CB 7260 C CG . ASN B 391 ? 0.8749 0.6732 0.9739 0.1552 -0.1888 -0.1349 391 ASN B CG 7261 O OD1 . ASN B 391 ? 0.8661 0.6764 0.9860 0.1670 -0.1902 -0.1416 391 ASN B OD1 7262 N ND2 . ASN B 391 ? 1.1116 0.8800 1.1876 0.1551 -0.1934 -0.1267 391 ASN B ND2 7263 N N . PHE B 392 ? 1.0383 0.7885 1.0702 0.1227 -0.1824 -0.1139 392 PHE B N 7264 C CA . PHE B 392 ? 1.0700 0.7896 1.0836 0.1187 -0.1794 -0.1100 392 PHE B CA 7265 C C . PHE B 392 ? 1.0681 0.7726 1.0893 0.1272 -0.1774 -0.1176 392 PHE B C 7266 O O . PHE B 392 ? 1.0935 0.7795 1.1055 0.1205 -0.1713 -0.1195 392 PHE B O 7267 C CB . PHE B 392 ? 0.9485 0.6467 0.9421 0.1208 -0.1876 -0.0969 392 PHE B CB 7268 C CG . PHE B 392 ? 0.9913 0.6558 0.9685 0.1176 -0.1855 -0.0912 392 PHE B CG 7269 C CD1 . PHE B 392 ? 1.0310 0.6866 0.9920 0.1023 -0.1786 -0.0861 392 PHE B CD1 7270 C CD2 . PHE B 392 ? 1.0552 0.6966 1.0343 0.1299 -0.1906 -0.0906 392 PHE B CD2 7271 C CE1 . PHE B 392 ? 1.1459 0.7703 1.0938 0.0980 -0.1767 -0.0806 392 PHE B CE1 7272 C CE2 . PHE B 392 ? 1.1209 0.7288 1.0861 0.1263 -0.1889 -0.0850 392 PHE B CE2 7273 C CZ . PHE B 392 ? 1.1560 0.7555 1.1059 0.1097 -0.1819 -0.0799 392 PHE B CZ 7274 N N . PHE B 393 ? 1.0868 0.7991 1.1257 0.1422 -0.1827 -0.1226 393 PHE B N 7275 C CA . PHE B 393 ? 1.2774 0.9746 1.3237 0.1524 -0.1812 -0.1304 393 PHE B CA 7276 C C . PHE B 393 ? 1.1863 0.9038 1.2476 0.1502 -0.1706 -0.1442 393 PHE B C 7277 O O . PHE B 393 ? 1.1106 0.8139 1.1725 0.1534 -0.1660 -0.1525 393 PHE B O 7278 C CB . PHE B 393 ? 1.4429 1.1374 1.5008 0.1713 -0.1920 -0.1291 393 PHE B CB 7279 C CG . PHE B 393 ? 1.4388 1.1087 1.4791 0.1753 -0.2024 -0.1151 393 PHE B CG 7280 C CD1 . PHE B 393 ? 1.3335 1.0170 1.3761 0.1822 -0.2130 -0.1085 393 PHE B CD1 7281 C CD2 . PHE B 393 ? 1.4786 1.1122 1.4997 0.1718 -0.2017 -0.1083 393 PHE B CD2 7282 C CE1 . PHE B 393 ? 1.3650 1.0274 1.3892 0.1866 -0.2224 -0.0951 393 PHE B CE1 7283 C CE2 . PHE B 393 ? 1.4713 1.0829 1.4753 0.1755 -0.2104 -0.0937 393 PHE B CE2 7284 C CZ . PHE B 393 ? 1.4060 1.0325 1.4105 0.1833 -0.2206 -0.0869 393 PHE B CZ 7285 N N . LYS B 394 ? 1.0776 0.8277 1.1506 0.1447 -0.1667 -0.1464 394 LYS B N 7286 C CA . LYS B 394 ? 1.0163 0.7875 1.1001 0.1404 -0.1555 -0.1570 394 LYS B CA 7287 C C . LYS B 394 ? 0.9270 0.6859 0.9918 0.1253 -0.1478 -0.1572 394 LYS B C 7288 O O . LYS B 394 ? 1.0070 0.7652 1.0720 0.1240 -0.1401 -0.1669 394 LYS B O 7289 C CB . LYS B 394 ? 0.9076 0.7154 1.0091 0.1378 -0.1534 -0.1573 394 LYS B CB 7290 C CG . LYS B 394 ? 0.9401 0.7736 1.0642 0.1447 -0.1459 -0.1680 394 LYS B CG 7291 C CD . LYS B 394 ? 0.9818 0.8501 1.1218 0.1380 -0.1414 -0.1668 394 LYS B CD 7292 C CE . LYS B 394 ? 1.0561 0.9514 1.2169 0.1430 -0.1315 -0.1762 394 LYS B CE 7293 N NZ . LYS B 394 ? 1.0721 0.9810 1.2574 0.1585 -0.1363 -0.1803 394 LYS B NZ 7294 N N . VAL B 395 ? 0.8430 0.5927 0.8914 0.1146 -0.1503 -0.1468 395 VAL B N 7295 C CA . VAL B 395 ? 0.9425 0.6806 0.9733 0.0998 -0.1443 -0.1453 395 VAL B CA 7296 C C . VAL B 395 ? 0.9929 0.6983 1.0131 0.1006 -0.1443 -0.1486 395 VAL B C 7297 O O . VAL B 395 ? 1.0472 0.7443 1.0569 0.0892 -0.1387 -0.1512 395 VAL B O 7298 C CB . VAL B 395 ? 0.8859 0.6214 0.9022 0.0898 -0.1475 -0.1326 395 VAL B CB 7299 C CG1 . VAL B 395 ? 0.7322 0.4593 0.7328 0.0743 -0.1411 -0.1310 395 VAL B CG1 7300 C CG2 . VAL B 395 ? 0.8168 0.5817 0.8437 0.0889 -0.1482 -0.1304 395 VAL B CG2 7301 N N . ALA B 396 ? 1.0316 0.7180 1.0555 0.1141 -0.1510 -0.1485 396 ALA B N 7302 C CA . ALA B 396 ? 1.0670 0.7199 1.0831 0.1159 -0.1515 -0.1520 396 ALA B CA 7303 C C . ALA B 396 ? 1.1563 0.8159 1.1848 0.1233 -0.1458 -0.1686 396 ALA B C 7304 O O . ALA B 396 ? 1.2836 0.9264 1.3056 0.1184 -0.1417 -0.1768 396 ALA B O 7305 C CB . ALA B 396 ? 1.0787 0.7056 1.0921 0.1279 -0.1615 -0.1431 396 ALA B CB 7306 N N . LEU B 397 ? 1.1156 0.8012 1.1625 0.1349 -0.1455 -0.1739 397 LEU B N 7307 C CA . LEU B 397 ? 1.1252 0.8215 1.1852 0.1442 -0.1395 -0.1895 397 LEU B CA 7308 C C . LEU B 397 ? 1.1065 0.8219 1.1627 0.1320 -0.1289 -0.1977 397 LEU B C 7309 O O . LEU B 397 ? 1.1567 0.8749 1.2162 0.1362 -0.1228 -0.2117 397 LEU B O 7310 C CB . LEU B 397 ? 1.1145 0.8381 1.1970 0.1586 -0.1414 -0.1914 397 LEU B CB 7311 C CG . LEU B 397 ? 1.0935 0.8299 1.1921 0.1718 -0.1355 -0.2069 397 LEU B CG 7312 C CD1 . LEU B 397 ? 1.0813 0.7847 1.1794 0.1858 -0.1407 -0.2125 397 LEU B CD1 7313 C CD2 . LEU B 397 ? 0.9160 0.6899 1.0387 0.1807 -0.1348 -0.2073 397 LEU B CD2 7314 N N . MET B 398 ? 0.9949 0.7239 1.0435 0.1178 -0.1269 -0.1890 398 MET B N 7315 C CA . MET B 398 ? 0.9992 0.7473 1.0430 0.1057 -0.1178 -0.1940 398 MET B CA 7316 C C . MET B 398 ? 1.0914 0.8170 1.1205 0.0979 -0.1152 -0.2019 398 MET B C 7317 O O . MET B 398 ? 1.1428 0.8812 1.1711 0.0954 -0.1080 -0.2133 398 MET B O 7318 C CB . MET B 398 ? 1.0345 0.7968 1.0727 0.0929 -0.1179 -0.1817 398 MET B CB 7319 C CG . MET B 398 ? 0.9715 0.7490 1.0017 0.0794 -0.1098 -0.1844 398 MET B CG 7320 S SD . MET B 398 ? 1.1723 0.9682 1.1995 0.0675 -0.1100 -0.1703 398 MET B SD 7321 C CE . MET B 398 ? 0.5660 0.3312 0.5726 0.0560 -0.1145 -0.1622 398 MET B CE 7322 N N . THR B 399 ? 1.1434 0.8359 1.1609 0.0937 -0.1213 -0.1956 399 THR B N 7323 C CA . THR B 399 ? 1.1576 0.8270 1.1622 0.0837 -0.1198 -0.2017 399 THR B CA 7324 C C . THR B 399 ? 1.0550 0.7005 1.0627 0.0946 -0.1209 -0.2156 399 THR B C 7325 O O . THR B 399 ? 0.9281 0.5511 0.9269 0.0874 -0.1206 -0.2228 399 THR B O 7326 C CB . THR B 399 ? 1.2764 0.9213 1.2678 0.0723 -0.1248 -0.1875 399 THR B CB 7327 O OG1 . THR B 399 ? 1.2731 0.8909 1.2654 0.0826 -0.1324 -0.1803 399 THR B OG1 7328 C CG2 . THR B 399 ? 1.3132 0.9812 1.3015 0.0632 -0.1239 -0.1748 399 THR B CG2 7329 N N . LYS B 400 ? 1.0557 0.7063 1.0771 0.1121 -0.1224 -0.2197 400 LYS B N 7330 C CA . LYS B 400 ? 1.1343 0.7616 1.1605 0.1255 -0.1240 -0.2326 400 LYS B CA 7331 C C . LYS B 400 ? 1.1668 0.7871 1.1858 0.1198 -0.1186 -0.2500 400 LYS B C 7332 O O . LYS B 400 ? 1.1806 0.7658 1.1944 0.1202 -0.1219 -0.2565 400 LYS B O 7333 C CB . LYS B 400 ? 1.1798 0.8280 1.2246 0.1446 -0.1233 -0.2380 400 LYS B CB 7334 C CG . LYS B 400 ? 1.2380 0.8634 1.2895 0.1612 -0.1251 -0.2514 400 LYS B CG 7335 C CD . LYS B 400 ? 1.3188 0.9638 1.3907 0.1811 -0.1261 -0.2533 400 LYS B CD 7336 C CE . LYS B 400 ? 1.3641 1.0509 1.4471 0.1850 -0.1158 -0.2650 400 LYS B CE 7337 N NZ . LYS B 400 ? 1.3711 1.0689 1.4743 0.2068 -0.1154 -0.2736 400 LYS B NZ 7338 N N . ASN B 401 ? 1.1989 0.8522 1.2175 0.1144 -0.1106 -0.2575 401 ASN B N 7339 C CA . ASN B 401 ? 1.2407 0.8923 1.2516 0.1099 -0.1058 -0.2752 401 ASN B CA 7340 C C . ASN B 401 ? 1.1514 0.8155 1.1494 0.0900 -0.1027 -0.2724 401 ASN B C 7341 O O . ASN B 401 ? 1.1186 0.8072 1.1130 0.0868 -0.0963 -0.2828 401 ASN B O 7342 C CB . ASN B 401 ? 1.2898 0.9668 1.3106 0.1247 -0.0988 -0.2908 401 ASN B CB 7343 C CG . ASN B 401 ? 1.5676 1.2186 1.5954 0.1420 -0.1017 -0.3035 401 ASN B CG 7344 O OD1 . ASN B 401 ? 1.6464 1.2627 1.6663 0.1396 -0.1054 -0.3125 401 ASN B OD1 7345 N ND2 . ASN B 401 ? 1.7776 1.4448 1.8217 0.1595 -0.1004 -0.3044 401 ASN B ND2 7346 N N . MET B 402 ? 1.0830 0.7307 1.0740 0.0774 -0.1076 -0.2576 402 MET B N 7347 C CA . MET B 402 ? 0.9951 0.6536 0.9755 0.0588 -0.1057 -0.2524 402 MET B CA 7348 C C . MET B 402 ? 0.9996 0.6232 0.9710 0.0478 -0.1100 -0.2561 402 MET B C 7349 O O . MET B 402 ? 1.0433 0.6558 1.0087 0.0348 -0.1128 -0.2432 402 MET B O 7350 C CB . MET B 402 ? 0.8782 0.5487 0.8589 0.0529 -0.1073 -0.2320 402 MET B CB 7351 C CG . MET B 402 ? 0.8381 0.5441 0.8289 0.0610 -0.1033 -0.2280 402 MET B CG 7352 S SD . MET B 402 ? 1.0603 0.7869 1.0482 0.0489 -0.1031 -0.2090 402 MET B SD 7353 C CE . MET B 402 ? 0.6691 0.4384 0.6704 0.0569 -0.0966 -0.2098 402 MET B CE 7354 N N . SER B 403 ? 0.9788 0.5860 0.9501 0.0534 -0.1100 -0.2746 403 SER B N 7355 C CA . SER B 403 ? 1.0168 0.5849 0.9828 0.0456 -0.1148 -0.2813 403 SER B CA 7356 C C . SER B 403 ? 1.1639 0.7249 1.1213 0.0237 -0.1165 -0.2739 403 SER B C 7357 O O . SER B 403 ? 1.3207 0.8473 1.2759 0.0161 -0.1207 -0.2770 403 SER B O 7358 C CB . SER B 403 ? 1.0766 0.6404 1.0425 0.0528 -0.1130 -0.3063 403 SER B CB 7359 O OG . SER B 403 ? 1.2423 0.8269 1.2163 0.0717 -0.1088 -0.3132 403 SER B OG 7360 N N . SER B 404 ? 1.1295 0.7220 1.0833 0.0136 -0.1132 -0.2641 404 SER B N 7361 C CA . SER B 404 ? 1.0930 0.6823 1.0401 -0.0066 -0.1144 -0.2574 404 SER B CA 7362 C C . SER B 404 ? 1.1642 0.7610 1.1103 -0.0129 -0.1146 -0.2343 404 SER B C 7363 O O . SER B 404 ? 1.2534 0.8501 1.1950 -0.0291 -0.1150 -0.2265 404 SER B O 7364 C CB . SER B 404 ? 1.0649 0.6846 1.0071 -0.0155 -0.1108 -0.2691 404 SER B CB 7365 O OG . SER B 404 ? 1.0413 0.6520 0.9819 -0.0120 -0.1113 -0.2916 404 SER B OG 7366 N N . LEU B 405 ? 1.0975 0.7021 1.0481 -0.0002 -0.1145 -0.2242 405 LEU B N 7367 C CA . LEU B 405 ? 0.9190 0.5330 0.8679 -0.0042 -0.1149 -0.2040 405 LEU B CA 7368 C C . LEU B 405 ? 1.0490 0.6315 0.9928 -0.0137 -0.1188 -0.1914 405 LEU B C 7369 O O . LEU B 405 ? 1.1759 0.7254 1.1208 -0.0075 -0.1229 -0.1911 405 LEU B O 7370 C CB . LEU B 405 ? 0.7324 0.3558 0.6880 0.0121 -0.1158 -0.1975 405 LEU B CB 7371 C CG . LEU B 405 ? 0.8856 0.5326 0.8401 0.0086 -0.1147 -0.1818 405 LEU B CG 7372 C CD1 . LEU B 405 ? 1.0285 0.7095 0.9823 0.0006 -0.1090 -0.1860 405 LEU B CD1 7373 C CD2 . LEU B 405 ? 0.9042 0.5597 0.8665 0.0238 -0.1169 -0.1758 405 LEU B CD2 7374 N N . GLU B 406 ? 1.0292 0.6224 0.9678 -0.0284 -0.1172 -0.1806 406 GLU B N 7375 C CA . GLU B 406 ? 1.0975 0.6662 1.0310 -0.0382 -0.1194 -0.1657 406 GLU B CA 7376 C C . GLU B 406 ? 1.0170 0.6029 0.9465 -0.0385 -0.1185 -0.1476 406 GLU B C 7377 O O . GLU B 406 ? 1.2176 0.7845 1.1426 -0.0378 -0.1209 -0.1332 406 GLU B O 7378 C CB . GLU B 406 ? 1.2197 0.7837 1.1513 -0.0575 -0.1182 -0.1695 406 GLU B CB 7379 C CG . GLU B 406 ? 1.3736 0.9163 1.3084 -0.0593 -0.1202 -0.1882 406 GLU B CG 7380 C CD . GLU B 406 ? 1.4594 0.9879 1.3938 -0.0793 -0.1209 -0.1885 406 GLU B CD 7381 O OE1 . GLU B 406 ? 1.3423 0.8505 1.2795 -0.0828 -0.1234 -0.2042 406 GLU B OE1 7382 O OE2 . GLU B 406 ? 1.5743 1.1122 1.5063 -0.0914 -0.1189 -0.1736 406 GLU B OE2 7383 N N . THR B 407 ? 0.8382 0.4596 0.7689 -0.0390 -0.1149 -0.1484 407 THR B N 7384 C CA . THR B 407 ? 0.9858 0.6246 0.9132 -0.0391 -0.1140 -0.1335 407 THR B CA 7385 C C . THR B 407 ? 1.0685 0.7307 1.0015 -0.0255 -0.1138 -0.1353 407 THR B C 7386 O O . THR B 407 ? 1.1004 0.7855 1.0387 -0.0239 -0.1107 -0.1453 407 THR B O 7387 C CB . THR B 407 ? 1.0277 0.6892 0.9523 -0.0538 -0.1098 -0.1298 407 THR B CB 7388 O OG1 . THR B 407 ? 0.9703 0.6126 0.8910 -0.0680 -0.1097 -0.1251 407 THR B OG1 7389 C CG2 . THR B 407 ? 1.0075 0.6892 0.9294 -0.0511 -0.1087 -0.1169 407 THR B CG2 7390 N N . LEU B 408 ? 1.0584 0.7154 0.9904 -0.0161 -0.1174 -0.1250 408 LEU B N 7391 C CA . LEU B 408 ? 1.0014 0.6801 0.9406 -0.0043 -0.1181 -0.1257 408 LEU B CA 7392 C C . LEU B 408 ? 0.9585 0.6467 0.8922 -0.0055 -0.1193 -0.1118 408 LEU B C 7393 O O . LEU B 408 ? 1.0519 0.7216 0.9785 -0.0029 -0.1234 -0.1016 408 LEU B O 7394 C CB . LEU B 408 ? 1.0462 0.7096 0.9918 0.0114 -0.1228 -0.1299 408 LEU B CB 7395 C CG . LEU B 408 ? 0.9659 0.6517 0.9238 0.0246 -0.1234 -0.1346 408 LEU B CG 7396 C CD1 . LEU B 408 ? 0.9621 0.6412 0.9213 0.0360 -0.1303 -0.1256 408 LEU B CD1 7397 C CD2 . LEU B 408 ? 0.7976 0.5169 0.7595 0.0193 -0.1183 -0.1355 408 LEU B CD2 7398 N N . ASP B 409 ? 0.8722 0.5886 0.8085 -0.0091 -0.1158 -0.1114 409 ASP B N 7399 C CA . ASP B 409 ? 0.8521 0.5797 0.7846 -0.0083 -0.1171 -0.1007 409 ASP B CA 7400 C C . ASP B 409 ? 0.9611 0.7070 0.9043 0.0029 -0.1193 -0.1035 409 ASP B C 7401 O O . ASP B 409 ? 1.0420 0.8114 0.9929 0.0015 -0.1154 -0.1079 409 ASP B O 7402 C CB . ASP B 409 ? 0.7693 0.5142 0.6973 -0.0205 -0.1121 -0.0967 409 ASP B CB 7403 C CG . ASP B 409 ? 0.9948 0.7518 0.9189 -0.0184 -0.1133 -0.0873 409 ASP B CG 7404 O OD1 . ASP B 409 ? 1.0513 0.7988 0.9727 -0.0095 -0.1187 -0.0825 409 ASP B OD1 7405 O OD2 . ASP B 409 ? 1.0380 0.8141 0.9617 -0.0250 -0.1093 -0.0853 409 ASP B OD2 7406 N N . VAL B 410 ? 0.9717 0.7070 0.9159 0.0139 -0.1257 -0.1003 410 VAL B N 7407 C CA . VAL B 410 ? 1.0356 0.7886 0.9912 0.0236 -0.1288 -0.1021 410 VAL B CA 7408 C C . VAL B 410 ? 1.0731 0.8290 1.0215 0.0251 -0.1334 -0.0925 410 VAL B C 7409 O O . VAL B 410 ? 1.0899 0.8481 1.0435 0.0352 -0.1399 -0.0919 410 VAL B O 7410 C CB . VAL B 410 ? 0.9938 0.7382 0.9593 0.0367 -0.1335 -0.1077 410 VAL B CB 7411 C CG1 . VAL B 410 ? 0.8873 0.6424 0.8647 0.0378 -0.1280 -0.1195 410 VAL B CG1 7412 C CG2 . VAL B 410 ? 1.0501 0.7632 1.0052 0.0396 -0.1379 -0.1031 410 VAL B CG2 7413 N N . SER B 411 ? 1.0638 0.8207 1.0003 0.0152 -0.1301 -0.0859 411 SER B N 7414 C CA . SER B 411 ? 1.0957 0.8555 1.0227 0.0164 -0.1336 -0.0774 411 SER B CA 7415 C C . SER B 411 ? 1.1360 0.9202 1.0728 0.0186 -0.1340 -0.0805 411 SER B C 7416 O O . SER B 411 ? 1.3374 1.1371 1.2881 0.0177 -0.1304 -0.0874 411 SER B O 7417 C CB . SER B 411 ? 1.0660 0.8203 0.9779 0.0055 -0.1291 -0.0693 411 SER B CB 7418 O OG . SER B 411 ? 1.0990 0.8742 1.0139 -0.0021 -0.1232 -0.0709 411 SER B OG 7419 N N . LEU B 412 ? 0.9477 0.7348 0.8768 0.0214 -0.1382 -0.0753 412 LEU B N 7420 C CA . LEU B 412 ? 0.9508 0.7578 0.8888 0.0234 -0.1396 -0.0784 412 LEU B CA 7421 C C . LEU B 412 ? 1.0008 0.8201 0.9601 0.0294 -0.1418 -0.0865 412 LEU B C 7422 O O . LEU B 412 ? 1.0876 0.9246 1.0587 0.0276 -0.1396 -0.0897 412 LEU B O 7423 C CB . LEU B 412 ? 0.9817 0.8018 0.9172 0.0138 -0.1321 -0.0771 412 LEU B CB 7424 C CG . LEU B 412 ? 1.0085 0.8259 0.9265 0.0121 -0.1327 -0.0698 412 LEU B CG 7425 C CD1 . LEU B 412 ? 0.9146 0.7387 0.8265 0.0016 -0.1242 -0.0664 412 LEU B CD1 7426 C CD2 . LEU B 412 ? 0.8801 0.7075 0.8003 0.0189 -0.1387 -0.0719 412 LEU B CD2 7427 N N . ASN B 413 ? 0.9166 0.7264 0.8815 0.0369 -0.1459 -0.0891 413 ASN B N 7428 C CA . ASN B 413 ? 0.9489 0.7711 0.9345 0.0443 -0.1492 -0.0959 413 ASN B CA 7429 C C . ASN B 413 ? 1.0200 0.8418 1.0075 0.0541 -0.1603 -0.0952 413 ASN B C 7430 O O . ASN B 413 ? 1.1007 0.9198 1.0749 0.0540 -0.1646 -0.0906 413 ASN B O 7431 C CB . ASN B 413 ? 0.9154 0.7319 0.9093 0.0477 -0.1465 -0.1010 413 ASN B CB 7432 C CG . ASN B 413 ? 0.9781 0.8039 0.9763 0.0395 -0.1363 -0.1050 413 ASN B CG 7433 O OD1 . ASN B 413 ? 1.1086 0.9265 1.0940 0.0312 -0.1314 -0.1026 413 ASN B OD1 7434 N ND2 . ASN B 413 ? 0.8725 0.7165 0.8892 0.0417 -0.1331 -0.1109 413 ASN B ND2 7435 N N . SER B 414 ? 0.9318 0.7576 0.9356 0.0630 -0.1652 -0.1001 414 SER B N 7436 C CA . SER B 414 ? 0.9340 0.7615 0.9420 0.0731 -0.1769 -0.1004 414 SER B CA 7437 C C . SER B 414 ? 0.9197 0.7338 0.9288 0.0837 -0.1825 -0.1002 414 SER B C 7438 O O . SER B 414 ? 0.9231 0.7460 0.9483 0.0932 -0.1901 -0.1043 414 SER B O 7439 C CB . SER B 414 ? 1.0462 0.8971 1.0790 0.0744 -0.1791 -0.1071 414 SER B CB 7440 O OG . SER B 414 ? 1.2533 1.1159 1.2884 0.0648 -0.1726 -0.1075 414 SER B OG 7441 N N . LEU B 415 ? 0.8232 0.6158 0.8164 0.0822 -0.1791 -0.0955 415 LEU B N 7442 C CA . LEU B 415 ? 0.9011 0.6769 0.8948 0.0922 -0.1835 -0.0951 415 LEU B CA 7443 C C . LEU B 415 ? 1.1102 0.8769 1.0960 0.1037 -0.1963 -0.0893 415 LEU B C 7444 O O . LEU B 415 ? 0.9725 0.7386 0.9431 0.1026 -0.2010 -0.0833 415 LEU B O 7445 C CB . LEU B 415 ? 0.8737 0.6266 0.8526 0.0861 -0.1765 -0.0914 415 LEU B CB 7446 C CG . LEU B 415 ? 0.8532 0.6108 0.8399 0.0782 -0.1657 -0.0986 415 LEU B CG 7447 C CD1 . LEU B 415 ? 0.7746 0.5082 0.7443 0.0706 -0.1608 -0.0944 415 LEU B CD1 7448 C CD2 . LEU B 415 ? 0.9172 0.6820 0.9245 0.0878 -0.1658 -0.1080 415 LEU B CD2 7449 N N . ASN B 416 ? 1.0247 0.7848 1.0203 0.1157 -0.2018 -0.0913 416 ASN B N 7450 C CA . ASN B 416 ? 0.9943 0.7440 0.9820 0.1280 -0.2141 -0.0851 416 ASN B CA 7451 C C . ASN B 416 ? 1.1523 0.8886 1.1491 0.1404 -0.2175 -0.0865 416 ASN B C 7452 O O . ASN B 416 ? 1.1820 0.9298 1.2009 0.1439 -0.2140 -0.0961 416 ASN B O 7453 C CB . ASN B 416 ? 1.0382 0.8109 1.0361 0.1333 -0.2241 -0.0883 416 ASN B CB 7454 C CG . ASN B 416 ? 0.9821 0.7777 1.0115 0.1385 -0.2252 -0.0991 416 ASN B CG 7455 O OD1 . ASN B 416 ? 1.1112 0.9265 1.1553 0.1303 -0.2189 -0.1055 416 ASN B OD1 7456 N ND2 . ASN B 416 ? 0.8554 0.6493 0.8962 0.1525 -0.2332 -0.1004 416 ASN B ND2 7457 N N . SER B 417 ? 1.2691 0.9812 1.2487 0.1477 -0.2240 -0.0766 417 SER B N 7458 C CA . SER B 417 ? 1.3024 0.9955 1.2875 0.1593 -0.2267 -0.0764 417 SER B CA 7459 C C . SER B 417 ? 1.3007 1.0029 1.2987 0.1770 -0.2401 -0.0773 417 SER B C 7460 O O . SER B 417 ? 1.2307 0.9132 1.2263 0.1893 -0.2461 -0.0725 417 SER B O 7461 C CB . SER B 417 ? 1.2841 0.9421 1.2445 0.1567 -0.2253 -0.0641 417 SER B CB 7462 O OG . SER B 417 ? 1.1998 0.8545 1.1374 0.1534 -0.2295 -0.0522 417 SER B OG 7463 N N . HIS B 418 ? 1.3346 1.0669 1.3478 0.1782 -0.2451 -0.0835 418 HIS B N 7464 C CA . HIS B 418 ? 1.3571 1.1029 1.3858 0.1941 -0.2586 -0.0856 418 HIS B CA 7465 C C . HIS B 418 ? 1.4484 1.2096 1.5087 0.2020 -0.2562 -0.0971 418 HIS B C 7466 O O . HIS B 418 ? 1.4311 1.2098 1.5104 0.2142 -0.2663 -0.1008 418 HIS B O 7467 C CB . HIS B 418 ? 1.2928 1.0634 1.3236 0.1921 -0.2670 -0.0872 418 HIS B CB 7468 C CG . HIS B 418 ? 1.3715 1.1292 1.3718 0.1917 -0.2741 -0.0759 418 HIS B CG 7469 N ND1 . HIS B 418 ? 1.4222 1.1864 1.4081 0.1793 -0.2706 -0.0748 418 HIS B ND1 7470 C CD2 . HIS B 418 ? 1.3020 1.0411 1.2829 0.2027 -0.2839 -0.0646 418 HIS B CD2 7471 C CE1 . HIS B 418 ? 1.3622 1.1138 1.3207 0.1827 -0.2776 -0.0641 418 HIS B CE1 7472 N NE2 . HIS B 418 ? 1.3242 1.0603 1.2787 0.1966 -0.2857 -0.0570 418 HIS B NE2 7473 N N . ALA B 419 ? 1.5057 1.2619 1.5716 0.1952 -0.2430 -0.1030 419 ALA B N 7474 C CA . ALA B 419 ? 1.4365 1.2085 1.5307 0.2022 -0.2385 -0.1144 419 ALA B CA 7475 C C . ALA B 419 ? 1.5451 1.3123 1.6508 0.2222 -0.2491 -0.1143 419 ALA B C 7476 O O . ALA B 419 ? 1.6068 1.3444 1.6956 0.2300 -0.2542 -0.1061 419 ALA B O 7477 C CB . ALA B 419 ? 1.4114 1.1702 1.5022 0.1946 -0.2242 -0.1194 419 ALA B CB 7478 N N . TYR B 420 ? 1.6050 1.4024 1.7406 0.2305 -0.2524 -0.1228 420 TYR B N 7479 C CA . TYR B 420 ? 1.6706 1.4701 1.8241 0.2505 -0.2609 -0.1252 420 TYR B CA 7480 C C . TYR B 420 ? 1.5771 1.3484 1.7261 0.2581 -0.2544 -0.1271 420 TYR B C 7481 O O . TYR B 420 ? 1.3868 1.1342 1.5280 0.2718 -0.2627 -0.1209 420 TYR B O 7482 C CB . TYR B 420 ? 1.8156 1.6559 2.0057 0.2541 -0.2600 -0.1363 420 TYR B CB 7483 C CG . TYR B 420 ? 1.9517 1.8113 2.1505 0.2374 -0.2451 -0.1433 420 TYR B CG 7484 C CD1 . TYR B 420 ? 1.9748 1.8283 2.1750 0.2344 -0.2305 -0.1498 420 TYR B CD1 7485 C CD2 . TYR B 420 ? 1.9283 1.8113 2.1330 0.2252 -0.2460 -0.1434 420 TYR B CD2 7486 C CE1 . TYR B 420 ? 1.9374 1.8090 2.1438 0.2200 -0.2172 -0.1550 420 TYR B CE1 7487 C CE2 . TYR B 420 ? 1.9280 1.8272 2.1403 0.2106 -0.2325 -0.1482 420 TYR B CE2 7488 C CZ . TYR B 420 ? 1.9266 1.8207 2.1392 0.2082 -0.2182 -0.1534 420 TYR B CZ 7489 O OH . TYR B 420 ? 1.8321 1.7432 2.0508 0.1944 -0.2051 -0.1570 420 TYR B OH 7490 N N . ASP B 421 ? 1.6737 1.4480 1.8277 0.2491 -0.2396 -0.1359 421 ASP B N 7491 C CA . ASP B 421 ? 1.6881 1.4373 1.8381 0.2537 -0.2318 -0.1408 421 ASP B CA 7492 C C . ASP B 421 ? 1.8086 1.5244 1.9275 0.2395 -0.2265 -0.1336 421 ASP B C 7493 O O . ASP B 421 ? 1.8971 1.6196 2.0098 0.2232 -0.2159 -0.1367 421 ASP B O 7494 C CB . ASP B 421 ? 1.5595 1.3335 1.7309 0.2515 -0.2186 -0.1552 421 ASP B CB 7495 C CG . ASP B 421 ? 1.5298 1.2825 1.7019 0.2604 -0.2119 -0.1637 421 ASP B CG 7496 O OD1 . ASP B 421 ? 1.5050 1.2202 1.6545 0.2573 -0.2115 -0.1594 421 ASP B OD1 7497 O OD2 . ASP B 421 ? 1.5132 1.2872 1.7091 0.2703 -0.2067 -0.1753 421 ASP B OD2 7498 N N . ARG B 422 ? 1.7879 1.4690 1.8883 0.2456 -0.2339 -0.1232 422 ARG B N 7499 C CA . ARG B 422 ? 1.7008 1.3507 1.7725 0.2317 -0.2298 -0.1142 422 ARG B CA 7500 C C . ARG B 422 ? 1.7192 1.3376 1.7857 0.2316 -0.2224 -0.1194 422 ARG B C 7501 O O . ARG B 422 ? 1.7291 1.3118 1.7762 0.2297 -0.2246 -0.1095 422 ARG B O 7502 C CB . ARG B 422 ? 1.6169 1.2475 1.6678 0.2351 -0.2415 -0.0972 422 ARG B CB 7503 C CG . ARG B 422 ? 1.5120 1.1713 1.5634 0.2335 -0.2495 -0.0926 422 ARG B CG 7504 C CD . ARG B 422 ? 1.5234 1.1638 1.5477 0.2330 -0.2583 -0.0757 422 ARG B CD 7505 N NE . ARG B 422 ? 1.6492 1.3170 1.6753 0.2351 -0.2681 -0.0735 422 ARG B NE 7506 C CZ . ARG B 422 ? 1.8131 1.4732 1.8169 0.2363 -0.2772 -0.0605 422 ARG B CZ 7507 N NH1 . ARG B 422 ? 1.9755 1.6016 1.9538 0.2352 -0.2768 -0.0467 422 ARG B NH1 7508 N NH2 . ARG B 422 ? 1.7373 1.4239 1.7440 0.2385 -0.2866 -0.0612 422 ARG B NH2 7509 N N . THR B 423 ? 1.7398 1.3718 1.8234 0.2331 -0.2134 -0.1350 423 THR B N 7510 C CA . THR B 423 ? 1.7547 1.3591 1.8353 0.2340 -0.2065 -0.1434 423 THR B CA 7511 C C . THR B 423 ? 1.6677 1.2600 1.7304 0.2131 -0.1966 -0.1442 423 THR B C 7512 O O . THR B 423 ? 1.4564 1.0751 1.5199 0.1998 -0.1893 -0.1479 423 THR B O 7513 C CB . THR B 423 ? 1.3356 0.9592 1.4408 0.2463 -0.2009 -0.1610 423 THR B CB 7514 O OG1 . THR B 423 ? 1.3582 0.9898 1.4811 0.2672 -0.2106 -0.1602 423 THR B OG1 7515 C CG2 . THR B 423 ? 1.2885 0.8820 1.3883 0.2470 -0.1943 -0.1713 423 THR B CG2 7516 N N . CYS B 424 ? 1.6809 1.2329 1.7287 0.2105 -0.1969 -0.1405 424 CYS B N 7517 C CA . CYS B 424 ? 1.4530 0.9893 1.4837 0.1908 -0.1892 -0.1399 424 CYS B CA 7518 C C . CYS B 424 ? 1.3344 0.8665 1.3717 0.1894 -0.1805 -0.1579 424 CYS B C 7519 O O . CYS B 424 ? 1.2085 0.7262 1.2559 0.2045 -0.1821 -0.1669 424 CYS B O 7520 C CB . CYS B 424 ? 1.3183 0.8126 1.3297 0.1871 -0.1944 -0.1248 424 CYS B CB 7521 S SG . CYS B 424 ? 2.2725 1.7619 2.2615 0.1610 -0.1885 -0.1141 424 CYS B SG 7522 N N . ALA B 425 ? 1.4206 0.9659 1.4516 0.1721 -0.1715 -0.1634 425 ALA B N 7523 C CA . ALA B 425 ? 1.4342 0.9785 1.4680 0.1681 -0.1629 -0.1809 425 ALA B CA 7524 C C . ALA B 425 ? 1.5226 1.0680 1.5419 0.1459 -0.1562 -0.1804 425 ALA B C 7525 O O . ALA B 425 ? 1.4897 1.0573 1.5120 0.1397 -0.1482 -0.1926 425 ALA B O 7526 C CB . ALA B 425 ? 1.2430 0.8248 1.2955 0.1776 -0.1574 -0.1949 425 ALA B CB 7527 N N . TRP B 426 ? 1.5749 1.0979 1.5787 0.1345 -0.1594 -0.1658 426 TRP B N 7528 C CA . TRP B 426 ? 1.4410 0.9671 1.4321 0.1133 -0.1538 -0.1635 426 TRP B CA 7529 C C . TRP B 426 ? 1.4424 0.9541 1.4316 0.1058 -0.1484 -0.1787 426 TRP B C 7530 O O . TRP B 426 ? 1.5518 1.0372 1.5450 0.1150 -0.1504 -0.1877 426 TRP B O 7531 C CB . TRP B 426 ? 1.3226 0.8271 1.2983 0.1034 -0.1578 -0.1443 426 TRP B CB 7532 C CG . TRP B 426 ? 1.1891 0.7178 1.1609 0.1017 -0.1601 -0.1308 426 TRP B CG 7533 C CD1 . TRP B 426 ? 1.0636 0.5857 1.0317 0.1107 -0.1680 -0.1167 426 TRP B CD1 7534 C CD2 . TRP B 426 ? 1.2451 0.8077 1.2160 0.0907 -0.1548 -0.1307 426 TRP B CD2 7535 N NE1 . TRP B 426 ? 1.0692 0.6188 1.0341 0.1059 -0.1681 -0.1093 426 TRP B NE1 7536 C CE2 . TRP B 426 ? 1.1762 0.7501 1.1434 0.0937 -0.1600 -0.1174 426 TRP B CE2 7537 C CE3 . TRP B 426 ? 1.2984 0.8827 1.2711 0.0793 -0.1467 -0.1405 426 TRP B CE3 7538 C CZ2 . TRP B 426 ? 1.1781 0.7823 1.1442 0.0856 -0.1570 -0.1144 426 TRP B CZ2 7539 C CZ3 . TRP B 426 ? 1.2417 0.8563 1.2135 0.0716 -0.1437 -0.1359 426 TRP B CZ3 7540 C CH2 . TRP B 426 ? 1.1836 0.8070 1.1526 0.0747 -0.1488 -0.1234 426 TRP B CH2 7541 N N . ALA B 427 ? 1.3540 0.8832 1.3373 0.0895 -0.1421 -0.1820 427 ALA B N 7542 C CA . ALA B 427 ? 1.3579 0.8739 1.3372 0.0795 -0.1382 -0.1954 427 ALA B CA 7543 C C . ALA B 427 ? 1.3061 0.7811 1.2759 0.0702 -0.1422 -0.1862 427 ALA B C 7544 O O . ALA B 427 ? 1.1621 0.6347 1.1230 0.0590 -0.1431 -0.1698 427 ALA B O 7545 C CB . ALA B 427 ? 1.4006 0.9478 1.3757 0.0646 -0.1314 -0.1992 427 ALA B CB 7546 N N . GLU B 428 ? 1.4388 0.8815 1.4110 0.0750 -0.1442 -0.1969 428 GLU B N 7547 C CA . GLU B 428 ? 1.5784 0.9773 1.5442 0.0681 -0.1484 -0.1880 428 GLU B CA 7548 C C . GLU B 428 ? 1.4230 0.8203 1.3797 0.0443 -0.1452 -0.1834 428 GLU B C 7549 O O . GLU B 428 ? 1.5237 0.8881 1.4754 0.0346 -0.1475 -0.1741 428 GLU B O 7550 C CB . GLU B 428 ? 1.8710 1.2370 1.8433 0.0780 -0.1507 -0.2043 428 GLU B CB 7551 C CG . GLU B 428 ? 2.1021 1.4751 2.0859 0.1026 -0.1527 -0.2130 428 GLU B CG 7552 C CD . GLU B 428 ? 2.1914 1.6104 2.1821 0.1078 -0.1465 -0.2275 428 GLU B CD 7553 O OE1 . GLU B 428 ? 2.1729 1.6151 2.1722 0.1225 -0.1472 -0.2244 428 GLU B OE1 7554 O OE2 . GLU B 428 ? 2.2004 1.6329 2.1880 0.0971 -0.1410 -0.2414 428 GLU B OE2 7555 N N . SER B 429 ? 1.3006 0.7347 1.2561 0.0348 -0.1398 -0.1890 429 SER B N 7556 C CA . SER B 429 ? 1.2993 0.7363 1.2487 0.0133 -0.1366 -0.1894 429 SER B CA 7557 C C . SER B 429 ? 1.2469 0.7066 1.1893 0.0014 -0.1343 -0.1714 429 SER B C 7558 O O . SER B 429 ? 1.3283 0.7903 1.2665 -0.0166 -0.1318 -0.1690 429 SER B O 7559 C CB . SER B 429 ? 1.3082 0.7675 1.2603 0.0101 -0.1324 -0.2113 429 SER B CB 7560 O OG . SER B 429 ? 1.2043 0.7030 1.1599 0.0199 -0.1288 -0.2150 429 SER B OG 7561 N N . ILE B 430 ? 1.0532 0.5304 0.9954 0.0117 -0.1352 -0.1598 430 ILE B N 7562 C CA . ILE B 430 ? 1.0801 0.5798 1.0156 0.0024 -0.1331 -0.1443 430 ILE B CA 7563 C C . ILE B 430 ? 1.1982 0.6732 1.1249 -0.0104 -0.1340 -0.1278 430 ILE B C 7564 O O . ILE B 430 ? 1.2789 0.7210 1.2033 -0.0050 -0.1383 -0.1194 430 ILE B O 7565 C CB . ILE B 430 ? 1.0984 0.6167 1.0352 0.0165 -0.1355 -0.1352 430 ILE B CB 7566 C CG1 . ILE B 430 ? 1.1368 0.6706 1.0851 0.0327 -0.1357 -0.1495 430 ILE B CG1 7567 C CG2 . ILE B 430 ? 1.1070 0.6562 1.0389 0.0075 -0.1321 -0.1259 430 ILE B CG2 7568 C CD1 . ILE B 430 ? 1.1339 0.6941 1.0867 0.0278 -0.1297 -0.1655 430 ILE B CD1 7569 N N . LEU B 431 ? 1.1632 0.6545 1.0853 -0.0271 -0.1298 -0.1225 431 LEU B N 7570 C CA . LEU B 431 ? 1.2571 0.7296 1.1716 -0.0404 -0.1292 -0.1060 431 LEU B CA 7571 C C . LEU B 431 ? 1.3076 0.8045 1.2144 -0.0426 -0.1270 -0.0901 431 LEU B C 7572 O O . LEU B 431 ? 1.5362 1.0186 1.4344 -0.0446 -0.1277 -0.0726 431 LEU B O 7573 C CB . LEU B 431 ? 1.3018 0.7698 1.2187 -0.0601 -0.1260 -0.1128 431 LEU B CB 7574 C CG . LEU B 431 ? 1.3286 0.7761 1.2529 -0.0614 -0.1278 -0.1323 431 LEU B CG 7575 C CD1 . LEU B 431 ? 1.2203 0.6648 1.1467 -0.0831 -0.1256 -0.1359 431 LEU B CD1 7576 C CD2 . LEU B 431 ? 1.3709 0.7762 1.2966 -0.0504 -0.1329 -0.1307 431 LEU B CD2 7577 N N . VAL B 432 ? 1.1876 0.7211 1.0968 -0.0419 -0.1241 -0.0961 432 VAL B N 7578 C CA . VAL B 432 ? 1.1203 0.6781 1.0231 -0.0427 -0.1222 -0.0835 432 VAL B CA 7579 C C . VAL B 432 ? 1.0186 0.5981 0.9252 -0.0270 -0.1245 -0.0874 432 VAL B C 7580 O O . VAL B 432 ? 1.1293 0.7271 1.0445 -0.0231 -0.1232 -0.1011 432 VAL B O 7581 C CB . VAL B 432 ? 1.0836 0.6669 0.9867 -0.0583 -0.1164 -0.0848 432 VAL B CB 7582 C CG1 . VAL B 432 ? 0.9926 0.5964 0.8882 -0.0592 -0.1143 -0.0709 432 VAL B CG1 7583 C CG2 . VAL B 432 ? 0.9557 0.5197 0.8591 -0.0749 -0.1145 -0.0844 432 VAL B CG2 7584 N N . LEU B 433 ? 0.9948 0.5729 0.8952 -0.0182 -0.1280 -0.0752 433 LEU B N 7585 C CA . LEU B 433 ? 1.1294 0.7250 1.0351 -0.0032 -0.1316 -0.0785 433 LEU B CA 7586 C C . LEU B 433 ? 1.2340 0.8470 1.1316 -0.0022 -0.1323 -0.0667 433 LEU B C 7587 O O . LEU B 433 ? 1.2477 0.8467 1.1354 0.0028 -0.1364 -0.0543 433 LEU B O 7588 C CB . LEU B 433 ? 1.1654 0.7373 1.0740 0.0120 -0.1383 -0.0791 433 LEU B CB 7589 C CG . LEU B 433 ? 1.0794 0.6682 0.9961 0.0283 -0.1431 -0.0827 433 LEU B CG 7590 C CD1 . LEU B 433 ? 1.0689 0.6861 0.9982 0.0280 -0.1387 -0.0972 433 LEU B CD1 7591 C CD2 . LEU B 433 ? 1.0517 0.6166 0.9727 0.0433 -0.1497 -0.0838 433 LEU B CD2 7592 N N . ASN B 434 ? 1.1813 0.8245 1.0824 -0.0066 -0.1283 -0.0706 434 ASN B N 7593 C CA . ASN B 434 ? 1.1609 0.8218 1.0558 -0.0046 -0.1292 -0.0621 434 ASN B CA 7594 C C . ASN B 434 ? 1.2803 0.9515 1.1823 0.0105 -0.1353 -0.0656 434 ASN B C 7595 O O . ASN B 434 ? 1.2995 0.9888 1.2146 0.0140 -0.1343 -0.0762 434 ASN B O 7596 C CB . ASN B 434 ? 1.0767 0.7635 0.9724 -0.0155 -0.1227 -0.0636 434 ASN B CB 7597 C CG . ASN B 434 ? 1.3727 1.0714 1.2585 -0.0154 -0.1228 -0.0533 434 ASN B CG 7598 O OD1 . ASN B 434 ? 1.3157 1.0241 1.2025 -0.0053 -0.1273 -0.0533 434 ASN B OD1 7599 N ND2 . ASN B 434 ? 1.6868 1.3847 1.5631 -0.0266 -0.1179 -0.0449 434 ASN B ND2 7600 N N . LEU B 435 ? 1.2098 0.8698 1.1032 0.0192 -0.1417 -0.0564 435 LEU B N 7601 C CA . LEU B 435 ? 1.0049 0.6745 0.9049 0.0335 -0.1491 -0.0588 435 LEU B CA 7602 C C . LEU B 435 ? 1.0035 0.6880 0.8941 0.0342 -0.1513 -0.0518 435 LEU B C 7603 O O . LEU B 435 ? 1.1039 0.7951 0.9966 0.0452 -0.1588 -0.0519 435 LEU B O 7604 C CB . LEU B 435 ? 1.0310 0.6762 0.9288 0.0453 -0.1567 -0.0547 435 LEU B CB 7605 C CG . LEU B 435 ? 1.1882 0.8180 1.0973 0.0490 -0.1561 -0.0639 435 LEU B CG 7606 C CD1 . LEU B 435 ? 1.2202 0.8186 1.1228 0.0578 -0.1624 -0.0561 435 LEU B CD1 7607 C CD2 . LEU B 435 ? 1.2609 0.9119 1.1892 0.0579 -0.1573 -0.0770 435 LEU B CD2 7608 N N . SER B 436 ? 0.9418 0.6326 0.8229 0.0225 -0.1449 -0.0467 436 SER B N 7609 C CA . SER B 436 ? 0.9832 0.6845 0.8515 0.0227 -0.1459 -0.0391 436 SER B CA 7610 C C . SER B 436 ? 1.0225 0.7497 0.9009 0.0271 -0.1481 -0.0470 436 SER B C 7611 O O . SER B 436 ? 1.1851 0.9272 1.0778 0.0233 -0.1440 -0.0558 436 SER B O 7612 C CB . SER B 436 ? 1.0333 0.7358 0.8908 0.0090 -0.1375 -0.0320 436 SER B CB 7613 O OG . SER B 436 ? 1.0049 0.7309 0.8704 0.0022 -0.1318 -0.0386 436 SER B OG 7614 N N . SER B 437 ? 1.0750 0.8069 0.9454 0.0352 -0.1548 -0.0435 437 SER B N 7615 C CA . SER B 437 ? 1.1361 0.8904 1.0148 0.0389 -0.1578 -0.0505 437 SER B CA 7616 C C . SER B 437 ? 1.1790 0.9416 1.0784 0.0472 -0.1637 -0.0604 437 SER B C 7617 O O . SER B 437 ? 1.2864 1.0669 1.2016 0.0448 -0.1610 -0.0683 437 SER B O 7618 C CB . SER B 437 ? 1.0936 0.8648 0.9759 0.0286 -0.1492 -0.0535 437 SER B CB 7619 O OG . SER B 437 ? 1.0953 0.8654 0.9595 0.0231 -0.1449 -0.0450 437 SER B OG 7620 N N . ASN B 438 ? 1.1174 0.8678 1.0176 0.0572 -0.1714 -0.0592 438 ASN B N 7621 C CA . ASN B 438 ? 1.1537 0.9148 1.0733 0.0667 -0.1784 -0.0677 438 ASN B CA 7622 C C . ASN B 438 ? 1.2423 1.0000 1.1540 0.0785 -0.1906 -0.0640 438 ASN B C 7623 O O . ASN B 438 ? 1.2909 1.0475 1.1839 0.0785 -0.1931 -0.0578 438 ASN B O 7624 C CB . ASN B 438 ? 1.1710 0.9243 1.1048 0.0694 -0.1765 -0.0725 438 ASN B CB 7625 C CG . ASN B 438 ? 1.1091 0.8637 1.0470 0.0582 -0.1652 -0.0759 438 ASN B CG 7626 O OD1 . ASN B 438 ? 1.0738 0.8137 0.9983 0.0506 -0.1600 -0.0704 438 ASN B OD1 7627 N ND2 . ASN B 438 ? 1.1103 0.8832 1.0672 0.0570 -0.1615 -0.0849 438 ASN B ND2 7628 N N . MET B 439 ? 1.1673 0.9245 1.0929 0.0891 -0.1980 -0.0681 439 MET B N 7629 C CA . MET B 439 ? 1.0422 0.7989 0.9631 0.1015 -0.2110 -0.0657 439 MET B CA 7630 C C . MET B 439 ? 1.1185 0.8547 1.0372 0.1109 -0.2155 -0.0605 439 MET B C 7631 O O . MET B 439 ? 1.0919 0.8297 1.0163 0.1236 -0.2266 -0.0611 439 MET B O 7632 C CB . MET B 439 ? 0.9275 0.7079 0.8713 0.1064 -0.2179 -0.0764 439 MET B CB 7633 C CG . MET B 439 ? 0.8054 0.6040 0.7528 0.0977 -0.2142 -0.0816 439 MET B CG 7634 S SD . MET B 439 ? 1.8533 1.6769 1.8270 0.1032 -0.2242 -0.0931 439 MET B SD 7635 C CE . MET B 439 ? 1.7346 1.5531 1.6924 0.1169 -0.2410 -0.0893 439 MET B CE 7636 N N . LEU B 440 ? 1.1758 0.8924 1.0868 0.1047 -0.2071 -0.0555 440 LEU B N 7637 C CA . LEU B 440 ? 1.2124 0.9052 1.1205 0.1126 -0.2103 -0.0501 440 LEU B CA 7638 C C . LEU B 440 ? 1.2075 0.8880 1.0960 0.1224 -0.2205 -0.0382 440 LEU B C 7639 O O . LEU B 440 ? 1.2034 0.8818 1.0705 0.1176 -0.2195 -0.0294 440 LEU B O 7640 C CB . LEU B 440 ? 1.2288 0.9011 1.1290 0.1018 -0.1997 -0.0461 440 LEU B CB 7641 C CG . LEU B 440 ? 1.2412 0.9238 1.1605 0.0948 -0.1909 -0.0583 440 LEU B CG 7642 C CD1 . LEU B 440 ? 1.3198 0.9846 1.2304 0.0823 -0.1810 -0.0555 440 LEU B CD1 7643 C CD2 . LEU B 440 ? 1.2056 0.8897 1.1453 0.1071 -0.1955 -0.0669 440 LEU B CD2 7644 N N . THR B 441 ? 1.2498 0.9230 1.1456 0.1368 -0.2300 -0.0377 441 THR B N 7645 C CA . THR B 441 ? 1.2224 0.8798 1.0988 0.1475 -0.2399 -0.0247 441 THR B CA 7646 C C . THR B 441 ? 1.1950 0.8185 1.0610 0.1467 -0.2354 -0.0141 441 THR B C 7647 O O . THR B 441 ? 1.0193 0.6332 0.8891 0.1352 -0.2244 -0.0168 441 THR B O 7648 C CB . THR B 441 ? 1.2894 0.9585 1.1802 0.1646 -0.2539 -0.0295 441 THR B CB 7649 O OG1 . THR B 441 ? 1.3839 1.0315 1.2799 0.1757 -0.2575 -0.0256 441 THR B OG1 7650 C CG2 . THR B 441 ? 1.2816 0.9800 1.2010 0.1629 -0.2532 -0.0461 441 THR B CG2 7651 N N . GLY B 442 ? 1.3511 0.9559 1.2045 0.1587 -0.2443 -0.0021 442 GLY B N 7652 C CA . GLY B 442 ? 1.3312 0.9010 1.1730 0.1573 -0.2403 0.0101 442 GLY B CA 7653 C C . GLY B 442 ? 1.2048 0.7575 1.0660 0.1633 -0.2396 0.0033 442 GLY B C 7654 O O . GLY B 442 ? 1.1714 0.6960 1.0280 0.1570 -0.2330 0.0086 442 GLY B O 7655 N N . SER B 443 ? 1.1494 0.7191 1.0330 0.1754 -0.2464 -0.0089 443 SER B N 7656 C CA . SER B 443 ? 1.2309 0.7882 1.1346 0.1833 -0.2457 -0.0174 443 SER B CA 7657 C C . SER B 443 ? 1.2375 0.7881 1.1474 0.1681 -0.2320 -0.0260 443 SER B C 7658 O O . SER B 443 ? 1.2243 0.7601 1.1470 0.1718 -0.2292 -0.0334 443 SER B O 7659 C CB . SER B 443 ? 1.2416 0.8277 1.1712 0.1954 -0.2524 -0.0312 443 SER B CB 7660 O OG . SER B 443 ? 1.2040 0.8218 1.1423 0.1850 -0.2476 -0.0414 443 SER B OG 7661 N N . VAL B 444 ? 1.2052 0.7680 1.1060 0.1517 -0.2239 -0.0258 444 VAL B N 7662 C CA . VAL B 444 ? 1.1447 0.7048 1.0488 0.1358 -0.2114 -0.0329 444 VAL B CA 7663 C C . VAL B 444 ? 1.2936 0.8157 1.1890 0.1315 -0.2075 -0.0259 444 VAL B C 7664 O O . VAL B 444 ? 1.3316 0.8471 1.2335 0.1214 -0.1989 -0.0344 444 VAL B O 7665 C CB . VAL B 444 ? 1.1022 0.6802 0.9946 0.1203 -0.2050 -0.0301 444 VAL B CB 7666 C CG1 . VAL B 444 ? 1.0167 0.5736 0.8836 0.1137 -0.2038 -0.0124 444 VAL B CG1 7667 C CG2 . VAL B 444 ? 1.1818 0.7702 1.0845 0.1064 -0.1936 -0.0418 444 VAL B CG2 7668 N N . PHE B 445 ? 1.4028 0.8998 1.2836 0.1391 -0.2141 -0.0104 445 PHE B N 7669 C CA . PHE B 445 ? 1.4496 0.9073 1.3231 0.1353 -0.2111 -0.0021 445 PHE B CA 7670 C C . PHE B 445 ? 1.4993 0.9362 1.3879 0.1505 -0.2162 -0.0088 445 PHE B C 7671 O O . PHE B 445 ? 1.4778 0.8805 1.3643 0.1481 -0.2138 -0.0054 445 PHE B O 7672 C CB . PHE B 445 ? 1.3748 0.8132 1.2235 0.1341 -0.2139 0.0204 445 PHE B CB 7673 C CG . PHE B 445 ? 1.2849 0.7391 1.1179 0.1180 -0.2069 0.0272 445 PHE B CG 7674 C CD1 . PHE B 445 ? 1.2449 0.7290 1.0707 0.1214 -0.2109 0.0284 445 PHE B CD1 7675 C CD2 . PHE B 445 ? 1.2235 0.6635 1.0500 0.0996 -0.1965 0.0318 445 PHE B CD2 7676 C CE1 . PHE B 445 ? 1.2880 0.7870 1.0996 0.1079 -0.2042 0.0338 445 PHE B CE1 7677 C CE2 . PHE B 445 ? 1.2480 0.7046 1.0614 0.0856 -0.1896 0.0381 445 PHE B CE2 7678 C CZ . PHE B 445 ? 1.3215 0.8075 1.1270 0.0903 -0.1932 0.0390 445 PHE B CZ 7679 N N . ARG B 446 ? 1.5576 1.0156 1.4624 0.1661 -0.2231 -0.0187 446 ARG B N 7680 C CA . ARG B 446 ? 1.6136 1.0588 1.5361 0.1819 -0.2271 -0.0279 446 ARG B CA 7681 C C . ARG B 446 ? 1.5994 1.0457 1.5370 0.1741 -0.2173 -0.0463 446 ARG B C 7682 O O . ARG B 446 ? 1.5135 0.9405 1.4625 0.1834 -0.2177 -0.0545 446 ARG B O 7683 C CB . ARG B 446 ? 1.6752 1.1495 1.6133 0.1994 -0.2365 -0.0342 446 ARG B CB 7684 C CG . ARG B 446 ? 1.8394 1.3051 1.7678 0.2154 -0.2497 -0.0189 446 ARG B CG 7685 C CD . ARG B 446 ? 1.8874 1.3834 1.8360 0.2327 -0.2593 -0.0277 446 ARG B CD 7686 N NE . ARG B 446 ? 1.9398 1.4256 1.8810 0.2506 -0.2732 -0.0142 446 ARG B NE 7687 C CZ . ARG B 446 ? 1.9153 1.4166 1.8429 0.2533 -0.2820 -0.0041 446 ARG B CZ 7688 N NH1 . ARG B 446 ? 1.8381 1.3646 1.7588 0.2393 -0.2780 -0.0065 446 ARG B NH1 7689 N NH2 . ARG B 446 ? 1.9007 1.3923 1.8212 0.2707 -0.2952 0.0082 446 ARG B NH2 7690 N N . CYS B 447 ? 1.5295 0.9988 1.4663 0.1576 -0.2086 -0.0529 447 CYS B N 7691 C CA . CYS B 447 ? 1.4693 0.9497 1.4202 0.1508 -0.1997 -0.0713 447 CYS B CA 7692 C C . CYS B 447 ? 1.2798 0.7633 1.2202 0.1286 -0.1899 -0.0711 447 CYS B C 7693 O O . CYS B 447 ? 1.2439 0.7577 1.1840 0.1202 -0.1862 -0.0730 447 CYS B O 7694 C CB . CYS B 447 ? 1.5240 1.0442 1.4938 0.1588 -0.2003 -0.0838 447 CYS B CB 7695 S SG . CYS B 447 ? 1.5126 1.0506 1.5019 0.1564 -0.1902 -0.1067 447 CYS B SG 7696 N N . LEU B 448 ? 1.1270 0.5791 1.0598 0.1192 -0.1860 -0.0688 448 LEU B N 7697 C CA . LEU B 448 ? 1.1387 0.5934 1.0636 0.0980 -0.1772 -0.0693 448 LEU B CA 7698 C C . LEU B 448 ? 1.2414 0.6725 1.1713 0.0915 -0.1724 -0.0809 448 LEU B C 7699 O O . LEU B 448 ? 1.2521 0.6501 1.1838 0.0996 -0.1763 -0.0803 448 LEU B O 7700 C CB . LEU B 448 ? 1.1437 0.5858 1.0490 0.0878 -0.1774 -0.0491 448 LEU B CB 7701 C CG . LEU B 448 ? 1.1459 0.6115 1.0417 0.0910 -0.1812 -0.0377 448 LEU B CG 7702 C CD1 . LEU B 448 ? 1.2698 0.7113 1.1463 0.0899 -0.1844 -0.0163 448 LEU B CD1 7703 C CD2 . LEU B 448 ? 0.9681 0.4676 0.8633 0.0778 -0.1744 -0.0423 448 LEU B CD2 7704 N N . PRO B 449 ? 1.3416 0.7897 1.2739 0.0770 -0.1645 -0.0918 449 PRO B N 7705 C CA . PRO B 449 ? 1.4601 0.8911 1.3971 0.0694 -0.1601 -0.1057 449 PRO B CA 7706 C C . PRO B 449 ? 1.4803 0.8658 1.4103 0.0647 -0.1623 -0.0970 449 PRO B C 7707 O O . PRO B 449 ? 1.3843 0.7589 1.3021 0.0539 -0.1619 -0.0799 449 PRO B O 7708 C CB . PRO B 449 ? 1.4595 0.9159 1.3931 0.0508 -0.1525 -0.1095 449 PRO B CB 7709 C CG . PRO B 449 ? 1.3569 0.8510 1.2919 0.0550 -0.1523 -0.1064 449 PRO B CG 7710 C CD . PRO B 449 ? 1.2880 0.7734 1.2182 0.0674 -0.1599 -0.0915 449 PRO B CD 7711 N N . PRO B 450 ? 1.5171 0.8758 1.4554 0.0730 -0.1644 -0.1086 450 PRO B N 7712 C CA . PRO B 450 ? 1.5147 0.8260 1.4488 0.0703 -0.1672 -0.1008 450 PRO B CA 7713 C C . PRO B 450 ? 1.4116 0.7111 1.3352 0.0472 -0.1629 -0.0893 450 PRO B C 7714 O O . PRO B 450 ? 1.4405 0.7201 1.3539 0.0445 -0.1650 -0.0686 450 PRO B O 7715 C CB . PRO B 450 ? 1.5713 0.8664 1.5172 0.0760 -0.1667 -0.1232 450 PRO B CB 7716 C CG . PRO B 450 ? 1.5150 0.8436 1.4716 0.0926 -0.1668 -0.1367 450 PRO B CG 7717 C CD . PRO B 450 ? 1.5111 0.8827 1.4634 0.0857 -0.1636 -0.1300 450 PRO B CD 7718 N N . LYS B 451 ? 1.2858 0.5992 1.2119 0.0311 -0.1569 -0.1019 451 LYS B N 7719 C CA . LYS B 451 ? 1.2983 0.5985 1.2183 0.0088 -0.1530 -0.0936 451 LYS B CA 7720 C C . LYS B 451 ? 1.3159 0.6508 1.2279 -0.0047 -0.1479 -0.0831 451 LYS B C 7721 O O . LYS B 451 ? 1.2439 0.5860 1.1561 -0.0234 -0.1430 -0.0865 451 LYS B O 7722 C CB . LYS B 451 ? 1.4031 0.6927 1.3313 -0.0023 -0.1505 -0.1143 451 LYS B CB 7723 C CG . LYS B 451 ? 1.5049 0.7521 1.4405 0.0069 -0.1551 -0.1250 451 LYS B CG 7724 C CD . LYS B 451 ? 1.6113 0.8126 1.5437 -0.0038 -0.1568 -0.1092 451 LYS B CD 7725 C CE . LYS B 451 ? 1.5628 0.7180 1.5034 0.0049 -0.1616 -0.1204 451 LYS B CE 7726 N NZ . LYS B 451 ? 1.4663 0.6067 1.4143 -0.0104 -0.1600 -0.1403 451 LYS B NZ 7727 N N . VAL B 452 ? 1.2701 0.6266 1.1756 0.0046 -0.1493 -0.0711 452 VAL B N 7728 C CA . VAL B 452 ? 1.2376 0.6280 1.1361 -0.0066 -0.1445 -0.0633 452 VAL B CA 7729 C C . VAL B 452 ? 1.2885 0.6659 1.1783 -0.0252 -0.1404 -0.0474 452 VAL B C 7730 O O . VAL B 452 ? 1.5237 0.8665 1.4089 -0.0262 -0.1425 -0.0344 452 VAL B O 7731 C CB . VAL B 452 ? 1.2074 0.6198 1.0994 0.0063 -0.1475 -0.0526 452 VAL B CB 7732 C CG1 . VAL B 452 ? 0.8881 0.3422 0.7787 -0.0018 -0.1424 -0.0548 452 VAL B CG1 7733 C CG2 . VAL B 452 ? 1.2787 0.6921 1.1791 0.0275 -0.1537 -0.0616 452 VAL B CG2 7734 N N . LYS B 453 ? 1.0976 0.5037 0.9859 -0.0397 -0.1345 -0.0476 453 LYS B N 7735 C CA . LYS B 453 ? 1.1561 0.5569 1.0381 -0.0581 -0.1295 -0.0330 453 LYS B CA 7736 C C . LYS B 453 ? 1.3277 0.7606 1.1997 -0.0598 -0.1259 -0.0208 453 LYS B C 7737 O O . LYS B 453 ? 1.5765 1.0052 1.4397 -0.0698 -0.1222 -0.0037 453 LYS B O 7738 C CB . LYS B 453 ? 1.2495 0.6529 1.1407 -0.0767 -0.1253 -0.0457 453 LYS B CB 7739 C CG . LYS B 453 ? 1.5289 0.9068 1.4308 -0.0745 -0.1288 -0.0641 453 LYS B CG 7740 C CD . LYS B 453 ? 1.6941 1.0235 1.5954 -0.0739 -0.1322 -0.0544 453 LYS B CD 7741 C CE . LYS B 453 ? 1.6594 0.9622 1.5705 -0.0654 -0.1370 -0.0736 453 LYS B CE 7742 N NZ . LYS B 453 ? 1.6653 0.9613 1.5856 -0.0823 -0.1353 -0.0896 453 LYS B NZ 7743 N N . VAL B 454 ? 1.2562 0.7215 1.1302 -0.0504 -0.1266 -0.0297 454 VAL B N 7744 C CA . VAL B 454 ? 1.2561 0.7518 1.1216 -0.0503 -0.1240 -0.0205 454 VAL B CA 7745 C C . VAL B 454 ? 1.3230 0.8325 1.1882 -0.0312 -0.1297 -0.0240 454 VAL B C 7746 O O . VAL B 454 ? 1.3827 0.8989 1.2588 -0.0229 -0.1321 -0.0394 454 VAL B O 7747 C CB . VAL B 454 ? 1.1568 0.6856 1.0278 -0.0630 -0.1178 -0.0290 454 VAL B CB 7748 C CG1 . VAL B 454 ? 1.0250 0.5794 0.8864 -0.0644 -0.1144 -0.0174 454 VAL B CG1 7749 C CG2 . VAL B 454 ? 1.2493 0.7671 1.1257 -0.0818 -0.1135 -0.0312 454 VAL B CG2 7750 N N . LEU B 455 ? 1.3261 0.8409 1.1792 -0.0242 -0.1318 -0.0101 455 LEU B N 7751 C CA . LEU B 455 ? 1.2495 0.7768 1.1030 -0.0065 -0.1384 -0.0132 455 LEU B CA 7752 C C . LEU B 455 ? 1.2494 0.8028 1.0926 -0.0052 -0.1376 -0.0054 455 LEU B C 7753 O O . LEU B 455 ? 1.4269 0.9722 1.2553 -0.0015 -0.1398 0.0096 455 LEU B O 7754 C CB . LEU B 455 ? 1.2125 0.7102 1.0619 0.0073 -0.1460 -0.0056 455 LEU B CB 7755 C CG . LEU B 455 ? 1.1877 0.6946 1.0432 0.0267 -0.1543 -0.0122 455 LEU B CG 7756 C CD1 . LEU B 455 ? 1.2039 0.7284 1.0776 0.0289 -0.1530 -0.0324 455 LEU B CD1 7757 C CD2 . LEU B 455 ? 1.1049 0.5798 0.9577 0.0396 -0.1617 -0.0047 455 LEU B CD2 7758 N N . ASP B 456 ? 1.1618 0.7461 1.0122 -0.0079 -0.1345 -0.0155 456 ASP B N 7759 C CA . ASP B 456 ? 1.2142 0.8231 1.0561 -0.0067 -0.1338 -0.0102 456 ASP B CA 7760 C C . ASP B 456 ? 1.2221 0.8425 1.0661 0.0098 -0.1419 -0.0141 456 ASP B C 7761 O O . ASP B 456 ? 1.3025 0.9415 1.1601 0.0138 -0.1428 -0.0268 456 ASP B O 7762 C CB . ASP B 456 ? 1.2199 0.8557 1.0683 -0.0181 -0.1264 -0.0173 456 ASP B CB 7763 C CG . ASP B 456 ? 1.3575 1.0131 1.1946 -0.0198 -0.1237 -0.0093 456 ASP B CG 7764 O OD1 . ASP B 456 ? 1.3175 0.9772 1.1471 -0.0083 -0.1294 -0.0058 456 ASP B OD1 7765 O OD2 . ASP B 456 ? 1.4171 1.0846 1.2530 -0.0322 -0.1163 -0.0070 456 ASP B OD2 7766 N N . LEU B 457 ? 1.1359 0.7457 0.9663 0.0190 -0.1478 -0.0027 457 LEU B N 7767 C CA . LEU B 457 ? 1.1308 0.7502 0.9627 0.0347 -0.1571 -0.0057 457 LEU B CA 7768 C C . LEU B 457 ? 1.1046 0.7434 0.9234 0.0369 -0.1585 -0.0004 457 LEU B C 7769 O O . LEU B 457 ? 1.0207 0.6637 0.8355 0.0496 -0.1674 0.0004 457 LEU B O 7770 C CB . LEU B 457 ? 1.0860 0.6797 0.9133 0.0469 -0.1653 0.0015 457 LEU B CB 7771 C CG . LEU B 457 ? 1.1097 0.6959 0.9552 0.0568 -0.1703 -0.0099 457 LEU B CG 7772 C CD1 . LEU B 457 ? 1.1330 0.6871 0.9728 0.0658 -0.1762 -0.0005 457 LEU B CD1 7773 C CD2 . LEU B 457 ? 1.0653 0.6766 0.9225 0.0682 -0.1770 -0.0199 457 LEU B CD2 7774 N N . HIS B 458 ? 1.0891 0.7403 0.9015 0.0251 -0.1502 0.0025 458 HIS B N 7775 C CA . HIS B 458 ? 1.0650 0.7336 0.8635 0.0275 -0.1507 0.0070 458 HIS B CA 7776 C C . HIS B 458 ? 1.0357 0.7281 0.8455 0.0348 -0.1557 -0.0059 458 HIS B C 7777 O O . HIS B 458 ? 0.9284 0.6290 0.7576 0.0341 -0.1553 -0.0178 458 HIS B O 7778 C CB . HIS B 458 ? 1.1151 0.7923 0.9053 0.0136 -0.1399 0.0130 458 HIS B CB 7779 C CG . HIS B 458 ? 1.0579 0.7578 0.8626 0.0059 -0.1341 0.0014 458 HIS B CG 7780 N ND1 . HIS B 458 ? 1.1009 0.7996 0.9177 -0.0058 -0.1272 -0.0029 458 HIS B ND1 7781 C CD2 . HIS B 458 ? 1.0040 0.7280 0.8126 0.0085 -0.1343 -0.0063 458 HIS B CD2 7782 C CE1 . HIS B 458 ? 1.1078 0.8297 0.9347 -0.0095 -0.1236 -0.0119 458 HIS B CE1 7783 N NE2 . HIS B 458 ? 1.0253 0.7619 0.8481 -0.0011 -0.1275 -0.0138 458 HIS B NE2 7784 N N . ASN B 459 ? 1.1744 0.8777 0.9715 0.0418 -0.1604 -0.0034 459 ASN B N 7785 C CA . ASN B 459 ? 1.1713 0.8958 0.9786 0.0485 -0.1661 -0.0152 459 ASN B CA 7786 C C . ASN B 459 ? 1.1050 0.8272 0.9285 0.0591 -0.1758 -0.0231 459 ASN B C 7787 O O . ASN B 459 ? 1.1091 0.8467 0.9519 0.0603 -0.1774 -0.0349 459 ASN B O 7788 C CB . ASN B 459 ? 1.1196 0.8627 0.9400 0.0388 -0.1580 -0.0239 459 ASN B CB 7789 C CG . ASN B 459 ? 1.1674 0.9315 0.9924 0.0438 -0.1623 -0.0328 459 ASN B CG 7790 O OD1 . ASN B 459 ? 0.9539 0.7201 0.7678 0.0530 -0.1703 -0.0318 459 ASN B OD1 7791 N ND2 . ASN B 459 ? 1.3187 1.0981 1.1601 0.0380 -0.1573 -0.0416 459 ASN B ND2 7792 N N . ASN B 460 ? 1.0758 0.7791 0.8918 0.0672 -0.1822 -0.0156 460 ASN B N 7793 C CA . ASN B 460 ? 1.2693 0.9723 1.0997 0.0794 -0.1925 -0.0222 460 ASN B CA 7794 C C . ASN B 460 ? 1.2963 0.9993 1.1135 0.0929 -0.2050 -0.0174 460 ASN B C 7795 O O . ASN B 460 ? 1.3523 1.0636 1.1519 0.0935 -0.2065 -0.0136 460 ASN B O 7796 C CB . ASN B 460 ? 1.3762 1.0588 1.2160 0.0798 -0.1909 -0.0213 460 ASN B CB 7797 C CG . ASN B 460 ? 1.2624 0.9535 1.1236 0.0721 -0.1835 -0.0330 460 ASN B CG 7798 O OD1 . ASN B 460 ? 1.3449 1.0259 1.2055 0.0618 -0.1747 -0.0315 460 ASN B OD1 7799 N ND2 . ASN B 460 ? 1.0961 0.8069 0.9766 0.0768 -0.1869 -0.0447 460 ASN B ND2 7800 N N . ARG B 461 ? 1.1540 0.8491 0.9798 0.1045 -0.2143 -0.0183 461 ARG B N 7801 C CA . ARG B 461 ? 1.1955 0.8951 1.0132 0.1185 -0.2280 -0.0162 461 ARG B CA 7802 C C . ARG B 461 ? 1.3634 1.0399 1.1732 0.1293 -0.2348 -0.0053 461 ARG B C 7803 O O . ARG B 461 ? 1.3231 1.0029 1.1428 0.1425 -0.2465 -0.0088 461 ARG B O 7804 C CB . ARG B 461 ? 1.0836 0.8063 0.9254 0.1244 -0.2360 -0.0315 461 ARG B CB 7805 C CG . ARG B 461 ? 1.1715 0.9150 1.0221 0.1144 -0.2298 -0.0416 461 ARG B CG 7806 C CD . ARG B 461 ? 1.4788 1.2438 1.3392 0.1213 -0.2410 -0.0520 461 ARG B CD 7807 N NE . ARG B 461 ? 1.7072 1.4850 1.5578 0.1149 -0.2379 -0.0554 461 ARG B NE 7808 C CZ . ARG B 461 ? 1.7072 1.5025 1.5763 0.1091 -0.2354 -0.0669 461 ARG B CZ 7809 N NH1 . ARG B 461 ? 1.7387 1.5423 1.6367 0.1082 -0.2352 -0.0754 461 ARG B NH1 7810 N NH2 . ARG B 461 ? 1.5629 1.3673 1.4217 0.1045 -0.2330 -0.0697 461 ARG B NH2 7811 N N . ILE B 462 ? 1.4520 1.1054 1.2446 0.1236 -0.2277 0.0085 462 ILE B N 7812 C CA . ILE B 462 ? 1.5113 1.1378 1.2970 0.1322 -0.2323 0.0204 462 ILE B CA 7813 C C . ILE B 462 ? 1.7194 1.3374 1.4761 0.1407 -0.2394 0.0368 462 ILE B C 7814 O O . ILE B 462 ? 1.7774 1.3917 1.5122 0.1326 -0.2322 0.0478 462 ILE B O 7815 C CB . ILE B 462 ? 1.4036 1.0059 1.1893 0.1203 -0.2205 0.0266 462 ILE B CB 7816 C CG1 . ILE B 462 ? 1.2750 0.8858 1.0870 0.1123 -0.2133 0.0105 462 ILE B CG1 7817 C CG2 . ILE B 462 ? 1.4030 0.9742 1.1825 0.1294 -0.2254 0.0391 462 ILE B CG2 7818 C CD1 . ILE B 462 ? 1.1538 0.7494 0.9648 0.0964 -0.2004 0.0132 462 ILE B CD1 7819 N N . MET B 463 ? 1.8252 1.4417 1.5823 0.1574 -0.2533 0.0385 463 MET B N 7820 C CA . MET B 463 ? 1.8584 1.4601 1.5888 0.1678 -0.2608 0.0566 463 MET B CA 7821 C C . MET B 463 ? 1.9119 1.4883 1.6523 0.1779 -0.2659 0.0623 463 MET B C 7822 O O . MET B 463 ? 1.7492 1.2970 1.4747 0.1778 -0.2630 0.0792 463 MET B O 7823 C CB . MET B 463 ? 1.8775 1.5014 1.5998 0.1813 -0.2755 0.0530 463 MET B CB 7824 C CG . MET B 463 ? 1.9046 1.5596 1.6340 0.1756 -0.2751 0.0367 463 MET B CG 7825 S SD . MET B 463 ? 1.6405 1.3212 1.3819 0.1925 -0.2953 0.0237 463 MET B SD 7826 C CE . MET B 463 ? 1.3156 0.9757 1.0374 0.2109 -0.3082 0.0423 463 MET B CE 7827 N N . SER B 464 ? 2.1145 1.7026 1.8816 0.1867 -0.2733 0.0475 464 SER B N 7828 C CA . SER B 464 ? 2.2931 1.8622 2.0764 0.1975 -0.2781 0.0478 464 SER B CA 7829 C C . SER B 464 ? 2.4266 1.9643 2.2120 0.1874 -0.2659 0.0533 464 SER B C 7830 O O . SER B 464 ? 2.4655 2.0062 2.2728 0.1799 -0.2584 0.0396 464 SER B O 7831 C CB . SER B 464 ? 1.2410 0.8345 1.0572 0.2038 -0.2835 0.0275 464 SER B CB 7832 O OG . SER B 464 ? 0.8036 0.4274 0.6272 0.1943 -0.2803 0.0143 464 SER B OG 7833 N N . ILE B 465 ? 2.4469 1.9551 2.2102 0.1868 -0.2639 0.0731 465 ILE B N 7834 C CA . ILE B 465 ? 2.4537 1.9289 2.2209 0.1779 -0.2541 0.0783 465 ILE B CA 7835 C C . ILE B 465 ? 2.4132 1.8594 2.1874 0.1935 -0.2621 0.0842 465 ILE B C 7836 O O . ILE B 465 ? 2.4221 1.8594 2.1817 0.2078 -0.2725 0.0986 465 ILE B O 7837 C CB . ILE B 465 ? 1.3954 0.8519 1.1375 0.1634 -0.2440 0.0967 465 ILE B CB 7838 C CG1 . ILE B 465 ? 1.3931 0.8745 1.1317 0.1462 -0.2334 0.0898 465 ILE B CG1 7839 C CG2 . ILE B 465 ? 1.2081 0.6272 0.9564 0.1555 -0.2362 0.1022 465 ILE B CG2 7840 C CD1 . ILE B 465 ? 1.2753 0.7374 1.0073 0.1270 -0.2192 0.0986 465 ILE B CD1 7841 N N . PRO B 466 ? 2.3197 1.7513 2.1159 0.1912 -0.2572 0.0730 466 PRO B N 7842 C CA . PRO B 466 ? 2.3189 1.7218 2.1252 0.2060 -0.2635 0.0757 466 PRO B CA 7843 C C . PRO B 466 ? 2.3327 1.6917 2.1270 0.1988 -0.2573 0.0918 466 PRO B C 7844 O O . PRO B 466 ? 2.3038 1.6561 2.0828 0.1813 -0.2476 0.1010 466 PRO B O 7845 C CB . PRO B 466 ? 2.2563 1.6704 2.0932 0.2058 -0.2598 0.0521 466 PRO B CB 7846 C CG . PRO B 466 ? 2.2184 1.6666 2.0598 0.1904 -0.2517 0.0390 466 PRO B CG 7847 C CD . PRO B 466 ? 2.2463 1.6933 2.0613 0.1772 -0.2466 0.0541 466 PRO B CD 7848 N N . LYS B 467 ? 2.3428 1.6723 2.1459 0.2125 -0.2631 0.0947 467 LYS B N 7849 C CA . LYS B 467 ? 2.3524 1.6357 2.1486 0.2075 -0.2585 0.1086 467 LYS B CA 7850 C C . LYS B 467 ? 2.5507 1.8193 2.3681 0.1974 -0.2495 0.0909 467 LYS B C 7851 O O . LYS B 467 ? 2.5861 1.8173 2.4101 0.2022 -0.2501 0.0932 467 LYS B O 7852 C CB . LYS B 467 ? 2.1863 1.4423 1.9789 0.2295 -0.2707 0.1230 467 LYS B CB 7853 C CG . LYS B 467 ? 2.1018 1.3736 1.9171 0.2515 -0.2818 0.1075 467 LYS B CG 7854 C CD . LYS B 467 ? 2.0556 1.3720 1.8682 0.2601 -0.2907 0.1037 467 LYS B CD 7855 C CE . LYS B 467 ? 1.9940 1.3326 1.8341 0.2783 -0.2997 0.0853 467 LYS B CE 7856 N NZ . LYS B 467 ? 1.9043 1.2902 1.7471 0.2802 -0.3054 0.0763 467 LYS B NZ 7857 N N . ASP B 468 ? 2.6149 1.9129 2.4424 0.1838 -0.2414 0.0730 468 ASP B N 7858 C CA . ASP B 468 ? 2.6221 1.9128 2.4681 0.1736 -0.2327 0.0544 468 ASP B CA 7859 C C . ASP B 468 ? 2.7098 2.0021 2.5478 0.1482 -0.2202 0.0553 468 ASP B C 7860 O O . ASP B 468 ? 2.7513 2.0453 2.6028 0.1372 -0.2127 0.0387 468 ASP B O 7861 C CB . ASP B 468 ? 2.5537 1.8796 2.4220 0.1810 -0.2339 0.0306 468 ASP B CB 7862 C CG . ASP B 468 ? 2.5934 1.9106 2.4787 0.2038 -0.2429 0.0234 468 ASP B CG 7863 O OD1 . ASP B 468 ? 2.6759 1.9538 2.5595 0.2114 -0.2461 0.0318 468 ASP B OD1 7864 O OD2 . ASP B 468 ? 2.5424 1.8921 2.4437 0.2141 -0.2467 0.0095 468 ASP B OD2 7865 N N . VAL B 469 ? 2.7700 2.0633 2.5860 0.1393 -0.2181 0.0744 469 VAL B N 7866 C CA . VAL B 469 ? 2.7709 2.0700 2.5794 0.1157 -0.2063 0.0767 469 VAL B CA 7867 C C . VAL B 469 ? 2.7830 2.0408 2.5907 0.1027 -0.2001 0.0848 469 VAL B C 7868 O O . VAL B 469 ? 2.7329 1.9923 2.5378 0.0822 -0.1903 0.0860 469 VAL B O 7869 C CB . VAL B 469 ? 2.2806 1.5989 2.0658 0.1112 -0.2053 0.0938 469 VAL B CB 7870 C CG1 . VAL B 469 ? 2.1274 1.4707 1.9118 0.0905 -0.1940 0.0873 469 VAL B CG1 7871 C CG2 . VAL B 469 ? 2.2997 1.6454 2.0813 0.1295 -0.2160 0.0923 469 VAL B CG2 7872 N N . THR B 470 ? 2.8373 2.0584 2.6489 0.1149 -0.2063 0.0902 470 THR B N 7873 C CA . THR B 470 ? 2.8919 2.0692 2.7048 0.1038 -0.2017 0.0976 470 THR B CA 7874 C C . THR B 470 ? 2.9376 2.0941 2.7726 0.1090 -0.2030 0.0768 470 THR B C 7875 O O . THR B 470 ? 2.9854 2.1038 2.8248 0.1005 -0.2001 0.0788 470 THR B O 7876 C CB . THR B 470 ? 2.9053 2.0479 2.7010 0.1113 -0.2065 0.1259 470 THR B CB 7877 O OG1 . THR B 470 ? 2.9139 2.0553 2.7106 0.1372 -0.2187 0.1274 470 THR B OG1 7878 C CG2 . THR B 470 ? 2.8678 2.0263 2.6397 0.1011 -0.2019 0.1472 470 THR B CG2 7879 N N . HIS B 471 ? 2.8641 2.0462 2.7135 0.1229 -0.2073 0.0567 471 HIS B N 7880 C CA . HIS B 471 ? 2.6928 1.8627 2.5629 0.1285 -0.2074 0.0341 471 HIS B CA 7881 C C . HIS B 471 ? 2.4815 1.6758 2.3604 0.1105 -0.1980 0.0141 471 HIS B C 7882 O O . HIS B 471 ? 2.4550 1.6542 2.3502 0.1144 -0.1969 -0.0083 471 HIS B O 7883 C CB . HIS B 471 ? 2.6289 1.8153 2.5112 0.1537 -0.2163 0.0234 471 HIS B CB 7884 C CG . HIS B 471 ? 2.5910 1.7558 2.4660 0.1735 -0.2269 0.0418 471 HIS B CG 7885 N ND1 . HIS B 471 ? 2.5560 1.7441 2.4187 0.1831 -0.2336 0.0557 471 HIS B ND1 7886 C CD2 . HIS B 471 ? 2.5371 1.6590 2.4151 0.1861 -0.2326 0.0487 471 HIS B CD2 7887 C CE1 . HIS B 471 ? 2.5010 1.6630 2.3587 0.2008 -0.2431 0.0708 471 HIS B CE1 7888 N NE2 . HIS B 471 ? 2.5098 1.6308 2.3770 0.2032 -0.2425 0.0675 471 HIS B NE2 7889 N N . LEU B 472 ? 2.2918 1.5020 2.1590 0.0913 -0.1911 0.0230 472 LEU B N 7890 C CA . LEU B 472 ? 2.0828 1.3200 1.9560 0.0738 -0.1825 0.0074 472 LEU B CA 7891 C C . LEU B 472 ? 1.9673 1.1953 1.8292 0.0507 -0.1751 0.0217 472 LEU B C 7892 O O . LEU B 472 ? 1.8082 1.0638 1.6595 0.0418 -0.1711 0.0303 472 LEU B O 7893 C CB . LEU B 472 ? 1.9977 1.2836 1.8717 0.0792 -0.1828 0.0002 472 LEU B CB 7894 C CG . LEU B 472 ? 1.9621 1.2581 1.8491 0.1019 -0.1903 -0.0122 472 LEU B CG 7895 C CD1 . LEU B 472 ? 1.8387 1.1748 1.7237 0.1108 -0.1939 -0.0108 472 LEU B CD1 7896 C CD2 . LEU B 472 ? 1.9460 1.2456 1.8514 0.1022 -0.1868 -0.0373 472 LEU B CD2 7897 N N . GLN B 473 ? 1.9903 1.1791 1.8559 0.0413 -0.1733 0.0233 473 GLN B N 7898 C CA . GLN B 473 ? 1.9355 1.1044 1.7917 0.0216 -0.1676 0.0418 473 GLN B CA 7899 C C . GLN B 473 ? 1.7030 0.8765 1.5682 -0.0016 -0.1597 0.0289 473 GLN B C 7900 O O . GLN B 473 ? 1.5023 0.6421 1.3764 -0.0100 -0.1592 0.0237 473 GLN B O 7901 C CB . GLN B 473 ? 2.0839 1.2001 1.9385 0.0266 -0.1718 0.0564 473 GLN B CB 7902 C CG . GLN B 473 ? 2.1600 1.2633 2.0136 0.0537 -0.1820 0.0602 473 GLN B CG 7903 C CD . GLN B 473 ? 2.1976 1.2475 2.0588 0.0606 -0.1866 0.0622 473 GLN B CD 7904 O OE1 . GLN B 473 ? 2.2343 1.2544 2.1010 0.0441 -0.1823 0.0614 473 GLN B OE1 7905 N NE2 . GLN B 473 ? 2.1220 1.1597 1.9845 0.0852 -0.1957 0.0643 473 GLN B NE2 7906 N N . ALA B 474 ? 1.6682 0.8829 1.5315 -0.0120 -0.1540 0.0238 474 ALA B N 7907 C CA . ALA B 474 ? 1.5737 0.7969 1.4459 -0.0331 -0.1474 0.0112 474 ALA B CA 7908 C C . ALA B 474 ? 1.4935 0.7614 1.3602 -0.0439 -0.1411 0.0130 474 ALA B C 7909 O O . ALA B 474 ? 1.4004 0.6816 1.2738 -0.0616 -0.1355 0.0040 474 ALA B O 7910 C CB . ALA B 474 ? 1.4449 0.6686 1.3325 -0.0282 -0.1496 -0.0166 474 ALA B CB 7911 N N . LEU B 475 ? 1.2405 0.5312 1.0954 -0.0327 -0.1425 0.0240 475 LEU B N 7912 C CA . LEU B 475 ? 1.2202 0.5518 1.0689 -0.0408 -0.1369 0.0267 475 LEU B CA 7913 C C . LEU B 475 ? 1.4122 0.7410 1.2556 -0.0622 -0.1290 0.0415 475 LEU B C 7914 O O . LEU B 475 ? 1.5476 0.8426 1.3880 -0.0686 -0.1283 0.0560 475 LEU B O 7915 C CB . LEU B 475 ? 1.3591 0.7096 1.1948 -0.0251 -0.1407 0.0373 475 LEU B CB 7916 C CG . LEU B 475 ? 1.3785 0.7418 1.2190 -0.0039 -0.1484 0.0254 475 LEU B CG 7917 C CD1 . LEU B 475 ? 1.2249 0.5574 1.0609 0.0138 -0.1569 0.0355 475 LEU B CD1 7918 C CD2 . LEU B 475 ? 1.3420 0.7450 1.1750 -0.0002 -0.1477 0.0271 475 LEU B CD2 7919 N N . GLN B 476 ? 1.4876 0.8525 1.3309 -0.0730 -0.1228 0.0385 476 GLN B N 7920 C CA . GLN B 476 ? 1.5363 0.9063 1.3760 -0.0928 -0.1145 0.0520 476 GLN B CA 7921 C C . GLN B 476 ? 1.5061 0.9141 1.3343 -0.0904 -0.1108 0.0594 476 GLN B C 7922 O O . GLN B 476 ? 1.7114 1.1229 1.5286 -0.0981 -0.1051 0.0779 476 GLN B O 7923 C CB . GLN B 476 ? 1.5755 0.9531 1.4309 -0.1113 -0.1103 0.0368 476 GLN B CB 7924 C CG . GLN B 476 ? 1.6017 0.9442 1.4698 -0.1146 -0.1143 0.0247 476 GLN B CG 7925 C CD . GLN B 476 ? 1.5326 0.8812 1.4142 -0.1361 -0.1101 0.0133 476 GLN B CD 7926 O OE1 . GLN B 476 ? 1.5498 0.8662 1.4401 -0.1467 -0.1110 0.0114 476 GLN B OE1 7927 N NE2 . GLN B 476 ? 1.3100 0.7000 1.1941 -0.1426 -0.1059 0.0058 476 GLN B NE2 7928 N N . GLU B 477 ? 1.3094 0.7461 1.1406 -0.0798 -0.1136 0.0445 477 GLU B N 7929 C CA . GLU B 477 ? 1.3068 0.7779 1.1280 -0.0749 -0.1114 0.0489 477 GLU B CA 7930 C C . GLU B 477 ? 1.3167 0.7890 1.1318 -0.0532 -0.1198 0.0472 477 GLU B C 7931 O O . GLU B 477 ? 1.1875 0.6464 1.0115 -0.0428 -0.1262 0.0357 477 GLU B O 7932 C CB . GLU B 477 ? 1.4162 0.9229 1.2477 -0.0826 -0.1072 0.0336 477 GLU B CB 7933 C CG . GLU B 477 ? 1.5666 1.0784 1.4054 -0.1042 -0.0994 0.0346 477 GLU B CG 7934 C CD . GLU B 477 ? 1.6256 1.1773 1.4709 -0.1098 -0.0951 0.0241 477 GLU B CD 7935 O OE1 . GLU B 477 ? 1.6580 1.2337 1.4977 -0.0987 -0.0961 0.0225 477 GLU B OE1 7936 O OE2 . GLU B 477 ? 1.5421 1.1008 1.3986 -0.1252 -0.0912 0.0175 477 GLU B OE2 7937 N N . LEU B 478 ? 1.3649 0.8535 1.1649 -0.0464 -0.1199 0.0584 478 LEU B N 7938 C CA . LEU B 478 ? 1.2428 0.7358 1.0361 -0.0265 -0.1285 0.0579 478 LEU B CA 7939 C C . LEU B 478 ? 1.3283 0.8530 1.1098 -0.0233 -0.1269 0.0617 478 LEU B C 7940 O O . LEU B 478 ? 1.4946 1.0259 1.2641 -0.0322 -0.1202 0.0747 478 LEU B O 7941 C CB . LEU B 478 ? 1.0774 0.5378 0.8591 -0.0170 -0.1342 0.0738 478 LEU B CB 7942 C CG . LEU B 478 ? 1.0920 0.5586 0.8697 0.0043 -0.1446 0.0709 478 LEU B CG 7943 C CD1 . LEU B 478 ? 0.9736 0.4567 0.7707 0.0104 -0.1480 0.0482 478 LEU B CD1 7944 C CD2 . LEU B 478 ? 1.0660 0.4981 0.8366 0.0159 -0.1518 0.0834 478 LEU B CD2 7945 N N . ASN B 479 ? 1.2249 0.7696 1.0106 -0.0106 -0.1329 0.0500 479 ASN B N 7946 C CA . ASN B 479 ? 1.1509 0.7242 0.9266 -0.0065 -0.1326 0.0512 479 ASN B CA 7947 C C . ASN B 479 ? 1.1885 0.7667 0.9616 0.0123 -0.1434 0.0474 479 ASN B C 7948 O O . ASN B 479 ? 1.1390 0.7297 0.9271 0.0186 -0.1477 0.0321 479 ASN B O 7949 C CB . ASN B 479 ? 1.1070 0.7094 0.8947 -0.0154 -0.1265 0.0380 479 ASN B CB 7950 C CG . ASN B 479 ? 1.2537 0.8838 1.0312 -0.0123 -0.1251 0.0395 479 ASN B CG 7951 O OD1 . ASN B 479 ? 1.1999 0.8306 0.9629 -0.0009 -0.1308 0.0461 479 ASN B OD1 7952 N ND2 . ASN B 479 ? 1.3053 0.9584 1.0897 -0.0220 -0.1180 0.0330 479 ASN B ND2 7953 N N . VAL B 480 ? 1.3171 0.8860 1.0712 0.0210 -0.1480 0.0618 480 VAL B N 7954 C CA . VAL B 480 ? 1.3324 0.9080 1.0822 0.0387 -0.1593 0.0592 480 VAL B CA 7955 C C . VAL B 480 ? 1.3393 0.9397 1.0732 0.0411 -0.1589 0.0621 480 VAL B C 7956 O O . VAL B 480 ? 1.3817 0.9867 1.1043 0.0547 -0.1680 0.0647 480 VAL B O 7957 C CB . VAL B 480 ? 1.3979 0.9452 1.1367 0.0496 -0.1668 0.0729 480 VAL B CB 7958 C CG1 . VAL B 480 ? 1.3941 0.9183 1.1512 0.0519 -0.1696 0.0661 480 VAL B CG1 7959 C CG2 . VAL B 480 ? 1.4765 1.0080 1.1947 0.0413 -0.1600 0.0940 480 VAL B CG2 7960 N N . ALA B 481 ? 1.2897 0.9068 1.0232 0.0282 -0.1487 0.0608 481 ALA B N 7961 C CA . ALA B 481 ? 1.3136 0.9550 1.0329 0.0297 -0.1468 0.0620 481 ALA B CA 7962 C C . ALA B 481 ? 1.2909 0.9521 1.0162 0.0420 -0.1562 0.0476 481 ALA B C 7963 O O . ALA B 481 ? 1.3072 0.9646 1.0480 0.0496 -0.1641 0.0381 481 ALA B O 7964 C CB . ALA B 481 ? 1.3165 0.9737 1.0403 0.0143 -0.1344 0.0600 481 ALA B CB 7965 N N . SER B 482 ? 1.2993 0.9821 1.0134 0.0439 -0.1552 0.0458 482 SER B N 7966 C CA . SER B 482 ? 1.2848 0.9869 1.0042 0.0544 -0.1642 0.0321 482 SER B CA 7967 C C . SER B 482 ? 1.2923 0.9875 1.0237 0.0666 -0.1770 0.0252 482 SER B C 7968 O O . SER B 482 ? 1.2684 0.9749 1.0214 0.0678 -0.1801 0.0106 482 SER B O 7969 C CB . SER B 482 ? 1.1163 0.8395 0.8534 0.0468 -0.1583 0.0180 482 SER B CB 7970 O OG . SER B 482 ? 1.0706 0.8093 0.7943 0.0422 -0.1508 0.0208 482 SER B OG 7971 N N . ASN B 483 ? 1.2118 0.8894 0.9294 0.0759 -0.1842 0.0364 483 ASN B N 7972 C CA . ASN B 483 ? 1.1580 0.8308 0.8858 0.0894 -0.1974 0.0310 483 ASN B CA 7973 C C . ASN B 483 ? 1.3091 0.9876 1.0182 0.1041 -0.2097 0.0348 483 ASN B C 7974 O O . ASN B 483 ? 1.3597 1.0548 1.0539 0.1051 -0.2099 0.0335 483 ASN B O 7975 C CB . ASN B 483 ? 1.2042 0.8498 0.9391 0.0898 -0.1974 0.0381 483 ASN B CB 7976 C CG . ASN B 483 ? 1.2276 0.8728 0.9900 0.0824 -0.1923 0.0253 483 ASN B CG 7977 O OD1 . ASN B 483 ? 1.1729 0.8216 0.9402 0.0687 -0.1814 0.0232 483 ASN B OD1 7978 N ND2 . ASN B 483 ? 1.2102 0.8530 0.9904 0.0920 -0.2004 0.0168 483 ASN B ND2 7979 N N . GLN B 484 ? 1.3377 1.0032 1.0479 0.1162 -0.2206 0.0387 484 GLN B N 7980 C CA . GLN B 484 ? 1.3763 1.0472 1.0699 0.1315 -0.2343 0.0421 484 GLN B CA 7981 C C . GLN B 484 ? 1.4610 1.1065 1.1364 0.1395 -0.2383 0.0614 484 GLN B C 7982 O O . GLN B 484 ? 1.3027 0.9482 0.9706 0.1547 -0.2520 0.0642 484 GLN B O 7983 C CB . GLN B 484 ? 1.4008 1.0865 1.1175 0.1416 -0.2472 0.0258 484 GLN B CB 7984 C CG . GLN B 484 ? 1.4684 1.1781 1.2050 0.1349 -0.2446 0.0073 484 GLN B CG 7985 C CD . GLN B 484 ? 1.5601 1.2858 1.3178 0.1453 -0.2585 -0.0070 484 GLN B CD 7986 O OE1 . GLN B 484 ? 1.5719 1.2952 1.3244 0.1588 -0.2716 -0.0036 484 GLN B OE1 7987 N NE2 . GLN B 484 ? 1.4919 1.2347 1.2744 0.1389 -0.2558 -0.0225 484 GLN B NE2 7988 N N . LEU B 485 ? 1.5672 1.1912 1.2367 0.1292 -0.2268 0.0747 485 LEU B N 7989 C CA . LEU B 485 ? 1.5979 1.1934 1.2528 0.1347 -0.2289 0.0942 485 LEU B CA 7990 C C . LEU B 485 ? 1.6396 1.2357 1.2592 0.1407 -0.2310 0.1116 485 LEU B C 7991 O O . LEU B 485 ? 1.6327 1.2400 1.2363 0.1318 -0.2214 0.1157 485 LEU B O 7992 C CB . LEU B 485 ? 1.5133 1.0849 1.1750 0.1200 -0.2157 0.1022 485 LEU B CB 7993 C CG . LEU B 485 ? 1.4234 0.9802 1.1137 0.1194 -0.2164 0.0922 485 LEU B CG 7994 C CD1 . LEU B 485 ? 1.3454 0.8844 1.0420 0.1020 -0.2025 0.0962 485 LEU B CD1 7995 C CD2 . LEU B 485 ? 1.3977 0.9337 1.0878 0.1358 -0.2284 0.0996 485 LEU B CD2 7996 N N . LYS B 486 ? 1.5913 1.1764 1.1988 0.1565 -0.2434 0.1219 486 LYS B N 7997 C CA . LYS B 486 ? 1.5787 1.1625 1.1505 0.1638 -0.2461 0.1406 486 LYS B CA 7998 C C . LYS B 486 ? 1.6749 1.2250 1.2336 0.1606 -0.2395 0.1654 486 LYS B C 7999 O O . LYS B 486 ? 1.6510 1.1973 1.1866 0.1526 -0.2290 0.1818 486 LYS B O 8000 C CB . LYS B 486 ? 1.4965 1.0932 1.0597 0.1840 -0.2650 0.1368 486 LYS B CB 8001 C CG . LYS B 486 ? 1.4730 1.1037 1.0438 0.1859 -0.2710 0.1144 486 LYS B CG 8002 C CD . LYS B 486 ? 1.6446 1.2903 1.1956 0.2037 -0.2880 0.1143 486 LYS B CD 8003 C CE . LYS B 486 ? 1.7086 1.3857 1.2539 0.2024 -0.2898 0.0973 486 LYS B CE 8004 N NZ . LYS B 486 ? 1.7061 1.3965 1.2201 0.2176 -0.3032 0.1015 486 LYS B NZ 8005 N N . SER B 487 ? 1.7514 1.2769 1.3261 0.1665 -0.2452 0.1680 487 SER B N 8006 C CA . SER B 487 ? 1.7625 1.2521 1.3306 0.1615 -0.2382 0.1895 487 SER B CA 8007 C C . SER B 487 ? 1.7360 1.2033 1.3352 0.1562 -0.2358 0.1808 487 SER B C 8008 O O . SER B 487 ? 1.7793 1.2602 1.4042 0.1582 -0.2400 0.1591 487 SER B O 8009 C CB . SER B 487 ? 1.7226 1.1961 1.2656 0.1783 -0.2488 0.2113 487 SER B CB 8010 O OG . SER B 487 ? 1.6688 1.1454 1.1781 0.1744 -0.2417 0.2310 487 SER B OG 8011 N N . VAL B 488 ? 1.7007 1.1341 1.2974 0.1492 -0.2287 0.1978 488 VAL B N 8012 C CA . VAL B 488 ? 1.6900 1.0989 1.3139 0.1432 -0.2254 0.1900 488 VAL B CA 8013 C C . VAL B 488 ? 1.9468 1.3173 1.5662 0.1541 -0.2318 0.2080 488 VAL B C 8014 O O . VAL B 488 ? 2.0568 1.4064 1.6548 0.1504 -0.2271 0.2321 488 VAL B O 8015 C CB . VAL B 488 ? 1.4037 0.8059 1.0338 0.1194 -0.2085 0.1904 488 VAL B CB 8016 C CG1 . VAL B 488 ? 1.2597 0.6958 0.9052 0.1094 -0.2030 0.1674 488 VAL B CG1 8017 C CG2 . VAL B 488 ? 1.2245 0.6193 0.8266 0.1104 -0.1993 0.2155 488 VAL B CG2 8018 N N . PRO B 489 ? 2.0386 1.3994 1.6787 0.1677 -0.2421 0.1969 489 PRO B N 8019 C CA . PRO B 489 ? 2.0772 1.4009 1.7142 0.1806 -0.2493 0.2134 489 PRO B CA 8020 C C . PRO B 489 ? 2.1297 1.4165 1.7574 0.1658 -0.2377 0.2342 489 PRO B C 8021 O O . PRO B 489 ? 2.1206 1.4030 1.7607 0.1463 -0.2252 0.2268 489 PRO B O 8022 C CB . PRO B 489 ? 1.9923 1.3101 1.6617 0.1885 -0.2550 0.1926 489 PRO B CB 8023 C CG . PRO B 489 ? 1.9718 1.3325 1.6543 0.1895 -0.2578 0.1688 489 PRO B CG 8024 C CD . PRO B 489 ? 1.9683 1.3509 1.6369 0.1714 -0.2464 0.1693 489 PRO B CD 8025 N N . ASP B 490 ? 2.1432 1.4050 1.7493 0.1750 -0.2419 0.2605 490 ASP B N 8026 C CA . ASP B 490 ? 2.1161 1.3426 1.7112 0.1613 -0.2311 0.2841 490 ASP B CA 8027 C C . ASP B 490 ? 1.9719 1.1607 1.5931 0.1548 -0.2279 0.2778 490 ASP B C 8028 O O . ASP B 490 ? 1.8586 1.0263 1.4917 0.1713 -0.2384 0.2750 490 ASP B O 8029 C CB . ASP B 490 ? 2.2250 1.4328 1.7910 0.1753 -0.2379 0.3147 490 ASP B CB 8030 C CG . ASP B 490 ? 2.2419 1.4857 1.7779 0.1817 -0.2407 0.3224 490 ASP B CG 8031 O OD1 . ASP B 490 ? 2.2588 1.5282 1.7871 0.1662 -0.2297 0.3185 490 ASP B OD1 8032 O OD2 . ASP B 490 ? 2.1989 1.4455 1.7188 0.2028 -0.2544 0.3321 490 ASP B OD2 8033 N N . GLY B 491 ? 1.9758 1.1571 1.6064 0.1312 -0.2138 0.2745 491 GLY B N 8034 C CA . GLY B 491 ? 2.0266 1.1704 1.6798 0.1225 -0.2099 0.2691 491 GLY B CA 8035 C C . GLY B 491 ? 2.0653 1.2230 1.7471 0.1136 -0.2065 0.2377 491 GLY B C 8036 O O . GLY B 491 ? 2.1038 1.2348 1.8063 0.1159 -0.2087 0.2266 491 GLY B O 8037 N N . VAL B 492 ? 1.9798 1.1788 1.6625 0.1039 -0.2009 0.2234 492 VAL B N 8038 C CA . VAL B 492 ? 1.8366 1.0522 1.5443 0.0946 -0.1968 0.1950 492 VAL B CA 8039 C C . VAL B 492 ? 1.8234 1.0320 1.5373 0.0685 -0.1829 0.1945 492 VAL B C 8040 O O . VAL B 492 ? 1.9524 1.1317 1.6827 0.0608 -0.1805 0.1884 492 VAL B O 8041 C CB . VAL B 492 ? 1.6572 0.9216 1.3661 0.0993 -0.1992 0.1776 492 VAL B CB 8042 C CG1 . VAL B 492 ? 1.5824 0.8548 1.3027 0.1222 -0.2126 0.1642 492 VAL B CG1 8043 C CG2 . VAL B 492 ? 1.6083 0.8962 1.2905 0.0978 -0.1970 0.1935 492 VAL B CG2 8044 N N . PHE B 493 ? 1.6573 0.8938 1.3586 0.0554 -0.1744 0.2001 493 PHE B N 8045 C CA . PHE B 493 ? 1.6115 0.8477 1.3180 0.0302 -0.1611 0.2010 493 PHE B CA 8046 C C . PHE B 493 ? 1.6582 0.8488 1.3671 0.0187 -0.1565 0.2176 493 PHE B C 8047 O O . PHE B 493 ? 1.5248 0.7124 1.2399 -0.0033 -0.1458 0.2195 493 PHE B O 8048 C CB . PHE B 493 ? 1.6020 0.8699 1.2891 0.0217 -0.1532 0.2125 493 PHE B CB 8049 C CG . PHE B 493 ? 1.6201 0.9306 1.3029 0.0324 -0.1576 0.1985 493 PHE B CG 8050 C CD1 . PHE B 493 ? 1.6931 1.0147 1.3549 0.0497 -0.1654 0.2089 493 PHE B CD1 8051 C CD2 . PHE B 493 ? 1.7404 1.0795 1.4400 0.0250 -0.1543 0.1749 493 PHE B CD2 8052 C CE1 . PHE B 493 ? 1.8051 1.1647 1.4641 0.0588 -0.1701 0.1950 493 PHE B CE1 8053 C CE2 . PHE B 493 ? 1.8042 1.1806 1.5013 0.0343 -0.1583 0.1624 493 PHE B CE2 8054 C CZ . PHE B 493 ? 1.8442 1.2304 1.5215 0.0509 -0.1663 0.1719 493 PHE B CZ 8055 N N . ASP B 494 ? 1.8433 0.9987 1.5479 0.0334 -0.1647 0.2301 494 ASP B N 8056 C CA . ASP B 494 ? 2.0365 1.1435 1.7454 0.0245 -0.1619 0.2454 494 ASP B CA 8057 C C . ASP B 494 ? 2.0044 1.0923 1.7411 0.0174 -0.1620 0.2217 494 ASP B C 8058 O O . ASP B 494 ? 1.9960 1.0654 1.7429 -0.0035 -0.1539 0.2226 494 ASP B O 8059 C CB . ASP B 494 ? 2.1315 1.2056 1.8278 0.0449 -0.1718 0.2655 494 ASP B CB 8060 C CG . ASP B 494 ? 2.0488 1.1436 1.7157 0.0562 -0.1742 0.2867 494 ASP B CG 8061 O OD1 . ASP B 494 ? 2.0474 1.1730 1.7014 0.0443 -0.1654 0.2922 494 ASP B OD1 8062 O OD2 . ASP B 494 ? 1.9410 1.0218 1.5977 0.0778 -0.1852 0.2973 494 ASP B OD2 8063 N N . ARG B 495 ? 1.9702 1.0639 1.7193 0.0348 -0.1712 0.2002 495 ARG B N 8064 C CA . ARG B 495 ? 2.0038 1.0794 1.7777 0.0319 -0.1724 0.1765 495 ARG B CA 8065 C C . ARG B 495 ? 1.9095 1.0188 1.6965 0.0155 -0.1650 0.1530 495 ARG B C 8066 O O . ARG B 495 ? 1.8901 0.9871 1.6959 0.0081 -0.1638 0.1336 495 ARG B O 8067 C CB . ARG B 495 ? 1.9720 1.0410 1.7547 0.0579 -0.1843 0.1634 495 ARG B CB 8068 C CG . ARG B 495 ? 1.9513 0.9746 1.7516 0.0610 -0.1876 0.1544 495 ARG B CG 8069 C CD . ARG B 495 ? 2.0053 0.9798 1.7960 0.0641 -0.1901 0.1820 495 ARG B CD 8070 N NE . ARG B 495 ? 2.0715 0.9981 1.8793 0.0612 -0.1910 0.1748 495 ARG B NE 8071 C CZ . ARG B 495 ? 2.1379 1.0151 1.9419 0.0627 -0.1930 0.1962 495 ARG B CZ 8072 N NH1 . ARG B 495 ? 2.1676 1.0384 1.9501 0.0674 -0.1939 0.2274 495 ARG B NH1 8073 N NH2 . ARG B 495 ? 2.0638 0.8973 1.8851 0.0597 -0.1941 0.1866 495 ARG B NH2 8074 N N . LEU B 496 ? 1.7705 0.9220 1.5470 0.0103 -0.1604 0.1546 496 LEU B N 8075 C CA . LEU B 496 ? 1.6543 0.8388 1.4414 -0.0057 -0.1530 0.1359 496 LEU B CA 8076 C C . LEU B 496 ? 1.6060 0.7767 1.3972 -0.0317 -0.1429 0.1431 496 LEU B C 8077 O O . LEU B 496 ? 1.5439 0.7444 1.3317 -0.0464 -0.1348 0.1447 496 LEU B O 8078 C CB . LEU B 496 ? 1.6216 0.8534 1.3963 -0.0026 -0.1513 0.1363 496 LEU B CB 8079 C CG . LEU B 496 ? 1.5619 0.8179 1.3349 0.0198 -0.1607 0.1262 496 LEU B CG 8080 C CD1 . LEU B 496 ? 1.4813 0.7849 1.2515 0.0155 -0.1567 0.1171 496 LEU B CD1 8081 C CD2 . LEU B 496 ? 1.4861 0.7325 1.2787 0.0320 -0.1676 0.1045 496 LEU B CD2 8082 N N . THR B 497 ? 1.6722 0.7982 1.4723 -0.0370 -0.1438 0.1467 497 THR B N 8083 C CA . THR B 497 ? 1.8265 0.9320 1.6319 -0.0617 -0.1353 0.1567 497 THR B CA 8084 C C . THR B 497 ? 1.8304 0.9667 1.6473 -0.0831 -0.1272 0.1411 497 THR B C 8085 O O . THR B 497 ? 1.7018 0.8351 1.5204 -0.1046 -0.1188 0.1526 497 THR B O 8086 C CB . THR B 497 ? 1.9859 1.0382 1.8050 -0.0632 -0.1393 0.1540 497 THR B CB 8087 O OG1 . THR B 497 ? 1.9508 1.0041 1.7863 -0.0541 -0.1452 0.1241 497 THR B OG1 8088 C CG2 . THR B 497 ? 2.0631 1.0786 1.8698 -0.0464 -0.1455 0.1770 497 THR B CG2 8089 N N . SER B 498 ? 1.8976 1.0642 1.7232 -0.0770 -0.1297 0.1157 498 SER B N 8090 C CA . SER B 498 ? 1.7480 0.9433 1.5858 -0.0947 -0.1237 0.0984 498 SER B CA 8091 C C . SER B 498 ? 1.5715 0.8160 1.3991 -0.0960 -0.1185 0.1016 498 SER B C 8092 O O . SER B 498 ? 1.5351 0.8073 1.3702 -0.1109 -0.1126 0.0921 498 SER B O 8093 C CB . SER B 498 ? 1.6916 0.8885 1.5454 -0.0880 -0.1290 0.0685 498 SER B CB 8094 O OG . SER B 498 ? 1.7543 0.9543 1.6228 -0.1083 -0.1247 0.0540 498 SER B OG 8095 N N . LEU B 499 ? 1.5413 0.7958 1.3517 -0.0798 -0.1213 0.1147 499 LEU B N 8096 C CA . LEU B 499 ? 1.6390 0.9363 1.4374 -0.0789 -0.1172 0.1192 499 LEU B CA 8097 C C . LEU B 499 ? 1.7837 1.0947 1.5799 -0.1010 -0.1059 0.1317 499 LEU B C 8098 O O . LEU B 499 ? 1.9828 1.2664 1.7781 -0.1132 -0.1017 0.1485 499 LEU B O 8099 C CB . LEU B 499 ? 1.5780 0.8745 1.3562 -0.0597 -0.1224 0.1355 499 LEU B CB 8100 C CG . LEU B 499 ? 1.5410 0.8788 1.3048 -0.0533 -0.1209 0.1382 499 LEU B CG 8101 C CD1 . LEU B 499 ? 1.4141 0.7870 1.1904 -0.0520 -0.1214 0.1137 499 LEU B CD1 8102 C CD2 . LEU B 499 ? 1.6341 0.9659 1.3814 -0.0315 -0.1296 0.1489 499 LEU B CD2 8103 N N . GLN B 500 ? 1.6667 1.0198 1.4633 -0.1060 -0.1010 0.1238 500 GLN B N 8104 C CA . GLN B 500 ? 1.6908 1.0630 1.4868 -0.1256 -0.0901 0.1341 500 GLN B CA 8105 C C . GLN B 500 ? 1.7500 1.1673 1.5362 -0.1210 -0.0864 0.1328 500 GLN B C 8106 O O . GLN B 500 ? 1.7240 1.1606 1.5043 -0.1320 -0.0773 0.1451 500 GLN B O 8107 C CB . GLN B 500 ? 1.6109 0.9843 1.4286 -0.1450 -0.0867 0.1191 500 GLN B CB 8108 C CG . GLN B 500 ? 1.6548 0.9851 1.4850 -0.1499 -0.0911 0.1144 500 GLN B CG 8109 C CD . GLN B 500 ? 1.6713 1.0074 1.5221 -0.1683 -0.0889 0.0967 500 GLN B CD 8110 O OE1 . GLN B 500 ? 1.6708 1.0420 1.5262 -0.1801 -0.0827 0.0932 500 GLN B OE1 8111 N NE2 . GLN B 500 ? 1.5493 0.8520 1.4127 -0.1703 -0.0943 0.0846 500 GLN B NE2 8112 N N . TYR B 501 ? 1.7269 1.1614 1.5132 -0.1048 -0.0933 0.1169 501 TYR B N 8113 C CA . TYR B 501 ? 1.6499 1.1241 1.4282 -0.0982 -0.0915 0.1134 501 TYR B CA 8114 C C . TYR B 501 ? 1.6263 1.0986 1.3930 -0.0757 -0.1009 0.1125 501 TYR B C 8115 O O . TYR B 501 ? 1.6097 1.0624 1.3833 -0.0653 -0.1091 0.1036 501 TYR B O 8116 C CB . TYR B 501 ? 1.6847 1.1866 1.4799 -0.1040 -0.0902 0.0916 501 TYR B CB 8117 C CG . TYR B 501 ? 1.9008 1.4115 1.7075 -0.1260 -0.0815 0.0917 501 TYR B CG 8118 C CD1 . TYR B 501 ? 1.9699 1.4512 1.7868 -0.1400 -0.0802 0.0947 501 TYR B CD1 8119 C CD2 . TYR B 501 ? 2.0066 1.5553 1.8155 -0.1327 -0.0749 0.0884 501 TYR B CD2 8120 C CE1 . TYR B 501 ? 2.0316 1.5225 1.8609 -0.1609 -0.0729 0.0942 501 TYR B CE1 8121 C CE2 . TYR B 501 ? 2.0290 1.5885 1.8502 -0.1525 -0.0675 0.0885 501 TYR B CE2 8122 C CZ . TYR B 501 ? 2.0599 1.5911 1.8915 -0.1670 -0.0667 0.0913 501 TYR B CZ 8123 O OH . TYR B 501 ? 2.1003 1.6436 1.9457 -0.1875 -0.0600 0.0907 501 TYR B OH 8124 N N . ILE B 502 ? 1.5317 1.0251 1.2810 -0.0678 -0.0999 0.1215 502 ILE B N 8125 C CA . ILE B 502 ? 1.3267 0.8214 1.0647 -0.0468 -0.1096 0.1207 502 ILE B CA 8126 C C . ILE B 502 ? 1.2123 0.7406 0.9360 -0.0416 -0.1074 0.1227 502 ILE B C 8127 O O . ILE B 502 ? 1.2547 0.7901 0.9639 -0.0480 -0.0998 0.1382 502 ILE B O 8128 C CB . ILE B 502 ? 1.3513 0.8118 1.0756 -0.0380 -0.1148 0.1390 502 ILE B CB 8129 C CG1 . ILE B 502 ? 1.2650 0.7308 0.9780 -0.0158 -0.1259 0.1374 502 ILE B CG1 8130 C CG2 . ILE B 502 ? 1.4497 0.9042 1.1568 -0.0480 -0.1060 0.1632 502 ILE B CG2 8131 C CD1 . ILE B 502 ? 1.2206 0.6510 0.9282 -0.0040 -0.1342 0.1483 502 ILE B CD1 8132 N N . TRP B 503 ? 1.2604 0.8098 0.9891 -0.0302 -0.1136 0.1065 503 TRP B N 8133 C CA . TRP B 503 ? 1.4650 1.0453 1.1818 -0.0239 -0.1129 0.1052 503 TRP B CA 8134 C C . TRP B 503 ? 1.5812 1.1574 1.2818 -0.0049 -0.1234 0.1100 503 TRP B C 8135 O O . TRP B 503 ? 1.6251 1.2011 1.3347 0.0072 -0.1333 0.0976 503 TRP B O 8136 C CB . TRP B 503 ? 1.4939 1.1014 1.2276 -0.0248 -0.1129 0.0844 503 TRP B CB 8137 C CG . TRP B 503 ? 1.5328 1.1550 1.2775 -0.0422 -0.1022 0.0811 503 TRP B CG 8138 C CD1 . TRP B 503 ? 1.5697 1.2203 1.3106 -0.0472 -0.0949 0.0810 503 TRP B CD1 8139 C CD2 . TRP B 503 ? 1.5874 1.1977 1.3491 -0.0562 -0.0982 0.0765 503 TRP B CD2 8140 N NE1 . TRP B 503 ? 1.6991 1.3574 1.4544 -0.0633 -0.0868 0.0775 503 TRP B NE1 8141 C CE2 . TRP B 503 ? 1.6559 1.2900 1.4238 -0.0695 -0.0890 0.0744 503 TRP B CE2 8142 C CE3 . TRP B 503 ? 1.4945 1.0765 1.2670 -0.0582 -0.1020 0.0732 503 TRP B CE3 8143 C CZ2 . TRP B 503 ? 1.5282 1.1598 1.3124 -0.0852 -0.0841 0.0692 503 TRP B CZ2 8144 C CZ3 . TRP B 503 ? 1.4499 1.0280 1.2378 -0.0738 -0.0969 0.0672 503 TRP B CZ3 8145 C CH2 . TRP B 503 ? 1.5025 1.1059 1.2961 -0.0875 -0.0884 0.0653 503 TRP B CH2 8146 N N . LEU B 504 ? 1.5430 1.1172 1.2197 -0.0022 -0.1213 0.1281 504 LEU B N 8147 C CA . LEU B 504 ? 1.4794 1.0493 1.1381 0.0160 -0.1319 0.1343 504 LEU B CA 8148 C C . LEU B 504 ? 1.4436 1.0448 1.0889 0.0245 -0.1339 0.1285 504 LEU B C 8149 O O . LEU B 504 ? 1.3894 0.9930 1.0228 0.0405 -0.1446 0.1282 504 LEU B O 8150 C CB . LEU B 504 ? 1.4387 0.9828 1.0774 0.0164 -0.1304 0.1590 504 LEU B CB 8151 C CG . LEU B 504 ? 1.4558 0.9627 1.1050 0.0169 -0.1349 0.1641 504 LEU B CG 8152 C CD1 . LEU B 504 ? 1.4274 0.9082 1.0595 0.0119 -0.1297 0.1905 504 LEU B CD1 8153 C CD2 . LEU B 504 ? 1.4224 0.9232 1.0745 0.0365 -0.1499 0.1557 504 LEU B CD2 8154 N N . HIS B 505 ? 1.4218 1.0472 1.0702 0.0144 -0.1242 0.1229 505 HIS B N 8155 C CA . HIS B 505 ? 1.4590 1.1131 1.0932 0.0216 -0.1244 0.1182 505 HIS B CA 8156 C C . HIS B 505 ? 1.4603 1.1270 1.1000 0.0363 -0.1372 0.1007 505 HIS B C 8157 O O . HIS B 505 ? 1.6033 1.2588 1.2589 0.0417 -0.1459 0.0922 505 HIS B O 8158 C CB . HIS B 505 ? 1.5002 1.1776 1.1402 0.0084 -0.1116 0.1141 505 HIS B CB 8159 C CG . HIS B 505 ? 1.6063 1.2941 1.2739 0.0020 -0.1109 0.0953 505 HIS B CG 8160 N ND1 . HIS B 505 ? 1.6852 1.3615 1.3720 -0.0115 -0.1057 0.0940 505 HIS B ND1 8161 C CD2 . HIS B 505 ? 1.6243 1.3331 1.3029 0.0071 -0.1147 0.0774 505 HIS B CD2 8162 C CE1 . HIS B 505 ? 1.6871 1.3780 1.3941 -0.0137 -0.1063 0.0765 505 HIS B CE1 8163 N NE2 . HIS B 505 ? 1.6479 1.3581 1.3509 -0.0028 -0.1114 0.0670 505 HIS B NE2 8164 N N . ASP B 506 ? 1.4287 1.1192 1.0555 0.0428 -0.1381 0.0955 506 ASP B N 8165 C CA . ASP B 506 ? 1.4528 1.1578 1.0837 0.0559 -0.1501 0.0790 506 ASP B CA 8166 C C . ASP B 506 ? 1.4996 1.1904 1.1329 0.0693 -0.1651 0.0772 506 ASP B C 8167 O O . ASP B 506 ? 1.3364 1.0346 0.9887 0.0747 -0.1734 0.0609 506 ASP B O 8168 C CB . ASP B 506 ? 1.4174 1.1393 1.0737 0.0499 -0.1476 0.0601 506 ASP B CB 8169 C CG . ASP B 506 ? 1.5595 1.3040 1.2099 0.0439 -0.1375 0.0575 506 ASP B CG 8170 O OD1 . ASP B 506 ? 1.6300 1.3921 1.2734 0.0526 -0.1422 0.0479 506 ASP B OD1 8171 O OD2 . ASP B 506 ? 1.5637 1.3086 1.2168 0.0307 -0.1251 0.0648 506 ASP B OD2 8172 N N . ASN B 507 ? 1.5642 1.2358 1.1787 0.0749 -0.1682 0.0946 507 ASN B N 8173 C CA . ASN B 507 ? 1.5046 1.1629 1.1183 0.0895 -0.1828 0.0956 507 ASN B CA 8174 C C . ASN B 507 ? 1.5647 1.2263 1.1471 0.1026 -0.1902 0.1068 507 ASN B C 8175 O O . ASN B 507 ? 1.6599 1.3196 1.2183 0.0991 -0.1819 0.1231 507 ASN B O 8176 C CB . ASN B 507 ? 1.5321 1.1597 1.1547 0.0861 -0.1818 0.1064 507 ASN B CB 8177 C CG . ASN B 507 ? 1.5098 1.1334 1.1647 0.0832 -0.1839 0.0904 507 ASN B CG 8178 O OD1 . ASN B 507 ? 1.4551 1.0812 1.1260 0.0695 -0.1740 0.0840 507 ASN B OD1 8179 N ND2 . ASN B 507 ? 1.5226 1.1414 1.1871 0.0965 -0.1968 0.0840 507 ASN B ND2 8180 N N . PRO B 508 ? 1.6210 1.2888 1.2035 0.1180 -0.2059 0.0980 508 PRO B N 8181 C CA . PRO B 508 ? 1.6257 1.2993 1.1790 0.1328 -0.2162 0.1055 508 PRO B CA 8182 C C . PRO B 508 ? 1.5657 1.2139 1.1028 0.1407 -0.2210 0.1270 508 PRO B C 8183 O O . PRO B 508 ? 1.5490 1.1934 1.0874 0.1551 -0.2361 0.1253 508 PRO B O 8184 C CB . PRO B 508 ? 1.6146 1.3042 1.1835 0.1443 -0.2320 0.0850 508 PRO B CB 8185 C CG . PRO B 508 ? 1.6486 1.3280 1.2525 0.1391 -0.2319 0.0758 508 PRO B CG 8186 C CD . PRO B 508 ? 1.5964 1.2723 1.2090 0.1212 -0.2144 0.0774 508 PRO B CD 8187 N N . TRP B 509 ? 1.5248 1.1564 1.0475 0.1315 -0.2086 0.1475 509 TRP B N 8188 C CA . TRP B 509 ? 1.6484 1.2515 1.1581 0.1371 -0.2115 0.1698 509 TRP B CA 8189 C C . TRP B 509 ? 1.6835 1.2904 1.1586 0.1537 -0.2216 0.1833 509 TRP B C 8190 O O . TRP B 509 ? 1.6980 1.3228 1.1473 0.1540 -0.2169 0.1878 509 TRP B O 8191 C CB . TRP B 509 ? 1.7087 1.2925 1.2153 0.1204 -0.1945 0.1880 509 TRP B CB 8192 C CG . TRP B 509 ? 1.7106 1.2900 1.2486 0.1036 -0.1845 0.1762 509 TRP B CG 8193 C CD1 . TRP B 509 ? 1.6567 1.2541 1.2024 0.0889 -0.1717 0.1680 509 TRP B CD1 8194 C CD2 . TRP B 509 ? 1.7106 1.2669 1.2755 0.1005 -0.1867 0.1713 509 TRP B CD2 8195 N NE1 . TRP B 509 ? 1.5287 1.1162 1.1036 0.0768 -0.1664 0.1587 509 TRP B NE1 8196 C CE2 . TRP B 509 ? 1.5901 1.1524 1.1767 0.0835 -0.1752 0.1600 509 TRP B CE2 8197 C CE3 . TRP B 509 ? 1.7462 1.2780 1.3187 0.1114 -0.1974 0.1750 509 TRP B CE3 8198 C CZ2 . TRP B 509 ? 1.5844 1.1293 1.1983 0.0769 -0.1742 0.1517 509 TRP B CZ2 8199 C CZ3 . TRP B 509 ? 1.6813 1.1954 1.2820 0.1051 -0.1958 0.1663 509 TRP B CZ3 8200 C CH2 . TRP B 509 ? 1.5844 1.1051 1.2046 0.0879 -0.1843 0.1545 509 TRP B CH2 8201 N N . ASP B 510 ? 1.7085 1.2995 1.1827 0.1681 -0.2356 0.1897 510 ASP B N 8202 C CA . ASP B 510 ? 1.6299 1.2213 1.0704 0.1845 -0.2459 0.2056 510 ASP B CA 8203 C C . ASP B 510 ? 1.6879 1.2581 1.1030 0.1786 -0.2339 0.2356 510 ASP B C 8204 O O . ASP B 510 ? 1.6545 1.1939 1.0800 0.1734 -0.2298 0.2492 510 ASP B O 8205 C CB . ASP B 510 ? 1.5104 1.0910 0.9600 0.2022 -0.2648 0.2043 510 ASP B CB 8206 C CG . ASP B 510 ? 1.6603 1.2450 1.0745 0.2208 -0.2777 0.2192 510 ASP B CG 8207 O OD1 . ASP B 510 ? 1.7893 1.3484 1.1932 0.2290 -0.2819 0.2405 510 ASP B OD1 8208 O OD2 . ASP B 510 ? 1.5447 1.1577 0.9410 0.2278 -0.2839 0.2097 510 ASP B OD2 8209 N N . CYS B 511 ? 1.7701 1.3568 1.1522 0.1793 -0.2281 0.2458 511 CYS B N 8210 C CA . CYS B 511 ? 1.8700 1.4413 1.2279 0.1714 -0.2139 0.2747 511 CYS B CA 8211 C C . CYS B 511 ? 2.0567 1.6202 1.3772 0.1877 -0.2221 0.2991 511 CYS B C 8212 O O . CYS B 511 ? 2.0918 1.6552 1.3832 0.1839 -0.2109 0.3212 511 CYS B O 8213 C CB . CYS B 511 ? 1.7679 1.3620 1.1168 0.1572 -0.1966 0.2723 511 CYS B CB 8214 S SG . CYS B 511 ? 2.1585 1.7496 1.5485 0.1338 -0.1819 0.2569 511 CYS B SG 8215 N N . THR B 512 ? 2.1141 1.6721 1.4360 0.2058 -0.2415 0.2957 512 THR B N 8216 C CA . THR B 512 ? 2.2361 1.7837 1.5253 0.2226 -0.2512 0.3196 512 THR B CA 8217 C C . THR B 512 ? 2.3609 1.8672 1.6540 0.2173 -0.2446 0.3464 512 THR B C 8218 O O . THR B 512 ? 2.3845 1.8684 1.7103 0.2134 -0.2466 0.3396 512 THR B O 8219 C CB . THR B 512 ? 2.2843 1.8405 1.5774 0.2440 -0.2750 0.3063 512 THR B CB 8220 O OG1 . THR B 512 ? 2.2430 1.8317 1.5508 0.2442 -0.2809 0.2746 512 THR B OG1 8221 C CG2 . THR B 512 ? 2.3588 1.9192 1.6093 0.2629 -0.2858 0.3266 512 THR B CG2 8222 N N . CYS B 513 ? 2.4443 1.9403 1.7037 0.2177 -0.2368 0.3767 513 CYS B N 8223 C CA . CYS B 513 ? 2.5078 1.9644 1.7702 0.2074 -0.2258 0.4042 513 CYS B CA 8224 C C . CYS B 513 ? 2.5182 1.9372 1.8025 0.2152 -0.2368 0.4096 513 CYS B C 8225 O O . CYS B 513 ? 2.5849 1.9731 1.8905 0.2009 -0.2268 0.4171 513 CYS B O 8226 C CB . CYS B 513 ? 2.5434 1.9971 1.7634 0.2084 -0.2166 0.4379 513 CYS B CB 8227 S SG . CYS B 513 ? 2.4531 1.9168 1.6689 0.1815 -0.1882 0.4473 513 CYS B SG 8228 N N . PRO B 514 ? 2.4001 1.8218 1.6802 0.2379 -0.2576 0.4052 514 PRO B N 8229 C CA . PRO B 514 ? 2.3719 1.7578 1.6717 0.2471 -0.2677 0.4120 514 PRO B CA 8230 C C . PRO B 514 ? 2.3740 1.7415 1.7193 0.2336 -0.2626 0.3930 514 PRO B C 8231 O O . PRO B 514 ? 2.4405 1.7713 1.8005 0.2365 -0.2653 0.4033 514 PRO B O 8232 C CB . PRO B 514 ? 2.2410 1.6458 1.5360 0.2723 -0.2913 0.4002 514 PRO B CB 8233 C CG . PRO B 514 ? 2.2224 1.6619 1.4795 0.2786 -0.2930 0.4027 514 PRO B CG 8234 C CD . PRO B 514 ? 2.2608 1.7172 1.5177 0.2565 -0.2730 0.3951 514 PRO B CD 8235 N N . GLY B 515 ? 2.2047 1.5963 1.5711 0.2199 -0.2555 0.3663 515 GLY B N 8236 C CA . GLY B 515 ? 2.1393 1.5179 1.5470 0.2090 -0.2520 0.3464 515 GLY B CA 8237 C C . GLY B 515 ? 2.1359 1.5277 1.5602 0.1854 -0.2350 0.3315 515 GLY B C 8238 O O . GLY B 515 ? 1.9957 1.3804 1.4533 0.1764 -0.2324 0.3132 515 GLY B O 8239 N N . ILE B 516 ? 2.1828 1.5951 1.5837 0.1760 -0.2236 0.3391 516 ILE B N 8240 C CA . ILE B 516 ? 2.1057 1.5319 1.5204 0.1539 -0.2069 0.3277 516 ILE B CA 8241 C C . ILE B 516 ? 2.0759 1.4754 1.4869 0.1358 -0.1900 0.3517 516 ILE B C 8242 O O . ILE B 516 ? 1.7915 1.2015 1.2105 0.1164 -0.1747 0.3477 516 ILE B O 8243 C CB . ILE B 516 ? 2.0970 1.5653 1.4923 0.1538 -0.2036 0.3179 516 ILE B CB 8244 C CG1 . ILE B 516 ? 2.1116 1.5969 1.5277 0.1336 -0.1891 0.3007 516 ILE B CG1 8245 C CG2 . ILE B 516 ? 2.1534 1.6250 1.5079 0.1565 -0.1974 0.3453 516 ILE B CG2 8246 C CD1 . ILE B 516 ? 2.1419 1.6282 1.5964 0.1306 -0.1942 0.2733 516 ILE B CD1 8247 N N . ARG B 517 ? 2.2613 1.6261 1.6617 0.1422 -0.1932 0.3769 517 ARG B N 8248 C CA . ARG B 517 ? 2.3695 1.7039 1.7675 0.1255 -0.1784 0.4022 517 ARG B CA 8249 C C . ARG B 517 ? 2.4681 1.7823 1.9039 0.1071 -0.1709 0.3887 517 ARG B C 8250 O O . ARG B 517 ? 2.4917 1.8082 1.9344 0.0856 -0.1550 0.3917 517 ARG B O 8251 C CB . ARG B 517 ? 2.3427 1.6418 1.7221 0.1385 -0.1855 0.4320 517 ARG B CB 8252 C CG . ARG B 517 ? 2.3495 1.6159 1.7240 0.1215 -0.1702 0.4619 517 ARG B CG 8253 C CD . ARG B 517 ? 2.3921 1.6104 1.7683 0.1314 -0.1785 0.4822 517 ARG B CD 8254 N NE . ARG B 517 ? 2.4167 1.6145 1.8287 0.1346 -0.1878 0.4598 517 ARG B NE 8255 C CZ . ARG B 517 ? 2.3790 1.5488 1.8202 0.1172 -0.1799 0.4543 517 ARG B CZ 8256 N NH1 . ARG B 517 ? 2.4405 1.5990 1.8817 0.0943 -0.1629 0.4700 517 ARG B NH1 8257 N NH2 . ARG B 517 ? 2.2195 1.3736 1.6906 0.1227 -0.1890 0.4326 517 ARG B NH2 8258 N N . TYR B 518 ? 2.4499 1.7462 1.9102 0.1160 -0.1827 0.3733 518 TYR B N 8259 C CA . TYR B 518 ? 2.3231 1.5969 1.8179 0.1014 -0.1776 0.3600 518 TYR B CA 8260 C C . TYR B 518 ? 2.1583 1.4585 1.6692 0.0809 -0.1649 0.3413 518 TYR B C 8261 O O . TYR B 518 ? 2.0601 1.3441 1.5860 0.0608 -0.1531 0.3442 518 TYR B O 8262 C CB . TYR B 518 ? 2.2722 1.5369 1.7903 0.1168 -0.1926 0.3392 518 TYR B CB 8263 C CG . TYR B 518 ? 2.2457 1.4932 1.7986 0.1030 -0.1877 0.3209 518 TYR B CG 8264 C CD1 . TYR B 518 ? 2.2556 1.4596 1.8184 0.0936 -0.1828 0.3341 518 TYR B CD1 8265 C CD2 . TYR B 518 ? 2.1978 1.4725 1.7731 0.0993 -0.1881 0.2905 518 TYR B CD2 8266 C CE1 . TYR B 518 ? 2.2189 1.4075 1.8122 0.0813 -0.1789 0.3159 518 TYR B CE1 8267 C CE2 . TYR B 518 ? 2.1413 1.4018 1.7462 0.0874 -0.1838 0.2736 518 TYR B CE2 8268 C CZ . TYR B 518 ? 2.0987 1.3166 1.7120 0.0785 -0.1794 0.2857 518 TYR B CZ 8269 O OH . TYR B 518 ? 1.8880 1.0919 1.5295 0.0669 -0.1758 0.2676 518 TYR B OH 8270 N N . LEU B 519 ? 2.1144 1.4551 1.6230 0.0862 -0.1680 0.3219 519 LEU B N 8271 C CA . LEU B 519 ? 2.1690 1.5367 1.6939 0.0696 -0.1577 0.3021 519 LEU B CA 8272 C C . LEU B 519 ? 2.1758 1.5543 1.6848 0.0528 -0.1412 0.3192 519 LEU B C 8273 O O . LEU B 519 ? 2.0888 1.4743 1.6146 0.0334 -0.1294 0.3119 519 LEU B O 8274 C CB . LEU B 519 ? 2.1852 1.5914 1.7111 0.0811 -0.1661 0.2783 519 LEU B CB 8275 C CG . LEU B 519 ? 2.0575 1.4786 1.6151 0.0736 -0.1654 0.2489 519 LEU B CG 8276 C CD1 . LEU B 519 ? 1.9784 1.4345 1.5353 0.0865 -0.1748 0.2288 519 LEU B CD1 8277 C CD2 . LEU B 519 ? 1.9973 1.4270 1.5649 0.0503 -0.1490 0.2468 519 LEU B CD2 8278 N N . SER B 520 ? 2.2309 1.6122 1.7073 0.0608 -0.1406 0.3423 520 SER B N 8279 C CA . SER B 520 ? 2.1709 1.5653 1.6294 0.0469 -0.1245 0.3605 520 SER B CA 8280 C C . SER B 520 ? 2.1626 1.5234 1.6303 0.0280 -0.1127 0.3812 520 SER B C 8281 O O . SER B 520 ? 2.1228 1.4939 1.5998 0.0077 -0.0979 0.3823 520 SER B O 8282 C CB . SER B 520 ? 2.1372 1.5452 1.5562 0.0621 -0.1273 0.3792 520 SER B CB 8283 O OG . SER B 520 ? 2.1913 1.6151 1.5931 0.0490 -0.1105 0.3961 520 SER B OG 8284 N N . GLU B 521 ? 2.1689 1.4894 1.6352 0.0348 -0.1195 0.3975 521 GLU B N 8285 C CA . GLU B 521 ? 2.1863 1.4691 1.6651 0.0172 -0.1102 0.4154 521 GLU B CA 8286 C C . GLU B 521 ? 2.1135 1.3938 1.6293 -0.0003 -0.1060 0.3913 521 GLU B C 8287 O O . GLU B 521 ? 2.0682 1.3367 1.5972 -0.0223 -0.0935 0.3991 521 GLU B O 8288 C CB . GLU B 521 ? 2.2039 1.4414 1.6794 0.0303 -0.1210 0.4318 521 GLU B CB 8289 C CG . GLU B 521 ? 2.1994 1.4383 1.6387 0.0517 -0.1290 0.4538 521 GLU B CG 8290 C CD . GLU B 521 ? 2.1894 1.4237 1.6017 0.0427 -0.1155 0.4889 521 GLU B CD 8291 O OE1 . GLU B 521 ? 2.1537 1.3805 1.5780 0.0190 -0.0999 0.4977 521 GLU B OE1 8292 O OE2 . GLU B 521 ? 2.1624 1.4020 1.5414 0.0594 -0.1205 0.5080 521 GLU B OE2 8293 N N . TRP B 522 ? 2.0367 1.3295 1.5692 0.0096 -0.1167 0.3621 522 TRP B N 8294 C CA . TRP B 522 ? 1.8769 1.1692 1.4428 -0.0042 -0.1144 0.3375 522 TRP B CA 8295 C C . TRP B 522 ? 1.7538 1.0820 1.3260 -0.0224 -0.1011 0.3283 522 TRP B C 8296 O O . TRP B 522 ? 1.7123 1.0311 1.2999 -0.0436 -0.0903 0.3318 522 TRP B O 8297 C CB . TRP B 522 ? 1.8314 1.1287 1.4127 0.0121 -0.1288 0.3103 522 TRP B CB 8298 C CG . TRP B 522 ? 1.8125 1.0889 1.4259 0.0024 -0.1293 0.2922 522 TRP B CG 8299 C CD1 . TRP B 522 ? 1.8106 1.0445 1.4359 0.0056 -0.1352 0.2953 522 TRP B CD1 8300 C CD2 . TRP B 522 ? 1.8261 1.1233 1.4626 -0.0115 -0.1240 0.2678 522 TRP B CD2 8301 N NE1 . TRP B 522 ? 1.8518 1.0793 1.5056 -0.0055 -0.1337 0.2733 522 TRP B NE1 8302 C CE2 . TRP B 522 ? 1.8546 1.1212 1.5153 -0.0162 -0.1269 0.2568 522 TRP B CE2 8303 C CE3 . TRP B 522 ? 1.7292 1.0679 1.3680 -0.0196 -0.1173 0.2544 522 TRP B CE3 8304 C CZ2 . TRP B 522 ? 1.8079 1.0855 1.4931 -0.0288 -0.1235 0.2330 522 TRP B CZ2 8305 C CZ3 . TRP B 522 ? 1.6453 0.9939 1.3093 -0.0319 -0.1139 0.2322 522 TRP B CZ3 8306 C CH2 . TRP B 522 ? 1.7255 1.0446 1.4118 -0.0365 -0.1171 0.2218 522 TRP B CH2 8307 N N . ILE B 523 ? 1.7685 1.1373 1.3297 -0.0142 -0.1021 0.3166 523 ILE B N 8308 C CA . ILE B 523 ? 1.7792 1.1837 1.3474 -0.0292 -0.0903 0.3062 523 ILE B CA 8309 C C . ILE B 523 ? 1.8744 1.2746 1.4388 -0.0496 -0.0742 0.3287 523 ILE B C 8310 O O . ILE B 523 ? 1.7883 1.2037 1.3703 -0.0680 -0.0639 0.3208 523 ILE B O 8311 C CB . ILE B 523 ? 1.7003 1.1462 1.2488 -0.0167 -0.0919 0.2987 523 ILE B CB 8312 C CG1 . ILE B 523 ? 1.6894 1.1394 1.2373 0.0052 -0.1087 0.2813 523 ILE B CG1 8313 C CG2 . ILE B 523 ? 1.4906 0.9716 1.0525 -0.0305 -0.0815 0.2830 523 ILE B CG2 8314 C CD1 . ILE B 523 ? 1.6102 1.0844 1.1811 0.0042 -0.1117 0.2510 523 ILE B CD1 8315 N N . ASN B 524 ? 2.0414 1.4220 1.5829 -0.0460 -0.0721 0.3573 524 ASN B N 8316 C CA . ASN B 524 ? 2.0413 1.4181 1.5767 -0.0643 -0.0562 0.3827 524 ASN B CA 8317 C C . ASN B 524 ? 2.0513 1.3912 1.6125 -0.0838 -0.0519 0.3881 524 ASN B C 8318 O O . ASN B 524 ? 1.9839 1.3323 1.5594 -0.1059 -0.0389 0.3912 524 ASN B O 8319 C CB . ASN B 524 ? 2.0170 1.3865 1.5169 -0.0528 -0.0552 0.4128 524 ASN B CB 8320 C CG . ASN B 524 ? 1.9680 1.3800 1.4404 -0.0393 -0.0545 0.4102 524 ASN B CG 8321 O OD1 . ASN B 524 ? 1.8588 1.3072 1.3371 -0.0461 -0.0471 0.3953 524 ASN B OD1 8322 N ND2 . ASN B 524 ? 2.0102 1.4174 1.4520 -0.0195 -0.0626 0.4246 524 ASN B ND2 8323 N N . LYS B 525 ? 2.1054 1.4049 1.6734 -0.0754 -0.0632 0.3884 525 LYS B N 8324 C CA . LYS B 525 ? 2.1332 1.3939 1.7265 -0.0920 -0.0612 0.3903 525 LYS B CA 8325 C C . LYS B 525 ? 2.1450 1.4200 1.7698 -0.1052 -0.0604 0.3601 525 LYS B C 8326 O O . LYS B 525 ? 2.2051 1.4591 1.8526 -0.1244 -0.0557 0.3588 525 LYS B O 8327 C CB . LYS B 525 ? 2.1078 1.3228 1.7014 -0.0769 -0.0746 0.3948 525 LYS B CB 8328 C CG . LYS B 525 ? 2.1248 1.2924 1.7258 -0.0911 -0.0695 0.4180 525 LYS B CG 8329 C CD . LYS B 525 ? 2.0459 1.1675 1.6620 -0.0816 -0.0823 0.4103 525 LYS B CD 8330 C CE . LYS B 525 ? 1.9249 1.0383 1.5756 -0.0970 -0.0823 0.3834 525 LYS B CE 8331 N NZ . LYS B 525 ? 1.9065 0.9659 1.5729 -0.0955 -0.0897 0.3839 525 LYS B NZ 8332 N N . HIS B 526 ? 2.1052 1.4158 1.7309 -0.0948 -0.0655 0.3360 526 HIS B N 8333 C CA . HIS B 526 ? 2.0255 1.3549 1.6779 -0.1053 -0.0648 0.3077 526 HIS B CA 8334 C C . HIS B 526 ? 1.9749 1.3552 1.6206 -0.1053 -0.0588 0.2981 526 HIS B C 8335 O O . HIS B 526 ? 1.7602 1.1629 1.4082 -0.0928 -0.0662 0.2764 526 HIS B O 8336 C CB . HIS B 526 ? 1.9756 1.2921 1.6414 -0.0908 -0.0791 0.2835 526 HIS B CB 8337 C CG . HIS B 526 ? 2.0507 1.3181 1.7196 -0.0846 -0.0869 0.2922 526 HIS B CG 8338 N ND1 . HIS B 526 ? 2.1539 1.3863 1.8397 -0.1017 -0.0829 0.2982 526 HIS B ND1 8339 C CD2 . HIS B 526 ? 2.0633 1.3106 1.7215 -0.0626 -0.0990 0.2954 526 HIS B CD2 8340 C CE1 . HIS B 526 ? 2.2072 1.3983 1.8921 -0.0901 -0.0918 0.3049 526 HIS B CE1 8341 N NE2 . HIS B 526 ? 2.1594 1.3595 1.8277 -0.0660 -0.1017 0.3037 526 HIS B NE2 8342 N N . SER B 527 ? 2.1327 1.5309 1.7711 -0.1192 -0.0450 0.3146 527 SER B N 8343 C CA . SER B 527 ? 2.1905 1.6363 1.8211 -0.1188 -0.0379 0.3080 527 SER B CA 8344 C C . SER B 527 ? 2.2268 1.6967 1.8841 -0.1293 -0.0366 0.2817 527 SER B C 8345 O O . SER B 527 ? 2.2265 1.7300 1.8815 -0.1206 -0.0383 0.2654 527 SER B O 8346 C CB . SER B 527 ? 2.1706 1.6293 1.7872 -0.1310 -0.0224 0.3339 527 SER B CB 8347 O OG . SER B 527 ? 2.1884 1.6244 1.7790 -0.1218 -0.0230 0.3604 527 SER B OG 8348 N N . GLY B 528 ? 2.2235 1.6753 1.9057 -0.1477 -0.0339 0.2776 528 GLY B N 8349 C CA . GLY B 528 ? 2.0918 1.5653 1.7993 -0.1592 -0.0325 0.2544 528 GLY B CA 8350 C C . GLY B 528 ? 2.0098 1.4814 1.7280 -0.1464 -0.0453 0.2277 528 GLY B C 8351 O O . GLY B 528 ? 1.9310 1.4289 1.6640 -0.1500 -0.0451 0.2076 528 GLY B O 8352 N N . VAL B 529 ? 2.0484 1.4898 1.7595 -0.1311 -0.0561 0.2283 529 VAL B N 8353 C CA . VAL B 529 ? 1.9723 1.4090 1.6944 -0.1184 -0.0680 0.2045 529 VAL B CA 8354 C C . VAL B 529 ? 1.8447 1.3167 1.5585 -0.1023 -0.0725 0.1906 529 VAL B C 8355 O O . VAL B 529 ? 1.8562 1.3401 1.5844 -0.0983 -0.0778 0.1682 529 VAL B O 8356 C CB . VAL B 529 ? 1.4631 0.8573 1.1811 -0.1058 -0.0782 0.2103 529 VAL B CB 8357 C CG1 . VAL B 529 ? 1.4426 0.8352 1.1726 -0.0918 -0.0897 0.1858 529 VAL B CG1 8358 C CG2 . VAL B 529 ? 1.4570 0.8127 1.1860 -0.1220 -0.0746 0.2219 529 VAL B CG2 8359 N N . VAL B 530 ? 1.7657 1.2544 1.4563 -0.0936 -0.0700 0.2040 530 VAL B N 8360 C CA . VAL B 530 ? 1.7241 1.2433 1.4050 -0.0776 -0.0750 0.1921 530 VAL B CA 8361 C C . VAL B 530 ? 1.7809 1.3398 1.4697 -0.0857 -0.0672 0.1802 530 VAL B C 8362 O O . VAL B 530 ? 1.9072 1.4823 1.5901 -0.0964 -0.0559 0.1920 530 VAL B O 8363 C CB . VAL B 530 ? 1.6008 1.1220 1.2518 -0.0636 -0.0765 0.2099 530 VAL B CB 8364 C CG1 . VAL B 530 ? 1.4164 0.9614 1.0591 -0.0448 -0.0855 0.1950 530 VAL B CG1 8365 C CG2 . VAL B 530 ? 1.6596 1.1406 1.3014 -0.0577 -0.0822 0.2271 530 VAL B CG2 8366 N N . ARG B 531 ? 1.6239 1.1990 1.3264 -0.0801 -0.0729 0.1576 531 ARG B N 8367 C CA . ARG B 531 ? 1.4971 1.1084 1.2085 -0.0861 -0.0668 0.1454 531 ARG B CA 8368 C C . ARG B 531 ? 1.4672 1.1038 1.1642 -0.0700 -0.0705 0.1397 531 ARG B C 8369 O O . ARG B 531 ? 1.4611 1.0876 1.1453 -0.0541 -0.0798 0.1407 531 ARG B O 8370 C CB . ARG B 531 ? 1.4849 1.0988 1.2217 -0.0917 -0.0700 0.1245 531 ARG B CB 8371 C CG . ARG B 531 ? 1.5345 1.1281 1.2880 -0.1096 -0.0662 0.1261 531 ARG B CG 8372 C CD . ARG B 531 ? 1.5943 1.1939 1.3449 -0.1262 -0.0541 0.1432 531 ARG B CD 8373 N NE . ARG B 531 ? 1.6342 1.2291 1.4062 -0.1459 -0.0497 0.1388 531 ARG B NE 8374 C CZ . ARG B 531 ? 1.6897 1.2503 1.4704 -0.1547 -0.0517 0.1423 531 ARG B CZ 8375 N NH1 . ARG B 531 ? 1.6066 1.1338 1.3766 -0.1445 -0.0580 0.1511 531 ARG B NH1 8376 N NH2 . ARG B 531 ? 1.7199 1.2797 1.5206 -0.1733 -0.0481 0.1364 531 ARG B NH2 8377 N N . ASN B 532 ? 1.5337 1.2029 1.2334 -0.0737 -0.0637 0.1332 532 ASN B N 8378 C CA . ASN B 532 ? 1.6731 1.3664 1.3617 -0.0591 -0.0674 0.1249 532 ASN B CA 8379 C C . ASN B 532 ? 1.8334 1.5432 1.5407 -0.0554 -0.0724 0.1024 532 ASN B C 8380 O O . ASN B 532 ? 1.8082 1.5125 1.5361 -0.0637 -0.0730 0.0930 532 ASN B O 8381 C CB . ASN B 532 ? 1.6824 1.4009 1.3559 -0.0616 -0.0566 0.1348 532 ASN B CB 8382 C CG . ASN B 532 ? 1.6009 1.3448 1.2919 -0.0751 -0.0466 0.1282 532 ASN B CG 8383 O OD1 . ASN B 532 ? 1.6659 1.4027 1.3754 -0.0898 -0.0430 0.1276 532 ASN B OD1 8384 N ND2 . ASN B 532 ? 1.4002 1.1742 1.0852 -0.0696 -0.0424 0.1229 532 ASN B ND2 8385 N N . SER B 533 ? 1.8807 1.6105 1.5802 -0.0428 -0.0762 0.0940 533 SER B N 8386 C CA . SER B 533 ? 1.7940 1.5398 1.5099 -0.0382 -0.0810 0.0743 533 SER B CA 8387 C C . SER B 533 ? 1.6169 1.3827 1.3504 -0.0510 -0.0723 0.0676 533 SER B C 8388 O O . SER B 533 ? 1.4226 1.2029 1.1701 -0.0484 -0.0748 0.0529 533 SER B O 8389 C CB . SER B 533 ? 1.8081 1.5703 1.5111 -0.0231 -0.0862 0.0680 533 SER B CB 8390 O OG . SER B 533 ? 1.7735 1.5494 1.4933 -0.0190 -0.0908 0.0502 533 SER B OG 8391 N N . ALA B 534 ? 1.6424 1.4094 1.3758 -0.0648 -0.0622 0.0793 534 ALA B N 8392 C CA . ALA B 534 ? 1.5435 1.3307 1.2936 -0.0777 -0.0540 0.0747 534 ALA B CA 8393 C C . ALA B 534 ? 1.5942 1.3642 1.3601 -0.0923 -0.0529 0.0755 534 ALA B C 8394 O O . ALA B 534 ? 1.5651 1.3420 1.3495 -0.0974 -0.0543 0.0630 534 ALA B O 8395 C CB . ALA B 534 ? 1.4684 1.2759 1.2084 -0.0827 -0.0427 0.0861 534 ALA B CB 8396 N N . GLY B 535 ? 1.6293 1.3765 1.3875 -0.0988 -0.0507 0.0903 535 GLY B N 8397 C CA . GLY B 535 ? 1.6891 1.4152 1.4617 -0.1123 -0.0507 0.0909 535 GLY B CA 8398 C C . GLY B 535 ? 1.7668 1.4789 1.5348 -0.1259 -0.0429 0.1096 535 GLY B C 8399 O O . GLY B 535 ? 1.8015 1.4911 1.5806 -0.1371 -0.0437 0.1110 535 GLY B O 8400 N N . SER B 536 ? 1.7820 1.5073 1.5341 -0.1251 -0.0352 0.1240 536 SER B N 8401 C CA . SER B 536 ? 1.6962 1.4111 1.4436 -0.1385 -0.0262 0.1443 536 SER B CA 8402 C C . SER B 536 ? 1.6440 1.3308 1.3694 -0.1303 -0.0289 0.1614 536 SER B C 8403 O O . SER B 536 ? 1.4053 1.0885 1.1148 -0.1124 -0.0367 0.1589 536 SER B O 8404 C CB . SER B 536 ? 1.5606 1.3097 1.3062 -0.1457 -0.0136 0.1517 536 SER B CB 8405 O OG . SER B 536 ? 1.5100 1.2852 1.2449 -0.1305 -0.0145 0.1436 536 SER B OG 8406 N N . VAL B 537 ? 1.7800 1.4471 1.5057 -0.1438 -0.0228 0.1790 537 VAL B N 8407 C CA . VAL B 537 ? 1.8577 1.4953 1.5636 -0.1381 -0.0245 0.1983 537 VAL B CA 8408 C C . VAL B 537 ? 1.8687 1.5227 1.5464 -0.1224 -0.0231 0.2077 537 VAL B C 8409 O O . VAL B 537 ? 1.8788 1.5636 1.5505 -0.1250 -0.0133 0.2116 537 VAL B O 8410 C CB . VAL B 537 ? 1.8456 1.4660 1.5568 -0.1578 -0.0149 0.2185 537 VAL B CB 8411 C CG1 . VAL B 537 ? 1.8030 1.3817 1.5273 -0.1636 -0.0222 0.2172 537 VAL B CG1 8412 C CG2 . VAL B 537 ? 1.7629 1.4134 1.4925 -0.1762 -0.0035 0.2159 537 VAL B CG2 8413 N N . ALA B 538 ? 1.8533 1.4874 1.5137 -0.1056 -0.0333 0.2106 538 ALA B N 8414 C CA . ALA B 538 ? 1.8393 1.4881 1.4716 -0.0890 -0.0344 0.2171 538 ALA B CA 8415 C C . ALA B 538 ? 1.9138 1.5343 1.5283 -0.0730 -0.0460 0.2246 538 ALA B C 8416 O O . ALA B 538 ? 1.9720 1.5877 1.5908 -0.0599 -0.0586 0.2087 538 ALA B O 8417 C CB . ALA B 538 ? 1.6566 1.3385 1.2914 -0.0789 -0.0375 0.1959 538 ALA B CB 8418 N N . PRO B 539 ? 1.8453 1.4480 1.4409 -0.0741 -0.0418 0.2496 539 PRO B N 8419 C CA . PRO B 539 ? 1.8684 1.4471 1.4429 -0.0575 -0.0523 0.2604 539 PRO B CA 8420 C C . PRO B 539 ? 1.9638 1.5662 1.5112 -0.0384 -0.0570 0.2585 539 PRO B C 8421 O O . PRO B 539 ? 1.9241 1.5123 1.4550 -0.0220 -0.0683 0.2627 539 PRO B O 8422 C CB . PRO B 539 ? 1.8719 1.4271 1.4358 -0.0680 -0.0434 0.2897 539 PRO B CB 8423 C CG . PRO B 539 ? 1.8782 1.4369 1.4665 -0.0920 -0.0311 0.2899 539 PRO B CG 8424 C CD . PRO B 539 ? 1.8246 1.4235 1.4228 -0.0935 -0.0273 0.2695 539 PRO B CD 8425 N N . ASP B 540 ? 2.0706 1.7089 1.6140 -0.0402 -0.0487 0.2517 540 ASP B N 8426 C CA . ASP B 540 ? 2.1200 1.7831 1.6397 -0.0227 -0.0532 0.2456 540 ASP B CA 8427 C C . ASP B 540 ? 2.0376 1.7050 1.5685 -0.0094 -0.0682 0.2201 540 ASP B C 8428 O O . ASP B 540 ? 2.0227 1.6960 1.5352 0.0081 -0.0784 0.2158 540 ASP B O 8429 C CB . ASP B 540 ? 2.1341 1.8340 1.6494 -0.0286 -0.0395 0.2437 540 ASP B CB 8430 C CG . ASP B 540 ? 2.1430 1.8499 1.6292 -0.0292 -0.0280 0.2688 540 ASP B CG 8431 O OD1 . ASP B 540 ? 2.1727 1.8535 1.6444 -0.0280 -0.0294 0.2899 540 ASP B OD1 8432 O OD2 . ASP B 540 ? 2.0303 1.7693 1.5083 -0.0302 -0.0173 0.2676 540 ASP B OD2 8433 N N . SER B 541 ? 1.8967 1.5617 1.4581 -0.0184 -0.0693 0.2037 541 SER B N 8434 C CA . SER B 541 ? 1.6872 1.3592 1.2646 -0.0094 -0.0808 0.1790 541 SER B CA 8435 C C . SER B 541 ? 1.5883 1.2478 1.1551 0.0095 -0.0969 0.1755 541 SER B C 8436 O O . SER B 541 ? 1.5548 1.2316 1.1210 0.0213 -0.1053 0.1591 541 SER B O 8437 C CB . SER B 541 ? 1.6499 1.3108 1.2592 -0.0221 -0.0802 0.1679 541 SER B CB 8438 O OG . SER B 541 ? 1.6320 1.3083 1.2531 -0.0392 -0.0668 0.1689 541 SER B OG 8439 N N . ALA B 542 ? 1.4767 1.1062 1.0367 0.0122 -0.1015 0.1908 542 ALA B N 8440 C CA . ALA B 542 ? 1.5445 1.1624 1.0930 0.0309 -0.1169 0.1904 542 ALA B CA 8441 C C . ALA B 542 ? 1.7659 1.4003 1.2809 0.0437 -0.1188 0.1992 542 ALA B C 8442 O O . ALA B 542 ? 1.7857 1.4206 1.2800 0.0390 -0.1087 0.2191 542 ALA B O 8443 C CB . ALA B 542 ? 1.3824 0.9629 0.9328 0.0306 -0.1206 0.2055 542 ALA B CB 8444 N N . LYS B 543 ? 1.8493 1.4982 1.3593 0.0596 -0.1316 0.1841 543 LYS B N 8445 C CA . LYS B 543 ? 1.8880 1.5549 1.3660 0.0729 -0.1351 0.1885 543 LYS B CA 8446 C C . LYS B 543 ? 1.9489 1.6089 1.4152 0.0926 -0.1537 0.1865 543 LYS B C 8447 O O . LYS B 543 ? 2.0560 1.7006 1.5423 0.0967 -0.1641 0.1788 543 LYS B O 8448 C CB . LYS B 543 ? 1.7675 1.4678 1.2468 0.0727 -0.1312 0.1700 543 LYS B CB 8449 C CG . LYS B 543 ? 1.7331 1.4443 1.2303 0.0546 -0.1151 0.1669 543 LYS B CG 8450 C CD . LYS B 543 ? 1.6971 1.4228 1.1722 0.0484 -0.0996 0.1829 543 LYS B CD 8451 C CE . LYS B 543 ? 1.5868 1.3385 1.0774 0.0383 -0.0883 0.1695 543 LYS B CE 8452 N NZ . LYS B 543 ? 1.4914 1.2532 0.9746 0.0254 -0.0701 0.1859 543 LYS B NZ 8453 N N . CYS B 544 ? 1.8209 1.4941 1.2549 0.1052 -0.1579 0.1931 544 CYS B N 8454 C CA . CYS B 544 ? 1.7547 1.4231 1.1740 0.1243 -0.1758 0.1937 544 CYS B CA 8455 C C . CYS B 544 ? 1.6865 1.3807 1.1062 0.1365 -0.1886 0.1693 544 CYS B C 8456 O O . CYS B 544 ? 1.5737 1.2922 0.9868 0.1345 -0.1827 0.1585 544 CYS B O 8457 C CB . CYS B 544 ? 1.8834 1.5466 1.2633 0.1320 -0.1742 0.2196 544 CYS B CB 8458 S SG . CYS B 544 ? 2.4310 2.0592 1.8060 0.1206 -0.1622 0.2529 544 CYS B SG 8459 N N . SER B 545 ? 1.7807 1.4695 1.2088 0.1494 -0.2063 0.1607 545 SER B N 8460 C CA . SER B 545 ? 1.8379 1.5494 1.2665 0.1616 -0.2206 0.1387 545 SER B CA 8461 C C . SER B 545 ? 1.9060 1.6316 1.2942 0.1750 -0.2261 0.1460 545 SER B C 8462 O O . SER B 545 ? 1.7703 1.4900 1.1431 0.1895 -0.2403 0.1535 545 SER B O 8463 C CB . SER B 545 ? 1.8624 1.5651 1.3121 0.1717 -0.2382 0.1293 545 SER B CB 8464 O OG . SER B 545 ? 1.9302 1.6059 1.3989 0.1656 -0.2348 0.1398 545 SER B OG 8465 N N . GLY B 546 ? 2.0072 1.7525 1.3779 0.1710 -0.2152 0.1436 546 GLY B N 8466 C CA . GLY B 546 ? 2.0630 1.8248 1.3937 0.1839 -0.2193 0.1482 546 GLY B CA 8467 C C . GLY B 546 ? 2.0270 1.8021 1.3342 0.1768 -0.2007 0.1581 546 GLY B C 8468 O O . GLY B 546 ? 1.9448 1.7442 1.2401 0.1807 -0.1995 0.1433 546 GLY B O 8469 N N . SER B 547 ? 2.0682 1.8274 1.3693 0.1664 -0.1859 0.1831 547 SER B N 8470 C CA . SER B 547 ? 2.0415 1.8137 1.3225 0.1585 -0.1666 0.1951 547 SER B CA 8471 C C . SER B 547 ? 2.0243 1.8012 1.3362 0.1402 -0.1513 0.1858 547 SER B C 8472 O O . SER B 547 ? 1.9855 1.7855 1.2911 0.1369 -0.1404 0.1785 547 SER B O 8473 C CB . SER B 547 ? 2.0147 1.7693 1.2713 0.1564 -0.1580 0.2290 547 SER B CB 8474 O OG . SER B 547 ? 1.9291 1.6523 1.2089 0.1486 -0.1592 0.2406 547 SER B OG 8475 N N . GLY B 548 ? 2.0369 1.7929 1.3821 0.1293 -0.1511 0.1855 548 GLY B N 8476 C CA . GLY B 548 ? 1.9605 1.7185 1.3351 0.1114 -0.1371 0.1793 548 GLY B CA 8477 C C . GLY B 548 ? 1.9502 1.6929 1.3214 0.0973 -0.1212 0.2055 548 GLY B C 8478 O O . GLY B 548 ? 1.8392 1.5854 1.2296 0.0811 -0.1072 0.2053 548 GLY B O 8479 N N . LYS B 549 ? 2.0591 1.7850 1.4059 0.1035 -0.1239 0.2284 549 LYS B N 8480 C CA . LYS B 549 ? 2.0866 1.7961 1.4266 0.0911 -0.1094 0.2565 549 LYS B CA 8481 C C . LYS B 549 ? 2.0333 1.7135 1.4066 0.0778 -0.1088 0.2588 549 LYS B C 8482 O O . LYS B 549 ? 2.0379 1.6989 1.4234 0.0852 -0.1231 0.2528 549 LYS B O 8483 C CB . LYS B 549 ? 2.0899 1.7884 1.3928 0.1033 -0.1137 0.2814 549 LYS B CB 8484 C CG . LYS B 549 ? 1.9968 1.7236 1.2606 0.1135 -0.1091 0.2863 549 LYS B CG 8485 C CD . LYS B 549 ? 1.9631 1.6775 1.1899 0.1262 -0.1144 0.3120 549 LYS B CD 8486 C CE . LYS B 549 ? 1.8227 1.5671 1.0083 0.1407 -0.1143 0.3122 549 LYS B CE 8487 N NZ . LYS B 549 ? 1.7183 1.4528 0.8695 0.1583 -0.1270 0.3295 549 LYS B NZ 8488 N N . PRO B 550 ? 2.0098 1.6882 1.3986 0.0584 -0.0923 0.2665 550 PRO B N 8489 C CA . PRO B 550 ? 2.0922 1.7413 1.5088 0.0440 -0.0897 0.2721 550 PRO B CA 8490 C C . PRO B 550 ? 2.0678 1.6814 1.4755 0.0506 -0.0984 0.2913 550 PRO B C 8491 O O . PRO B 550 ? 2.0715 1.6772 1.4526 0.0525 -0.0934 0.3166 550 PRO B O 8492 C CB . PRO B 550 ? 2.1438 1.8003 1.5636 0.0245 -0.0694 0.2863 550 PRO B CB 8493 C CG . PRO B 550 ? 2.0603 1.7564 1.4721 0.0270 -0.0628 0.2726 550 PRO B CG 8494 C CD . PRO B 550 ? 1.9728 1.6807 1.3574 0.0492 -0.0760 0.2654 550 PRO B CD 8495 N N . VAL B 551 ? 2.0609 1.6539 1.4910 0.0544 -0.1109 0.2794 551 VAL B N 8496 C CA . VAL B 551 ? 2.1337 1.6933 1.5586 0.0637 -0.1215 0.2936 551 VAL B CA 8497 C C . VAL B 551 ? 2.2458 1.7771 1.6649 0.0516 -0.1105 0.3229 551 VAL B C 8498 O O . VAL B 551 ? 2.2592 1.7661 1.6617 0.0610 -0.1167 0.3426 551 VAL B O 8499 C CB . VAL B 551 ? 2.0902 1.6326 1.5472 0.0660 -0.1332 0.2746 551 VAL B CB 8500 C CG1 . VAL B 551 ? 2.1489 1.6610 1.5991 0.0802 -0.1464 0.2868 551 VAL B CG1 8501 C CG2 . VAL B 551 ? 1.9840 1.5546 1.4528 0.0740 -0.1419 0.2453 551 VAL B CG2 8502 N N . ARG B 552 ? 2.2925 1.8269 1.7263 0.0306 -0.0944 0.3259 552 ARG B N 8503 C CA . ARG B 552 ? 2.2750 1.7827 1.7085 0.0158 -0.0830 0.3524 552 ARG B CA 8504 C C . ARG B 552 ? 2.3088 1.8283 1.7082 0.0158 -0.0717 0.3789 552 ARG B C 8505 O O . ARG B 552 ? 2.4259 1.9240 1.8205 0.0048 -0.0619 0.4051 552 ARG B O 8506 C CB . ARG B 552 ? 2.1508 1.6569 1.6168 -0.0076 -0.0714 0.3442 552 ARG B CB 8507 C CG . ARG B 552 ? 2.0786 1.6246 1.5545 -0.0142 -0.0641 0.3237 552 ARG B CG 8508 C CD . ARG B 552 ? 2.1367 1.7112 1.5880 -0.0169 -0.0504 0.3381 552 ARG B CD 8509 N NE . ARG B 552 ? 2.1851 1.7841 1.6555 -0.0347 -0.0365 0.3295 552 ARG B NE 8510 C CZ . ARG B 552 ? 2.2647 1.8562 1.7481 -0.0555 -0.0226 0.3442 552 ARG B CZ 8511 N NH1 . ARG B 552 ? 2.2799 1.8378 1.7588 -0.0617 -0.0203 0.3686 552 ARG B NH1 8512 N NH2 . ARG B 552 ? 2.2478 1.8652 1.7495 -0.0702 -0.0112 0.3347 552 ARG B NH2 8513 N N . SER B 553 ? 2.1816 1.7354 1.5578 0.0280 -0.0729 0.3718 553 SER B N 8514 C CA . SER B 553 ? 2.1302 1.6988 1.4699 0.0318 -0.0635 0.3950 553 SER B CA 8515 C C . SER B 553 ? 2.1876 1.7326 1.4997 0.0487 -0.0747 0.4158 553 SER B C 8516 O O . SER B 553 ? 2.2862 1.8208 1.5752 0.0464 -0.0659 0.4461 553 SER B O 8517 C CB . SER B 553 ? 1.9961 1.6080 1.3192 0.0418 -0.0631 0.3776 553 SER B CB 8518 O OG . SER B 553 ? 1.8882 1.5042 1.1919 0.0648 -0.0811 0.3681 553 SER B OG 8519 N N . ILE B 554 ? 2.0981 1.6354 1.4141 0.0657 -0.0941 0.3997 554 ILE B N 8520 C CA . ILE B 554 ? 2.1262 1.6474 1.4160 0.0859 -0.1083 0.4144 554 ILE B CA 8521 C C . ILE B 554 ? 2.2633 1.7413 1.5512 0.0820 -0.1066 0.4448 554 ILE B C 8522 O O . ILE B 554 ? 2.1947 1.6439 1.5132 0.0697 -0.1052 0.4432 554 ILE B O 8523 C CB . ILE B 554 ? 2.0105 1.5342 1.3125 0.1032 -0.1295 0.3879 554 ILE B CB 8524 C CG1 . ILE B 554 ? 1.8479 1.4133 1.1472 0.1084 -0.1317 0.3608 554 ILE B CG1 8525 C CG2 . ILE B 554 ? 2.1007 1.6084 1.3783 0.1246 -0.1455 0.4026 554 ILE B CG2 8526 C CD1 . ILE B 554 ? 1.8102 1.3856 1.1034 0.1303 -0.1530 0.3430 554 ILE B CD1 8527 N N . ILE B 555 ? 2.4151 1.8888 1.6660 0.0931 -0.1070 0.4722 555 ILE B N 8528 C CA . ILE B 555 ? 2.5140 1.9471 1.7578 0.0911 -0.1052 0.5050 555 ILE B CA 8529 C C . ILE B 555 ? 2.5077 1.9266 1.7282 0.1166 -0.1244 0.5148 555 ILE B C 8530 O O . ILE B 555 ? 2.5366 1.9753 1.7191 0.1315 -0.1276 0.5258 555 ILE B O 8531 C CB . ILE B 555 ? 2.0361 1.4734 1.2560 0.0783 -0.0847 0.5372 555 ILE B CB 8532 C CG1 . ILE B 555 ? 1.9186 1.3805 1.1580 0.0554 -0.0657 0.5263 555 ILE B CG1 8533 C CG2 . ILE B 555 ? 2.0594 1.4500 1.2781 0.0726 -0.0813 0.5716 555 ILE B CG2 8534 C CD1 . ILE B 555 ? 1.8674 1.3074 1.1527 0.0355 -0.0623 0.5127 555 ILE B CD1 8535 N N . CYS B 556 ? 2.4718 1.8572 1.7149 0.1221 -0.1373 0.5105 556 CYS B N 8536 C CA . CYS B 556 ? 2.5107 1.8830 1.7372 0.1470 -0.1570 0.5173 556 CYS B CA 8537 C C . CYS B 556 ? 2.5862 1.9121 1.8068 0.1473 -0.1561 0.5514 556 CYS B C 8538 O O . CYS B 556 ? 2.5320 1.8228 1.7837 0.1386 -0.1562 0.5499 556 CYS B O 8539 C CB . CYS B 556 ? 2.5238 1.8965 1.7802 0.1572 -0.1745 0.4849 556 CYS B CB 8540 S SG . CYS B 556 ? 2.9189 2.3418 2.1871 0.1560 -0.1763 0.4442 556 CYS B SG 8541 N N . PRO B 557 ? 2.7226 2.0483 1.9027 0.1580 -0.1554 0.5822 557 PRO B N 8542 C CA . PRO B 557 ? 2.8147 2.0993 1.9804 0.1594 -0.1528 0.6211 557 PRO B CA 8543 C C . PRO B 557 ? 2.8002 2.0523 1.9701 0.1806 -0.1736 0.6255 557 PRO B C 8544 O O . PRO B 557 ? 2.8129 2.0821 1.9830 0.2005 -0.1923 0.6042 557 PRO B O 8545 C CB . PRO B 557 ? 2.8490 2.1577 1.9653 0.1669 -0.1462 0.6471 557 PRO B CB 8546 C CG . PRO B 557 ? 2.7651 2.1252 1.8756 0.1627 -0.1400 0.6213 557 PRO B CG 8547 C CD . PRO B 557 ? 2.6843 2.0542 1.8274 0.1676 -0.1543 0.5809 557 PRO B CD 8548 N N . CYS C 1 ? 0.9042 0.8142 0.7701 0.0634 -0.4197 -0.1288 11 CYS C N 8549 C CA . CYS C 1 ? 0.8568 0.7777 0.7327 0.0644 -0.4201 -0.1284 11 CYS C CA 8550 C C . CYS C 1 ? 0.8674 0.8198 0.7469 0.0662 -0.4166 -0.1304 11 CYS C C 8551 O O . CYS C 1 ? 0.9095 0.8736 0.7831 0.0668 -0.4153 -0.1296 11 CYS C O 8552 C CB . CYS C 1 ? 0.8679 0.7761 0.7434 0.0643 -0.4259 -0.1154 11 CYS C CB 8553 S SG . CYS C 1 ? 1.0695 0.9407 0.9367 0.0621 -0.4311 -0.1106 11 CYS C SG 8554 N N . SER C 2 ? 0.8241 0.7904 0.7133 0.0672 -0.4150 -0.1326 12 SER C N 8555 C CA . SER C 2 ? 1.0416 1.0374 0.9327 0.0691 -0.4116 -0.1338 12 SER C CA 8556 C C . SER C 2 ? 1.2553 1.2584 1.1517 0.0711 -0.4129 -0.1239 12 SER C C 8557 O O . SER C 2 ? 1.2864 1.2763 1.1898 0.0705 -0.4152 -0.1208 12 SER C O 8558 C CB . SER C 2 ? 0.8647 0.8774 0.7624 0.0686 -0.4057 -0.1488 12 SER C CB 8559 O OG . SER C 2 ? 0.9441 0.9423 0.8504 0.0668 -0.4046 -0.1551 12 SER C OG 8560 N N . LYS C 3 ? 1.2744 1.2985 1.1678 0.0737 -0.4114 -0.1187 13 LYS C N 8561 C CA . LYS C 3 ? 1.2986 1.3332 1.1978 0.0764 -0.4109 -0.1104 13 LYS C CA 8562 C C . LYS C 3 ? 1.4342 1.4828 1.3424 0.0765 -0.4065 -0.1193 13 LYS C C 8563 O O . LYS C 3 ? 1.5378 1.5896 1.4478 0.0743 -0.4036 -0.1319 13 LYS C O 8564 C CB . LYS C 3 ? 1.3357 1.3893 1.2289 0.0797 -0.4094 -0.1024 13 LYS C CB 8565 C CG . LYS C 3 ? 1.3329 1.3730 1.2186 0.0791 -0.4127 -0.0930 13 LYS C CG 8566 C CD . LYS C 3 ? 1.2299 1.2901 1.1084 0.0810 -0.4101 -0.0906 13 LYS C CD 8567 C CE . LYS C 3 ? 1.0812 1.1507 0.9555 0.0793 -0.4083 -0.1041 13 LYS C CE 8568 N NZ . LYS C 3 ? 0.9208 1.0044 0.7879 0.0804 -0.4073 -0.1011 13 LYS C NZ 8569 N N . LYS C 4 ? 1.4661 1.5228 1.3812 0.0789 -0.4051 -0.1132 14 LYS C N 8570 C CA . LYS C 4 ? 1.5317 1.5972 1.4570 0.0783 -0.4007 -0.1207 14 LYS C CA 8571 C C . LYS C 4 ? 1.8171 1.9101 1.7394 0.0789 -0.3946 -0.1304 14 LYS C C 8572 O O . LYS C 4 ? 1.9002 1.9991 1.8167 0.0772 -0.3936 -0.1400 14 LYS C O 8573 C CB . LYS C 4 ? 1.3832 1.4456 1.3179 0.0807 -0.4010 -0.1110 14 LYS C CB 8574 C CG . LYS C 4 ? 1.3277 1.3929 1.2754 0.0792 -0.3967 -0.1175 14 LYS C CG 8575 C CD . LYS C 4 ? 1.2843 1.3385 1.2369 0.0746 -0.3962 -0.1287 14 LYS C CD 8576 C CE . LYS C 4 ? 1.2971 1.3530 1.2647 0.0728 -0.3913 -0.1338 14 LYS C CE 8577 N NZ . LYS C 4 ? 1.3145 1.3689 1.2875 0.0686 -0.3874 -0.1472 14 LYS C NZ 8578 N N . LYS C 5 ? 1.9046 2.0140 1.8308 0.0814 -0.3905 -0.1285 15 LYS C N 8579 C CA . LYS C 5 ? 1.9053 2.0409 1.8284 0.0818 -0.3846 -0.1382 15 LYS C CA 8580 C C . LYS C 5 ? 1.9631 2.1187 1.8817 0.0870 -0.3821 -0.1295 15 LYS C C 8581 O O . LYS C 5 ? 1.9402 2.1144 1.8599 0.0878 -0.3765 -0.1349 15 LYS C O 8582 C CB . LYS C 5 ? 1.8238 1.9605 1.7583 0.0782 -0.3794 -0.1497 15 LYS C CB 8583 C CG . LYS C 5 ? 1.7102 1.8232 1.6536 0.0740 -0.3813 -0.1543 15 LYS C CG 8584 C CD . LYS C 5 ? 1.6643 1.7745 1.6023 0.0715 -0.3821 -0.1643 15 LYS C CD 8585 C CE . LYS C 5 ? 1.6284 1.7569 1.5698 0.0687 -0.3749 -0.1809 15 LYS C CE 8586 N NZ . LYS C 5 ? 1.5267 1.6481 1.4676 0.0661 -0.3747 -0.1917 15 LYS C NZ 8587 N N . LYS C 6 ? 1.9717 2.1231 1.8856 0.0905 -0.3856 -0.1161 16 LYS C N 8588 C CA . LYS C 6 ? 1.8677 2.0375 1.7776 0.0963 -0.3828 -0.1063 16 LYS C CA 8589 C C . LYS C 6 ? 1.7305 1.9121 1.6286 0.0984 -0.3846 -0.1016 16 LYS C C 8590 O O . LYS C 6 ? 1.6545 1.8544 1.5480 0.1034 -0.3819 -0.0939 16 LYS C O 8591 C CB . LYS C 6 ? 1.8134 1.9700 1.7321 0.0996 -0.3835 -0.0928 16 LYS C CB 8592 C CG . LYS C 6 ? 1.7744 1.9249 1.7056 0.0991 -0.3803 -0.0951 16 LYS C CG 8593 C CD . LYS C 6 ? 1.7270 1.8635 1.6682 0.1024 -0.3815 -0.0820 16 LYS C CD 8594 C CE . LYS C 6 ? 1.6302 1.7557 1.5859 0.1009 -0.3795 -0.0847 16 LYS C CE 8595 N NZ . LYS C 6 ? 1.5038 1.6131 1.4709 0.1037 -0.3817 -0.0730 16 LYS C NZ 8596 O OXT . LYS C 6 ? 1.6821 1.8547 1.5755 0.0953 -0.3883 -0.1050 16 LYS C OXT 8868 C C01 . PXS X . ? 1.5931 1.3537 1.6503 0.0605 -0.5067 -0.0455 581 PXS C C01 8869 C C02 . PXS X . ? 1.3725 1.1421 1.4118 0.0612 -0.5015 -0.0494 581 PXS C C02 8870 C C03 . PXS X . ? 1.0853 0.8435 1.1048 0.0614 -0.5097 -0.0453 581 PXS C C03 8871 C C04 . PXS X . ? 0.9199 0.6882 0.9249 0.0620 -0.5041 -0.0479 581 PXS C C04 8872 C C05 . PXS X . ? 0.7830 0.5379 0.7649 0.0611 -0.5086 -0.0469 581 PXS C C05 8873 C C06 . PXS X . ? 0.7478 0.5122 0.7158 0.0614 -0.5025 -0.0492 581 PXS C C06 8874 C C07 . PXS X . ? 0.9498 0.7069 0.8992 0.0604 -0.4990 -0.0547 581 PXS C C07 8875 C C08 . PXS X . ? 0.8767 0.6387 0.8107 0.0601 -0.4951 -0.0551 581 PXS C C08 8876 C C09 . PXS X . ? 0.7875 0.5460 0.7070 0.0595 -0.4893 -0.0620 581 PXS C C09 8877 C C10 . PXS X . ? 0.8666 0.6283 0.7715 0.0589 -0.4860 -0.0617 581 PXS C C10 8878 C C11 . PXS X . ? 0.9117 0.6583 0.7994 0.0576 -0.4841 -0.0658 581 PXS C C11 8879 C C12 . PXS X . ? 0.9372 0.6912 0.8141 0.0571 -0.4780 -0.0679 581 PXS C C12 8880 C C13 . PXS X . ? 0.9853 0.7318 0.8526 0.0569 -0.4726 -0.0760 581 PXS C C13 8881 C C14 . PXS X . ? 0.8718 0.6203 0.7270 0.0560 -0.4676 -0.0775 581 PXS C C14 8882 C C15 . PXS X . ? 0.8227 0.5831 0.6798 0.0572 -0.4592 -0.0880 581 PXS C C15 8883 C C16 . PXS X . ? 0.8726 0.6614 0.7359 0.0584 -0.4536 -0.0902 581 PXS C C16 8884 O O17 . PXS X . ? 0.8923 0.6977 0.7625 0.0597 -0.4467 -0.1005 581 PXS C O17 8885 C C18 . PXS X . ? 0.9677 0.7906 0.8350 0.0601 -0.4414 -0.1038 581 PXS C C18 8886 C C19 . PXS X . ? 1.0779 0.9117 0.9486 0.0609 -0.4342 -0.1167 581 PXS C C19 8887 C C20 . PXS X . ? 1.0874 0.9496 0.9642 0.0621 -0.4304 -0.1193 581 PXS C C20 8888 O O21 . PXS X . ? 1.1063 0.9335 0.9849 0.0612 -0.4336 -0.1216 581 PXS C O21 8889 C C22 . PXS X . ? 1.0166 0.8229 0.8904 0.0610 -0.4322 -0.1266 581 PXS C C22 8890 C C23 . PXS X . ? 0.9647 0.7675 0.8502 0.0618 -0.4293 -0.1336 581 PXS C C23 8891 C C24 . PXS X . ? 0.9217 0.6952 0.8022 0.0620 -0.4328 -0.1305 581 PXS C C24 8892 C C25 . PXS X . ? 0.9717 0.7308 0.8487 0.0612 -0.4424 -0.1184 581 PXS C C25 8893 C C26 . PXS X . ? 0.8816 0.6578 0.7676 0.0608 -0.4463 -0.1119 581 PXS C C26 8894 C C27 . PXS X . ? 0.8025 0.5824 0.7047 0.0613 -0.4471 -0.1120 581 PXS C C27 8895 C C28 . PXS X . ? 0.8560 0.6216 0.7590 0.0608 -0.4567 -0.1014 581 PXS C C28 8896 C C29 . PXS X . ? 0.8906 0.6712 0.8029 0.0607 -0.4602 -0.0949 581 PXS C C29 8897 C C30 . PXS X . ? 0.8549 0.6386 0.7851 0.0609 -0.4620 -0.0932 581 PXS C C30 8898 C C31 . PXS X . ? 0.9907 0.7705 0.9256 0.0608 -0.4707 -0.0828 581 PXS C C31 8899 C C32 . PXS X . ? 1.0486 0.8302 1.0027 0.0609 -0.4726 -0.0809 581 PXS C C32 8900 C C33 . PXS X . ? 1.0612 0.8335 1.0219 0.0608 -0.4704 -0.0852 581 PXS C C33 8901 C C34 . PXS X . ? 1.0906 0.8615 1.0706 0.0606 -0.4736 -0.0812 581 PXS C C34 8902 C C35 . PXS X . ? 1.1651 0.9535 1.1651 0.0601 -0.4641 -0.0876 581 PXS C C35 8903 C C36 . PXS X . ? 1.1754 0.9792 1.1900 0.0599 -0.4633 -0.0847 581 PXS C C36 8904 C C37 . PXS X . ? 1.2670 1.0858 1.3018 0.0588 -0.4535 -0.0909 581 PXS C C37 8905 O O38 . PXS X . ? 0.9303 0.7236 0.7926 0.0604 -0.4322 -0.1259 581 PXS C O38 8906 O O39 . PXS X . ? 0.9241 0.7208 0.7861 0.0582 -0.4547 -0.0833 581 PXS C O39 # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 MET 1 1 ? ? ? A . n A 1 2 LEU 2 2 ? ? ? A . n A 1 3 ARG 3 3 ? ? ? A . n A 1 4 ALA 4 4 ? ? ? A . n A 1 5 LEU 5 5 ? ? ? A . n A 1 6 TRP 6 6 ? ? ? A . n A 1 7 LEU 7 7 ? ? ? A . n A 1 8 PHE 8 8 ? ? ? A . n A 1 9 TRP 9 9 ? ? ? A . n A 1 10 ILE 10 10 ? ? ? A . n A 1 11 LEU 11 11 ? ? ? A . n A 1 12 VAL 12 12 ? ? ? A . n A 1 13 ALA 13 13 ? ? ? A . n A 1 14 ILE 14 14 ? ? ? A . n A 1 15 THR 15 15 ? ? ? A . n A 1 16 VAL 16 16 ? ? ? A . n A 1 17 LEU 17 17 ? ? ? A . n A 1 18 PHE 18 18 ? ? ? A . n A 1 19 SER 19 19 ? ? ? A . n A 1 20 LYS 20 20 ? ? ? A . n A 1 21 ARG 21 21 ? ? ? A . n A 1 22 CYS 22 22 ? ? ? A . n A 1 23 SER 23 23 ? ? ? A . n A 1 24 ALA 24 24 ? ? ? A . n A 1 25 GLN 25 25 ? ? ? A . n A 1 26 GLU 26 26 26 GLU GLU A . n A 1 27 SER 27 27 27 SER SER A . n A 1 28 LEU 28 28 28 LEU LEU A . n A 1 29 SER 29 29 29 SER SER A . n A 1 30 CYS 30 30 30 CYS CYS A . n A 1 31 ASP 31 31 31 ASP ASP A . n A 1 32 ALA 32 32 32 ALA ALA A . n A 1 33 SER 33 33 33 SER SER A . n A 1 34 GLY 34 34 34 GLY GLY A . n A 1 35 VAL 35 35 35 VAL VAL A . n A 1 36 CYS 36 36 36 CYS CYS A . n A 1 37 ASP 37 37 37 ASP ASP A . n A 1 38 GLY 38 38 38 GLY GLY A . n A 1 39 ARG 39 39 39 ARG ARG A . n A 1 40 SER 40 40 40 SER SER A . n A 1 41 ARG 41 41 41 ARG ARG A . n A 1 42 SER 42 42 42 SER SER A . n A 1 43 PHE 43 43 43 PHE PHE A . n A 1 44 THR 44 44 44 THR THR A . n A 1 45 SER 45 45 45 SER SER A . n A 1 46 ILE 46 46 46 ILE ILE A . n A 1 47 PRO 47 47 47 PRO PRO A . n A 1 48 SER 48 48 48 SER SER A . n A 1 49 GLY 49 49 49 GLY GLY A . n A 1 50 LEU 50 50 50 LEU LEU A . n A 1 51 THR 51 51 51 THR THR A . n A 1 52 ALA 52 52 52 ALA ALA A . n A 1 53 ALA 53 53 53 ALA ALA A . n A 1 54 MET 54 54 54 MET MET A . n A 1 55 LYS 55 55 55 LYS LYS A . n A 1 56 SER 56 56 56 SER SER A . n A 1 57 LEU 57 57 57 LEU LEU A . n A 1 58 ASP 58 58 58 ASP ASP A . n A 1 59 LEU 59 59 59 LEU LEU A . n A 1 60 SER 60 60 60 SER SER A . n A 1 61 PHE 61 61 61 PHE PHE A . n A 1 62 ASN 62 62 62 ASN ASN A . n A 1 63 LYS 63 63 63 LYS LYS A . n A 1 64 ILE 64 64 64 ILE ILE A . n A 1 65 THR 65 65 65 THR THR A . n A 1 66 TYR 66 66 66 TYR TYR A . n A 1 67 ILE 67 67 67 ILE ILE A . n A 1 68 GLY 68 68 68 GLY GLY A . n A 1 69 HIS 69 69 69 HIS HIS A . n A 1 70 GLY 70 70 70 GLY GLY A . n A 1 71 ASP 71 71 71 ASP ASP A . n A 1 72 LEU 72 72 72 LEU LEU A . n A 1 73 ARG 73 73 73 ARG ARG A . n A 1 74 ALA 74 74 74 ALA ALA A . n A 1 75 CYS 75 75 75 CYS CYS A . n A 1 76 ALA 76 76 76 ALA ALA A . n A 1 77 ASN 77 77 77 ASN ASN A . n A 1 78 LEU 78 78 78 LEU LEU A . n A 1 79 GLN 79 79 79 GLN GLN A . n A 1 80 VAL 80 80 80 VAL VAL A . n A 1 81 LEU 81 81 81 LEU LEU A . n A 1 82 ILE 82 82 82 ILE ILE A . n A 1 83 LEU 83 83 83 LEU LEU A . n A 1 84 LYS 84 84 84 LYS LYS A . n A 1 85 SER 85 85 85 SER SER A . n A 1 86 SER 86 86 86 SER SER A . n A 1 87 ARG 87 87 87 ARG ARG A . n A 1 88 ILE 88 88 88 ILE ILE A . n A 1 89 ASN 89 89 89 ASN ASN A . n A 1 90 THR 90 90 90 THR THR A . n A 1 91 ILE 91 91 91 ILE ILE A . n A 1 92 GLU 92 92 92 GLU GLU A . n A 1 93 GLY 93 93 93 GLY GLY A . n A 1 94 ASP 94 94 94 ASP ASP A . n A 1 95 ALA 95 95 95 ALA ALA A . n A 1 96 PHE 96 96 96 PHE PHE A . n A 1 97 TYR 97 97 97 TYR TYR A . n A 1 98 SER 98 98 98 SER SER A . n A 1 99 LEU 99 99 99 LEU LEU A . n A 1 100 GLY 100 100 100 GLY GLY A . n A 1 101 SER 101 101 101 SER SER A . n A 1 102 LEU 102 102 102 LEU LEU A . n A 1 103 GLU 103 103 103 GLU GLU A . n A 1 104 HIS 104 104 104 HIS HIS A . n A 1 105 LEU 105 105 105 LEU LEU A . n A 1 106 ASP 106 106 106 ASP ASP A . n A 1 107 LEU 107 107 107 LEU LEU A . n A 1 108 SER 108 108 108 SER SER A . n A 1 109 ASP 109 109 109 ASP ASP A . n A 1 110 ASN 110 110 110 ASN ASN A . n A 1 111 HIS 111 111 111 HIS HIS A . n A 1 112 LEU 112 112 112 LEU LEU A . n A 1 113 SER 113 113 113 SER SER A . n A 1 114 SER 114 114 114 SER SER A . n A 1 115 LEU 115 115 115 LEU LEU A . n A 1 116 SER 116 116 116 SER SER A . n A 1 117 SER 117 117 117 SER SER A . n A 1 118 SER 118 118 118 SER SER A . n A 1 119 TRP 119 119 119 TRP TRP A . n A 1 120 PHE 120 120 120 PHE PHE A . n A 1 121 GLY 121 121 121 GLY GLY A . n A 1 122 PRO 122 122 122 PRO PRO A . n A 1 123 LEU 123 123 123 LEU LEU A . n A 1 124 SER 124 124 124 SER SER A . n A 1 125 SER 125 125 125 SER SER A . n A 1 126 LEU 126 126 126 LEU LEU A . n A 1 127 LYS 127 127 127 LYS LYS A . n A 1 128 TYR 128 128 128 TYR TYR A . n A 1 129 LEU 129 129 129 LEU LEU A . n A 1 130 ASN 130 130 130 ASN ASN A . n A 1 131 LEU 131 131 131 LEU LEU A . n A 1 132 MET 132 132 132 MET MET A . n A 1 133 GLY 133 133 133 GLY GLY A . n A 1 134 ASN 134 134 134 ASN ASN A . n A 1 135 PRO 135 135 135 PRO PRO A . n A 1 136 TYR 136 136 136 TYR TYR A . n A 1 137 GLN 137 137 137 GLN GLN A . n A 1 138 THR 138 138 138 THR THR A . n A 1 139 LEU 139 139 139 LEU LEU A . n A 1 140 GLY 140 140 140 GLY GLY A . n A 1 141 VAL 141 141 141 VAL VAL A . n A 1 142 THR 142 142 142 THR THR A . n A 1 143 SER 143 143 143 SER SER A . n A 1 144 LEU 144 144 144 LEU LEU A . n A 1 145 PHE 145 145 145 PHE PHE A . n A 1 146 PRO 146 146 146 PRO PRO A . n A 1 147 ASN 147 147 147 ASN ASN A . n A 1 148 LEU 148 148 148 LEU LEU A . n A 1 149 THR 149 149 149 THR THR A . n A 1 150 ASN 150 150 150 ASN ASN A . n A 1 151 LEU 151 151 151 LEU LEU A . n A 1 152 GLN 152 152 152 GLN GLN A . n A 1 153 THR 153 153 153 THR THR A . n A 1 154 LEU 154 154 154 LEU LEU A . n A 1 155 ARG 155 155 155 ARG ARG A . n A 1 156 ILE 156 156 156 ILE ILE A . n A 1 157 GLY 157 157 157 GLY GLY A . n A 1 158 ASN 158 158 158 ASN ASN A . n A 1 159 VAL 159 159 159 VAL VAL A . n A 1 160 GLU 160 160 160 GLU GLU A . n A 1 161 THR 161 161 161 THR THR A . n A 1 162 PHE 162 162 162 PHE PHE A . n A 1 163 SER 163 163 163 SER SER A . n A 1 164 GLU 164 164 164 GLU GLU A . n A 1 165 ILE 165 165 165 ILE ILE A . n A 1 166 ARG 166 166 166 ARG ARG A . n A 1 167 ARG 167 167 167 ARG ARG A . n A 1 168 ILE 168 168 168 ILE ILE A . n A 1 169 ASP 169 169 169 ASP ASP A . n A 1 170 PHE 170 170 170 PHE PHE A . n A 1 171 ALA 171 171 171 ALA ALA A . n A 1 172 GLY 172 172 172 GLY GLY A . n A 1 173 LEU 173 173 173 LEU LEU A . n A 1 174 THR 174 174 174 THR THR A . n A 1 175 SER 175 175 175 SER SER A . n A 1 176 LEU 176 176 176 LEU LEU A . n A 1 177 ASN 177 177 177 ASN ASN A . n A 1 178 GLU 178 178 178 GLU GLU A . n A 1 179 LEU 179 179 179 LEU LEU A . n A 1 180 GLU 180 180 180 GLU GLU A . n A 1 181 ILE 181 181 181 ILE ILE A . n A 1 182 LYS 182 182 182 LYS LYS A . n A 1 183 ALA 183 183 183 ALA ALA A . n A 1 184 LEU 184 184 184 LEU LEU A . n A 1 185 SER 185 185 185 SER SER A . n A 1 186 LEU 186 186 186 LEU LEU A . n A 1 187 ARG 187 187 187 ARG ARG A . n A 1 188 ASN 188 188 188 ASN ASN A . n A 1 189 TYR 189 189 189 TYR TYR A . n A 1 190 GLN 190 190 190 GLN GLN A . n A 1 191 SER 191 191 191 SER SER A . n A 1 192 GLN 192 192 192 GLN GLN A . n A 1 193 SER 193 193 193 SER SER A . n A 1 194 LEU 194 194 194 LEU LEU A . n A 1 195 LYS 195 195 195 LYS LYS A . n A 1 196 SER 196 196 196 SER SER A . n A 1 197 ILE 197 197 197 ILE ILE A . n A 1 198 ARG 198 198 198 ARG ARG A . n A 1 199 ASP 199 199 199 ASP ASP A . n A 1 200 ILE 200 200 200 ILE ILE A . n A 1 201 HIS 201 201 201 HIS HIS A . n A 1 202 HIS 202 202 202 HIS HIS A . n A 1 203 LEU 203 203 203 LEU LEU A . n A 1 204 THR 204 204 204 THR THR A . n A 1 205 LEU 205 205 205 LEU LEU A . n A 1 206 HIS 206 206 206 HIS HIS A . n A 1 207 LEU 207 207 207 LEU LEU A . n A 1 208 SER 208 208 208 SER SER A . n A 1 209 GLU 209 209 209 GLU GLU A . n A 1 210 SER 210 210 210 SER SER A . n A 1 211 ALA 211 211 211 ALA ALA A . n A 1 212 PHE 212 212 212 PHE PHE A . n A 1 213 LEU 213 213 213 LEU LEU A . n A 1 214 LEU 214 214 214 LEU LEU A . n A 1 215 GLU 215 215 215 GLU GLU A . n A 1 216 ILE 216 216 216 ILE ILE A . n A 1 217 PHE 217 217 217 PHE PHE A . n A 1 218 ALA 218 218 218 ALA ALA A . n A 1 219 ASP 219 219 219 ASP ASP A . n A 1 220 ILE 220 220 220 ILE ILE A . n A 1 221 LEU 221 221 221 LEU LEU A . n A 1 222 SER 222 222 222 SER SER A . n A 1 223 SER 223 223 223 SER SER A . n A 1 224 VAL 224 224 224 VAL VAL A . n A 1 225 ARG 225 225 225 ARG ARG A . n A 1 226 TYR 226 226 226 TYR TYR A . n A 1 227 LEU 227 227 227 LEU LEU A . n A 1 228 GLU 228 228 228 GLU GLU A . n A 1 229 LEU 229 229 229 LEU LEU A . n A 1 230 ARG 230 230 230 ARG ARG A . n A 1 231 ASP 231 231 231 ASP ASP A . n A 1 232 THR 232 232 232 THR THR A . n A 1 233 ASN 233 233 233 ASN ASN A . n A 1 234 LEU 234 234 234 LEU LEU A . n A 1 235 ALA 235 235 235 ALA ALA A . n A 1 236 ARG 236 236 236 ARG ARG A . n A 1 237 PHE 237 237 237 PHE PHE A . n A 1 238 GLN 238 238 238 GLN GLN A . n A 1 239 PHE 239 239 239 PHE PHE A . n A 1 240 SER 240 240 240 SER SER A . n A 1 241 PRO 241 241 241 PRO PRO A . n A 1 242 LEU 242 242 242 LEU LEU A . n A 1 243 PRO 243 243 243 PRO PRO A . n A 1 244 VAL 244 244 244 VAL VAL A . n A 1 245 ASP 245 245 245 ASP ASP A . n A 1 246 GLU 246 246 246 GLU GLU A . n A 1 247 VAL 247 247 247 VAL VAL A . n A 1 248 SER 248 248 248 SER SER A . n A 1 249 SER 249 249 249 SER SER A . n A 1 250 PRO 250 250 250 PRO PRO A . n A 1 251 MET 251 251 251 MET MET A . n A 1 252 LYS 252 252 252 LYS LYS A . n A 1 253 LYS 253 253 253 LYS LYS A . n A 1 254 LEU 254 254 254 LEU LEU A . n A 1 255 ALA 255 255 255 ALA ALA A . n A 1 256 PHE 256 256 256 PHE PHE A . n A 1 257 ARG 257 257 257 ARG ARG A . n A 1 258 GLY 258 258 258 GLY GLY A . n A 1 259 SER 259 259 259 SER SER A . n A 1 260 VAL 260 260 260 VAL VAL A . n A 1 261 LEU 261 261 261 LEU LEU A . n A 1 262 THR 262 262 262 THR THR A . n A 1 263 ASP 263 263 263 ASP ASP A . n A 1 264 GLU 264 264 264 GLU GLU A . n A 1 265 SER 265 265 265 SER SER A . n A 1 266 PHE 266 266 266 PHE PHE A . n A 1 267 ASN 267 267 267 ASN ASN A . n A 1 268 GLU 268 268 268 GLU GLU A . n A 1 269 LEU 269 269 269 LEU LEU A . n A 1 270 LEU 270 270 270 LEU LEU A . n A 1 271 LYS 271 271 271 LYS LYS A . n A 1 272 LEU 272 272 272 LEU LEU A . n A 1 273 LEU 273 273 273 LEU LEU A . n A 1 274 ARG 274 274 274 ARG ARG A . n A 1 275 TYR 275 275 275 TYR TYR A . n A 1 276 ILE 276 276 276 ILE ILE A . n A 1 277 LEU 277 277 277 LEU LEU A . n A 1 278 GLU 278 278 278 GLU GLU A . n A 1 279 LEU 279 279 279 LEU LEU A . n A 1 280 SER 280 280 280 SER SER A . n A 1 281 GLU 281 281 281 GLU GLU A . n A 1 282 VAL 282 282 282 VAL VAL A . n A 1 283 GLU 283 283 283 GLU GLU A . n A 1 284 PHE 284 284 284 PHE PHE A . n A 1 285 ASP 285 285 285 ASP ASP A . n A 1 286 ASP 286 286 286 ASP ASP A . n A 1 287 CYS 287 287 287 CYS CYS A . n A 1 288 THR 288 288 288 THR THR A . n A 1 289 LEU 289 289 289 LEU LEU A . n A 1 290 ASN 290 290 290 ASN ASN A . n A 1 291 GLY 291 291 291 GLY GLY A . n A 1 292 LEU 292 292 292 LEU LEU A . n A 1 293 GLY 293 293 293 GLY GLY A . n A 1 294 ASP 294 294 294 ASP ASP A . n A 1 295 PHE 295 295 295 PHE PHE A . n A 1 296 ASN 296 296 296 ASN ASN A . n A 1 297 PRO 297 297 297 PRO PRO A . n A 1 298 SER 298 298 298 SER SER A . n A 1 299 GLU 299 299 299 GLU GLU A . n A 1 300 SER 300 300 300 SER SER A . n A 1 301 ASP 301 301 301 ASP ASP A . n A 1 302 VAL 302 302 302 VAL VAL A . n A 1 303 VAL 303 303 303 VAL VAL A . n A 1 304 SER 304 304 304 SER SER A . n A 1 305 GLU 305 305 305 GLU GLU A . n A 1 306 LEU 306 306 306 LEU LEU A . n A 1 307 GLY 307 307 307 GLY GLY A . n A 1 308 LYS 308 308 308 LYS LYS A . n A 1 309 VAL 309 309 309 VAL VAL A . n A 1 310 GLU 310 310 310 GLU GLU A . n A 1 311 THR 311 311 311 THR THR A . n A 1 312 VAL 312 312 312 VAL VAL A . n A 1 313 THR 313 313 313 THR THR A . n A 1 314 ILE 314 314 314 ILE ILE A . n A 1 315 ARG 315 315 315 ARG ARG A . n A 1 316 ARG 316 316 316 ARG ARG A . n A 1 317 LEU 317 317 317 LEU LEU A . n A 1 318 HIS 318 318 318 HIS HIS A . n A 1 319 ILE 319 319 319 ILE ILE A . n A 1 320 PRO 320 320 320 PRO PRO A . n A 1 321 GLN 321 321 321 GLN GLN A . n A 1 322 PHE 322 322 322 PHE PHE A . n A 1 323 TYR 323 323 323 TYR TYR A . n A 1 324 LEU 324 324 324 LEU LEU A . n A 1 325 PHE 325 325 325 PHE PHE A . n A 1 326 TYR 326 326 326 TYR TYR A . n A 1 327 ASP 327 327 327 ASP ASP A . n A 1 328 LEU 328 328 328 LEU LEU A . n A 1 329 SER 329 329 329 SER SER A . n A 1 330 THR 330 330 330 THR THR A . n A 1 331 VAL 331 331 331 VAL VAL A . n A 1 332 TYR 332 332 332 TYR TYR A . n A 1 333 SER 333 333 333 SER SER A . n A 1 334 LEU 334 334 334 LEU LEU A . n A 1 335 LEU 335 335 335 LEU LEU A . n A 1 336 GLU 336 336 336 GLU GLU A . n A 1 337 LYS 337 337 337 LYS LYS A . n A 1 338 VAL 338 338 338 VAL VAL A . n A 1 339 LYS 339 339 339 LYS LYS A . n A 1 340 ARG 340 340 340 ARG ARG A . n A 1 341 ILE 341 341 341 ILE ILE A . n A 1 342 THR 342 342 342 THR THR A . n A 1 343 VAL 343 343 343 VAL VAL A . n A 1 344 GLU 344 344 344 GLU GLU A . n A 1 345 ASN 345 345 345 ASN ASN A . n A 1 346 SER 346 346 346 SER SER A . n A 1 347 LYS 347 347 347 LYS LYS A . n A 1 348 VAL 348 348 348 VAL VAL A . n A 1 349 PHE 349 349 349 PHE PHE A . n A 1 350 LEU 350 350 350 LEU LEU A . n A 1 351 VAL 351 351 351 VAL VAL A . n A 1 352 PRO 352 352 352 PRO PRO A . n A 1 353 CYS 353 353 353 CYS CYS A . n A 1 354 SER 354 354 354 SER SER A . n A 1 355 PHE 355 355 355 PHE PHE A . n A 1 356 SER 356 356 356 SER SER A . n A 1 357 GLN 357 357 357 GLN GLN A . n A 1 358 HIS 358 358 358 HIS HIS A . n A 1 359 LEU 359 359 359 LEU LEU A . n A 1 360 LYS 360 360 360 LYS LYS A . n A 1 361 SER 361 361 361 SER SER A . n A 1 362 LEU 362 362 362 LEU LEU A . n A 1 363 GLU 363 363 363 GLU GLU A . n A 1 364 PHE 364 364 364 PHE PHE A . n A 1 365 LEU 365 365 365 LEU LEU A . n A 1 366 ASP 366 366 366 ASP ASP A . n A 1 367 LEU 367 367 367 LEU LEU A . n A 1 368 SER 368 368 368 SER SER A . n A 1 369 GLU 369 369 369 GLU GLU A . n A 1 370 ASN 370 370 370 ASN ASN A . n A 1 371 LEU 371 371 371 LEU LEU A . n A 1 372 MET 372 372 372 MET MET A . n A 1 373 VAL 373 373 373 VAL VAL A . n A 1 374 GLU 374 374 374 GLU GLU A . n A 1 375 GLU 375 375 375 GLU GLU A . n A 1 376 TYR 376 376 376 TYR TYR A . n A 1 377 LEU 377 377 377 LEU LEU A . n A 1 378 LYS 378 378 378 LYS LYS A . n A 1 379 ASN 379 379 379 ASN ASN A . n A 1 380 SER 380 380 380 SER SER A . n A 1 381 ALA 381 381 381 ALA ALA A . n A 1 382 CYS 382 382 382 CYS CYS A . n A 1 383 LYS 383 383 383 LYS LYS A . n A 1 384 GLY 384 384 384 GLY GLY A . n A 1 385 ALA 385 385 385 ALA ALA A . n A 1 386 TRP 386 386 386 TRP TRP A . n A 1 387 PRO 387 387 387 PRO PRO A . n A 1 388 SER 388 388 388 SER SER A . n A 1 389 LEU 389 389 389 LEU LEU A . n A 1 390 GLN 390 390 390 GLN GLN A . n A 1 391 THR 391 391 391 THR THR A . n A 1 392 LEU 392 392 392 LEU LEU A . n A 1 393 VAL 393 393 393 VAL VAL A . n A 1 394 LEU 394 394 394 LEU LEU A . n A 1 395 SER 395 395 395 SER SER A . n A 1 396 GLN 396 396 396 GLN GLN A . n A 1 397 ASN 397 397 397 ASN ASN A . n A 1 398 HIS 398 398 398 HIS HIS A . n A 1 399 LEU 399 399 399 LEU LEU A . n A 1 400 ARG 400 400 400 ARG ARG A . n A 1 401 SER 401 401 401 SER SER A . n A 1 402 MET 402 402 402 MET MET A . n A 1 403 GLN 403 403 403 GLN GLN A . n A 1 404 LYS 404 404 404 LYS LYS A . n A 1 405 THR 405 405 405 THR THR A . n A 1 406 GLY 406 406 406 GLY GLY A . n A 1 407 GLU 407 407 407 GLU GLU A . n A 1 408 ILE 408 408 408 ILE ILE A . n A 1 409 LEU 409 409 409 LEU LEU A . n A 1 410 LEU 410 410 410 LEU LEU A . n A 1 411 THR 411 411 411 THR THR A . n A 1 412 LEU 412 412 412 LEU LEU A . n A 1 413 LYS 413 413 413 LYS LYS A . n A 1 414 ASN 414 414 414 ASN ASN A . n A 1 415 LEU 415 415 415 LEU LEU A . n A 1 416 THR 416 416 416 THR THR A . n A 1 417 SER 417 417 417 SER SER A . n A 1 418 LEU 418 418 418 LEU LEU A . n A 1 419 ASP 419 419 419 ASP ASP A . n A 1 420 ILE 420 420 420 ILE ILE A . n A 1 421 SER 421 421 421 SER SER A . n A 1 422 ARG 422 422 422 ARG ARG A . n A 1 423 ASN 423 423 423 ASN ASN A . n A 1 424 THR 424 424 424 THR THR A . n A 1 425 PHE 425 425 425 PHE PHE A . n A 1 426 HIS 426 426 426 HIS HIS A . n A 1 427 PRO 427 427 427 PRO PRO A . n A 1 428 MET 428 428 428 MET MET A . n A 1 429 PRO 429 429 429 PRO PRO A . n A 1 430 ASP 430 430 430 ASP ASP A . n A 1 431 SER 431 431 431 SER SER A . n A 1 432 CYS 432 432 432 CYS CYS A . n A 1 433 GLN 433 433 433 GLN GLN A . n A 1 434 TRP 434 434 434 TRP TRP A . n A 1 435 PRO 435 435 435 PRO PRO A . n A 1 436 GLU 436 436 436 GLU GLU A . n A 1 437 LYS 437 437 437 LYS LYS A . n A 1 438 MET 438 438 438 MET MET A . n A 1 439 ARG 439 439 439 ARG ARG A . n A 1 440 PHE 440 440 440 PHE PHE A . n A 1 441 LEU 441 441 441 LEU LEU A . n A 1 442 ASN 442 442 442 ASN ASN A . n A 1 443 LEU 443 443 443 LEU LEU A . n A 1 444 SER 444 444 444 SER SER A . n A 1 445 SER 445 445 445 SER SER A . n A 1 446 THR 446 446 446 THR THR A . n A 1 447 GLY 447 447 447 GLY GLY A . n A 1 448 ILE 448 448 448 ILE ILE A . n A 1 449 ARG 449 449 449 ARG ARG A . n A 1 450 VAL 450 450 450 VAL VAL A . n A 1 451 VAL 451 451 451 VAL VAL A . n A 1 452 LYS 452 452 452 LYS LYS A . n A 1 453 THR 453 453 453 THR THR A . n A 1 454 CYS 454 454 454 CYS CYS A . n A 1 455 ILE 455 455 455 ILE ILE A . n A 1 456 PRO 456 456 456 PRO PRO A . n A 1 457 GLN 457 457 457 GLN GLN A . n A 1 458 THR 458 458 458 THR THR A . n A 1 459 LEU 459 459 459 LEU LEU A . n A 1 460 GLU 460 460 460 GLU GLU A . n A 1 461 VAL 461 461 461 VAL VAL A . n A 1 462 LEU 462 462 462 LEU LEU A . n A 1 463 ASP 463 463 463 ASP ASP A . n A 1 464 VAL 464 464 464 VAL VAL A . n A 1 465 SER 465 465 465 SER SER A . n A 1 466 ASN 466 466 466 ASN ASN A . n A 1 467 ASN 467 467 467 ASN ASN A . n A 1 468 ASN 468 468 468 ASN ASN A . n A 1 469 LEU 469 469 469 LEU LEU A . n A 1 470 ASP 470 470 470 ASP ASP A . n A 1 471 SER 471 471 471 SER SER A . n A 1 472 PHE 472 472 472 PHE PHE A . n A 1 473 SER 473 473 473 SER SER A . n A 1 474 LEU 474 474 474 LEU LEU A . n A 1 475 PHE 475 475 475 PHE PHE A . n A 1 476 LEU 476 476 476 LEU LEU A . n A 1 477 PRO 477 477 477 PRO PRO A . n A 1 478 ARG 478 478 478 ARG ARG A . n A 1 479 LEU 479 479 479 LEU LEU A . n A 1 480 GLN 480 480 480 GLN GLN A . n A 1 481 GLU 481 481 481 GLU GLU A . n A 1 482 LEU 482 482 482 LEU LEU A . n A 1 483 TYR 483 483 483 TYR TYR A . n A 1 484 ILE 484 484 484 ILE ILE A . n A 1 485 SER 485 485 485 SER SER A . n A 1 486 ARG 486 486 486 ARG ARG A . n A 1 487 ASN 487 487 487 ASN ASN A . n A 1 488 LYS 488 488 488 LYS LYS A . n A 1 489 LEU 489 489 489 LEU LEU A . n A 1 490 LYS 490 490 490 LYS LYS A . n A 1 491 THR 491 491 491 THR THR A . n A 1 492 LEU 492 492 492 LEU LEU A . n A 1 493 PRO 493 493 493 PRO PRO A . n A 1 494 ASP 494 494 494 ASP ASP A . n A 1 495 ALA 495 495 495 ALA ALA A . n A 1 496 SER 496 496 496 SER SER A . n A 1 497 LEU 497 497 497 LEU LEU A . n A 1 498 PHE 498 498 498 PHE PHE A . n A 1 499 PRO 499 499 499 PRO PRO A . n A 1 500 VAL 500 500 500 VAL VAL A . n A 1 501 LEU 501 501 501 LEU LEU A . n A 1 502 LEU 502 502 502 LEU LEU A . n A 1 503 VAL 503 503 503 VAL VAL A . n A 1 504 MET 504 504 504 MET MET A . n A 1 505 LYS 505 505 505 LYS LYS A . n A 1 506 ILE 506 506 506 ILE ILE A . n A 1 507 ALA 507 507 507 ALA ALA A . n A 1 508 SER 508 508 508 SER SER A . n A 1 509 ASN 509 509 509 ASN ASN A . n A 1 510 GLN 510 510 510 GLN GLN A . n A 1 511 LEU 511 511 511 LEU LEU A . n A 1 512 LYS 512 512 512 LYS LYS A . n A 1 513 SER 513 513 513 SER SER A . n A 1 514 VAL 514 514 514 VAL VAL A . n A 1 515 PRO 515 515 515 PRO PRO A . n A 1 516 ASP 516 516 516 ASP ASP A . n A 1 517 GLY 517 517 517 GLY GLY A . n A 1 518 ILE 518 518 518 ILE ILE A . n A 1 519 PHE 519 519 519 PHE PHE A . n A 1 520 ASP 520 520 520 ASP ASP A . n A 1 521 ARG 521 521 521 ARG ARG A . n A 1 522 LEU 522 522 522 LEU LEU A . n A 1 523 THR 523 523 523 THR THR A . n A 1 524 SER 524 524 524 SER SER A . n A 1 525 LEU 525 525 525 LEU LEU A . n A 1 526 GLN 526 526 526 GLN GLN A . n A 1 527 LYS 527 527 527 LYS LYS A . n A 1 528 ILE 528 528 528 ILE ILE A . n A 1 529 TRP 529 529 529 TRP TRP A . n A 1 530 LEU 530 530 530 LEU LEU A . n A 1 531 HIS 531 531 531 HIS HIS A . n A 1 532 THR 532 532 532 THR THR A . n A 1 533 ASN 533 533 533 ASN ASN A . n A 1 534 PRO 534 534 534 PRO PRO A . n A 1 535 TRP 535 535 535 TRP TRP A . n A 1 536 ASP 536 536 536 ASP ASP A . n A 1 537 CYS 537 537 537 CYS CYS A . n A 1 538 SER 538 538 538 SER SER A . n A 1 539 CYS 539 539 539 CYS CYS A . n A 1 540 PRO 540 540 540 PRO PRO A . n A 1 541 ARG 541 541 541 ARG ARG A . n A 1 542 ILE 542 542 542 ILE ILE A . n A 1 543 ASP 543 543 543 ASP ASP A . n A 1 544 TYR 544 544 544 TYR TYR A . n A 1 545 LEU 545 545 545 LEU LEU A . n A 1 546 SER 546 546 546 SER SER A . n A 1 547 ARG 547 547 547 ARG ARG A . n A 1 548 TRP 548 548 548 TRP TRP A . n A 1 549 LEU 549 549 549 LEU LEU A . n A 1 550 ASN 550 550 550 ASN ASN A . n A 1 551 LYS 551 551 551 LYS LYS A . n A 1 552 ASN 552 552 552 ASN ASN A . n A 1 553 SER 553 553 553 SER SER A . n A 1 554 GLN 554 554 554 GLN GLN A . n A 1 555 LYS 555 555 555 LYS LYS A . n A 1 556 GLU 556 556 556 GLU GLU A . n A 1 557 GLN 557 557 557 GLN GLN A . n A 1 558 GLY 558 558 558 GLY GLY A . n A 1 559 SER 559 559 559 SER SER A . n A 1 560 ALA 560 560 560 ALA ALA A . n A 1 561 LYS 561 561 561 LYS LYS A . n A 1 562 CYS 562 562 562 CYS CYS A . n A 1 563 SER 563 563 563 SER SER A . n A 1 564 GLY 564 564 564 GLY GLY A . n A 1 565 SER 565 565 565 SER SER A . n A 1 566 GLY 566 566 566 GLY GLY A . n A 1 567 LYS 567 567 567 LYS LYS A . n A 1 568 PRO 568 568 568 PRO PRO A . n A 1 569 VAL 569 569 569 VAL VAL A . n A 1 570 ARG 570 570 570 ARG ARG A . n A 1 571 SER 571 571 571 SER SER A . n A 1 572 ILE 572 572 572 ILE ILE A . n A 1 573 ILE 573 573 573 ILE ILE A . n A 1 574 CYS 574 574 574 CYS CYS A . n A 1 575 PRO 575 575 575 PRO PRO A . n A 1 576 THR 576 576 ? ? ? A . n A 1 577 LEU 577 577 ? ? ? A . n A 1 578 VAL 578 578 ? ? ? A . n A 1 579 PRO 579 579 ? ? ? A . n A 1 580 ARG 580 580 ? ? ? A . n B 2 1 MET 1 1 ? ? ? B . n B 2 2 SER 2 2 ? ? ? B . n B 2 3 GLN 3 3 ? ? ? B . n B 2 4 ASP 4 4 ? ? ? B . n B 2 5 ARG 5 5 ? ? ? B . n B 2 6 LYS 6 6 ? ? ? B . n B 2 7 PRO 7 7 ? ? ? B . n B 2 8 ILE 8 8 ? ? ? B . n B 2 9 VAL 9 9 ? ? ? B . n B 2 10 GLY 10 10 ? ? ? B . n B 2 11 SER 11 11 ? ? ? B . n B 2 12 PHE 12 12 ? ? ? B . n B 2 13 HIS 13 13 ? ? ? B . n B 2 14 PHE 14 14 ? ? ? B . n B 2 15 VAL 15 15 ? ? ? B . n B 2 16 CYS 16 16 ? ? ? B . n B 2 17 ALA 17 17 ? ? ? B . n B 2 18 LEU 18 18 ? ? ? B . n B 2 19 ALA 19 19 ? ? ? B . n B 2 20 LEU 20 20 ? ? ? B . n B 2 21 ILE 21 21 ? ? ? B . n B 2 22 VAL 22 22 ? ? ? B . n B 2 23 GLY 23 23 ? ? ? B . n B 2 24 SER 24 24 ? ? ? B . n B 2 25 MET 25 25 ? ? ? B . n B 2 26 THR 26 26 ? ? ? B . n B 2 27 PRO 27 27 ? ? ? B . n B 2 28 PHE 28 28 ? ? ? B . n B 2 29 SER 29 29 ? ? ? B . n B 2 30 ASN 30 30 ? ? ? B . n B 2 31 GLU 31 31 ? ? ? B . n B 2 32 LEU 32 32 ? ? ? B . n B 2 33 GLU 33 33 33 GLU GLU B . n B 2 34 SER 34 34 34 SER SER B . n B 2 35 MET 35 35 35 MET MET B . n B 2 36 VAL 36 36 36 VAL VAL B . n B 2 37 ASP 37 37 37 ASP ASP B . n B 2 38 TYR 38 38 38 TYR TYR B . n B 2 39 SER 39 39 39 SER SER B . n B 2 40 ASN 40 40 40 ASN ASN B . n B 2 41 ARG 41 41 41 ARG ARG B . n B 2 42 ASN 42 42 42 ASN ASN B . n B 2 43 LEU 43 43 43 LEU LEU B . n B 2 44 THR 44 44 44 THR THR B . n B 2 45 HIS 45 45 45 HIS HIS B . n B 2 46 VAL 46 46 46 VAL VAL B . n B 2 47 PRO 47 47 47 PRO PRO B . n B 2 48 LYS 48 48 48 LYS LYS B . n B 2 49 ASP 49 49 49 ASP ASP B . n B 2 50 LEU 50 50 50 LEU LEU B . n B 2 51 PRO 51 51 51 PRO PRO B . n B 2 52 PRO 52 52 52 PRO PRO B . n B 2 53 ARG 53 53 53 ARG ARG B . n B 2 54 THR 54 54 54 THR THR B . n B 2 55 LYS 55 55 55 LYS LYS B . n B 2 56 ALA 56 56 56 ALA ALA B . n B 2 57 LEU 57 57 57 LEU LEU B . n B 2 58 SER 58 58 58 SER SER B . n B 2 59 LEU 59 59 59 LEU LEU B . n B 2 60 SER 60 60 60 SER SER B . n B 2 61 GLN 61 61 61 GLN GLN B . n B 2 62 ASN 62 62 62 ASN ASN B . n B 2 63 SER 63 63 63 SER SER B . n B 2 64 ILE 64 64 64 ILE ILE B . n B 2 65 SER 65 65 65 SER SER B . n B 2 66 GLU 66 66 66 GLU GLU B . n B 2 67 LEU 67 67 67 LEU LEU B . n B 2 68 ARG 68 68 68 ARG ARG B . n B 2 69 MET 69 69 69 MET MET B . n B 2 70 PRO 70 70 70 PRO PRO B . n B 2 71 ASP 71 71 71 ASP ASP B . n B 2 72 ILE 72 72 72 ILE ILE B . n B 2 73 SER 73 73 73 SER SER B . n B 2 74 PHE 74 74 74 PHE PHE B . n B 2 75 LEU 75 75 75 LEU LEU B . n B 2 76 SER 76 76 76 SER SER B . n B 2 77 GLU 77 77 77 GLU GLU B . n B 2 78 LEU 78 78 78 LEU LEU B . n B 2 79 ARG 79 79 79 ARG ARG B . n B 2 80 VAL 80 80 80 VAL VAL B . n B 2 81 LEU 81 81 81 LEU LEU B . n B 2 82 ARG 82 82 82 ARG ARG B . n B 2 83 LEU 83 83 83 LEU LEU B . n B 2 84 SER 84 84 84 SER SER B . n B 2 85 HIS 85 85 85 HIS HIS B . n B 2 86 ASN 86 86 86 ASN ASN B . n B 2 87 ARG 87 87 87 ARG ARG B . n B 2 88 ILE 88 88 88 ILE ILE B . n B 2 89 ARG 89 89 89 ARG ARG B . n B 2 90 SER 90 90 90 SER SER B . n B 2 91 LEU 91 91 91 LEU LEU B . n B 2 92 ASP 92 92 92 ASP ASP B . n B 2 93 PHE 93 93 93 PHE PHE B . n B 2 94 HIS 94 94 94 HIS HIS B . n B 2 95 VAL 95 95 95 VAL VAL B . n B 2 96 PHE 96 96 96 PHE PHE B . n B 2 97 LEU 97 97 97 LEU LEU B . n B 2 98 PHE 98 98 98 PHE PHE B . n B 2 99 ASN 99 99 99 ASN ASN B . n B 2 100 GLN 100 100 100 GLN GLN B . n B 2 101 ASP 101 101 101 ASP ASP B . n B 2 102 LEU 102 102 102 LEU LEU B . n B 2 103 GLU 103 103 103 GLU GLU B . n B 2 104 TYR 104 104 104 TYR TYR B . n B 2 105 LEU 105 105 105 LEU LEU B . n B 2 106 ASP 106 106 106 ASP ASP B . n B 2 107 VAL 107 107 107 VAL VAL B . n B 2 108 SER 108 108 108 SER SER B . n B 2 109 HIS 109 109 109 HIS HIS B . n B 2 110 ASN 110 110 110 ASN ASN B . n B 2 111 ARG 111 111 111 ARG ARG B . n B 2 112 LEU 112 112 112 LEU LEU B . n B 2 113 GLN 113 113 113 GLN GLN B . n B 2 114 ASN 114 114 114 ASN ASN B . n B 2 115 ILE 115 115 115 ILE ILE B . n B 2 116 SER 116 116 116 SER SER B . n B 2 117 CYS 117 117 117 CYS CYS B . n B 2 118 CYS 118 118 118 CYS CYS B . n B 2 119 PRO 119 119 119 PRO PRO B . n B 2 120 MET 120 120 120 MET MET B . n B 2 121 ALA 121 121 121 ALA ALA B . n B 2 122 SER 122 122 122 SER SER B . n B 2 123 LEU 123 123 123 LEU LEU B . n B 2 124 ARG 124 124 124 ARG ARG B . n B 2 125 HIS 125 125 125 HIS HIS B . n B 2 126 LEU 126 126 126 LEU LEU B . n B 2 127 ASP 127 127 127 ASP ASP B . n B 2 128 LEU 128 128 128 LEU LEU B . n B 2 129 SER 129 129 129 SER SER B . n B 2 130 PHE 130 130 130 PHE PHE B . n B 2 131 ASN 131 131 131 ASN ASN B . n B 2 132 ASP 132 132 132 ASP ASP B . n B 2 133 PHE 133 133 133 PHE PHE B . n B 2 134 ASP 134 134 134 ASP ASP B . n B 2 135 VAL 135 135 135 VAL VAL B . n B 2 136 LEU 136 136 136 LEU LEU B . n B 2 137 PRO 137 137 137 PRO PRO B . n B 2 138 VAL 138 138 138 VAL VAL B . n B 2 139 CYS 139 139 139 CYS CYS B . n B 2 140 LYS 140 140 140 LYS LYS B . n B 2 141 GLU 141 141 141 GLU GLU B . n B 2 142 PHE 142 142 142 PHE PHE B . n B 2 143 GLY 143 143 143 GLY GLY B . n B 2 144 ASN 144 144 144 ASN ASN B . n B 2 145 LEU 145 145 145 LEU LEU B . n B 2 146 THR 146 146 146 THR THR B . n B 2 147 LYS 147 147 147 LYS LYS B . n B 2 148 LEU 148 148 148 LEU LEU B . n B 2 149 THR 149 149 149 THR THR B . n B 2 150 PHE 150 150 150 PHE PHE B . n B 2 151 LEU 151 151 151 LEU LEU B . n B 2 152 GLY 152 152 152 GLY GLY B . n B 2 153 LEU 153 153 153 LEU LEU B . n B 2 154 SER 154 154 154 SER SER B . n B 2 155 ALA 155 155 155 ALA ALA B . n B 2 156 ALA 156 156 156 ALA ALA B . n B 2 157 LYS 157 157 157 LYS LYS B . n B 2 158 PHE 158 158 158 PHE PHE B . n B 2 159 ARG 159 159 159 ARG ARG B . n B 2 160 GLN 160 160 160 GLN GLN B . n B 2 161 LEU 161 161 161 LEU LEU B . n B 2 162 ASP 162 162 162 ASP ASP B . n B 2 163 LEU 163 163 163 LEU LEU B . n B 2 164 LEU 164 164 164 LEU LEU B . n B 2 165 PRO 165 165 165 PRO PRO B . n B 2 166 VAL 166 166 166 VAL VAL B . n B 2 167 ALA 167 167 167 ALA ALA B . n B 2 168 HIS 168 168 168 HIS HIS B . n B 2 169 LEU 169 169 169 LEU LEU B . n B 2 170 HIS 170 170 170 HIS HIS B . n B 2 171 LEU 171 171 171 LEU LEU B . n B 2 172 SER 172 172 172 SER SER B . n B 2 173 CYS 173 173 173 CYS CYS B . n B 2 174 ILE 174 174 174 ILE ILE B . n B 2 175 LEU 175 175 175 LEU LEU B . n B 2 176 LEU 176 176 176 LEU LEU B . n B 2 177 ASP 177 177 177 ASP ASP B . n B 2 178 LEU 178 178 178 LEU LEU B . n B 2 179 VAL 179 179 179 VAL VAL B . n B 2 180 SER 180 180 180 SER SER B . n B 2 181 TYR 181 181 181 TYR TYR B . n B 2 182 HIS 182 182 182 HIS HIS B . n B 2 183 ILE 183 183 183 ILE ILE B . n B 2 184 LYS 184 184 184 LYS LYS B . n B 2 185 GLY 185 185 185 GLY GLY B . n B 2 186 GLY 186 186 186 GLY GLY B . n B 2 187 GLU 187 187 187 GLU GLU B . n B 2 188 THR 188 188 188 THR THR B . n B 2 189 GLU 189 189 189 GLU GLU B . n B 2 190 SER 190 190 190 SER SER B . n B 2 191 LEU 191 191 191 LEU LEU B . n B 2 192 GLN 192 192 192 GLN GLN B . n B 2 193 ILE 193 193 193 ILE ILE B . n B 2 194 PRO 194 194 194 PRO PRO B . n B 2 195 ASN 195 195 195 ASN ASN B . n B 2 196 THR 196 196 196 THR THR B . n B 2 197 THR 197 197 197 THR THR B . n B 2 198 VAL 198 198 198 VAL VAL B . n B 2 199 LEU 199 199 199 LEU LEU B . n B 2 200 HIS 200 200 200 HIS HIS B . n B 2 201 LEU 201 201 201 LEU LEU B . n B 2 202 VAL 202 202 202 VAL VAL B . n B 2 203 PHE 203 203 203 PHE PHE B . n B 2 204 HIS 204 204 204 HIS HIS B . n B 2 205 PRO 205 205 205 PRO PRO B . n B 2 206 ASN 206 206 206 ASN ASN B . n B 2 207 SER 207 207 207 SER SER B . n B 2 208 LEU 208 208 208 LEU LEU B . n B 2 209 PHE 209 209 209 PHE PHE B . n B 2 210 SER 210 210 210 SER SER B . n B 2 211 VAL 211 211 211 VAL VAL B . n B 2 212 GLN 212 212 212 GLN GLN B . n B 2 213 VAL 213 213 213 VAL VAL B . n B 2 214 ASN 214 214 214 ASN ASN B . n B 2 215 MET 215 215 215 MET MET B . n B 2 216 SER 216 216 216 SER SER B . n B 2 217 VAL 217 217 217 VAL VAL B . n B 2 218 ASN 218 218 218 ASN ASN B . n B 2 219 ALA 219 219 219 ALA ALA B . n B 2 220 LEU 220 220 220 LEU LEU B . n B 2 221 GLY 221 221 221 GLY GLY B . n B 2 222 HIS 222 222 222 HIS HIS B . n B 2 223 LEU 223 223 223 LEU LEU B . n B 2 224 GLN 224 224 224 GLN GLN B . n B 2 225 LEU 225 225 225 LEU LEU B . n B 2 226 SER 226 226 226 SER SER B . n B 2 227 ASN 227 227 227 ASN ASN B . n B 2 228 ILE 228 228 228 ILE ILE B . n B 2 229 LYS 229 229 229 LYS LYS B . n B 2 230 LEU 230 230 230 LEU LEU B . n B 2 231 ASN 231 231 231 ASN ASN B . n B 2 232 ASP 232 232 232 ASP ASP B . n B 2 233 GLU 233 233 233 GLU GLU B . n B 2 234 ASN 234 234 234 ASN ASN B . n B 2 235 CYS 235 235 235 CYS CYS B . n B 2 236 GLN 236 236 236 GLN GLN B . n B 2 237 ARG 237 237 237 ARG ARG B . n B 2 238 LEU 238 238 238 LEU LEU B . n B 2 239 MET 239 239 239 MET MET B . n B 2 240 THR 240 240 240 THR THR B . n B 2 241 PHE 241 241 241 PHE PHE B . n B 2 242 LEU 242 242 242 LEU LEU B . n B 2 243 SER 243 243 243 SER SER B . n B 2 244 GLU 244 244 244 GLU GLU B . n B 2 245 LEU 245 245 245 LEU LEU B . n B 2 246 THR 246 246 246 THR THR B . n B 2 247 ARG 247 247 247 ARG ARG B . n B 2 248 GLY 248 248 248 GLY GLY B . n B 2 249 PRO 249 249 249 PRO PRO B . n B 2 250 THR 250 250 250 THR THR B . n B 2 251 LEU 251 251 251 LEU LEU B . n B 2 252 LEU 252 252 252 LEU LEU B . n B 2 253 ASN 253 253 253 ASN ASN B . n B 2 254 VAL 254 254 254 VAL VAL B . n B 2 255 THR 255 255 255 THR THR B . n B 2 256 LEU 256 256 256 LEU LEU B . n B 2 257 GLN 257 257 257 GLN GLN B . n B 2 258 HIS 258 258 258 HIS HIS B . n B 2 259 ILE 259 259 259 ILE ILE B . n B 2 260 GLU 260 260 260 GLU GLU B . n B 2 261 THR 261 261 261 THR THR B . n B 2 262 THR 262 262 262 THR THR B . n B 2 263 TRP 263 263 263 TRP TRP B . n B 2 264 LYS 264 264 264 LYS LYS B . n B 2 265 CYS 265 265 265 CYS CYS B . n B 2 266 SER 266 266 266 SER SER B . n B 2 267 VAL 267 267 267 VAL VAL B . n B 2 268 LYS 268 268 268 LYS LYS B . n B 2 269 LEU 269 269 269 LEU LEU B . n B 2 270 PHE 270 270 270 PHE PHE B . n B 2 271 GLN 271 271 271 GLN GLN B . n B 2 272 PHE 272 272 272 PHE PHE B . n B 2 273 PHE 273 273 273 PHE PHE B . n B 2 274 TRP 274 274 274 TRP TRP B . n B 2 275 PRO 275 275 275 PRO PRO B . n B 2 276 ARG 276 276 276 ARG ARG B . n B 2 277 PRO 277 277 277 PRO PRO B . n B 2 278 VAL 278 278 278 VAL VAL B . n B 2 279 GLU 279 279 279 GLU GLU B . n B 2 280 TYR 280 280 280 TYR TYR B . n B 2 281 LEU 281 281 281 LEU LEU B . n B 2 282 ASN 282 282 282 ASN ASN B . n B 2 283 ILE 283 283 283 ILE ILE B . n B 2 284 TYR 284 284 284 TYR TYR B . n B 2 285 ASN 285 285 285 ASN ASN B . n B 2 286 LEU 286 286 286 LEU LEU B . n B 2 287 THR 287 287 287 THR THR B . n B 2 288 ILE 288 288 288 ILE ILE B . n B 2 289 THR 289 289 289 THR THR B . n B 2 290 GLU 290 290 290 GLU GLU B . n B 2 291 ARG 291 291 291 ARG ARG B . n B 2 292 ILE 292 292 292 ILE ILE B . n B 2 293 ASP 293 293 293 ASP ASP B . n B 2 294 ARG 294 294 294 ARG ARG B . n B 2 295 GLU 295 295 295 GLU GLU B . n B 2 296 GLU 296 296 296 GLU GLU B . n B 2 297 PHE 297 297 297 PHE PHE B . n B 2 298 THR 298 298 298 THR THR B . n B 2 299 TYR 299 299 299 TYR TYR B . n B 2 300 SER 300 300 300 SER SER B . n B 2 301 GLU 301 301 301 GLU GLU B . n B 2 302 THR 302 302 302 THR THR B . n B 2 303 ALA 303 303 303 ALA ALA B . n B 2 304 LEU 304 304 304 LEU LEU B . n B 2 305 LYS 305 305 305 LYS LYS B . n B 2 306 SER 306 306 306 SER SER B . n B 2 307 LEU 307 307 307 LEU LEU B . n B 2 308 MET 308 308 308 MET MET B . n B 2 309 ILE 309 309 309 ILE ILE B . n B 2 310 GLU 310 310 310 GLU GLU B . n B 2 311 HIS 311 311 311 HIS HIS B . n B 2 312 VAL 312 312 312 VAL VAL B . n B 2 313 LYS 313 313 313 LYS LYS B . n B 2 314 ASN 314 314 314 ASN ASN B . n B 2 315 GLN 315 315 315 GLN GLN B . n B 2 316 VAL 316 316 316 VAL VAL B . n B 2 317 PHE 317 317 317 PHE PHE B . n B 2 318 LEU 318 318 318 LEU LEU B . n B 2 319 PHE 319 319 319 PHE PHE B . n B 2 320 SER 320 320 320 SER SER B . n B 2 321 LYS 321 321 321 LYS LYS B . n B 2 322 GLU 322 322 322 GLU GLU B . n B 2 323 ALA 323 323 323 ALA ALA B . n B 2 324 LEU 324 324 324 LEU LEU B . n B 2 325 TYR 325 325 325 TYR TYR B . n B 2 326 SER 326 326 326 SER SER B . n B 2 327 VAL 327 327 327 VAL VAL B . n B 2 328 PHE 328 328 328 PHE PHE B . n B 2 329 ALA 329 329 329 ALA ALA B . n B 2 330 GLU 330 330 330 GLU GLU B . n B 2 331 MET 331 331 331 MET MET B . n B 2 332 ASN 332 332 332 ASN ASN B . n B 2 333 ILE 333 333 333 ILE ILE B . n B 2 334 LYS 334 334 334 LYS LYS B . n B 2 335 MET 335 335 335 MET MET B . n B 2 336 LEU 336 336 336 LEU LEU B . n B 2 337 SER 337 337 337 SER SER B . n B 2 338 ILE 338 338 338 ILE ILE B . n B 2 339 SER 339 339 339 SER SER B . n B 2 340 ASP 340 340 340 ASP ASP B . n B 2 341 THR 341 341 341 THR THR B . n B 2 342 PRO 342 342 342 PRO PRO B . n B 2 343 PHE 343 343 343 PHE PHE B . n B 2 344 ILE 344 344 344 ILE ILE B . n B 2 345 HIS 345 345 345 HIS HIS B . n B 2 346 MET 346 346 346 MET MET B . n B 2 347 VAL 347 347 347 VAL VAL B . n B 2 348 CYS 348 348 348 CYS CYS B . n B 2 349 PRO 349 349 349 PRO PRO B . n B 2 350 PRO 350 350 350 PRO PRO B . n B 2 351 SER 351 351 351 SER SER B . n B 2 352 PRO 352 352 352 PRO PRO B . n B 2 353 SER 353 353 353 SER SER B . n B 2 354 SER 354 354 354 SER SER B . n B 2 355 PHE 355 355 355 PHE PHE B . n B 2 356 THR 356 356 356 THR THR B . n B 2 357 PHE 357 357 357 PHE PHE B . n B 2 358 LEU 358 358 358 LEU LEU B . n B 2 359 ASN 359 359 359 ASN ASN B . n B 2 360 PHE 360 360 360 PHE PHE B . n B 2 361 THR 361 361 361 THR THR B . n B 2 362 GLN 362 362 362 GLN GLN B . n B 2 363 ASN 363 363 363 ASN ASN B . n B 2 364 VAL 364 364 364 VAL VAL B . n B 2 365 PHE 365 365 365 PHE PHE B . n B 2 366 THR 366 366 366 THR THR B . n B 2 367 ASP 367 367 367 ASP ASP B . n B 2 368 SER 368 368 368 SER SER B . n B 2 369 VAL 369 369 369 VAL VAL B . n B 2 370 PHE 370 370 370 PHE PHE B . n B 2 371 GLN 371 371 371 GLN GLN B . n B 2 372 GLY 372 372 372 GLY GLY B . n B 2 373 CYS 373 373 373 CYS CYS B . n B 2 374 SER 374 374 374 SER SER B . n B 2 375 THR 375 375 375 THR THR B . n B 2 376 LEU 376 376 376 LEU LEU B . n B 2 377 LYS 377 377 377 LYS LYS B . n B 2 378 ARG 378 378 378 ARG ARG B . n B 2 379 LEU 379 379 379 LEU LEU B . n B 2 380 GLN 380 380 380 GLN GLN B . n B 2 381 THR 381 381 381 THR THR B . n B 2 382 LEU 382 382 382 LEU LEU B . n B 2 383 ILE 383 383 383 ILE ILE B . n B 2 384 LEU 384 384 384 LEU LEU B . n B 2 385 GLN 385 385 385 GLN GLN B . n B 2 386 ARG 386 386 386 ARG ARG B . n B 2 387 ASN 387 387 387 ASN ASN B . n B 2 388 GLY 388 388 388 GLY GLY B . n B 2 389 LEU 389 389 389 LEU LEU B . n B 2 390 LYS 390 390 390 LYS LYS B . n B 2 391 ASN 391 391 391 ASN ASN B . n B 2 392 PHE 392 392 392 PHE PHE B . n B 2 393 PHE 393 393 393 PHE PHE B . n B 2 394 LYS 394 394 394 LYS LYS B . n B 2 395 VAL 395 395 395 VAL VAL B . n B 2 396 ALA 396 396 396 ALA ALA B . n B 2 397 LEU 397 397 397 LEU LEU B . n B 2 398 MET 398 398 398 MET MET B . n B 2 399 THR 399 399 399 THR THR B . n B 2 400 LYS 400 400 400 LYS LYS B . n B 2 401 ASN 401 401 401 ASN ASN B . n B 2 402 MET 402 402 402 MET MET B . n B 2 403 SER 403 403 403 SER SER B . n B 2 404 SER 404 404 404 SER SER B . n B 2 405 LEU 405 405 405 LEU LEU B . n B 2 406 GLU 406 406 406 GLU GLU B . n B 2 407 THR 407 407 407 THR THR B . n B 2 408 LEU 408 408 408 LEU LEU B . n B 2 409 ASP 409 409 409 ASP ASP B . n B 2 410 VAL 410 410 410 VAL VAL B . n B 2 411 SER 411 411 411 SER SER B . n B 2 412 LEU 412 412 412 LEU LEU B . n B 2 413 ASN 413 413 413 ASN ASN B . n B 2 414 SER 414 414 414 SER SER B . n B 2 415 LEU 415 415 415 LEU LEU B . n B 2 416 ASN 416 416 416 ASN ASN B . n B 2 417 SER 417 417 417 SER SER B . n B 2 418 HIS 418 418 418 HIS HIS B . n B 2 419 ALA 419 419 419 ALA ALA B . n B 2 420 TYR 420 420 420 TYR TYR B . n B 2 421 ASP 421 421 421 ASP ASP B . n B 2 422 ARG 422 422 422 ARG ARG B . n B 2 423 THR 423 423 423 THR THR B . n B 2 424 CYS 424 424 424 CYS CYS B . n B 2 425 ALA 425 425 425 ALA ALA B . n B 2 426 TRP 426 426 426 TRP TRP B . n B 2 427 ALA 427 427 427 ALA ALA B . n B 2 428 GLU 428 428 428 GLU GLU B . n B 2 429 SER 429 429 429 SER SER B . n B 2 430 ILE 430 430 430 ILE ILE B . n B 2 431 LEU 431 431 431 LEU LEU B . n B 2 432 VAL 432 432 432 VAL VAL B . n B 2 433 LEU 433 433 433 LEU LEU B . n B 2 434 ASN 434 434 434 ASN ASN B . n B 2 435 LEU 435 435 435 LEU LEU B . n B 2 436 SER 436 436 436 SER SER B . n B 2 437 SER 437 437 437 SER SER B . n B 2 438 ASN 438 438 438 ASN ASN B . n B 2 439 MET 439 439 439 MET MET B . n B 2 440 LEU 440 440 440 LEU LEU B . n B 2 441 THR 441 441 441 THR THR B . n B 2 442 GLY 442 442 442 GLY GLY B . n B 2 443 SER 443 443 443 SER SER B . n B 2 444 VAL 444 444 444 VAL VAL B . n B 2 445 PHE 445 445 445 PHE PHE B . n B 2 446 ARG 446 446 446 ARG ARG B . n B 2 447 CYS 447 447 447 CYS CYS B . n B 2 448 LEU 448 448 448 LEU LEU B . n B 2 449 PRO 449 449 449 PRO PRO B . n B 2 450 PRO 450 450 450 PRO PRO B . n B 2 451 LYS 451 451 451 LYS LYS B . n B 2 452 VAL 452 452 452 VAL VAL B . n B 2 453 LYS 453 453 453 LYS LYS B . n B 2 454 VAL 454 454 454 VAL VAL B . n B 2 455 LEU 455 455 455 LEU LEU B . n B 2 456 ASP 456 456 456 ASP ASP B . n B 2 457 LEU 457 457 457 LEU LEU B . n B 2 458 HIS 458 458 458 HIS HIS B . n B 2 459 ASN 459 459 459 ASN ASN B . n B 2 460 ASN 460 460 460 ASN ASN B . n B 2 461 ARG 461 461 461 ARG ARG B . n B 2 462 ILE 462 462 462 ILE ILE B . n B 2 463 MET 463 463 463 MET MET B . n B 2 464 SER 464 464 464 SER SER B . n B 2 465 ILE 465 465 465 ILE ILE B . n B 2 466 PRO 466 466 466 PRO PRO B . n B 2 467 LYS 467 467 467 LYS LYS B . n B 2 468 ASP 468 468 468 ASP ASP B . n B 2 469 VAL 469 469 469 VAL VAL B . n B 2 470 THR 470 470 470 THR THR B . n B 2 471 HIS 471 471 471 HIS HIS B . n B 2 472 LEU 472 472 472 LEU LEU B . n B 2 473 GLN 473 473 473 GLN GLN B . n B 2 474 ALA 474 474 474 ALA ALA B . n B 2 475 LEU 475 475 475 LEU LEU B . n B 2 476 GLN 476 476 476 GLN GLN B . n B 2 477 GLU 477 477 477 GLU GLU B . n B 2 478 LEU 478 478 478 LEU LEU B . n B 2 479 ASN 479 479 479 ASN ASN B . n B 2 480 VAL 480 480 480 VAL VAL B . n B 2 481 ALA 481 481 481 ALA ALA B . n B 2 482 SER 482 482 482 SER SER B . n B 2 483 ASN 483 483 483 ASN ASN B . n B 2 484 GLN 484 484 484 GLN GLN B . n B 2 485 LEU 485 485 485 LEU LEU B . n B 2 486 LYS 486 486 486 LYS LYS B . n B 2 487 SER 487 487 487 SER SER B . n B 2 488 VAL 488 488 488 VAL VAL B . n B 2 489 PRO 489 489 489 PRO PRO B . n B 2 490 ASP 490 490 490 ASP ASP B . n B 2 491 GLY 491 491 491 GLY GLY B . n B 2 492 VAL 492 492 492 VAL VAL B . n B 2 493 PHE 493 493 493 PHE PHE B . n B 2 494 ASP 494 494 494 ASP ASP B . n B 2 495 ARG 495 495 495 ARG ARG B . n B 2 496 LEU 496 496 496 LEU LEU B . n B 2 497 THR 497 497 497 THR THR B . n B 2 498 SER 498 498 498 SER SER B . n B 2 499 LEU 499 499 499 LEU LEU B . n B 2 500 GLN 500 500 500 GLN GLN B . n B 2 501 TYR 501 501 501 TYR TYR B . n B 2 502 ILE 502 502 502 ILE ILE B . n B 2 503 TRP 503 503 503 TRP TRP B . n B 2 504 LEU 504 504 504 LEU LEU B . n B 2 505 HIS 505 505 505 HIS HIS B . n B 2 506 ASP 506 506 506 ASP ASP B . n B 2 507 ASN 507 507 507 ASN ASN B . n B 2 508 PRO 508 508 508 PRO PRO B . n B 2 509 TRP 509 509 509 TRP TRP B . n B 2 510 ASP 510 510 510 ASP ASP B . n B 2 511 CYS 511 511 511 CYS CYS B . n B 2 512 THR 512 512 512 THR THR B . n B 2 513 CYS 513 513 513 CYS CYS B . n B 2 514 PRO 514 514 514 PRO PRO B . n B 2 515 GLY 515 515 515 GLY GLY B . n B 2 516 ILE 516 516 516 ILE ILE B . n B 2 517 ARG 517 517 517 ARG ARG B . n B 2 518 TYR 518 518 518 TYR TYR B . n B 2 519 LEU 519 519 519 LEU LEU B . n B 2 520 SER 520 520 520 SER SER B . n B 2 521 GLU 521 521 521 GLU GLU B . n B 2 522 TRP 522 522 522 TRP TRP B . n B 2 523 ILE 523 523 523 ILE ILE B . n B 2 524 ASN 524 524 524 ASN ASN B . n B 2 525 LYS 525 525 525 LYS LYS B . n B 2 526 HIS 526 526 526 HIS HIS B . n B 2 527 SER 527 527 527 SER SER B . n B 2 528 GLY 528 528 528 GLY GLY B . n B 2 529 VAL 529 529 529 VAL VAL B . n B 2 530 VAL 530 530 530 VAL VAL B . n B 2 531 ARG 531 531 531 ARG ARG B . n B 2 532 ASN 532 532 532 ASN ASN B . n B 2 533 SER 533 533 533 SER SER B . n B 2 534 ALA 534 534 534 ALA ALA B . n B 2 535 GLY 535 535 535 GLY GLY B . n B 2 536 SER 536 536 536 SER SER B . n B 2 537 VAL 537 537 537 VAL VAL B . n B 2 538 ALA 538 538 538 ALA ALA B . n B 2 539 PRO 539 539 539 PRO PRO B . n B 2 540 ASP 540 540 540 ASP ASP B . n B 2 541 SER 541 541 541 SER SER B . n B 2 542 ALA 542 542 542 ALA ALA B . n B 2 543 LYS 543 543 543 LYS LYS B . n B 2 544 CYS 544 544 544 CYS CYS B . n B 2 545 SER 545 545 545 SER SER B . n B 2 546 GLY 546 546 546 GLY GLY B . n B 2 547 SER 547 547 547 SER SER B . n B 2 548 GLY 548 548 548 GLY GLY B . n B 2 549 LYS 549 549 549 LYS LYS B . n B 2 550 PRO 550 550 550 PRO PRO B . n B 2 551 VAL 551 551 551 VAL VAL B . n B 2 552 ARG 552 552 552 ARG ARG B . n B 2 553 SER 553 553 553 SER SER B . n B 2 554 ILE 554 554 554 ILE ILE B . n B 2 555 ILE 555 555 555 ILE ILE B . n B 2 556 CYS 556 556 556 CYS CYS B . n B 2 557 PRO 557 557 557 PRO PRO B . n B 2 558 THR 558 558 ? ? ? B . n B 2 559 LEU 559 559 ? ? ? B . n B 2 560 VAL 560 560 ? ? ? B . n B 2 561 PRO 561 561 ? ? ? B . n B 2 562 ARG 562 562 ? ? ? B . n C 3 1 CYS 1 11 11 CYS CYS C . n C 3 2 SER 2 12 12 SER SER C . n C 3 3 LYS 3 13 13 LYS LYS C . n C 3 4 LYS 4 14 14 LYS LYS C . n C 3 5 LYS 5 15 15 LYS LYS C . n C 3 6 LYS 6 16 16 LYS LYS C . 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 D 4 NAG 1 811 811 NAG NAG A . E 4 NAG 1 821 821 NAG NAG A . F 4 NAG 1 831 831 NAG NAG A . G 4 NAG 2 832 832 NAG NAG A . H 4 NAG 1 911 911 NAG NAG B . I 4 NAG 1 921 921 NAG NAG B . J 4 NAG 1 931 931 NAG NAG B . K 4 NAG 2 932 932 NAG NAG B . L 4 NAG 1 941 941 NAG NAG B . M 4 NAG 2 942 942 NAG NAG B . N 5 BMA 3 943 943 BMA BMA B . O 4 NAG 1 951 951 NAG NAG B . P 4 NAG 2 952 952 NAG NAG B . Q 5 BMA 3 953 953 BMA BMA B . R 4 NAG 1 961 961 NAG NAG B . S 4 NAG 2 962 962 NAG NAG B . T 5 BMA 3 963 963 BMA BMA B . U 6 NDG 1 971 971 NDG NDG B . V 4 NAG 2 972 972 NAG NAG B . W 4 NAG 1 981 981 NAG NAG B . X 7 PXS 1 581 581 PXS PXS C . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 147 A ASN 147 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 414 A ASN 414 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 442 A ASN 442 ? ASN 'GLYCOSYLATION SITE' 4 B ASN 144 B ASN 144 ? ASN 'GLYCOSYLATION SITE' 5 B ASN 195 B ASN 195 ? ASN 'GLYCOSYLATION SITE' 6 B ASN 214 B ASN 214 ? ASN 'GLYCOSYLATION SITE' 7 B ASN 253 B ASN 253 ? ASN 'GLYCOSYLATION SITE' 8 B ASN 285 B ASN 285 ? ASN 'GLYCOSYLATION SITE' 9 B ASN 359 B ASN 359 ? ASN 'GLYCOSYLATION SITE' 10 B ASN 401 B ASN 401 ? ASN 'GLYCOSYLATION SITE' 11 B ASN 434 B ASN 434 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details trimeric _pdbx_struct_assembly.oligomeric_count 3 # _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 # 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)' 7620 ? 1 MORE 53 ? 1 'SSA (A^2)' 47840 ? # _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_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 2009-11-24 2 'Structure model' 1 1 2011-07-13 3 'Structure model' 1 2 2012-06-27 4 'Structure model' 1 3 2017-08-09 5 'Structure model' 1 4 2017-08-16 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Non-polymer description' 2 2 'Structure model' 'Version format compliance' 3 3 'Structure model' 'Non-polymer description' 4 4 'Structure model' 'Source and taxonomy' 5 5 'Structure model' 'Source and taxonomy' # loop_ _pdbx_audit_revision_category.ordinal _pdbx_audit_revision_category.revision_ordinal _pdbx_audit_revision_category.data_content_type _pdbx_audit_revision_category.category 1 4 'Structure model' entity_src_gen 2 5 'Structure model' pdbx_entity_src_syn # loop_ _pdbx_audit_revision_item.ordinal _pdbx_audit_revision_item.revision_ordinal _pdbx_audit_revision_item.data_content_type _pdbx_audit_revision_item.item 1 5 'Structure model' '_pdbx_entity_src_syn.ncbi_taxonomy_id' 2 5 'Structure model' '_pdbx_entity_src_syn.organism_scientific' # loop_ _pdbx_refine_tls.pdbx_refine_id _pdbx_refine_tls.id _pdbx_refine_tls.details _pdbx_refine_tls.method _pdbx_refine_tls.origin_x _pdbx_refine_tls.origin_y _pdbx_refine_tls.origin_z _pdbx_refine_tls.T[1][1] _pdbx_refine_tls.T[2][2] _pdbx_refine_tls.T[3][3] _pdbx_refine_tls.T[1][2] _pdbx_refine_tls.T[1][3] _pdbx_refine_tls.T[2][3] _pdbx_refine_tls.L[1][1] _pdbx_refine_tls.L[2][2] _pdbx_refine_tls.L[3][3] _pdbx_refine_tls.L[1][2] _pdbx_refine_tls.L[1][3] _pdbx_refine_tls.L[2][3] _pdbx_refine_tls.S[1][1] _pdbx_refine_tls.S[2][2] _pdbx_refine_tls.S[3][3] _pdbx_refine_tls.S[1][2] _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][2] 'X-RAY DIFFRACTION' 1 ? refined 14.6701 -35.8269 15.2995 0.3303 0.1446 0.3728 0.0646 -0.1518 -0.0488 2.2887 0.7151 1.3447 -0.8401 0.9857 -0.1251 0.2079 -0.0438 -0.1429 0.0934 0.0862 -0.0604 -0.1321 0.2734 0.0322 'X-RAY DIFFRACTION' 2 ? refined 55.8446 -34.5506 35.5039 0.3214 0.3344 0.2798 -0.0689 -0.0721 -0.0761 1.8496 1.1234 1.3299 -0.3520 0.1094 0.0207 -0.0058 -0.0532 0.0509 -0.2448 0.1595 0.0233 -0.0351 -0.2779 0.2688 'X-RAY DIFFRACTION' 3 ? refined 21.0865 -41.9193 42.8576 0.6976 0.6385 0.6195 0.0681 -0.4255 -0.1103 0.6819 0.7414 -0.3202 -0.0475 -0.6433 -0.0021 0.0239 0.0906 -0.0124 -0.4467 0.1462 0.2312 -0.0866 -0.0186 0.0657 # loop_ _pdbx_refine_tls_group.pdbx_refine_id _pdbx_refine_tls_group.id _pdbx_refine_tls_group.refine_tls_id _pdbx_refine_tls_group.beg_auth_asym_id _pdbx_refine_tls_group.beg_auth_seq_id _pdbx_refine_tls_group.end_auth_asym_id _pdbx_refine_tls_group.end_auth_seq_id _pdbx_refine_tls_group.selection_details _pdbx_refine_tls_group.beg_label_asym_id _pdbx_refine_tls_group.beg_label_seq_id _pdbx_refine_tls_group.end_label_asym_id _pdbx_refine_tls_group.end_label_seq_id _pdbx_refine_tls_group.selection 'X-RAY DIFFRACTION' 1 1 A 26 A 575 'chain A' ? ? ? ? ? 'X-RAY DIFFRACTION' 2 2 B 33 B 557 'chain B' ? ? ? ? ? 'X-RAY DIFFRACTION' 3 3 A 10 C 16 'chain C' ? ? ? ? ? # loop_ _software.pdbx_ordinal _software.name _software.version _software.date _software.type _software.contact_author _software.contact_author_email _software.classification _software.location _software.language _software.citation_id 1 PHENIX . ? package 'Paul D. Adams' PDAdams@lbl.gov refinement http://www.phenix-online.org/ C++ ? 2 PDB_EXTRACT 3.005 'June 11, 2008' package PDB help@deposit.rcsb.org 'data extraction' http://sw-tools.pdb.org/apps/PDB_EXTRACT/ C++ ? 3 XDS . ? ? ? ? 'data reduction' ? ? ? 4 XSCALE . ? ? ? ? 'data scaling' ? ? ? 5 PHASER . ? ? ? ? phasing ? ? ? # loop_ _pdbx_validate_close_contact.id _pdbx_validate_close_contact.PDB_model_num _pdbx_validate_close_contact.auth_atom_id_1 _pdbx_validate_close_contact.auth_asym_id_1 _pdbx_validate_close_contact.auth_comp_id_1 _pdbx_validate_close_contact.auth_seq_id_1 _pdbx_validate_close_contact.PDB_ins_code_1 _pdbx_validate_close_contact.label_alt_id_1 _pdbx_validate_close_contact.auth_atom_id_2 _pdbx_validate_close_contact.auth_asym_id_2 _pdbx_validate_close_contact.auth_comp_id_2 _pdbx_validate_close_contact.auth_seq_id_2 _pdbx_validate_close_contact.PDB_ins_code_2 _pdbx_validate_close_contact.label_alt_id_2 _pdbx_validate_close_contact.dist 1 1 OD1 B ASN 218 ? ? O6 B NAG 981 ? ? 1.79 2 1 CG B ASN 195 ? ? C1 B NAG 981 ? ? 2.08 # loop_ _pdbx_validate_rmsd_angle.id _pdbx_validate_rmsd_angle.PDB_model_num _pdbx_validate_rmsd_angle.auth_atom_id_1 _pdbx_validate_rmsd_angle.auth_asym_id_1 _pdbx_validate_rmsd_angle.auth_comp_id_1 _pdbx_validate_rmsd_angle.auth_seq_id_1 _pdbx_validate_rmsd_angle.PDB_ins_code_1 _pdbx_validate_rmsd_angle.label_alt_id_1 _pdbx_validate_rmsd_angle.auth_atom_id_2 _pdbx_validate_rmsd_angle.auth_asym_id_2 _pdbx_validate_rmsd_angle.auth_comp_id_2 _pdbx_validate_rmsd_angle.auth_seq_id_2 _pdbx_validate_rmsd_angle.PDB_ins_code_2 _pdbx_validate_rmsd_angle.label_alt_id_2 _pdbx_validate_rmsd_angle.auth_atom_id_3 _pdbx_validate_rmsd_angle.auth_asym_id_3 _pdbx_validate_rmsd_angle.auth_comp_id_3 _pdbx_validate_rmsd_angle.auth_seq_id_3 _pdbx_validate_rmsd_angle.PDB_ins_code_3 _pdbx_validate_rmsd_angle.label_alt_id_3 _pdbx_validate_rmsd_angle.angle_value _pdbx_validate_rmsd_angle.angle_target_value _pdbx_validate_rmsd_angle.angle_deviation _pdbx_validate_rmsd_angle.angle_standard_deviation _pdbx_validate_rmsd_angle.linker_flag 1 1 C A ASN 134 ? ? N A PRO 135 ? ? CA A PRO 135 ? ? 128.56 119.30 9.26 1.50 Y 2 1 C A SER 249 ? ? N A PRO 250 ? ? CA A PRO 250 ? ? 129.11 119.30 9.81 1.50 Y # 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 SER A 29 ? ? -99.19 -127.76 2 1 CYS A 30 ? ? 141.12 177.16 3 1 ARG A 39 ? ? -59.62 -119.64 4 1 SER A 40 ? ? -77.33 20.04 5 1 SER A 42 ? ? -67.18 89.37 6 1 PRO A 47 ? ? -36.60 121.16 7 1 LEU A 59 ? ? -113.91 51.10 8 1 PHE A 61 ? ? 71.40 44.51 9 1 LYS A 63 ? ? -105.73 52.01 10 1 SER A 86 ? ? -80.53 -145.98 11 1 ASP A 109 ? ? 70.50 38.08 12 1 HIS A 111 ? ? -103.90 40.37 13 1 LEU A 112 ? ? -68.37 95.75 14 1 LEU A 123 ? ? -86.85 46.68 15 1 SER A 124 ? ? -50.71 -7.63 16 1 PRO A 135 ? ? -66.12 30.98 17 1 ASN A 147 ? ? -105.29 49.01 18 1 LEU A 186 ? ? -53.31 100.35 19 1 GLN A 192 ? ? 82.13 18.64 20 1 ARG A 236 ? ? -118.74 53.33 21 1 SER A 240 ? ? -172.12 142.88 22 1 VAL A 244 ? ? -38.82 154.39 23 1 GLU A 246 ? ? -58.87 86.36 24 1 ARG A 257 ? ? -87.98 -78.68 25 1 ILE A 276 ? ? -115.00 71.70 26 1 ASP A 285 ? ? -92.18 -133.09 27 1 ASP A 286 ? ? -64.97 71.14 28 1 LEU A 292 ? ? -150.50 19.97 29 1 SER A 298 ? ? -44.55 153.55 30 1 GLN A 321 ? ? -111.24 54.42 31 1 LEU A 350 ? ? -170.57 128.83 32 1 ASN A 370 ? ? -115.64 -151.79 33 1 ALA A 381 ? ? -109.85 68.51 34 1 TRP A 386 ? ? 39.86 51.20 35 1 ASN A 397 ? ? -103.33 -154.36 36 1 SER A 417 ? ? -160.89 113.13 37 1 THR A 424 ? ? -60.91 66.00 38 1 ASN A 467 ? ? -126.69 -147.83 39 1 LEU A 479 ? ? -49.01 106.64 40 1 ILE A 484 ? ? -145.32 37.46 41 1 SER A 485 ? ? -69.56 -165.83 42 1 ARG A 486 ? ? 25.43 60.56 43 1 PHE A 498 ? ? -158.06 77.92 44 1 LEU A 501 ? ? -33.15 143.14 45 1 MET A 504 ? ? -152.53 89.53 46 1 SER A 508 ? ? 29.17 49.90 47 1 ASN A 509 ? ? -116.47 -165.76 48 1 PHE A 519 ? ? -86.74 35.86 49 1 THR A 523 ? ? -68.51 13.98 50 1 SER A 524 ? ? -130.11 -32.75 51 1 LYS A 527 ? ? -171.47 143.62 52 1 LEU A 530 ? ? -142.42 -10.55 53 1 HIS A 531 ? ? -47.28 -175.48 54 1 THR A 532 ? ? 26.95 83.92 55 1 TRP A 535 ? ? -90.63 -141.60 56 1 ASP A 536 ? ? -170.23 83.48 57 1 ILE A 542 ? ? -80.02 48.39 58 1 ASP A 543 ? ? -65.89 -76.74 59 1 TYR A 544 ? ? -52.53 -70.88 60 1 GLU A 556 ? ? 166.05 123.09 61 1 SER A 563 ? ? -63.34 93.06 62 1 ILE A 572 ? ? -10.75 130.29 63 1 ASN B 40 ? ? 56.76 8.06 64 1 THR B 44 ? ? -138.26 -31.38 65 1 PRO B 47 ? ? -32.57 101.71 66 1 ASN B 62 ? ? -123.64 -156.62 67 1 ASN B 86 ? ? -123.99 -149.75 68 1 GLN B 100 ? ? -59.29 -3.71 69 1 SER B 108 ? ? -58.24 176.02 70 1 ASN B 110 ? ? -104.57 -143.16 71 1 GLN B 113 ? ? -149.65 -25.19 72 1 ASN B 131 ? ? -128.97 -163.33 73 1 LEU B 136 ? ? -33.08 113.60 74 1 PHE B 142 ? ? -54.07 -8.69 75 1 LYS B 184 ? ? -124.56 -147.81 76 1 GLU B 187 ? ? -65.65 71.98 77 1 THR B 188 ? ? -30.86 127.07 78 1 LEU B 191 ? ? -169.07 117.91 79 1 ASN B 206 ? ? -140.38 46.27 80 1 ASN B 218 ? ? -94.19 -75.34 81 1 ASN B 227 ? ? 74.09 71.07 82 1 ASN B 231 ? ? -108.44 -157.69 83 1 PRO B 249 ? ? -60.61 -119.77 84 1 THR B 250 ? ? -74.16 -146.11 85 1 GLU B 301 ? ? -33.53 128.97 86 1 HIS B 311 ? ? 75.76 91.25 87 1 ASN B 332 ? ? -105.94 50.04 88 1 PHE B 360 ? ? -109.77 66.63 89 1 ASN B 363 ? ? -119.28 -144.91 90 1 ARG B 386 ? ? 75.32 48.91 91 1 ASN B 387 ? ? -128.35 -159.08 92 1 PHE B 392 ? ? -37.41 -31.73 93 1 MET B 402 ? ? -112.60 53.56 94 1 SER B 403 ? ? -41.29 -7.34 95 1 ASN B 413 ? ? -97.76 -149.20 96 1 ARG B 422 ? ? -98.40 43.04 97 1 ALA B 425 ? ? -156.03 41.66 98 1 SER B 437 ? ? 76.28 48.88 99 1 ASN B 438 ? ? -126.70 -145.07 100 1 LYS B 451 ? ? -99.47 38.43 101 1 ASN B 460 ? ? -115.71 -154.22 102 1 SER B 464 ? ? -48.61 84.24 103 1 LYS B 467 ? ? -94.82 37.04 104 1 GLN B 473 ? ? -108.15 79.82 105 1 ALA B 474 ? ? -166.86 -1.63 106 1 GLN B 476 ? ? -133.52 -35.63 107 1 ALA B 481 ? ? -56.03 -176.83 108 1 SER B 482 ? ? 22.47 56.82 109 1 ASN B 483 ? ? -118.54 -148.28 110 1 VAL B 492 ? ? -94.47 -75.31 111 1 PHE B 493 ? ? -47.52 -1.30 112 1 LEU B 496 ? ? -73.43 47.69 113 1 GLN B 500 ? ? -150.32 -19.97 114 1 HIS B 505 ? ? -57.41 178.60 115 1 SER B 533 ? ? -62.92 1.15 116 1 ALA B 538 ? ? -167.64 97.12 117 1 LYS C 14 ? ? -74.79 -123.09 # _pdbx_validate_peptide_omega.id 1 _pdbx_validate_peptide_omega.PDB_model_num 1 _pdbx_validate_peptide_omega.auth_comp_id_1 GLY _pdbx_validate_peptide_omega.auth_asym_id_1 B _pdbx_validate_peptide_omega.auth_seq_id_1 248 _pdbx_validate_peptide_omega.PDB_ins_code_1 ? _pdbx_validate_peptide_omega.label_alt_id_1 ? _pdbx_validate_peptide_omega.auth_comp_id_2 PRO _pdbx_validate_peptide_omega.auth_asym_id_2 B _pdbx_validate_peptide_omega.auth_seq_id_2 249 _pdbx_validate_peptide_omega.PDB_ins_code_2 ? _pdbx_validate_peptide_omega.label_alt_id_2 ? _pdbx_validate_peptide_omega.omega 142.77 # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A MET 1 ? A MET 1 2 1 Y 1 A LEU 2 ? A LEU 2 3 1 Y 1 A ARG 3 ? A ARG 3 4 1 Y 1 A ALA 4 ? A ALA 4 5 1 Y 1 A LEU 5 ? A LEU 5 6 1 Y 1 A TRP 6 ? A TRP 6 7 1 Y 1 A LEU 7 ? A LEU 7 8 1 Y 1 A PHE 8 ? A PHE 8 9 1 Y 1 A TRP 9 ? A TRP 9 10 1 Y 1 A ILE 10 ? A ILE 10 11 1 Y 1 A LEU 11 ? A LEU 11 12 1 Y 1 A VAL 12 ? A VAL 12 13 1 Y 1 A ALA 13 ? A ALA 13 14 1 Y 1 A ILE 14 ? A ILE 14 15 1 Y 1 A THR 15 ? A THR 15 16 1 Y 1 A VAL 16 ? A VAL 16 17 1 Y 1 A LEU 17 ? A LEU 17 18 1 Y 1 A PHE 18 ? A PHE 18 19 1 Y 1 A SER 19 ? A SER 19 20 1 Y 1 A LYS 20 ? A LYS 20 21 1 Y 1 A ARG 21 ? A ARG 21 22 1 Y 1 A CYS 22 ? A CYS 22 23 1 Y 1 A SER 23 ? A SER 23 24 1 Y 1 A ALA 24 ? A ALA 24 25 1 Y 1 A GLN 25 ? A GLN 25 26 1 Y 1 A THR 576 ? A THR 576 27 1 Y 1 A LEU 577 ? A LEU 577 28 1 Y 1 A VAL 578 ? A VAL 578 29 1 Y 1 A PRO 579 ? A PRO 579 30 1 Y 1 A ARG 580 ? A ARG 580 31 1 Y 1 B MET 1 ? B MET 1 32 1 Y 1 B SER 2 ? B SER 2 33 1 Y 1 B GLN 3 ? B GLN 3 34 1 Y 1 B ASP 4 ? B ASP 4 35 1 Y 1 B ARG 5 ? B ARG 5 36 1 Y 1 B LYS 6 ? B LYS 6 37 1 Y 1 B PRO 7 ? B PRO 7 38 1 Y 1 B ILE 8 ? B ILE 8 39 1 Y 1 B VAL 9 ? B VAL 9 40 1 Y 1 B GLY 10 ? B GLY 10 41 1 Y 1 B SER 11 ? B SER 11 42 1 Y 1 B PHE 12 ? B PHE 12 43 1 Y 1 B HIS 13 ? B HIS 13 44 1 Y 1 B PHE 14 ? B PHE 14 45 1 Y 1 B VAL 15 ? B VAL 15 46 1 Y 1 B CYS 16 ? B CYS 16 47 1 Y 1 B ALA 17 ? B ALA 17 48 1 Y 1 B LEU 18 ? B LEU 18 49 1 Y 1 B ALA 19 ? B ALA 19 50 1 Y 1 B LEU 20 ? B LEU 20 51 1 Y 1 B ILE 21 ? B ILE 21 52 1 Y 1 B VAL 22 ? B VAL 22 53 1 Y 1 B GLY 23 ? B GLY 23 54 1 Y 1 B SER 24 ? B SER 24 55 1 Y 1 B MET 25 ? B MET 25 56 1 Y 1 B THR 26 ? B THR 26 57 1 Y 1 B PRO 27 ? B PRO 27 58 1 Y 1 B PHE 28 ? B PHE 28 59 1 Y 1 B SER 29 ? B SER 29 60 1 Y 1 B ASN 30 ? B ASN 30 61 1 Y 1 B GLU 31 ? B GLU 31 62 1 Y 1 B LEU 32 ? B LEU 32 63 1 Y 1 B THR 558 ? B THR 558 64 1 Y 1 B LEU 559 ? B LEU 559 65 1 Y 1 B VAL 560 ? B VAL 560 66 1 Y 1 B PRO 561 ? B PRO 561 67 1 Y 1 B ARG 562 ? B ARG 562 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 4 N-ACETYL-D-GLUCOSAMINE NAG 5 BETA-D-MANNOSE BMA 6 '2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE' NDG 7 '(2S)-propane-1,2-diyl dihexadecanoate' PXS #