data_4BDS # _entry.id 4BDS # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.286 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 4BDS PDBE EBI-54265 WWPDB D_1290054265 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.content_type _pdbx_database_related.details PDB 1EHO unspecified 'MODEL OF (-)-COCAINE-BOUND BCHE COMPLEX.' PDB 1EHQ unspecified 'MODEL OF (+)-COCAINE-BOUND BCHE COMPLEX' PDB 1KCJ unspecified 'MODEL OF (-)-COCAINE-BOUND (-)-COCAINE HYDROLASE COMPLEX' PDB 1P0I unspecified 'CRYSTAL STRUCTURE OF HUMAN BUTYRYL CHOLINESTERASE' PDB 1P0M unspecified 'CRYSTAL STRUCTURE OF HUMAN BUTYRYL CHOLINESTERASE INCOMPLEX WITH A CHOLINE MOLECULE' PDB 1P0P unspecified 'CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH THE SUBSTRATE ANALOGBUTYRYLTHIOCHOLINE' PDB 1P0Q unspecified 'CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN BUTYRYL CHOLINESTERASE' PDB 1XLU unspecified 'X-RAY STRUCTURE OF DI-ISOPROPYL-PHOSPHORO-FLUORIDATE ( DFP)INHIBITED BUTYRYLCHOLINESTERASE AFTER AGING' PDB 1XLV unspecified 'ETHYLPHOSPHORYLATED BUTYRYLCHOLINESTERASE (AGED) OBTAINEDBY REACTION WITH ECHOTHIOPHATE' PDB 1XLW unspecified 'DIETHYLPHOSPHORYLATED BUTYRYLCHOLINESTERASE (NONAGED)OBTAINED BY REACTION WITH ECHOTHIOPHATE' PDB 2J4C unspecified 'STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH 10MM HGCL2' PDB 2WID unspecified 'AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY TABUN ANALOGUE TA1' PDB 2WIF unspecified 'AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY TABUN ANALOGUE TA1' PDB 2WIG unspecified 'NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY TABUN ANALOGUE TA4' PDB 2WIJ unspecified 'NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY TABUN ANALOGUE TA5' PDB 2WIK unspecified 'NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY TABUN ANALOGUE TA6' PDB 2WIL unspecified 'AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY TABUN ANALOGUE TA5' PDB 2WSL unspecified 'AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY TABUN ANALOGUE TA4' PDB 2XMB unspecified 'G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH SULFATE' PDB 2XMC unspecified 'G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH FLUORIDE ANION' PDB 2XMD unspecified 'G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH ECHOTHIOPHATE' PDB 2XMG unspecified 'G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH VX' PDB 2XQF unspecified 'X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY RACEMIC VX' PDB 2XQG unspecified 'X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY RACEMIC VR' PDB 2XQI unspecified 'X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY RACEMIC CVX' PDB 2XQJ unspecified 'X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY PURE ENANTIOMER VX-(R)' PDB 2XQK unspecified 'X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY PURE ENANTIOMER VX-(S)' PDB 2Y1K unspecified 'STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY CBDP (12H SOAK): PHOSPHOSERINE ADDUCT' PDB 4AQD unspecified 'CRYSTAL STRUCTURE OF FULLY GLYCOSYLATED HUMAN BUTYRYLCHOLINESTERASE' PDB 4AXB unspecified 'CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH 2-PAM' PDB 4B0O unspecified 'CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH BENZYL PYRIDINIUM-4 -METHYLTRICHLOROACETIMIDATE' PDB 4B0P unspecified 'CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH METHYL 2-( PENTAFLUOROBENZYLOXYIMINO)PYRIDINIUM' PDB 4BBZ unspecified 'STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY CBDP (2-MIN SOAK): CRESYL-PHOSPHOSERINE ADDUCT' # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4BDS _pdbx_database_status.deposit_site PDBE _pdbx_database_status.process_site PDBE _pdbx_database_status.SG_entry . _pdbx_database_status.recvd_initial_deposition_date 2012-10-06 _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_sf ? _pdbx_database_status.status_code_mr ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Nachon, F.' 1 'Carletti, E.' 2 'Ronco, C.' 3 'Trovaslet, M.' 4 'Nicolet, Y.' 5 'Jean, L.' 6 'Renard, P.-Y.' 7 # _citation.id primary _citation.title ;Crystal Structures of Human Cholinesterases in Complex with Huprine W and Tacrine: Elements of Specificity for Anti-Alzheimer'S Drugs Targeting Acetyl- and Butyrylcholinesterase. ; _citation.journal_abbrev Biochem.J. _citation.journal_volume 453 _citation.page_first 393 _citation.page_last ? _citation.year 2013 _citation.journal_id_ASTM BIJOAK _citation.country UK _citation.journal_id_ISSN 0264-6021 _citation.journal_id_CSD 0043 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 23679855 _citation.pdbx_database_id_DOI 10.1042/BJ20130013 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Nachon, F.' 1 primary 'Carletti, E.' 2 primary 'Ronco, C.' 3 primary 'Trovaslet, M.' 4 primary 'Nicolet, Y.' 5 primary 'Jean, L.' 6 primary 'Renard, P.' 7 # _cell.entry_id 4BDS _cell.length_a 155.660 _cell.length_b 155.660 _cell.length_c 127.880 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 16 _cell.pdbx_unique_axis ? # _symmetry.entry_id 4BDS _symmetry.space_group_name_H-M 'I 4 2 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 97 # 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 CHOLINESTERASE 59713.512 1 3.1.1.8 YES 'CATALYTIC DOMAIN, RESIDUES 29-557' ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 8 ? ? ? ? 3 non-polymer man ALPHA-L-FUCOSE 164.156 1 ? ? ? ? 4 non-polymer man BETA-L-FUCOSE 164.156 2 ? ? ? ? 5 non-polymer syn TACRINE 198.264 1 ? ? ? ? 6 non-polymer syn GLYCEROL 92.094 1 ? ? ? ? 7 non-polymer syn 'SULFATE ION' 96.063 2 ? ? ? ? 8 non-polymer syn 'CHLORIDE ION' 35.453 2 ? ? ? ? 9 non-polymer syn 1-formyl-L-proline 143.141 1 ? ? ? ? 10 non-polymer syn 'UNKNOWN ATOM OR ION' ? 7 ? ? ? ? 11 water nat water 18.015 279 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'BUTYRYLCHOLINESTERASE, ACYLCHOLINE ACYLHYDROLASE, BUTYRYLCHOLINE ESTERASE, CHOLINE ESTERASE II, PSEUDOCHOLINESTERASE' # _entity_poly.entity_id 1 _entity_poly.type 'polypeptide(L)' _entity_poly.nstd_linkage no _entity_poly.nstd_monomer no _entity_poly.pdbx_seq_one_letter_code ;EDDIIIATKNGKVRGMQLTVFGGTVTAFLGIPYAQPPLGRLRFKKPQSLTKWSDIWNATKYANSCCQNIDQSFPGFHGSE MWNPNTDLSEDCLYLNVWIPAPKPKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGALGFLALPGNP EAPGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAASVSLHLLSPGSHSLFTRAILQSGSFNAPWAVTSLYEAR NRTLNLAKLTGCSRENETEIIKCLRNKDPQEILLNEAFVVPYGTPLSVNFGPTVDGDFLTDMPDILLELGQFKKTQILVG VNKDEGTAFLVYGAPGFSKDNNSIITRKEFQEGLKIFFPGVSEFGKESILFHYTDWVDDQRPENYREALGDVVGDYNFIC PALEFTKKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPLERRDQYTKAEEILSRSIVKRWANFAKYGNP QETQNQSTSWPVFKSTEQKYLTLNTESTRIMTKLRAQQCRFWTSFFPKV ; _entity_poly.pdbx_seq_one_letter_code_can ;EDDIIIATKNGKVRGMQLTVFGGTVTAFLGIPYAQPPLGRLRFKKPQSLTKWSDIWNATKYANSCCQNIDQSFPGFHGSE MWNPNTDLSEDCLYLNVWIPAPKPKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGALGFLALPGNP EAPGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAASVSLHLLSPGSHSLFTRAILQSGSFNAPWAVTSLYEAR NRTLNLAKLTGCSRENETEIIKCLRNKDPQEILLNEAFVVPYGTPLSVNFGPTVDGDFLTDMPDILLELGQFKKTQILVG VNKDEGTAFLVYGAPGFSKDNNSIITRKEFQEGLKIFFPGVSEFGKESILFHYTDWVDDQRPENYREALGDVVGDYNFIC PALEFTKKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPLERRDQYTKAEEILSRSIVKRWANFAKYGNP QETQNQSTSWPVFKSTEQKYLTLNTESTRIMTKLRAQQCRFWTSFFPKV ; _entity_poly.pdbx_strand_id A _entity_poly.pdbx_target_identifier ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 GLU n 1 2 ASP n 1 3 ASP n 1 4 ILE n 1 5 ILE n 1 6 ILE n 1 7 ALA n 1 8 THR n 1 9 LYS n 1 10 ASN n 1 11 GLY n 1 12 LYS n 1 13 VAL n 1 14 ARG n 1 15 GLY n 1 16 MET n 1 17 GLN n 1 18 LEU n 1 19 THR n 1 20 VAL n 1 21 PHE n 1 22 GLY n 1 23 GLY n 1 24 THR n 1 25 VAL n 1 26 THR n 1 27 ALA n 1 28 PHE n 1 29 LEU n 1 30 GLY n 1 31 ILE n 1 32 PRO n 1 33 TYR n 1 34 ALA n 1 35 GLN n 1 36 PRO n 1 37 PRO n 1 38 LEU n 1 39 GLY n 1 40 ARG n 1 41 LEU n 1 42 ARG n 1 43 PHE n 1 44 LYS n 1 45 LYS n 1 46 PRO n 1 47 GLN n 1 48 SER n 1 49 LEU n 1 50 THR n 1 51 LYS n 1 52 TRP n 1 53 SER n 1 54 ASP n 1 55 ILE n 1 56 TRP n 1 57 ASN n 1 58 ALA n 1 59 THR n 1 60 LYS n 1 61 TYR n 1 62 ALA n 1 63 ASN n 1 64 SER n 1 65 CYS n 1 66 CYS n 1 67 GLN n 1 68 ASN n 1 69 ILE n 1 70 ASP n 1 71 GLN n 1 72 SER n 1 73 PHE n 1 74 PRO n 1 75 GLY n 1 76 PHE n 1 77 HIS n 1 78 GLY n 1 79 SER n 1 80 GLU n 1 81 MET n 1 82 TRP n 1 83 ASN n 1 84 PRO n 1 85 ASN n 1 86 THR n 1 87 ASP n 1 88 LEU n 1 89 SER n 1 90 GLU n 1 91 ASP n 1 92 CYS n 1 93 LEU n 1 94 TYR n 1 95 LEU n 1 96 ASN n 1 97 VAL n 1 98 TRP n 1 99 ILE n 1 100 PRO n 1 101 ALA n 1 102 PRO n 1 103 LYS n 1 104 PRO n 1 105 LYS n 1 106 ASN n 1 107 ALA n 1 108 THR n 1 109 VAL n 1 110 LEU n 1 111 ILE n 1 112 TRP n 1 113 ILE n 1 114 TYR n 1 115 GLY n 1 116 GLY n 1 117 GLY n 1 118 PHE n 1 119 GLN n 1 120 THR n 1 121 GLY n 1 122 THR n 1 123 SER n 1 124 SER n 1 125 LEU n 1 126 HIS n 1 127 VAL n 1 128 TYR n 1 129 ASP n 1 130 GLY n 1 131 LYS n 1 132 PHE n 1 133 LEU n 1 134 ALA n 1 135 ARG n 1 136 VAL n 1 137 GLU n 1 138 ARG n 1 139 VAL n 1 140 ILE n 1 141 VAL n 1 142 VAL n 1 143 SER n 1 144 MET n 1 145 ASN n 1 146 TYR n 1 147 ARG n 1 148 VAL n 1 149 GLY n 1 150 ALA n 1 151 LEU n 1 152 GLY n 1 153 PHE n 1 154 LEU n 1 155 ALA n 1 156 LEU n 1 157 PRO n 1 158 GLY n 1 159 ASN n 1 160 PRO n 1 161 GLU n 1 162 ALA n 1 163 PRO n 1 164 GLY n 1 165 ASN n 1 166 MET n 1 167 GLY n 1 168 LEU n 1 169 PHE n 1 170 ASP n 1 171 GLN n 1 172 GLN n 1 173 LEU n 1 174 ALA n 1 175 LEU n 1 176 GLN n 1 177 TRP n 1 178 VAL n 1 179 GLN n 1 180 LYS n 1 181 ASN n 1 182 ILE n 1 183 ALA n 1 184 ALA n 1 185 PHE n 1 186 GLY n 1 187 GLY n 1 188 ASN n 1 189 PRO n 1 190 LYS n 1 191 SER n 1 192 VAL n 1 193 THR n 1 194 LEU n 1 195 PHE n 1 196 GLY n 1 197 GLU n 1 198 SER n 1 199 ALA n 1 200 GLY n 1 201 ALA n 1 202 ALA n 1 203 SER n 1 204 VAL n 1 205 SER n 1 206 LEU n 1 207 HIS n 1 208 LEU n 1 209 LEU n 1 210 SER n 1 211 PRO n 1 212 GLY n 1 213 SER n 1 214 HIS n 1 215 SER n 1 216 LEU n 1 217 PHE n 1 218 THR n 1 219 ARG n 1 220 ALA n 1 221 ILE n 1 222 LEU n 1 223 GLN n 1 224 SER n 1 225 GLY n 1 226 SER n 1 227 PHE n 1 228 ASN n 1 229 ALA n 1 230 PRO n 1 231 TRP n 1 232 ALA n 1 233 VAL n 1 234 THR n 1 235 SER n 1 236 LEU n 1 237 TYR n 1 238 GLU n 1 239 ALA n 1 240 ARG n 1 241 ASN n 1 242 ARG n 1 243 THR n 1 244 LEU n 1 245 ASN n 1 246 LEU n 1 247 ALA n 1 248 LYS n 1 249 LEU n 1 250 THR n 1 251 GLY n 1 252 CYS n 1 253 SER n 1 254 ARG n 1 255 GLU n 1 256 ASN n 1 257 GLU n 1 258 THR n 1 259 GLU n 1 260 ILE n 1 261 ILE n 1 262 LYS n 1 263 CYS n 1 264 LEU n 1 265 ARG n 1 266 ASN n 1 267 LYS n 1 268 ASP n 1 269 PRO n 1 270 GLN n 1 271 GLU n 1 272 ILE n 1 273 LEU n 1 274 LEU n 1 275 ASN n 1 276 GLU n 1 277 ALA n 1 278 PHE n 1 279 VAL n 1 280 VAL n 1 281 PRO n 1 282 TYR n 1 283 GLY n 1 284 THR n 1 285 PRO n 1 286 LEU n 1 287 SER n 1 288 VAL n 1 289 ASN n 1 290 PHE n 1 291 GLY n 1 292 PRO n 1 293 THR n 1 294 VAL n 1 295 ASP n 1 296 GLY n 1 297 ASP n 1 298 PHE n 1 299 LEU n 1 300 THR n 1 301 ASP n 1 302 MET n 1 303 PRO n 1 304 ASP n 1 305 ILE n 1 306 LEU n 1 307 LEU n 1 308 GLU n 1 309 LEU n 1 310 GLY n 1 311 GLN n 1 312 PHE n 1 313 LYS n 1 314 LYS n 1 315 THR n 1 316 GLN n 1 317 ILE n 1 318 LEU n 1 319 VAL n 1 320 GLY n 1 321 VAL n 1 322 ASN n 1 323 LYS n 1 324 ASP n 1 325 GLU n 1 326 GLY n 1 327 THR n 1 328 ALA n 1 329 PHE n 1 330 LEU n 1 331 VAL n 1 332 TYR n 1 333 GLY n 1 334 ALA n 1 335 PRO n 1 336 GLY n 1 337 PHE n 1 338 SER n 1 339 LYS n 1 340 ASP n 1 341 ASN n 1 342 ASN n 1 343 SER n 1 344 ILE n 1 345 ILE n 1 346 THR n 1 347 ARG n 1 348 LYS n 1 349 GLU n 1 350 PHE n 1 351 GLN n 1 352 GLU n 1 353 GLY n 1 354 LEU n 1 355 LYS n 1 356 ILE n 1 357 PHE n 1 358 PHE n 1 359 PRO n 1 360 GLY n 1 361 VAL n 1 362 SER n 1 363 GLU n 1 364 PHE n 1 365 GLY n 1 366 LYS n 1 367 GLU n 1 368 SER n 1 369 ILE n 1 370 LEU n 1 371 PHE n 1 372 HIS n 1 373 TYR n 1 374 THR n 1 375 ASP n 1 376 TRP n 1 377 VAL n 1 378 ASP n 1 379 ASP n 1 380 GLN n 1 381 ARG n 1 382 PRO n 1 383 GLU n 1 384 ASN n 1 385 TYR n 1 386 ARG n 1 387 GLU n 1 388 ALA n 1 389 LEU n 1 390 GLY n 1 391 ASP n 1 392 VAL n 1 393 VAL n 1 394 GLY n 1 395 ASP n 1 396 TYR n 1 397 ASN n 1 398 PHE n 1 399 ILE n 1 400 CYS n 1 401 PRO n 1 402 ALA n 1 403 LEU n 1 404 GLU n 1 405 PHE n 1 406 THR n 1 407 LYS n 1 408 LYS n 1 409 PHE n 1 410 SER n 1 411 GLU n 1 412 TRP n 1 413 GLY n 1 414 ASN n 1 415 ASN n 1 416 ALA n 1 417 PHE n 1 418 PHE n 1 419 TYR n 1 420 TYR n 1 421 PHE n 1 422 GLU n 1 423 HIS n 1 424 ARG n 1 425 SER n 1 426 SER n 1 427 LYS n 1 428 LEU n 1 429 PRO n 1 430 TRP n 1 431 PRO n 1 432 GLU n 1 433 TRP n 1 434 MET n 1 435 GLY n 1 436 VAL n 1 437 MET n 1 438 HIS n 1 439 GLY n 1 440 TYR n 1 441 GLU n 1 442 ILE n 1 443 GLU n 1 444 PHE n 1 445 VAL n 1 446 PHE n 1 447 GLY n 1 448 LEU n 1 449 PRO n 1 450 LEU n 1 451 GLU n 1 452 ARG n 1 453 ARG n 1 454 ASP n 1 455 GLN n 1 456 TYR n 1 457 THR n 1 458 LYS n 1 459 ALA n 1 460 GLU n 1 461 GLU n 1 462 ILE n 1 463 LEU n 1 464 SER n 1 465 ARG n 1 466 SER n 1 467 ILE n 1 468 VAL n 1 469 LYS n 1 470 ARG n 1 471 TRP n 1 472 ALA n 1 473 ASN n 1 474 PHE n 1 475 ALA n 1 476 LYS n 1 477 TYR n 1 478 GLY n 1 479 ASN n 1 480 PRO n 1 481 GLN n 1 482 GLU n 1 483 THR n 1 484 GLN n 1 485 ASN n 1 486 GLN n 1 487 SER n 1 488 THR n 1 489 SER n 1 490 TRP n 1 491 PRO n 1 492 VAL n 1 493 PHE n 1 494 LYS n 1 495 SER n 1 496 THR n 1 497 GLU n 1 498 GLN n 1 499 LYS n 1 500 TYR n 1 501 LEU n 1 502 THR n 1 503 LEU n 1 504 ASN n 1 505 THR n 1 506 GLU n 1 507 SER n 1 508 THR n 1 509 ARG n 1 510 ILE n 1 511 MET n 1 512 THR n 1 513 LYS n 1 514 LEU n 1 515 ARG n 1 516 ALA n 1 517 GLN n 1 518 GLN n 1 519 CYS n 1 520 ARG n 1 521 PHE n 1 522 TRP n 1 523 THR n 1 524 SER n 1 525 PHE n 1 526 PHE n 1 527 PRO n 1 528 LYS n 1 529 VAL n # _entity_src_gen.entity_id 1 _entity_src_gen.pdbx_src_id 1 _entity_src_gen.pdbx_alt_source_flag sample _entity_src_gen.pdbx_seq_type ? _entity_src_gen.pdbx_beg_seq_num ? _entity_src_gen.pdbx_end_seq_num ? _entity_src_gen.gene_src_common_name HUMAN _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene ? _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain ? _entity_src_gen.gene_src_tissue ? _entity_src_gen.gene_src_tissue_fraction ? _entity_src_gen.gene_src_details ? _entity_src_gen.pdbx_gene_src_fragment ? _entity_src_gen.pdbx_gene_src_scientific_name 'HOMO SAPIENS' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 9606 _entity_src_gen.pdbx_gene_src_variant ? _entity_src_gen.pdbx_gene_src_cell_line ? _entity_src_gen.pdbx_gene_src_atcc ? _entity_src_gen.pdbx_gene_src_organ ? _entity_src_gen.pdbx_gene_src_organelle ? _entity_src_gen.pdbx_gene_src_cell ? _entity_src_gen.pdbx_gene_src_cellular_location ? _entity_src_gen.host_org_common_name 'CHINESE HAMSTER' _entity_src_gen.pdbx_host_org_scientific_name 'CRICETULUS GRISEUS' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 10029 _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 CHO-K1 _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type PLASMID _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name PGS _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code CHLE_HUMAN _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ? _struct_ref.pdbx_align_begin ? _struct_ref.pdbx_db_accession P06276 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 4BDS _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 1 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 529 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession P06276 _struct_ref_seq.db_align_beg 29 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 557 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 1 _struct_ref_seq.pdbx_auth_seq_align_end 529 # loop_ _struct_ref_seq_dif.align_id _struct_ref_seq_dif.pdbx_pdb_id_code _struct_ref_seq_dif.mon_id _struct_ref_seq_dif.pdbx_pdb_strand_id _struct_ref_seq_dif.seq_num _struct_ref_seq_dif.pdbx_pdb_ins_code _struct_ref_seq_dif.pdbx_seq_db_name _struct_ref_seq_dif.pdbx_seq_db_accession_code _struct_ref_seq_dif.db_mon_id _struct_ref_seq_dif.pdbx_seq_db_seq_num _struct_ref_seq_dif.details _struct_ref_seq_dif.pdbx_auth_seq_num _struct_ref_seq_dif.pdbx_ordinal 1 4BDS GLN A 17 ? UNP P06276 ASN 45 'engineered mutation' 17 1 1 4BDS GLN A 455 ? UNP P06276 ASN 483 'engineered mutation' 455 2 1 4BDS GLN A 481 ? UNP P06276 ASN 509 'engineered mutation' 481 3 1 4BDS GLN A 486 ? UNP P06276 ASN 514 'engineered mutation' 486 4 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight 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 CL non-polymer . 'CHLORIDE ION' ? 'Cl -1' 35.453 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 FPK 'L-peptide linking' n 1-formyl-L-proline ? 'C6 H9 N O3' 143.141 FUC saccharide . ALPHA-L-FUCOSE ? 'C6 H12 O5' 164.156 FUL L-saccharide . BETA-L-FUCOSE 6-DEOXY-BETA-L-GALACTOSE 'C6 H12 O5' 164.156 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 GOL non-polymer . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3' 92.094 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 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 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 SO4 non-polymer . 'SULFATE ION' ? 'O4 S -2' 96.063 THA non-polymer . TACRINE ? 'C13 H14 N2' 198.264 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 UNX non-polymer . 'UNKNOWN ATOM OR ION' ? ? ? VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 4BDS _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.2 _exptl_crystal.density_percent_sol 62 _exptl_crystal.description NONE # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method ? _exptl_crystal_grow.temp ? _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 6.5 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details '0.1 M MES PH 6.5, 2.1 M AMMONIUM SULFATE, 293 K' # _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 'ADSC QUANTUM 4' _diffrn_detector.pdbx_collection_date 2006-03-11 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.9330 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'ESRF BEAMLINE ID14-2' _diffrn_source.pdbx_synchrotron_site ESRF _diffrn_source.pdbx_synchrotron_beamline ID14-2 _diffrn_source.pdbx_wavelength 0.9330 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4BDS _reflns.observed_criterion_sigma_I -3.0 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 40.90 _reflns.d_resolution_high 2.10 _reflns.number_obs 45776 _reflns.number_all ? _reflns.percent_possible_obs 99.8 _reflns.pdbx_Rmerge_I_obs 0.07 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 18.40 _reflns.B_iso_Wilson_estimate 34.86 _reflns.pdbx_redundancy 6.4 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 2.10 _reflns_shell.d_res_low 2.40 _reflns_shell.percent_possible_all 99.9 _reflns_shell.Rmerge_I_obs 0.42 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 4.80 _reflns_shell.pdbx_redundancy 6.5 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 4BDS _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 45772 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 1.36 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 40.904 _refine.ls_d_res_high 2.100 _refine.ls_percent_reflns_obs 99.79 _refine.ls_R_factor_obs 0.1765 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.1755 _refine.ls_R_factor_R_free 0.2087 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 3.1 _refine.ls_number_reflns_R_free 1422 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.B_iso_mean 40.4 _refine.aniso_B[1][1] ? _refine.aniso_B[2][2] ? _refine.aniso_B[3][3] ? _refine.aniso_B[1][2] ? _refine.aniso_B[1][3] ? _refine.aniso_B[2][3] ? _refine.solvent_model_details 'FLAT BULK SOLVENT MODEL' _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.11 _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii 0.90 _refine.pdbx_ls_cross_valid_method ? _refine.details ? _refine.pdbx_starting_model 'PDB ENTRY 1P0I' _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values ML _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details ? _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML 0.23 _refine.pdbx_overall_phase_error 21.39 _refine.overall_SU_B ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 4175 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 192 _refine_hist.number_atoms_solvent 279 _refine_hist.number_atoms_total 4646 _refine_hist.d_res_high 2.100 _refine_hist.d_res_low 40.904 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function f_bond_d 0.009 ? ? 4548 'X-RAY DIFFRACTION' ? f_angle_d 1.135 ? ? 6192 'X-RAY DIFFRACTION' ? f_dihedral_angle_d 19.796 ? ? 1694 'X-RAY DIFFRACTION' ? f_chiral_restr 0.080 ? ? 676 'X-RAY DIFFRACTION' ? f_plane_restr 0.005 ? ? 778 'X-RAY DIFFRACTION' ? # loop_ _refine_ls_shell.pdbx_refine_id _refine_ls_shell.pdbx_total_number_of_bins_used _refine_ls_shell.d_res_high _refine_ls_shell.d_res_low _refine_ls_shell.number_reflns_R_work _refine_ls_shell.R_factor_R_work _refine_ls_shell.percent_reflns_obs _refine_ls_shell.R_factor_R_free _refine_ls_shell.R_factor_R_free_error _refine_ls_shell.percent_reflns_R_free _refine_ls_shell.number_reflns_R_free _refine_ls_shell.number_reflns_all _refine_ls_shell.R_factor_all 'X-RAY DIFFRACTION' . 2.1000 2.1750 4332 0.2472 100.00 0.2908 . . 147 . . 'X-RAY DIFFRACTION' . 2.1750 2.2621 4389 0.2292 100.00 0.2596 . . 142 . . 'X-RAY DIFFRACTION' . 2.2621 2.3651 4409 0.2059 100.00 0.2448 . . 127 . . 'X-RAY DIFFRACTION' . 2.3651 2.4897 4384 0.1932 100.00 0.2391 . . 157 . . 'X-RAY DIFFRACTION' . 2.4897 2.6457 4407 0.1894 100.00 0.2683 . . 145 . . 'X-RAY DIFFRACTION' . 2.6457 2.8499 4394 0.1806 100.00 0.2544 . . 148 . . 'X-RAY DIFFRACTION' . 2.8499 3.1366 4453 0.1812 100.00 0.1984 . . 129 . . 'X-RAY DIFFRACTION' . 3.1366 3.5903 4453 0.1661 100.00 0.2146 . . 142 . . 'X-RAY DIFFRACTION' . 3.5903 4.5224 4497 0.1444 100.00 0.1655 . . 137 . . 'X-RAY DIFFRACTION' . 4.5224 40.9119 4632 0.1716 99.00 0.1904 . . 148 . . # _struct.entry_id 4BDS _struct.title 'Human butyrylcholinesterase in complex with tacrine' _struct.pdbx_descriptor 'CHOLINESTERASE (E.C.3.1.1.8)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4BDS _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text 'HYDROLASE, NERVE TRANSMISSION, INHIBITIOR, ALPHA-BETA HYDROLASE' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 2 ? D N N 3 ? E N N 2 ? F N N 4 ? G N N 2 ? H N N 2 ? I N N 2 ? J N N 4 ? K N N 2 ? L N N 2 ? M N N 5 ? N N N 6 ? O N N 7 ? P N N 7 ? Q N N 8 ? R N N 8 ? S N N 9 ? T N N 10 ? U N N 10 ? V N N 10 ? W N N 10 ? X N N 10 ? Y N N 10 ? Z N N 10 ? AA N N 11 ? # _struct_biol.id 1 # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 LEU A 38 ? ARG A 42 ? LEU A 38 ARG A 42 5 ? 5 HELX_P HELX_P2 2 PHE A 76 ? MET A 81 ? PHE A 76 MET A 81 1 ? 6 HELX_P HELX_P3 3 LEU A 125 ? ASP A 129 ? LEU A 125 ASP A 129 5 ? 5 HELX_P HELX_P4 4 GLY A 130 ? ARG A 138 ? GLY A 130 ARG A 138 1 ? 9 HELX_P HELX_P5 5 GLY A 149 ? LEU A 154 ? GLY A 149 LEU A 154 1 ? 6 HELX_P HELX_P6 6 ASN A 165 ? ILE A 182 ? ASN A 165 ILE A 182 1 ? 18 HELX_P HELX_P7 7 ALA A 183 ? PHE A 185 ? ALA A 183 PHE A 185 5 ? 3 HELX_P HELX_P8 8 SER A 198 ? SER A 210 ? SER A 198 SER A 210 1 ? 13 HELX_P HELX_P9 9 PRO A 211 ? PHE A 217 ? PRO A 211 PHE A 217 5 ? 7 HELX_P HELX_P10 10 SER A 235 ? THR A 250 ? SER A 235 THR A 250 1 ? 16 HELX_P HELX_P11 11 ASN A 256 ? ASN A 266 ? ASN A 256 ASN A 266 1 ? 11 HELX_P HELX_P12 12 ASP A 268 ? GLU A 276 ? ASP A 268 GLU A 276 1 ? 9 HELX_P HELX_P13 13 ALA A 277 ? VAL A 279 ? ALA A 277 VAL A 279 5 ? 3 HELX_P HELX_P14 14 MET A 302 ? LEU A 309 ? MET A 302 LEU A 309 1 ? 8 HELX_P HELX_P15 15 GLY A 326 ? VAL A 331 ? GLY A 326 VAL A 331 1 ? 6 HELX_P HELX_P16 16 THR A 346 ? PHE A 358 ? THR A 346 PHE A 358 1 ? 13 HELX_P HELX_P17 17 SER A 362 ? THR A 374 ? SER A 362 THR A 374 1 ? 13 HELX_P HELX_P18 18 GLU A 383 ? PHE A 398 ? GLU A 383 PHE A 398 1 ? 16 HELX_P HELX_P19 19 PHE A 398 ? GLU A 411 ? PHE A 398 GLU A 411 1 ? 14 HELX_P HELX_P20 20 PRO A 431 ? GLY A 435 ? PRO A 431 GLY A 435 5 ? 5 HELX_P HELX_P21 21 GLU A 441 ? PHE A 446 ? GLU A 441 PHE A 446 1 ? 6 HELX_P HELX_P22 22 GLY A 447 ? GLU A 451 ? GLY A 447 GLU A 451 5 ? 5 HELX_P HELX_P23 23 THR A 457 ? GLY A 478 ? THR A 457 GLY A 478 1 ? 22 HELX_P HELX_P24 24 ARG A 515 ? PHE A 525 ? ARG A 515 PHE A 525 1 ? 11 HELX_P HELX_P25 25 PHE A 526 ? VAL A 529 ? PHE A 526 VAL A 529 5 ? 4 # _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 65 SG ? ? ? 1_555 A CYS 92 SG ? ? A CYS 65 A CYS 92 1_555 ? ? ? ? ? ? ? 2.045 ? disulf2 disulf ? ? A CYS 252 SG ? ? ? 1_555 A CYS 263 SG ? ? A CYS 252 A CYS 263 1_555 ? ? ? ? ? ? ? 2.044 ? disulf3 disulf ? ? A CYS 400 SG ? ? ? 1_555 A CYS 519 SG ? ? A CYS 400 A CYS 519 1_555 ? ? ? ? ? ? ? 2.055 ? covale1 covale ? ? A ASN 57 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 57 A NAG 601 1_555 ? ? ? ? ? ? ? 1.444 ? covale2 covale ? ? A ASN 106 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 106 A NAG 611 1_555 ? ? ? ? ? ? ? 1.454 ? covale3 covale ? ? A ASN 241 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 241 A NAG 621 1_555 ? ? ? ? ? ? ? 1.454 ? covale4 covale ? ? A ASN 256 ND2 ? ? ? 1_555 H NAG . C1 ? ? A ASN 256 A NAG 631 1_555 ? ? ? ? ? ? ? 1.450 ? covale5 covale ? ? A ASN 341 ND2 ? ? ? 1_555 I NAG . C1 ? ? A ASN 341 A NAG 641 1_555 ? ? ? ? ? ? ? 1.440 ? covale6 covale ? ? A ASN 485 ND2 ? ? ? 1_555 L NAG . C1 ? ? A ASN 485 A NAG 651 1_555 ? ? ? ? ? ? ? 1.445 ? covale7 covale ? ? E NAG . O6 ? ? ? 1_555 F FUL . C1 ? ? A NAG 621 A FUL 622 1_555 ? ? ? ? ? ? ? 1.451 ? covale8 covale ? ? E NAG . O4 ? ? ? 1_555 G NAG . C1 ? ? A NAG 621 A NAG 623 1_555 ? ? ? ? ? ? ? 1.452 ? covale9 covale ? ? I NAG . O6 ? ? ? 1_555 J FUL . C1 ? ? A NAG 641 A FUL 642 1_555 ? ? ? ? ? ? ? 1.444 ? covale10 covale ? ? I NAG . O4 ? ? ? 1_555 K NAG . C1 ? ? A NAG 641 A NAG 643 1_555 ? ? ? ? ? ? ? 1.445 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # _struct_mon_prot_cis.pdbx_id 1 _struct_mon_prot_cis.label_comp_id ALA _struct_mon_prot_cis.label_seq_id 101 _struct_mon_prot_cis.label_asym_id A _struct_mon_prot_cis.label_alt_id . _struct_mon_prot_cis.pdbx_PDB_ins_code ? _struct_mon_prot_cis.auth_comp_id ALA _struct_mon_prot_cis.auth_seq_id 101 _struct_mon_prot_cis.auth_asym_id A _struct_mon_prot_cis.pdbx_label_comp_id_2 PRO _struct_mon_prot_cis.pdbx_label_seq_id_2 102 _struct_mon_prot_cis.pdbx_label_asym_id_2 A _struct_mon_prot_cis.pdbx_PDB_ins_code_2 ? _struct_mon_prot_cis.pdbx_auth_comp_id_2 PRO _struct_mon_prot_cis.pdbx_auth_seq_id_2 102 _struct_mon_prot_cis.pdbx_auth_asym_id_2 A _struct_mon_prot_cis.pdbx_PDB_model_num 1 _struct_mon_prot_cis.pdbx_omega_angle 0.44 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA ? 3 ? AB ? 11 ? AC ? 2 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense AA 1 2 ? anti-parallel AA 2 3 ? parallel AB 1 2 ? anti-parallel AB 2 3 ? anti-parallel AB 3 4 ? anti-parallel AB 4 5 ? parallel AB 5 6 ? parallel AB 6 7 ? parallel AB 7 8 ? parallel AB 8 9 ? parallel AB 9 10 ? parallel AB 10 11 ? anti-parallel AC 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 AA 1 ILE A 5 ? THR A 8 ? ILE A 5 THR A 8 AA 2 GLY A 11 ? ARG A 14 ? GLY A 11 ARG A 14 AA 3 ILE A 55 ? ASN A 57 ? ILE A 55 ASN A 57 AB 1 MET A 16 ? VAL A 20 ? MET A 16 VAL A 20 AB 2 GLY A 23 ? PRO A 32 ? GLY A 23 PRO A 32 AB 3 TYR A 94 ? PRO A 100 ? TYR A 94 PRO A 100 AB 4 ILE A 140 ? MET A 144 ? ILE A 140 MET A 144 AB 5 ALA A 107 ? ILE A 113 ? ALA A 107 ILE A 113 AB 6 GLY A 187 ? GLU A 197 ? GLY A 187 GLU A 197 AB 7 ARG A 219 ? GLN A 223 ? ARG A 219 GLN A 223 AB 8 ILE A 317 ? ASN A 322 ? ILE A 317 ASN A 322 AB 9 ALA A 416 ? PHE A 421 ? ALA A 416 PHE A 421 AB 10 LYS A 499 ? LEU A 503 ? LYS A 499 LEU A 503 AB 11 ILE A 510 ? THR A 512 ? ILE A 510 THR A 512 AC 1 SER A 64 ? CYS A 65 ? SER A 64 CYS A 65 AC 2 LEU A 88 ? SER A 89 ? LEU A 88 SER A 89 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id AA 1 2 N THR A 8 ? N THR A 8 O GLY A 11 ? O GLY A 11 AA 2 3 N ARG A 14 ? N ARG A 14 O TRP A 56 ? O TRP A 56 AB 1 2 N VAL A 20 ? N VAL A 20 O GLY A 23 ? O GLY A 23 AB 2 3 N ILE A 31 ? N ILE A 31 O LEU A 95 ? O LEU A 95 AB 3 4 N TRP A 98 ? N TRP A 98 O VAL A 141 ? O VAL A 141 AB 4 5 N ILE A 140 ? N ILE A 140 O THR A 108 ? O THR A 108 AB 5 6 O ALA A 107 ? O ALA A 107 N ASN A 188 ? N ASN A 188 AB 6 7 N LEU A 194 ? N LEU A 194 O ARG A 219 ? O ARG A 219 AB 7 8 N LEU A 222 ? N LEU A 222 O LEU A 318 ? O LEU A 318 AB 8 9 N VAL A 319 ? N VAL A 319 O PHE A 417 ? O PHE A 417 AB 9 10 N TYR A 420 ? N TYR A 420 O LEU A 501 ? O LEU A 501 AB 10 11 N TYR A 500 ? N TYR A 500 O MET A 511 ? O MET A 511 AC 1 2 O SER A 64 ? O SER A 64 N SER A 89 ? N SER A 89 # 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 ? ? ? ? 4 'BINDING SITE FOR RESIDUE FU4 A 612' AC2 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE THA A 701' AC3 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE GOL A 702' AC4 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE SO4 A 703' AC5 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE SO4 A 704' AC6 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE CL A 705' AC7 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE CL A 706' AC8 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE FPK A 710' AC9 Software ? ? ? ? 2 'Binding site for Mono-Saccharide NAG A 601 bound to ASN A 57' BC1 Software ? ? ? ? 4 'Binding site for Mono-Saccharide NAG A 611 bound to ASN A 106' BC2 Software ? ? ? ? 8 'Binding site for Poly-Saccharide residues NAG A 621 through NAG A 623 bound to ASN A 241' BC3 Software ? ? ? ? 1 'Binding site for Mono-Saccharide NAG A 631 bound to ASN A 256' BC4 Software ? ? ? ? 3 'Binding site for Poly-Saccharide residues NAG A 641 through NAG A 643 bound to ASN A 341' BC5 Software ? ? ? ? 3 'Binding site for Mono-Saccharide NAG A 651 bound to ASN A 485' # 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 4 ASN A 188 ? ASN A 188 . ? 1_555 ? 2 AC1 4 LYS A 190 ? LYS A 190 . ? 1_555 ? 3 AC1 4 NAG C . ? NAG A 611 . ? 1_555 ? 4 AC1 4 HOH AA . ? HOH A 2242 . ? 1_555 ? 5 AC2 8 TRP A 82 ? TRP A 82 . ? 1_555 ? 6 AC2 8 GLU A 197 ? GLU A 197 . ? 1_555 ? 7 AC2 8 TYR A 332 ? TYR A 332 . ? 1_555 ? 8 AC2 8 TRP A 430 ? TRP A 430 . ? 1_555 ? 9 AC2 8 HIS A 438 ? HIS A 438 . ? 1_555 ? 10 AC2 8 FPK S . ? FPK A 710 . ? 1_555 ? 11 AC2 8 HOH AA . ? HOH A 2056 . ? 1_555 ? 12 AC2 8 HOH AA . ? HOH A 2093 . ? 1_555 ? 13 AC3 5 LEU A 18 ? LEU A 18 . ? 1_555 ? 14 AC3 5 TYR A 61 ? TYR A 61 . ? 1_555 ? 15 AC3 5 TRP A 98 ? TRP A 98 . ? 1_555 ? 16 AC3 5 ASP A 129 ? ASP A 129 . ? 1_555 ? 17 AC3 5 LYS A 131 ? LYS A 131 . ? 1_555 ? 18 AC4 5 GLN A 316 ? GLN A 316 . ? 1_555 ? 19 AC4 5 GLY A 413 ? GLY A 413 . ? 1_555 ? 20 AC4 5 ASN A 414 ? ASN A 414 . ? 1_555 ? 21 AC4 5 ASN A 415 ? ASN A 415 . ? 1_555 ? 22 AC4 5 HOH AA . ? HOH A 2216 . ? 1_555 ? 23 AC5 7 TRP A 231 ? TRP A 231 . ? 1_555 ? 24 AC5 7 ARG A 242 ? ARG A 242 . ? 1_555 ? 25 AC5 7 SER A 287 ? SER A 287 . ? 1_555 ? 26 AC5 7 VAL A 288 ? VAL A 288 . ? 1_555 ? 27 AC5 7 HOH AA . ? HOH A 2145 . ? 1_555 ? 28 AC5 7 HOH AA . ? HOH A 2154 . ? 1_555 ? 29 AC5 7 HOH AA . ? HOH A 2155 . ? 1_555 ? 30 AC6 3 THR A 488 ? THR A 488 . ? 1_555 ? 31 AC6 3 THR A 508 ? THR A 508 . ? 1_555 ? 32 AC6 3 HOH AA . ? HOH A 2240 . ? 1_555 ? 33 AC7 2 TYR A 420 ? TYR A 420 . ? 1_555 ? 34 AC7 2 HOH AA . ? HOH A 2271 . ? 1_555 ? 35 AC8 8 GLY A 116 ? GLY A 116 . ? 1_555 ? 36 AC8 8 GLY A 117 ? GLY A 117 . ? 1_555 ? 37 AC8 8 SER A 198 ? SER A 198 . ? 1_555 ? 38 AC8 8 ALA A 199 ? ALA A 199 . ? 1_555 ? 39 AC8 8 LEU A 286 ? LEU A 286 . ? 1_555 ? 40 AC8 8 HIS A 438 ? HIS A 438 . ? 1_555 ? 41 AC8 8 THA M . ? THA A 701 . ? 1_555 ? 42 AC8 8 HOH AA . ? HOH A 2092 . ? 1_555 ? 43 AC9 2 ASN A 57 ? ASN A 57 . ? 1_555 ? 44 AC9 2 HOH AA . ? HOH A 2278 . ? 1_555 ? 45 BC1 4 ASN A 106 ? ASN A 106 . ? 1_555 ? 46 BC1 4 ASN A 188 ? ASN A 188 . ? 1_555 ? 47 BC1 4 LYS A 190 ? LYS A 190 . ? 1_555 ? 48 BC1 4 FUC D . ? FUC A 612 . ? 1_555 ? 49 BC2 8 TYR A 237 ? TYR A 237 . ? 1_555 ? 50 BC2 8 ASN A 241 ? ASN A 241 . ? 1_555 ? 51 BC2 8 ASN A 245 ? ASN A 245 . ? 1_555 ? 52 BC2 8 LYS A 248 ? LYS A 248 . ? 1_555 ? 53 BC2 8 LEU A 249 ? LEU A 249 . ? 1_555 ? 54 BC2 8 PHE A 278 ? PHE A 278 . ? 1_555 ? 55 BC2 8 PRO A 281 ? PRO A 281 . ? 1_555 ? 56 BC2 8 HOH AA . ? HOH A 2148 . ? 1_555 ? 57 BC3 1 ASN A 256 ? ASN A 256 . ? 1_555 ? 58 BC4 3 SER A 338 ? SER A 338 . ? 1_555 ? 59 BC4 3 ASN A 341 ? ASN A 341 . ? 1_555 ? 60 BC4 3 ASN A 342 ? ASN A 342 . ? 1_555 ? 61 BC5 3 ARG A 465 ? ARG A 465 . ? 1_555 ? 62 BC5 3 ASN A 485 ? ASN A 485 . ? 1_555 ? 63 BC5 3 HOH AA . ? HOH A 2279 . ? 1_555 ? # _database_PDB_matrix.entry_id 4BDS _database_PDB_matrix.origx[1][1] 1.000000 _database_PDB_matrix.origx[1][2] 0.000000 _database_PDB_matrix.origx[1][3] 0.000000 _database_PDB_matrix.origx[2][1] 0.000000 _database_PDB_matrix.origx[2][2] 1.000000 _database_PDB_matrix.origx[2][3] 0.000000 _database_PDB_matrix.origx[3][1] 0.000000 _database_PDB_matrix.origx[3][2] 0.000000 _database_PDB_matrix.origx[3][3] 1.000000 _database_PDB_matrix.origx_vector[1] 0.00000 _database_PDB_matrix.origx_vector[2] 0.00000 _database_PDB_matrix.origx_vector[3] 0.00000 # _atom_sites.entry_id 4BDS _atom_sites.fract_transf_matrix[1][1] 0.006424 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.006424 _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] 0.007820 _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 CL N O S X # 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 . ILE A 1 4 ? 120.831 136.892 14.650 1.00 75.40 ? 4 ILE A N 1 ATOM 2 C CA . ILE A 1 4 ? 121.976 137.679 15.104 1.00 73.53 ? 4 ILE A CA 1 ATOM 3 C C . ILE A 1 4 ? 123.312 137.082 14.642 1.00 66.32 ? 4 ILE A C 1 ATOM 4 O O . ILE A 1 4 ? 123.644 135.933 14.946 1.00 67.28 ? 4 ILE A O 1 ATOM 5 C CB . ILE A 1 4 ? 121.957 137.871 16.635 1.00 71.71 ? 4 ILE A CB 1 ATOM 6 C CG1 . ILE A 1 4 ? 123.222 138.595 17.110 1.00 68.87 ? 4 ILE A CG1 1 ATOM 7 C CG2 . ILE A 1 4 ? 121.764 136.537 17.341 1.00 70.01 ? 4 ILE A CG2 1 ATOM 8 C CD1 . ILE A 1 4 ? 123.242 140.074 16.782 1.00 69.64 ? 4 ILE A CD1 1 ATOM 9 N N . ILE A 1 5 ? 124.072 137.882 13.902 1.00 58.95 ? 5 ILE A N 1 ATOM 10 C CA . ILE A 1 5 ? 125.277 137.414 13.228 1.00 55.18 ? 5 ILE A CA 1 ATOM 11 C C . ILE A 1 5 ? 126.451 138.330 13.557 1.00 54.22 ? 5 ILE A C 1 ATOM 12 O O . ILE A 1 5 ? 126.354 139.552 13.424 1.00 59.04 ? 5 ILE A O 1 ATOM 13 C CB . ILE A 1 5 ? 125.048 137.366 11.699 1.00 53.59 ? 5 ILE A CB 1 ATOM 14 C CG1 . ILE A 1 5 ? 123.917 136.387 11.374 1.00 60.53 ? 5 ILE A CG1 1 ATOM 15 C CG2 . ILE A 1 5 ? 126.316 136.970 10.968 1.00 53.72 ? 5 ILE A CG2 1 ATOM 16 C CD1 . ILE A 1 5 ? 123.243 136.633 10.046 1.00 61.41 ? 5 ILE A CD1 1 ATOM 17 N N . ILE A 1 6 ? 127.557 137.742 14.000 1.00 50.99 ? 6 ILE A N 1 ATOM 18 C CA . ILE A 1 6 ? 128.717 138.529 14.404 1.00 47.97 ? 6 ILE A CA 1 ATOM 19 C C . ILE A 1 6 ? 129.927 138.180 13.549 1.00 56.90 ? 6 ILE A C 1 ATOM 20 O O . ILE A 1 6 ? 130.271 137.009 13.405 1.00 47.38 ? 6 ILE A O 1 ATOM 21 C CB . ILE A 1 6 ? 129.069 138.295 15.893 1.00 45.25 ? 6 ILE A CB 1 ATOM 22 C CG1 . ILE A 1 6 ? 127.970 138.844 16.805 1.00 51.44 ? 6 ILE A CG1 1 ATOM 23 C CG2 . ILE A 1 6 ? 130.406 138.944 16.240 1.00 44.90 ? 6 ILE A CG2 1 ATOM 24 C CD1 . ILE A 1 6 ? 127.830 140.359 16.756 1.00 50.70 ? 6 ILE A CD1 1 ATOM 25 N N . ALA A 1 7 ? 130.568 139.200 12.984 1.00 50.31 ? 7 ALA A N 1 ATOM 26 C CA . ALA A 1 7 ? 131.796 139.008 12.220 1.00 59.12 ? 7 ALA A CA 1 ATOM 27 C C . ALA A 1 7 ? 133.002 138.839 13.149 1.00 55.98 ? 7 ALA A C 1 ATOM 28 O O . ALA A 1 7 ? 133.280 139.712 13.971 1.00 57.79 ? 7 ALA A O 1 ATOM 29 C CB . ALA A 1 7 ? 132.013 140.182 11.273 1.00 59.55 ? 7 ALA A CB 1 ATOM 30 N N . THR A 1 8 ? 133.702 137.710 13.030 1.00 51.02 ? 8 THR A N 1 ATOM 31 C CA . THR A 1 8 ? 134.960 137.503 13.752 1.00 50.69 ? 8 THR A CA 1 ATOM 32 C C . THR A 1 8 ? 136.136 137.513 12.774 1.00 56.66 ? 8 THR A C 1 ATOM 33 O O . THR A 1 8 ? 135.940 137.614 11.561 1.00 53.00 ? 8 THR A O 1 ATOM 34 C CB . THR A 1 8 ? 134.983 136.167 14.535 1.00 47.64 ? 8 THR A CB 1 ATOM 35 O OG1 . THR A 1 8 ? 135.181 135.074 13.625 1.00 48.12 ? 8 THR A OG1 1 ATOM 36 C CG2 . THR A 1 8 ? 133.688 135.967 15.317 1.00 42.29 ? 8 THR A CG2 1 ATOM 37 N N . LYS A 1 9 ? 137.353 137.392 13.304 1.00 57.77 ? 9 LYS A N 1 ATOM 38 C CA . LYS A 1 9 ? 138.568 137.405 12.479 1.00 55.61 ? 9 LYS A CA 1 ATOM 39 C C . LYS A 1 9 ? 138.622 136.271 11.448 1.00 53.91 ? 9 LYS A C 1 ATOM 40 O O . LYS A 1 9 ? 139.147 136.451 10.345 1.00 55.06 ? 9 LYS A O 1 ATOM 41 C CB . LYS A 1 9 ? 139.822 137.368 13.364 1.00 53.62 ? 9 LYS A CB 1 ATOM 42 C CG . LYS A 1 9 ? 140.419 138.748 13.688 1.00 61.70 ? 9 LYS A CG 1 ATOM 43 C CD . LYS A 1 9 ? 139.346 139.748 14.100 1.00 63.54 ? 9 LYS A CD 1 ATOM 44 C CE . LYS A 1 9 ? 139.914 141.141 14.285 1.00 65.90 ? 9 LYS A CE 1 ATOM 45 N NZ . LYS A 1 9 ? 138.865 142.178 14.071 1.00 69.83 ? 9 LYS A NZ 1 ATOM 46 N N . ASN A 1 10 ? 138.073 135.113 11.807 1.00 50.84 ? 10 ASN A N 1 ATOM 47 C CA . ASN A 1 10 ? 138.133 133.934 10.945 1.00 58.59 ? 10 ASN A CA 1 ATOM 48 C C . ASN A 1 10 ? 136.833 133.658 10.190 1.00 58.26 ? 10 ASN A C 1 ATOM 49 O O . ASN A 1 10 ? 136.745 132.708 9.405 1.00 60.05 ? 10 ASN A O 1 ATOM 50 C CB . ASN A 1 10 ? 138.554 132.716 11.765 1.00 64.87 ? 10 ASN A CB 1 ATOM 51 C CG . ASN A 1 10 ? 139.815 132.971 12.558 1.00 71.86 ? 10 ASN A CG 1 ATOM 52 O OD1 . ASN A 1 10 ? 139.765 133.482 13.681 1.00 75.53 ? 10 ASN A OD1 1 ATOM 53 N ND2 . ASN A 1 10 ? 140.961 132.636 11.973 1.00 72.70 ? 10 ASN A ND2 1 ATOM 54 N N . GLY A 1 11 ? 135.830 134.498 10.421 1.00 55.51 ? 11 GLY A N 1 ATOM 55 C CA . GLY A 1 11 ? 134.581 134.394 9.692 1.00 50.42 ? 11 GLY A CA 1 ATOM 56 C C . GLY A 1 11 ? 133.365 134.754 10.520 1.00 56.87 ? 11 GLY A C 1 ATOM 57 O O . GLY A 1 11 ? 133.475 135.079 11.710 1.00 51.47 ? 11 GLY A O 1 ATOM 58 N N . LYS A 1 12 ? 132.200 134.688 9.880 1.00 50.92 ? 12 LYS A N 1 ATOM 59 C CA . LYS A 1 12 ? 130.933 135.002 10.530 1.00 57.72 ? 12 LYS A CA 1 ATOM 60 C C . LYS A 1 12 ? 130.402 133.856 11.389 1.00 54.53 ? 12 LYS A C 1 ATOM 61 O O . LYS A 1 12 ? 130.501 132.680 11.022 1.00 47.80 ? 12 LYS A O 1 ATOM 62 C CB . LYS A 1 12 ? 129.879 135.371 9.484 1.00 53.19 ? 12 LYS A CB 1 ATOM 63 C CG . LYS A 1 12 ? 130.279 136.516 8.590 1.00 58.81 ? 12 LYS A CG 1 ATOM 64 C CD . LYS A 1 12 ? 129.068 137.093 7.880 1.00 64.67 ? 12 LYS A CD 1 ATOM 65 C CE . LYS A 1 12 ? 129.437 138.361 7.130 1.00 71.09 ? 12 LYS A CE 1 ATOM 66 N NZ . LYS A 1 12 ? 128.228 139.132 6.721 1.00 75.84 ? 12 LYS A NZ 1 ATOM 67 N N . VAL A 1 13 ? 129.831 134.209 12.535 1.00 48.76 ? 13 VAL A N 1 ATOM 68 C CA . VAL A 1 13 ? 129.143 133.228 13.364 1.00 44.70 ? 13 VAL A CA 1 ATOM 69 C C . VAL A 1 13 ? 127.703 133.675 13.646 1.00 45.33 ? 13 VAL A C 1 ATOM 70 O O . VAL A 1 13 ? 127.443 134.864 13.850 1.00 51.12 ? 13 VAL A O 1 ATOM 71 C CB . VAL A 1 13 ? 129.907 132.959 14.686 1.00 51.63 ? 13 VAL A CB 1 ATOM 72 C CG1 . VAL A 1 13 ? 131.299 132.427 14.387 1.00 50.76 ? 13 VAL A CG1 1 ATOM 73 C CG2 . VAL A 1 13 ? 129.996 134.219 15.525 1.00 49.28 ? 13 VAL A CG2 1 ATOM 74 N N . ARG A 1 14 ? 126.772 132.722 13.626 1.00 45.25 ? 14 ARG A N 1 ATOM 75 C CA . ARG A 1 14 ? 125.379 132.983 14.004 1.00 53.08 ? 14 ARG A CA 1 ATOM 76 C C . ARG A 1 14 ? 125.052 132.370 15.370 1.00 48.61 ? 14 ARG A C 1 ATOM 77 O O . ARG A 1 14 ? 125.398 131.212 15.641 1.00 43.54 ? 14 ARG A O 1 ATOM 78 C CB . ARG A 1 14 ? 124.421 132.435 12.942 1.00 54.11 ? 14 ARG A CB 1 ATOM 79 C CG . ARG A 1 14 ? 123.019 132.111 13.452 1.00 52.00 ? 14 ARG A CG 1 ATOM 80 C CD . ARG A 1 14 ? 122.148 131.468 12.366 1.00 56.91 ? 14 ARG A CD 1 ATOM 81 N NE . ARG A 1 14 ? 121.758 132.427 11.333 1.00 64.73 ? 14 ARG A NE 1 ATOM 82 C CZ . ARG A 1 14 ? 122.112 132.344 10.051 1.00 68.72 ? 14 ARG A CZ 1 ATOM 83 N NH1 . ARG A 1 14 ? 122.863 131.333 9.627 1.00 54.66 ? 14 ARG A NH1 1 ATOM 84 N NH2 . ARG A 1 14 ? 121.709 133.270 9.188 1.00 68.20 ? 14 ARG A NH2 1 ATOM 85 N N . GLY A 1 15 ? 124.395 133.150 16.227 1.00 46.52 ? 15 GLY A N 1 ATOM 86 C CA . GLY A 1 15 ? 123.988 132.672 17.537 1.00 44.21 ? 15 GLY A CA 1 ATOM 87 C C . GLY A 1 15 ? 122.498 132.405 17.648 1.00 45.19 ? 15 GLY A C 1 ATOM 88 O O . GLY A 1 15 ? 121.807 132.253 16.632 1.00 46.45 ? 15 GLY A O 1 ATOM 89 N N . MET A 1 16 ? 122.005 132.332 18.883 1.00 41.77 ? 16 MET A N 1 ATOM 90 C CA . MET A 1 16 ? 120.588 132.083 19.133 1.00 46.09 ? 16 MET A CA 1 ATOM 91 C C . MET A 1 16 ? 120.105 132.887 20.339 1.00 48.38 ? 16 MET A C 1 ATOM 92 O O . MET A 1 16 ? 120.873 133.140 21.278 1.00 39.71 ? 16 MET A O 1 ATOM 93 C CB . MET A 1 16 ? 120.343 130.590 19.373 1.00 45.83 ? 16 MET A CB 1 ATOM 94 C CG . MET A 1 16 ? 120.993 130.060 20.651 1.00 46.80 ? 16 MET A CG 1 ATOM 95 S SD . MET A 1 16 ? 120.839 128.271 20.838 1.00 66.37 ? 16 MET A SD 1 ATOM 96 C CE . MET A 1 16 ? 119.084 128.082 20.522 1.00 55.23 ? 16 MET A CE 1 ATOM 97 N N . GLN A 1 17 ? 118.831 133.272 20.318 1.00 51.56 ? 17 GLN A N 1 ATOM 98 C CA . GLN A 1 17 ? 118.239 134.048 21.405 1.00 52.14 ? 17 GLN A CA 1 ATOM 99 C C . GLN A 1 17 ? 117.661 133.136 22.482 1.00 43.71 ? 17 GLN A C 1 ATOM 100 O O . GLN A 1 17 ? 117.013 132.141 22.176 1.00 48.43 ? 17 GLN A O 1 ATOM 101 C CB . GLN A 1 17 ? 117.143 134.966 20.866 1.00 61.33 ? 17 GLN A CB 1 ATOM 102 C CG . GLN A 1 17 ? 117.573 135.841 19.696 1.00 72.32 ? 17 GLN A CG 1 ATOM 103 C CD . GLN A 1 17 ? 118.352 137.068 20.129 1.00 79.44 ? 17 GLN A CD 1 ATOM 104 O OE1 . GLN A 1 17 ? 119.444 136.965 20.692 1.00 81.05 ? 17 GLN A OE1 1 ATOM 105 N NE2 . GLN A 1 17 ? 117.791 138.242 19.864 1.00 81.81 ? 17 GLN A NE2 1 ATOM 106 N N . LEU A 1 18 ? 117.899 133.479 23.741 1.00 40.53 ? 18 LEU A N 1 ATOM 107 C CA . LEU A 1 18 ? 117.354 132.721 24.859 1.00 43.96 ? 18 LEU A CA 1 ATOM 108 C C . LEU A 1 18 ? 116.476 133.635 25.694 1.00 50.70 ? 18 LEU A C 1 ATOM 109 O O . LEU A 1 18 ? 116.748 134.834 25.801 1.00 57.62 ? 18 LEU A O 1 ATOM 110 C CB . LEU A 1 18 ? 118.484 132.174 25.733 1.00 37.52 ? 18 LEU A CB 1 ATOM 111 C CG . LEU A 1 18 ? 119.507 131.259 25.059 1.00 40.56 ? 18 LEU A CG 1 ATOM 112 C CD1 . LEU A 1 18 ? 120.634 130.894 26.023 1.00 36.49 ? 18 LEU A CD1 1 ATOM 113 C CD2 . LEU A 1 18 ? 118.811 130.006 24.530 1.00 45.13 ? 18 LEU A CD2 1 ATOM 114 N N . THR A 1 19 ? 115.427 133.075 26.288 1.00 45.78 ? 19 THR A N 1 ATOM 115 C CA . THR A 1 19 ? 114.588 133.832 27.213 1.00 48.21 ? 19 THR A CA 1 ATOM 116 C C . THR A 1 19 ? 115.040 133.547 28.643 1.00 43.96 ? 19 THR A C 1 ATOM 117 O O . THR A 1 19 ? 115.155 132.387 29.046 1.00 41.72 ? 19 THR A O 1 ATOM 118 C CB . THR A 1 19 ? 113.097 133.486 27.026 1.00 53.71 ? 19 THR A CB 1 ATOM 119 O OG1 . THR A 1 19 ? 112.660 133.979 25.755 1.00 61.18 ? 19 THR A OG1 1 ATOM 120 C CG2 . THR A 1 19 ? 112.252 134.126 28.111 1.00 52.49 ? 19 THR A CG2 1 ATOM 121 N N . VAL A 1 20 ? 115.345 134.600 29.396 1.00 40.31 ? 20 VAL A N 1 ATOM 122 C CA . VAL A 1 20 ? 115.873 134.444 30.755 1.00 43.20 ? 20 VAL A CA 1 ATOM 123 C C . VAL A 1 20 ? 115.323 135.545 31.649 1.00 44.94 ? 20 VAL A C 1 ATOM 124 O O . VAL A 1 20 ? 115.615 136.730 31.429 1.00 44.65 ? 20 VAL A O 1 ATOM 125 C CB . VAL A 1 20 ? 117.422 134.550 30.802 1.00 37.28 ? 20 VAL A CB 1 ATOM 126 C CG1 . VAL A 1 20 ? 117.929 134.249 32.206 1.00 36.12 ? 20 VAL A CG1 1 ATOM 127 C CG2 . VAL A 1 20 ? 118.074 133.615 29.802 1.00 36.38 ? 20 VAL A CG2 1 ATOM 128 N N . PHE A 1 21 ? 114.529 135.155 32.644 1.00 45.16 ? 21 PHE A N 1 ATOM 129 C CA . PHE A 1 21 ? 113.958 136.102 33.610 1.00 45.86 ? 21 PHE A CA 1 ATOM 130 C C . PHE A 1 21 ? 113.235 137.279 32.947 1.00 45.09 ? 21 PHE A C 1 ATOM 131 O O . PHE A 1 21 ? 113.464 138.435 33.301 1.00 46.06 ? 21 PHE A O 1 ATOM 132 C CB . PHE A 1 21 ? 115.043 136.620 34.569 1.00 43.86 ? 21 PHE A CB 1 ATOM 133 C CG . PHE A 1 21 ? 115.785 135.525 35.302 1.00 42.79 ? 21 PHE A CG 1 ATOM 134 C CD1 . PHE A 1 21 ? 115.174 134.312 35.574 1.00 46.26 ? 21 PHE A CD1 1 ATOM 135 C CD2 . PHE A 1 21 ? 117.094 135.717 35.722 1.00 41.50 ? 21 PHE A CD2 1 ATOM 136 C CE1 . PHE A 1 21 ? 115.853 133.302 36.253 1.00 46.84 ? 21 PHE A CE1 1 ATOM 137 C CE2 . PHE A 1 21 ? 117.784 134.717 36.400 1.00 43.03 ? 21 PHE A CE2 1 ATOM 138 C CZ . PHE A 1 21 ? 117.161 133.509 36.667 1.00 47.81 ? 21 PHE A CZ 1 ATOM 139 N N . GLY A 1 22 ? 112.371 136.984 31.982 1.00 44.82 ? 22 GLY A N 1 ATOM 140 C CA . GLY A 1 22 ? 111.591 138.022 31.324 1.00 48.00 ? 22 GLY A CA 1 ATOM 141 C C . GLY A 1 22 ? 112.432 138.953 30.473 1.00 50.22 ? 22 GLY A C 1 ATOM 142 O O . GLY A 1 22 ? 111.999 140.046 30.113 1.00 54.81 ? 22 GLY A O 1 ATOM 143 N N . GLY A 1 23 ? 113.647 138.515 30.162 1.00 49.85 ? 23 GLY A N 1 ATOM 144 C CA . GLY A 1 23 ? 114.546 139.269 29.307 1.00 49.76 ? 23 GLY A CA 1 ATOM 145 C C . GLY A 1 23 ? 115.164 138.353 28.267 1.00 49.10 ? 23 GLY A C 1 ATOM 146 O O . GLY A 1 23 ? 114.689 137.234 28.060 1.00 50.56 ? 23 GLY A O 1 ATOM 147 N N . THR A 1 24 ? 116.223 138.818 27.612 1.00 44.28 ? 24 THR A N 1 ATOM 148 C CA . THR A 1 24 ? 116.856 138.037 26.553 1.00 45.83 ? 24 THR A CA 1 ATOM 149 C C . THR A 1 24 ? 118.382 137.974 26.699 1.00 44.75 ? 24 THR A C 1 ATOM 150 O O . THR A 1 24 ? 119.027 138.976 26.999 1.00 42.59 ? 24 THR A O 1 ATOM 151 C CB . THR A 1 24 ? 116.501 138.598 25.170 1.00 47.43 ? 24 THR A CB 1 ATOM 152 O OG1 . THR A 1 24 ? 115.079 138.542 24.981 1.00 56.82 ? 24 THR A OG1 1 ATOM 153 C CG2 . THR A 1 24 ? 117.175 137.789 24.080 1.00 49.64 ? 24 THR A CG2 1 ATOM 154 N N . VAL A 1 25 ? 118.940 136.783 26.491 1.00 41.44 ? 25 VAL A N 1 ATOM 155 C CA . VAL A 1 25 ? 120.383 136.583 26.396 1.00 39.64 ? 25 VAL A CA 1 ATOM 156 C C . VAL A 1 25 ? 120.709 135.963 25.034 1.00 42.57 ? 25 VAL A C 1 ATOM 157 O O . VAL A 1 25 ? 119.969 135.104 24.549 1.00 38.75 ? 25 VAL A O 1 ATOM 158 C CB . VAL A 1 25 ? 120.889 135.677 27.534 1.00 37.95 ? 25 VAL A CB 1 ATOM 159 C CG1 . VAL A 1 25 ? 122.356 135.277 27.319 1.00 34.73 ? 25 VAL A CG1 1 ATOM 160 C CG2 . VAL A 1 25 ? 120.719 136.378 28.889 1.00 36.12 ? 25 VAL A CG2 1 ATOM 161 N N . THR A 1 26 ? 121.787 136.424 24.400 1.00 38.25 ? 26 THR A N 1 ATOM 162 C CA . THR A 1 26 ? 122.235 135.851 23.128 1.00 38.54 ? 26 THR A CA 1 ATOM 163 C C . THR A 1 26 ? 123.382 134.871 23.357 1.00 39.89 ? 26 THR A C 1 ATOM 164 O O . THR A 1 26 ? 124.400 135.223 23.972 1.00 37.49 ? 26 THR A O 1 ATOM 165 C CB . THR A 1 26 ? 122.694 136.934 22.142 1.00 40.05 ? 26 THR A CB 1 ATOM 166 O OG1 . THR A 1 26 ? 121.672 137.929 22.023 1.00 41.92 ? 26 THR A OG1 1 ATOM 167 C CG2 . THR A 1 26 ? 122.955 136.325 20.771 1.00 47.55 ? 26 THR A CG2 1 ATOM 168 N N . ALA A 1 27 ? 123.214 133.643 22.872 1.00 39.45 ? 27 ALA A N 1 ATOM 169 C CA . ALA A 1 27 ? 124.196 132.593 23.112 1.00 38.50 ? 27 ALA A CA 1 ATOM 170 C C . ALA A 1 27 ? 124.827 132.113 21.816 1.00 35.20 ? 27 ALA A C 1 ATOM 171 O O . ALA A 1 27 ? 124.136 131.861 20.823 1.00 36.63 ? 27 ALA A O 1 ATOM 172 C CB . ALA A 1 27 ? 123.566 131.426 23.855 1.00 38.98 ? 27 ALA A CB 1 ATOM 173 N N . PHE A 1 28 ? 126.150 132.004 21.835 1.00 34.20 ? 28 PHE A N 1 ATOM 174 C CA . PHE A 1 28 ? 126.893 131.415 20.734 1.00 39.23 ? 28 PHE A CA 1 ATOM 175 C C . PHE A 1 28 ? 127.583 130.181 21.302 1.00 38.47 ? 28 PHE A C 1 ATOM 176 O O . PHE A 1 28 ? 128.599 130.297 21.994 1.00 37.60 ? 28 PHE A O 1 ATOM 177 C CB . PHE A 1 28 ? 127.942 132.394 20.198 1.00 39.86 ? 28 PHE A CB 1 ATOM 178 C CG . PHE A 1 28 ? 127.376 133.705 19.723 1.00 43.83 ? 28 PHE A CG 1 ATOM 179 C CD1 . PHE A 1 28 ? 127.086 134.723 20.626 1.00 41.70 ? 28 PHE A CD1 1 ATOM 180 C CD2 . PHE A 1 28 ? 127.160 133.929 18.375 1.00 38.86 ? 28 PHE A CD2 1 ATOM 181 C CE1 . PHE A 1 28 ? 126.570 135.937 20.187 1.00 42.56 ? 28 PHE A CE1 1 ATOM 182 C CE2 . PHE A 1 28 ? 126.650 135.138 17.928 1.00 50.12 ? 28 PHE A CE2 1 ATOM 183 C CZ . PHE A 1 28 ? 126.356 136.146 18.837 1.00 44.54 ? 28 PHE A CZ 1 ATOM 184 N N . LEU A 1 29 ? 127.012 129.012 21.028 1.00 32.98 ? 29 LEU A N 1 ATOM 185 C CA . LEU A 1 29 ? 127.514 127.751 21.565 1.00 31.64 ? 29 LEU A CA 1 ATOM 186 C C . LEU A 1 29 ? 128.300 126.991 20.497 1.00 36.16 ? 29 LEU A C 1 ATOM 187 O O . LEU A 1 29 ? 127.784 126.745 19.408 1.00 33.54 ? 29 LEU A O 1 ATOM 188 C CB . LEU A 1 29 ? 126.338 126.889 22.042 1.00 31.67 ? 29 LEU A CB 1 ATOM 189 C CG . LEU A 1 29 ? 125.355 127.557 23.011 1.00 34.59 ? 29 LEU A CG 1 ATOM 190 C CD1 . LEU A 1 29 ? 124.254 126.590 23.436 1.00 31.86 ? 29 LEU A CD1 1 ATOM 191 C CD2 . LEU A 1 29 ? 126.097 128.092 24.225 1.00 31.76 ? 29 LEU A CD2 1 ATOM 192 N N . GLY A 1 30 ? 129.546 126.627 20.803 1.00 31.84 ? 30 GLY A N 1 ATOM 193 C CA . GLY A 1 30 ? 130.339 125.798 19.903 1.00 31.32 ? 30 GLY A CA 1 ATOM 194 C C . GLY A 1 30 ? 131.124 126.515 18.811 1.00 40.26 ? 30 GLY A C 1 ATOM 195 O O . GLY A 1 30 ? 131.159 126.051 17.671 1.00 36.09 ? 30 GLY A O 1 ATOM 196 N N . ILE A 1 31 ? 131.763 127.638 19.141 1.00 32.16 ? 31 ILE A N 1 ATOM 197 C CA . ILE A 1 31 ? 132.642 128.299 18.182 1.00 33.29 ? 31 ILE A CA 1 ATOM 198 C C . ILE A 1 31 ? 134.031 127.634 18.214 1.00 35.75 ? 31 ILE A C 1 ATOM 199 O O . ILE A 1 31 ? 134.649 127.526 19.283 1.00 31.09 ? 31 ILE A O 1 ATOM 200 C CB . ILE A 1 31 ? 132.794 129.807 18.509 1.00 34.85 ? 31 ILE A CB 1 ATOM 201 C CG1 . ILE A 1 31 ? 131.426 130.490 18.640 1.00 36.23 ? 31 ILE A CG1 1 ATOM 202 C CG2 . ILE A 1 31 ? 133.645 130.506 17.455 1.00 38.92 ? 31 ILE A CG2 1 ATOM 203 C CD1 . ILE A 1 31 ? 131.498 131.936 19.173 1.00 35.16 ? 31 ILE A CD1 1 ATOM 204 N N . PRO A 1 32 ? 134.543 127.201 17.048 1.00 33.80 ? 32 PRO A N 1 ATOM 205 C CA . PRO A 1 32 ? 135.883 126.598 17.051 1.00 37.17 ? 32 PRO A CA 1 ATOM 206 C C . PRO A 1 32 ? 136.945 127.665 17.294 1.00 37.30 ? 32 PRO A C 1 ATOM 207 O O . PRO A 1 32 ? 136.752 128.815 16.880 1.00 39.18 ? 32 PRO A O 1 ATOM 208 C CB . PRO A 1 32 ? 136.014 126.023 15.629 1.00 35.07 ? 32 PRO A CB 1 ATOM 209 C CG . PRO A 1 32 ? 135.144 126.928 14.787 1.00 40.59 ? 32 PRO A CG 1 ATOM 210 C CD . PRO A 1 32 ? 133.984 127.320 15.686 1.00 35.89 ? 32 PRO A CD 1 ATOM 211 N N . TYR A 1 33 ? 138.034 127.310 17.972 1.00 39.26 ? 33 TYR A N 1 ATOM 212 C CA . TYR A 1 33 ? 139.104 128.282 18.222 1.00 32.32 ? 33 TYR A CA 1 ATOM 213 C C . TYR A 1 33 ? 140.477 127.725 17.842 1.00 35.92 ? 33 TYR A C 1 ATOM 214 O O . TYR A 1 33 ? 141.507 128.380 18.031 1.00 32.88 ? 33 TYR A O 1 ATOM 215 C CB . TYR A 1 33 ? 139.091 128.790 19.679 1.00 34.86 ? 33 TYR A CB 1 ATOM 216 C CG . TYR A 1 33 ? 139.466 127.763 20.737 1.00 29.22 ? 33 TYR A CG 1 ATOM 217 C CD1 . TYR A 1 33 ? 140.790 127.584 21.122 1.00 29.77 ? 33 TYR A CD1 1 ATOM 218 C CD2 . TYR A 1 33 ? 138.488 126.989 21.363 1.00 28.22 ? 33 TYR A CD2 1 ATOM 219 C CE1 . TYR A 1 33 ? 141.135 126.658 22.102 1.00 31.29 ? 33 TYR A CE1 1 ATOM 220 C CE2 . TYR A 1 33 ? 138.821 126.057 22.329 1.00 26.97 ? 33 TYR A CE2 1 ATOM 221 C CZ . TYR A 1 33 ? 140.145 125.896 22.696 1.00 29.78 ? 33 TYR A CZ 1 ATOM 222 O OH . TYR A 1 33 ? 140.492 124.979 23.662 1.00 28.06 ? 33 TYR A OH 1 ATOM 223 N N . ALA A 1 34 ? 140.485 126.509 17.307 1.00 39.47 ? 34 ALA A N 1 ATOM 224 C CA . ALA A 1 34 ? 141.729 125.897 16.864 1.00 38.68 ? 34 ALA A CA 1 ATOM 225 C C . ALA A 1 34 ? 141.494 124.801 15.847 1.00 36.78 ? 34 ALA A C 1 ATOM 226 O O . ALA A 1 34 ? 140.376 124.294 15.681 1.00 34.82 ? 34 ALA A O 1 ATOM 227 C CB . ALA A 1 34 ? 142.512 125.344 18.054 1.00 31.75 ? 34 ALA A CB 1 ATOM 228 N N . GLN A 1 35 ? 142.569 124.430 15.169 1.00 38.51 ? 35 GLN A N 1 ATOM 229 C CA . GLN A 1 35 ? 142.557 123.282 14.282 1.00 39.43 ? 35 GLN A CA 1 ATOM 230 C C . GLN A 1 35 ? 142.250 122.042 15.113 1.00 37.34 ? 35 GLN A C 1 ATOM 231 O O . GLN A 1 35 ? 142.869 121.841 16.156 1.00 33.50 ? 35 GLN A O 1 ATOM 232 C CB . GLN A 1 35 ? 143.942 123.134 13.672 1.00 48.65 ? 35 GLN A CB 1 ATOM 233 C CG . GLN A 1 35 ? 143.975 122.558 12.287 1.00 63.05 ? 35 GLN A CG 1 ATOM 234 C CD . GLN A 1 35 ? 144.864 123.377 11.381 1.00 77.89 ? 35 GLN A CD 1 ATOM 235 O OE1 . GLN A 1 35 ? 146.084 123.200 11.359 1.00 78.76 ? 35 GLN A OE1 1 ATOM 236 N NE2 . GLN A 1 35 ? 144.259 124.303 10.645 1.00 85.64 ? 35 GLN A NE2 1 ATOM 237 N N . PRO A 1 36 ? 141.287 121.214 14.667 1.00 35.95 ? 36 PRO A N 1 ATOM 238 C CA . PRO A 1 36 ? 141.049 119.936 15.349 1.00 34.30 ? 36 PRO A CA 1 ATOM 239 C C . PRO A 1 36 ? 142.364 119.159 15.447 1.00 34.33 ? 36 PRO A C 1 ATOM 240 O O . PRO A 1 36 ? 143.036 118.976 14.435 1.00 37.34 ? 36 PRO A O 1 ATOM 241 C CB . PRO A 1 36 ? 140.064 119.223 14.414 1.00 36.50 ? 36 PRO A CB 1 ATOM 242 C CG . PRO A 1 36 ? 139.352 120.320 13.711 1.00 36.73 ? 36 PRO A CG 1 ATOM 243 C CD . PRO A 1 36 ? 140.373 121.416 13.530 1.00 37.05 ? 36 PRO A CD 1 ATOM 244 N N . PRO A 1 37 ? 142.747 118.739 16.660 1.00 36.48 ? 37 PRO A N 1 ATOM 245 C CA . PRO A 1 37 ? 144.069 118.135 16.875 1.00 32.79 ? 37 PRO A CA 1 ATOM 246 C C . PRO A 1 37 ? 144.051 116.634 16.603 1.00 35.50 ? 37 PRO A C 1 ATOM 247 O O . PRO A 1 37 ? 144.178 115.831 17.535 1.00 36.38 ? 37 PRO A O 1 ATOM 248 C CB . PRO A 1 37 ? 144.332 118.417 18.354 1.00 30.99 ? 37 PRO A CB 1 ATOM 249 C CG . PRO A 1 37 ? 142.939 118.386 18.976 1.00 33.07 ? 37 PRO A CG 1 ATOM 250 C CD . PRO A 1 37 ? 141.986 118.890 17.917 1.00 31.04 ? 37 PRO A CD 1 ATOM 251 N N . LEU A 1 38 ? 143.902 116.281 15.325 1.00 41.18 ? 38 LEU A N 1 ATOM 252 C CA . LEU A 1 38 ? 143.721 114.903 14.880 1.00 41.25 ? 38 LEU A CA 1 ATOM 253 C C . LEU A 1 38 ? 144.914 114.424 14.055 1.00 40.95 ? 38 LEU A C 1 ATOM 254 O O . LEU A 1 38 ? 145.681 115.238 13.533 1.00 40.89 ? 38 LEU A O 1 ATOM 255 C CB . LEU A 1 38 ? 142.476 114.803 13.996 1.00 46.16 ? 38 LEU A CB 1 ATOM 256 C CG . LEU A 1 38 ? 141.169 115.474 14.415 1.00 51.76 ? 38 LEU A CG 1 ATOM 257 C CD1 . LEU A 1 38 ? 140.225 115.553 13.220 1.00 53.22 ? 38 LEU A CD1 1 ATOM 258 C CD2 . LEU A 1 38 ? 140.516 114.703 15.541 1.00 52.40 ? 38 LEU A CD2 1 ATOM 259 N N . GLY A 1 39 ? 145.043 113.105 13.909 1.00 41.33 ? 39 GLY A N 1 ATOM 260 C CA . GLY A 1 39 ? 146.099 112.520 13.092 1.00 40.28 ? 39 GLY A CA 1 ATOM 261 C C . GLY A 1 39 ? 147.484 112.923 13.566 1.00 44.10 ? 39 GLY A C 1 ATOM 262 O O . GLY A 1 39 ? 147.855 112.671 14.715 1.00 41.60 ? 39 GLY A O 1 ATOM 263 N N . ARG A 1 40 ? 148.243 113.570 12.688 1.00 45.69 ? 40 ARG A N 1 ATOM 264 C CA . ARG A 1 40 ? 149.568 114.072 13.045 1.00 49.57 ? 40 ARG A CA 1 ATOM 265 C C . ARG A 1 40 ? 149.531 115.155 14.128 1.00 48.11 ? 40 ARG A C 1 ATOM 266 O O . ARG A 1 40 ? 150.548 115.415 14.773 1.00 47.76 ? 40 ARG A O 1 ATOM 267 C CB . ARG A 1 40 ? 150.308 114.589 11.799 1.00 55.35 ? 40 ARG A CB 1 ATOM 268 C CG . ARG A 1 40 ? 149.530 115.616 10.973 1.00 63.56 ? 40 ARG A CG 1 ATOM 269 C CD . ARG A 1 40 ? 150.408 116.240 9.896 1.00 73.79 ? 40 ARG A CD 1 ATOM 270 N NE . ARG A 1 40 ? 151.636 116.780 10.472 1.00 83.94 ? 40 ARG A NE 1 ATOM 271 C CZ . ARG A 1 40 ? 151.761 118.017 10.950 1.00 87.17 ? 40 ARG A CZ 1 ATOM 272 N NH1 . ARG A 1 40 ? 150.733 118.855 10.916 1.00 86.17 ? 40 ARG A NH1 1 ATOM 273 N NH2 . ARG A 1 40 ? 152.917 118.416 11.464 1.00 87.66 ? 40 ARG A NH2 1 ATOM 274 N N . LEU A 1 41 ? 148.372 115.784 14.326 1.00 45.27 ? 41 LEU A N 1 ATOM 275 C CA . LEU A 1 41 ? 148.246 116.860 15.316 1.00 45.87 ? 41 LEU A CA 1 ATOM 276 C C . LEU A 1 41 ? 147.979 116.375 16.748 1.00 41.36 ? 41 LEU A C 1 ATOM 277 O O . LEU A 1 41 ? 148.048 117.162 17.698 1.00 34.59 ? 41 LEU A O 1 ATOM 278 C CB . LEU A 1 41 ? 147.178 117.876 14.882 1.00 50.51 ? 41 LEU A CB 1 ATOM 279 C CG . LEU A 1 41 ? 147.461 118.667 13.596 1.00 50.09 ? 41 LEU A CG 1 ATOM 280 C CD1 . LEU A 1 41 ? 146.330 119.631 13.267 1.00 48.48 ? 41 LEU A CD1 1 ATOM 281 C CD2 . LEU A 1 41 ? 148.771 119.415 13.709 1.00 44.43 ? 41 LEU A CD2 1 ATOM 282 N N . ARG A 1 42 ? 147.676 115.089 16.911 1.00 38.77 ? 42 ARG A N 1 ATOM 283 C CA . ARG A 1 42 ? 147.421 114.545 18.249 1.00 40.36 ? 42 ARG A CA 1 ATOM 284 C C . ARG A 1 42 ? 148.673 114.648 19.118 1.00 41.57 ? 42 ARG A C 1 ATOM 285 O O . ARG A 1 42 ? 149.755 114.297 18.659 1.00 33.59 ? 42 ARG A O 1 ATOM 286 C CB . ARG A 1 42 ? 146.971 113.084 18.159 1.00 38.22 ? 42 ARG A CB 1 ATOM 287 C CG . ARG A 1 42 ? 146.803 112.403 19.516 1.00 40.45 ? 42 ARG A CG 1 ATOM 288 C CD . ARG A 1 42 ? 146.631 110.880 19.380 1.00 37.71 ? 42 ARG A CD 1 ATOM 289 N NE . ARG A 1 42 ? 145.300 110.505 18.903 1.00 35.35 ? 42 ARG A NE 1 ATOM 290 C CZ . ARG A 1 42 ? 144.890 109.251 18.702 1.00 39.11 ? 42 ARG A CZ 1 ATOM 291 N NH1 . ARG A 1 42 ? 145.710 108.229 18.929 1.00 34.97 ? 42 ARG A NH1 1 ATOM 292 N NH2 . ARG A 1 42 ? 143.658 109.015 18.269 1.00 34.78 ? 42 ARG A NH2 1 ATOM 293 N N . PHE A 1 43 ? 148.512 115.127 20.355 1.00 35.18 ? 43 PHE A N 1 ATOM 294 C CA . PHE A 1 43 ? 149.618 115.357 21.315 1.00 30.50 ? 43 PHE A CA 1 ATOM 295 C C . PHE A 1 43 ? 150.414 116.653 21.092 1.00 33.74 ? 43 PHE A C 1 ATOM 296 O O . PHE A 1 43 ? 151.262 117.006 21.916 1.00 32.08 ? 43 PHE A O 1 ATOM 297 C CB . PHE A 1 43 ? 150.615 114.183 21.398 1.00 31.33 ? 43 PHE A CB 1 ATOM 298 C CG . PHE A 1 43 ? 149.997 112.854 21.776 1.00 35.86 ? 43 PHE A CG 1 ATOM 299 C CD1 . PHE A 1 43 ? 149.307 112.700 22.969 1.00 31.73 ? 43 PHE A CD1 1 ATOM 300 C CD2 . PHE A 1 43 ? 150.160 111.744 20.952 1.00 33.77 ? 43 PHE A CD2 1 ATOM 301 C CE1 . PHE A 1 43 ? 148.761 111.465 23.320 1.00 32.10 ? 43 PHE A CE1 1 ATOM 302 C CE2 . PHE A 1 43 ? 149.624 110.511 21.295 1.00 32.52 ? 43 PHE A CE2 1 ATOM 303 C CZ . PHE A 1 43 ? 148.924 110.369 22.476 1.00 33.51 ? 43 PHE A CZ 1 ATOM 304 N N . LYS A 1 44 ? 150.167 117.353 19.988 1.00 35.69 ? 44 LYS A N 1 ATOM 305 C CA . LYS A 1 44 ? 150.863 118.623 19.753 1.00 36.95 ? 44 LYS A CA 1 ATOM 306 C C . LYS A 1 44 ? 150.102 119.813 20.313 1.00 34.70 ? 44 LYS A C 1 ATOM 307 O O . LYS A 1 44 ? 148.896 119.729 20.559 1.00 30.33 ? 44 LYS A O 1 ATOM 308 C CB . LYS A 1 44 ? 151.094 118.853 18.263 1.00 39.81 ? 44 LYS A CB 1 ATOM 309 C CG . LYS A 1 44 ? 152.051 117.851 17.618 1.00 41.57 ? 44 LYS A CG 1 ATOM 310 C CD . LYS A 1 44 ? 152.491 118.348 16.259 1.00 48.56 ? 44 LYS A CD 1 ATOM 311 C CE . LYS A 1 44 ? 153.748 117.639 15.798 1.00 61.76 ? 44 LYS A CE 1 ATOM 312 N NZ . LYS A 1 44 ? 153.548 116.162 15.724 1.00 65.88 ? 44 LYS A NZ 1 ATOM 313 N N . LYS A 1 45 ? 150.817 120.924 20.496 1.00 31.62 ? 45 LYS A N 1 ATOM 314 C CA . LYS A 1 45 ? 150.191 122.193 20.815 1.00 31.70 ? 45 LYS A CA 1 ATOM 315 C C . LYS A 1 45 ? 149.095 122.483 19.792 1.00 35.46 ? 45 LYS A C 1 ATOM 316 O O . LYS A 1 45 ? 149.169 122.022 18.651 1.00 32.77 ? 45 LYS A O 1 ATOM 317 C CB . LYS A 1 45 ? 151.236 123.315 20.845 1.00 32.04 ? 45 LYS A CB 1 ATOM 318 C CG . LYS A 1 45 ? 152.219 123.184 21.999 1.00 36.17 ? 45 LYS A CG 1 ATOM 319 C CD . LYS A 1 45 ? 153.401 124.155 21.899 1.00 39.96 ? 45 LYS A CD 1 ATOM 320 C CE . LYS A 1 45 ? 153.002 125.581 22.245 1.00 45.14 ? 45 LYS A CE 1 ATOM 321 N NZ . LYS A 1 45 ? 154.172 126.523 22.280 1.00 45.66 ? 45 LYS A NZ 1 ATOM 322 N N . PRO A 1 46 ? 148.055 123.221 20.206 1.00 30.71 ? 46 PRO A N 1 ATOM 323 C CA . PRO A 1 46 ? 146.965 123.547 19.281 1.00 31.26 ? 46 PRO A CA 1 ATOM 324 C C . PRO A 1 46 ? 147.467 124.455 18.171 1.00 33.05 ? 46 PRO A C 1 ATOM 325 O O . PRO A 1 46 ? 148.231 125.379 18.440 1.00 33.45 ? 46 PRO A O 1 ATOM 326 C CB . PRO A 1 46 ? 145.962 124.296 20.175 1.00 30.07 ? 46 PRO A CB 1 ATOM 327 C CG . PRO A 1 46 ? 146.788 124.849 21.289 1.00 29.47 ? 46 PRO A CG 1 ATOM 328 C CD . PRO A 1 46 ? 147.846 123.806 21.540 1.00 29.44 ? 46 PRO A CD 1 ATOM 329 N N . GLN A 1 47 ? 147.062 124.178 16.940 1.00 36.96 ? 47 GLN A N 1 ATOM 330 C CA . GLN A 1 47 ? 147.478 124.975 15.794 1.00 39.90 ? 47 GLN A CA 1 ATOM 331 C C . GLN A 1 47 ? 146.413 126.012 15.478 1.00 46.42 ? 47 GLN A C 1 ATOM 332 O O . GLN A 1 47 ? 145.218 125.772 15.699 1.00 39.42 ? 47 GLN A O 1 ATOM 333 C CB . GLN A 1 47 ? 147.704 124.076 14.577 1.00 37.88 ? 47 GLN A CB 1 ATOM 334 C CG . GLN A 1 47 ? 148.756 122.992 14.787 1.00 59.13 ? 47 GLN A CG 1 ATOM 335 C CD . GLN A 1 47 ? 150.108 123.564 15.168 1.00 61.03 ? 47 GLN A CD 1 ATOM 336 O OE1 . GLN A 1 47 ? 150.606 124.487 14.520 1.00 66.03 ? 47 GLN A OE1 1 ATOM 337 N NE2 . GLN A 1 47 ? 150.703 123.031 16.239 1.00 53.64 ? 47 GLN A NE2 1 ATOM 338 N N . SER A 1 48 ? 146.844 127.159 14.958 1.00 51.82 ? 48 SER A N 1 ATOM 339 C CA . SER A 1 48 ? 145.927 128.257 14.660 1.00 56.47 ? 48 SER A CA 1 ATOM 340 C C . SER A 1 48 ? 144.883 127.880 13.621 1.00 57.09 ? 48 SER A C 1 ATOM 341 O O . SER A 1 48 ? 145.078 126.963 12.826 1.00 61.72 ? 48 SER A O 1 ATOM 342 C CB . SER A 1 48 ? 146.687 129.514 14.220 1.00 62.83 ? 48 SER A CB 1 ATOM 343 O OG . SER A 1 48 ? 146.780 130.439 15.293 1.00 67.18 ? 48 SER A OG 1 ATOM 344 N N . LEU A 1 49 ? 143.770 128.601 13.637 1.00 59.31 ? 49 LEU A N 1 ATOM 345 C CA . LEU A 1 49 ? 142.630 128.247 12.810 1.00 66.00 ? 49 LEU A CA 1 ATOM 346 C C . LEU A 1 49 ? 142.746 128.794 11.395 1.00 77.33 ? 49 LEU A C 1 ATOM 347 O O . LEU A 1 49 ? 143.492 129.738 11.134 1.00 80.68 ? 49 LEU A O 1 ATOM 348 C CB . LEU A 1 49 ? 141.335 128.727 13.465 1.00 63.83 ? 49 LEU A CB 1 ATOM 349 C CG . LEU A 1 49 ? 140.051 127.996 13.086 1.00 63.41 ? 49 LEU A CG 1 ATOM 350 C CD1 . LEU A 1 49 ? 140.299 126.503 13.012 1.00 61.01 ? 49 LEU A CD1 1 ATOM 351 C CD2 . LEU A 1 49 ? 138.969 128.307 14.099 1.00 64.37 ? 49 LEU A CD2 1 ATOM 352 N N . THR A 1 50 ? 141.990 128.176 10.495 1.00 83.90 ? 50 THR A N 1 ATOM 353 C CA . THR A 1 50 ? 141.962 128.528 9.087 1.00 93.30 ? 50 THR A CA 1 ATOM 354 C C . THR A 1 50 ? 141.417 129.936 8.867 1.00 95.66 ? 50 THR A C 1 ATOM 355 O O . THR A 1 50 ? 142.030 130.930 9.263 1.00 99.52 ? 50 THR A O 1 ATOM 356 C CB . THR A 1 50 ? 141.053 127.545 8.320 1.00 96.87 ? 50 THR A CB 1 ATOM 357 O OG1 . THR A 1 50 ? 139.680 127.833 8.619 1.00 98.02 ? 50 THR A OG1 1 ATOM 358 C CG2 . THR A 1 50 ? 141.356 126.108 8.727 1.00 93.37 ? 50 THR A CG2 1 ATOM 359 N N . LYS A 1 51 ? 140.270 129.984 8.195 1.00 93.48 ? 51 LYS A N 1 ATOM 360 C CA . LYS A 1 51 ? 139.488 131.185 7.905 1.00 87.41 ? 51 LYS A CA 1 ATOM 361 C C . LYS A 1 51 ? 138.352 130.714 7.002 1.00 85.39 ? 51 LYS A C 1 ATOM 362 O O . LYS A 1 51 ? 138.607 130.136 5.948 1.00 88.73 ? 51 LYS A O 1 ATOM 363 C CB . LYS A 1 51 ? 140.317 132.285 7.217 1.00 85.63 ? 51 LYS A CB 1 ATOM 364 C CG . LYS A 1 51 ? 141.424 131.798 6.275 1.00 87.56 ? 51 LYS A CG 1 ATOM 365 C CD . LYS A 1 51 ? 142.691 132.639 6.445 1.00 82.67 ? 51 LYS A CD 1 ATOM 366 C CE . LYS A 1 51 ? 143.953 131.843 6.122 1.00 75.82 ? 51 LYS A CE 1 ATOM 367 N NZ . LYS A 1 51 ? 143.997 131.360 4.709 1.00 69.49 ? 51 LYS A NZ 1 ATOM 368 N N . TRP A 1 52 ? 137.105 130.918 7.424 1.00 78.70 ? 52 TRP A N 1 ATOM 369 C CA . TRP A 1 52 ? 135.961 130.456 6.629 1.00 73.95 ? 52 TRP A CA 1 ATOM 370 C C . TRP A 1 52 ? 135.133 131.604 6.040 1.00 72.91 ? 52 TRP A C 1 ATOM 371 O O . TRP A 1 52 ? 135.064 132.695 6.610 1.00 66.75 ? 52 TRP A O 1 ATOM 372 C CB . TRP A 1 52 ? 135.078 129.484 7.423 1.00 69.07 ? 52 TRP A CB 1 ATOM 373 C CG . TRP A 1 52 ? 134.402 130.092 8.609 1.00 67.22 ? 52 TRP A CG 1 ATOM 374 C CD1 . TRP A 1 52 ? 133.176 130.688 8.637 1.00 68.08 ? 52 TRP A CD1 1 ATOM 375 C CD2 . TRP A 1 52 ? 134.912 130.157 9.946 1.00 64.07 ? 52 TRP A CD2 1 ATOM 376 N NE1 . TRP A 1 52 ? 132.892 131.127 9.910 1.00 63.40 ? 52 TRP A NE1 1 ATOM 377 C CE2 . TRP A 1 52 ? 133.940 130.811 10.732 1.00 60.74 ? 52 TRP A CE2 1 ATOM 378 C CE3 . TRP A 1 52 ? 136.095 129.730 10.554 1.00 65.21 ? 52 TRP A CE3 1 ATOM 379 C CZ2 . TRP A 1 52 ? 134.116 131.047 12.095 1.00 61.57 ? 52 TRP A CZ2 1 ATOM 380 C CZ3 . TRP A 1 52 ? 136.268 129.964 11.912 1.00 63.96 ? 52 TRP A CZ3 1 ATOM 381 C CH2 . TRP A 1 52 ? 135.284 130.615 12.666 1.00 61.07 ? 52 TRP A CH2 1 ATOM 382 N N . SER A 1 53 ? 134.503 131.337 4.897 1.00 77.62 ? 53 SER A N 1 ATOM 383 C CA . SER A 1 53 ? 133.857 132.373 4.094 1.00 78.89 ? 53 SER A CA 1 ATOM 384 C C . SER A 1 53 ? 132.350 132.424 4.297 1.00 79.90 ? 53 SER A C 1 ATOM 385 O O . SER A 1 53 ? 131.705 133.426 3.981 1.00 81.27 ? 53 SER A O 1 ATOM 386 C CB . SER A 1 53 ? 134.137 132.129 2.615 1.00 80.16 ? 53 SER A CB 1 ATOM 387 O OG . SER A 1 53 ? 133.426 130.990 2.161 1.00 84.58 ? 53 SER A OG 1 ATOM 388 N N . ASP A 1 54 ? 131.788 131.332 4.802 1.00 78.96 ? 54 ASP A N 1 ATOM 389 C CA . ASP A 1 54 ? 130.354 131.261 5.050 1.00 80.48 ? 54 ASP A CA 1 ATOM 390 C C . ASP A 1 54 ? 130.027 131.602 6.504 1.00 72.01 ? 54 ASP A C 1 ATOM 391 O O . ASP A 1 54 ? 130.867 132.145 7.227 1.00 64.83 ? 54 ASP A O 1 ATOM 392 C CB . ASP A 1 54 ? 129.814 129.876 4.676 1.00 87.91 ? 54 ASP A CB 1 ATOM 393 C CG . ASP A 1 54 ? 130.776 128.754 5.035 1.00 92.58 ? 54 ASP A CG 1 ATOM 394 O OD1 . ASP A 1 54 ? 131.990 129.023 5.177 1.00 93.57 ? 54 ASP A OD1 1 ATOM 395 O OD2 . ASP A 1 54 ? 130.319 127.599 5.165 1.00 94.20 ? 54 ASP A OD2 1 ATOM 396 N N . ILE A 1 55 ? 128.802 131.292 6.920 1.00 68.99 ? 55 ILE A N 1 ATOM 397 C CA . ILE A 1 55 ? 128.351 131.570 8.280 1.00 63.60 ? 55 ILE A CA 1 ATOM 398 C C . ILE A 1 55 ? 128.413 130.318 9.143 1.00 61.44 ? 55 ILE A C 1 ATOM 399 O O . ILE A 1 55 ? 127.805 129.299 8.808 1.00 60.00 ? 55 ILE A O 1 ATOM 400 C CB . ILE A 1 55 ? 126.905 132.101 8.292 1.00 64.70 ? 55 ILE A CB 1 ATOM 401 C CG1 . ILE A 1 55 ? 126.819 133.433 7.543 1.00 66.03 ? 55 ILE A CG1 1 ATOM 402 C CG2 . ILE A 1 55 ? 126.394 132.237 9.725 1.00 61.95 ? 55 ILE A CG2 1 ATOM 403 C CD1 . ILE A 1 55 ? 125.445 134.053 7.550 1.00 58.68 ? 55 ILE A CD1 1 ATOM 404 N N . TRP A 1 56 ? 129.148 130.395 10.251 1.00 53.67 ? 56 TRP A N 1 ATOM 405 C CA . TRP A 1 56 ? 129.239 129.277 11.177 1.00 50.73 ? 56 TRP A CA 1 ATOM 406 C C . TRP A 1 56 ? 128.067 129.275 12.140 1.00 51.91 ? 56 TRP A C 1 ATOM 407 O O . TRP A 1 56 ? 127.869 130.238 12.884 1.00 56.29 ? 56 TRP A O 1 ATOM 408 C CB . TRP A 1 56 ? 130.533 129.331 11.985 1.00 51.44 ? 56 TRP A CB 1 ATOM 409 C CG . TRP A 1 56 ? 130.637 128.185 12.933 1.00 52.02 ? 56 TRP A CG 1 ATOM 410 C CD1 . TRP A 1 56 ? 130.023 128.057 14.152 1.00 46.43 ? 56 TRP A CD1 1 ATOM 411 C CD2 . TRP A 1 56 ? 131.389 126.987 12.734 1.00 56.05 ? 56 TRP A CD2 1 ATOM 412 N NE1 . TRP A 1 56 ? 130.353 126.849 14.721 1.00 48.76 ? 56 TRP A NE1 1 ATOM 413 C CE2 . TRP A 1 56 ? 131.193 126.175 13.871 1.00 52.84 ? 56 TRP A CE2 1 ATOM 414 C CE3 . TRP A 1 56 ? 132.214 126.523 11.707 1.00 61.25 ? 56 TRP A CE3 1 ATOM 415 C CZ2 . TRP A 1 56 ? 131.795 124.924 14.005 1.00 53.90 ? 56 TRP A CZ2 1 ATOM 416 C CZ3 . TRP A 1 56 ? 132.809 125.281 11.841 1.00 60.79 ? 56 TRP A CZ3 1 ATOM 417 C CH2 . TRP A 1 56 ? 132.596 124.496 12.980 1.00 56.31 ? 56 TRP A CH2 1 ATOM 418 N N . ASN A 1 57 ? 127.307 128.185 12.144 1.00 51.72 ? 57 ASN A N 1 ATOM 419 C CA . ASN A 1 57 ? 126.206 128.037 13.087 1.00 53.69 ? 57 ASN A CA 1 ATOM 420 C C . ASN A 1 57 ? 126.697 127.655 14.485 1.00 46.71 ? 57 ASN A C 1 ATOM 421 O O . ASN A 1 57 ? 127.193 126.551 14.704 1.00 42.56 ? 57 ASN A O 1 ATOM 422 C CB . ASN A 1 57 ? 125.176 127.031 12.569 1.00 64.83 ? 57 ASN A CB 1 ATOM 423 C CG . ASN A 1 57 ? 124.350 127.589 11.424 1.00 81.39 ? 57 ASN A CG 1 ATOM 424 O OD1 . ASN A 1 57 ? 124.397 128.789 11.141 1.00 81.05 ? 57 ASN A OD1 1 ATOM 425 N ND2 . ASN A 1 57 ? 123.575 126.727 10.769 1.00 99.69 ? 57 ASN A ND2 1 ATOM 426 N N . ALA A 1 58 ? 126.571 128.589 15.422 1.00 42.70 ? 58 ALA A N 1 ATOM 427 C CA . ALA A 1 58 ? 126.952 128.347 16.809 1.00 37.95 ? 58 ALA A CA 1 ATOM 428 C C . ALA A 1 58 ? 125.707 128.279 17.692 1.00 37.59 ? 58 ALA A C 1 ATOM 429 O O . ALA A 1 58 ? 125.493 129.134 18.563 1.00 39.83 ? 58 ALA A O 1 ATOM 430 C CB . ALA A 1 58 ? 127.892 129.445 17.295 1.00 37.16 ? 58 ALA A CB 1 ATOM 431 N N . THR A 1 59 ? 124.898 127.247 17.474 1.00 40.81 ? 59 THR A N 1 ATOM 432 C CA . THR A 1 59 ? 123.576 127.152 18.084 1.00 40.62 ? 59 THR A CA 1 ATOM 433 C C . THR A 1 59 ? 123.392 125.869 18.899 1.00 41.11 ? 59 THR A C 1 ATOM 434 O O . THR A 1 59 ? 122.261 125.481 19.212 1.00 41.61 ? 59 THR A O 1 ATOM 435 C CB . THR A 1 59 ? 122.483 127.195 17.002 1.00 46.33 ? 59 THR A CB 1 ATOM 436 O OG1 . THR A 1 59 ? 122.779 126.213 15.999 1.00 46.75 ? 59 THR A OG1 1 ATOM 437 C CG2 . THR A 1 59 ? 122.435 128.563 16.345 1.00 44.88 ? 59 THR A CG2 1 ATOM 438 N N . LYS A 1 60 ? 124.502 125.213 19.233 1.00 39.34 ? 60 LYS A N 1 ATOM 439 C CA . LYS A 1 60 ? 124.473 124.004 20.058 1.00 34.71 ? 60 LYS A CA 1 ATOM 440 C C . LYS A 1 60 ? 125.865 123.716 20.618 1.00 46.69 ? 60 LYS A C 1 ATOM 441 O O . LYS A 1 60 ? 126.878 124.034 19.985 1.00 32.96 ? 60 LYS A O 1 ATOM 442 C CB . LYS A 1 60 ? 123.918 122.791 19.275 1.00 36.07 ? 60 LYS A CB 1 ATOM 443 C CG . LYS A 1 60 ? 124.911 122.052 18.382 1.00 65.72 ? 60 LYS A CG 1 ATOM 444 C CD . LYS A 1 60 ? 124.225 120.845 17.710 1.00 73.13 ? 60 LYS A CD 1 ATOM 445 C CE . LYS A 1 60 ? 125.213 119.903 17.006 1.00 77.22 ? 60 LYS A CE 1 ATOM 446 N NZ . LYS A 1 60 ? 125.900 120.512 15.827 1.00 76.97 ? 60 LYS A NZ 1 ATOM 447 N N . TYR A 1 61 ? 125.913 123.150 21.822 1.00 31.66 ? 61 TYR A N 1 ATOM 448 C CA . TYR A 1 61 ? 127.182 122.767 22.436 1.00 34.64 ? 61 TYR A CA 1 ATOM 449 C C . TYR A 1 61 ? 127.935 121.812 21.502 1.00 32.76 ? 61 TYR A C 1 ATOM 450 O O . TYR A 1 61 ? 127.308 121.018 20.802 1.00 31.78 ? 61 TYR A O 1 ATOM 451 C CB . TYR A 1 61 ? 126.919 122.080 23.774 1.00 33.73 ? 61 TYR A CB 1 ATOM 452 C CG . TYR A 1 61 ? 126.477 122.985 24.911 1.00 31.64 ? 61 TYR A CG 1 ATOM 453 C CD1 . TYR A 1 61 ? 127.318 123.977 25.399 1.00 29.65 ? 61 TYR A CD1 1 ATOM 454 C CD2 . TYR A 1 61 ? 125.242 122.808 25.533 1.00 32.59 ? 61 TYR A CD2 1 ATOM 455 C CE1 . TYR A 1 61 ? 126.940 124.786 26.466 1.00 31.17 ? 61 TYR A CE1 1 ATOM 456 C CE2 . TYR A 1 61 ? 124.856 123.612 26.602 1.00 28.64 ? 61 TYR A CE2 1 ATOM 457 C CZ . TYR A 1 61 ? 125.708 124.594 27.062 1.00 31.06 ? 61 TYR A CZ 1 ATOM 458 O OH . TYR A 1 61 ? 125.335 125.398 28.127 1.00 31.02 ? 61 TYR A OH 1 ATOM 459 N N . ALA A 1 62 ? 129.265 121.905 21.470 1.00 29.80 ? 62 ALA A N 1 ATOM 460 C CA . ALA A 1 62 ? 130.075 121.055 20.586 1.00 42.45 ? 62 ALA A CA 1 ATOM 461 C C . ALA A 1 62 ? 130.480 119.780 21.322 1.00 42.13 ? 62 ALA A C 1 ATOM 462 O O . ALA A 1 62 ? 130.178 119.646 22.503 1.00 28.53 ? 62 ALA A O 1 ATOM 463 C CB . ALA A 1 62 ? 131.321 121.818 20.092 1.00 30.18 ? 62 ALA A CB 1 ATOM 464 N N . ASN A 1 63 ? 131.159 118.859 20.633 1.00 29.99 ? 63 ASN A N 1 ATOM 465 C CA . ASN A 1 63 ? 131.737 117.660 21.264 1.00 32.61 ? 63 ASN A CA 1 ATOM 466 C C . ASN A 1 63 ? 132.592 117.984 22.509 1.00 28.97 ? 63 ASN A C 1 ATOM 467 O O . ASN A 1 63 ? 133.277 119.003 22.527 1.00 27.22 ? 63 ASN A O 1 ATOM 468 C CB . ASN A 1 63 ? 132.622 116.898 20.268 1.00 30.21 ? 63 ASN A CB 1 ATOM 469 C CG . ASN A 1 63 ? 131.879 116.451 19.015 1.00 33.14 ? 63 ASN A CG 1 ATOM 470 O OD1 . ASN A 1 63 ? 130.672 116.193 19.034 1.00 37.05 ? 63 ASN A OD1 1 ATOM 471 N ND2 . ASN A 1 63 ? 132.616 116.336 17.917 1.00 35.16 ? 63 ASN A ND2 1 ATOM 472 N N . SER A 1 64 ? 132.566 117.109 23.523 1.00 27.12 ? 64 SER A N 1 ATOM 473 C CA . SER A 1 64 ? 133.445 117.210 24.698 1.00 29.20 ? 64 SER A CA 1 ATOM 474 C C . SER A 1 64 ? 134.710 116.429 24.372 1.00 31.97 ? 64 SER A C 1 ATOM 475 O O . SER A 1 64 ? 134.641 115.510 23.557 1.00 26.89 ? 64 SER A O 1 ATOM 476 C CB . SER A 1 64 ? 132.789 116.587 25.937 1.00 25.47 ? 64 SER A CB 1 ATOM 477 O OG . SER A 1 64 ? 131.541 117.193 26.256 1.00 32.13 ? 64 SER A OG 1 ATOM 478 N N . CYS A 1 65 ? 135.851 116.763 24.986 1.00 25.06 ? 65 CYS A N 1 ATOM 479 C CA . CYS A 1 65 ? 137.083 116.025 24.683 1.00 27.35 ? 65 CYS A CA 1 ATOM 480 C C . CYS A 1 65 ? 137.056 114.575 25.221 1.00 30.94 ? 65 CYS A C 1 ATOM 481 O O . CYS A 1 65 ? 136.373 114.278 26.220 1.00 26.64 ? 65 CYS A O 1 ATOM 482 C CB . CYS A 1 65 ? 138.327 116.786 25.166 1.00 24.54 ? 65 CYS A CB 1 ATOM 483 S SG . CYS A 1 65 ? 138.445 118.517 24.530 1.00 25.23 ? 65 CYS A SG 1 ATOM 484 N N . CYS A 1 66 ? 137.772 113.676 24.541 1.00 29.04 ? 66 CYS A N 1 ATOM 485 C CA . CYS A 1 66 ? 137.835 112.268 24.946 1.00 35.34 ? 66 CYS A CA 1 ATOM 486 C C . CYS A 1 66 ? 138.222 112.138 26.415 1.00 34.41 ? 66 CYS A C 1 ATOM 487 O O . CYS A 1 66 ? 139.118 112.838 26.885 1.00 31.59 ? 66 CYS A O 1 ATOM 488 C CB . CYS A 1 66 ? 138.856 111.498 24.098 1.00 31.29 ? 66 CYS A CB 1 ATOM 489 S SG . CYS A 1 66 ? 138.429 111.356 22.360 1.00 46.29 ? 66 CYS A SG 1 ATOM 490 N N . GLN A 1 67 ? 137.550 111.245 27.133 1.00 30.04 ? 67 GLN A N 1 ATOM 491 C CA . GLN A 1 67 ? 137.807 111.073 28.557 1.00 38.73 ? 67 GLN A CA 1 ATOM 492 C C . GLN A 1 67 ? 137.124 109.826 29.114 1.00 44.79 ? 67 GLN A C 1 ATOM 493 O O . GLN A 1 67 ? 136.106 109.376 28.582 1.00 31.10 ? 67 GLN A O 1 ATOM 494 C CB . GLN A 1 67 ? 137.304 112.295 29.323 1.00 28.27 ? 67 GLN A CB 1 ATOM 495 C CG . GLN A 1 67 ? 135.823 112.596 29.112 1.00 28.02 ? 67 GLN A CG 1 ATOM 496 C CD . GLN A 1 67 ? 135.432 113.966 29.675 1.00 32.08 ? 67 GLN A CD 1 ATOM 497 O OE1 . GLN A 1 67 ? 135.007 114.081 30.825 1.00 26.36 ? 67 GLN A OE1 1 ATOM 498 N NE2 . GLN A 1 67 ? 135.580 115.005 28.862 1.00 26.36 ? 67 GLN A NE2 1 ATOM 499 N N . ASN A 1 68 ? 137.679 109.279 30.194 1.00 30.72 ? 68 ASN A N 1 ATOM 500 C CA . ASN A 1 68 ? 136.988 108.229 30.929 1.00 34.36 ? 68 ASN A CA 1 ATOM 501 C C . ASN A 1 68 ? 135.813 108.821 31.708 1.00 30.36 ? 68 ASN A C 1 ATOM 502 O O . ASN A 1 68 ? 135.821 109.992 32.068 1.00 33.92 ? 68 ASN A O 1 ATOM 503 C CB . ASN A 1 68 ? 137.951 107.450 31.835 1.00 32.04 ? 68 ASN A CB 1 ATOM 504 C CG . ASN A 1 68 ? 138.981 106.636 31.032 1.00 39.79 ? 68 ASN A CG 1 ATOM 505 O OD1 . ASN A 1 68 ? 138.623 105.707 30.313 1.00 38.36 ? 68 ASN A OD1 1 ATOM 506 N ND2 . ASN A 1 68 ? 140.257 106.994 31.149 1.00 38.42 ? 68 ASN A ND2 1 ATOM 507 N N . ILE A 1 69 ? 134.792 108.010 31.936 1.00 30.98 ? 69 ILE A N 1 ATOM 508 C CA . ILE A 1 69 ? 133.561 108.470 32.571 1.00 30.90 ? 69 ILE A CA 1 ATOM 509 C C . ILE A 1 69 ? 133.442 107.829 33.963 1.00 31.14 ? 69 ILE A C 1 ATOM 510 O O . ILE A 1 69 ? 133.957 106.733 34.187 1.00 31.36 ? 69 ILE A O 1 ATOM 511 C CB . ILE A 1 69 ? 132.340 108.124 31.662 1.00 50.46 ? 69 ILE A CB 1 ATOM 512 C CG1 . ILE A 1 69 ? 132.111 109.233 30.636 1.00 50.34 ? 69 ILE A CG1 1 ATOM 513 C CG2 . ILE A 1 69 ? 131.065 107.882 32.457 1.00 51.77 ? 69 ILE A CG2 1 ATOM 514 C CD1 . ILE A 1 69 ? 133.078 109.201 29.484 1.00 50.17 ? 69 ILE A CD1 1 ATOM 515 N N . ASP A 1 70 ? 132.795 108.524 34.896 1.00 30.62 ? 70 ASP A N 1 ATOM 516 C CA . ASP A 1 70 ? 132.502 107.981 36.229 1.00 35.42 ? 70 ASP A CA 1 ATOM 517 C C . ASP A 1 70 ? 131.347 106.968 36.140 1.00 35.88 ? 70 ASP A C 1 ATOM 518 O O . ASP A 1 70 ? 130.216 107.360 35.857 1.00 30.23 ? 70 ASP A O 1 ATOM 519 C CB . ASP A 1 70 ? 132.126 109.145 37.167 1.00 32.31 ? 70 ASP A CB 1 ATOM 520 C CG . ASP A 1 70 ? 131.875 108.706 38.606 1.00 34.99 ? 70 ASP A CG 1 ATOM 521 O OD1 . ASP A 1 70 ? 131.744 107.492 38.871 1.00 40.92 ? 70 ASP A OD1 1 ATOM 522 O OD2 . ASP A 1 70 ? 131.797 109.591 39.485 1.00 29.88 ? 70 ASP A OD2 1 ATOM 523 N N . GLN A 1 71 ? 131.633 105.684 36.388 1.00 31.56 ? 71 GLN A N 1 ATOM 524 C CA . GLN A 1 71 ? 130.614 104.622 36.326 1.00 38.27 ? 71 GLN A CA 1 ATOM 525 C C . GLN A 1 71 ? 130.345 104.018 37.698 1.00 36.91 ? 71 GLN A C 1 ATOM 526 O O . GLN A 1 71 ? 129.715 102.966 37.803 1.00 34.60 ? 71 GLN A O 1 ATOM 527 C CB . GLN A 1 71 ? 131.048 103.480 35.406 1.00 34.30 ? 71 GLN A CB 1 ATOM 528 C CG . GLN A 1 71 ? 131.545 103.888 34.028 1.00 58.34 ? 71 GLN A CG 1 ATOM 529 C CD . GLN A 1 71 ? 132.333 102.764 33.352 1.00 59.95 ? 71 GLN A CD 1 ATOM 530 O OE1 . GLN A 1 71 ? 133.416 102.983 32.795 1.00 62.92 ? 71 GLN A OE1 1 ATOM 531 N NE2 . GLN A 1 71 ? 131.791 101.556 33.404 1.00 52.41 ? 71 GLN A NE2 1 ATOM 532 N N . SER A 1 72 ? 130.815 104.678 38.749 1.00 33.96 ? 72 SER A N 1 ATOM 533 C CA . SER A 1 72 ? 130.696 104.122 40.094 1.00 36.75 ? 72 SER A CA 1 ATOM 534 C C . SER A 1 72 ? 129.260 104.052 40.629 1.00 32.46 ? 72 SER A C 1 ATOM 535 O O . SER A 1 72 ? 128.944 103.162 41.419 1.00 32.52 ? 72 SER A O 1 ATOM 536 C CB . SER A 1 72 ? 131.605 104.883 41.064 1.00 32.75 ? 72 SER A CB 1 ATOM 537 O OG . SER A 1 72 ? 132.933 104.890 40.569 1.00 35.48 ? 72 SER A OG 1 ATOM 538 N N . PHE A 1 73 ? 128.396 104.972 40.197 1.00 31.15 ? 73 PHE A N 1 ATOM 539 C CA . PHE A 1 73 ? 127.004 104.986 40.653 1.00 36.21 ? 73 PHE A CA 1 ATOM 540 C C . PHE A 1 73 ? 125.994 105.219 39.515 1.00 31.53 ? 73 PHE A C 1 ATOM 541 O O . PHE A 1 73 ? 125.350 106.269 39.468 1.00 35.07 ? 73 PHE A O 1 ATOM 542 C CB . PHE A 1 73 ? 126.807 106.067 41.730 1.00 36.05 ? 73 PHE A CB 1 ATOM 543 C CG . PHE A 1 73 ? 127.800 105.996 42.871 1.00 34.97 ? 73 PHE A CG 1 ATOM 544 C CD1 . PHE A 1 73 ? 127.666 105.031 43.868 1.00 32.28 ? 73 PHE A CD1 1 ATOM 545 C CD2 . PHE A 1 73 ? 128.851 106.908 42.958 1.00 37.74 ? 73 PHE A CD2 1 ATOM 546 C CE1 . PHE A 1 73 ? 128.570 104.963 44.926 1.00 31.27 ? 73 PHE A CE1 1 ATOM 547 C CE2 . PHE A 1 73 ? 129.769 106.846 44.012 1.00 31.21 ? 73 PHE A CE2 1 ATOM 548 C CZ . PHE A 1 73 ? 129.625 105.874 44.999 1.00 29.98 ? 73 PHE A CZ 1 ATOM 549 N N . PRO A 1 74 ? 125.846 104.244 38.601 1.00 33.79 ? 74 PRO A N 1 ATOM 550 C CA . PRO A 1 74 ? 124.905 104.388 37.475 1.00 37.20 ? 74 PRO A CA 1 ATOM 551 C C . PRO A 1 74 ? 123.495 104.763 37.943 1.00 38.10 ? 74 PRO A C 1 ATOM 552 O O . PRO A 1 74 ? 123.033 104.219 38.944 1.00 33.58 ? 74 PRO A O 1 ATOM 553 C CB . PRO A 1 74 ? 124.864 102.982 36.854 1.00 35.19 ? 74 PRO A CB 1 ATOM 554 C CG . PRO A 1 74 ? 126.091 102.291 37.329 1.00 35.38 ? 74 PRO A CG 1 ATOM 555 C CD . PRO A 1 74 ? 126.457 102.904 38.661 1.00 34.04 ? 74 PRO A CD 1 ATOM 556 N N . GLY A 1 75 ? 122.834 105.678 37.238 1.00 33.11 ? 75 GLY A N 1 ATOM 557 C CA . GLY A 1 75 ? 121.486 106.095 37.597 1.00 43.95 ? 75 GLY A CA 1 ATOM 558 C C . GLY A 1 75 ? 121.390 107.146 38.695 1.00 40.02 ? 75 GLY A C 1 ATOM 559 O O . GLY A 1 75 ? 120.288 107.614 39.005 1.00 32.00 ? 75 GLY A O 1 ATOM 560 N N . PHE A 1 76 ? 122.536 107.520 39.271 1.00 32.91 ? 76 PHE A N 1 ATOM 561 C CA . PHE A 1 76 ? 122.587 108.460 40.403 1.00 34.96 ? 76 PHE A CA 1 ATOM 562 C C . PHE A 1 76 ? 123.022 109.865 39.969 1.00 30.04 ? 76 PHE A C 1 ATOM 563 O O . PHE A 1 76 ? 124.144 110.060 39.481 1.00 35.16 ? 76 PHE A O 1 ATOM 564 C CB . PHE A 1 76 ? 123.529 107.913 41.496 1.00 29.45 ? 76 PHE A CB 1 ATOM 565 C CG . PHE A 1 76 ? 123.698 108.828 42.700 1.00 28.48 ? 76 PHE A CG 1 ATOM 566 C CD1 . PHE A 1 76 ? 122.604 109.215 43.471 1.00 28.45 ? 76 PHE A CD1 1 ATOM 567 C CD2 . PHE A 1 76 ? 124.961 109.263 43.077 1.00 27.76 ? 76 PHE A CD2 1 ATOM 568 C CE1 . PHE A 1 76 ? 122.769 110.040 44.580 1.00 27.73 ? 76 PHE A CE1 1 ATOM 569 C CE2 . PHE A 1 76 ? 125.142 110.079 44.191 1.00 27.06 ? 76 PHE A CE2 1 ATOM 570 C CZ . PHE A 1 76 ? 124.049 110.467 44.941 1.00 27.05 ? 76 PHE A CZ 1 ATOM 571 N N . HIS A 1 77 ? 122.149 110.849 40.178 1.00 29.22 ? 77 HIS A N 1 ATOM 572 C CA . HIS A 1 77 ? 122.408 112.219 39.726 1.00 32.71 ? 77 HIS A CA 1 ATOM 573 C C . HIS A 1 77 ? 123.650 112.853 40.351 1.00 32.15 ? 77 HIS A C 1 ATOM 574 O O . HIS A 1 77 ? 124.268 113.742 39.757 1.00 29.13 ? 77 HIS A O 1 ATOM 575 C CB . HIS A 1 77 ? 121.193 113.119 39.985 1.00 28.08 ? 77 HIS A CB 1 ATOM 576 C CG . HIS A 1 77 ? 121.339 114.503 39.428 1.00 47.42 ? 77 HIS A CG 1 ATOM 577 N ND1 . HIS A 1 77 ? 121.422 114.755 38.074 1.00 41.61 ? 77 HIS A ND1 1 ATOM 578 C CD2 . HIS A 1 77 ? 121.428 115.708 40.040 1.00 48.35 ? 77 HIS A CD2 1 ATOM 579 C CE1 . HIS A 1 77 ? 121.552 116.054 37.876 1.00 37.44 ? 77 HIS A CE1 1 ATOM 580 N NE2 . HIS A 1 77 ? 121.561 116.656 39.053 1.00 44.88 ? 77 HIS A NE2 1 ATOM 581 N N . GLY A 1 78 ? 124.007 112.412 41.554 1.00 26.72 ? 78 GLY A N 1 ATOM 582 C CA . GLY A 1 78 ? 125.111 113.024 42.285 1.00 25.96 ? 78 GLY A CA 1 ATOM 583 C C . GLY A 1 78 ? 126.447 112.863 41.582 1.00 30.61 ? 78 GLY A C 1 ATOM 584 O O . GLY A 1 78 ? 127.307 113.761 41.626 1.00 26.50 ? 78 GLY A O 1 ATOM 585 N N . SER A 1 79 ? 126.630 111.718 40.933 1.00 26.37 ? 79 SER A N 1 ATOM 586 C CA . SER A 1 79 ? 127.851 111.467 40.172 1.00 32.40 ? 79 SER A CA 1 ATOM 587 C C . SER A 1 79 ? 127.640 111.774 38.690 1.00 34.39 ? 79 SER A C 1 ATOM 588 O O . SER A 1 79 ? 128.513 112.352 38.032 1.00 27.03 ? 79 SER A O 1 ATOM 589 C CB . SER A 1 79 ? 128.300 110.018 40.345 1.00 28.57 ? 79 SER A CB 1 ATOM 590 O OG . SER A 1 79 ? 127.256 109.111 40.007 1.00 33.65 ? 79 SER A OG 1 ATOM 591 N N . GLU A 1 80 ? 126.474 111.392 38.171 1.00 27.23 ? 80 GLU A N 1 ATOM 592 C CA . GLU A 1 80 ? 126.215 111.522 36.743 1.00 27.65 ? 80 GLU A CA 1 ATOM 593 C C . GLU A 1 80 ? 126.128 112.978 36.248 1.00 27.01 ? 80 GLU A C 1 ATOM 594 O O . GLU A 1 80 ? 126.407 113.247 35.086 1.00 29.34 ? 80 GLU A O 1 ATOM 595 C CB . GLU A 1 80 ? 125.004 110.663 36.308 1.00 28.78 ? 80 GLU A CB 1 ATOM 596 C CG . GLU A 1 80 ? 125.335 109.156 36.302 1.00 29.70 ? 80 GLU A CG 1 ATOM 597 C CD . GLU A 1 80 ? 124.213 108.257 35.745 1.00 38.51 ? 80 GLU A CD 1 ATOM 598 O OE1 . GLU A 1 80 ? 123.072 108.735 35.533 1.00 37.43 ? 80 GLU A OE1 1 ATOM 599 O OE2 . GLU A 1 80 ? 124.483 107.056 35.519 1.00 32.81 ? 80 GLU A OE2 1 ATOM 600 N N . MET A 1 81 ? 125.797 113.918 37.129 1.00 26.41 ? 81 MET A N 1 ATOM 601 C CA . MET A 1 81 ? 125.740 115.335 36.735 1.00 25.94 ? 81 MET A CA 1 ATOM 602 C C . MET A 1 81 ? 127.097 115.889 36.256 1.00 27.23 ? 81 MET A C 1 ATOM 603 O O . MET A 1 81 ? 127.143 116.933 35.587 1.00 30.06 ? 81 MET A O 1 ATOM 604 C CB . MET A 1 81 ? 125.220 116.194 37.894 1.00 25.58 ? 81 MET A CB 1 ATOM 605 C CG . MET A 1 81 ? 126.160 116.203 39.114 1.00 28.01 ? 81 MET A CG 1 ATOM 606 S SD . MET A 1 81 ? 125.498 117.149 40.510 1.00 37.04 ? 81 MET A SD 1 ATOM 607 C CE . MET A 1 81 ? 125.879 118.821 39.955 1.00 31.78 ? 81 MET A CE 1 ATOM 608 N N . TRP A 1 82 ? 128.190 115.217 36.624 1.00 25.20 ? 82 TRP A N 1 ATOM 609 C CA . TRP A 1 82 ? 129.551 115.653 36.255 1.00 27.27 ? 82 TRP A CA 1 ATOM 610 C C . TRP A 1 82 ? 130.063 114.982 34.966 1.00 29.39 ? 82 TRP A C 1 ATOM 611 O O . TRP A 1 82 ? 131.040 115.443 34.348 1.00 24.99 ? 82 TRP A O 1 ATOM 612 C CB . TRP A 1 82 ? 130.531 115.387 37.407 1.00 24.50 ? 82 TRP A CB 1 ATOM 613 C CG . TRP A 1 82 ? 130.118 116.062 38.693 1.00 24.75 ? 82 TRP A CG 1 ATOM 614 C CD1 . TRP A 1 82 ? 129.594 115.460 39.806 1.00 25.32 ? 82 TRP A CD1 1 ATOM 615 C CD2 . TRP A 1 82 ? 130.187 117.470 38.991 1.00 23.65 ? 82 TRP A CD2 1 ATOM 616 N NE1 . TRP A 1 82 ? 129.329 116.409 40.777 1.00 23.96 ? 82 TRP A NE1 1 ATOM 617 C CE2 . TRP A 1 82 ? 129.684 117.647 40.302 1.00 29.62 ? 82 TRP A CE2 1 ATOM 618 C CE3 . TRP A 1 82 ? 130.623 118.593 38.278 1.00 23.36 ? 82 TRP A CE3 1 ATOM 619 C CZ2 . TRP A 1 82 ? 129.607 118.909 40.916 1.00 26.51 ? 82 TRP A CZ2 1 ATOM 620 C CZ3 . TRP A 1 82 ? 130.540 119.852 38.889 1.00 23.11 ? 82 TRP A CZ3 1 ATOM 621 C CH2 . TRP A 1 82 ? 130.033 119.995 40.193 1.00 23.16 ? 82 TRP A CH2 1 ATOM 622 N N . ASN A 1 83 ? 129.412 113.887 34.574 1.00 26.06 ? 83 ASN A N 1 ATOM 623 C CA . ASN A 1 83 ? 129.741 113.205 33.326 1.00 26.76 ? 83 ASN A CA 1 ATOM 624 C C . ASN A 1 83 ? 129.394 114.060 32.098 1.00 30.74 ? 83 ASN A C 1 ATOM 625 O O . ASN A 1 83 ? 128.443 114.855 32.132 1.00 27.63 ? 83 ASN A O 1 ATOM 626 C CB . ASN A 1 83 ? 129.037 111.825 33.254 1.00 27.85 ? 83 ASN A CB 1 ATOM 627 C CG . ASN A 1 83 ? 129.688 110.791 34.173 1.00 34.92 ? 83 ASN A CG 1 ATOM 628 O OD1 . ASN A 1 83 ? 130.852 110.951 34.583 1.00 28.13 ? 83 ASN A OD1 1 ATOM 629 N ND2 . ASN A 1 83 ? 128.948 109.735 34.509 1.00 28.93 ? 83 ASN A ND2 1 ATOM 630 N N . PRO A 1 84 ? 130.153 113.888 31.003 1.00 31.16 ? 84 PRO A N 1 ATOM 631 C CA . PRO A 1 84 ? 129.925 114.666 29.775 1.00 29.13 ? 84 PRO A CA 1 ATOM 632 C C . PRO A 1 84 ? 128.476 114.553 29.264 1.00 27.90 ? 84 PRO A C 1 ATOM 633 O O . PRO A 1 84 ? 127.900 113.467 29.287 1.00 28.79 ? 84 PRO A O 1 ATOM 634 C CB . PRO A 1 84 ? 130.875 114.015 28.761 1.00 36.65 ? 84 PRO A CB 1 ATOM 635 C CG . PRO A 1 84 ? 131.905 113.281 29.585 1.00 35.58 ? 84 PRO A CG 1 ATOM 636 C CD . PRO A 1 84 ? 131.205 112.861 30.839 1.00 33.70 ? 84 PRO A CD 1 ATOM 637 N N . ASN A 1 85 ? 127.894 115.661 28.811 1.00 28.16 ? 85 ASN A N 1 ATOM 638 C CA . ASN A 1 85 ? 126.525 115.635 28.286 1.00 29.80 ? 85 ASN A CA 1 ATOM 639 C C . ASN A 1 85 ? 126.482 115.866 26.782 1.00 29.25 ? 85 ASN A C 1 ATOM 640 O O . ASN A 1 85 ? 125.466 116.287 26.227 1.00 32.02 ? 85 ASN A O 1 ATOM 641 C CB . ASN A 1 85 ? 125.633 116.655 29.008 1.00 28.21 ? 85 ASN A CB 1 ATOM 642 C CG . ASN A 1 85 ? 126.168 118.077 28.919 1.00 30.18 ? 85 ASN A CG 1 ATOM 643 O OD1 . ASN A 1 85 ? 127.369 118.305 28.694 1.00 26.77 ? 85 ASN A OD1 1 ATOM 644 N ND2 . ASN A 1 85 ? 125.278 119.048 29.115 1.00 28.00 ? 85 ASN A ND2 1 ATOM 645 N N . THR A 1 86 ? 127.582 115.552 26.119 1.00 45.76 ? 86 THR A N 1 ATOM 646 C CA . THR A 1 86 ? 127.716 115.826 24.704 1.00 29.79 ? 86 THR A CA 1 ATOM 647 C C . THR A 1 86 ? 128.674 114.751 24.152 1.00 34.22 ? 86 THR A C 1 ATOM 648 O O . THR A 1 86 ? 129.528 114.273 24.910 1.00 29.88 ? 86 THR A O 1 ATOM 649 C CB . THR A 1 86 ? 128.295 117.249 24.575 1.00 48.93 ? 86 THR A CB 1 ATOM 650 O OG1 . THR A 1 86 ? 127.384 118.113 23.879 1.00 41.08 ? 86 THR A OG1 1 ATOM 651 C CG2 . THR A 1 86 ? 129.582 117.215 23.891 1.00 28.56 ? 86 THR A CG2 1 ATOM 652 N N . ASP A 1 87 ? 128.541 114.355 22.878 1.00 31.47 ? 87 ASP A N 1 ATOM 653 C CA . ASP A 1 87 ? 129.451 113.355 22.271 1.00 35.19 ? 87 ASP A CA 1 ATOM 654 C C . ASP A 1 87 ? 130.925 113.618 22.583 1.00 31.24 ? 87 ASP A C 1 ATOM 655 O O . ASP A 1 87 ? 131.362 114.772 22.612 1.00 30.18 ? 87 ASP A O 1 ATOM 656 C CB . ASP A 1 87 ? 129.335 113.299 20.737 1.00 38.51 ? 87 ASP A CB 1 ATOM 657 C CG . ASP A 1 87 ? 127.990 112.811 20.252 1.00 42.53 ? 87 ASP A CG 1 ATOM 658 O OD1 . ASP A 1 87 ? 127.817 111.586 20.059 1.00 42.06 ? 87 ASP A OD1 1 ATOM 659 O OD2 . ASP A 1 87 ? 127.113 113.663 20.018 1.00 53.44 ? 87 ASP A OD2 1 ATOM 660 N N . LEU A 1 88 ? 131.675 112.539 22.815 1.00 31.76 ? 88 LEU A N 1 ATOM 661 C CA . LEU A 1 88 ? 133.122 112.604 23.013 1.00 39.71 ? 88 LEU A CA 1 ATOM 662 C C . LEU A 1 88 ? 133.821 112.551 21.660 1.00 43.65 ? 88 LEU A C 1 ATOM 663 O O . LEU A 1 88 ? 133.408 111.799 20.784 1.00 33.28 ? 88 LEU A O 1 ATOM 664 C CB . LEU A 1 88 ? 133.590 111.412 23.851 1.00 39.57 ? 88 LEU A CB 1 ATOM 665 C CG . LEU A 1 88 ? 132.995 111.287 25.252 1.00 36.97 ? 88 LEU A CG 1 ATOM 666 C CD1 . LEU A 1 88 ? 133.711 110.203 26.050 1.00 34.22 ? 88 LEU A CD1 1 ATOM 667 C CD2 . LEU A 1 88 ? 133.069 112.630 25.967 1.00 33.04 ? 88 LEU A CD2 1 ATOM 668 N N . SER A 1 89 ? 134.889 113.323 21.488 1.00 40.62 ? 89 SER A N 1 ATOM 669 C CA . SER A 1 89 ? 135.612 113.314 20.215 1.00 37.39 ? 89 SER A CA 1 ATOM 670 C C . SER A 1 89 ? 136.954 114.001 20.382 1.00 38.85 ? 89 SER A C 1 ATOM 671 O O . SER A 1 89 ? 137.088 114.870 21.238 1.00 29.69 ? 89 SER A O 1 ATOM 672 C CB . SER A 1 89 ? 134.792 114.045 19.147 1.00 33.24 ? 89 SER A CB 1 ATOM 673 O OG . SER A 1 89 ? 135.539 114.210 17.959 1.00 36.81 ? 89 SER A OG 1 ATOM 674 N N . GLU A 1 90 ? 137.953 113.640 19.578 1.00 34.20 ? 90 GLU A N 1 ATOM 675 C CA . GLU A 1 90 ? 139.205 114.404 19.627 1.00 36.51 ? 90 GLU A CA 1 ATOM 676 C C . GLU A 1 90 ? 138.973 115.788 19.022 1.00 31.77 ? 90 GLU A C 1 ATOM 677 O O . GLU A 1 90 ? 139.730 116.731 19.270 1.00 29.14 ? 90 GLU A O 1 ATOM 678 C CB . GLU A 1 90 ? 140.345 113.695 18.888 1.00 36.13 ? 90 GLU A CB 1 ATOM 679 C CG . GLU A 1 90 ? 140.746 112.342 19.449 1.00 34.92 ? 90 GLU A CG 1 ATOM 680 C CD . GLU A 1 90 ? 141.965 111.776 18.742 1.00 37.46 ? 90 GLU A CD 1 ATOM 681 O OE1 . GLU A 1 90 ? 143.093 112.237 19.032 1.00 35.38 ? 90 GLU A OE1 1 ATOM 682 O OE2 . GLU A 1 90 ? 141.794 110.876 17.891 1.00 36.82 ? 90 GLU A OE2 1 ATOM 683 N N . ASP A 1 91 ? 137.923 115.890 18.212 1.00 32.65 ? 91 ASP A N 1 ATOM 684 C CA . ASP A 1 91 ? 137.545 117.148 17.595 1.00 31.93 ? 91 ASP A CA 1 ATOM 685 C C . ASP A 1 91 ? 136.722 117.906 18.629 1.00 29.57 ? 91 ASP A C 1 ATOM 686 O O . ASP A 1 91 ? 135.492 117.894 18.577 1.00 33.41 ? 91 ASP A O 1 ATOM 687 C CB . ASP A 1 91 ? 136.724 116.870 16.324 1.00 36.06 ? 91 ASP A CB 1 ATOM 688 C CG . ASP A 1 91 ? 136.281 118.143 15.611 1.00 38.59 ? 91 ASP A CG 1 ATOM 689 O OD1 . ASP A 1 91 ? 136.639 119.267 16.046 1.00 33.25 ? 91 ASP A OD1 1 ATOM 690 O OD2 . ASP A 1 91 ? 135.565 118.010 14.600 1.00 38.78 ? 91 ASP A OD2 1 ATOM 691 N N . CYS A 1 92 ? 137.397 118.553 19.579 1.00 27.99 ? 92 CYS A N 1 ATOM 692 C CA . CYS A 1 92 ? 136.696 119.144 20.712 1.00 29.02 ? 92 CYS A CA 1 ATOM 693 C C . CYS A 1 92 ? 137.170 120.548 21.098 1.00 33.04 ? 92 CYS A C 1 ATOM 694 O O . CYS A 1 92 ? 136.799 121.056 22.164 1.00 27.24 ? 92 CYS A O 1 ATOM 695 C CB . CYS A 1 92 ? 136.825 118.221 21.928 1.00 26.55 ? 92 CYS A CB 1 ATOM 696 S SG . CYS A 1 92 ? 138.538 118.049 22.541 1.00 27.65 ? 92 CYS A SG 1 ATOM 697 N N . LEU A 1 93 ? 137.981 121.179 20.253 1.00 25.15 ? 93 LEU A N 1 ATOM 698 C CA . LEU A 1 93 ? 138.526 122.497 20.610 1.00 26.80 ? 93 LEU A CA 1 ATOM 699 C C . LEU A 1 93 ? 137.537 123.609 20.220 1.00 27.61 ? 93 LEU A C 1 ATOM 700 O O . LEU A 1 93 ? 137.604 124.178 19.124 1.00 30.47 ? 93 LEU A O 1 ATOM 701 C CB . LEU A 1 93 ? 139.931 122.700 20.015 1.00 25.12 ? 93 LEU A CB 1 ATOM 702 C CG . LEU A 1 93 ? 141.003 121.737 20.550 1.00 34.09 ? 93 LEU A CG 1 ATOM 703 C CD1 . LEU A 1 93 ? 142.433 122.091 20.085 1.00 25.81 ? 93 LEU A CD1 1 ATOM 704 C CD2 . LEU A 1 93 ? 140.946 121.649 22.081 1.00 29.60 ? 93 LEU A CD2 1 ATOM 705 N N . TYR A 1 94 ? 136.591 123.874 21.120 1.00 27.09 ? 94 TYR A N 1 ATOM 706 C CA . TYR A 1 94 ? 135.495 124.803 20.862 1.00 25.04 ? 94 TYR A CA 1 ATOM 707 C C . TYR A 1 94 ? 135.243 125.604 22.126 1.00 27.10 ? 94 TYR A C 1 ATOM 708 O O . TYR A 1 94 ? 135.629 125.171 23.220 1.00 26.40 ? 94 TYR A O 1 ATOM 709 C CB . TYR A 1 94 ? 134.219 124.052 20.439 1.00 24.51 ? 94 TYR A CB 1 ATOM 710 C CG . TYR A 1 94 ? 134.373 123.262 19.144 1.00 34.53 ? 94 TYR A CG 1 ATOM 711 C CD1 . TYR A 1 94 ? 134.828 121.946 19.155 1.00 26.34 ? 94 TYR A CD1 1 ATOM 712 C CD2 . TYR A 1 94 ? 134.056 123.832 17.911 1.00 27.45 ? 94 TYR A CD2 1 ATOM 713 C CE1 . TYR A 1 94 ? 134.981 121.221 17.971 1.00 27.95 ? 94 TYR A CE1 1 ATOM 714 C CE2 . TYR A 1 94 ? 134.210 123.106 16.720 1.00 29.06 ? 94 TYR A CE2 1 ATOM 715 C CZ . TYR A 1 94 ? 134.678 121.808 16.764 1.00 29.30 ? 94 TYR A CZ 1 ATOM 716 O OH . TYR A 1 94 ? 134.838 121.085 15.588 1.00 32.93 ? 94 TYR A OH 1 ATOM 717 N N . LEU A 1 95 ? 134.635 126.780 21.966 1.00 22.60 ? 95 LEU A N 1 ATOM 718 C CA . LEU A 1 95 ? 134.283 127.636 23.095 1.00 24.94 ? 95 LEU A CA 1 ATOM 719 C C . LEU A 1 95 ? 132.854 128.186 22.945 1.00 28.31 ? 95 LEU A C 1 ATOM 720 O O . LEU A 1 95 ? 132.244 128.097 21.860 1.00 24.55 ? 95 LEU A O 1 ATOM 721 C CB . LEU A 1 95 ? 135.305 128.771 23.273 1.00 25.13 ? 95 LEU A CB 1 ATOM 722 C CG . LEU A 1 95 ? 135.595 129.733 22.112 1.00 30.47 ? 95 LEU A CG 1 ATOM 723 C CD1 . LEU A 1 95 ? 134.481 130.779 21.902 1.00 26.67 ? 95 LEU A CD1 1 ATOM 724 C CD2 . LEU A 1 95 ? 136.936 130.430 22.320 1.00 28.70 ? 95 LEU A CD2 1 ATOM 725 N N . ASN A 1 96 ? 132.337 128.744 24.039 1.00 21.49 ? 96 ASN A N 1 ATOM 726 C CA . ASN A 1 96 ? 130.968 129.258 24.116 1.00 24.69 ? 96 ASN A CA 1 ATOM 727 C C . ASN A 1 96 ? 130.976 130.706 24.586 1.00 27.51 ? 96 ASN A C 1 ATOM 728 O O . ASN A 1 96 ? 131.835 131.096 25.382 1.00 21.76 ? 96 ASN A O 1 ATOM 729 C CB . ASN A 1 96 ? 130.155 128.449 25.130 1.00 23.89 ? 96 ASN A CB 1 ATOM 730 C CG . ASN A 1 96 ? 130.218 126.958 24.877 1.00 29.22 ? 96 ASN A CG 1 ATOM 731 O OD1 . ASN A 1 96 ? 129.918 126.483 23.779 1.00 30.58 ? 96 ASN A OD1 1 ATOM 732 N ND2 . ASN A 1 96 ? 130.616 126.211 25.895 1.00 24.75 ? 96 ASN A ND2 1 ATOM 733 N N . VAL A 1 97 ? 130.012 131.497 24.120 1.00 24.66 ? 97 VAL A N 1 ATOM 734 C CA . VAL A 1 97 ? 129.921 132.904 24.522 1.00 29.54 ? 97 VAL A CA 1 ATOM 735 C C . VAL A 1 97 ? 128.465 133.281 24.842 1.00 31.28 ? 97 VAL A C 1 ATOM 736 O O . VAL A 1 97 ? 127.556 133.049 24.023 1.00 28.13 ? 97 VAL A O 1 ATOM 737 C CB . VAL A 1 97 ? 130.445 133.863 23.420 1.00 28.46 ? 97 VAL A CB 1 ATOM 738 C CG1 . VAL A 1 97 ? 130.520 135.288 23.951 1.00 26.42 ? 97 VAL A CG1 1 ATOM 739 C CG2 . VAL A 1 97 ? 131.817 133.432 22.912 1.00 28.49 ? 97 VAL A CG2 1 ATOM 740 N N . TRP A 1 98 ? 128.237 133.838 26.031 1.00 24.74 ? 98 TRP A N 1 ATOM 741 C CA . TRP A 1 98 ? 126.915 134.368 26.376 1.00 24.38 ? 98 TRP A CA 1 ATOM 742 C C . TRP A 1 98 ? 127.022 135.874 26.506 1.00 34.53 ? 98 TRP A C 1 ATOM 743 O O . TRP A 1 98 ? 127.950 136.393 27.145 1.00 32.31 ? 98 TRP A O 1 ATOM 744 C CB . TRP A 1 98 ? 126.396 133.801 27.694 1.00 23.75 ? 98 TRP A CB 1 ATOM 745 C CG . TRP A 1 98 ? 125.989 132.347 27.659 1.00 31.13 ? 98 TRP A CG 1 ATOM 746 C CD1 . TRP A 1 98 ? 124.747 131.847 27.384 1.00 30.67 ? 98 TRP A CD1 1 ATOM 747 C CD2 . TRP A 1 98 ? 126.823 131.219 27.947 1.00 27.06 ? 98 TRP A CD2 1 ATOM 748 N NE1 . TRP A 1 98 ? 124.761 130.474 27.475 1.00 32.98 ? 98 TRP A NE1 1 ATOM 749 C CE2 . TRP A 1 98 ? 126.025 130.063 27.817 1.00 31.50 ? 98 TRP A CE2 1 ATOM 750 C CE3 . TRP A 1 98 ? 128.173 131.073 28.284 1.00 21.23 ? 98 TRP A CE3 1 ATOM 751 C CZ2 . TRP A 1 98 ? 126.533 128.770 28.022 1.00 22.18 ? 98 TRP A CZ2 1 ATOM 752 C CZ3 . TRP A 1 98 ? 128.679 129.790 28.493 1.00 21.96 ? 98 TRP A CZ3 1 ATOM 753 C CH2 . TRP A 1 98 ? 127.856 128.655 28.357 1.00 25.40 ? 98 TRP A CH2 1 ATOM 754 N N . ILE A 1 99 ? 126.053 136.566 25.923 1.00 28.87 ? 99 ILE A N 1 ATOM 755 C CA . ILE A 1 99 ? 126.070 138.017 25.837 1.00 34.30 ? 99 ILE A CA 1 ATOM 756 C C . ILE A 1 99 ? 124.705 138.592 26.200 1.00 34.78 ? 99 ILE A C 1 ATOM 757 O O . ILE A 1 99 ? 123.668 138.026 25.829 1.00 38.06 ? 99 ILE A O 1 ATOM 758 C CB . ILE A 1 99 ? 126.489 138.432 24.415 1.00 42.52 ? 99 ILE A CB 1 ATOM 759 C CG1 . ILE A 1 99 ? 128.005 138.497 24.344 1.00 45.42 ? 99 ILE A CG1 1 ATOM 760 C CG2 . ILE A 1 99 ? 125.898 139.747 23.995 1.00 48.31 ? 99 ILE A CG2 1 ATOM 761 C CD1 . ILE A 1 99 ? 128.514 137.978 23.074 1.00 52.62 ? 99 ILE A CD1 1 ATOM 762 N N . PRO A 1 100 ? 124.700 139.699 26.959 1.00 36.40 ? 100 PRO A N 1 ATOM 763 C CA . PRO A 1 100 ? 123.452 140.376 27.330 1.00 39.12 ? 100 PRO A CA 1 ATOM 764 C C . PRO A 1 100 ? 122.744 140.904 26.096 1.00 39.44 ? 100 PRO A C 1 ATOM 765 O O . PRO A 1 100 ? 123.418 141.236 25.118 1.00 37.90 ? 100 PRO A O 1 ATOM 766 C CB . PRO A 1 100 ? 123.926 141.561 28.187 1.00 36.81 ? 100 PRO A CB 1 ATOM 767 C CG . PRO A 1 100 ? 125.320 141.184 28.644 1.00 38.30 ? 100 PRO A CG 1 ATOM 768 C CD . PRO A 1 100 ? 125.892 140.350 27.538 1.00 32.32 ? 100 PRO A CD 1 ATOM 769 N N . ALA A 1 101 ? 121.411 140.951 26.138 1.00 40.29 ? 101 ALA A N 1 ATOM 770 C CA . ALA A 1 101 ? 120.620 141.681 25.158 1.00 44.32 ? 101 ALA A CA 1 ATOM 771 C C . ALA A 1 101 ? 119.904 142.796 25.911 1.00 49.21 ? 101 ALA A C 1 ATOM 772 O O . ALA A 1 101 ? 119.321 142.558 26.969 1.00 50.46 ? 101 ALA A O 1 ATOM 773 C CB . ALA A 1 101 ? 119.617 140.773 24.465 1.00 43.73 ? 101 ALA A CB 1 ATOM 774 N N . PRO A 1 102 ? 119.964 144.028 25.390 1.00 49.22 ? 102 PRO A N 1 ATOM 775 C CA . PRO A 1 102 ? 120.639 144.445 24.156 1.00 49.64 ? 102 PRO A CA 1 ATOM 776 C C . PRO A 1 102 ? 122.157 144.334 24.288 1.00 47.93 ? 102 PRO A C 1 ATOM 777 O O . PRO A 1 102 ? 122.682 144.394 25.405 1.00 41.84 ? 102 PRO A O 1 ATOM 778 C CB . PRO A 1 102 ? 120.238 145.923 24.016 1.00 54.70 ? 102 PRO A CB 1 ATOM 779 C CG . PRO A 1 102 ? 119.121 146.142 25.019 1.00 55.14 ? 102 PRO A CG 1 ATOM 780 C CD . PRO A 1 102 ? 119.397 145.175 26.117 1.00 53.31 ? 102 PRO A CD 1 ATOM 781 N N . LYS A 1 103 ? 122.823 144.127 23.154 1.00 44.58 ? 103 LYS A N 1 ATOM 782 C CA . LYS A 1 103 ? 124.271 144.029 23.062 1.00 43.90 ? 103 LYS A CA 1 ATOM 783 C C . LYS A 1 103 ? 124.930 145.135 23.878 1.00 43.03 ? 103 LYS A C 1 ATOM 784 O O . LYS A 1 103 ? 124.597 146.300 23.719 1.00 39.68 ? 103 LYS A O 1 ATOM 785 C CB . LYS A 1 103 ? 124.668 144.150 21.590 1.00 49.46 ? 103 LYS A CB 1 ATOM 786 C CG . LYS A 1 103 ? 126.139 143.932 21.262 1.00 49.32 ? 103 LYS A CG 1 ATOM 787 C CD . LYS A 1 103 ? 126.427 144.520 19.871 1.00 56.34 ? 103 LYS A CD 1 ATOM 788 C CE . LYS A 1 103 ? 127.869 144.308 19.424 1.00 58.74 ? 103 LYS A CE 1 ATOM 789 N NZ . LYS A 1 103 ? 128.029 143.051 18.646 1.00 55.97 ? 103 LYS A NZ 1 ATOM 790 N N . PRO A 1 104 ? 125.854 144.764 24.777 1.00 39.96 ? 104 PRO A N 1 ATOM 791 C CA . PRO A 1 104 ? 126.513 145.751 25.639 1.00 37.65 ? 104 PRO A CA 1 ATOM 792 C C . PRO A 1 104 ? 127.547 146.527 24.833 1.00 46.03 ? 104 PRO A C 1 ATOM 793 O O . PRO A 1 104 ? 127.804 146.157 23.686 1.00 45.08 ? 104 PRO A O 1 ATOM 794 C CB . PRO A 1 104 ? 127.201 144.886 26.697 1.00 32.92 ? 104 PRO A CB 1 ATOM 795 C CG . PRO A 1 104 ? 127.503 143.603 25.994 1.00 36.10 ? 104 PRO A CG 1 ATOM 796 C CD . PRO A 1 104 ? 126.407 143.409 24.949 1.00 32.35 ? 104 PRO A CD 1 ATOM 797 N N . LYS A 1 105 ? 128.124 147.581 25.404 1.00 44.44 ? 105 LYS A N 1 ATOM 798 C CA . LYS A 1 105 ? 129.100 148.370 24.660 1.00 46.83 ? 105 LYS A CA 1 ATOM 799 C C . LYS A 1 105 ? 130.558 148.036 24.993 1.00 52.16 ? 105 LYS A C 1 ATOM 800 O O . LYS A 1 105 ? 131.400 147.974 24.095 1.00 61.69 ? 105 LYS A O 1 ATOM 801 C CB . LYS A 1 105 ? 128.816 149.869 24.799 1.00 42.71 ? 105 LYS A CB 1 ATOM 802 C CG . LYS A 1 105 ? 127.474 150.266 24.184 1.00 44.18 ? 105 LYS A CG 1 ATOM 803 C CD . LYS A 1 105 ? 127.449 151.698 23.695 1.00 48.69 ? 105 LYS A CD 1 ATOM 804 C CE . LYS A 1 105 ? 126.265 151.918 22.750 1.00 57.01 ? 105 LYS A CE 1 ATOM 805 N NZ . LYS A 1 105 ? 124.984 151.432 23.347 1.00 57.19 ? 105 LYS A NZ 1 ATOM 806 N N . ASN A 1 106 ? 130.853 147.806 26.269 1.00 42.27 ? 106 ASN A N 1 ATOM 807 C CA . ASN A 1 106 ? 132.226 147.523 26.685 1.00 40.95 ? 106 ASN A CA 1 ATOM 808 C C . ASN A 1 106 ? 132.204 146.667 27.950 1.00 32.32 ? 106 ASN A C 1 ATOM 809 O O . ASN A 1 106 ? 132.797 147.026 28.961 1.00 32.45 ? 106 ASN A O 1 ATOM 810 C CB . ASN A 1 106 ? 132.978 148.840 26.935 1.00 45.54 ? 106 ASN A CB 1 ATOM 811 C CG . ASN A 1 106 ? 134.477 148.737 26.659 1.00 59.61 ? 106 ASN A CG 1 ATOM 812 O OD1 . ASN A 1 106 ? 134.920 147.936 25.826 1.00 52.35 ? 106 ASN A OD1 1 ATOM 813 N ND2 . ASN A 1 106 ? 135.269 149.545 27.387 1.00 75.47 ? 106 ASN A ND2 1 ATOM 814 N N . ALA A 1 107 ? 131.501 145.537 27.884 1.00 29.64 ? 107 ALA A N 1 ATOM 815 C CA . ALA A 1 107 ? 131.245 144.701 29.054 1.00 28.18 ? 107 ALA A CA 1 ATOM 816 C C . ALA A 1 107 ? 132.477 143.935 29.541 1.00 31.45 ? 107 ALA A C 1 ATOM 817 O O . ALA A 1 107 ? 133.252 143.401 28.742 1.00 30.11 ? 107 ALA A O 1 ATOM 818 C CB . ALA A 1 107 ? 130.111 143.715 28.754 1.00 27.87 ? 107 ALA A CB 1 ATOM 819 N N . THR A 1 108 ? 132.629 143.866 30.860 1.00 28.13 ? 108 THR A N 1 ATOM 820 C CA . THR A 1 108 ? 133.617 143.000 31.502 1.00 25.21 ? 108 THR A CA 1 ATOM 821 C C . THR A 1 108 ? 133.362 141.539 31.124 1.00 27.19 ? 108 THR A C 1 ATOM 822 O O . THR A 1 108 ? 132.199 141.124 30.980 1.00 26.34 ? 108 THR A O 1 ATOM 823 C CB . THR A 1 108 ? 133.550 143.182 33.029 1.00 23.95 ? 108 THR A CB 1 ATOM 824 O OG1 . THR A 1 108 ? 134.152 144.436 33.372 1.00 29.78 ? 108 THR A OG1 1 ATOM 825 C CG2 . THR A 1 108 ? 134.275 142.049 33.770 1.00 24.70 ? 108 THR A CG2 1 ATOM 826 N N . VAL A 1 109 ? 134.436 140.764 30.955 1.00 26.32 ? 109 VAL A N 1 ATOM 827 C CA . VAL A 1 109 ? 134.320 139.381 30.498 1.00 25.83 ? 109 VAL A CA 1 ATOM 828 C C . VAL A 1 109 ? 134.771 138.378 31.559 1.00 29.24 ? 109 VAL A C 1 ATOM 829 O O . VAL A 1 109 ? 135.837 138.533 32.165 1.00 27.45 ? 109 VAL A O 1 ATOM 830 C CB . VAL A 1 109 ? 135.154 139.144 29.220 1.00 27.20 ? 109 VAL A CB 1 ATOM 831 C CG1 . VAL A 1 109 ? 134.963 137.712 28.713 1.00 24.98 ? 109 VAL A CG1 1 ATOM 832 C CG2 . VAL A 1 109 ? 134.755 140.147 28.143 1.00 29.68 ? 109 VAL A CG2 1 ATOM 833 N N A LEU A 1 110 ? 133.949 137.357 31.782 0.60 24.65 ? 110 LEU A N 1 ATOM 834 N N B LEU A 1 110 ? 133.956 137.351 31.777 0.40 25.24 ? 110 LEU A N 1 ATOM 835 C CA A LEU A 1 110 ? 134.289 136.275 32.702 0.60 25.38 ? 110 LEU A CA 1 ATOM 836 C CA B LEU A 1 110 ? 134.304 136.280 32.704 0.40 25.23 ? 110 LEU A CA 1 ATOM 837 C C A LEU A 1 110 ? 134.579 134.995 31.914 0.60 25.79 ? 110 LEU A C 1 ATOM 838 C C B LEU A 1 110 ? 134.582 135.000 31.917 0.40 25.64 ? 110 LEU A C 1 ATOM 839 O O A LEU A 1 110 ? 133.731 134.518 31.152 0.60 24.93 ? 110 LEU A O 1 ATOM 840 O O B LEU A 1 110 ? 133.729 134.529 31.160 0.40 25.13 ? 110 LEU A O 1 ATOM 841 C CB A LEU A 1 110 ? 133.142 136.044 33.692 0.60 23.97 ? 110 LEU A CB 1 ATOM 842 C CB B LEU A 1 110 ? 133.174 136.050 33.716 0.40 25.09 ? 110 LEU A CB 1 ATOM 843 C CG A LEU A 1 110 ? 133.228 136.809 35.013 0.60 27.29 ? 110 LEU A CG 1 ATOM 844 C CG B LEU A 1 110 ? 133.137 136.923 34.975 0.40 28.16 ? 110 LEU A CG 1 ATOM 845 C CD1 A LEU A 1 110 ? 131.866 136.897 35.684 0.60 28.50 ? 110 LEU A CD1 1 ATOM 846 C CD1 B LEU A 1 110 ? 133.078 138.401 34.635 0.40 25.59 ? 110 LEU A CD1 1 ATOM 847 C CD2 A LEU A 1 110 ? 134.233 136.132 35.939 0.60 17.69 ? 110 LEU A CD2 1 ATOM 848 C CD2 B LEU A 1 110 ? 131.959 136.542 35.857 0.40 28.71 ? 110 LEU A CD2 1 ATOM 849 N N . ILE A 1 111 ? 135.779 134.443 32.086 1.00 25.93 ? 111 ILE A N 1 ATOM 850 C CA . ILE A 1 111 ? 136.155 133.217 31.378 1.00 24.10 ? 111 ILE A CA 1 ATOM 851 C C . ILE A 1 111 ? 136.273 132.010 32.315 1.00 22.84 ? 111 ILE A C 1 ATOM 852 O O . ILE A 1 111 ? 137.173 131.977 33.166 1.00 19.16 ? 111 ILE A O 1 ATOM 853 C CB . ILE A 1 111 ? 137.478 133.390 30.615 1.00 24.05 ? 111 ILE A CB 1 ATOM 854 C CG1 . ILE A 1 111 ? 137.393 134.568 29.634 1.00 21.15 ? 111 ILE A CG1 1 ATOM 855 C CG2 . ILE A 1 111 ? 137.840 132.088 29.885 1.00 23.73 ? 111 ILE A CG2 1 ATOM 856 C CD1 . ILE A 1 111 ? 138.682 134.776 28.832 1.00 23.53 ? 111 ILE A CD1 1 ATOM 857 N N . TRP A 1 112 ? 135.375 131.032 32.145 1.00 16.79 ? 112 TRP A N 1 ATOM 858 C CA . TRP A 1 112 ? 135.312 129.833 32.998 1.00 19.70 ? 112 TRP A CA 1 ATOM 859 C C . TRP A 1 112 ? 136.220 128.697 32.520 1.00 22.30 ? 112 TRP A C 1 ATOM 860 O O . TRP A 1 112 ? 136.217 128.347 31.331 1.00 19.13 ? 112 TRP A O 1 ATOM 861 C CB . TRP A 1 112 ? 133.875 129.290 33.061 1.00 17.78 ? 112 TRP A CB 1 ATOM 862 C CG . TRP A 1 112 ? 133.721 128.015 33.897 1.00 18.64 ? 112 TRP A CG 1 ATOM 863 C CD1 . TRP A 1 112 ? 133.492 126.740 33.445 1.00 21.33 ? 112 TRP A CD1 1 ATOM 864 C CD2 . TRP A 1 112 ? 133.806 127.923 35.328 1.00 16.41 ? 112 TRP A CD2 1 ATOM 865 N NE1 . TRP A 1 112 ? 133.413 125.859 34.516 1.00 20.38 ? 112 TRP A NE1 1 ATOM 866 C CE2 . TRP A 1 112 ? 133.603 126.566 35.679 1.00 21.95 ? 112 TRP A CE2 1 ATOM 867 C CE3 . TRP A 1 112 ? 134.005 128.864 36.347 1.00 23.19 ? 112 TRP A CE3 1 ATOM 868 C CZ2 . TRP A 1 112 ? 133.612 126.132 37.009 1.00 17.53 ? 112 TRP A CZ2 1 ATOM 869 C CZ3 . TRP A 1 112 ? 134.011 128.433 37.667 1.00 19.69 ? 112 TRP A CZ3 1 ATOM 870 C CH2 . TRP A 1 112 ? 133.815 127.079 37.987 1.00 16.47 ? 112 TRP A CH2 1 ATOM 871 N N . ILE A 1 113 ? 136.968 128.105 33.449 1.00 17.33 ? 113 ILE A N 1 ATOM 872 C CA . ILE A 1 113 ? 137.775 126.918 33.159 1.00 20.68 ? 113 ILE A CA 1 ATOM 873 C C . ILE A 1 113 ? 137.357 125.788 34.099 1.00 21.90 ? 113 ILE A C 1 ATOM 874 O O . ILE A 1 113 ? 137.616 125.868 35.304 1.00 18.71 ? 113 ILE A O 1 ATOM 875 C CB . ILE A 1 113 ? 139.293 127.201 33.371 1.00 24.71 ? 113 ILE A CB 1 ATOM 876 C CG1 . ILE A 1 113 ? 139.750 128.430 32.568 1.00 15.02 ? 113 ILE A CG1 1 ATOM 877 C CG2 . ILE A 1 113 ? 140.125 125.956 33.010 1.00 18.09 ? 113 ILE A CG2 1 ATOM 878 C CD1 . ILE A 1 113 ? 141.274 128.788 32.749 1.00 19.44 ? 113 ILE A CD1 1 ATOM 879 N N . TYR A 1 114 ? 136.719 124.741 33.563 1.00 19.44 ? 114 TYR A N 1 ATOM 880 C CA . TYR A 1 114 ? 136.199 123.642 34.398 1.00 15.40 ? 114 TYR A CA 1 ATOM 881 C C . TYR A 1 114 ? 137.295 122.786 35.039 1.00 17.94 ? 114 TYR A C 1 ATOM 882 O O . TYR A 1 114 ? 138.449 122.732 34.550 1.00 18.96 ? 114 TYR A O 1 ATOM 883 C CB . TYR A 1 114 ? 135.239 122.738 33.594 1.00 15.84 ? 114 TYR A CB 1 ATOM 884 C CG . TYR A 1 114 ? 135.850 122.133 32.331 1.00 16.67 ? 114 TYR A CG 1 ATOM 885 C CD1 . TYR A 1 114 ? 136.726 121.042 32.395 1.00 22.38 ? 114 TYR A CD1 1 ATOM 886 C CD2 . TYR A 1 114 ? 135.518 122.633 31.073 1.00 19.06 ? 114 TYR A CD2 1 ATOM 887 C CE1 . TYR A 1 114 ? 137.272 120.482 31.228 1.00 18.30 ? 114 TYR A CE1 1 ATOM 888 C CE2 . TYR A 1 114 ? 136.059 122.096 29.917 1.00 20.34 ? 114 TYR A CE2 1 ATOM 889 C CZ . TYR A 1 114 ? 136.927 121.019 29.997 1.00 23.42 ? 114 TYR A CZ 1 ATOM 890 O OH . TYR A 1 114 ? 137.457 120.499 28.832 1.00 22.13 ? 114 TYR A OH 1 ATOM 891 N N . GLY A 1 115 ? 136.939 122.121 36.135 1.00 18.67 ? 115 GLY A N 1 ATOM 892 C CA . GLY A 1 115 ? 137.840 121.179 36.770 1.00 18.39 ? 115 GLY A CA 1 ATOM 893 C C . GLY A 1 115 ? 137.499 119.733 36.402 1.00 21.83 ? 115 GLY A C 1 ATOM 894 O O . GLY A 1 115 ? 136.698 119.486 35.501 1.00 20.07 ? 115 GLY A O 1 ATOM 895 N N . GLY A 1 116 ? 138.088 118.772 37.110 1.00 25.98 ? 116 GLY A N 1 ATOM 896 C CA . GLY A 1 116 ? 137.926 117.366 36.762 1.00 24.30 ? 116 GLY A CA 1 ATOM 897 C C . GLY A 1 116 ? 139.264 116.636 36.808 1.00 26.74 ? 116 GLY A C 1 ATOM 898 O O . GLY A 1 116 ? 139.495 115.663 36.079 1.00 21.78 ? 116 GLY A O 1 ATOM 899 N N . GLY A 1 117 ? 140.164 117.115 37.659 1.00 26.11 ? 117 GLY A N 1 ATOM 900 C CA . GLY A 1 117 ? 141.432 116.434 37.877 1.00 27.29 ? 117 GLY A CA 1 ATOM 901 C C . GLY A 1 117 ? 142.340 116.389 36.661 1.00 24.31 ? 117 GLY A C 1 ATOM 902 O O . GLY A 1 117 ? 143.254 115.564 36.617 1.00 26.62 ? 117 GLY A O 1 ATOM 903 N N . PHE A 1 118 ? 142.107 117.280 35.690 1.00 20.32 ? 118 PHE A N 1 ATOM 904 C CA . PHE A 1 118 ? 142.820 117.245 34.408 1.00 25.62 ? 118 PHE A CA 1 ATOM 905 C C . PHE A 1 118 ? 142.611 115.926 33.645 1.00 29.37 ? 118 PHE A C 1 ATOM 906 O O . PHE A 1 118 ? 143.355 115.648 32.704 1.00 28.07 ? 118 PHE A O 1 ATOM 907 C CB . PHE A 1 118 ? 144.339 117.485 34.570 1.00 18.62 ? 118 PHE A CB 1 ATOM 908 C CG . PHE A 1 118 ? 144.695 118.800 35.200 1.00 20.91 ? 118 PHE A CG 1 ATOM 909 C CD1 . PHE A 1 118 ? 144.600 119.986 34.473 1.00 21.89 ? 118 PHE A CD1 1 ATOM 910 C CD2 . PHE A 1 118 ? 145.153 118.851 36.507 1.00 16.90 ? 118 PHE A CD2 1 ATOM 911 C CE1 . PHE A 1 118 ? 144.933 121.209 35.049 1.00 22.80 ? 118 PHE A CE1 1 ATOM 912 C CE2 . PHE A 1 118 ? 145.500 120.074 37.094 1.00 21.08 ? 118 PHE A CE2 1 ATOM 913 C CZ . PHE A 1 118 ? 145.388 121.253 36.360 1.00 19.25 ? 118 PHE A CZ 1 ATOM 914 N N . GLN A 1 119 ? 141.634 115.107 34.049 1.00 26.50 ? 119 GLN A N 1 ATOM 915 C CA . GLN A 1 119 ? 141.354 113.866 33.319 1.00 25.22 ? 119 GLN A CA 1 ATOM 916 C C . GLN A 1 119 ? 139.946 113.853 32.712 1.00 29.66 ? 119 GLN A C 1 ATOM 917 O O . GLN A 1 119 ? 139.668 113.058 31.817 1.00 25.08 ? 119 GLN A O 1 ATOM 918 C CB . GLN A 1 119 ? 141.532 112.606 34.194 1.00 25.53 ? 119 GLN A CB 1 ATOM 919 C CG . GLN A 1 119 ? 142.752 112.575 35.121 1.00 33.61 ? 119 GLN A CG 1 ATOM 920 C CD . GLN A 1 119 ? 144.067 112.875 34.407 1.00 36.46 ? 119 GLN A CD 1 ATOM 921 O OE1 . GLN A 1 119 ? 144.538 112.093 33.575 1.00 35.21 ? 119 GLN A OE1 1 ATOM 922 N NE2 . GLN A 1 119 ? 144.659 114.018 34.726 1.00 35.62 ? 119 GLN A NE2 1 ATOM 923 N N . THR A 1 120 ? 139.060 114.713 33.211 1.00 23.69 ? 120 THR A N 1 ATOM 924 C CA . THR A 1 120 ? 137.665 114.731 32.769 1.00 23.49 ? 120 THR A CA 1 ATOM 925 C C . THR A 1 120 ? 137.156 116.176 32.700 1.00 20.21 ? 120 THR A C 1 ATOM 926 O O . THR A 1 120 ? 137.900 117.109 33.009 1.00 20.55 ? 120 THR A O 1 ATOM 927 C CB . THR A 1 120 ? 136.745 113.975 33.758 1.00 26.20 ? 120 THR A CB 1 ATOM 928 O OG1 . THR A 1 120 ? 136.847 114.593 35.050 1.00 23.98 ? 120 THR A OG1 1 ATOM 929 C CG2 . THR A 1 120 ? 137.112 112.466 33.858 1.00 21.49 ? 120 THR A CG2 1 ATOM 930 N N . GLY A 1 121 ? 135.881 116.347 32.334 1.00 21.28 ? 121 GLY A N 1 ATOM 931 C CA . GLY A 1 121 ? 135.247 117.650 32.369 1.00 19.65 ? 121 GLY A CA 1 ATOM 932 C C . GLY A 1 121 ? 134.808 118.147 31.002 1.00 22.39 ? 121 GLY A C 1 ATOM 933 O O . GLY A 1 121 ? 135.305 117.680 29.967 1.00 23.55 ? 121 GLY A O 1 ATOM 934 N N . THR A 1 122 ? 133.861 119.088 30.994 1.00 21.67 ? 122 THR A N 1 ATOM 935 C CA . THR A 1 122 ? 133.416 119.709 29.746 1.00 24.90 ? 122 THR A CA 1 ATOM 936 C C . THR A 1 122 ? 132.707 121.028 30.065 1.00 30.16 ? 122 THR A C 1 ATOM 937 O O . THR A 1 122 ? 132.160 121.177 31.153 1.00 22.09 ? 122 THR A O 1 ATOM 938 C CB . THR A 1 122 ? 132.499 118.775 28.944 1.00 27.43 ? 122 THR A CB 1 ATOM 939 O OG1 . THR A 1 122 ? 132.171 119.385 27.690 1.00 31.43 ? 122 THR A OG1 1 ATOM 940 C CG2 . THR A 1 122 ? 131.217 118.462 29.722 1.00 25.45 ? 122 THR A CG2 1 ATOM 941 N N . SER A 1 123 ? 132.728 121.991 29.146 1.00 18.67 ? 123 SER A N 1 ATOM 942 C CA . SER A 1 123 ? 132.146 123.295 29.453 1.00 22.95 ? 123 SER A CA 1 ATOM 943 C C . SER A 1 123 ? 130.621 123.320 29.262 1.00 22.92 ? 123 SER A C 1 ATOM 944 O O . SER A 1 123 ? 129.971 124.332 29.542 1.00 27.18 ? 123 SER A O 1 ATOM 945 C CB . SER A 1 123 ? 132.811 124.399 28.624 1.00 20.40 ? 123 SER A CB 1 ATOM 946 O OG . SER A 1 123 ? 132.538 124.202 27.243 1.00 24.96 ? 123 SER A OG 1 ATOM 947 N N . SER A 1 124 ? 130.044 122.212 28.809 1.00 25.18 ? 124 SER A N 1 ATOM 948 C CA . SER A 1 124 ? 128.611 122.194 28.485 1.00 29.45 ? 124 SER A CA 1 ATOM 949 C C . SER A 1 124 ? 127.710 121.719 29.632 1.00 27.16 ? 124 SER A C 1 ATOM 950 O O . SER A 1 124 ? 126.507 121.623 29.457 1.00 30.48 ? 124 SER A O 1 ATOM 951 C CB . SER A 1 124 ? 128.345 121.342 27.229 1.00 29.79 ? 124 SER A CB 1 ATOM 952 O OG . SER A 1 124 ? 129.002 120.086 27.305 1.00 29.63 ? 124 SER A OG 1 ATOM 953 N N . LEU A 1 125 ? 128.284 121.418 30.795 1.00 23.58 ? 125 LEU A N 1 ATOM 954 C CA . LEU A 1 125 ? 127.483 120.988 31.948 1.00 24.10 ? 125 LEU A CA 1 ATOM 955 C C . LEU A 1 125 ? 126.471 122.071 32.362 1.00 26.33 ? 125 LEU A C 1 ATOM 956 O O . LEU A 1 125 ? 126.731 123.278 32.242 1.00 22.90 ? 125 LEU A O 1 ATOM 957 C CB . LEU A 1 125 ? 128.383 120.615 33.148 1.00 24.42 ? 125 LEU A CB 1 ATOM 958 C CG . LEU A 1 125 ? 129.384 119.461 32.972 1.00 25.86 ? 125 LEU A CG 1 ATOM 959 C CD1 . LEU A 1 125 ? 130.099 119.125 34.279 1.00 22.41 ? 125 LEU A CD1 1 ATOM 960 C CD2 . LEU A 1 125 ? 128.692 118.209 32.393 1.00 22.56 ? 125 LEU A CD2 1 ATOM 961 N N . HIS A 1 126 ? 125.324 121.612 32.848 1.00 25.31 ? 126 HIS A N 1 ATOM 962 C CA . HIS A 1 126 ? 124.223 122.457 33.295 1.00 29.26 ? 126 HIS A CA 1 ATOM 963 C C . HIS A 1 126 ? 124.686 123.470 34.356 1.00 31.40 ? 126 HIS A C 1 ATOM 964 O O . HIS A 1 126 ? 124.268 124.634 34.343 1.00 28.61 ? 126 HIS A O 1 ATOM 965 C CB . HIS A 1 126 ? 123.110 121.535 33.839 1.00 32.15 ? 126 HIS A CB 1 ATOM 966 C CG . HIS A 1 126 ? 121.911 122.249 34.380 1.00 44.75 ? 126 HIS A CG 1 ATOM 967 N ND1 . HIS A 1 126 ? 121.280 123.273 33.705 1.00 56.41 ? 126 HIS A ND1 1 ATOM 968 C CD2 . HIS A 1 126 ? 121.204 122.058 35.520 1.00 47.65 ? 126 HIS A CD2 1 ATOM 969 C CE1 . HIS A 1 126 ? 120.248 123.696 34.417 1.00 56.17 ? 126 HIS A CE1 1 ATOM 970 N NE2 . HIS A 1 126 ? 120.178 122.973 35.521 1.00 50.65 ? 126 HIS A NE2 1 ATOM 971 N N . VAL A 1 127 ? 125.554 123.028 35.265 1.00 23.73 ? 127 VAL A N 1 ATOM 972 C CA . VAL A 1 127 ? 126.042 123.897 36.343 1.00 29.81 ? 127 VAL A CA 1 ATOM 973 C C . VAL A 1 127 ? 127.035 124.978 35.887 1.00 25.50 ? 127 VAL A C 1 ATOM 974 O O . VAL A 1 127 ? 127.411 125.845 36.686 1.00 25.29 ? 127 VAL A O 1 ATOM 975 C CB . VAL A 1 127 ? 126.648 123.082 37.528 1.00 25.04 ? 127 VAL A CB 1 ATOM 976 C CG1 . VAL A 1 127 ? 125.554 122.295 38.225 1.00 28.60 ? 127 VAL A CG1 1 ATOM 977 C CG2 . VAL A 1 127 ? 127.771 122.156 37.053 1.00 22.48 ? 127 VAL A CG2 1 ATOM 978 N N . TYR A 1 128 ? 127.443 124.935 34.614 1.00 22.03 ? 128 TYR A N 1 ATOM 979 C CA . TYR A 1 128 ? 128.332 125.962 34.041 1.00 20.39 ? 128 TYR A CA 1 ATOM 980 C C . TYR A 1 128 ? 127.625 126.856 33.015 1.00 21.84 ? 128 TYR A C 1 ATOM 981 O O . TYR A 1 128 ? 128.295 127.540 32.222 1.00 19.92 ? 128 TYR A O 1 ATOM 982 C CB . TYR A 1 128 ? 129.552 125.334 33.341 1.00 19.43 ? 128 TYR A CB 1 ATOM 983 C CG . TYR A 1 128 ? 130.350 124.311 34.132 1.00 20.47 ? 128 TYR A CG 1 ATOM 984 C CD1 . TYR A 1 128 ? 130.490 124.401 35.519 1.00 17.89 ? 128 TYR A CD1 1 ATOM 985 C CD2 . TYR A 1 128 ? 130.995 123.260 33.473 1.00 19.24 ? 128 TYR A CD2 1 ATOM 986 C CE1 . TYR A 1 128 ? 131.248 123.452 36.229 1.00 16.91 ? 128 TYR A CE1 1 ATOM 987 C CE2 . TYR A 1 128 ? 131.754 122.321 34.166 1.00 19.26 ? 128 TYR A CE2 1 ATOM 988 C CZ . TYR A 1 128 ? 131.871 122.418 35.545 1.00 20.30 ? 128 TYR A CZ 1 ATOM 989 O OH . TYR A 1 128 ? 132.612 121.467 36.233 1.00 19.79 ? 128 TYR A OH 1 ATOM 990 N N . ASP A 1 129 ? 126.291 126.838 33.011 1.00 22.82 ? 129 ASP A N 1 ATOM 991 C CA . ASP A 1 129 ? 125.508 127.637 32.058 1.00 28.88 ? 129 ASP A CA 1 ATOM 992 C C . ASP A 1 129 ? 125.617 129.147 32.332 1.00 28.75 ? 129 ASP A C 1 ATOM 993 O O . ASP A 1 129 ? 125.033 129.656 33.300 1.00 23.09 ? 129 ASP A O 1 ATOM 994 C CB . ASP A 1 129 ? 124.036 127.217 32.121 1.00 27.88 ? 129 ASP A CB 1 ATOM 995 C CG . ASP A 1 129 ? 123.218 127.743 30.947 1.00 33.36 ? 129 ASP A CG 1 ATOM 996 O OD1 . ASP A 1 129 ? 123.594 128.770 30.325 1.00 31.34 ? 129 ASP A OD1 1 ATOM 997 O OD2 . ASP A 1 129 ? 122.174 127.127 30.657 1.00 32.84 ? 129 ASP A OD2 1 ATOM 998 N N . GLY A 1 130 ? 126.322 129.873 31.464 1.00 21.06 ? 130 GLY A N 1 ATOM 999 C CA . GLY A 1 130 ? 126.591 131.290 31.712 1.00 21.06 ? 130 GLY A CA 1 ATOM 1000 C C . GLY A 1 130 ? 125.446 132.267 31.445 1.00 30.35 ? 130 GLY A C 1 ATOM 1001 O O . GLY A 1 130 ? 125.604 133.486 31.626 1.00 26.78 ? 130 GLY A O 1 ATOM 1002 N N . LYS A 1 131 ? 124.288 131.758 31.032 1.00 23.45 ? 131 LYS A N 1 ATOM 1003 C CA . LYS A 1 131 ? 123.187 132.644 30.638 1.00 27.36 ? 131 LYS A CA 1 ATOM 1004 C C . LYS A 1 131 ? 122.630 133.490 31.800 1.00 32.64 ? 131 LYS A C 1 ATOM 1005 O O . LYS A 1 131 ? 122.155 134.616 31.587 1.00 31.28 ? 131 LYS A O 1 ATOM 1006 C CB . LYS A 1 131 ? 122.066 131.858 29.940 1.00 31.32 ? 131 LYS A CB 1 ATOM 1007 C CG . LYS A 1 131 ? 121.141 131.078 30.879 1.00 33.45 ? 131 LYS A CG 1 ATOM 1008 C CD . LYS A 1 131 ? 120.196 130.151 30.092 1.00 39.89 ? 131 LYS A CD 1 ATOM 1009 C CE . LYS A 1 131 ? 119.213 129.433 31.018 1.00 35.38 ? 131 LYS A CE 1 ATOM 1010 N NZ . LYS A 1 131 ? 118.345 128.463 30.276 1.00 42.12 ? 131 LYS A NZ 1 ATOM 1011 N N . PHE A 1 132 ? 122.695 132.969 33.024 1.00 28.35 ? 132 PHE A N 1 ATOM 1012 C CA . PHE A 1 132 ? 122.176 133.723 34.168 1.00 30.42 ? 132 PHE A CA 1 ATOM 1013 C C . PHE A 1 132 ? 123.073 134.910 34.533 1.00 29.10 ? 132 PHE A C 1 ATOM 1014 O O . PHE A 1 132 ? 122.574 136.007 34.804 1.00 32.36 ? 132 PHE A O 1 ATOM 1015 C CB . PHE A 1 132 ? 121.976 132.810 35.380 1.00 33.67 ? 132 PHE A CB 1 ATOM 1016 C CG . PHE A 1 132 ? 121.072 131.634 35.115 1.00 36.06 ? 132 PHE A CG 1 ATOM 1017 C CD1 . PHE A 1 132 ? 119.719 131.825 34.857 1.00 35.30 ? 132 PHE A CD1 1 ATOM 1018 C CD2 . PHE A 1 132 ? 121.576 130.336 35.138 1.00 33.57 ? 132 PHE A CD2 1 ATOM 1019 C CE1 . PHE A 1 132 ? 118.880 130.739 34.608 1.00 37.08 ? 132 PHE A CE1 1 ATOM 1020 C CE2 . PHE A 1 132 ? 120.749 129.246 34.903 1.00 35.99 ? 132 PHE A CE2 1 ATOM 1021 C CZ . PHE A 1 132 ? 119.395 129.445 34.633 1.00 34.71 ? 132 PHE A CZ 1 ATOM 1022 N N . LEU A 1 133 ? 124.390 134.687 34.553 1.00 25.90 ? 133 LEU A N 1 ATOM 1023 C CA . LEU A 1 133 ? 125.353 135.763 34.814 1.00 27.34 ? 133 LEU A CA 1 ATOM 1024 C C . LEU A 1 133 ? 125.199 136.894 33.795 1.00 32.09 ? 133 LEU A C 1 ATOM 1025 O O . LEU A 1 133 ? 125.182 138.083 34.149 1.00 28.12 ? 133 LEU A O 1 ATOM 1026 C CB . LEU A 1 133 ? 126.788 135.217 34.773 1.00 22.41 ? 133 LEU A CB 1 ATOM 1027 C CG . LEU A 1 133 ? 127.205 134.435 36.013 1.00 27.90 ? 133 LEU A CG 1 ATOM 1028 C CD1 . LEU A 1 133 ? 128.461 133.575 35.746 1.00 23.30 ? 133 LEU A CD1 1 ATOM 1029 C CD2 . LEU A 1 133 ? 127.429 135.404 37.165 1.00 30.05 ? 133 LEU A CD2 1 ATOM 1030 N N . ALA A 1 134 ? 125.070 136.516 32.526 1.00 24.35 ? 134 ALA A N 1 ATOM 1031 C CA . ALA A 1 134 ? 124.901 137.488 31.450 1.00 33.97 ? 134 ALA A CA 1 ATOM 1032 C C . ALA A 1 134 ? 123.610 138.292 31.632 1.00 37.26 ? 134 ALA A C 1 ATOM 1033 O O . ALA A 1 134 ? 123.595 139.521 31.452 1.00 32.07 ? 134 ALA A O 1 ATOM 1034 C CB . ALA A 1 134 ? 124.923 136.783 30.099 1.00 32.10 ? 134 ALA A CB 1 ATOM 1035 N N . ARG A 1 135 ? 122.534 137.601 32.004 1.00 33.96 ? 135 ARG A N 1 ATOM 1036 C CA . ARG A 1 135 ? 121.234 138.250 32.194 1.00 34.13 ? 135 ARG A CA 1 ATOM 1037 C C . ARG A 1 135 ? 121.214 139.182 33.406 1.00 36.57 ? 135 ARG A C 1 ATOM 1038 O O . ARG A 1 135 ? 120.748 140.318 33.321 1.00 36.50 ? 135 ARG A O 1 ATOM 1039 C CB . ARG A 1 135 ? 120.129 137.200 32.364 1.00 31.63 ? 135 ARG A CB 1 ATOM 1040 C CG . ARG A 1 135 ? 118.756 137.787 32.770 1.00 33.00 ? 135 ARG A CG 1 ATOM 1041 C CD . ARG A 1 135 ? 118.185 138.696 31.694 1.00 34.87 ? 135 ARG A CD 1 ATOM 1042 N NE . ARG A 1 135 ? 116.809 139.112 31.990 1.00 45.66 ? 135 ARG A NE 1 ATOM 1043 C CZ . ARG A 1 135 ? 116.470 140.331 32.404 1.00 50.30 ? 135 ARG A CZ 1 ATOM 1044 N NH1 . ARG A 1 135 ? 117.402 141.263 32.570 1.00 54.12 ? 135 ARG A NH1 1 ATOM 1045 N NH2 . ARG A 1 135 ? 115.201 140.623 32.651 1.00 50.06 ? 135 ARG A NH2 1 ATOM 1046 N N . VAL A 1 136 ? 121.718 138.689 34.534 1.00 32.44 ? 136 VAL A N 1 ATOM 1047 C CA . VAL A 1 136 ? 121.577 139.391 35.807 1.00 35.71 ? 136 VAL A CA 1 ATOM 1048 C C . VAL A 1 136 ? 122.621 140.498 36.014 1.00 39.10 ? 136 VAL A C 1 ATOM 1049 O O . VAL A 1 136 ? 122.286 141.578 36.497 1.00 30.52 ? 136 VAL A O 1 ATOM 1050 C CB . VAL A 1 136 ? 121.600 138.384 36.991 1.00 35.55 ? 136 VAL A CB 1 ATOM 1051 C CG1 . VAL A 1 136 ? 121.577 139.111 38.332 1.00 37.60 ? 136 VAL A CG1 1 ATOM 1052 C CG2 . VAL A 1 136 ? 120.408 137.428 36.885 1.00 34.69 ? 136 VAL A CG2 1 ATOM 1053 N N . GLU A 1 137 ? 123.879 140.234 35.656 1.00 36.16 ? 137 GLU A N 1 ATOM 1054 C CA . GLU A 1 137 ? 124.947 141.213 35.891 1.00 35.22 ? 137 GLU A CA 1 ATOM 1055 C C . GLU A 1 137 ? 125.455 141.930 34.636 1.00 33.55 ? 137 GLU A C 1 ATOM 1056 O O . GLU A 1 137 ? 126.326 142.807 34.730 1.00 34.51 ? 137 GLU A O 1 ATOM 1057 C CB . GLU A 1 137 ? 126.128 140.557 36.619 1.00 26.38 ? 137 GLU A CB 1 ATOM 1058 C CG . GLU A 1 137 ? 125.822 140.164 38.053 1.00 26.82 ? 137 GLU A CG 1 ATOM 1059 C CD . GLU A 1 137 ? 125.537 141.352 38.963 1.00 31.64 ? 137 GLU A CD 1 ATOM 1060 O OE1 . GLU A 1 137 ? 126.064 142.464 38.713 1.00 37.11 ? 137 GLU A OE1 1 ATOM 1061 O OE2 . GLU A 1 137 ? 124.766 141.171 39.933 1.00 36.48 ? 137 GLU A OE2 1 ATOM 1062 N N . ARG A 1 138 ? 124.917 141.557 33.476 1.00 29.42 ? 138 ARG A N 1 ATOM 1063 C CA . ARG A 1 138 ? 125.337 142.139 32.196 1.00 28.44 ? 138 ARG A CA 1 ATOM 1064 C C . ARG A 1 138 ? 126.840 142.010 31.947 1.00 33.84 ? 138 ARG A C 1 ATOM 1065 O O . ARG A 1 138 ? 127.477 142.918 31.412 1.00 29.64 ? 138 ARG A O 1 ATOM 1066 C CB . ARG A 1 138 ? 124.912 143.612 32.071 1.00 30.30 ? 138 ARG A CB 1 ATOM 1067 C CG . ARG A 1 138 ? 123.397 143.833 32.054 1.00 57.65 ? 138 ARG A CG 1 ATOM 1068 C CD . ARG A 1 138 ? 123.041 145.199 31.455 1.00 67.99 ? 138 ARG A CD 1 ATOM 1069 N NE . ARG A 1 138 ? 122.571 145.067 30.077 1.00 74.72 ? 138 ARG A NE 1 ATOM 1070 C CZ . ARG A 1 138 ? 123.153 145.619 29.015 1.00 72.71 ? 138 ARG A CZ 1 ATOM 1071 N NH1 . ARG A 1 138 ? 124.242 146.372 29.154 1.00 69.45 ? 138 ARG A NH1 1 ATOM 1072 N NH2 . ARG A 1 138 ? 122.636 145.418 27.808 1.00 69.62 ? 138 ARG A NH2 1 ATOM 1073 N N . VAL A 1 139 ? 127.414 140.887 32.347 1.00 27.10 ? 139 VAL A N 1 ATOM 1074 C CA . VAL A 1 139 ? 128.781 140.598 31.951 1.00 25.55 ? 139 VAL A CA 1 ATOM 1075 C C . VAL A 1 139 ? 128.703 139.628 30.782 1.00 25.23 ? 139 VAL A C 1 ATOM 1076 O O . VAL A 1 139 ? 127.648 139.064 30.519 1.00 26.21 ? 139 VAL A O 1 ATOM 1077 C CB . VAL A 1 139 ? 129.583 139.976 33.097 1.00 24.18 ? 139 VAL A CB 1 ATOM 1078 C CG1 . VAL A 1 139 ? 129.779 140.991 34.213 1.00 25.91 ? 139 VAL A CG1 1 ATOM 1079 C CG2 . VAL A 1 139 ? 128.890 138.720 33.616 1.00 22.45 ? 139 VAL A CG2 1 ATOM 1080 N N . ILE A 1 140 ? 129.806 139.458 30.068 1.00 27.76 ? 140 ILE A N 1 ATOM 1081 C CA . ILE A 1 140 ? 129.896 138.423 29.047 1.00 23.24 ? 140 ILE A CA 1 ATOM 1082 C C . ILE A 1 140 ? 130.580 137.197 29.663 1.00 27.65 ? 140 ILE A C 1 ATOM 1083 O O . ILE A 1 140 ? 131.558 137.337 30.405 1.00 30.27 ? 140 ILE A O 1 ATOM 1084 C CB . ILE A 1 140 ? 130.671 138.953 27.831 1.00 29.52 ? 140 ILE A CB 1 ATOM 1085 C CG1 . ILE A 1 140 ? 129.827 140.028 27.132 1.00 28.32 ? 140 ILE A CG1 1 ATOM 1086 C CG2 . ILE A 1 140 ? 131.073 137.813 26.898 1.00 31.67 ? 140 ILE A CG2 1 ATOM 1087 C CD1 . ILE A 1 140 ? 130.448 140.613 25.887 1.00 33.85 ? 140 ILE A CD1 1 ATOM 1088 N N . VAL A 1 141 ? 130.041 136.008 29.404 1.00 25.27 ? 141 VAL A N 1 ATOM 1089 C CA . VAL A 1 141 ? 130.619 134.775 29.944 1.00 25.65 ? 141 VAL A CA 1 ATOM 1090 C C . VAL A 1 141 ? 131.176 133.926 28.794 1.00 27.28 ? 141 VAL A C 1 ATOM 1091 O O . VAL A 1 141 ? 130.494 133.701 27.781 1.00 25.87 ? 141 VAL A O 1 ATOM 1092 C CB . VAL A 1 141 ? 129.578 133.985 30.778 1.00 27.93 ? 141 VAL A CB 1 ATOM 1093 C CG1 . VAL A 1 141 ? 130.179 132.685 31.369 1.00 21.46 ? 141 VAL A CG1 1 ATOM 1094 C CG2 . VAL A 1 141 ? 129.021 134.871 31.878 1.00 21.70 ? 141 VAL A CG2 1 ATOM 1095 N N . VAL A 1 142 ? 132.427 133.496 28.930 1.00 23.75 ? 142 VAL A N 1 ATOM 1096 C CA . VAL A 1 142 ? 133.058 132.626 27.940 1.00 25.01 ? 142 VAL A CA 1 ATOM 1097 C C . VAL A 1 142 ? 133.503 131.351 28.649 1.00 29.81 ? 142 VAL A C 1 ATOM 1098 O O . VAL A 1 142 ? 133.969 131.405 29.805 1.00 22.32 ? 142 VAL A O 1 ATOM 1099 C CB . VAL A 1 142 ? 134.290 133.308 27.299 1.00 28.51 ? 142 VAL A CB 1 ATOM 1100 C CG1 . VAL A 1 142 ? 134.980 132.382 26.281 1.00 19.77 ? 142 VAL A CG1 1 ATOM 1101 C CG2 . VAL A 1 142 ? 133.884 134.620 26.638 1.00 24.50 ? 142 VAL A CG2 1 ATOM 1102 N N . SER A 1 143 ? 133.323 130.207 27.988 1.00 28.50 ? 143 SER A N 1 ATOM 1103 C CA . SER A 1 143 ? 133.896 128.953 28.475 1.00 19.94 ? 143 SER A CA 1 ATOM 1104 C C . SER A 1 143 ? 134.425 128.141 27.291 1.00 24.86 ? 143 SER A C 1 ATOM 1105 O O . SER A 1 143 ? 133.938 128.302 26.168 1.00 24.71 ? 143 SER A O 1 ATOM 1106 C CB . SER A 1 143 ? 132.889 128.162 29.313 1.00 20.95 ? 143 SER A CB 1 ATOM 1107 O OG . SER A 1 143 ? 131.785 127.682 28.550 1.00 21.80 ? 143 SER A OG 1 ATOM 1108 N N . MET A 1 144 ? 135.436 127.306 27.531 1.00 22.48 ? 144 MET A N 1 ATOM 1109 C CA . MET A 1 144 ? 136.071 126.534 26.456 1.00 24.23 ? 144 MET A CA 1 ATOM 1110 C C . MET A 1 144 ? 136.300 125.069 26.843 1.00 29.30 ? 144 MET A C 1 ATOM 1111 O O . MET A 1 144 ? 136.481 124.757 28.034 1.00 24.98 ? 144 MET A O 1 ATOM 1112 C CB . MET A 1 144 ? 137.410 127.181 26.054 1.00 19.47 ? 144 MET A CB 1 ATOM 1113 C CG . MET A 1 144 ? 138.648 126.660 26.810 1.00 21.54 ? 144 MET A CG 1 ATOM 1114 S SD . MET A 1 144 ? 138.753 127.110 28.573 1.00 20.75 ? 144 MET A SD 1 ATOM 1115 C CE . MET A 1 144 ? 139.160 128.858 28.460 1.00 17.12 ? 144 MET A CE 1 ATOM 1116 N N . ASN A 1 145 ? 136.275 124.169 25.852 1.00 21.69 ? 145 ASN A N 1 ATOM 1117 C CA . ASN A 1 145 ? 136.762 122.805 26.077 1.00 22.96 ? 145 ASN A CA 1 ATOM 1118 C C . ASN A 1 145 ? 138.273 122.740 25.830 1.00 28.27 ? 145 ASN A C 1 ATOM 1119 O O . ASN A 1 145 ? 138.769 123.313 24.846 1.00 24.73 ? 145 ASN A O 1 ATOM 1120 C CB . ASN A 1 145 ? 136.015 121.773 25.208 1.00 24.44 ? 145 ASN A CB 1 ATOM 1121 C CG . ASN A 1 145 ? 134.557 121.631 25.599 1.00 27.06 ? 145 ASN A CG 1 ATOM 1122 O OD1 . ASN A 1 145 ? 134.147 122.109 26.663 1.00 21.42 ? 145 ASN A OD1 1 ATOM 1123 N ND2 . ASN A 1 145 ? 133.760 120.979 24.743 1.00 24.84 ? 145 ASN A ND2 1 ATOM 1124 N N . TYR A 1 146 ? 138.996 122.074 26.739 1.00 22.78 ? 146 TYR A N 1 ATOM 1125 C CA . TYR A 1 146 ? 140.428 121.822 26.566 1.00 21.00 ? 146 TYR A CA 1 ATOM 1126 C C . TYR A 1 146 ? 140.713 120.324 26.713 1.00 25.22 ? 146 TYR A C 1 ATOM 1127 O O . TYR A 1 146 ? 140.006 119.636 27.448 1.00 20.62 ? 146 TYR A O 1 ATOM 1128 C CB . TYR A 1 146 ? 141.254 122.633 27.581 1.00 18.41 ? 146 TYR A CB 1 ATOM 1129 C CG . TYR A 1 146 ? 140.983 122.298 29.049 1.00 18.78 ? 146 TYR A CG 1 ATOM 1130 C CD1 . TYR A 1 146 ? 139.969 122.939 29.761 1.00 19.59 ? 146 TYR A CD1 1 ATOM 1131 C CD2 . TYR A 1 146 ? 141.755 121.358 29.720 1.00 20.74 ? 146 TYR A CD2 1 ATOM 1132 C CE1 . TYR A 1 146 ? 139.736 122.650 31.105 1.00 19.99 ? 146 TYR A CE1 1 ATOM 1133 C CE2 . TYR A 1 146 ? 141.525 121.055 31.045 1.00 17.88 ? 146 TYR A CE2 1 ATOM 1134 C CZ . TYR A 1 146 ? 140.517 121.702 31.735 1.00 22.28 ? 146 TYR A CZ 1 ATOM 1135 O OH . TYR A 1 146 ? 140.303 121.392 33.064 1.00 22.17 ? 146 TYR A OH 1 ATOM 1136 N N . ARG A 1 147 ? 141.735 119.821 26.015 1.00 25.19 ? 147 ARG A N 1 ATOM 1137 C CA . ARG A 1 147 ? 142.106 118.399 26.084 1.00 22.32 ? 147 ARG A CA 1 ATOM 1138 C C . ARG A 1 147 ? 142.513 117.956 27.492 1.00 26.99 ? 147 ARG A C 1 ATOM 1139 O O . ARG A 1 147 ? 143.192 118.686 28.217 1.00 19.99 ? 147 ARG A O 1 ATOM 1140 C CB . ARG A 1 147 ? 143.251 118.090 25.116 1.00 22.71 ? 147 ARG A CB 1 ATOM 1141 C CG . ARG A 1 147 ? 142.845 118.081 23.644 1.00 33.09 ? 147 ARG A CG 1 ATOM 1142 C CD . ARG A 1 147 ? 144.072 117.949 22.736 1.00 33.50 ? 147 ARG A CD 1 ATOM 1143 N NE . ARG A 1 147 ? 144.747 119.239 22.562 1.00 28.85 ? 147 ARG A NE 1 ATOM 1144 C CZ . ARG A 1 147 ? 145.877 119.412 21.878 1.00 30.31 ? 147 ARG A CZ 1 ATOM 1145 N NH1 . ARG A 1 147 ? 146.481 118.366 21.301 1.00 27.77 ? 147 ARG A NH1 1 ATOM 1146 N NH2 . ARG A 1 147 ? 146.400 120.635 21.761 1.00 26.15 ? 147 ARG A NH2 1 ATOM 1147 N N . VAL A 1 148 ? 142.100 116.750 27.871 1.00 22.48 ? 148 VAL A N 1 ATOM 1148 C CA . VAL A 1 148 ? 142.383 116.217 29.199 1.00 23.39 ? 148 VAL A CA 1 ATOM 1149 C C . VAL A 1 148 ? 142.993 114.809 29.067 1.00 26.71 ? 148 VAL A C 1 ATOM 1150 O O . VAL A 1 148 ? 143.025 114.237 27.963 1.00 23.06 ? 148 VAL A O 1 ATOM 1151 C CB . VAL A 1 148 ? 141.084 116.199 30.065 1.00 25.88 ? 148 VAL A CB 1 ATOM 1152 C CG1 . VAL A 1 148 ? 140.616 117.623 30.340 1.00 22.01 ? 148 VAL A CG1 1 ATOM 1153 C CG2 . VAL A 1 148 ? 139.969 115.416 29.362 1.00 22.56 ? 148 VAL A CG2 1 ATOM 1154 N N . GLY A 1 149 ? 143.484 114.251 30.169 1.00 21.81 ? 149 GLY A N 1 ATOM 1155 C CA . GLY A 1 149 ? 144.097 112.927 30.123 1.00 23.13 ? 149 GLY A CA 1 ATOM 1156 C C . GLY A 1 149 ? 145.413 112.943 29.362 1.00 29.03 ? 149 GLY A C 1 ATOM 1157 O O . GLY A 1 149 ? 146.038 114.007 29.197 1.00 24.86 ? 149 GLY A O 1 ATOM 1158 N N . ALA A 1 150 ? 145.845 111.772 28.905 1.00 25.60 ? 150 ALA A N 1 ATOM 1159 C CA . ALA A 1 150 ? 147.071 111.662 28.132 1.00 30.83 ? 150 ALA A CA 1 ATOM 1160 C C . ALA A 1 150 ? 146.997 112.511 26.870 1.00 34.54 ? 150 ALA A C 1 ATOM 1161 O O . ALA A 1 150 ? 148.005 113.073 26.442 1.00 35.88 ? 150 ALA A O 1 ATOM 1162 C CB . ALA A 1 150 ? 147.372 110.193 27.776 1.00 30.66 ? 150 ALA A CB 1 ATOM 1163 N N . LEU A 1 151 ? 145.808 112.601 26.271 1.00 32.33 ? 151 LEU A N 1 ATOM 1164 C CA . LEU A 1 151 ? 145.656 113.360 25.032 1.00 32.24 ? 151 LEU A CA 1 ATOM 1165 C C . LEU A 1 151 ? 145.974 114.839 25.244 1.00 32.56 ? 151 LEU A C 1 ATOM 1166 O O . LEU A 1 151 ? 146.340 115.536 24.296 1.00 31.29 ? 151 LEU A O 1 ATOM 1167 C CB . LEU A 1 151 ? 144.245 113.194 24.441 1.00 30.46 ? 151 LEU A CB 1 ATOM 1168 C CG . LEU A 1 151 ? 143.892 111.797 23.899 1.00 28.77 ? 151 LEU A CG 1 ATOM 1169 C CD1 . LEU A 1 151 ? 142.410 111.678 23.591 1.00 32.75 ? 151 LEU A CD1 1 ATOM 1170 C CD2 . LEU A 1 151 ? 144.708 111.459 22.664 1.00 30.63 ? 151 LEU A CD2 1 ATOM 1171 N N . GLY A 1 152 ? 145.832 115.312 26.483 1.00 28.85 ? 152 GLY A N 1 ATOM 1172 C CA . GLY A 1 152 ? 146.078 116.712 26.792 1.00 28.04 ? 152 GLY A CA 1 ATOM 1173 C C . GLY A 1 152 ? 147.354 116.972 27.583 1.00 31.51 ? 152 GLY A C 1 ATOM 1174 O O . GLY A 1 152 ? 147.846 118.112 27.649 1.00 24.48 ? 152 GLY A O 1 ATOM 1175 N N . PHE A 1 153 ? 147.902 115.934 28.203 1.00 23.71 ? 153 PHE A N 1 ATOM 1176 C CA . PHE A 1 153 ? 149.031 116.162 29.098 1.00 26.03 ? 153 PHE A CA 1 ATOM 1177 C C . PHE A 1 153 ? 150.217 115.191 28.988 1.00 29.92 ? 153 PHE A C 1 ATOM 1178 O O . PHE A 1 153 ? 151.184 115.304 29.757 1.00 26.94 ? 153 PHE A O 1 ATOM 1179 C CB . PHE A 1 153 ? 148.525 116.302 30.529 1.00 22.30 ? 153 PHE A CB 1 ATOM 1180 C CG . PHE A 1 153 ? 147.696 117.550 30.750 1.00 27.80 ? 153 PHE A CG 1 ATOM 1181 C CD1 . PHE A 1 153 ? 148.311 118.766 31.036 1.00 26.77 ? 153 PHE A CD1 1 ATOM 1182 C CD2 . PHE A 1 153 ? 146.300 117.506 30.659 1.00 23.27 ? 153 PHE A CD2 1 ATOM 1183 C CE1 . PHE A 1 153 ? 147.550 119.943 31.247 1.00 26.51 ? 153 PHE A CE1 1 ATOM 1184 C CE2 . PHE A 1 153 ? 145.522 118.662 30.861 1.00 21.76 ? 153 PHE A CE2 1 ATOM 1185 C CZ . PHE A 1 153 ? 146.144 119.889 31.154 1.00 25.91 ? 153 PHE A CZ 1 ATOM 1186 N N . LEU A 1 154 ? 150.155 114.267 28.026 1.00 31.56 ? 154 LEU A N 1 ATOM 1187 C CA . LEU A 1 154 ? 151.301 113.398 27.725 1.00 33.44 ? 154 LEU A CA 1 ATOM 1188 C C . LEU A 1 154 ? 152.565 114.226 27.552 1.00 36.49 ? 154 LEU A C 1 ATOM 1189 O O . LEU A 1 154 ? 152.562 115.211 26.811 1.00 34.38 ? 154 LEU A O 1 ATOM 1190 C CB . LEU A 1 154 ? 151.074 112.592 26.445 1.00 34.59 ? 154 LEU A CB 1 ATOM 1191 C CG . LEU A 1 154 ? 152.115 111.503 26.146 1.00 40.31 ? 154 LEU A CG 1 ATOM 1192 C CD1 . LEU A 1 154 ? 151.916 110.365 27.121 1.00 43.28 ? 154 LEU A CD1 1 ATOM 1193 C CD2 . LEU A 1 154 ? 151.999 110.984 24.709 1.00 39.94 ? 154 LEU A CD2 1 ATOM 1194 N N . ALA A 1 155 ? 153.641 113.825 28.228 1.00 35.81 ? 155 ALA A N 1 ATOM 1195 C CA . ALA A 1 155 ? 154.870 114.613 28.219 1.00 50.43 ? 155 ALA A CA 1 ATOM 1196 C C . ALA A 1 155 ? 156.115 113.813 27.850 1.00 57.92 ? 155 ALA A C 1 ATOM 1197 O O . ALA A 1 155 ? 156.378 112.752 28.414 1.00 41.04 ? 155 ALA A O 1 ATOM 1198 C CB . ALA A 1 155 ? 155.073 115.324 29.576 1.00 36.53 ? 155 ALA A CB 1 ATOM 1199 N N . LEU A 1 156 ? 156.847 114.335 26.871 1.00 41.56 ? 156 LEU A N 1 ATOM 1200 C CA . LEU A 1 156 ? 158.239 113.986 26.628 1.00 57.71 ? 156 LEU A CA 1 ATOM 1201 C C . LEU A 1 156 ? 158.986 115.317 26.552 1.00 61.66 ? 156 LEU A C 1 ATOM 1202 O O . LEU A 1 156 ? 159.068 115.919 25.480 1.00 62.19 ? 156 LEU A O 1 ATOM 1203 C CB . LEU A 1 156 ? 158.392 113.238 25.308 1.00 58.40 ? 156 LEU A CB 1 ATOM 1204 C CG . LEU A 1 156 ? 158.034 111.754 25.292 1.00 58.89 ? 156 LEU A CG 1 ATOM 1205 C CD1 . LEU A 1 156 ? 158.386 111.141 23.948 1.00 61.67 ? 156 LEU A CD1 1 ATOM 1206 C CD2 . LEU A 1 156 ? 158.753 111.036 26.415 1.00 57.75 ? 156 LEU A CD2 1 ATOM 1207 N N . PRO A 1 157 ? 159.516 115.787 27.695 1.00 64.78 ? 157 PRO A N 1 ATOM 1208 C CA . PRO A 1 157 ? 160.063 117.147 27.837 1.00 66.33 ? 157 PRO A CA 1 ATOM 1209 C C . PRO A 1 157 ? 161.043 117.530 26.726 1.00 62.25 ? 157 PRO A C 1 ATOM 1210 O O . PRO A 1 157 ? 162.032 116.829 26.520 1.00 66.65 ? 157 PRO A O 1 ATOM 1211 C CB . PRO A 1 157 ? 160.786 117.090 29.186 1.00 71.01 ? 157 PRO A CB 1 ATOM 1212 C CG . PRO A 1 157 ? 160.068 116.024 29.952 1.00 68.17 ? 157 PRO A CG 1 ATOM 1213 C CD . PRO A 1 157 ? 159.670 114.996 28.930 1.00 64.96 ? 157 PRO A CD 1 ATOM 1214 N N . GLY A 1 158 ? 160.749 118.618 26.014 1.00 57.69 ? 158 GLY A N 1 ATOM 1215 C CA . GLY A 1 158 ? 161.620 119.118 24.962 1.00 62.58 ? 158 GLY A CA 1 ATOM 1216 C C . GLY A 1 158 ? 161.244 118.695 23.554 1.00 68.16 ? 158 GLY A C 1 ATOM 1217 O O . GLY A 1 158 ? 161.709 119.277 22.573 1.00 74.32 ? 158 GLY A O 1 ATOM 1218 N N . ASN A 1 159 ? 160.393 117.680 23.460 1.00 60.95 ? 159 ASN A N 1 ATOM 1219 C CA . ASN A 1 159 ? 159.983 117.109 22.185 1.00 55.86 ? 159 ASN A CA 1 ATOM 1220 C C . ASN A 1 159 ? 158.637 117.676 21.732 1.00 55.08 ? 159 ASN A C 1 ATOM 1221 O O . ASN A 1 159 ? 157.598 117.379 22.334 1.00 49.39 ? 159 ASN A O 1 ATOM 1222 C CB . ASN A 1 159 ? 159.892 115.591 22.337 1.00 54.91 ? 159 ASN A CB 1 ATOM 1223 C CG . ASN A 1 159 ? 159.569 114.885 21.041 1.00 56.80 ? 159 ASN A CG 1 ATOM 1224 O OD1 . ASN A 1 159 ? 159.023 115.475 20.111 1.00 54.57 ? 159 ASN A OD1 1 ATOM 1225 N ND2 . ASN A 1 159 ? 159.897 113.599 20.978 1.00 62.26 ? 159 ASN A ND2 1 ATOM 1226 N N . PRO A 1 160 ? 158.640 118.467 20.644 1.00 56.18 ? 160 PRO A N 1 ATOM 1227 C CA . PRO A 1 160 ? 157.397 119.132 20.222 1.00 51.36 ? 160 PRO A CA 1 ATOM 1228 C C . PRO A 1 160 ? 156.331 118.177 19.674 1.00 51.46 ? 160 PRO A C 1 ATOM 1229 O O . PRO A 1 160 ? 155.218 118.626 19.374 1.00 49.14 ? 160 PRO A O 1 ATOM 1230 C CB . PRO A 1 160 ? 157.867 120.126 19.149 1.00 50.33 ? 160 PRO A CB 1 ATOM 1231 C CG . PRO A 1 160 ? 159.176 119.574 18.650 1.00 54.85 ? 160 PRO A CG 1 ATOM 1232 C CD . PRO A 1 160 ? 159.796 118.820 19.796 1.00 56.08 ? 160 PRO A CD 1 ATOM 1233 N N . GLU A 1 161 ? 156.656 116.888 19.558 1.00 54.62 ? 161 GLU A N 1 ATOM 1234 C CA . GLU A 1 161 ? 155.660 115.881 19.184 1.00 53.71 ? 161 GLU A CA 1 ATOM 1235 C C . GLU A 1 161 ? 154.779 115.516 20.382 1.00 50.93 ? 161 GLU A C 1 ATOM 1236 O O . GLU A 1 161 ? 153.674 114.984 20.213 1.00 46.72 ? 161 GLU A O 1 ATOM 1237 C CB . GLU A 1 161 ? 156.329 114.617 18.620 1.00 57.79 ? 161 GLU A CB 1 ATOM 1238 C CG . GLU A 1 161 ? 157.279 114.869 17.454 1.00 68.04 ? 161 GLU A CG 1 ATOM 1239 C CD . GLU A 1 161 ? 156.581 115.482 16.256 1.00 78.18 ? 161 GLU A CD 1 ATOM 1240 O OE1 . GLU A 1 161 ? 155.547 114.931 15.827 1.00 82.07 ? 161 GLU A OE1 1 ATOM 1241 O OE2 . GLU A 1 161 ? 157.061 116.516 15.747 1.00 83.54 ? 161 GLU A OE2 1 ATOM 1242 N N . ALA A 1 162 ? 155.280 115.796 21.584 1.00 49.85 ? 162 ALA A N 1 ATOM 1243 C CA . ALA A 1 162 ? 154.524 115.575 22.819 1.00 51.52 ? 162 ALA A CA 1 ATOM 1244 C C . ALA A 1 162 ? 155.206 116.292 23.982 1.00 49.55 ? 162 ALA A C 1 ATOM 1245 O O . ALA A 1 162 ? 155.783 115.649 24.863 1.00 40.39 ? 162 ALA A O 1 ATOM 1246 C CB . ALA A 1 162 ? 154.405 114.082 23.114 1.00 52.33 ? 162 ALA A CB 1 ATOM 1247 N N . PRO A 1 163 ? 155.132 117.633 23.993 1.00 43.42 ? 163 PRO A N 1 ATOM 1248 C CA . PRO A 1 163 ? 155.953 118.430 24.907 1.00 40.05 ? 163 PRO A CA 1 ATOM 1249 C C . PRO A 1 163 ? 155.347 118.556 26.299 1.00 44.24 ? 163 PRO A C 1 ATOM 1250 O O . PRO A 1 163 ? 156.018 119.071 27.204 1.00 38.35 ? 163 PRO A O 1 ATOM 1251 C CB . PRO A 1 163 ? 155.974 119.801 24.228 1.00 40.76 ? 163 PRO A CB 1 ATOM 1252 C CG . PRO A 1 163 ? 154.620 119.902 23.596 1.00 40.86 ? 163 PRO A CG 1 ATOM 1253 C CD . PRO A 1 163 ? 154.290 118.484 23.127 1.00 41.11 ? 163 PRO A CD 1 ATOM 1254 N N . GLY A 1 164 ? 154.111 118.091 26.468 1.00 28.68 ? 164 GLY A N 1 ATOM 1255 C CA . GLY A 1 164 ? 153.392 118.291 27.711 1.00 27.35 ? 164 GLY A CA 1 ATOM 1256 C C . GLY A 1 164 ? 152.568 119.569 27.726 1.00 28.31 ? 164 GLY A C 1 ATOM 1257 O O . GLY A 1 164 ? 152.740 120.436 26.866 1.00 26.66 ? 164 GLY A O 1 ATOM 1258 N N . ASN A 1 165 ? 151.655 119.673 28.692 1.00 25.98 ? 165 ASN A N 1 ATOM 1259 C CA . ASN A 1 165 ? 150.879 120.901 28.909 1.00 25.53 ? 165 ASN A CA 1 ATOM 1260 C C . ASN A 1 165 ? 149.950 121.330 27.762 1.00 22.99 ? 165 ASN A C 1 ATOM 1261 O O . ASN A 1 165 ? 149.506 122.484 27.721 1.00 22.66 ? 165 ASN A O 1 ATOM 1262 C CB . ASN A 1 165 ? 151.801 122.075 29.311 1.00 25.06 ? 165 ASN A CB 1 ATOM 1263 C CG . ASN A 1 165 ? 152.359 121.919 30.711 1.00 26.28 ? 165 ASN A CG 1 ATOM 1264 O OD1 . ASN A 1 165 ? 151.971 121.002 31.448 1.00 25.43 ? 165 ASN A OD1 1 ATOM 1265 N ND2 . ASN A 1 165 ? 153.277 122.810 31.091 1.00 26.09 ? 165 ASN A ND2 1 ATOM 1266 N N . MET A 1 166 ? 149.657 120.423 26.834 1.00 24.22 ? 166 MET A N 1 ATOM 1267 C CA . MET A 1 166 ? 148.812 120.778 25.695 1.00 25.97 ? 166 MET A CA 1 ATOM 1268 C C . MET A 1 166 ? 147.431 121.332 26.105 1.00 25.18 ? 166 MET A C 1 ATOM 1269 O O . MET A 1 166 ? 146.953 122.330 25.534 1.00 22.86 ? 166 MET A O 1 ATOM 1270 C CB . MET A 1 166 ? 148.659 119.587 24.736 1.00 26.22 ? 166 MET A CB 1 ATOM 1271 C CG . MET A 1 166 ? 149.974 119.085 24.162 1.00 31.39 ? 166 MET A CG 1 ATOM 1272 S SD . MET A 1 166 ? 150.892 117.976 25.271 1.00 29.85 ? 166 MET A SD 1 ATOM 1273 C CE . MET A 1 166 ? 149.969 116.440 25.028 1.00 27.37 ? 166 MET A CE 1 ATOM 1274 N N . GLY A 1 167 ? 146.788 120.702 27.085 1.00 26.03 ? 167 GLY A N 1 ATOM 1275 C CA . GLY A 1 167 ? 145.492 121.187 27.558 1.00 21.16 ? 167 GLY A CA 1 ATOM 1276 C C . GLY A 1 167 ? 145.576 122.614 28.096 1.00 29.41 ? 167 GLY A C 1 ATOM 1277 O O . GLY A 1 167 ? 144.616 123.399 27.991 1.00 21.50 ? 167 GLY A O 1 ATOM 1278 N N . LEU A 1 168 ? 146.719 122.957 28.686 1.00 26.74 ? 168 LEU A N 1 ATOM 1279 C CA . LEU A 1 168 ? 146.920 124.323 29.174 1.00 27.46 ? 168 LEU A CA 1 ATOM 1280 C C . LEU A 1 168 ? 147.127 125.281 27.992 1.00 27.90 ? 168 LEU A C 1 ATOM 1281 O O . LEU A 1 168 ? 146.651 126.423 28.012 1.00 25.91 ? 168 LEU A O 1 ATOM 1282 C CB . LEU A 1 168 ? 148.097 124.395 30.157 1.00 22.37 ? 168 LEU A CB 1 ATOM 1283 C CG . LEU A 1 168 ? 147.849 123.812 31.555 1.00 24.85 ? 168 LEU A CG 1 ATOM 1284 C CD1 . LEU A 1 168 ? 149.171 123.667 32.333 1.00 18.47 ? 168 LEU A CD1 1 ATOM 1285 C CD2 . LEU A 1 168 ? 146.858 124.670 32.339 1.00 21.20 ? 168 LEU A CD2 1 ATOM 1286 N N . PHE A 1 169 ? 147.824 124.817 26.955 1.00 23.06 ? 169 PHE A N 1 ATOM 1287 C CA . PHE A 1 169 ? 147.971 125.635 25.751 1.00 22.88 ? 169 PHE A CA 1 ATOM 1288 C C . PHE A 1 169 ? 146.631 125.812 25.005 1.00 24.40 ? 169 PHE A C 1 ATOM 1289 O O . PHE A 1 169 ? 146.400 126.856 24.376 1.00 24.36 ? 169 PHE A O 1 ATOM 1290 C CB . PHE A 1 169 ? 149.078 125.089 24.842 1.00 23.54 ? 169 PHE A CB 1 ATOM 1291 C CG . PHE A 1 169 ? 150.463 125.560 25.230 1.00 30.43 ? 169 PHE A CG 1 ATOM 1292 C CD1 . PHE A 1 169 ? 150.798 126.908 25.142 1.00 29.15 ? 169 PHE A CD1 1 ATOM 1293 C CD2 . PHE A 1 169 ? 151.425 124.660 25.678 1.00 29.81 ? 169 PHE A CD2 1 ATOM 1294 C CE1 . PHE A 1 169 ? 152.078 127.361 25.493 1.00 34.46 ? 169 PHE A CE1 1 ATOM 1295 C CE2 . PHE A 1 169 ? 152.707 125.104 26.034 1.00 33.26 ? 169 PHE A CE2 1 ATOM 1296 C CZ . PHE A 1 169 ? 153.032 126.451 25.938 1.00 36.75 ? 169 PHE A CZ 1 ATOM 1297 N N . ASP A 1 170 ? 145.751 124.814 25.095 1.00 21.38 ? 170 ASP A N 1 ATOM 1298 C CA . ASP A 1 170 ? 144.390 124.941 24.560 1.00 25.48 ? 170 ASP A CA 1 ATOM 1299 C C . ASP A 1 170 ? 143.681 126.118 25.247 1.00 26.46 ? 170 ASP A C 1 ATOM 1300 O O . ASP A 1 170 ? 143.153 127.015 24.580 1.00 23.15 ? 170 ASP A O 1 ATOM 1301 C CB . ASP A 1 170 ? 143.575 123.653 24.778 1.00 20.97 ? 170 ASP A CB 1 ATOM 1302 C CG . ASP A 1 170 ? 144.088 122.459 23.951 1.00 28.59 ? 170 ASP A CG 1 ATOM 1303 O OD1 . ASP A 1 170 ? 144.882 122.652 23.010 1.00 32.82 ? 170 ASP A OD1 1 ATOM 1304 O OD2 . ASP A 1 170 ? 143.677 121.308 24.238 1.00 26.11 ? 170 ASP A OD2 1 ATOM 1305 N N . GLN A 1 171 ? 143.670 126.101 26.582 1.00 21.79 ? 171 GLN A N 1 ATOM 1306 C CA . GLN A 1 171 ? 143.151 127.211 27.368 1.00 22.76 ? 171 GLN A CA 1 ATOM 1307 C C . GLN A 1 171 ? 143.748 128.554 26.933 1.00 22.79 ? 171 GLN A C 1 ATOM 1308 O O . GLN A 1 171 ? 143.024 129.540 26.805 1.00 20.75 ? 171 GLN A O 1 ATOM 1309 C CB . GLN A 1 171 ? 143.430 126.993 28.866 1.00 24.01 ? 171 GLN A CB 1 ATOM 1310 C CG . GLN A 1 171 ? 142.678 125.815 29.502 1.00 26.60 ? 171 GLN A CG 1 ATOM 1311 C CD . GLN A 1 171 ? 143.154 125.543 30.916 1.00 26.80 ? 171 GLN A CD 1 ATOM 1312 O OE1 . GLN A 1 171 ? 143.753 126.419 31.560 1.00 23.22 ? 171 GLN A OE1 1 ATOM 1313 N NE2 . GLN A 1 171 ? 142.894 124.326 31.414 1.00 21.08 ? 171 GLN A NE2 1 ATOM 1314 N N . GLN A 1 172 ? 145.059 128.604 26.707 1.00 23.04 ? 172 GLN A N 1 ATOM 1315 C CA . GLN A 1 172 ? 145.702 129.881 26.406 1.00 24.62 ? 172 GLN A CA 1 ATOM 1316 C C . GLN A 1 172 ? 145.243 130.387 25.042 1.00 33.69 ? 172 GLN A C 1 ATOM 1317 O O . GLN A 1 172 ? 145.017 131.590 24.848 1.00 27.84 ? 172 GLN A O 1 ATOM 1318 C CB . GLN A 1 172 ? 147.223 129.742 26.427 1.00 26.28 ? 172 GLN A CB 1 ATOM 1319 C CG . GLN A 1 172 ? 147.998 131.060 26.437 1.00 23.44 ? 172 GLN A CG 1 ATOM 1320 C CD . GLN A 1 172 ? 149.505 130.810 26.448 1.00 25.72 ? 172 GLN A CD 1 ATOM 1321 O OE1 . GLN A 1 172 ? 150.072 130.400 25.442 1.00 28.22 ? 172 GLN A OE1 1 ATOM 1322 N NE2 . GLN A 1 172 ? 150.145 131.014 27.601 1.00 24.04 ? 172 GLN A NE2 1 ATOM 1323 N N . LEU A 1 173 ? 145.097 129.466 24.096 1.00 28.40 ? 173 LEU A N 1 ATOM 1324 C CA . LEU A 1 173 ? 144.701 129.868 22.755 1.00 30.76 ? 173 LEU A CA 1 ATOM 1325 C C . LEU A 1 173 ? 143.287 130.461 22.783 1.00 22.79 ? 173 LEU A C 1 ATOM 1326 O O . LEU A 1 173 ? 142.997 131.421 22.067 1.00 29.81 ? 173 LEU A O 1 ATOM 1327 C CB . LEU A 1 173 ? 144.807 128.689 21.781 1.00 28.53 ? 173 LEU A CB 1 ATOM 1328 C CG . LEU A 1 173 ? 144.630 129.037 20.298 1.00 31.94 ? 173 LEU A CG 1 ATOM 1329 C CD1 . LEU A 1 173 ? 145.626 130.112 19.839 1.00 30.19 ? 173 LEU A CD1 1 ATOM 1330 C CD2 . LEU A 1 173 ? 144.745 127.784 19.441 1.00 31.04 ? 173 LEU A CD2 1 ATOM 1331 N N . ALA A 1 174 ? 142.421 129.910 23.636 1.00 24.67 ? 174 ALA A N 1 ATOM 1332 C CA . ALA A 1 174 ? 141.079 130.474 23.806 1.00 25.32 ? 174 ALA A CA 1 ATOM 1333 C C . ALA A 1 174 ? 141.112 131.885 24.410 1.00 26.16 ? 174 ALA A C 1 ATOM 1334 O O . ALA A 1 174 ? 140.337 132.753 23.991 1.00 29.24 ? 174 ALA A O 1 ATOM 1335 C CB . ALA A 1 174 ? 140.182 129.543 24.640 1.00 22.69 ? 174 ALA A CB 1 ATOM 1336 N N . LEU A 1 175 ? 141.999 132.120 25.383 1.00 27.19 ? 175 LEU A N 1 ATOM 1337 C CA . LEU A 1 175 ? 142.160 133.470 25.954 1.00 30.00 ? 175 LEU A CA 1 ATOM 1338 C C . LEU A 1 175 ? 142.589 134.458 24.872 1.00 30.01 ? 175 LEU A C 1 ATOM 1339 O O . LEU A 1 175 ? 142.170 135.620 24.868 1.00 31.48 ? 175 LEU A O 1 ATOM 1340 C CB . LEU A 1 175 ? 143.180 133.488 27.098 1.00 26.55 ? 175 LEU A CB 1 ATOM 1341 C CG . LEU A 1 175 ? 143.042 132.463 28.228 1.00 30.82 ? 175 LEU A CG 1 ATOM 1342 C CD1 . LEU A 1 175 ? 143.987 132.790 29.377 1.00 23.35 ? 175 LEU A CD1 1 ATOM 1343 C CD2 . LEU A 1 175 ? 141.604 132.339 28.722 1.00 29.98 ? 175 LEU A CD2 1 ATOM 1344 N N . GLN A 1 176 ? 143.416 133.980 23.948 1.00 28.85 ? 176 GLN A N 1 ATOM 1345 C CA . GLN A 1 176 ? 143.872 134.789 22.828 1.00 30.54 ? 176 GLN A CA 1 ATOM 1346 C C . GLN A 1 176 ? 142.702 135.076 21.886 1.00 31.20 ? 176 GLN A C 1 ATOM 1347 O O . GLN A 1 176 ? 142.600 136.176 21.325 1.00 29.39 ? 176 GLN A O 1 ATOM 1348 C CB . GLN A 1 176 ? 144.998 134.059 22.092 1.00 36.83 ? 176 GLN A CB 1 ATOM 1349 C CG . GLN A 1 176 ? 145.628 134.839 20.971 1.00 53.38 ? 176 GLN A CG 1 ATOM 1350 C CD . GLN A 1 176 ? 146.247 136.132 21.461 1.00 69.56 ? 176 GLN A CD 1 ATOM 1351 O OE1 . GLN A 1 176 ? 145.653 137.202 21.333 1.00 75.26 ? 176 GLN A OE1 1 ATOM 1352 N NE2 . GLN A 1 176 ? 147.444 136.038 22.034 1.00 72.21 ? 176 GLN A NE2 1 ATOM 1353 N N . TRP A 1 177 ? 141.817 134.091 21.723 1.00 33.05 ? 177 TRP A N 1 ATOM 1354 C CA . TRP A 1 177 ? 140.630 134.265 20.879 1.00 32.51 ? 177 TRP A CA 1 ATOM 1355 C C . TRP A 1 177 ? 139.776 135.421 21.416 1.00 28.66 ? 177 TRP A C 1 ATOM 1356 O O . TRP A 1 177 ? 139.354 136.306 20.664 1.00 30.81 ? 177 TRP A O 1 ATOM 1357 C CB . TRP A 1 177 ? 139.805 132.968 20.786 1.00 31.16 ? 177 TRP A CB 1 ATOM 1358 C CG . TRP A 1 177 ? 138.620 133.097 19.852 1.00 34.23 ? 177 TRP A CG 1 ATOM 1359 C CD1 . TRP A 1 177 ? 138.573 132.763 18.518 1.00 33.90 ? 177 TRP A CD1 1 ATOM 1360 C CD2 . TRP A 1 177 ? 137.326 133.628 20.176 1.00 29.50 ? 177 TRP A CD2 1 ATOM 1361 N NE1 . TRP A 1 177 ? 137.325 133.048 18.002 1.00 30.00 ? 177 TRP A NE1 1 ATOM 1362 C CE2 . TRP A 1 177 ? 136.543 133.579 18.997 1.00 31.18 ? 177 TRP A CE2 1 ATOM 1363 C CE3 . TRP A 1 177 ? 136.752 134.135 21.349 1.00 28.11 ? 177 TRP A CE3 1 ATOM 1364 C CZ2 . TRP A 1 177 ? 135.215 134.023 18.961 1.00 28.21 ? 177 TRP A CZ2 1 ATOM 1365 C CZ3 . TRP A 1 177 ? 135.433 134.569 21.314 1.00 27.98 ? 177 TRP A CZ3 1 ATOM 1366 C CH2 . TRP A 1 177 ? 134.681 134.513 20.126 1.00 29.33 ? 177 TRP A CH2 1 ATOM 1367 N N . VAL A 1 178 ? 139.546 135.421 22.725 1.00 27.05 ? 178 VAL A N 1 ATOM 1368 C CA . VAL A 1 178 ? 138.846 136.520 23.380 1.00 27.99 ? 178 VAL A CA 1 ATOM 1369 C C . VAL A 1 178 ? 139.559 137.877 23.202 1.00 26.35 ? 178 VAL A C 1 ATOM 1370 O O . VAL A 1 178 ? 138.902 138.886 22.917 1.00 28.02 ? 178 VAL A O 1 ATOM 1371 C CB . VAL A 1 178 ? 138.621 136.226 24.882 1.00 25.66 ? 178 VAL A CB 1 ATOM 1372 C CG1 . VAL A 1 178 ? 138.051 137.441 25.584 1.00 22.41 ? 178 VAL A CG1 1 ATOM 1373 C CG2 . VAL A 1 178 ? 137.691 135.032 25.054 1.00 22.72 ? 178 VAL A CG2 1 ATOM 1374 N N . GLN A 1 179 ? 140.887 137.914 23.355 1.00 27.42 ? 179 GLN A N 1 ATOM 1375 C CA . GLN A 1 179 ? 141.611 139.174 23.155 1.00 28.39 ? 179 GLN A CA 1 ATOM 1376 C C . GLN A 1 179 ? 141.369 139.715 21.744 1.00 30.82 ? 179 GLN A C 1 ATOM 1377 O O . GLN A 1 179 ? 141.167 140.916 21.559 1.00 34.16 ? 179 GLN A O 1 ATOM 1378 C CB . GLN A 1 179 ? 143.124 139.028 23.416 1.00 34.56 ? 179 GLN A CB 1 ATOM 1379 C CG . GLN A 1 179 ? 143.533 138.968 24.892 1.00 28.85 ? 179 GLN A CG 1 ATOM 1380 C CD . GLN A 1 179 ? 143.022 140.159 25.695 1.00 26.27 ? 179 GLN A CD 1 ATOM 1381 O OE1 . GLN A 1 179 ? 143.428 141.292 25.463 1.00 28.54 ? 179 GLN A OE1 1 ATOM 1382 N NE2 . GLN A 1 179 ? 142.115 139.903 26.629 1.00 29.99 ? 179 GLN A NE2 1 ATOM 1383 N N . LYS A 1 180 ? 141.363 138.824 20.753 1.00 33.57 ? 180 LYS A N 1 ATOM 1384 C CA . LYS A 1 180 ? 141.229 139.253 19.358 1.00 39.96 ? 180 LYS A CA 1 ATOM 1385 C C . LYS A 1 180 ? 139.791 139.507 18.878 1.00 36.26 ? 180 LYS A C 1 ATOM 1386 O O . LYS A 1 180 ? 139.565 140.326 17.985 1.00 36.61 ? 180 LYS A O 1 ATOM 1387 C CB . LYS A 1 180 ? 141.957 138.271 18.430 1.00 41.27 ? 180 LYS A CB 1 ATOM 1388 C CG . LYS A 1 180 ? 143.467 138.504 18.419 1.00 53.70 ? 180 LYS A CG 1 ATOM 1389 C CD . LYS A 1 180 ? 144.274 137.212 18.402 1.00 59.34 ? 180 LYS A CD 1 ATOM 1390 C CE . LYS A 1 180 ? 144.323 136.593 17.015 1.00 63.92 ? 180 LYS A CE 1 ATOM 1391 N NZ . LYS A 1 180 ? 145.337 135.509 16.946 1.00 66.67 ? 180 LYS A NZ 1 ATOM 1392 N N . ASN A 1 181 ? 138.822 138.837 19.490 1.00 31.55 ? 181 ASN A N 1 ATOM 1393 C CA . ASN A 1 181 ? 137.469 138.811 18.938 1.00 36.44 ? 181 ASN A CA 1 ATOM 1394 C C . ASN A 1 181 ? 136.357 139.389 19.815 1.00 33.95 ? 181 ASN A C 1 ATOM 1395 O O . ASN A 1 181 ? 135.286 139.704 19.305 1.00 30.81 ? 181 ASN A O 1 ATOM 1396 C CB . ASN A 1 181 ? 137.081 137.369 18.561 1.00 36.14 ? 181 ASN A CB 1 ATOM 1397 C CG . ASN A 1 181 ? 137.915 136.816 17.418 1.00 34.95 ? 181 ASN A CG 1 ATOM 1398 O OD1 . ASN A 1 181 ? 137.808 137.270 16.278 1.00 34.56 ? 181 ASN A OD1 1 ATOM 1399 N ND2 . ASN A 1 181 ? 138.733 135.811 17.715 1.00 33.21 ? 181 ASN A ND2 1 ATOM 1400 N N . ILE A 1 182 ? 136.581 139.498 21.123 1.00 28.04 ? 182 ILE A N 1 ATOM 1401 C CA . ILE A 1 182 ? 135.471 139.797 22.031 1.00 31.97 ? 182 ILE A CA 1 ATOM 1402 C C . ILE A 1 182 ? 134.866 141.213 21.884 1.00 34.95 ? 182 ILE A C 1 ATOM 1403 O O . ILE A 1 182 ? 133.685 141.418 22.193 1.00 33.45 ? 182 ILE A O 1 ATOM 1404 C CB . ILE A 1 182 ? 135.825 139.488 23.509 1.00 27.37 ? 182 ILE A CB 1 ATOM 1405 C CG1 . ILE A 1 182 ? 134.566 139.110 24.290 1.00 26.01 ? 182 ILE A CG1 1 ATOM 1406 C CG2 . ILE A 1 182 ? 136.549 140.666 24.165 1.00 26.09 ? 182 ILE A CG2 1 ATOM 1407 C CD1 . ILE A 1 182 ? 134.011 137.726 23.953 1.00 28.42 ? 182 ILE A CD1 1 ATOM 1408 N N . ALA A 1 183 ? 135.645 142.178 21.392 1.00 34.69 ? 183 ALA A N 1 ATOM 1409 C CA . ALA A 1 183 ? 135.101 143.520 21.164 1.00 31.81 ? 183 ALA A CA 1 ATOM 1410 C C . ALA A 1 183 ? 133.973 143.453 20.148 1.00 41.70 ? 183 ALA A C 1 ATOM 1411 O O . ALA A 1 183 ? 133.017 144.221 20.221 1.00 40.39 ? 183 ALA A O 1 ATOM 1412 C CB . ALA A 1 183 ? 136.183 144.480 20.689 1.00 33.19 ? 183 ALA A CB 1 ATOM 1413 N N . ALA A 1 184 ? 134.080 142.522 19.206 1.00 39.10 ? 184 ALA A N 1 ATOM 1414 C CA . ALA A 1 184 ? 133.080 142.410 18.146 1.00 41.52 ? 184 ALA A CA 1 ATOM 1415 C C . ALA A 1 184 ? 131.726 142.012 18.731 1.00 43.67 ? 184 ALA A C 1 ATOM 1416 O O . ALA A 1 184 ? 130.673 142.278 18.142 1.00 45.71 ? 184 ALA A O 1 ATOM 1417 C CB . ALA A 1 184 ? 133.530 141.409 17.098 1.00 41.08 ? 184 ALA A CB 1 ATOM 1418 N N . PHE A 1 185 ? 131.781 141.382 19.902 1.00 38.15 ? 185 PHE A N 1 ATOM 1419 C CA . PHE A 1 185 ? 130.613 140.909 20.631 1.00 35.46 ? 185 PHE A CA 1 ATOM 1420 C C . PHE A 1 185 ? 130.202 141.920 21.709 1.00 43.62 ? 185 PHE A C 1 ATOM 1421 O O . PHE A 1 185 ? 129.289 141.658 22.500 1.00 43.69 ? 185 PHE A O 1 ATOM 1422 C CB . PHE A 1 185 ? 130.952 139.585 21.322 1.00 36.87 ? 185 PHE A CB 1 ATOM 1423 C CG . PHE A 1 185 ? 131.130 138.417 20.381 1.00 36.92 ? 185 PHE A CG 1 ATOM 1424 C CD1 . PHE A 1 185 ? 132.360 138.168 19.779 1.00 35.65 ? 185 PHE A CD1 1 ATOM 1425 C CD2 . PHE A 1 185 ? 130.073 137.545 20.130 1.00 35.50 ? 185 PHE A CD2 1 ATOM 1426 C CE1 . PHE A 1 185 ? 132.527 137.082 18.923 1.00 35.82 ? 185 PHE A CE1 1 ATOM 1427 C CE2 . PHE A 1 185 ? 130.228 136.451 19.280 1.00 36.86 ? 185 PHE A CE2 1 ATOM 1428 C CZ . PHE A 1 185 ? 131.457 136.221 18.675 1.00 37.12 ? 185 PHE A CZ 1 ATOM 1429 N N . GLY A 1 186 ? 130.896 143.056 21.757 1.00 41.58 ? 186 GLY A N 1 ATOM 1430 C CA . GLY A 1 186 ? 130.617 144.084 22.744 1.00 36.43 ? 186 GLY A CA 1 ATOM 1431 C C . GLY A 1 186 ? 131.359 143.925 24.064 1.00 37.10 ? 186 GLY A C 1 ATOM 1432 O O . GLY A 1 186 ? 130.973 144.530 25.069 1.00 33.57 ? 186 GLY A O 1 ATOM 1433 N N . GLY A 1 187 ? 132.425 143.125 24.071 1.00 31.35 ? 187 GLY A N 1 ATOM 1434 C CA . GLY A 1 187 ? 133.195 142.911 25.285 1.00 29.21 ? 187 GLY A CA 1 ATOM 1435 C C . GLY A 1 187 ? 134.431 143.791 25.379 1.00 34.75 ? 187 GLY A C 1 ATOM 1436 O O . GLY A 1 187 ? 134.895 144.339 24.376 1.00 35.13 ? 187 GLY A O 1 ATOM 1437 N N . ASN A 1 188 ? 134.960 143.930 26.592 1.00 36.48 ? 188 ASN A N 1 ATOM 1438 C CA . ASN A 1 188 ? 136.193 144.682 26.841 1.00 32.94 ? 188 ASN A CA 1 ATOM 1439 C C . ASN A 1 188 ? 137.391 143.741 27.053 1.00 29.94 ? 188 ASN A C 1 ATOM 1440 O O . ASN A 1 188 ? 137.512 143.118 28.108 1.00 28.05 ? 188 ASN A O 1 ATOM 1441 C CB . ASN A 1 188 ? 136.007 145.582 28.070 1.00 30.33 ? 188 ASN A CB 1 ATOM 1442 C CG . ASN A 1 188 ? 137.180 146.540 28.293 1.00 30.19 ? 188 ASN A CG 1 ATOM 1443 O OD1 . ASN A 1 188 ? 138.158 146.546 27.539 1.00 34.43 ? 188 ASN A OD1 1 ATOM 1444 N ND2 . ASN A 1 188 ? 137.075 147.361 29.326 1.00 29.42 ? 188 ASN A ND2 1 ATOM 1445 N N . PRO A 1 189 ? 138.282 143.636 26.051 1.00 31.04 ? 189 PRO A N 1 ATOM 1446 C CA . PRO A 1 189 ? 139.463 142.768 26.178 1.00 32.64 ? 189 PRO A CA 1 ATOM 1447 C C . PRO A 1 189 ? 140.399 143.213 27.313 1.00 34.63 ? 189 PRO A C 1 ATOM 1448 O O . PRO A 1 189 ? 141.244 142.426 27.754 1.00 30.81 ? 189 PRO A O 1 ATOM 1449 C CB . PRO A 1 189 ? 140.161 142.931 24.824 1.00 31.73 ? 189 PRO A CB 1 ATOM 1450 C CG . PRO A 1 189 ? 139.718 144.284 24.323 1.00 35.00 ? 189 PRO A CG 1 ATOM 1451 C CD . PRO A 1 189 ? 138.301 144.432 24.808 1.00 36.25 ? 189 PRO A CD 1 ATOM 1452 N N . LYS A 1 190 ? 140.249 144.455 27.774 1.00 29.10 ? 190 LYS A N 1 ATOM 1453 C CA . LYS A 1 190 ? 141.070 144.968 28.874 1.00 31.04 ? 190 LYS A CA 1 ATOM 1454 C C . LYS A 1 190 ? 140.451 144.704 30.245 1.00 29.69 ? 190 LYS A C 1 ATOM 1455 O O . LYS A 1 190 ? 140.986 145.148 31.262 1.00 33.57 ? 190 LYS A O 1 ATOM 1456 C CB . LYS A 1 190 ? 141.313 146.471 28.718 1.00 31.70 ? 190 LYS A CB 1 ATOM 1457 C CG . LYS A 1 190 ? 142.162 146.836 27.519 1.00 33.63 ? 190 LYS A CG 1 ATOM 1458 C CD . LYS A 1 190 ? 142.306 148.346 27.386 1.00 43.03 ? 190 LYS A CD 1 ATOM 1459 C CE . LYS A 1 190 ? 143.170 148.687 26.189 1.00 60.07 ? 190 LYS A CE 1 ATOM 1460 N NZ . LYS A 1 190 ? 144.417 147.858 26.213 1.00 67.73 ? 190 LYS A NZ 1 ATOM 1461 N N . SER A 1 191 ? 139.319 144.001 30.277 1.00 28.37 ? 191 SER A N 1 ATOM 1462 C CA . SER A 1 191 ? 138.677 143.688 31.556 1.00 28.41 ? 191 SER A CA 1 ATOM 1463 C C . SER A 1 191 ? 138.168 142.259 31.553 1.00 33.84 ? 191 SER A C 1 ATOM 1464 O O . SER A 1 191 ? 136.957 142.004 31.501 1.00 35.75 ? 191 SER A O 1 ATOM 1465 C CB . SER A 1 191 ? 137.537 144.665 31.868 1.00 26.84 ? 191 SER A CB 1 ATOM 1466 O OG . SER A 1 191 ? 136.932 144.355 33.112 1.00 24.67 ? 191 SER A OG 1 ATOM 1467 N N . VAL A 1 192 ? 139.119 141.333 31.624 1.00 21.65 ? 192 VAL A N 1 ATOM 1468 C CA . VAL A 1 192 ? 138.843 139.903 31.581 1.00 20.47 ? 192 VAL A CA 1 ATOM 1469 C C . VAL A 1 192 ? 139.259 139.261 32.907 1.00 20.96 ? 192 VAL A C 1 ATOM 1470 O O . VAL A 1 192 ? 140.408 139.417 33.346 1.00 24.36 ? 192 VAL A O 1 ATOM 1471 C CB . VAL A 1 192 ? 139.640 139.254 30.436 1.00 26.20 ? 192 VAL A CB 1 ATOM 1472 C CG1 . VAL A 1 192 ? 139.486 137.736 30.456 1.00 23.16 ? 192 VAL A CG1 1 ATOM 1473 C CG2 . VAL A 1 192 ? 139.218 139.838 29.089 1.00 25.18 ? 192 VAL A CG2 1 ATOM 1474 N N . THR A 1 193 ? 138.334 138.545 33.543 1.00 23.96 ? 193 THR A N 1 ATOM 1475 C CA . THR A 1 193 ? 138.635 137.813 34.771 1.00 21.51 ? 193 THR A CA 1 ATOM 1476 C C . THR A 1 193 ? 138.509 136.308 34.511 1.00 27.32 ? 193 THR A C 1 ATOM 1477 O O . THR A 1 193 ? 137.470 135.853 34.028 1.00 21.26 ? 193 THR A O 1 ATOM 1478 C CB . THR A 1 193 ? 137.673 138.228 35.901 1.00 18.01 ? 193 THR A CB 1 ATOM 1479 O OG1 . THR A 1 193 ? 137.918 139.596 36.244 1.00 21.11 ? 193 THR A OG1 1 ATOM 1480 C CG2 . THR A 1 193 ? 137.877 137.374 37.157 1.00 18.89 ? 193 THR A CG2 1 ATOM 1481 N N . LEU A 1 194 ? 139.565 135.541 34.793 1.00 22.84 ? 194 LEU A N 1 ATOM 1482 C CA . LEU A 1 194 ? 139.486 134.081 34.661 1.00 20.32 ? 194 LEU A CA 1 ATOM 1483 C C . LEU A 1 194 ? 138.849 133.556 35.934 1.00 22.96 ? 194 LEU A C 1 ATOM 1484 O O . LEU A 1 194 ? 139.156 134.056 37.026 1.00 18.22 ? 194 LEU A O 1 ATOM 1485 C CB . LEU A 1 194 ? 140.886 133.455 34.505 1.00 21.48 ? 194 LEU A CB 1 ATOM 1486 C CG . LEU A 1 194 ? 141.843 134.071 33.471 1.00 22.91 ? 194 LEU A CG 1 ATOM 1487 C CD1 . LEU A 1 194 ? 143.216 133.366 33.451 1.00 22.29 ? 194 LEU A CD1 1 ATOM 1488 C CD2 . LEU A 1 194 ? 141.207 134.063 32.070 1.00 17.01 ? 194 LEU A CD2 1 ATOM 1489 N N . PHE A 1 195 ? 137.949 132.580 35.812 1.00 22.13 ? 195 PHE A N 1 ATOM 1490 C CA . PHE A 1 195 ? 137.524 131.841 36.994 1.00 17.97 ? 195 PHE A CA 1 ATOM 1491 C C . PHE A 1 195 ? 137.393 130.345 36.722 1.00 25.95 ? 195 PHE A C 1 ATOM 1492 O O . PHE A 1 195 ? 137.169 129.940 35.581 1.00 25.39 ? 195 PHE A O 1 ATOM 1493 C CB . PHE A 1 195 ? 136.295 132.476 37.705 1.00 17.98 ? 195 PHE A CB 1 ATOM 1494 C CG . PHE A 1 195 ? 134.962 132.331 36.980 1.00 16.83 ? 195 PHE A CG 1 ATOM 1495 C CD1 . PHE A 1 195 ? 134.841 132.547 35.620 1.00 18.49 ? 195 PHE A CD1 1 ATOM 1496 C CD2 . PHE A 1 195 ? 133.807 132.030 37.709 1.00 17.69 ? 195 PHE A CD2 1 ATOM 1497 C CE1 . PHE A 1 195 ? 133.582 132.421 34.982 1.00 20.39 ? 195 PHE A CE1 1 ATOM 1498 C CE2 . PHE A 1 195 ? 132.557 131.902 37.088 1.00 18.84 ? 195 PHE A CE2 1 ATOM 1499 C CZ . PHE A 1 195 ? 132.450 132.100 35.717 1.00 21.40 ? 195 PHE A CZ 1 ATOM 1500 N N . GLY A 1 196 ? 137.580 129.531 37.767 1.00 17.78 ? 196 GLY A N 1 ATOM 1501 C CA . GLY A 1 196 ? 137.592 128.080 37.633 1.00 14.05 ? 196 GLY A CA 1 ATOM 1502 C C . GLY A 1 196 ? 137.537 127.380 38.978 1.00 23.02 ? 196 GLY A C 1 ATOM 1503 O O . GLY A 1 196 ? 137.734 128.015 40.030 1.00 16.70 ? 196 GLY A O 1 ATOM 1504 N N . GLU A 1 197 ? 137.266 126.076 38.950 1.00 17.43 ? 197 GLU A N 1 ATOM 1505 C CA . GLU A 1 197 ? 137.089 125.300 40.177 1.00 19.69 ? 197 GLU A CA 1 ATOM 1506 C C . GLU A 1 197 ? 137.905 124.014 40.116 1.00 21.62 ? 197 GLU A C 1 ATOM 1507 O O . GLU A 1 197 ? 138.029 123.394 39.047 1.00 15.30 ? 197 GLU A O 1 ATOM 1508 C CB . GLU A 1 197 ? 135.592 124.996 40.439 1.00 15.69 ? 197 GLU A CB 1 ATOM 1509 C CG . GLU A 1 197 ? 135.313 124.264 41.766 1.00 15.26 ? 197 GLU A CG 1 ATOM 1510 C CD . GLU A 1 197 ? 135.297 122.745 41.603 1.00 22.96 ? 197 GLU A CD 1 ATOM 1511 O OE1 . GLU A 1 197 ? 135.461 122.277 40.445 1.00 19.85 ? 197 GLU A OE1 1 ATOM 1512 O OE2 . GLU A 1 197 ? 135.103 122.019 42.620 1.00 19.57 ? 197 GLU A OE2 1 ATOM 1513 N N A SER A 1 198 ? 138.459 123.617 41.258 0.55 18.66 ? 198 SER A N 1 ATOM 1514 N N B SER A 1 198 ? 138.451 123.612 41.263 0.45 18.71 ? 198 SER A N 1 ATOM 1515 C CA A SER A 1 198 ? 139.274 122.409 41.337 0.55 17.68 ? 198 SER A CA 1 ATOM 1516 C CA B SER A 1 198 ? 139.320 122.436 41.358 0.45 17.97 ? 198 SER A CA 1 ATOM 1517 C C A SER A 1 198 ? 140.444 122.492 40.350 0.55 20.20 ? 198 SER A C 1 ATOM 1518 C C B SER A 1 198 ? 140.467 122.499 40.343 0.45 20.45 ? 198 SER A C 1 ATOM 1519 O O A SER A 1 198 ? 141.247 123.424 40.433 0.55 19.73 ? 198 SER A O 1 ATOM 1520 O O B SER A 1 198 ? 141.277 123.428 40.396 0.45 19.93 ? 198 SER A O 1 ATOM 1521 C CB A SER A 1 198 ? 138.417 121.162 41.107 0.55 21.70 ? 198 SER A CB 1 ATOM 1522 C CB B SER A 1 198 ? 138.520 121.129 41.273 0.45 21.43 ? 198 SER A CB 1 ATOM 1523 O OG A SER A 1 198 ? 138.840 120.099 41.943 0.55 23.41 ? 198 SER A OG 1 ATOM 1524 O OG B SER A 1 198 ? 137.867 120.971 40.027 0.45 20.64 ? 198 SER A OG 1 ATOM 1525 N N . ALA A 1 199 ? 140.548 121.542 39.417 1.00 19.27 ? 199 ALA A N 1 ATOM 1526 C CA . ALA A 1 199 ? 141.660 121.572 38.449 1.00 19.95 ? 199 ALA A CA 1 ATOM 1527 C C . ALA A 1 199 ? 141.600 122.813 37.532 1.00 20.57 ? 199 ALA A C 1 ATOM 1528 O O . ALA A 1 199 ? 142.627 123.256 36.992 1.00 20.49 ? 199 ALA A O 1 ATOM 1529 C CB . ALA A 1 199 ? 141.754 120.265 37.630 1.00 20.47 ? 199 ALA A CB 1 ATOM 1530 N N . GLY A 1 200 ? 140.396 123.362 37.350 1.00 17.19 ? 200 GLY A N 1 ATOM 1531 C CA . GLY A 1 200 ? 140.244 124.615 36.628 1.00 16.83 ? 200 GLY A CA 1 ATOM 1532 C C . GLY A 1 200 ? 140.852 125.768 37.411 1.00 15.54 ? 200 GLY A C 1 ATOM 1533 O O . GLY A 1 200 ? 141.475 126.679 36.844 1.00 16.69 ? 200 GLY A O 1 ATOM 1534 N N . ALA A 1 201 ? 140.681 125.743 38.730 1.00 14.72 ? 201 ALA A N 1 ATOM 1535 C CA . ALA A 1 201 ? 141.316 126.763 39.573 1.00 19.61 ? 201 ALA A CA 1 ATOM 1536 C C . ALA A 1 201 ? 142.836 126.595 39.606 1.00 21.46 ? 201 ALA A C 1 ATOM 1537 O O . ALA A 1 201 ? 143.574 127.587 39.640 1.00 19.88 ? 201 ALA A O 1 ATOM 1538 C CB . ALA A 1 201 ? 140.732 126.745 40.980 1.00 14.36 ? 201 ALA A CB 1 ATOM 1539 N N . ALA A 1 202 ? 143.308 125.345 39.621 1.00 18.69 ? 202 ALA A N 1 ATOM 1540 C CA . ALA A 1 202 ? 144.748 125.093 39.499 1.00 21.39 ? 202 ALA A CA 1 ATOM 1541 C C . ALA A 1 202 ? 145.264 125.692 38.186 1.00 20.22 ? 202 ALA A C 1 ATOM 1542 O O . ALA A 1 202 ? 146.308 126.356 38.165 1.00 22.89 ? 202 ALA A O 1 ATOM 1543 C CB . ALA A 1 202 ? 145.048 123.590 39.571 1.00 21.07 ? 202 ALA A CB 1 ATOM 1544 N N . SER A 1 203 ? 144.509 125.481 37.104 1.00 20.29 ? 203 SER A N 1 ATOM 1545 C CA . SER A 1 203 ? 144.827 126.073 35.805 1.00 20.07 ? 203 SER A CA 1 ATOM 1546 C C . SER A 1 203 ? 144.887 127.602 35.906 1.00 19.64 ? 203 SER A C 1 ATOM 1547 O O . SER A 1 203 ? 145.838 128.230 35.424 1.00 23.37 ? 203 SER A O 1 ATOM 1548 C CB . SER A 1 203 ? 143.780 125.668 34.767 1.00 23.63 ? 203 SER A CB 1 ATOM 1549 O OG . SER A 1 203 ? 143.732 124.264 34.598 1.00 23.87 ? 203 SER A OG 1 ATOM 1550 N N . VAL A 1 204 ? 143.885 128.202 36.547 1.00 20.61 ? 204 VAL A N 1 ATOM 1551 C CA . VAL A 1 204 ? 143.885 129.657 36.722 1.00 20.18 ? 204 VAL A CA 1 ATOM 1552 C C . VAL A 1 204 ? 145.179 130.119 37.416 1.00 19.39 ? 204 VAL A C 1 ATOM 1553 O O . VAL A 1 204 ? 145.832 131.065 36.965 1.00 19.17 ? 204 VAL A O 1 ATOM 1554 C CB . VAL A 1 204 ? 142.650 130.152 37.512 1.00 22.27 ? 204 VAL A CB 1 ATOM 1555 C CG1 . VAL A 1 204 ? 142.803 131.632 37.890 1.00 23.40 ? 204 VAL A CG1 1 ATOM 1556 C CG2 . VAL A 1 204 ? 141.382 129.973 36.701 1.00 21.18 ? 204 VAL A CG2 1 ATOM 1557 N N . SER A 1 205 ? 145.575 129.431 38.480 1.00 17.62 ? 205 SER A N 1 ATOM 1558 C CA . SER A 1 205 ? 146.790 129.831 39.202 1.00 22.83 ? 205 SER A CA 1 ATOM 1559 C C . SER A 1 205 ? 148.038 129.710 38.326 1.00 20.88 ? 205 SER A C 1 ATOM 1560 O O . SER A 1 205 ? 148.974 130.503 38.466 1.00 22.13 ? 205 SER A O 1 ATOM 1561 C CB . SER A 1 205 ? 146.960 129.046 40.514 1.00 22.80 ? 205 SER A CB 1 ATOM 1562 O OG . SER A 1 205 ? 147.243 127.668 40.301 1.00 23.74 ? 205 SER A OG 1 ATOM 1563 N N . LEU A 1 206 ? 148.032 128.745 37.409 1.00 18.50 ? 206 LEU A N 1 ATOM 1564 C CA . LEU A 1 206 ? 149.180 128.521 36.523 1.00 24.21 ? 206 LEU A CA 1 ATOM 1565 C C . LEU A 1 206 ? 149.251 129.592 35.430 1.00 22.84 ? 206 LEU A C 1 ATOM 1566 O O . LEU A 1 206 ? 150.341 129.978 35.002 1.00 23.89 ? 206 LEU A O 1 ATOM 1567 C CB . LEU A 1 206 ? 149.135 127.102 35.913 1.00 21.31 ? 206 LEU A CB 1 ATOM 1568 C CG . LEU A 1 206 ? 149.588 125.965 36.841 1.00 23.15 ? 206 LEU A CG 1 ATOM 1569 C CD1 . LEU A 1 206 ? 149.473 124.572 36.184 1.00 22.63 ? 206 LEU A CD1 1 ATOM 1570 C CD2 . LEU A 1 206 ? 151.028 126.213 37.343 1.00 17.60 ? 206 LEU A CD2 1 ATOM 1571 N N . HIS A 1 207 ? 148.091 130.068 34.973 1.00 18.37 ? 207 HIS A N 1 ATOM 1572 C CA . HIS A 1 207 ? 148.058 131.224 34.071 1.00 17.24 ? 207 HIS A CA 1 ATOM 1573 C C . HIS A 1 207 ? 148.630 132.480 34.756 1.00 18.10 ? 207 HIS A C 1 ATOM 1574 O O . HIS A 1 207 ? 149.202 133.345 34.090 1.00 19.34 ? 207 HIS A O 1 ATOM 1575 C CB . HIS A 1 207 ? 146.629 131.475 33.540 1.00 21.44 ? 207 HIS A CB 1 ATOM 1576 C CG . HIS A 1 207 ? 146.175 130.472 32.513 1.00 17.50 ? 207 HIS A CG 1 ATOM 1577 N ND1 . HIS A 1 207 ? 146.692 130.429 31.233 1.00 18.79 ? 207 HIS A ND1 1 ATOM 1578 C CD2 . HIS A 1 207 ? 145.261 129.469 32.582 1.00 18.46 ? 207 HIS A CD2 1 ATOM 1579 C CE1 . HIS A 1 207 ? 146.124 129.437 30.561 1.00 21.88 ? 207 HIS A CE1 1 ATOM 1580 N NE2 . HIS A 1 207 ? 145.248 128.841 31.355 1.00 16.71 ? 207 HIS A NE2 1 ATOM 1581 N N . LEU A 1 208 ? 148.482 132.586 36.083 1.00 19.67 ? 208 LEU A N 1 ATOM 1582 C CA . LEU A 1 208 ? 149.116 133.673 36.822 1.00 21.70 ? 208 LEU A CA 1 ATOM 1583 C C . LEU A 1 208 ? 150.638 133.557 36.771 1.00 25.20 ? 208 LEU A C 1 ATOM 1584 O O . LEU A 1 208 ? 151.344 134.561 36.919 1.00 26.03 ? 208 LEU A O 1 ATOM 1585 C CB . LEU A 1 208 ? 148.650 133.703 38.290 1.00 19.51 ? 208 LEU A CB 1 ATOM 1586 C CG . LEU A 1 208 ? 147.268 134.319 38.595 1.00 22.62 ? 208 LEU A CG 1 ATOM 1587 C CD1 . LEU A 1 208 ? 146.844 134.006 40.023 1.00 20.19 ? 208 LEU A CD1 1 ATOM 1588 C CD2 . LEU A 1 208 ? 147.239 135.835 38.368 1.00 17.62 ? 208 LEU A CD2 1 ATOM 1589 N N . LEU A 1 209 ? 151.150 132.338 36.574 1.00 23.28 ? 209 LEU A N 1 ATOM 1590 C CA . LEU A 1 209 ? 152.602 132.138 36.521 1.00 29.80 ? 209 LEU A CA 1 ATOM 1591 C C . LEU A 1 209 ? 153.177 132.122 35.097 1.00 32.10 ? 209 LEU A C 1 ATOM 1592 O O . LEU A 1 209 ? 154.378 132.311 34.917 1.00 38.84 ? 209 LEU A O 1 ATOM 1593 C CB . LEU A 1 209 ? 153.008 130.834 37.223 1.00 36.35 ? 209 LEU A CB 1 ATOM 1594 C CG . LEU A 1 209 ? 152.629 130.544 38.676 1.00 39.85 ? 209 LEU A CG 1 ATOM 1595 C CD1 . LEU A 1 209 ? 153.384 129.339 39.198 1.00 42.42 ? 209 LEU A CD1 1 ATOM 1596 C CD2 . LEU A 1 209 ? 152.888 131.717 39.567 1.00 38.20 ? 209 LEU A CD2 1 ATOM 1597 N N . SER A 1 210 ? 152.343 131.874 34.087 1.00 24.92 ? 210 SER A N 1 ATOM 1598 C CA . SER A 1 210 ? 152.876 131.717 32.724 1.00 26.23 ? 210 SER A CA 1 ATOM 1599 C C . SER A 1 210 ? 153.041 133.059 32.012 1.00 25.78 ? 210 SER A C 1 ATOM 1600 O O . SER A 1 210 ? 152.062 133.769 31.796 1.00 27.09 ? 210 SER A O 1 ATOM 1601 C CB . SER A 1 210 ? 151.966 130.806 31.896 1.00 26.04 ? 210 SER A CB 1 ATOM 1602 O OG . SER A 1 210 ? 152.567 130.495 30.653 1.00 29.59 ? 210 SER A OG 1 ATOM 1603 N N . PRO A 1 211 ? 154.276 133.406 31.627 1.00 35.08 ? 211 PRO A N 1 ATOM 1604 C CA . PRO A 1 211 ? 154.480 134.722 31.003 1.00 41.08 ? 211 PRO A CA 1 ATOM 1605 C C . PRO A 1 211 ? 153.672 134.876 29.715 1.00 36.47 ? 211 PRO A C 1 ATOM 1606 O O . PRO A 1 211 ? 153.260 135.993 29.400 1.00 37.72 ? 211 PRO A O 1 ATOM 1607 C CB . PRO A 1 211 ? 155.996 134.754 30.722 1.00 42.12 ? 211 PRO A CB 1 ATOM 1608 C CG . PRO A 1 211 ? 156.581 133.819 31.746 1.00 44.65 ? 211 PRO A CG 1 ATOM 1609 C CD . PRO A 1 211 ? 155.547 132.699 31.867 1.00 37.00 ? 211 PRO A CD 1 ATOM 1610 N N . GLY A 1 212 ? 153.430 133.774 29.007 1.00 29.86 ? 212 GLY A N 1 ATOM 1611 C CA . GLY A 1 212 ? 152.605 133.793 27.808 1.00 33.72 ? 212 GLY A CA 1 ATOM 1612 C C . GLY A 1 212 ? 151.136 134.127 28.053 1.00 36.74 ? 212 GLY A C 1 ATOM 1613 O O . GLY A 1 212 ? 150.430 134.527 27.128 1.00 36.52 ? 212 GLY A O 1 ATOM 1614 N N . SER A 1 213 ? 150.657 133.954 29.284 1.00 29.20 ? 213 SER A N 1 ATOM 1615 C CA . SER A 1 213 ? 149.270 134.312 29.590 1.00 26.36 ? 213 SER A CA 1 ATOM 1616 C C . SER A 1 213 ? 149.106 135.713 30.214 1.00 28.83 ? 213 SER A C 1 ATOM 1617 O O . SER A 1 213 ? 147.978 136.179 30.384 1.00 30.71 ? 213 SER A O 1 ATOM 1618 C CB . SER A 1 213 ? 148.628 133.264 30.507 1.00 24.22 ? 213 SER A CB 1 ATOM 1619 O OG . SER A 1 213 ? 148.615 131.968 29.905 1.00 25.75 ? 213 SER A OG 1 ATOM 1620 N N . HIS A 1 214 ? 150.211 136.381 30.546 1.00 27.81 ? 214 HIS A N 1 ATOM 1621 C CA A HIS A 1 214 ? 150.191 137.645 31.309 0.45 30.25 ? 214 HIS A CA 1 ATOM 1622 C CA B HIS A 1 214 ? 150.109 137.597 31.342 0.55 29.63 ? 214 HIS A CA 1 ATOM 1623 C C . HIS A 1 214 ? 149.306 138.723 30.688 1.00 29.73 ? 214 HIS A C 1 ATOM 1624 O O . HIS A 1 214 ? 148.510 139.371 31.368 1.00 32.04 ? 214 HIS A O 1 ATOM 1625 C CB A HIS A 1 214 ? 151.626 138.186 31.471 0.45 33.28 ? 214 HIS A CB 1 ATOM 1626 C CB B HIS A 1 214 ? 151.485 138.063 31.838 0.55 32.70 ? 214 HIS A CB 1 ATOM 1627 C CG A HIS A 1 214 ? 151.737 139.420 32.322 0.45 35.94 ? 214 HIS A CG 1 ATOM 1628 C CG B HIS A 1 214 ? 152.023 137.230 32.963 0.55 30.18 ? 214 HIS A CG 1 ATOM 1629 N ND1 A HIS A 1 214 ? 151.323 140.666 31.896 0.45 36.41 ? 214 HIS A ND1 1 ATOM 1630 N ND1 B HIS A 1 214 ? 153.178 137.551 33.646 0.55 25.25 ? 214 HIS A ND1 1 ATOM 1631 C CD2 A HIS A 1 214 ? 152.265 139.606 33.556 0.45 35.11 ? 214 HIS A CD2 1 ATOM 1632 C CD2 B HIS A 1 214 ? 151.555 136.089 33.529 0.55 24.75 ? 214 HIS A CD2 1 ATOM 1633 C CE1 A HIS A 1 214 ? 151.566 141.558 32.840 0.45 30.97 ? 214 HIS A CE1 1 ATOM 1634 C CE1 B HIS A 1 214 ? 153.400 136.646 34.582 0.55 23.16 ? 214 HIS A CE1 1 ATOM 1635 N NE2 A HIS A 1 214 ? 152.142 140.943 33.856 0.45 29.36 ? 214 HIS A NE2 1 ATOM 1636 N NE2 B HIS A 1 214 ? 152.431 135.747 34.531 0.55 35.02 ? 214 HIS A NE2 1 ATOM 1637 N N . SER A 1 215 ? 149.465 138.933 29.385 1.00 28.67 ? 215 SER A N 1 ATOM 1638 C CA . SER A 1 215 ? 148.717 140.000 28.713 1.00 37.87 ? 215 SER A CA 1 ATOM 1639 C C . SER A 1 215 ? 147.286 139.575 28.356 1.00 33.60 ? 215 SER A C 1 ATOM 1640 O O . SER A 1 215 ? 146.528 140.362 27.791 1.00 32.65 ? 215 SER A O 1 ATOM 1641 C CB . SER A 1 215 ? 149.444 140.435 27.439 1.00 47.55 ? 215 SER A CB 1 ATOM 1642 O OG . SER A 1 215 ? 149.381 139.401 26.466 1.00 55.40 ? 215 SER A OG 1 ATOM 1643 N N . LEU A 1 216 ? 146.920 138.335 28.682 1.00 27.06 ? 216 LEU A N 1 ATOM 1644 C CA . LEU A 1 216 ? 145.659 137.771 28.204 1.00 24.47 ? 216 LEU A CA 1 ATOM 1645 C C . LEU A 1 216 ? 144.494 137.898 29.191 1.00 29.80 ? 216 LEU A C 1 ATOM 1646 O O . LEU A 1 216 ? 143.363 137.480 28.884 1.00 27.96 ? 216 LEU A O 1 ATOM 1647 C CB . LEU A 1 216 ? 145.842 136.294 27.823 1.00 26.14 ? 216 LEU A CB 1 ATOM 1648 C CG . LEU A 1 216 ? 146.961 135.945 26.834 1.00 32.27 ? 216 LEU A CG 1 ATOM 1649 C CD1 . LEU A 1 216 ? 146.883 134.468 26.422 1.00 22.40 ? 216 LEU A CD1 1 ATOM 1650 C CD2 . LEU A 1 216 ? 146.907 136.846 25.622 1.00 32.25 ? 216 LEU A CD2 1 ATOM 1651 N N . PHE A 1 217 ? 144.756 138.443 30.377 1.00 25.52 ? 217 PHE A N 1 ATOM 1652 C CA . PHE A 1 217 ? 143.683 138.604 31.366 1.00 22.62 ? 217 PHE A CA 1 ATOM 1653 C C . PHE A 1 217 ? 144.022 139.650 32.407 1.00 25.12 ? 217 PHE A C 1 ATOM 1654 O O . PHE A 1 217 ? 145.167 140.110 32.480 1.00 26.28 ? 217 PHE A O 1 ATOM 1655 C CB . PHE A 1 217 ? 143.306 137.259 32.023 1.00 19.20 ? 217 PHE A CB 1 ATOM 1656 C CG . PHE A 1 217 ? 144.356 136.696 32.951 1.00 25.43 ? 217 PHE A CG 1 ATOM 1657 C CD1 . PHE A 1 217 ? 145.480 136.045 32.447 1.00 23.65 ? 217 PHE A CD1 1 ATOM 1658 C CD2 . PHE A 1 217 ? 144.190 136.769 34.336 1.00 23.59 ? 217 PHE A CD2 1 ATOM 1659 C CE1 . PHE A 1 217 ? 146.446 135.500 33.305 1.00 21.28 ? 217 PHE A CE1 1 ATOM 1660 C CE2 . PHE A 1 217 ? 145.152 136.237 35.208 1.00 21.59 ? 217 PHE A CE2 1 ATOM 1661 C CZ . PHE A 1 217 ? 146.279 135.595 34.696 1.00 21.26 ? 217 PHE A CZ 1 ATOM 1662 N N . THR A 1 218 ? 143.027 140.038 33.200 1.00 22.74 ? 218 THR A N 1 ATOM 1663 C CA . THR A 1 218 ? 143.192 141.140 34.153 1.00 25.43 ? 218 THR A CA 1 ATOM 1664 C C . THR A 1 218 ? 143.296 140.636 35.597 1.00 22.92 ? 218 THR A C 1 ATOM 1665 O O . THR A 1 218 ? 144.196 141.040 36.339 1.00 26.40 ? 218 THR A O 1 ATOM 1666 C CB . THR A 1 218 ? 141.979 142.090 34.093 1.00 30.18 ? 218 THR A CB 1 ATOM 1667 O OG1 . THR A 1 218 ? 141.662 142.390 32.724 1.00 30.48 ? 218 THR A OG1 1 ATOM 1668 C CG2 . THR A 1 218 ? 142.248 143.384 34.876 1.00 31.72 ? 218 THR A CG2 1 ATOM 1669 N N . ARG A 1 219 ? 142.356 139.767 35.993 1.00 20.11 ? 219 ARG A N 1 ATOM 1670 C CA . ARG A 1 219 ? 142.229 139.343 37.393 1.00 22.99 ? 219 ARG A CA 1 ATOM 1671 C C . ARG A 1 219 ? 141.865 137.860 37.444 1.00 24.99 ? 219 ARG A C 1 ATOM 1672 O O . ARG A 1 219 ? 141.544 137.266 36.410 1.00 21.28 ? 219 ARG A O 1 ATOM 1673 C CB . ARG A 1 219 ? 141.124 140.156 38.095 1.00 22.59 ? 219 ARG A CB 1 ATOM 1674 C CG . ARG A 1 219 ? 141.606 141.386 38.802 1.00 41.91 ? 219 ARG A CG 1 ATOM 1675 C CD . ARG A 1 219 ? 140.470 142.077 39.556 1.00 40.49 ? 219 ARG A CD 1 ATOM 1676 N NE . ARG A 1 219 ? 139.571 142.752 38.640 1.00 37.32 ? 219 ARG A NE 1 ATOM 1677 C CZ . ARG A 1 219 ? 139.785 143.966 38.152 1.00 34.32 ? 219 ARG A CZ 1 ATOM 1678 N NH1 . ARG A 1 219 ? 140.878 144.643 38.494 1.00 31.11 ? 219 ARG A NH1 1 ATOM 1679 N NH2 . ARG A 1 219 ? 138.908 144.500 37.313 1.00 32.04 ? 219 ARG A NH2 1 ATOM 1680 N N . ALA A 1 220 ? 141.888 137.261 38.637 1.00 16.98 ? 220 ALA A N 1 ATOM 1681 C CA . ALA A 1 220 ? 141.654 135.818 38.734 1.00 16.12 ? 220 ALA A CA 1 ATOM 1682 C C . ALA A 1 220 ? 140.850 135.389 39.963 1.00 18.32 ? 220 ALA A C 1 ATOM 1683 O O . ALA A 1 220 ? 140.984 135.972 41.059 1.00 16.82 ? 220 ALA A O 1 ATOM 1684 C CB . ALA A 1 220 ? 142.995 135.044 38.668 1.00 19.81 ? 220 ALA A CB 1 ATOM 1685 N N . ILE A 1 221 ? 140.051 134.337 39.780 1.00 15.35 ? 221 ILE A N 1 ATOM 1686 C CA . ILE A 1 221 ? 139.238 133.762 40.857 1.00 18.49 ? 221 ILE A CA 1 ATOM 1687 C C . ILE A 1 221 ? 139.525 132.262 40.970 1.00 24.32 ? 221 ILE A C 1 ATOM 1688 O O . ILE A 1 221 ? 139.435 131.536 39.962 1.00 21.05 ? 221 ILE A O 1 ATOM 1689 C CB . ILE A 1 221 ? 137.728 133.942 40.540 1.00 20.13 ? 221 ILE A CB 1 ATOM 1690 C CG1 . ILE A 1 221 ? 137.329 135.425 40.516 1.00 16.27 ? 221 ILE A CG1 1 ATOM 1691 C CG2 . ILE A 1 221 ? 136.833 133.131 41.506 1.00 16.05 ? 221 ILE A CG2 1 ATOM 1692 C CD1 . ILE A 1 221 ? 135.795 135.633 40.316 1.00 16.76 ? 221 ILE A CD1 1 ATOM 1693 N N . LEU A 1 222 ? 139.837 131.784 42.176 1.00 14.72 ? 222 LEU A N 1 ATOM 1694 C CA . LEU A 1 222 ? 140.243 130.369 42.365 1.00 14.39 ? 222 LEU A CA 1 ATOM 1695 C C . LEU A 1 222 ? 139.316 129.618 43.349 1.00 17.88 ? 222 LEU A C 1 ATOM 1696 O O . LEU A 1 222 ? 139.419 129.791 44.583 1.00 18.28 ? 222 LEU A O 1 ATOM 1697 C CB . LEU A 1 222 ? 141.709 130.285 42.861 1.00 14.47 ? 222 LEU A CB 1 ATOM 1698 C CG . LEU A 1 222 ? 142.887 130.625 41.939 1.00 24.89 ? 222 LEU A CG 1 ATOM 1699 C CD1 . LEU A 1 222 ? 142.894 132.110 41.579 1.00 33.38 ? 222 LEU A CD1 1 ATOM 1700 C CD2 . LEU A 1 222 ? 144.217 130.262 42.595 1.00 21.69 ? 222 LEU A CD2 1 ATOM 1701 N N . GLN A 1 223 ? 138.397 128.810 42.820 1.00 17.88 ? 223 GLN A N 1 ATOM 1702 C CA . GLN A 1 223 ? 137.458 128.064 43.669 1.00 20.02 ? 223 GLN A CA 1 ATOM 1703 C C . GLN A 1 223 ? 137.953 126.636 43.962 1.00 21.74 ? 223 GLN A C 1 ATOM 1704 O O . GLN A 1 223 ? 138.052 125.818 43.043 1.00 16.53 ? 223 GLN A O 1 ATOM 1705 C CB . GLN A 1 223 ? 136.070 128.030 42.997 1.00 17.23 ? 223 GLN A CB 1 ATOM 1706 C CG . GLN A 1 223 ? 135.462 129.439 42.793 1.00 16.16 ? 223 GLN A CG 1 ATOM 1707 C CD . GLN A 1 223 ? 134.242 129.466 41.873 1.00 22.06 ? 223 GLN A CD 1 ATOM 1708 O OE1 . GLN A 1 223 ? 133.989 130.469 41.204 1.00 22.81 ? 223 GLN A OE1 1 ATOM 1709 N NE2 . GLN A 1 223 ? 133.478 128.374 41.846 1.00 16.95 ? 223 GLN A NE2 1 ATOM 1710 N N . SER A 1 224 ? 138.277 126.335 45.226 1.00 18.38 ? 224 SER A N 1 ATOM 1711 C CA . SER A 1 224 ? 138.711 124.970 45.611 1.00 19.90 ? 224 SER A CA 1 ATOM 1712 C C . SER A 1 224 ? 139.884 124.390 44.789 1.00 21.49 ? 224 SER A C 1 ATOM 1713 O O . SER A 1 224 ? 139.841 123.218 44.370 1.00 17.38 ? 224 SER A O 1 ATOM 1714 C CB . SER A 1 224 ? 137.544 123.956 45.565 1.00 16.31 ? 224 SER A CB 1 ATOM 1715 O OG . SER A 1 224 ? 136.431 124.362 46.372 1.00 17.64 ? 224 SER A OG 1 ATOM 1716 N N . GLY A 1 225 ? 140.933 125.173 44.561 1.00 17.84 ? 225 GLY A N 1 ATOM 1717 C CA . GLY A 1 225 ? 142.100 124.616 43.882 1.00 21.29 ? 225 GLY A CA 1 ATOM 1718 C C . GLY A 1 225 ? 143.229 125.611 43.690 1.00 21.98 ? 225 GLY A C 1 ATOM 1719 O O . GLY A 1 225 ? 142.993 126.821 43.623 1.00 20.65 ? 225 GLY A O 1 ATOM 1720 N N . SER A 1 226 ? 144.457 125.105 43.605 1.00 18.70 ? 226 SER A N 1 ATOM 1721 C CA . SER A 1 226 ? 145.619 125.945 43.306 1.00 17.69 ? 226 SER A CA 1 ATOM 1722 C C . SER A 1 226 ? 146.760 125.011 42.894 1.00 24.10 ? 226 SER A C 1 ATOM 1723 O O . SER A 1 226 ? 146.727 123.826 43.238 1.00 21.14 ? 226 SER A O 1 ATOM 1724 C CB . SER A 1 226 ? 145.989 126.825 44.524 1.00 17.00 ? 226 SER A CB 1 ATOM 1725 O OG . SER A 1 226 ? 146.188 126.035 45.705 1.00 17.71 ? 226 SER A OG 1 ATOM 1726 N N . PHE A 1 227 ? 147.757 125.507 42.157 1.00 20.72 ? 227 PHE A N 1 ATOM 1727 C CA . PHE A 1 227 ? 148.781 124.593 41.621 1.00 23.21 ? 227 PHE A CA 1 ATOM 1728 C C . PHE A 1 227 ? 149.609 123.902 42.706 1.00 29.00 ? 227 PHE A C 1 ATOM 1729 O O . PHE A 1 227 ? 150.198 122.853 42.462 1.00 32.13 ? 227 PHE A O 1 ATOM 1730 C CB . PHE A 1 227 ? 149.738 125.316 40.665 1.00 27.40 ? 227 PHE A CB 1 ATOM 1731 C CG . PHE A 1 227 ? 150.694 126.224 41.355 1.00 32.54 ? 227 PHE A CG 1 ATOM 1732 C CD1 . PHE A 1 227 ? 151.845 125.726 41.961 1.00 40.69 ? 227 PHE A CD1 1 ATOM 1733 C CD2 . PHE A 1 227 ? 150.455 127.582 41.399 1.00 31.99 ? 227 PHE A CD2 1 ATOM 1734 C CE1 . PHE A 1 227 ? 152.706 126.567 42.617 1.00 44.24 ? 227 PHE A CE1 1 ATOM 1735 C CE2 . PHE A 1 227 ? 151.325 128.423 42.036 1.00 39.16 ? 227 PHE A CE2 1 ATOM 1736 C CZ . PHE A 1 227 ? 152.452 127.917 42.647 1.00 40.57 ? 227 PHE A CZ 1 ATOM 1737 N N . ASN A 1 228 ? 149.700 124.510 43.887 1.00 19.45 ? 228 ASN A N 1 ATOM 1738 C CA . ASN A 1 228 ? 150.512 123.928 44.957 1.00 20.60 ? 228 ASN A CA 1 ATOM 1739 C C . ASN A 1 228 ? 149.800 122.764 45.661 1.00 22.40 ? 228 ASN A C 1 ATOM 1740 O O . ASN A 1 228 ? 150.329 122.187 46.602 1.00 20.18 ? 228 ASN A O 1 ATOM 1741 C CB . ASN A 1 228 ? 150.949 125.010 45.962 1.00 18.12 ? 228 ASN A CB 1 ATOM 1742 C CG . ASN A 1 228 ? 149.762 125.759 46.574 1.00 22.82 ? 228 ASN A CG 1 ATOM 1743 O OD1 . ASN A 1 228 ? 148.782 126.079 45.889 1.00 25.69 ? 228 ASN A OD1 1 ATOM 1744 N ND2 . ASN A 1 228 ? 149.846 126.033 47.869 1.00 18.12 ? 228 ASN A ND2 1 ATOM 1745 N N . ALA A 1 229 ? 148.600 122.413 45.206 1.00 19.93 ? 229 ALA A N 1 ATOM 1746 C CA . ALA A 1 229 ? 147.926 121.235 45.739 1.00 24.65 ? 229 ALA A CA 1 ATOM 1747 C C . ALA A 1 229 ? 148.739 120.002 45.334 1.00 26.34 ? 229 ALA A C 1 ATOM 1748 O O . ALA A 1 229 ? 149.314 119.978 44.243 1.00 25.02 ? 229 ALA A O 1 ATOM 1749 C CB . ALA A 1 229 ? 146.499 121.153 45.190 1.00 20.51 ? 229 ALA A CB 1 ATOM 1750 N N . PRO A 1 230 ? 148.791 118.974 46.204 1.00 22.32 ? 230 PRO A N 1 ATOM 1751 C CA . PRO A 1 230 ? 149.672 117.833 45.904 1.00 26.90 ? 230 PRO A CA 1 ATOM 1752 C C . PRO A 1 230 ? 149.307 117.054 44.628 1.00 31.56 ? 230 PRO A C 1 ATOM 1753 O O . PRO A 1 230 ? 150.189 116.367 44.097 1.00 27.23 ? 230 PRO A O 1 ATOM 1754 C CB . PRO A 1 230 ? 149.539 116.932 47.149 1.00 27.62 ? 230 PRO A CB 1 ATOM 1755 C CG . PRO A 1 230 ? 148.215 117.298 47.765 1.00 31.46 ? 230 PRO A CG 1 ATOM 1756 C CD . PRO A 1 230 ? 148.016 118.778 47.447 1.00 26.03 ? 230 PRO A CD 1 ATOM 1757 N N . TRP A 1 231 ? 148.063 117.158 44.145 1.00 26.45 ? 231 TRP A N 1 ATOM 1758 C CA . TRP A 1 231 ? 147.638 116.440 42.923 1.00 22.72 ? 231 TRP A CA 1 ATOM 1759 C C . TRP A 1 231 ? 147.852 117.238 41.628 1.00 22.62 ? 231 TRP A C 1 ATOM 1760 O O . TRP A 1 231 ? 147.656 116.701 40.531 1.00 24.54 ? 231 TRP A O 1 ATOM 1761 C CB . TRP A 1 231 ? 146.145 116.058 43.003 1.00 22.03 ? 231 TRP A CB 1 ATOM 1762 C CG . TRP A 1 231 ? 145.283 117.243 43.459 1.00 25.52 ? 231 TRP A CG 1 ATOM 1763 C CD1 . TRP A 1 231 ? 144.891 117.523 44.742 1.00 24.74 ? 231 TRP A CD1 1 ATOM 1764 C CD2 . TRP A 1 231 ? 144.743 118.295 42.638 1.00 20.59 ? 231 TRP A CD2 1 ATOM 1765 N NE1 . TRP A 1 231 ? 144.128 118.681 44.769 1.00 23.29 ? 231 TRP A NE1 1 ATOM 1766 C CE2 . TRP A 1 231 ? 144.022 119.170 43.493 1.00 21.76 ? 231 TRP A CE2 1 ATOM 1767 C CE3 . TRP A 1 231 ? 144.783 118.575 41.269 1.00 21.84 ? 231 TRP A CE3 1 ATOM 1768 C CZ2 . TRP A 1 231 ? 143.365 120.322 43.019 1.00 21.98 ? 231 TRP A CZ2 1 ATOM 1769 C CZ3 . TRP A 1 231 ? 144.114 119.725 40.796 1.00 21.57 ? 231 TRP A CZ3 1 ATOM 1770 C CH2 . TRP A 1 231 ? 143.424 120.578 41.673 1.00 18.98 ? 231 TRP A CH2 1 ATOM 1771 N N . ALA A 1 232 ? 148.245 118.507 41.743 1.00 27.34 ? 232 ALA A N 1 ATOM 1772 C CA . ALA A 1 232 ? 148.159 119.445 40.609 1.00 26.38 ? 232 ALA A CA 1 ATOM 1773 C C . ALA A 1 232 ? 149.318 119.463 39.586 1.00 29.59 ? 232 ALA A C 1 ATOM 1774 O O . ALA A 1 232 ? 149.104 119.766 38.406 1.00 28.48 ? 232 ALA A O 1 ATOM 1775 C CB . ALA A 1 232 ? 147.907 120.870 41.131 1.00 30.65 ? 232 ALA A CB 1 ATOM 1776 N N . VAL A 1 233 ? 150.540 119.188 40.026 1.00 28.51 ? 233 VAL A N 1 ATOM 1777 C CA . VAL A 1 233 ? 151.676 119.210 39.108 1.00 33.99 ? 233 VAL A CA 1 ATOM 1778 C C . VAL A 1 233 ? 152.433 117.883 39.154 1.00 39.05 ? 233 VAL A C 1 ATOM 1779 O O . VAL A 1 233 ? 152.776 117.405 40.232 1.00 33.45 ? 233 VAL A O 1 ATOM 1780 C CB . VAL A 1 233 ? 152.664 120.353 39.453 1.00 32.89 ? 233 VAL A CB 1 ATOM 1781 C CG1 . VAL A 1 233 ? 153.853 120.330 38.508 1.00 32.27 ? 233 VAL A CG1 1 ATOM 1782 C CG2 . VAL A 1 233 ? 151.949 121.715 39.417 1.00 29.59 ? 233 VAL A CG2 1 ATOM 1783 N N . THR A 1 234 ? 152.680 117.299 37.984 1.00 31.36 ? 234 THR A N 1 ATOM 1784 C CA . THR A 1 234 ? 153.418 116.038 37.866 1.00 40.96 ? 234 THR A CA 1 ATOM 1785 C C . THR A 1 234 ? 154.908 116.326 37.655 1.00 40.86 ? 234 THR A C 1 ATOM 1786 O O . THR A 1 234 ? 155.261 117.195 36.855 1.00 42.82 ? 234 THR A O 1 ATOM 1787 C CB . THR A 1 234 ? 152.905 115.218 36.667 1.00 41.51 ? 234 THR A CB 1 ATOM 1788 O OG1 . THR A 1 234 ? 151.481 115.060 36.758 1.00 43.96 ? 234 THR A OG1 1 ATOM 1789 C CG2 . THR A 1 234 ? 153.569 113.846 36.619 1.00 47.82 ? 234 THR A CG2 1 ATOM 1790 N N . SER A 1 235 ? 155.780 115.621 38.374 1.00 43.65 ? 235 SER A N 1 ATOM 1791 C CA . SER A 1 235 ? 157.229 115.815 38.220 1.00 48.28 ? 235 SER A CA 1 ATOM 1792 C C . SER A 1 235 ? 157.756 115.229 36.903 1.00 42.53 ? 235 SER A C 1 ATOM 1793 O O . SER A 1 235 ? 157.121 114.360 36.307 1.00 43.54 ? 235 SER A O 1 ATOM 1794 C CB . SER A 1 235 ? 157.984 115.174 39.384 1.00 53.49 ? 235 SER A CB 1 ATOM 1795 O OG . SER A 1 235 ? 157.968 113.762 39.270 1.00 55.42 ? 235 SER A OG 1 ATOM 1796 N N . LEU A 1 236 ? 158.915 115.702 36.453 1.00 44.09 ? 236 LEU A N 1 ATOM 1797 C CA . LEU A 1 236 ? 159.510 115.191 35.215 1.00 55.03 ? 236 LEU A CA 1 ATOM 1798 C C . LEU A 1 236 ? 159.774 113.689 35.288 1.00 53.79 ? 236 LEU A C 1 ATOM 1799 O O . LEU A 1 236 ? 159.551 112.967 34.318 1.00 51.65 ? 236 LEU A O 1 ATOM 1800 C CB . LEU A 1 236 ? 160.796 115.948 34.867 1.00 58.02 ? 236 LEU A CB 1 ATOM 1801 C CG . LEU A 1 236 ? 160.683 116.902 33.672 1.00 59.93 ? 236 LEU A CG 1 ATOM 1802 C CD1 . LEU A 1 236 ? 159.280 117.526 33.574 1.00 48.95 ? 236 LEU A CD1 1 ATOM 1803 C CD2 . LEU A 1 236 ? 161.747 117.990 33.764 1.00 65.31 ? 236 LEU A CD2 1 ATOM 1804 N N . TYR A 1 237 ? 160.234 113.239 36.451 1.00 58.11 ? 237 TYR A N 1 ATOM 1805 C CA . TYR A 1 237 ? 160.447 111.823 36.727 1.00 68.47 ? 237 TYR A CA 1 ATOM 1806 C C . TYR A 1 237 ? 159.155 111.009 36.571 1.00 62.94 ? 237 TYR A C 1 ATOM 1807 O O . TYR A 1 237 ? 159.124 110.021 35.832 1.00 55.63 ? 237 TYR A O 1 ATOM 1808 C CB . TYR A 1 237 ? 161.046 111.660 38.131 1.00 82.20 ? 237 TYR A CB 1 ATOM 1809 C CG . TYR A 1 237 ? 161.035 110.249 38.684 1.00 97.83 ? 237 TYR A CG 1 ATOM 1810 C CD1 . TYR A 1 237 ? 161.888 109.271 38.179 1.00 106.66 ? 237 TYR A CD1 1 ATOM 1811 C CD2 . TYR A 1 237 ? 160.186 109.900 39.729 1.00 103.64 ? 237 TYR A CD2 1 ATOM 1812 C CE1 . TYR A 1 237 ? 161.882 107.980 38.691 1.00 112.26 ? 237 TYR A CE1 1 ATOM 1813 C CE2 . TYR A 1 237 ? 160.174 108.613 40.247 1.00 109.31 ? 237 TYR A CE2 1 ATOM 1814 C CZ . TYR A 1 237 ? 161.023 107.658 39.724 1.00 113.29 ? 237 TYR A CZ 1 ATOM 1815 O OH . TYR A 1 237 ? 161.014 106.380 40.235 1.00 118.21 ? 237 TYR A OH 1 ATOM 1816 N N . GLU A 1 238 ? 158.092 111.428 37.252 1.00 46.15 ? 238 GLU A N 1 ATOM 1817 C CA . GLU A 1 238 ? 156.819 110.726 37.158 1.00 52.66 ? 238 GLU A CA 1 ATOM 1818 C C . GLU A 1 238 ? 156.307 110.711 35.719 1.00 50.47 ? 238 GLU A C 1 ATOM 1819 O O . GLU A 1 238 ? 155.870 109.674 35.219 1.00 45.91 ? 238 GLU A O 1 ATOM 1820 C CB . GLU A 1 238 ? 155.767 111.376 38.060 1.00 58.81 ? 238 GLU A CB 1 ATOM 1821 C CG . GLU A 1 238 ? 156.010 111.230 39.552 1.00 68.73 ? 238 GLU A CG 1 ATOM 1822 C CD . GLU A 1 238 ? 155.131 112.170 40.373 1.00 71.44 ? 238 GLU A CD 1 ATOM 1823 O OE1 . GLU A 1 238 ? 154.844 113.292 39.895 1.00 64.53 ? 238 GLU A OE1 1 ATOM 1824 O OE2 . GLU A 1 238 ? 154.725 111.787 41.494 1.00 74.84 ? 238 GLU A OE2 1 ATOM 1825 N N . ALA A 1 239 ? 156.354 111.866 35.058 1.00 51.07 ? 239 ALA A N 1 ATOM 1826 C CA . ALA A 1 239 ? 155.823 111.987 33.698 1.00 47.21 ? 239 ALA A CA 1 ATOM 1827 C C . ALA A 1 239 ? 156.511 111.045 32.707 1.00 48.15 ? 239 ALA A C 1 ATOM 1828 O O . ALA A 1 239 ? 155.849 110.424 31.871 1.00 47.47 ? 239 ALA A O 1 ATOM 1829 C CB . ALA A 1 239 ? 155.909 113.430 33.214 1.00 39.69 ? 239 ALA A CB 1 ATOM 1830 N N . ARG A 1 240 ? 157.836 110.944 32.795 1.00 45.00 ? 240 ARG A N 1 ATOM 1831 C CA . ARG A 1 240 ? 158.579 110.008 31.942 1.00 47.72 ? 240 ARG A CA 1 ATOM 1832 C C . ARG A 1 240 ? 158.180 108.546 32.179 1.00 48.79 ? 240 ARG A C 1 ATOM 1833 O O . ARG A 1 240 ? 157.866 107.833 31.226 1.00 57.57 ? 240 ARG A O 1 ATOM 1834 C CB . ARG A 1 240 ? 160.094 110.164 32.120 1.00 54.82 ? 240 ARG A CB 1 ATOM 1835 C CG . ARG A 1 240 ? 160.898 109.186 31.257 1.00 62.47 ? 240 ARG A CG 1 ATOM 1836 C CD . ARG A 1 240 ? 162.398 109.427 31.360 1.00 71.58 ? 240 ARG A CD 1 ATOM 1837 N NE . ARG A 1 240 ? 163.156 108.611 30.410 1.00 75.16 ? 240 ARG A NE 1 ATOM 1838 C CZ . ARG A 1 240 ? 163.309 108.917 29.124 1.00 76.09 ? 240 ARG A CZ 1 ATOM 1839 N NH1 . ARG A 1 240 ? 162.749 110.016 28.630 1.00 70.67 ? 240 ARG A NH1 1 ATOM 1840 N NH2 . ARG A 1 240 ? 164.019 108.123 28.331 1.00 81.05 ? 240 ARG A NH2 1 ATOM 1841 N N . ASN A 1 241 ? 158.194 108.107 33.441 1.00 57.65 ? 241 ASN A N 1 ATOM 1842 C CA . ASN A 1 241 ? 157.798 106.739 33.799 1.00 62.53 ? 241 ASN A CA 1 ATOM 1843 C C . ASN A 1 241 ? 156.379 106.421 33.319 1.00 56.82 ? 241 ASN A C 1 ATOM 1844 O O . ASN A 1 241 ? 156.099 105.296 32.896 1.00 54.74 ? 241 ASN A O 1 ATOM 1845 C CB . ASN A 1 241 ? 157.922 106.510 35.318 1.00 71.20 ? 241 ASN A CB 1 ATOM 1846 C CG . ASN A 1 241 ? 158.167 105.033 35.691 1.00 81.89 ? 241 ASN A CG 1 ATOM 1847 O OD1 . ASN A 1 241 ? 159.144 104.422 35.249 1.00 76.32 ? 241 ASN A OD1 1 ATOM 1848 N ND2 . ASN A 1 241 ? 157.293 104.477 36.541 1.00 99.24 ? 241 ASN A ND2 1 ATOM 1849 N N . ARG A 1 242 ? 155.494 107.419 33.362 1.00 47.82 ? 242 ARG A N 1 ATOM 1850 C CA . ARG A 1 242 ? 154.099 107.223 32.953 1.00 44.42 ? 242 ARG A CA 1 ATOM 1851 C C . ARG A 1 242 ? 153.920 107.160 31.429 1.00 45.48 ? 242 ARG A C 1 ATOM 1852 O O . ARG A 1 242 ? 153.161 106.328 30.917 1.00 43.12 ? 242 ARG A O 1 ATOM 1853 C CB . ARG A 1 242 ? 153.194 108.291 33.585 1.00 45.12 ? 242 ARG A CB 1 ATOM 1854 C CG . ARG A 1 242 ? 153.155 108.196 35.103 1.00 46.90 ? 242 ARG A CG 1 ATOM 1855 C CD . ARG A 1 242 ? 152.498 109.394 35.744 1.00 47.87 ? 242 ARG A CD 1 ATOM 1856 N NE . ARG A 1 242 ? 152.743 109.419 37.182 1.00 38.86 ? 242 ARG A NE 1 ATOM 1857 C CZ . ARG A 1 242 ? 152.129 110.238 38.030 1.00 43.99 ? 242 ARG A CZ 1 ATOM 1858 N NH1 . ARG A 1 242 ? 151.217 111.098 37.587 1.00 35.65 ? 242 ARG A NH1 1 ATOM 1859 N NH2 . ARG A 1 242 ? 152.420 110.195 39.325 1.00 41.24 ? 242 ARG A NH2 1 ATOM 1860 N N . THR A 1 243 ? 154.625 108.032 30.714 1.00 48.37 ? 243 THR A N 1 ATOM 1861 C CA . THR A 1 243 ? 154.654 107.992 29.253 1.00 48.67 ? 243 THR A CA 1 ATOM 1862 C C . THR A 1 243 ? 155.195 106.648 28.748 1.00 51.18 ? 243 THR A C 1 ATOM 1863 O O . THR A 1 243 ? 154.619 106.032 27.852 1.00 52.49 ? 243 THR A O 1 ATOM 1864 C CB . THR A 1 243 ? 155.502 109.145 28.681 1.00 47.86 ? 243 THR A CB 1 ATOM 1865 O OG1 . THR A 1 243 ? 154.792 110.380 28.832 1.00 44.75 ? 243 THR A OG1 1 ATOM 1866 C CG2 . THR A 1 243 ? 155.805 108.925 27.206 1.00 47.65 ? 243 THR A CG2 1 ATOM 1867 N N . LEU A 1 244 ? 156.295 106.191 29.334 1.00 50.93 ? 244 LEU A N 1 ATOM 1868 C CA . LEU A 1 244 ? 156.890 104.919 28.939 1.00 57.13 ? 244 LEU A CA 1 ATOM 1869 C C . LEU A 1 244 ? 156.002 103.736 29.305 1.00 55.26 ? 244 LEU A C 1 ATOM 1870 O O . LEU A 1 244 ? 155.917 102.758 28.561 1.00 54.36 ? 244 LEU A O 1 ATOM 1871 C CB . LEU A 1 244 ? 158.267 104.753 29.577 1.00 64.45 ? 244 LEU A CB 1 ATOM 1872 C CG . LEU A 1 244 ? 159.311 105.758 29.106 1.00 63.66 ? 244 LEU A CG 1 ATOM 1873 C CD1 . LEU A 1 244 ? 160.644 105.515 29.804 1.00 65.05 ? 244 LEU A CD1 1 ATOM 1874 C CD2 . LEU A 1 244 ? 159.449 105.670 27.594 1.00 64.26 ? 244 LEU A CD2 1 ATOM 1875 N N . ASN A 1 245 ? 155.350 103.828 30.460 1.00 52.92 ? 245 ASN A N 1 ATOM 1876 C CA . ASN A 1 245 ? 154.408 102.796 30.880 1.00 54.38 ? 245 ASN A CA 1 ATOM 1877 C C . ASN A 1 245 ? 153.226 102.703 29.918 1.00 51.53 ? 245 ASN A C 1 ATOM 1878 O O . ASN A 1 245 ? 152.818 101.602 29.538 1.00 55.19 ? 245 ASN A O 1 ATOM 1879 C CB . ASN A 1 245 ? 153.936 103.039 32.319 1.00 53.77 ? 245 ASN A CB 1 ATOM 1880 C CG . ASN A 1 245 ? 154.963 102.594 33.353 1.00 58.13 ? 245 ASN A CG 1 ATOM 1881 O OD1 . ASN A 1 245 ? 156.021 102.065 33.006 1.00 62.91 ? 245 ASN A OD1 1 ATOM 1882 N ND2 . ASN A 1 245 ? 154.658 102.821 34.630 1.00 53.92 ? 245 ASN A ND2 1 ATOM 1883 N N . LEU A 1 246 ? 152.694 103.859 29.519 1.00 47.01 ? 246 LEU A N 1 ATOM 1884 C CA . LEU A 1 246 ? 151.639 103.912 28.511 1.00 55.22 ? 246 LEU A CA 1 ATOM 1885 C C . LEU A 1 246 ? 152.068 103.249 27.195 1.00 58.50 ? 246 LEU A C 1 ATOM 1886 O O . LEU A 1 246 ? 151.315 102.459 26.618 1.00 54.98 ? 246 LEU A O 1 ATOM 1887 C CB . LEU A 1 246 ? 151.209 105.356 28.251 1.00 49.37 ? 246 LEU A CB 1 ATOM 1888 C CG . LEU A 1 246 ? 150.009 105.482 27.313 1.00 50.03 ? 246 LEU A CG 1 ATOM 1889 C CD1 . LEU A 1 246 ? 148.815 104.736 27.901 1.00 41.88 ? 246 LEU A CD1 1 ATOM 1890 C CD2 . LEU A 1 246 ? 149.663 106.949 27.042 1.00 39.31 ? 246 LEU A CD2 1 ATOM 1891 N N . ALA A 1 247 ? 153.276 103.571 26.732 1.00 49.05 ? 247 ALA A N 1 ATOM 1892 C CA . ALA A 1 247 ? 153.825 102.975 25.515 1.00 51.45 ? 247 ALA A CA 1 ATOM 1893 C C . ALA A 1 247 ? 153.884 101.458 25.614 1.00 63.33 ? 247 ALA A C 1 ATOM 1894 O O . ALA A 1 247 ? 153.561 100.751 24.655 1.00 65.87 ? 247 ALA A O 1 ATOM 1895 C CB . ALA A 1 247 ? 155.210 103.526 25.236 1.00 58.41 ? 247 ALA A CB 1 ATOM 1896 N N . LYS A 1 248 ? 154.311 100.958 26.768 1.00 55.85 ? 248 LYS A N 1 ATOM 1897 C CA . LYS A 1 248 ? 154.431 99.516 26.954 1.00 62.02 ? 248 LYS A CA 1 ATOM 1898 C C . LYS A 1 248 ? 153.060 98.852 26.877 1.00 58.89 ? 248 LYS A C 1 ATOM 1899 O O . LYS A 1 248 ? 152.865 97.900 26.125 1.00 61.20 ? 248 LYS A O 1 ATOM 1900 C CB . LYS A 1 248 ? 155.119 99.193 28.284 1.00 61.45 ? 248 LYS A CB 1 ATOM 1901 C CG . LYS A 1 248 ? 155.368 97.712 28.496 1.00 65.11 ? 248 LYS A CG 1 ATOM 1902 C CD . LYS A 1 248 ? 156.181 97.439 29.753 1.00 77.11 ? 248 LYS A CD 1 ATOM 1903 C CE . LYS A 1 248 ? 156.767 96.027 29.716 1.00 77.57 ? 248 LYS A CE 1 ATOM 1904 N NZ . LYS A 1 248 ? 155.704 95.012 29.488 1.00 78.68 ? 248 LYS A NZ 1 ATOM 1905 N N . LEU A 1 249 ? 152.107 99.391 27.633 1.00 57.88 ? 249 LEU A N 1 ATOM 1906 C CA . LEU A 1 249 ? 150.754 98.840 27.689 1.00 56.03 ? 249 LEU A CA 1 ATOM 1907 C C . LEU A 1 249 ? 150.054 98.800 26.331 1.00 63.00 ? 249 LEU A C 1 ATOM 1908 O O . LEU A 1 249 ? 149.170 97.972 26.109 1.00 58.06 ? 249 LEU A O 1 ATOM 1909 C CB . LEU A 1 249 ? 149.910 99.630 28.687 1.00 53.14 ? 249 LEU A CB 1 ATOM 1910 C CG . LEU A 1 249 ? 150.380 99.548 30.139 1.00 53.67 ? 249 LEU A CG 1 ATOM 1911 C CD1 . LEU A 1 249 ? 149.650 100.561 31.007 1.00 52.92 ? 249 LEU A CD1 1 ATOM 1912 C CD2 . LEU A 1 249 ? 150.184 98.147 30.680 1.00 57.04 ? 249 LEU A CD2 1 ATOM 1913 N N . THR A 1 250 ? 150.458 99.688 25.427 1.00 54.44 ? 250 THR A N 1 ATOM 1914 C CA . THR A 1 250 ? 149.834 99.787 24.112 1.00 60.62 ? 250 THR A CA 1 ATOM 1915 C C . THR A 1 250 ? 150.691 99.158 23.012 1.00 63.82 ? 250 THR A C 1 ATOM 1916 O O . THR A 1 250 ? 150.331 99.200 21.834 1.00 66.43 ? 250 THR A O 1 ATOM 1917 C CB . THR A 1 250 ? 149.537 101.255 23.751 1.00 57.65 ? 250 THR A CB 1 ATOM 1918 O OG1 . THR A 1 250 ? 150.747 102.019 23.829 1.00 50.57 ? 250 THR A OG1 1 ATOM 1919 C CG2 . THR A 1 250 ? 148.519 101.842 24.712 1.00 51.54 ? 250 THR A CG2 1 ATOM 1920 N N . GLY A 1 251 ? 151.823 98.575 23.395 1.00 65.66 ? 251 GLY A N 1 ATOM 1921 C CA . GLY A 1 251 ? 152.718 97.948 22.434 1.00 67.73 ? 251 GLY A CA 1 ATOM 1922 C C . GLY A 1 251 ? 153.503 98.946 21.598 1.00 67.60 ? 251 GLY A C 1 ATOM 1923 O O . GLY A 1 251 ? 153.861 98.660 20.453 1.00 67.31 ? 251 GLY A O 1 ATOM 1924 N N . CYS A 1 252 ? 153.782 100.109 22.181 1.00 59.16 ? 252 CYS A N 1 ATOM 1925 C CA . CYS A 1 252 ? 154.458 101.195 21.477 1.00 60.71 ? 252 CYS A CA 1 ATOM 1926 C C . CYS A 1 252 ? 155.852 101.491 22.014 1.00 65.13 ? 252 CYS A C 1 ATOM 1927 O O . CYS A 1 252 ? 156.454 102.510 21.665 1.00 58.90 ? 252 CYS A O 1 ATOM 1928 C CB . CYS A 1 252 ? 153.622 102.473 21.546 1.00 54.63 ? 252 CYS A CB 1 ATOM 1929 S SG . CYS A 1 252 ? 152.209 102.456 20.447 1.00 53.88 ? 252 CYS A SG 1 ATOM 1930 N N . SER A 1 253 ? 156.359 100.616 22.875 1.00 67.67 ? 253 SER A N 1 ATOM 1931 C CA . SER A 1 253 ? 157.722 100.763 23.375 1.00 72.03 ? 253 SER A CA 1 ATOM 1932 C C . SER A 1 253 ? 158.717 100.732 22.218 1.00 71.25 ? 253 SER A C 1 ATOM 1933 O O . SER A 1 253 ? 158.809 99.744 21.498 1.00 74.56 ? 253 SER A O 1 ATOM 1934 C CB . SER A 1 253 ? 158.048 99.669 24.394 1.00 73.74 ? 253 SER A CB 1 ATOM 1935 O OG . SER A 1 253 ? 157.216 99.786 25.539 1.00 71.30 ? 253 SER A OG 1 ATOM 1936 N N . ARG A 1 254 ? 159.430 101.836 22.025 1.00 74.43 ? 254 ARG A N 1 ATOM 1937 C CA . ARG A 1 254 ? 160.454 101.923 20.987 1.00 78.85 ? 254 ARG A CA 1 ATOM 1938 C C . ARG A 1 254 ? 161.715 102.533 21.596 1.00 82.43 ? 254 ARG A C 1 ATOM 1939 O O . ARG A 1 254 ? 161.765 102.793 22.798 1.00 80.30 ? 254 ARG A O 1 ATOM 1940 C CB . ARG A 1 254 ? 159.970 102.783 19.812 1.00 76.57 ? 254 ARG A CB 1 ATOM 1941 C CG . ARG A 1 254 ? 158.637 102.357 19.195 1.00 73.97 ? 254 ARG A CG 1 ATOM 1942 C CD . ARG A 1 254 ? 158.775 101.120 18.302 1.00 76.67 ? 254 ARG A CD 1 ATOM 1943 N NE . ARG A 1 254 ? 157.517 100.818 17.620 1.00 75.85 ? 254 ARG A NE 1 ATOM 1944 C CZ . ARG A 1 254 ? 156.559 100.040 18.119 1.00 72.38 ? 254 ARG A CZ 1 ATOM 1945 N NH1 . ARG A 1 254 ? 156.713 99.470 19.307 1.00 71.26 ? 254 ARG A NH1 1 ATOM 1946 N NH2 . ARG A 1 254 ? 155.446 99.830 17.431 1.00 66.41 ? 254 ARG A NH2 1 ATOM 1947 N N . GLU A 1 255 ? 162.729 102.763 20.766 1.00 86.46 ? 255 GLU A N 1 ATOM 1948 C CA . GLU A 1 255 ? 163.975 103.383 21.220 1.00 91.07 ? 255 GLU A CA 1 ATOM 1949 C C . GLU A 1 255 ? 164.100 104.847 20.771 1.00 88.33 ? 255 GLU A C 1 ATOM 1950 O O . GLU A 1 255 ? 164.665 105.674 21.489 1.00 88.18 ? 255 GLU A O 1 ATOM 1951 C CB . GLU A 1 255 ? 165.198 102.559 20.795 1.00 104.72 ? 255 GLU A CB 1 ATOM 1952 C CG . GLU A 1 255 ? 165.473 102.525 19.293 1.00 114.03 ? 255 GLU A CG 1 ATOM 1953 C CD . GLU A 1 255 ? 164.282 102.042 18.480 1.00 115.23 ? 255 GLU A CD 1 ATOM 1954 O OE1 . GLU A 1 255 ? 163.927 100.848 18.585 1.00 118.79 ? 255 GLU A OE1 1 ATOM 1955 O OE2 . GLU A 1 255 ? 163.686 102.867 17.754 1.00 110.05 ? 255 GLU A OE2 1 ATOM 1956 N N . ASN A 1 256 ? 163.579 105.163 19.587 1.00 86.33 ? 256 ASN A N 1 ATOM 1957 C CA . ASN A 1 256 ? 163.422 106.554 19.172 1.00 87.38 ? 256 ASN A CA 1 ATOM 1958 C C . ASN A 1 256 ? 162.151 107.072 19.839 1.00 79.89 ? 256 ASN A C 1 ATOM 1959 O O . ASN A 1 256 ? 161.052 106.602 19.534 1.00 73.57 ? 256 ASN A O 1 ATOM 1960 C CB . ASN A 1 256 ? 163.330 106.658 17.640 1.00 99.53 ? 256 ASN A CB 1 ATOM 1961 C CG . ASN A 1 256 ? 163.479 108.092 17.122 1.00 113.41 ? 256 ASN A CG 1 ATOM 1962 O OD1 . ASN A 1 256 ? 162.894 109.031 17.667 1.00 110.27 ? 256 ASN A OD1 1 ATOM 1963 N ND2 . ASN A 1 256 ? 164.267 108.256 16.053 1.00 132.73 ? 256 ASN A ND2 1 ATOM 1964 N N . GLU A 1 257 ? 162.300 108.013 20.771 1.00 73.73 ? 257 GLU A N 1 ATOM 1965 C CA . GLU A 1 257 ? 161.153 108.514 21.524 1.00 67.83 ? 257 GLU A CA 1 ATOM 1966 C C . GLU A 1 257 ? 160.100 109.093 20.595 1.00 63.53 ? 257 GLU A C 1 ATOM 1967 O O . GLU A 1 257 ? 158.903 108.988 20.861 1.00 59.87 ? 257 GLU A O 1 ATOM 1968 C CB . GLU A 1 257 ? 161.574 109.563 22.556 1.00 71.09 ? 257 GLU A CB 1 ATOM 1969 C CG . GLU A 1 257 ? 162.389 109.007 23.716 1.00 76.55 ? 257 GLU A CG 1 ATOM 1970 C CD . GLU A 1 257 ? 162.669 110.053 24.778 1.00 71.46 ? 257 GLU A CD 1 ATOM 1971 O OE1 . GLU A 1 257 ? 162.546 111.260 24.474 1.00 63.58 ? 257 GLU A OE1 1 ATOM 1972 O OE2 . GLU A 1 257 ? 163.005 109.665 25.918 1.00 74.45 ? 257 GLU A OE2 1 ATOM 1973 N N . THR A 1 258 ? 160.550 109.694 19.499 1.00 64.92 ? 258 THR A N 1 ATOM 1974 C CA . THR A 1 258 ? 159.629 110.228 18.505 1.00 68.26 ? 258 THR A CA 1 ATOM 1975 C C . THR A 1 258 ? 158.843 109.090 17.849 1.00 64.93 ? 258 THR A C 1 ATOM 1976 O O . THR A 1 258 ? 157.674 109.259 17.498 1.00 55.80 ? 258 THR A O 1 ATOM 1977 C CB . THR A 1 258 ? 160.363 111.076 17.450 1.00 76.47 ? 258 THR A CB 1 ATOM 1978 O OG1 . THR A 1 258 ? 161.259 111.979 18.111 1.00 79.25 ? 258 THR A OG1 1 ATOM 1979 C CG2 . THR A 1 258 ? 159.367 111.879 16.621 1.00 77.83 ? 258 THR A CG2 1 ATOM 1980 N N . GLU A 1 259 ? 159.480 107.926 17.709 1.00 63.31 ? 259 GLU A N 1 ATOM 1981 C CA . GLU A 1 259 ? 158.800 106.738 17.184 1.00 61.23 ? 259 GLU A CA 1 ATOM 1982 C C . GLU A 1 259 ? 157.732 106.202 18.136 1.00 58.67 ? 259 GLU A C 1 ATOM 1983 O O . GLU A 1 259 ? 156.708 105.686 17.690 1.00 58.02 ? 259 GLU A O 1 ATOM 1984 C CB . GLU A 1 259 ? 159.793 105.621 16.866 1.00 65.22 ? 259 GLU A CB 1 ATOM 1985 C CG . GLU A 1 259 ? 160.513 105.768 15.550 1.00 85.40 ? 259 GLU A CG 1 ATOM 1986 C CD . GLU A 1 259 ? 161.336 104.539 15.228 1.00 92.57 ? 259 GLU A CD 1 ATOM 1987 O OE1 . GLU A 1 259 ? 160.950 103.439 15.680 1.00 94.84 ? 259 GLU A OE1 1 ATOM 1988 O OE2 . GLU A 1 259 ? 162.365 104.668 14.530 1.00 97.71 ? 259 GLU A OE2 1 ATOM 1989 N N . ILE A 1 260 ? 157.980 106.295 19.439 1.00 57.61 ? 260 ILE A N 1 ATOM 1990 C CA . ILE A 1 260 ? 156.942 105.998 20.422 1.00 58.59 ? 260 ILE A CA 1 ATOM 1991 C C . ILE A 1 260 ? 155.696 106.839 20.133 1.00 59.09 ? 260 ILE A C 1 ATOM 1992 O O . ILE A 1 260 ? 154.589 106.308 20.028 1.00 51.15 ? 260 ILE A O 1 ATOM 1993 C CB . ILE A 1 260 ? 157.414 106.274 21.868 1.00 56.88 ? 260 ILE A CB 1 ATOM 1994 C CG1 . ILE A 1 260 ? 158.577 105.353 22.245 1.00 63.43 ? 260 ILE A CG1 1 ATOM 1995 C CG2 . ILE A 1 260 ? 156.264 106.103 22.849 1.00 51.65 ? 260 ILE A CG2 1 ATOM 1996 C CD1 . ILE A 1 260 ? 159.127 105.608 23.637 1.00 64.69 ? 260 ILE A CD1 1 ATOM 1997 N N . ILE A 1 261 ? 155.891 108.149 19.990 1.00 61.53 ? 261 ILE A N 1 ATOM 1998 C CA . ILE A 1 261 ? 154.790 109.074 19.731 1.00 58.23 ? 261 ILE A CA 1 ATOM 1999 C C . ILE A 1 261 ? 154.040 108.719 18.451 1.00 49.24 ? 261 ILE A C 1 ATOM 2000 O O . ILE A 1 261 ? 152.808 108.757 18.416 1.00 47.70 ? 261 ILE A O 1 ATOM 2001 C CB . ILE A 1 261 ? 155.272 110.535 19.623 1.00 55.62 ? 261 ILE A CB 1 ATOM 2002 C CG1 . ILE A 1 261 ? 156.025 110.950 20.887 1.00 48.18 ? 261 ILE A CG1 1 ATOM 2003 C CG2 . ILE A 1 261 ? 154.085 111.460 19.371 1.00 45.72 ? 261 ILE A CG2 1 ATOM 2004 C CD1 . ILE A 1 261 ? 155.218 110.756 22.146 1.00 44.97 ? 261 ILE A CD1 1 ATOM 2005 N N . LYS A 1 262 ? 154.783 108.381 17.401 1.00 51.98 ? 262 LYS A N 1 ATOM 2006 C CA . LYS A 1 262 ? 154.166 107.978 16.140 1.00 53.28 ? 262 LYS A CA 1 ATOM 2007 C C . LYS A 1 262 ? 153.257 106.765 16.349 1.00 56.21 ? 262 LYS A C 1 ATOM 2008 O O . LYS A 1 262 ? 152.116 106.742 15.873 1.00 54.54 ? 262 LYS A O 1 ATOM 2009 C CB . LYS A 1 262 ? 155.229 107.685 15.076 1.00 56.66 ? 262 LYS A CB 1 ATOM 2010 C CG . LYS A 1 262 ? 154.821 108.109 13.657 1.00 77.06 ? 262 LYS A CG 1 ATOM 2011 C CD . LYS A 1 262 ? 155.751 107.527 12.588 1.00 78.96 ? 262 LYS A CD 1 ATOM 2012 C CE . LYS A 1 262 ? 155.533 108.169 11.214 1.00 81.24 ? 262 LYS A CE 1 ATOM 2013 N NZ . LYS A 1 262 ? 156.078 109.561 11.132 1.00 80.22 ? 262 LYS A NZ 1 ATOM 2014 N N . CYS A 1 263 ? 153.761 105.771 17.078 1.00 56.43 ? 263 CYS A N 1 ATOM 2015 C CA . CYS A 1 263 ? 152.995 104.563 17.377 1.00 58.25 ? 263 CYS A CA 1 ATOM 2016 C C . CYS A 1 263 ? 151.713 104.892 18.152 1.00 51.74 ? 263 CYS A C 1 ATOM 2017 O O . CYS A 1 263 ? 150.642 104.347 17.870 1.00 51.93 ? 263 CYS A O 1 ATOM 2018 C CB . CYS A 1 263 ? 153.863 103.573 18.163 1.00 56.30 ? 263 CYS A CB 1 ATOM 2019 S SG . CYS A 1 263 ? 153.048 102.014 18.636 1.00 57.93 ? 263 CYS A SG 1 ATOM 2020 N N . LEU A 1 264 ? 151.828 105.790 19.128 1.00 49.40 ? 264 LEU A N 1 ATOM 2021 C CA . LEU A 1 264 ? 150.676 106.189 19.937 1.00 48.70 ? 264 LEU A CA 1 ATOM 2022 C C . LEU A 1 264 ? 149.623 106.935 19.119 1.00 48.32 ? 264 LEU A C 1 ATOM 2023 O O . LEU A 1 264 ? 148.431 106.875 19.427 1.00 48.16 ? 264 LEU A O 1 ATOM 2024 C CB . LEU A 1 264 ? 151.119 107.020 21.141 1.00 44.87 ? 264 LEU A CB 1 ATOM 2025 C CG . LEU A 1 264 ? 151.703 106.175 22.275 1.00 63.78 ? 264 LEU A CG 1 ATOM 2026 C CD1 . LEU A 1 264 ? 152.485 107.033 23.246 1.00 44.44 ? 264 LEU A CD1 1 ATOM 2027 C CD2 . LEU A 1 264 ? 150.602 105.417 23.003 1.00 45.02 ? 264 LEU A CD2 1 ATOM 2028 N N . ARG A 1 265 ? 150.068 107.617 18.067 1.00 49.98 ? 265 ARG A N 1 ATOM 2029 C CA . ARG A 1 265 ? 149.164 108.326 17.172 1.00 46.63 ? 265 ARG A CA 1 ATOM 2030 C C . ARG A 1 265 ? 148.319 107.392 16.296 1.00 50.40 ? 265 ARG A C 1 ATOM 2031 O O . ARG A 1 265 ? 147.294 107.804 15.751 1.00 52.53 ? 265 ARG A O 1 ATOM 2032 C CB . ARG A 1 265 ? 149.943 109.310 16.298 1.00 47.44 ? 265 ARG A CB 1 ATOM 2033 C CG . ARG A 1 265 ? 150.454 110.539 17.050 1.00 51.51 ? 265 ARG A CG 1 ATOM 2034 C CD . ARG A 1 265 ? 150.622 111.725 16.112 1.00 55.86 ? 265 ARG A CD 1 ATOM 2035 N NE . ARG A 1 265 ? 151.901 112.391 16.315 1.00 62.15 ? 265 ARG A NE 1 ATOM 2036 C CZ . ARG A 1 265 ? 153.020 112.070 15.671 1.00 66.19 ? 265 ARG A CZ 1 ATOM 2037 N NH1 . ARG A 1 265 ? 153.022 111.092 14.769 1.00 68.34 ? 265 ARG A NH1 1 ATOM 2038 N NH2 . ARG A 1 265 ? 154.138 112.731 15.930 1.00 63.71 ? 265 ARG A NH2 1 ATOM 2039 N N . ASN A 1 266 ? 148.739 106.139 16.162 1.00 50.42 ? 266 ASN A N 1 ATOM 2040 C CA . ASN A 1 266 ? 147.987 105.188 15.352 1.00 52.56 ? 266 ASN A CA 1 ATOM 2041 C C . ASN A 1 266 ? 147.015 104.361 16.174 1.00 52.23 ? 266 ASN A C 1 ATOM 2042 O O . ASN A 1 266 ? 146.304 103.510 15.640 1.00 66.32 ? 266 ASN A O 1 ATOM 2043 C CB . ASN A 1 266 ? 148.934 104.279 14.566 1.00 74.38 ? 266 ASN A CB 1 ATOM 2044 C CG . ASN A 1 266 ? 149.528 104.974 13.359 1.00 77.35 ? 266 ASN A CG 1 ATOM 2045 O OD1 . ASN A 1 266 ? 148.838 105.711 12.655 1.00 81.52 ? 266 ASN A OD1 1 ATOM 2046 N ND2 . ASN A 1 266 ? 150.815 104.753 13.119 0.61 77.60 ? 266 ASN A ND2 1 ATOM 2047 N N . LYS A 1 267 ? 146.984 104.617 17.475 1.00 50.03 ? 267 LYS A N 1 ATOM 2048 C CA . LYS A 1 267 ? 146.058 103.921 18.359 1.00 49.79 ? 267 LYS A CA 1 ATOM 2049 C C . LYS A 1 267 ? 144.740 104.679 18.426 1.00 54.65 ? 267 LYS A C 1 ATOM 2050 O O . LYS A 1 267 ? 144.719 105.915 18.445 1.00 52.82 ? 267 LYS A O 1 ATOM 2051 C CB . LYS A 1 267 ? 146.648 103.782 19.768 1.00 48.47 ? 267 LYS A CB 1 ATOM 2052 C CG . LYS A 1 267 ? 148.096 103.297 19.810 1.00 49.76 ? 267 LYS A CG 1 ATOM 2053 C CD . LYS A 1 267 ? 148.307 102.048 18.957 1.00 60.51 ? 267 LYS A CD 1 ATOM 2054 C CE . LYS A 1 267 ? 147.762 100.802 19.622 1.00 64.27 ? 267 LYS A CE 1 ATOM 2055 N NZ . LYS A 1 267 ? 148.136 99.557 18.862 1.00 72.78 ? 267 LYS A NZ 1 ATOM 2056 N N . ASP A 1 268 ? 143.637 103.943 18.452 1.00 61.60 ? 268 ASP A N 1 ATOM 2057 C CA . ASP A 1 268 ? 142.333 104.568 18.617 1.00 66.37 ? 268 ASP A CA 1 ATOM 2058 C C . ASP A 1 268 ? 142.239 105.139 20.034 1.00 56.35 ? 268 ASP A C 1 ATOM 2059 O O . ASP A 1 268 ? 142.807 104.572 20.971 1.00 49.31 ? 268 ASP A O 1 ATOM 2060 C CB . ASP A 1 268 ? 141.212 103.567 18.305 1.00 76.42 ? 268 ASP A CB 1 ATOM 2061 C CG . ASP A 1 268 ? 140.082 103.617 19.310 1.00 85.86 ? 268 ASP A CG 1 ATOM 2062 O OD1 . ASP A 1 268 ? 139.176 104.470 19.170 1.00 85.94 ? 268 ASP A OD1 1 ATOM 2063 O OD2 . ASP A 1 268 ? 140.099 102.787 20.241 1.00 93.47 ? 268 ASP A OD2 1 ATOM 2064 N N . PRO A 1 269 ? 141.561 106.286 20.184 1.00 52.73 ? 269 PRO A N 1 ATOM 2065 C CA . PRO A 1 269 ? 141.472 106.972 21.480 1.00 50.10 ? 269 PRO A CA 1 ATOM 2066 C C . PRO A 1 269 ? 141.057 106.041 22.628 1.00 50.82 ? 269 PRO A C 1 ATOM 2067 O O . PRO A 1 269 ? 141.542 106.211 23.747 1.00 43.64 ? 269 PRO A O 1 ATOM 2068 C CB . PRO A 1 269 ? 140.419 108.069 21.239 1.00 52.00 ? 269 PRO A CB 1 ATOM 2069 C CG . PRO A 1 269 ? 140.074 108.017 19.749 1.00 56.28 ? 269 PRO A CG 1 ATOM 2070 C CD . PRO A 1 269 ? 141.072 107.129 19.080 1.00 56.38 ? 269 PRO A CD 1 ATOM 2071 N N . GLN A 1 270 ? 140.211 105.050 22.348 1.00 45.16 ? 270 GLN A N 1 ATOM 2072 C CA . GLN A 1 270 ? 139.753 104.126 23.386 1.00 49.38 ? 270 GLN A CA 1 ATOM 2073 C C . GLN A 1 270 ? 140.868 103.261 24.011 1.00 49.89 ? 270 GLN A C 1 ATOM 2074 O O . GLN A 1 270 ? 140.819 102.951 25.204 1.00 45.98 ? 270 GLN A O 1 ATOM 2075 C CB . GLN A 1 270 ? 138.597 103.254 22.870 1.00 54.22 ? 270 GLN A CB 1 ATOM 2076 C CG . GLN A 1 270 ? 137.857 102.487 23.960 1.00 62.52 ? 270 GLN A CG 1 ATOM 2077 C CD . GLN A 1 270 ? 137.472 103.375 25.134 1.00 73.41 ? 270 GLN A CD 1 ATOM 2078 O OE1 . GLN A 1 270 ? 137.740 103.041 26.290 1.00 76.13 ? 270 GLN A OE1 1 ATOM 2079 N NE2 . GLN A 1 270 ? 136.848 104.517 24.841 1.00 74.33 ? 270 GLN A NE2 1 ATOM 2080 N N . GLU A 1 271 ? 141.873 102.877 23.229 1.00 47.11 ? 271 GLU A N 1 ATOM 2081 C CA . GLU A 1 271 ? 142.966 102.081 23.795 1.00 47.80 ? 271 GLU A CA 1 ATOM 2082 C C . GLU A 1 271 ? 143.873 102.915 24.694 1.00 50.90 ? 271 GLU A C 1 ATOM 2083 O O . GLU A 1 271 ? 144.403 102.423 25.693 1.00 50.13 ? 271 GLU A O 1 ATOM 2084 C CB . GLU A 1 271 ? 143.797 101.391 22.710 1.00 52.86 ? 271 GLU A CB 1 ATOM 2085 C CG . GLU A 1 271 ? 144.860 100.453 23.289 1.00 60.71 ? 271 GLU A CG 1 ATOM 2086 C CD . GLU A 1 271 ? 145.542 99.587 22.241 1.00 68.85 ? 271 GLU A CD 1 ATOM 2087 O OE1 . GLU A 1 271 ? 145.184 99.697 21.046 1.00 72.74 ? 271 GLU A OE1 1 ATOM 2088 O OE2 . GLU A 1 271 ? 146.436 98.793 22.619 1.00 67.41 ? 271 GLU A OE2 1 ATOM 2089 N N . ILE A 1 272 ? 144.058 104.179 24.333 1.00 49.32 ? 272 ILE A N 1 ATOM 2090 C CA . ILE A 1 272 ? 144.811 105.091 25.177 1.00 42.76 ? 272 ILE A CA 1 ATOM 2091 C C . ILE A 1 272 ? 144.060 105.328 26.484 1.00 43.29 ? 272 ILE A C 1 ATOM 2092 O O . ILE A 1 272 ? 144.640 105.208 27.568 1.00 44.56 ? 272 ILE A O 1 ATOM 2093 C CB . ILE A 1 272 ? 145.063 106.426 24.468 1.00 44.57 ? 272 ILE A CB 1 ATOM 2094 C CG1 . ILE A 1 272 ? 146.056 106.224 23.325 1.00 46.94 ? 272 ILE A CG1 1 ATOM 2095 C CG2 . ILE A 1 272 ? 145.593 107.467 25.455 1.00 46.19 ? 272 ILE A CG2 1 ATOM 2096 C CD1 . ILE A 1 272 ? 145.892 107.211 22.195 1.00 50.72 ? 272 ILE A CD1 1 ATOM 2097 N N . LEU A 1 273 ? 142.770 105.646 26.375 1.00 39.72 ? 273 LEU A N 1 ATOM 2098 C CA . LEU A 1 273 ? 141.936 105.904 27.548 1.00 43.44 ? 273 LEU A CA 1 ATOM 2099 C C . LEU A 1 273 ? 141.890 104.698 28.472 1.00 45.12 ? 273 LEU A C 1 ATOM 2100 O O . LEU A 1 273 ? 141.894 104.843 29.701 1.00 43.99 ? 273 LEU A O 1 ATOM 2101 C CB . LEU A 1 273 ? 140.512 106.282 27.136 1.00 42.27 ? 273 LEU A CB 1 ATOM 2102 C CG . LEU A 1 273 ? 140.318 107.689 26.578 1.00 43.64 ? 273 LEU A CG 1 ATOM 2103 C CD1 . LEU A 1 273 ? 138.928 107.819 25.964 1.00 45.79 ? 273 LEU A CD1 1 ATOM 2104 C CD2 . LEU A 1 273 ? 140.528 108.744 27.667 1.00 35.42 ? 273 LEU A CD2 1 ATOM 2105 N N . LEU A 1 274 ? 141.855 103.509 27.879 1.00 43.03 ? 274 LEU A N 1 ATOM 2106 C CA . LEU A 1 274 ? 141.752 102.284 28.657 1.00 49.29 ? 274 LEU A CA 1 ATOM 2107 C C . LEU A 1 274 ? 142.969 102.058 29.547 1.00 50.38 ? 274 LEU A C 1 ATOM 2108 O O . LEU A 1 274 ? 142.840 101.556 30.665 1.00 50.00 ? 274 LEU A O 1 ATOM 2109 C CB . LEU A 1 274 ? 141.544 101.080 27.743 1.00 55.26 ? 274 LEU A CB 1 ATOM 2110 C CG . LEU A 1 274 ? 140.209 100.378 27.982 1.00 65.34 ? 274 LEU A CG 1 ATOM 2111 C CD1 . LEU A 1 274 ? 139.365 100.354 26.713 1.00 68.38 ? 274 LEU A CD1 1 ATOM 2112 C CD2 . LEU A 1 274 ? 140.413 98.968 28.533 1.00 72.68 ? 274 LEU A CD2 1 ATOM 2113 N N . ASN A 1 275 ? 144.145 102.440 29.058 1.00 51.30 ? 275 ASN A N 1 ATOM 2114 C CA . ASN A 1 275 ? 145.387 102.162 29.774 1.00 54.71 ? 275 ASN A CA 1 ATOM 2115 C C . ASN A 1 275 ? 145.921 103.287 30.667 1.00 50.78 ? 275 ASN A C 1 ATOM 2116 O O . ASN A 1 275 ? 146.919 103.096 31.367 1.00 54.10 ? 275 ASN A O 1 ATOM 2117 C CB . ASN A 1 275 ? 146.461 101.673 28.800 1.00 46.33 ? 275 ASN A CB 1 ATOM 2118 C CG . ASN A 1 275 ? 146.220 100.244 28.351 1.00 49.53 ? 275 ASN A CG 1 ATOM 2119 O OD1 . ASN A 1 275 ? 146.737 99.308 28.947 1.00 55.87 ? 275 ASN A OD1 1 ATOM 2120 N ND2 . ASN A 1 275 ? 145.415 100.072 27.313 1.00 50.04 ? 275 ASN A ND2 1 ATOM 2121 N N . GLU A 1 276 ? 145.256 104.442 30.650 1.00 42.39 ? 276 GLU A N 1 ATOM 2122 C CA . GLU A 1 276 ? 145.658 105.581 31.479 1.00 44.31 ? 276 GLU A CA 1 ATOM 2123 C C . GLU A 1 276 ? 145.693 105.239 32.980 1.00 40.90 ? 276 GLU A C 1 ATOM 2124 O O . GLU A 1 276 ? 146.599 105.666 33.706 1.00 41.08 ? 276 GLU A O 1 ATOM 2125 C CB . GLU A 1 276 ? 144.741 106.800 31.234 1.00 43.81 ? 276 GLU A CB 1 ATOM 2126 C CG . GLU A 1 276 ? 144.957 107.533 29.903 1.00 48.57 ? 276 GLU A CG 1 ATOM 2127 C CD . GLU A 1 276 ? 144.088 108.789 29.767 1.00 55.76 ? 276 GLU A CD 1 ATOM 2128 O OE1 . GLU A 1 276 ? 143.164 108.980 30.592 1.00 59.04 ? 276 GLU A OE1 1 ATOM 2129 O OE2 . GLU A 1 276 ? 144.330 109.587 28.832 1.00 52.06 ? 276 GLU A OE2 1 ATOM 2130 N N . ALA A 1 277 ? 144.712 104.470 33.442 1.00 42.96 ? 277 ALA A N 1 ATOM 2131 C CA . ALA A 1 277 ? 144.605 104.137 34.864 1.00 54.42 ? 277 ALA A CA 1 ATOM 2132 C C . ALA A 1 277 ? 145.790 103.321 35.407 1.00 57.78 ? 277 ALA A C 1 ATOM 2133 O O . ALA A 1 277 ? 146.080 103.351 36.608 1.00 58.71 ? 277 ALA A O 1 ATOM 2134 C CB . ALA A 1 277 ? 143.293 103.408 35.137 1.00 57.45 ? 277 ALA A CB 1 ATOM 2135 N N . PHE A 1 278 ? 146.482 102.606 34.527 1.00 53.92 ? 278 PHE A N 1 ATOM 2136 C CA . PHE A 1 278 ? 147.523 101.687 34.974 1.00 56.54 ? 278 PHE A CA 1 ATOM 2137 C C . PHE A 1 278 ? 148.959 102.189 34.829 1.00 55.19 ? 278 PHE A C 1 ATOM 2138 O O . PHE A 1 278 ? 149.891 101.430 35.075 1.00 53.00 ? 278 PHE A O 1 ATOM 2139 C CB . PHE A 1 278 ? 147.386 100.342 34.258 1.00 61.23 ? 278 PHE A CB 1 ATOM 2140 C CG . PHE A 1 278 ? 145.987 99.823 34.226 1.00 65.65 ? 278 PHE A CG 1 ATOM 2141 C CD1 . PHE A 1 278 ? 145.454 99.163 35.321 1.00 74.24 ? 278 PHE A CD1 1 ATOM 2142 C CD2 . PHE A 1 278 ? 145.199 100.001 33.104 1.00 67.90 ? 278 PHE A CD2 1 ATOM 2143 C CE1 . PHE A 1 278 ? 144.160 98.686 35.293 1.00 80.82 ? 278 PHE A CE1 1 ATOM 2144 C CE2 . PHE A 1 278 ? 143.905 99.529 33.069 1.00 75.91 ? 278 PHE A CE2 1 ATOM 2145 C CZ . PHE A 1 278 ? 143.384 98.870 34.164 1.00 81.05 ? 278 PHE A CZ 1 ATOM 2146 N N . VAL A 1 279 ? 149.165 103.447 34.446 1.00 49.54 ? 279 VAL A N 1 ATOM 2147 C CA . VAL A 1 279 ? 150.549 103.916 34.315 1.00 51.76 ? 279 VAL A CA 1 ATOM 2148 C C . VAL A 1 279 ? 151.247 104.101 35.676 1.00 52.66 ? 279 VAL A C 1 ATOM 2149 O O . VAL A 1 279 ? 152.448 104.372 35.741 1.00 56.10 ? 279 VAL A O 1 ATOM 2150 C CB . VAL A 1 279 ? 150.677 105.164 33.406 1.00 54.77 ? 279 VAL A CB 1 ATOM 2151 C CG1 . VAL A 1 279 ? 150.230 104.821 31.986 1.00 53.24 ? 279 VAL A CG1 1 ATOM 2152 C CG2 . VAL A 1 279 ? 149.870 106.331 33.959 1.00 49.98 ? 279 VAL A CG2 1 ATOM 2153 N N . VAL A 1 280 ? 150.486 103.926 36.754 1.00 56.02 ? 280 VAL A N 1 ATOM 2154 C CA . VAL A 1 280 ? 151.013 103.978 38.114 1.00 57.93 ? 280 VAL A CA 1 ATOM 2155 C C . VAL A 1 280 ? 150.684 102.668 38.844 1.00 63.88 ? 280 VAL A C 1 ATOM 2156 O O . VAL A 1 280 ? 149.636 102.068 38.598 1.00 64.99 ? 280 VAL A O 1 ATOM 2157 C CB . VAL A 1 280 ? 150.429 105.184 38.896 1.00 51.55 ? 280 VAL A CB 1 ATOM 2158 C CG1 . VAL A 1 280 ? 150.868 106.502 38.260 1.00 49.49 ? 280 VAL A CG1 1 ATOM 2159 C CG2 . VAL A 1 280 ? 148.913 105.110 38.952 1.00 47.54 ? 280 VAL A CG2 1 ATOM 2160 N N . PRO A 1 281 ? 151.580 102.216 39.740 1.00 69.48 ? 281 PRO A N 1 ATOM 2161 C CA . PRO A 1 281 ? 151.390 100.941 40.447 1.00 74.88 ? 281 PRO A CA 1 ATOM 2162 C C . PRO A 1 281 ? 150.154 100.968 41.338 1.00 74.29 ? 281 PRO A C 1 ATOM 2163 O O . PRO A 1 281 ? 149.342 100.040 41.310 1.00 73.12 ? 281 PRO A O 1 ATOM 2164 C CB . PRO A 1 281 ? 152.657 100.815 41.301 1.00 77.60 ? 281 PRO A CB 1 ATOM 2165 C CG . PRO A 1 281 ? 153.168 102.203 41.447 1.00 76.45 ? 281 PRO A CG 1 ATOM 2166 C CD . PRO A 1 281 ? 152.801 102.915 40.177 1.00 74.11 ? 281 PRO A CD 1 ATOM 2167 N N . TYR A 1 282 ? 150.021 102.028 42.124 1.00 71.92 ? 282 TYR A N 1 ATOM 2168 C CA . TYR A 1 282 ? 148.826 102.225 42.925 1.00 76.29 ? 282 TYR A CA 1 ATOM 2169 C C . TYR A 1 282 ? 148.272 103.618 42.690 1.00 74.30 ? 282 TYR A C 1 ATOM 2170 O O . TYR A 1 282 ? 149.019 104.591 42.595 1.00 79.45 ? 282 TYR A O 1 ATOM 2171 C CB . TYR A 1 282 ? 149.103 101.990 44.415 1.00 87.34 ? 282 TYR A CB 1 ATOM 2172 C CG . TYR A 1 282 ? 150.447 102.493 44.897 1.00 95.74 ? 282 TYR A CG 1 ATOM 2173 C CD1 . TYR A 1 282 ? 150.702 103.854 45.014 1.00 95.85 ? 282 TYR A CD1 1 ATOM 2174 C CD2 . TYR A 1 282 ? 151.457 101.603 45.248 1.00 99.86 ? 282 TYR A CD2 1 ATOM 2175 C CE1 . TYR A 1 282 ? 151.926 104.319 45.461 1.00 97.85 ? 282 TYR A CE1 1 ATOM 2176 C CE2 . TYR A 1 282 ? 152.687 102.058 45.695 1.00 102.52 ? 282 TYR A CE2 1 ATOM 2177 C CZ . TYR A 1 282 ? 152.914 103.418 45.799 1.00 102.01 ? 282 TYR A CZ 1 ATOM 2178 O OH . TYR A 1 282 ? 154.133 103.882 46.241 1.00 104.31 ? 282 TYR A OH 1 ATOM 2179 N N . GLY A 1 283 ? 146.956 103.702 42.569 1.00 65.78 ? 283 GLY A N 1 ATOM 2180 C CA . GLY A 1 283 ? 146.298 104.981 42.444 1.00 56.36 ? 283 GLY A CA 1 ATOM 2181 C C . GLY A 1 283 ? 145.487 105.247 43.691 1.00 52.38 ? 283 GLY A C 1 ATOM 2182 O O . GLY A 1 283 ? 145.416 104.405 44.590 1.00 53.87 ? 283 GLY A O 1 ATOM 2183 N N . THR A 1 284 ? 144.896 106.433 43.749 1.00 41.46 ? 284 THR A N 1 ATOM 2184 C CA . THR A 1 284 ? 143.994 106.810 44.821 1.00 41.55 ? 284 THR A CA 1 ATOM 2185 C C . THR A 1 284 ? 142.806 107.470 44.128 1.00 39.47 ? 284 THR A C 1 ATOM 2186 O O . THR A 1 284 ? 142.869 107.728 42.928 1.00 37.94 ? 284 THR A O 1 ATOM 2187 C CB . THR A 1 284 ? 144.663 107.836 45.772 1.00 40.83 ? 284 THR A CB 1 ATOM 2188 O OG1 . THR A 1 284 ? 144.737 109.106 45.119 1.00 37.93 ? 284 THR A OG1 1 ATOM 2189 C CG2 . THR A 1 284 ? 146.069 107.380 46.175 1.00 42.78 ? 284 THR A CG2 1 ATOM 2190 N N . PRO A 1 285 ? 141.715 107.745 44.868 1.00 44.30 ? 285 PRO A N 1 ATOM 2191 C CA . PRO A 1 285 ? 140.609 108.485 44.248 1.00 38.09 ? 285 PRO A CA 1 ATOM 2192 C C . PRO A 1 285 ? 140.991 109.878 43.752 1.00 45.30 ? 285 PRO A C 1 ATOM 2193 O O . PRO A 1 285 ? 140.224 110.471 42.989 1.00 43.19 ? 285 PRO A O 1 ATOM 2194 C CB . PRO A 1 285 ? 139.599 108.598 45.389 1.00 39.34 ? 285 PRO A CB 1 ATOM 2195 C CG . PRO A 1 285 ? 139.794 107.317 46.152 1.00 42.37 ? 285 PRO A CG 1 ATOM 2196 C CD . PRO A 1 285 ? 141.300 107.109 46.134 1.00 46.07 ? 285 PRO A CD 1 ATOM 2197 N N . LEU A 1 286 ? 142.141 110.395 44.179 1.00 34.68 ? 286 LEU A N 1 ATOM 2198 C CA . LEU A 1 286 ? 142.590 111.718 43.740 1.00 32.44 ? 286 LEU A CA 1 ATOM 2199 C C . LEU A 1 286 ? 143.723 111.667 42.719 1.00 31.80 ? 286 LEU A C 1 ATOM 2200 O O . LEU A 1 286 ? 144.314 112.700 42.402 1.00 31.76 ? 286 LEU A O 1 ATOM 2201 C CB . LEU A 1 286 ? 143.013 112.566 44.938 1.00 35.58 ? 286 LEU A CB 1 ATOM 2202 C CG . LEU A 1 286 ? 141.824 112.952 45.817 1.00 40.70 ? 286 LEU A CG 1 ATOM 2203 C CD1 . LEU A 1 286 ? 141.812 112.172 47.109 1.00 40.14 ? 286 LEU A CD1 1 ATOM 2204 C CD2 . LEU A 1 286 ? 141.823 114.440 46.079 1.00 35.19 ? 286 LEU A CD2 1 ATOM 2205 N N . SER A 1 287 ? 144.016 110.476 42.198 1.00 37.72 ? 287 SER A N 1 ATOM 2206 C CA . SER A 1 287 ? 145.092 110.325 41.217 1.00 38.66 ? 287 SER A CA 1 ATOM 2207 C C . SER A 1 287 ? 144.926 111.231 39.996 1.00 36.64 ? 287 SER A C 1 ATOM 2208 O O . SER A 1 287 ? 143.832 111.368 39.455 1.00 34.53 ? 287 SER A O 1 ATOM 2209 C CB . SER A 1 287 ? 145.229 108.866 40.771 1.00 35.59 ? 287 SER A CB 1 ATOM 2210 O OG . SER A 1 287 ? 145.870 108.093 41.764 1.00 40.00 ? 287 SER A OG 1 ATOM 2211 N N . VAL A 1 288 ? 146.028 111.850 39.589 1.00 30.38 ? 288 VAL A N 1 ATOM 2212 C CA . VAL A 1 288 ? 146.090 112.664 38.386 1.00 29.00 ? 288 VAL A CA 1 ATOM 2213 C C . VAL A 1 288 ? 147.258 112.118 37.572 1.00 29.94 ? 288 VAL A C 1 ATOM 2214 O O . VAL A 1 288 ? 148.400 112.576 37.701 1.00 35.10 ? 288 VAL A O 1 ATOM 2215 C CB . VAL A 1 288 ? 146.315 114.165 38.739 1.00 30.35 ? 288 VAL A CB 1 ATOM 2216 C CG1 . VAL A 1 288 ? 146.589 114.999 37.489 1.00 26.84 ? 288 VAL A CG1 1 ATOM 2217 C CG2 . VAL A 1 288 ? 145.094 114.721 39.497 1.00 27.06 ? 288 VAL A CG2 1 ATOM 2218 N N . ASN A 1 289 ? 146.987 111.112 36.753 1.00 30.74 ? 289 ASN A N 1 ATOM 2219 C CA . ASN A 1 289 ? 148.068 110.413 36.061 1.00 44.71 ? 289 ASN A CA 1 ATOM 2220 C C . ASN A 1 289 ? 148.766 111.244 34.990 1.00 37.15 ? 289 ASN A C 1 ATOM 2221 O O . ASN A 1 289 ? 149.980 111.126 34.797 1.00 38.09 ? 289 ASN A O 1 ATOM 2222 C CB . ASN A 1 289 ? 147.563 109.095 35.479 1.00 49.83 ? 289 ASN A CB 1 ATOM 2223 C CG . ASN A 1 289 ? 147.191 108.098 36.555 1.00 56.01 ? 289 ASN A CG 1 ATOM 2224 O OD1 . ASN A 1 289 ? 147.846 108.019 37.596 1.00 60.11 ? 289 ASN A OD1 1 ATOM 2225 N ND2 . ASN A 1 289 ? 146.130 107.343 36.319 1.00 58.97 ? 289 ASN A ND2 1 ATOM 2226 N N . PHE A 1 290 ? 147.986 112.071 34.294 1.00 31.24 ? 290 PHE A N 1 ATOM 2227 C CA . PHE A 1 290 ? 148.508 112.966 33.273 1.00 34.83 ? 290 PHE A CA 1 ATOM 2228 C C . PHE A 1 290 ? 148.065 114.395 33.565 1.00 31.40 ? 290 PHE A C 1 ATOM 2229 O O . PHE A 1 290 ? 146.924 114.770 33.279 1.00 31.48 ? 290 PHE A O 1 ATOM 2230 C CB . PHE A 1 290 ? 148.048 112.511 31.882 1.00 28.77 ? 290 PHE A CB 1 ATOM 2231 C CG . PHE A 1 290 ? 148.642 111.185 31.457 1.00 34.81 ? 290 PHE A CG 1 ATOM 2232 C CD1 . PHE A 1 290 ? 149.935 111.123 30.949 1.00 32.04 ? 290 PHE A CD1 1 ATOM 2233 C CD2 . PHE A 1 290 ? 147.924 109.999 31.601 1.00 34.84 ? 290 PHE A CD2 1 ATOM 2234 C CE1 . PHE A 1 290 ? 150.501 109.902 30.571 1.00 37.34 ? 290 PHE A CE1 1 ATOM 2235 C CE2 . PHE A 1 290 ? 148.482 108.772 31.223 1.00 35.46 ? 290 PHE A CE2 1 ATOM 2236 C CZ . PHE A 1 290 ? 149.768 108.725 30.706 1.00 39.34 ? 290 PHE A CZ 1 ATOM 2237 N N . GLY A 1 291 ? 148.961 115.190 34.143 1.00 25.52 ? 291 GLY A N 1 ATOM 2238 C CA . GLY A 1 291 ? 148.640 116.574 34.478 1.00 29.74 ? 291 GLY A CA 1 ATOM 2239 C C . GLY A 1 291 ? 149.737 117.549 34.077 1.00 28.68 ? 291 GLY A C 1 ATOM 2240 O O . GLY A 1 291 ? 150.670 117.168 33.374 1.00 25.62 ? 291 GLY A O 1 ATOM 2241 N N . PRO A 1 292 ? 149.620 118.818 34.497 1.00 24.73 ? 292 PRO A N 1 ATOM 2242 C CA . PRO A 1 292 ? 150.647 119.828 34.190 1.00 25.80 ? 292 PRO A CA 1 ATOM 2243 C C . PRO A 1 292 ? 152.064 119.357 34.562 1.00 26.38 ? 292 PRO A C 1 ATOM 2244 O O . PRO A 1 292 ? 152.237 118.633 35.549 1.00 26.20 ? 292 PRO A O 1 ATOM 2245 C CB . PRO A 1 292 ? 150.237 121.022 35.061 1.00 22.07 ? 292 PRO A CB 1 ATOM 2246 C CG . PRO A 1 292 ? 148.725 120.890 35.204 1.00 22.34 ? 292 PRO A CG 1 ATOM 2247 C CD . PRO A 1 292 ? 148.476 119.382 35.238 1.00 22.55 ? 292 PRO A CD 1 ATOM 2248 N N . THR A 1 293 ? 153.056 119.735 33.759 1.00 25.70 ? 293 THR A N 1 ATOM 2249 C CA . THR A 1 293 ? 154.456 119.456 34.069 1.00 26.97 ? 293 THR A CA 1 ATOM 2250 C C . THR A 1 293 ? 155.278 120.726 33.873 1.00 30.80 ? 293 THR A C 1 ATOM 2251 O O . THR A 1 293 ? 154.787 121.714 33.308 1.00 28.75 ? 293 THR A O 1 ATOM 2252 C CB . THR A 1 293 ? 155.057 118.392 33.131 1.00 32.26 ? 293 THR A CB 1 ATOM 2253 O OG1 . THR A 1 293 ? 154.707 118.715 31.781 1.00 32.89 ? 293 THR A OG1 1 ATOM 2254 C CG2 . THR A 1 293 ? 154.542 117.010 33.467 1.00 38.33 ? 293 THR A CG2 1 ATOM 2255 N N . VAL A 1 294 ? 156.528 120.696 34.330 1.00 28.30 ? 294 VAL A N 1 ATOM 2256 C CA . VAL A 1 294 ? 157.474 121.780 34.053 1.00 29.03 ? 294 VAL A CA 1 ATOM 2257 C C . VAL A 1 294 ? 158.069 121.538 32.665 1.00 30.77 ? 294 VAL A C 1 ATOM 2258 O O . VAL A 1 294 ? 159.039 120.809 32.523 1.00 32.44 ? 294 VAL A O 1 ATOM 2259 C CB . VAL A 1 294 ? 158.589 121.848 35.130 1.00 33.16 ? 294 VAL A CB 1 ATOM 2260 C CG1 . VAL A 1 294 ? 159.626 122.936 34.786 1.00 30.77 ? 294 VAL A CG1 1 ATOM 2261 C CG2 . VAL A 1 294 ? 157.969 122.118 36.505 1.00 28.09 ? 294 VAL A CG2 1 ATOM 2262 N N . ASP A 1 295 ? 157.468 122.137 31.642 1.00 30.79 ? 295 ASP A N 1 ATOM 2263 C CA . ASP A 1 295 ? 157.814 121.827 30.248 1.00 34.43 ? 295 ASP A CA 1 ATOM 2264 C C . ASP A 1 295 ? 158.871 122.767 29.632 1.00 33.66 ? 295 ASP A C 1 ATOM 2265 O O . ASP A 1 295 ? 159.338 122.536 28.513 1.00 37.74 ? 295 ASP A O 1 ATOM 2266 C CB . ASP A 1 295 ? 156.546 121.909 29.402 1.00 31.40 ? 295 ASP A CB 1 ATOM 2267 C CG . ASP A 1 295 ? 155.925 123.307 29.440 1.00 34.65 ? 295 ASP A CG 1 ATOM 2268 O OD1 . ASP A 1 295 ? 156.234 124.068 30.394 1.00 29.43 ? 295 ASP A OD1 1 ATOM 2269 O OD2 . ASP A 1 295 ? 155.141 123.651 28.528 1.00 30.03 ? 295 ASP A OD2 1 ATOM 2270 N N . GLY A 1 296 ? 159.217 123.842 30.335 1.00 35.08 ? 296 GLY A N 1 ATOM 2271 C CA . GLY A 1 296 ? 160.163 124.817 29.806 1.00 39.09 ? 296 GLY A CA 1 ATOM 2272 C C . GLY A 1 296 ? 159.549 125.749 28.767 1.00 43.58 ? 296 GLY A C 1 ATOM 2273 O O . GLY A 1 296 ? 160.261 126.449 28.040 1.00 36.00 ? 296 GLY A O 1 ATOM 2274 N N . ASP A 1 297 ? 158.219 125.751 28.691 1.00 40.43 ? 297 ASP A N 1 ATOM 2275 C CA . ASP A 1 297 ? 157.506 126.573 27.723 1.00 34.38 ? 297 ASP A CA 1 ATOM 2276 C C . ASP A 1 297 ? 156.368 127.320 28.416 1.00 35.81 ? 297 ASP A C 1 ATOM 2277 O O . ASP A 1 297 ? 156.470 128.524 28.662 1.00 33.03 ? 297 ASP A O 1 ATOM 2278 C CB . ASP A 1 297 ? 156.987 125.705 26.571 1.00 34.51 ? 297 ASP A CB 1 ATOM 2279 C CG . ASP A 1 297 ? 156.485 126.530 25.400 1.00 38.12 ? 297 ASP A CG 1 ATOM 2280 O OD1 . ASP A 1 297 ? 156.356 127.767 25.549 1.00 38.40 ? 297 ASP A OD1 1 ATOM 2281 O OD2 . ASP A 1 297 ? 156.206 125.940 24.334 1.00 38.22 ? 297 ASP A OD2 1 ATOM 2282 N N . PHE A 1 298 ? 155.281 126.618 28.733 1.00 29.32 ? 298 PHE A N 1 ATOM 2283 C CA . PHE A 1 298 ? 154.200 127.224 29.507 1.00 27.47 ? 298 PHE A CA 1 ATOM 2284 C C . PHE A 1 298 ? 154.651 127.488 30.951 1.00 31.95 ? 298 PHE A C 1 ATOM 2285 O O . PHE A 1 298 ? 154.269 128.497 31.557 1.00 30.35 ? 298 PHE A O 1 ATOM 2286 C CB . PHE A 1 298 ? 152.960 126.318 29.504 1.00 26.45 ? 298 PHE A CB 1 ATOM 2287 C CG . PHE A 1 298 ? 151.737 126.952 30.129 1.00 24.81 ? 298 PHE A CG 1 ATOM 2288 C CD1 . PHE A 1 298 ? 151.496 126.843 31.492 1.00 24.99 ? 298 PHE A CD1 1 ATOM 2289 C CD2 . PHE A 1 298 ? 150.828 127.647 29.349 1.00 28.84 ? 298 PHE A CD2 1 ATOM 2290 C CE1 . PHE A 1 298 ? 150.360 127.418 32.070 1.00 24.68 ? 298 PHE A CE1 1 ATOM 2291 C CE2 . PHE A 1 298 ? 149.698 128.230 29.914 1.00 29.17 ? 298 PHE A CE2 1 ATOM 2292 C CZ . PHE A 1 298 ? 149.462 128.117 31.276 1.00 25.25 ? 298 PHE A CZ 1 ATOM 2293 N N . LEU A 1 299 ? 155.468 126.579 31.487 1.00 29.75 ? 299 LEU A N 1 ATOM 2294 C CA . LEU A 1 299 ? 155.933 126.638 32.875 1.00 30.20 ? 299 LEU A CA 1 ATOM 2295 C C . LEU A 1 299 ? 157.461 126.536 32.888 1.00 37.88 ? 299 LEU A C 1 ATOM 2296 O O . LEU A 1 299 ? 158.013 125.473 32.577 1.00 29.43 ? 299 LEU A O 1 ATOM 2297 C CB . LEU A 1 299 ? 155.361 125.453 33.650 1.00 33.69 ? 299 LEU A CB 1 ATOM 2298 C CG . LEU A 1 299 ? 154.541 125.673 34.919 1.00 44.66 ? 299 LEU A CG 1 ATOM 2299 C CD1 . LEU A 1 299 ? 154.236 124.332 35.596 1.00 40.76 ? 299 LEU A CD1 1 ATOM 2300 C CD2 . LEU A 1 299 ? 155.256 126.608 35.882 1.00 47.04 ? 299 LEU A CD2 1 ATOM 2301 N N . THR A 1 300 ? 158.144 127.620 33.263 1.00 35.04 ? 300 THR A N 1 ATOM 2302 C CA . THR A 1 300 ? 159.603 127.702 33.096 1.00 37.11 ? 300 THR A CA 1 ATOM 2303 C C . THR A 1 300 ? 160.442 127.114 34.229 1.00 36.88 ? 300 THR A C 1 ATOM 2304 O O . THR A 1 300 ? 161.644 126.939 34.071 1.00 39.90 ? 300 THR A O 1 ATOM 2305 C CB . THR A 1 300 ? 160.065 129.157 32.886 1.00 39.03 ? 300 THR A CB 1 ATOM 2306 O OG1 . THR A 1 300 ? 159.677 129.952 34.020 1.00 35.13 ? 300 THR A OG1 1 ATOM 2307 C CG2 . THR A 1 300 ? 159.425 129.726 31.635 1.00 43.90 ? 300 THR A CG2 1 ATOM 2308 N N . ASP A 1 301 ? 159.821 126.820 35.366 1.00 35.44 ? 301 ASP A N 1 ATOM 2309 C CA . ASP A 1 301 ? 160.555 126.320 36.532 1.00 38.33 ? 301 ASP A CA 1 ATOM 2310 C C . ASP A 1 301 ? 159.530 125.718 37.481 1.00 32.13 ? 301 ASP A C 1 ATOM 2311 O O . ASP A 1 301 ? 158.333 125.871 37.272 1.00 26.94 ? 301 ASP A O 1 ATOM 2312 C CB . ASP A 1 301 ? 161.302 127.479 37.219 1.00 37.55 ? 301 ASP A CB 1 ATOM 2313 C CG . ASP A 1 301 ? 162.379 127.008 38.214 1.00 41.51 ? 301 ASP A CG 1 ATOM 2314 O OD1 . ASP A 1 301 ? 162.590 125.782 38.383 1.00 36.71 ? 301 ASP A OD1 1 ATOM 2315 O OD2 . ASP A 1 301 ? 163.034 127.887 38.821 1.00 43.75 ? 301 ASP A OD2 1 ATOM 2316 N N . MET A 1 302 ? 159.981 125.039 38.526 1.00 32.88 ? 302 MET A N 1 ATOM 2317 C CA . MET A 1 302 ? 159.038 124.510 39.507 1.00 29.86 ? 302 MET A CA 1 ATOM 2318 C C . MET A 1 302 ? 158.202 125.643 40.100 1.00 29.08 ? 302 MET A C 1 ATOM 2319 O O . MET A 1 302 ? 158.733 126.651 40.560 1.00 32.08 ? 302 MET A O 1 ATOM 2320 C CB . MET A 1 302 ? 159.787 123.732 40.577 1.00 30.18 ? 302 MET A CB 1 ATOM 2321 C CG . MET A 1 302 ? 160.758 122.718 39.953 1.00 31.62 ? 302 MET A CG 1 ATOM 2322 S SD . MET A 1 302 ? 161.586 121.693 41.180 1.00 61.31 ? 302 MET A SD 1 ATOM 2323 C CE . MET A 1 302 ? 160.149 120.908 41.919 1.00 81.46 ? 302 MET A CE 1 ATOM 2324 N N . PRO A 1 303 ? 156.878 125.496 40.045 1.00 30.21 ? 303 PRO A N 1 ATOM 2325 C CA . PRO A 1 303 ? 155.980 126.601 40.400 1.00 27.49 ? 303 PRO A CA 1 ATOM 2326 C C . PRO A 1 303 ? 156.045 127.028 41.874 1.00 31.30 ? 303 PRO A C 1 ATOM 2327 O O . PRO A 1 303 ? 155.761 128.200 42.169 1.00 25.48 ? 303 PRO A O 1 ATOM 2328 C CB . PRO A 1 303 ? 154.584 126.070 40.004 1.00 30.76 ? 303 PRO A CB 1 ATOM 2329 C CG . PRO A 1 303 ? 154.747 124.579 39.836 1.00 28.87 ? 303 PRO A CG 1 ATOM 2330 C CD . PRO A 1 303 ? 156.170 124.384 39.385 1.00 26.85 ? 303 PRO A CD 1 ATOM 2331 N N . ASP A 1 304 ? 156.418 126.122 42.775 1.00 23.03 ? 304 ASP A N 1 ATOM 2332 C CA . ASP A 1 304 ? 156.624 126.494 44.174 1.00 35.58 ? 304 ASP A CA 1 ATOM 2333 C C . ASP A 1 304 ? 157.740 127.540 44.306 1.00 35.14 ? 304 ASP A C 1 ATOM 2334 O O . ASP A 1 304 ? 157.685 128.431 45.166 1.00 31.19 ? 304 ASP A O 1 ATOM 2335 C CB . ASP A 1 304 ? 156.970 125.264 45.024 1.00 42.73 ? 304 ASP A CB 1 ATOM 2336 C CG . ASP A 1 304 ? 158.002 124.362 44.361 1.00 57.97 ? 304 ASP A CG 1 ATOM 2337 O OD1 . ASP A 1 304 ? 157.801 124.001 43.178 1.00 66.17 ? 304 ASP A OD1 1 ATOM 2338 O OD2 . ASP A 1 304 ? 159.010 124.007 45.020 1.00 56.90 ? 304 ASP A OD2 1 ATOM 2339 N N . ILE A 1 305 ? 158.754 127.413 43.455 1.00 31.16 ? 305 ILE A N 1 ATOM 2340 C CA . ILE A 1 305 ? 159.877 128.346 43.449 1.00 34.72 ? 305 ILE A CA 1 ATOM 2341 C C . ILE A 1 305 ? 159.421 129.718 42.946 1.00 32.17 ? 305 ILE A C 1 ATOM 2342 O O . ILE A 1 305 ? 159.715 130.729 43.577 1.00 29.39 ? 305 ILE A O 1 ATOM 2343 C CB . ILE A 1 305 ? 161.052 127.821 42.594 1.00 28.37 ? 305 ILE A CB 1 ATOM 2344 C CG1 . ILE A 1 305 ? 161.406 126.383 42.998 1.00 29.03 ? 305 ILE A CG1 1 ATOM 2345 C CG2 . ILE A 1 305 ? 162.269 128.738 42.737 1.00 29.96 ? 305 ILE A CG2 1 ATOM 2346 C CD1 . ILE A 1 305 ? 162.760 125.863 42.439 1.00 31.18 ? 305 ILE A CD1 1 ATOM 2347 N N . LEU A 1 306 ? 158.693 129.734 41.825 1.00 25.39 ? 306 LEU A N 1 ATOM 2348 C CA . LEU A 1 306 ? 158.163 130.966 41.234 1.00 33.18 ? 306 LEU A CA 1 ATOM 2349 C C . LEU A 1 306 ? 157.264 131.709 42.226 1.00 31.84 ? 306 LEU A C 1 ATOM 2350 O O . LEU A 1 306 ? 157.368 132.939 42.378 1.00 28.37 ? 306 LEU A O 1 ATOM 2351 C CB . LEU A 1 306 ? 157.387 130.659 39.940 1.00 26.17 ? 306 LEU A CB 1 ATOM 2352 C CG . LEU A 1 306 ? 158.201 130.000 38.809 1.00 26.59 ? 306 LEU A CG 1 ATOM 2353 C CD1 . LEU A 1 306 ? 157.298 129.584 37.635 1.00 25.19 ? 306 LEU A CD1 1 ATOM 2354 C CD2 . LEU A 1 306 ? 159.324 130.900 38.307 1.00 27.36 ? 306 LEU A CD2 1 ATOM 2355 N N . LEU A 1 307 ? 156.390 130.958 42.898 1.00 33.17 ? 307 LEU A N 1 ATOM 2356 C CA . LEU A 1 307 ? 155.497 131.520 43.917 1.00 31.87 ? 307 LEU A CA 1 ATOM 2357 C C . LEU A 1 307 ? 156.285 132.112 45.087 1.00 28.90 ? 307 LEU A C 1 ATOM 2358 O O . LEU A 1 307 ? 156.063 133.271 45.486 1.00 29.12 ? 307 LEU A O 1 ATOM 2359 C CB . LEU A 1 307 ? 154.519 130.457 44.437 1.00 29.01 ? 307 LEU A CB 1 ATOM 2360 C CG . LEU A 1 307 ? 153.506 130.971 45.470 1.00 32.51 ? 307 LEU A CG 1 ATOM 2361 C CD1 . LEU A 1 307 ? 152.642 132.077 44.867 1.00 35.40 ? 307 LEU A CD1 1 ATOM 2362 C CD2 . LEU A 1 307 ? 152.624 129.850 45.995 1.00 24.76 ? 307 LEU A CD2 1 ATOM 2363 N N . GLU A 1 308 ? 157.207 131.318 45.630 1.00 26.84 ? 308 GLU A N 1 ATOM 2364 C CA . GLU A 1 308 ? 158.010 131.762 46.759 1.00 26.97 ? 308 GLU A CA 1 ATOM 2365 C C . GLU A 1 308 ? 158.777 133.042 46.424 1.00 33.28 ? 308 GLU A C 1 ATOM 2366 O O . GLU A 1 308 ? 158.869 133.946 47.260 1.00 29.89 ? 308 GLU A O 1 ATOM 2367 C CB . GLU A 1 308 ? 158.965 130.651 47.210 1.00 28.42 ? 308 GLU A CB 1 ATOM 2368 C CG . GLU A 1 308 ? 159.919 131.049 48.331 1.00 32.53 ? 308 GLU A CG 1 ATOM 2369 C CD . GLU A 1 308 ? 159.214 131.288 49.662 1.00 40.52 ? 308 GLU A CD 1 ATOM 2370 O OE1 . GLU A 1 308 ? 158.034 130.907 49.798 1.00 42.24 ? 308 GLU A OE1 1 ATOM 2371 O OE2 . GLU A 1 308 ? 159.846 131.843 50.581 1.00 47.16 ? 308 GLU A OE2 1 ATOM 2372 N N . LEU A 1 309 ? 159.282 133.137 45.194 1.00 25.97 ? 309 LEU A N 1 ATOM 2373 C CA . LEU A 1 309 ? 160.157 134.259 44.817 1.00 27.66 ? 309 LEU A CA 1 ATOM 2374 C C . LEU A 1 309 ? 159.430 135.388 44.089 1.00 27.60 ? 309 LEU A C 1 ATOM 2375 O O . LEU A 1 309 ? 160.072 136.269 43.515 1.00 28.05 ? 309 LEU A O 1 ATOM 2376 C CB . LEU A 1 309 ? 161.360 133.771 43.994 1.00 28.89 ? 309 LEU A CB 1 ATOM 2377 C CG . LEU A 1 309 ? 162.220 132.742 44.724 1.00 29.80 ? 309 LEU A CG 1 ATOM 2378 C CD1 . LEU A 1 309 ? 163.428 132.315 43.890 1.00 31.60 ? 309 LEU A CD1 1 ATOM 2379 C CD2 . LEU A 1 309 ? 162.654 133.299 46.081 1.00 30.45 ? 309 LEU A CD2 1 ATOM 2380 N N . GLY A 1 310 ? 158.096 135.362 44.121 1.00 32.17 ? 310 GLY A N 1 ATOM 2381 C CA . GLY A 1 310 ? 157.291 136.459 43.597 1.00 34.48 ? 310 GLY A CA 1 ATOM 2382 C C . GLY A 1 310 ? 157.287 136.641 42.088 1.00 35.76 ? 310 GLY A C 1 ATOM 2383 O O . GLY A 1 310 ? 157.143 137.765 41.597 1.00 30.54 ? 310 GLY A O 1 ATOM 2384 N N . GLN A 1 311 ? 157.439 135.546 41.349 1.00 25.08 ? 311 GLN A N 1 ATOM 2385 C CA . GLN A 1 311 ? 157.469 135.617 39.889 1.00 25.59 ? 311 GLN A CA 1 ATOM 2386 C C . GLN A 1 311 ? 156.119 135.235 39.294 1.00 32.09 ? 311 GLN A C 1 ATOM 2387 O O . GLN A 1 311 ? 155.937 134.109 38.809 1.00 31.47 ? 311 GLN A O 1 ATOM 2388 C CB . GLN A 1 311 ? 158.564 134.699 39.339 1.00 30.88 ? 311 GLN A CB 1 ATOM 2389 C CG . GLN A 1 311 ? 159.903 134.982 39.969 1.00 34.40 ? 311 GLN A CG 1 ATOM 2390 C CD . GLN A 1 311 ? 160.399 136.380 39.638 1.00 39.96 ? 311 GLN A CD 1 ATOM 2391 O OE1 . GLN A 1 311 ? 160.664 137.194 40.532 1.00 40.28 ? 311 GLN A OE1 1 ATOM 2392 N NE2 . GLN A 1 311 ? 160.528 136.665 38.342 1.00 33.10 ? 311 GLN A NE2 1 ATOM 2393 N N . PHE A 1 312 ? 155.176 136.174 39.342 1.00 23.62 ? 312 PHE A N 1 ATOM 2394 C CA . PHE A 1 312 ? 153.828 135.964 38.810 1.00 22.86 ? 312 PHE A CA 1 ATOM 2395 C C . PHE A 1 312 ? 153.155 137.315 38.518 1.00 29.43 ? 312 PHE A C 1 ATOM 2396 O O . PHE A 1 312 ? 153.621 138.370 38.972 1.00 24.23 ? 312 PHE A O 1 ATOM 2397 C CB . PHE A 1 312 ? 152.973 135.158 39.797 1.00 26.25 ? 312 PHE A CB 1 ATOM 2398 C CG . PHE A 1 312 ? 153.072 135.642 41.218 1.00 28.54 ? 312 PHE A CG 1 ATOM 2399 C CD1 . PHE A 1 312 ? 152.339 136.744 41.649 1.00 27.12 ? 312 PHE A CD1 1 ATOM 2400 C CD2 . PHE A 1 312 ? 153.909 135.004 42.121 1.00 31.07 ? 312 PHE A CD2 1 ATOM 2401 C CE1 . PHE A 1 312 ? 152.438 137.198 42.967 1.00 31.01 ? 312 PHE A CE1 1 ATOM 2402 C CE2 . PHE A 1 312 ? 154.017 135.444 43.435 1.00 26.05 ? 312 PHE A CE2 1 ATOM 2403 C CZ . PHE A 1 312 ? 153.280 136.550 43.860 1.00 29.14 ? 312 PHE A CZ 1 ATOM 2404 N N . LYS A 1 313 ? 152.064 137.271 37.760 1.00 22.06 ? 313 LYS A N 1 ATOM 2405 C CA . LYS A 1 313 ? 151.288 138.460 37.417 1.00 29.42 ? 313 LYS A CA 1 ATOM 2406 C C . LYS A 1 313 ? 150.828 139.173 38.689 1.00 26.69 ? 313 LYS A C 1 ATOM 2407 O O . LYS A 1 313 ? 150.253 138.543 39.584 1.00 26.04 ? 313 LYS A O 1 ATOM 2408 C CB . LYS A 1 313 ? 150.056 138.050 36.583 1.00 27.76 ? 313 LYS A CB 1 ATOM 2409 C CG . LYS A 1 313 ? 149.169 139.219 36.132 1.00 29.55 ? 313 LYS A CG 1 ATOM 2410 C CD . LYS A 1 313 ? 147.977 138.727 35.312 1.00 32.97 ? 313 LYS A CD 1 ATOM 2411 C CE . LYS A 1 313 ? 147.083 139.885 34.860 1.00 34.25 ? 313 LYS A CE 1 ATOM 2412 N NZ . LYS A 1 313 ? 147.670 140.703 33.752 1.00 27.21 ? 313 LYS A NZ 1 ATOM 2413 N N . LYS A 1 314 ? 151.086 140.473 38.772 1.00 22.77 ? 314 LYS A N 1 ATOM 2414 C CA . LYS A 1 314 ? 150.686 141.259 39.934 1.00 31.46 ? 314 LYS A CA 1 ATOM 2415 C C . LYS A 1 314 ? 149.278 141.801 39.694 1.00 28.85 ? 314 LYS A C 1 ATOM 2416 O O . LYS A 1 314 ? 149.086 142.700 38.871 1.00 25.96 ? 314 LYS A O 1 ATOM 2417 C CB . LYS A 1 314 ? 151.678 142.409 40.187 1.00 34.17 ? 314 LYS A CB 1 ATOM 2418 C CG . LYS A 1 314 ? 153.118 141.943 40.488 1.00 35.34 ? 314 LYS A CG 1 ATOM 2419 C CD . LYS A 1 314 ? 153.128 140.799 41.513 1.00 37.14 ? 314 LYS A CD 1 ATOM 2420 C CE . LYS A 1 314 ? 154.547 140.394 41.922 1.00 41.18 ? 314 LYS A CE 1 ATOM 2421 N NZ . LYS A 1 314 ? 155.362 139.896 40.785 1.00 40.12 ? 314 LYS A NZ 1 ATOM 2422 N N . THR A 1 315 ? 148.293 141.225 40.380 1.00 30.21 ? 315 THR A N 1 ATOM 2423 C CA . THR A 1 315 ? 146.894 141.614 40.207 1.00 20.82 ? 315 THR A CA 1 ATOM 2424 C C . THR A 1 315 ? 146.089 141.140 41.426 1.00 26.13 ? 315 THR A C 1 ATOM 2425 O O . THR A 1 315 ? 146.659 140.554 42.356 1.00 25.63 ? 315 THR A O 1 ATOM 2426 C CB . THR A 1 315 ? 146.312 141.022 38.913 1.00 27.52 ? 315 THR A CB 1 ATOM 2427 O OG1 . THR A 1 315 ? 145.038 141.618 38.642 1.00 24.28 ? 315 THR A OG1 1 ATOM 2428 C CG2 . THR A 1 315 ? 146.152 139.486 39.024 1.00 19.49 ? 315 THR A CG2 1 ATOM 2429 N N . GLN A 1 316 ? 144.780 141.381 41.433 1.00 23.60 ? 316 GLN A N 1 ATOM 2430 C CA . GLN A 1 316 ? 143.944 140.978 42.568 1.00 26.39 ? 316 GLN A CA 1 ATOM 2431 C C . GLN A 1 316 ? 143.511 139.531 42.375 1.00 24.17 ? 316 GLN A C 1 ATOM 2432 O O . GLN A 1 316 ? 143.329 139.087 41.240 1.00 24.84 ? 316 GLN A O 1 ATOM 2433 C CB . GLN A 1 316 ? 142.693 141.874 42.692 1.00 20.30 ? 316 GLN A CB 1 ATOM 2434 C CG . GLN A 1 316 ? 142.980 143.378 42.924 1.00 27.67 ? 316 GLN A CG 1 ATOM 2435 C CD . GLN A 1 316 ? 143.426 144.087 41.654 1.00 27.00 ? 316 GLN A CD 1 ATOM 2436 O OE1 . GLN A 1 316 ? 142.930 143.808 40.558 1.00 22.86 ? 316 GLN A OE1 1 ATOM 2437 N NE2 . GLN A 1 316 ? 144.384 144.986 41.795 1.00 34.39 ? 316 GLN A NE2 1 ATOM 2438 N N . ILE A 1 317 ? 143.348 138.791 43.470 1.00 18.65 ? 317 ILE A N 1 ATOM 2439 C CA . ILE A 1 317 ? 142.777 137.444 43.386 1.00 18.67 ? 317 ILE A CA 1 ATOM 2440 C C . ILE A 1 317 ? 141.669 137.238 44.418 1.00 22.37 ? 317 ILE A C 1 ATOM 2441 O O . ILE A 1 317 ? 141.680 137.864 45.483 1.00 21.01 ? 317 ILE A O 1 ATOM 2442 C CB . ILE A 1 317 ? 143.835 136.325 43.618 1.00 23.29 ? 317 ILE A CB 1 ATOM 2443 C CG1 . ILE A 1 317 ? 144.522 136.514 44.972 1.00 20.20 ? 317 ILE A CG1 1 ATOM 2444 C CG2 . ILE A 1 317 ? 144.869 136.294 42.498 1.00 19.57 ? 317 ILE A CG2 1 ATOM 2445 C CD1 . ILE A 1 317 ? 145.511 135.369 45.308 1.00 24.32 ? 317 ILE A CD1 1 ATOM 2446 N N . LEU A 1 318 ? 140.729 136.349 44.089 1.00 20.68 ? 318 LEU A N 1 ATOM 2447 C CA . LEU A 1 318 ? 139.663 135.924 44.994 1.00 20.58 ? 318 LEU A CA 1 ATOM 2448 C C . LEU A 1 318 ? 139.815 134.411 45.103 1.00 24.87 ? 318 LEU A C 1 ATOM 2449 O O . LEU A 1 318 ? 139.790 133.701 44.078 1.00 17.61 ? 318 LEU A O 1 ATOM 2450 C CB . LEU A 1 318 ? 138.284 136.289 44.410 1.00 16.15 ? 318 LEU A CB 1 ATOM 2451 C CG . LEU A 1 318 ? 137.019 136.178 45.270 1.00 24.95 ? 318 LEU A CG 1 ATOM 2452 C CD1 . LEU A 1 318 ? 135.847 136.885 44.597 1.00 28.20 ? 318 LEU A CD1 1 ATOM 2453 C CD2 . LEU A 1 318 ? 136.662 134.719 45.536 1.00 23.67 ? 318 LEU A CD2 1 ATOM 2454 N N . VAL A 1 319 ? 139.991 133.915 46.328 1.00 15.15 ? 319 VAL A N 1 ATOM 2455 C CA . VAL A 1 319 ? 140.241 132.480 46.559 1.00 14.82 ? 319 VAL A CA 1 ATOM 2456 C C . VAL A 1 319 ? 139.312 131.953 47.649 1.00 20.05 ? 319 VAL A C 1 ATOM 2457 O O . VAL A 1 319 ? 138.991 132.689 48.590 1.00 17.51 ? 319 VAL A O 1 ATOM 2458 C CB . VAL A 1 319 ? 141.687 132.245 47.065 1.00 18.87 ? 319 VAL A CB 1 ATOM 2459 C CG1 . VAL A 1 319 ? 142.035 130.745 47.052 1.00 18.83 ? 319 VAL A CG1 1 ATOM 2460 C CG2 . VAL A 1 319 ? 142.703 133.034 46.226 1.00 20.68 ? 319 VAL A CG2 1 ATOM 2461 N N . GLY A 1 320 ? 138.900 130.688 47.559 1.00 16.44 ? 320 GLY A N 1 ATOM 2462 C CA . GLY A 1 320 ? 138.096 130.096 48.618 1.00 19.73 ? 320 GLY A CA 1 ATOM 2463 C C . GLY A 1 320 ? 137.971 128.581 48.556 1.00 23.65 ? 320 GLY A C 1 ATOM 2464 O O . GLY A 1 320 ? 138.454 127.951 47.603 1.00 19.96 ? 320 GLY A O 1 ATOM 2465 N N . VAL A 1 321 ? 137.319 128.002 49.574 1.00 20.09 ? 321 VAL A N 1 ATOM 2466 C CA . VAL A 1 321 ? 137.165 126.551 49.703 1.00 18.13 ? 321 VAL A CA 1 ATOM 2467 C C . VAL A 1 321 ? 135.828 126.265 50.363 1.00 24.62 ? 321 VAL A C 1 ATOM 2468 O O . VAL A 1 321 ? 135.189 127.178 50.900 1.00 20.10 ? 321 VAL A O 1 ATOM 2469 C CB . VAL A 1 321 ? 138.266 125.932 50.581 1.00 18.63 ? 321 VAL A CB 1 ATOM 2470 C CG1 . VAL A 1 321 ? 139.658 126.116 49.933 1.00 16.88 ? 321 VAL A CG1 1 ATOM 2471 C CG2 . VAL A 1 321 ? 138.225 126.561 51.985 1.00 16.47 ? 321 VAL A CG2 1 ATOM 2472 N N . ASN A 1 322 ? 135.415 125.000 50.320 1.00 17.45 ? 322 ASN A N 1 ATOM 2473 C CA . ASN A 1 322 ? 134.153 124.569 50.901 1.00 19.43 ? 322 ASN A CA 1 ATOM 2474 C C . ASN A 1 322 ? 134.396 123.856 52.229 1.00 23.60 ? 322 ASN A C 1 ATOM 2475 O O . ASN A 1 322 ? 135.484 123.332 52.469 1.00 18.81 ? 322 ASN A O 1 ATOM 2476 C CB . ASN A 1 322 ? 133.410 123.640 49.927 1.00 22.83 ? 322 ASN A CB 1 ATOM 2477 C CG . ASN A 1 322 ? 133.013 124.341 48.620 1.00 25.93 ? 322 ASN A CG 1 ATOM 2478 O OD1 . ASN A 1 322 ? 133.142 125.562 48.494 1.00 21.83 ? 322 ASN A OD1 1 ATOM 2479 N ND2 . ASN A 1 322 ? 132.510 123.568 47.651 1.00 23.32 ? 322 ASN A ND2 1 ATOM 2480 N N . LYS A 1 323 ? 133.384 123.823 53.090 1.00 27.59 ? 323 LYS A N 1 ATOM 2481 C CA . LYS A 1 323 ? 133.537 123.219 54.415 1.00 23.90 ? 323 LYS A CA 1 ATOM 2482 C C . LYS A 1 323 ? 133.915 121.725 54.409 1.00 28.87 ? 323 LYS A C 1 ATOM 2483 O O . LYS A 1 323 ? 134.654 121.271 55.292 1.00 21.49 ? 323 LYS A O 1 ATOM 2484 C CB . LYS A 1 323 ? 132.253 123.428 55.227 1.00 28.39 ? 323 LYS A CB 1 ATOM 2485 C CG . LYS A 1 323 ? 132.268 122.818 56.615 1.00 33.34 ? 323 LYS A CG 1 ATOM 2486 C CD . LYS A 1 323 ? 130.996 123.203 57.354 1.00 43.98 ? 323 LYS A CD 1 ATOM 2487 C CE . LYS A 1 323 ? 130.867 122.471 58.674 1.00 51.61 ? 323 LYS A CE 1 ATOM 2488 N NZ . LYS A 1 323 ? 129.636 122.889 59.392 1.00 64.02 ? 323 LYS A NZ 1 ATOM 2489 N N . ASP A 1 324 ? 133.405 120.954 53.446 1.00 20.77 ? 324 ASP A N 1 ATOM 2490 C CA . ASP A 1 324 ? 133.694 119.520 53.427 1.00 21.39 ? 324 ASP A CA 1 ATOM 2491 C C . ASP A 1 324 ? 134.300 119.040 52.095 1.00 24.60 ? 324 ASP A C 1 ATOM 2492 O O . ASP A 1 324 ? 133.796 118.089 51.487 1.00 22.87 ? 324 ASP A O 1 ATOM 2493 C CB . ASP A 1 324 ? 132.421 118.709 53.780 1.00 22.76 ? 324 ASP A CB 1 ATOM 2494 C CG . ASP A 1 324 ? 131.851 119.071 55.164 1.00 30.47 ? 324 ASP A CG 1 ATOM 2495 O OD1 . ASP A 1 324 ? 132.440 118.655 56.184 1.00 30.22 ? 324 ASP A OD1 1 ATOM 2496 O OD2 . ASP A 1 324 ? 130.810 119.766 55.235 1.00 28.63 ? 324 ASP A OD2 1 ATOM 2497 N N . GLU A 1 325 ? 135.380 119.687 51.658 1.00 20.84 ? 325 GLU A N 1 ATOM 2498 C CA . GLU A 1 325 ? 136.069 119.316 50.413 1.00 23.24 ? 325 GLU A CA 1 ATOM 2499 C C . GLU A 1 325 ? 136.366 117.812 50.301 1.00 24.60 ? 325 GLU A C 1 ATOM 2500 O O . GLU A 1 325 ? 136.269 117.233 49.224 1.00 25.30 ? 325 GLU A O 1 ATOM 2501 C CB . GLU A 1 325 ? 137.409 120.069 50.282 1.00 21.76 ? 325 GLU A CB 1 ATOM 2502 C CG . GLU A 1 325 ? 137.313 121.611 50.214 1.00 23.55 ? 325 GLU A CG 1 ATOM 2503 C CD . GLU A 1 325 ? 136.809 122.105 48.871 1.00 21.52 ? 325 GLU A CD 1 ATOM 2504 O OE1 . GLU A 1 325 ? 136.479 121.273 47.995 1.00 21.16 ? 325 GLU A OE1 1 ATOM 2505 O OE2 . GLU A 1 325 ? 136.724 123.337 48.687 1.00 20.48 ? 325 GLU A OE2 1 ATOM 2506 N N . GLY A 1 326 ? 136.734 117.186 51.412 1.00 20.76 ? 326 GLY A N 1 ATOM 2507 C CA . GLY A 1 326 ? 137.259 115.830 51.365 1.00 21.64 ? 326 GLY A CA 1 ATOM 2508 C C . GLY A 1 326 ? 136.262 114.683 51.265 1.00 37.53 ? 326 GLY A C 1 ATOM 2509 O O . GLY A 1 326 ? 136.630 113.591 50.828 1.00 23.52 ? 326 GLY A O 1 ATOM 2510 N N . THR A 1 327 ? 135.010 114.903 51.651 1.00 23.01 ? 327 THR A N 1 ATOM 2511 C CA . THR A 1 327 ? 134.075 113.773 51.785 1.00 24.02 ? 327 THR A CA 1 ATOM 2512 C C . THR A 1 327 ? 133.718 113.025 50.495 1.00 24.54 ? 327 THR A C 1 ATOM 2513 O O . THR A 1 327 ? 133.547 111.809 50.520 1.00 25.40 ? 327 THR A O 1 ATOM 2514 C CB . THR A 1 327 ? 132.769 114.166 52.489 1.00 25.09 ? 327 THR A CB 1 ATOM 2515 O OG1 . THR A 1 327 ? 132.169 115.257 51.792 1.00 25.23 ? 327 THR A OG1 1 ATOM 2516 C CG2 . THR A 1 327 ? 133.037 114.579 53.940 1.00 25.29 ? 327 THR A CG2 1 ATOM 2517 N N . ALA A 1 328 ? 133.609 113.735 49.377 1.00 26.95 ? 328 ALA A N 1 ATOM 2518 C CA . ALA A 1 328 ? 133.233 113.106 48.095 1.00 25.33 ? 328 ALA A CA 1 ATOM 2519 C C . ALA A 1 328 ? 134.102 111.886 47.757 1.00 25.60 ? 328 ALA A C 1 ATOM 2520 O O . ALA A 1 328 ? 133.622 110.892 47.203 1.00 27.41 ? 328 ALA A O 1 ATOM 2521 C CB . ALA A 1 328 ? 133.312 114.134 46.972 1.00 25.31 ? 328 ALA A CB 1 ATOM 2522 N N . PHE A 1 329 ? 135.380 111.963 48.122 1.00 26.99 ? 329 PHE A N 1 ATOM 2523 C CA . PHE A 1 329 ? 136.364 110.971 47.700 1.00 31.85 ? 329 PHE A CA 1 ATOM 2524 C C . PHE A 1 329 ? 136.313 109.689 48.519 1.00 26.03 ? 329 PHE A C 1 ATOM 2525 O O . PHE A 1 329 ? 136.761 108.635 48.059 1.00 30.83 ? 329 PHE A O 1 ATOM 2526 C CB . PHE A 1 329 ? 137.774 111.595 47.715 1.00 27.87 ? 329 PHE A CB 1 ATOM 2527 C CG . PHE A 1 329 ? 137.891 112.799 46.821 1.00 29.40 ? 329 PHE A CG 1 ATOM 2528 C CD1 . PHE A 1 329 ? 138.158 112.641 45.468 1.00 27.65 ? 329 PHE A CD1 1 ATOM 2529 C CD2 . PHE A 1 329 ? 137.680 114.085 47.321 1.00 30.06 ? 329 PHE A CD2 1 ATOM 2530 C CE1 . PHE A 1 329 ? 138.230 113.739 44.626 1.00 29.53 ? 329 PHE A CE1 1 ATOM 2531 C CE2 . PHE A 1 329 ? 137.757 115.199 46.486 1.00 23.18 ? 329 PHE A CE2 1 ATOM 2532 C CZ . PHE A 1 329 ? 138.030 115.019 45.132 1.00 25.30 ? 329 PHE A CZ 1 ATOM 2533 N N . LEU A 1 330 ? 135.761 109.777 49.725 1.00 30.07 ? 330 LEU A N 1 ATOM 2534 C CA . LEU A 1 330 ? 135.722 108.629 50.638 1.00 35.32 ? 330 LEU A CA 1 ATOM 2535 C C . LEU A 1 330 ? 134.897 107.454 50.101 1.00 33.22 ? 330 LEU A C 1 ATOM 2536 O O . LEU A 1 330 ? 135.196 106.294 50.391 1.00 32.84 ? 330 LEU A O 1 ATOM 2537 C CB . LEU A 1 330 ? 135.215 109.063 52.019 1.00 34.66 ? 330 LEU A CB 1 ATOM 2538 C CG . LEU A 1 330 ? 135.969 110.250 52.636 1.00 35.83 ? 330 LEU A CG 1 ATOM 2539 C CD1 . LEU A 1 330 ? 135.419 110.602 54.009 1.00 25.61 ? 330 LEU A CD1 1 ATOM 2540 C CD2 . LEU A 1 330 ? 137.467 109.969 52.717 1.00 31.48 ? 330 LEU A CD2 1 ATOM 2541 N N . VAL A 1 331 ? 133.868 107.741 49.312 1.00 30.68 ? 331 VAL A N 1 ATOM 2542 C CA . VAL A 1 331 ? 133.023 106.660 48.803 1.00 36.46 ? 331 VAL A CA 1 ATOM 2543 C C . VAL A 1 331 ? 133.552 106.032 47.510 1.00 38.03 ? 331 VAL A C 1 ATOM 2544 O O . VAL A 1 331 ? 132.883 105.201 46.901 1.00 37.06 ? 331 VAL A O 1 ATOM 2545 C CB . VAL A 1 331 ? 131.552 107.102 48.635 1.00 38.57 ? 331 VAL A CB 1 ATOM 2546 C CG1 . VAL A 1 331 ? 131.003 107.590 49.972 1.00 36.36 ? 331 VAL A CG1 1 ATOM 2547 C CG2 . VAL A 1 331 ? 131.409 108.190 47.551 1.00 31.11 ? 331 VAL A CG2 1 ATOM 2548 N N . TYR A 1 332 ? 134.751 106.432 47.094 1.00 32.44 ? 332 TYR A N 1 ATOM 2549 C CA . TYR A 1 332 ? 135.367 105.861 45.896 1.00 34.65 ? 332 TYR A CA 1 ATOM 2550 C C . TYR A 1 332 ? 136.558 104.967 46.281 1.00 42.74 ? 332 TYR A C 1 ATOM 2551 O O . TYR A 1 332 ? 137.544 104.878 45.537 1.00 42.81 ? 332 TYR A O 1 ATOM 2552 C CB . TYR A 1 332 ? 135.819 106.969 44.929 1.00 31.86 ? 332 TYR A CB 1 ATOM 2553 C CG . TYR A 1 332 ? 134.691 107.678 44.214 1.00 32.01 ? 332 TYR A CG 1 ATOM 2554 C CD1 . TYR A 1 332 ? 134.060 108.779 44.783 1.00 30.43 ? 332 TYR A CD1 1 ATOM 2555 C CD2 . TYR A 1 332 ? 134.250 107.241 42.966 1.00 34.14 ? 332 TYR A CD2 1 ATOM 2556 C CE1 . TYR A 1 332 ? 133.018 109.427 44.124 1.00 30.94 ? 332 TYR A CE1 1 ATOM 2557 C CE2 . TYR A 1 332 ? 133.214 107.880 42.308 1.00 34.60 ? 332 TYR A CE2 1 ATOM 2558 C CZ . TYR A 1 332 ? 132.605 108.973 42.892 1.00 32.97 ? 332 TYR A CZ 1 ATOM 2559 O OH . TYR A 1 332 ? 131.575 109.611 42.238 1.00 33.76 ? 332 TYR A OH 1 ATOM 2560 N N . GLY A 1 333 ? 136.475 104.317 47.444 1.00 43.65 ? 333 GLY A N 1 ATOM 2561 C CA . GLY A 1 333 ? 137.502 103.361 47.838 1.00 47.19 ? 333 GLY A CA 1 ATOM 2562 C C . GLY A 1 333 ? 137.792 103.116 49.315 1.00 45.38 ? 333 GLY A C 1 ATOM 2563 O O . GLY A 1 333 ? 138.280 102.044 49.664 1.00 53.41 ? 333 GLY A O 1 ATOM 2564 N N . ALA A 1 334 ? 137.526 104.087 50.190 1.00 38.06 ? 334 ALA A N 1 ATOM 2565 C CA . ALA A 1 334 ? 137.808 103.891 51.616 1.00 34.72 ? 334 ALA A CA 1 ATOM 2566 C C . ALA A 1 334 ? 136.846 102.868 52.251 1.00 41.85 ? 334 ALA A C 1 ATOM 2567 O O . ALA A 1 334 ? 135.623 102.934 52.048 1.00 42.87 ? 334 ALA A O 1 ATOM 2568 C CB . ALA A 1 334 ? 137.779 105.222 52.364 1.00 34.18 ? 334 ALA A CB 1 ATOM 2569 N N . PRO A 1 335 ? 137.398 101.898 53.005 1.00 40.90 ? 335 PRO A N 1 ATOM 2570 C CA . PRO A 1 335 ? 136.561 100.814 53.546 1.00 39.46 ? 335 PRO A CA 1 ATOM 2571 C C . PRO A 1 335 ? 135.612 101.328 54.628 1.00 39.47 ? 335 PRO A C 1 ATOM 2572 O O . PRO A 1 335 ? 135.970 102.248 55.378 1.00 37.40 ? 335 PRO A O 1 ATOM 2573 C CB . PRO A 1 335 ? 137.583 99.840 54.152 1.00 42.11 ? 335 PRO A CB 1 ATOM 2574 C CG . PRO A 1 335 ? 138.908 100.232 53.580 1.00 43.83 ? 335 PRO A CG 1 ATOM 2575 C CD . PRO A 1 335 ? 138.824 101.707 53.319 1.00 38.92 ? 335 PRO A CD 1 ATOM 2576 N N . GLY A 1 336 ? 134.415 100.753 54.694 1.00 41.02 ? 336 GLY A N 1 ATOM 2577 C CA . GLY A 1 336 ? 133.405 101.185 55.642 1.00 48.28 ? 336 GLY A CA 1 ATOM 2578 C C . GLY A 1 336 ? 132.497 102.293 55.125 1.00 46.19 ? 336 GLY A C 1 ATOM 2579 O O . GLY A 1 336 ? 131.442 102.559 55.708 1.00 49.27 ? 336 GLY A O 1 ATOM 2580 N N . PHE A 1 337 ? 132.891 102.942 54.033 1.00 37.50 ? 337 PHE A N 1 ATOM 2581 C CA . PHE A 1 337 ? 132.136 104.092 53.543 1.00 37.74 ? 337 PHE A CA 1 ATOM 2582 C C . PHE A 1 337 ? 131.076 103.722 52.497 1.00 43.48 ? 337 PHE A C 1 ATOM 2583 O O . PHE A 1 337 ? 131.227 102.758 51.740 1.00 51.12 ? 337 PHE A O 1 ATOM 2584 C CB . PHE A 1 337 ? 133.074 105.185 53.014 1.00 33.26 ? 337 PHE A CB 1 ATOM 2585 C CG . PHE A 1 337 ? 133.805 105.938 54.092 1.00 42.73 ? 337 PHE A CG 1 ATOM 2586 C CD1 . PHE A 1 337 ? 134.998 105.450 54.614 1.00 39.87 ? 337 PHE A CD1 1 ATOM 2587 C CD2 . PHE A 1 337 ? 133.314 107.152 54.571 1.00 30.90 ? 337 PHE A CD2 1 ATOM 2588 C CE1 . PHE A 1 337 ? 135.688 106.156 55.608 1.00 31.14 ? 337 PHE A CE1 1 ATOM 2589 C CE2 . PHE A 1 337 ? 133.995 107.855 55.564 1.00 47.96 ? 337 PHE A CE2 1 ATOM 2590 C CZ . PHE A 1 337 ? 135.185 107.358 56.083 1.00 30.15 ? 337 PHE A CZ 1 ATOM 2591 N N . SER A 1 338 ? 129.998 104.499 52.482 1.00 40.11 ? 338 SER A N 1 ATOM 2592 C CA . SER A 1 338 ? 128.885 104.291 51.557 1.00 42.81 ? 338 SER A CA 1 ATOM 2593 C C . SER A 1 338 ? 128.015 105.533 51.546 1.00 37.73 ? 338 SER A C 1 ATOM 2594 O O . SER A 1 338 ? 127.692 106.076 52.600 1.00 41.37 ? 338 SER A O 1 ATOM 2595 C CB . SER A 1 338 ? 128.028 103.093 51.980 1.00 41.74 ? 338 SER A CB 1 ATOM 2596 O OG . SER A 1 338 ? 126.786 103.094 51.275 1.00 43.30 ? 338 SER A OG 1 ATOM 2597 N N . LYS A 1 339 ? 127.612 105.978 50.363 1.00 45.57 ? 339 LYS A N 1 ATOM 2598 C CA . LYS A 1 339 ? 126.689 107.098 50.282 1.00 42.98 ? 339 LYS A CA 1 ATOM 2599 C C . LYS A 1 339 ? 125.309 106.669 50.788 1.00 42.00 ? 339 LYS A C 1 ATOM 2600 O O . LYS A 1 339 ? 124.437 107.517 50.994 1.00 45.02 ? 339 LYS A O 1 ATOM 2601 C CB . LYS A 1 339 ? 126.571 107.603 48.842 1.00 36.97 ? 339 LYS A CB 1 ATOM 2602 C CG . LYS A 1 339 ? 125.633 106.732 47.969 1.00 39.61 ? 339 LYS A CG 1 ATOM 2603 C CD . LYS A 1 339 ? 125.508 107.267 46.550 1.00 39.64 ? 339 LYS A CD 1 ATOM 2604 C CE . LYS A 1 339 ? 124.439 106.502 45.742 1.00 42.71 ? 339 LYS A CE 1 ATOM 2605 N NZ . LYS A 1 339 ? 123.051 106.718 46.261 1.00 44.44 ? 339 LYS A NZ 1 ATOM 2606 N N . ASP A 1 340 ? 125.110 105.361 50.975 1.00 42.13 ? 340 ASP A N 1 ATOM 2607 C CA . ASP A 1 340 ? 123.791 104.829 51.326 1.00 48.43 ? 340 ASP A CA 1 ATOM 2608 C C . ASP A 1 340 ? 123.621 104.436 52.801 1.00 54.04 ? 340 ASP A C 1 ATOM 2609 O O . ASP A 1 340 ? 122.598 103.857 53.173 1.00 49.59 ? 340 ASP A O 1 ATOM 2610 C CB . ASP A 1 340 ? 123.415 103.638 50.426 1.00 47.63 ? 340 ASP A CB 1 ATOM 2611 C CG . ASP A 1 340 ? 123.259 104.033 48.958 1.00 49.47 ? 340 ASP A CG 1 ATOM 2612 O OD1 . ASP A 1 340 ? 122.608 105.062 48.660 1.00 46.85 ? 340 ASP A OD1 1 ATOM 2613 O OD2 . ASP A 1 340 ? 123.801 103.310 48.099 1.00 47.87 ? 340 ASP A OD2 1 ATOM 2614 N N . ASN A 1 341 ? 124.623 104.722 53.630 1.00 44.79 ? 341 ASN A N 1 ATOM 2615 C CA . ASN A 1 341 ? 124.442 104.664 55.087 1.00 59.49 ? 341 ASN A CA 1 ATOM 2616 C C . ASN A 1 341 ? 125.287 105.733 55.771 1.00 55.59 ? 341 ASN A C 1 ATOM 2617 O O . ASN A 1 341 ? 125.955 106.510 55.094 1.00 40.99 ? 341 ASN A O 1 ATOM 2618 C CB . ASN A 1 341 ? 124.683 103.258 55.674 1.00 48.38 ? 341 ASN A CB 1 ATOM 2619 C CG . ASN A 1 341 ? 126.090 102.733 55.422 1.00 49.44 ? 341 ASN A CG 1 ATOM 2620 O OD1 . ASN A 1 341 ? 127.065 103.497 55.352 1.00 45.12 ? 341 ASN A OD1 1 ATOM 2621 N ND2 . ASN A 1 341 ? 126.198 101.415 55.284 1.00 60.06 ? 341 ASN A ND2 1 ATOM 2622 N N . ASN A 1 342 ? 125.255 105.792 57.097 1.00 44.84 ? 342 ASN A N 1 ATOM 2623 C CA . ASN A 1 342 ? 125.924 106.887 57.796 1.00 45.22 ? 342 ASN A CA 1 ATOM 2624 C C . ASN A 1 342 ? 127.452 106.750 57.909 1.00 40.88 ? 342 ASN A C 1 ATOM 2625 O O . ASN A 1 342 ? 128.103 107.619 58.474 1.00 39.53 ? 342 ASN A O 1 ATOM 2626 C CB . ASN A 1 342 ? 125.293 107.122 59.170 1.00 48.15 ? 342 ASN A CB 1 ATOM 2627 C CG . ASN A 1 342 ? 125.401 105.915 60.070 1.00 60.14 ? 342 ASN A CG 1 ATOM 2628 O OD1 . ASN A 1 342 ? 126.097 104.951 59.753 1.00 63.08 ? 342 ASN A OD1 1 ATOM 2629 N ND2 . ASN A 1 342 ? 124.708 105.958 61.203 1.00 73.06 ? 342 ASN A ND2 1 ATOM 2630 N N . SER A 1 343 ? 128.003 105.653 57.389 1.00 41.43 ? 343 SER A N 1 ATOM 2631 C CA . SER A 1 343 ? 129.460 105.440 57.323 1.00 40.04 ? 343 SER A CA 1 ATOM 2632 C C . SER A 1 343 ? 130.223 105.596 58.648 1.00 43.77 ? 343 SER A C 1 ATOM 2633 O O . SER A 1 343 ? 131.318 106.161 58.671 1.00 41.76 ? 343 SER A O 1 ATOM 2634 C CB . SER A 1 343 ? 130.092 106.336 56.246 1.00 37.82 ? 343 SER A CB 1 ATOM 2635 O OG . SER A 1 343 ? 129.507 106.113 54.970 1.00 39.78 ? 343 SER A OG 1 ATOM 2636 N N . ILE A 1 344 ? 129.658 105.093 59.744 1.00 42.13 ? 344 ILE A N 1 ATOM 2637 C CA . ILE A 1 344 ? 130.373 105.087 61.018 1.00 42.95 ? 344 ILE A CA 1 ATOM 2638 C C . ILE A 1 344 ? 131.513 104.073 60.947 1.00 43.03 ? 344 ILE A C 1 ATOM 2639 O O . ILE A 1 344 ? 131.283 102.872 60.990 1.00 50.09 ? 344 ILE A O 1 ATOM 2640 C CB . ILE A 1 344 ? 129.450 104.706 62.202 1.00 55.63 ? 344 ILE A CB 1 ATOM 2641 C CG1 . ILE A 1 344 ? 128.275 105.682 62.326 1.00 52.37 ? 344 ILE A CG1 1 ATOM 2642 C CG2 . ILE A 1 344 ? 130.243 104.660 63.506 1.00 55.27 ? 344 ILE A CG2 1 ATOM 2643 C CD1 . ILE A 1 344 ? 128.680 107.083 62.761 1.00 45.50 ? 344 ILE A CD1 1 ATOM 2644 N N . ILE A 1 345 ? 132.744 104.548 60.828 1.00 40.82 ? 345 ILE A N 1 ATOM 2645 C CA . ILE A 1 345 ? 133.875 103.637 60.711 1.00 41.09 ? 345 ILE A CA 1 ATOM 2646 C C . ILE A 1 345 ? 134.637 103.470 62.023 1.00 48.99 ? 345 ILE A C 1 ATOM 2647 O O . ILE A 1 345 ? 134.502 104.281 62.941 1.00 49.62 ? 345 ILE A O 1 ATOM 2648 C CB . ILE A 1 345 ? 134.855 104.095 59.622 1.00 45.08 ? 345 ILE A CB 1 ATOM 2649 C CG1 . ILE A 1 345 ? 135.235 105.568 59.832 1.00 36.11 ? 345 ILE A CG1 1 ATOM 2650 C CG2 . ILE A 1 345 ? 134.248 103.868 58.238 1.00 37.61 ? 345 ILE A CG2 1 ATOM 2651 C CD1 . ILE A 1 345 ? 136.536 105.954 59.147 1.00 33.81 ? 345 ILE A CD1 1 ATOM 2652 N N . THR A 1 346 ? 135.444 102.414 62.102 1.00 52.07 ? 346 THR A N 1 ATOM 2653 C CA . THR A 1 346 ? 136.268 102.162 63.282 1.00 54.51 ? 346 THR A CA 1 ATOM 2654 C C . THR A 1 346 ? 137.682 102.733 63.143 1.00 53.74 ? 346 THR A C 1 ATOM 2655 O O . THR A 1 346 ? 138.104 103.121 62.050 1.00 41.09 ? 346 THR A O 1 ATOM 2656 C CB . THR A 1 346 ? 136.385 100.664 63.560 1.00 51.43 ? 346 THR A CB 1 ATOM 2657 O OG1 . THR A 1 346 ? 136.852 100.002 62.377 1.00 49.70 ? 346 THR A OG1 1 ATOM 2658 C CG2 . THR A 1 346 ? 135.038 100.099 63.951 1.00 52.94 ? 346 THR A CG2 1 ATOM 2659 N N . ARG A 1 347 ? 138.407 102.779 64.258 1.00 52.84 ? 347 ARG A N 1 ATOM 2660 C CA . ARG A 1 347 ? 139.805 103.192 64.253 1.00 51.43 ? 347 ARG A CA 1 ATOM 2661 C C . ARG A 1 347 ? 140.559 102.410 63.187 1.00 47.52 ? 347 ARG A C 1 ATOM 2662 O O . ARG A 1 347 ? 141.270 102.981 62.353 1.00 44.34 ? 347 ARG A O 1 ATOM 2663 C CB . ARG A 1 347 ? 140.435 102.934 65.621 1.00 46.43 ? 347 ARG A CB 1 ATOM 2664 C CG . ARG A 1 347 ? 141.935 103.198 65.677 1.00 50.67 ? 347 ARG A CG 1 ATOM 2665 C CD . ARG A 1 347 ? 142.455 103.058 67.102 1.00 57.50 ? 347 ARG A CD 1 ATOM 2666 N NE . ARG A 1 347 ? 143.843 103.494 67.225 1.00 63.32 ? 347 ARG A NE 1 ATOM 2667 C CZ . ARG A 1 347 ? 144.219 104.761 67.380 1.00 64.36 ? 347 ARG A CZ 1 ATOM 2668 N NH1 . ARG A 1 347 ? 143.312 105.731 67.430 1.00 59.10 ? 347 ARG A NH1 1 ATOM 2669 N NH2 . ARG A 1 347 ? 145.506 105.062 67.487 1.00 67.29 ? 347 ARG A NH2 1 ATOM 2670 N N . LYS A 1 348 ? 140.358 101.099 63.207 1.00 49.32 ? 348 LYS A N 1 ATOM 2671 C CA . LYS A 1 348 ? 140.986 100.197 62.258 1.00 49.77 ? 348 LYS A CA 1 ATOM 2672 C C . LYS A 1 348 ? 140.675 100.579 60.811 1.00 48.65 ? 348 LYS A C 1 ATOM 2673 O O . LYS A 1 348 ? 141.570 100.576 59.960 1.00 47.65 ? 348 LYS A O 1 ATOM 2674 C CB . LYS A 1 348 ? 140.545 98.760 62.539 1.00 55.39 ? 348 LYS A CB 1 ATOM 2675 C CG . LYS A 1 348 ? 141.306 97.734 61.734 1.00 61.06 ? 348 LYS A CG 1 ATOM 2676 C CD . LYS A 1 348 ? 142.175 96.873 62.622 1.00 68.65 ? 348 LYS A CD 1 ATOM 2677 C CE . LYS A 1 348 ? 141.560 95.496 62.807 1.00 72.12 ? 348 LYS A CE 1 ATOM 2678 N NZ . LYS A 1 348 ? 142.539 94.512 63.350 1.00 77.69 ? 348 LYS A NZ 1 ATOM 2679 N N . GLU A 1 349 ? 139.417 100.923 60.537 1.00 49.00 ? 349 GLU A N 1 ATOM 2680 C CA . GLU A 1 349 ? 139.012 101.334 59.193 1.00 40.87 ? 349 GLU A CA 1 ATOM 2681 C C . GLU A 1 349 ? 139.638 102.677 58.781 1.00 44.21 ? 349 GLU A C 1 ATOM 2682 O O . GLU A 1 349 ? 140.014 102.877 57.616 1.00 43.01 ? 349 GLU A O 1 ATOM 2683 C CB . GLU A 1 349 ? 137.477 101.368 59.075 1.00 41.18 ? 349 GLU A CB 1 ATOM 2684 C CG . GLU A 1 349 ? 136.845 99.957 58.994 1.00 56.01 ? 349 GLU A CG 1 ATOM 2685 C CD . GLU A 1 349 ? 135.331 99.956 59.150 1.00 52.53 ? 349 GLU A CD 1 ATOM 2686 O OE1 . GLU A 1 349 ? 134.807 100.778 59.929 1.00 49.80 ? 349 GLU A OE1 1 ATOM 2687 O OE2 . GLU A 1 349 ? 134.666 99.114 58.509 1.00 56.43 ? 349 GLU A OE2 1 ATOM 2688 N N . PHE A 1 350 ? 139.729 103.599 59.735 1.00 40.66 ? 350 PHE A N 1 ATOM 2689 C CA . PHE A 1 350 ? 140.436 104.858 59.516 1.00 39.92 ? 350 PHE A CA 1 ATOM 2690 C C . PHE A 1 350 ? 141.860 104.535 59.057 1.00 41.24 ? 350 PHE A C 1 ATOM 2691 O O . PHE A 1 350 ? 142.336 105.070 58.052 1.00 36.52 ? 350 PHE A O 1 ATOM 2692 C CB . PHE A 1 350 ? 140.435 105.686 60.806 1.00 37.61 ? 350 PHE A CB 1 ATOM 2693 C CG . PHE A 1 350 ? 141.130 107.024 60.691 1.00 40.80 ? 350 PHE A CG 1 ATOM 2694 C CD1 . PHE A 1 350 ? 140.422 108.161 60.310 1.00 30.89 ? 350 PHE A CD1 1 ATOM 2695 C CD2 . PHE A 1 350 ? 142.486 107.151 60.999 1.00 39.62 ? 350 PHE A CD2 1 ATOM 2696 C CE1 . PHE A 1 350 ? 141.056 109.403 60.217 1.00 38.11 ? 350 PHE A CE1 1 ATOM 2697 C CE2 . PHE A 1 350 ? 143.132 108.388 60.906 1.00 39.06 ? 350 PHE A CE2 1 ATOM 2698 C CZ . PHE A 1 350 ? 142.416 109.517 60.519 1.00 29.57 ? 350 PHE A CZ 1 ATOM 2699 N N . GLN A 1 351 ? 142.522 103.624 59.768 1.00 41.25 ? 351 GLN A N 1 ATOM 2700 C CA . GLN A 1 351 ? 143.886 103.240 59.410 1.00 43.28 ? 351 GLN A CA 1 ATOM 2701 C C . GLN A 1 351 ? 144.008 102.689 57.980 1.00 42.97 ? 351 GLN A C 1 ATOM 2702 O O . GLN A 1 351 ? 144.881 103.123 57.214 1.00 36.44 ? 351 GLN A O 1 ATOM 2703 C CB . GLN A 1 351 ? 144.458 102.271 60.440 1.00 44.73 ? 351 GLN A CB 1 ATOM 2704 C CG . GLN A 1 351 ? 144.819 102.960 61.763 1.00 47.64 ? 351 GLN A CG 1 ATOM 2705 C CD . GLN A 1 351 ? 145.188 101.968 62.843 1.00 49.40 ? 351 GLN A CD 1 ATOM 2706 O OE1 . GLN A 1 351 ? 144.472 100.997 63.074 1.00 51.29 ? 351 GLN A OE1 1 ATOM 2707 N NE2 . GLN A 1 351 ? 146.314 102.201 63.504 1.00 45.01 ? 351 GLN A NE2 1 ATOM 2708 N N . GLU A 1 352 ? 143.122 101.763 57.617 1.00 42.63 ? 352 GLU A N 1 ATOM 2709 C CA . GLU A 1 352 ? 143.071 101.243 56.251 1.00 42.36 ? 352 GLU A CA 1 ATOM 2710 C C . GLU A 1 352 ? 142.760 102.348 55.245 1.00 36.35 ? 352 GLU A C 1 ATOM 2711 O O . GLU A 1 352 ? 143.235 102.316 54.108 1.00 41.48 ? 352 GLU A O 1 ATOM 2712 C CB . GLU A 1 352 ? 142.028 100.126 56.136 1.00 45.58 ? 352 GLU A CB 1 ATOM 2713 C CG . GLU A 1 352 ? 142.336 98.913 57.005 1.00 58.75 ? 352 GLU A CG 1 ATOM 2714 C CD . GLU A 1 352 ? 143.628 98.228 56.605 1.00 69.13 ? 352 GLU A CD 1 ATOM 2715 O OE1 . GLU A 1 352 ? 143.916 98.162 55.391 1.00 73.46 ? 352 GLU A OE1 1 ATOM 2716 O OE2 . GLU A 1 352 ? 144.360 97.762 57.502 1.00 72.87 ? 352 GLU A OE2 1 ATOM 2717 N N . GLY A 1 353 ? 141.948 103.314 55.666 1.00 34.48 ? 353 GLY A N 1 ATOM 2718 C CA . GLY A 1 353 ? 141.635 104.471 54.837 1.00 38.59 ? 353 GLY A CA 1 ATOM 2719 C C . GLY A 1 353 ? 142.857 105.312 54.487 1.00 40.01 ? 353 GLY A C 1 ATOM 2720 O O . GLY A 1 353 ? 142.990 105.775 53.351 1.00 35.91 ? 353 GLY A O 1 ATOM 2721 N N . LEU A 1 354 ? 143.750 105.518 55.455 1.00 37.64 ? 354 LEU A N 1 ATOM 2722 C CA . LEU A 1 354 ? 144.968 106.295 55.205 1.00 34.74 ? 354 LEU A CA 1 ATOM 2723 C C . LEU A 1 354 ? 145.855 105.578 54.194 1.00 36.24 ? 354 LEU A C 1 ATOM 2724 O O . LEU A 1 354 ? 146.537 106.226 53.397 1.00 31.61 ? 354 LEU A O 1 ATOM 2725 C CB . LEU A 1 354 ? 145.757 106.554 56.496 1.00 32.68 ? 354 LEU A CB 1 ATOM 2726 C CG . LEU A 1 354 ? 145.116 107.472 57.539 1.00 36.87 ? 354 LEU A CG 1 ATOM 2727 C CD1 . LEU A 1 354 ? 146.051 107.694 58.730 1.00 31.66 ? 354 LEU A CD1 1 ATOM 2728 C CD2 . LEU A 1 354 ? 144.715 108.807 56.915 1.00 35.53 ? 354 LEU A CD2 1 ATOM 2729 N N . LYS A 1 355 ? 145.841 104.244 54.226 1.00 33.85 ? 355 LYS A N 1 ATOM 2730 C CA . LYS A 1 355 ? 146.634 103.474 53.271 1.00 41.71 ? 355 LYS A CA 1 ATOM 2731 C C . LYS A 1 355 ? 146.126 103.687 51.839 1.00 41.50 ? 355 LYS A C 1 ATOM 2732 O O . LYS A 1 355 ? 146.920 103.780 50.900 1.00 44.11 ? 355 LYS A O 1 ATOM 2733 C CB . LYS A 1 355 ? 146.647 101.986 53.641 1.00 41.25 ? 355 LYS A CB 1 ATOM 2734 C CG . LYS A 1 355 ? 147.512 101.663 54.854 1.00 56.66 ? 355 LYS A CG 1 ATOM 2735 C CD . LYS A 1 355 ? 147.327 100.219 55.317 1.00 66.35 ? 355 LYS A CD 1 ATOM 2736 C CE . LYS A 1 355 ? 147.394 99.244 54.151 1.00 71.20 ? 355 LYS A CE 1 ATOM 2737 N NZ . LYS A 1 355 ? 148.618 99.446 53.328 1.00 74.75 ? 355 LYS A NZ 1 ATOM 2738 N N . ILE A 1 356 ? 144.803 103.772 51.696 1.00 35.97 ? 356 ILE A N 1 ATOM 2739 C CA . ILE A 1 356 ? 144.153 104.103 50.429 1.00 36.67 ? 356 ILE A CA 1 ATOM 2740 C C . ILE A 1 356 ? 144.552 105.494 49.896 1.00 32.96 ? 356 ILE A C 1 ATOM 2741 O O . ILE A 1 356 ? 144.862 105.641 48.715 1.00 36.45 ? 356 ILE A O 1 ATOM 2742 C CB . ILE A 1 356 ? 142.612 104.067 50.565 1.00 39.78 ? 356 ILE A CB 1 ATOM 2743 C CG1 . ILE A 1 356 ? 142.105 102.655 50.895 1.00 44.91 ? 356 ILE A CG1 1 ATOM 2744 C CG2 . ILE A 1 356 ? 141.942 104.602 49.304 1.00 44.32 ? 356 ILE A CG2 1 ATOM 2745 C CD1 . ILE A 1 356 ? 142.361 101.630 49.818 1.00 46.35 ? 356 ILE A CD1 1 ATOM 2746 N N . PHE A 1 357 ? 144.542 106.513 50.753 1.00 29.75 ? 357 PHE A N 1 ATOM 2747 C CA . PHE A 1 357 ? 144.843 107.876 50.296 1.00 28.15 ? 357 PHE A CA 1 ATOM 2748 C C . PHE A 1 357 ? 146.331 108.262 50.355 1.00 36.06 ? 357 PHE A C 1 ATOM 2749 O O . PHE A 1 357 ? 146.725 109.300 49.808 1.00 33.86 ? 357 PHE A O 1 ATOM 2750 C CB . PHE A 1 357 ? 144.006 108.909 51.072 1.00 35.46 ? 357 PHE A CB 1 ATOM 2751 C CG . PHE A 1 357 ? 142.545 108.912 50.692 1.00 32.71 ? 357 PHE A CG 1 ATOM 2752 C CD1 . PHE A 1 357 ? 142.099 109.648 49.599 1.00 31.11 ? 357 PHE A CD1 1 ATOM 2753 C CD2 . PHE A 1 357 ? 141.621 108.177 51.425 1.00 35.71 ? 357 PHE A CD2 1 ATOM 2754 C CE1 . PHE A 1 357 ? 140.738 109.643 49.231 1.00 33.51 ? 357 PHE A CE1 1 ATOM 2755 C CE2 . PHE A 1 357 ? 140.262 108.158 51.070 1.00 35.46 ? 357 PHE A CE2 1 ATOM 2756 C CZ . PHE A 1 357 ? 139.821 108.896 49.970 1.00 33.27 ? 357 PHE A CZ 1 ATOM 2757 N N . PHE A 1 358 ? 147.145 107.456 51.037 1.00 32.31 ? 358 PHE A N 1 ATOM 2758 C CA . PHE A 1 358 ? 148.586 107.743 51.149 1.00 34.48 ? 358 PHE A CA 1 ATOM 2759 C C . PHE A 1 358 ? 149.428 106.479 50.920 1.00 45.47 ? 358 PHE A C 1 ATOM 2760 O O . PHE A 1 358 ? 150.209 106.077 51.790 1.00 46.35 ? 358 PHE A O 1 ATOM 2761 C CB . PHE A 1 358 ? 148.900 108.369 52.513 1.00 29.94 ? 358 PHE A CB 1 ATOM 2762 C CG . PHE A 1 358 ? 148.159 109.660 52.774 1.00 35.14 ? 358 PHE A CG 1 ATOM 2763 C CD1 . PHE A 1 358 ? 146.890 109.653 53.348 1.00 31.36 ? 358 PHE A CD1 1 ATOM 2764 C CD2 . PHE A 1 358 ? 148.729 110.882 52.436 1.00 33.90 ? 358 PHE A CD2 1 ATOM 2765 C CE1 . PHE A 1 358 ? 146.202 110.850 53.578 1.00 25.21 ? 358 PHE A CE1 1 ATOM 2766 C CE2 . PHE A 1 358 ? 148.057 112.084 52.665 1.00 25.48 ? 358 PHE A CE2 1 ATOM 2767 C CZ . PHE A 1 358 ? 146.796 112.073 53.241 1.00 28.04 ? 358 PHE A CZ 1 ATOM 2768 N N . PRO A 1 359 ? 149.282 105.859 49.733 1.00 48.53 ? 359 PRO A N 1 ATOM 2769 C CA . PRO A 1 359 ? 149.861 104.539 49.467 1.00 53.91 ? 359 PRO A CA 1 ATOM 2770 C C . PRO A 1 359 ? 151.385 104.511 49.425 1.00 56.87 ? 359 PRO A C 1 ATOM 2771 O O . PRO A 1 359 ? 151.969 103.491 49.790 1.00 61.69 ? 359 PRO A O 1 ATOM 2772 C CB . PRO A 1 359 ? 149.277 104.174 48.097 1.00 57.67 ? 359 PRO A CB 1 ATOM 2773 C CG . PRO A 1 359 ? 148.948 105.475 47.458 1.00 49.31 ? 359 PRO A CG 1 ATOM 2774 C CD . PRO A 1 359 ? 148.547 106.382 48.566 1.00 46.23 ? 359 PRO A CD 1 ATOM 2775 N N . GLY A 1 360 ? 152.024 105.591 48.994 1.00 58.32 ? 360 GLY A N 1 ATOM 2776 C CA . GLY A 1 360 ? 153.478 105.602 48.925 1.00 63.70 ? 360 GLY A CA 1 ATOM 2777 C C . GLY A 1 360 ? 154.167 106.205 50.142 1.00 62.88 ? 360 GLY A C 1 ATOM 2778 O O . GLY A 1 360 ? 155.385 106.378 50.150 1.00 63.30 ? 360 GLY A O 1 ATOM 2779 N N . VAL A 1 361 ? 153.386 106.521 51.172 1.00 56.31 ? 361 VAL A N 1 ATOM 2780 C CA . VAL A 1 361 ? 153.895 107.194 52.364 1.00 48.17 ? 361 VAL A CA 1 ATOM 2781 C C . VAL A 1 361 ? 154.380 106.183 53.406 1.00 47.45 ? 361 VAL A C 1 ATOM 2782 O O . VAL A 1 361 ? 153.770 105.121 53.580 1.00 43.87 ? 361 VAL A O 1 ATOM 2783 C CB . VAL A 1 361 ? 152.804 108.121 52.981 1.00 41.10 ? 361 VAL A CB 1 ATOM 2784 C CG1 . VAL A 1 361 ? 153.198 108.592 54.375 1.00 39.41 ? 361 VAL A CG1 1 ATOM 2785 C CG2 . VAL A 1 361 ? 152.529 109.314 52.069 1.00 32.98 ? 361 VAL A CG2 1 ATOM 2786 N N . SER A 1 362 ? 155.479 106.505 54.090 1.00 40.82 ? 362 SER A N 1 ATOM 2787 C CA . SER A 1 362 ? 156.013 105.633 55.140 1.00 44.13 ? 362 SER A CA 1 ATOM 2788 C C . SER A 1 362 ? 155.000 105.392 56.262 1.00 43.20 ? 362 SER A C 1 ATOM 2789 O O . SER A 1 362 ? 154.047 106.175 56.454 1.00 41.36 ? 362 SER A O 1 ATOM 2790 C CB . SER A 1 362 ? 157.278 106.246 55.743 1.00 44.33 ? 362 SER A CB 1 ATOM 2791 O OG . SER A 1 362 ? 156.941 107.364 56.548 1.00 45.33 ? 362 SER A OG 1 ATOM 2792 N N . GLU A 1 363 ? 155.224 104.318 57.011 1.00 44.45 ? 363 GLU A N 1 ATOM 2793 C CA . GLU A 1 363 ? 154.413 104.001 58.180 1.00 52.71 ? 363 GLU A CA 1 ATOM 2794 C C . GLU A 1 363 ? 154.444 105.127 59.213 1.00 42.91 ? 363 GLU A C 1 ATOM 2795 O O . GLU A 1 363 ? 153.423 105.431 59.836 1.00 46.10 ? 363 GLU A O 1 ATOM 2796 C CB . GLU A 1 363 ? 154.878 102.682 58.819 1.00 54.92 ? 363 GLU A CB 1 ATOM 2797 C CG . GLU A 1 363 ? 153.751 101.682 59.038 1.00 69.02 ? 363 GLU A CG 1 ATOM 2798 C CD . GLU A 1 363 ? 153.015 101.319 57.748 1.00 78.16 ? 363 GLU A CD 1 ATOM 2799 O OE1 . GLU A 1 363 ? 153.614 101.427 56.655 1.00 81.58 ? 363 GLU A OE1 1 ATOM 2800 O OE2 . GLU A 1 363 ? 151.835 100.915 57.826 1.00 79.51 ? 363 GLU A OE2 1 ATOM 2801 N N . PHE A 1 364 ? 155.606 105.748 59.386 1.00 43.71 ? 364 PHE A N 1 ATOM 2802 C CA . PHE A 1 364 ? 155.722 106.885 60.296 1.00 42.80 ? 364 PHE A CA 1 ATOM 2803 C C . PHE A 1 364 ? 154.843 108.044 59.828 1.00 39.56 ? 364 PHE A C 1 ATOM 2804 O O . PHE A 1 364 ? 154.193 108.708 60.636 1.00 38.51 ? 364 PHE A O 1 ATOM 2805 C CB . PHE A 1 364 ? 157.178 107.344 60.432 1.00 44.57 ? 364 PHE A CB 1 ATOM 2806 C CG . PHE A 1 364 ? 157.338 108.623 61.209 1.00 52.81 ? 364 PHE A CG 1 ATOM 2807 C CD1 . PHE A 1 364 ? 157.147 108.643 62.583 1.00 44.84 ? 364 PHE A CD1 1 ATOM 2808 C CD2 . PHE A 1 364 ? 157.682 109.804 60.565 1.00 42.49 ? 364 PHE A CD2 1 ATOM 2809 C CE1 . PHE A 1 364 ? 157.292 109.821 63.302 1.00 54.39 ? 364 PHE A CE1 1 ATOM 2810 C CE2 . PHE A 1 364 ? 157.829 110.995 61.278 1.00 42.19 ? 364 PHE A CE2 1 ATOM 2811 C CZ . PHE A 1 364 ? 157.630 111.002 62.644 1.00 43.24 ? 364 PHE A CZ 1 ATOM 2812 N N . GLY A 1 365 ? 154.821 108.274 58.519 1.00 39.06 ? 365 GLY A N 1 ATOM 2813 C CA . GLY A 1 365 ? 154.003 109.324 57.935 1.00 35.65 ? 365 GLY A CA 1 ATOM 2814 C C . GLY A 1 365 ? 152.522 109.123 58.199 1.00 35.85 ? 365 GLY A C 1 ATOM 2815 O O . GLY A 1 365 ? 151.813 110.080 58.536 1.00 32.52 ? 365 GLY A O 1 ATOM 2816 N N . LYS A 1 366 ? 152.051 107.883 58.071 1.00 35.02 ? 366 LYS A N 1 ATOM 2817 C CA . LYS A 1 366 ? 150.632 107.609 58.274 1.00 35.87 ? 366 LYS A CA 1 ATOM 2818 C C . LYS A 1 366 ? 150.246 107.754 59.745 1.00 36.49 ? 366 LYS A C 1 ATOM 2819 O O . LYS A 1 366 ? 149.168 108.299 60.054 1.00 33.41 ? 366 LYS A O 1 ATOM 2820 C CB . LYS A 1 366 ? 150.227 106.224 57.728 1.00 35.22 ? 366 LYS A CB 1 ATOM 2821 C CG . LYS A 1 366 ? 150.290 106.115 56.207 1.00 47.36 ? 366 LYS A CG 1 ATOM 2822 C CD . LYS A 1 366 ? 149.708 104.799 55.690 1.00 51.84 ? 366 LYS A CD 1 ATOM 2823 C CE . LYS A 1 366 ? 150.767 103.696 55.630 1.00 60.58 ? 366 LYS A CE 1 ATOM 2824 N NZ . LYS A 1 366 ? 151.945 104.125 54.823 1.00 60.01 ? 366 LYS A NZ 1 ATOM 2825 N N . GLU A 1 367 ? 151.120 107.266 60.632 1.00 36.76 ? 367 GLU A N 1 ATOM 2826 C CA . GLU A 1 367 ? 150.928 107.399 62.077 1.00 44.68 ? 367 GLU A CA 1 ATOM 2827 C C . GLU A 1 367 ? 150.830 108.868 62.489 1.00 36.53 ? 367 GLU A C 1 ATOM 2828 O O . GLU A 1 367 ? 149.984 109.235 63.301 1.00 43.43 ? 367 GLU A O 1 ATOM 2829 C CB . GLU A 1 367 ? 152.075 106.738 62.867 1.00 40.90 ? 367 GLU A CB 1 ATOM 2830 C CG . GLU A 1 367 ? 152.061 105.214 62.899 1.00 75.54 ? 367 GLU A CG 1 ATOM 2831 C CD . GLU A 1 367 ? 153.046 104.632 63.916 1.00 83.66 ? 367 GLU A CD 1 ATOM 2832 O OE1 . GLU A 1 367 ? 154.277 104.744 63.710 1.00 83.27 ? 367 GLU A OE1 1 ATOM 2833 O OE2 . GLU A 1 367 ? 152.587 104.057 64.926 1.00 89.32 ? 367 GLU A OE2 1 ATOM 2834 N N . SER A 1 368 ? 151.700 109.704 61.934 1.00 35.83 ? 368 SER A N 1 ATOM 2835 C CA . SER A 1 368 ? 151.689 111.125 62.280 1.00 34.93 ? 368 SER A CA 1 ATOM 2836 C C . SER A 1 368 ? 150.370 111.809 61.854 1.00 32.70 ? 368 SER A C 1 ATOM 2837 O O . SER A 1 368 ? 149.884 112.715 62.536 1.00 32.57 ? 368 SER A O 1 ATOM 2838 C CB . SER A 1 368 ? 152.918 111.845 61.703 1.00 36.30 ? 368 SER A CB 1 ATOM 2839 O OG . SER A 1 368 ? 152.674 112.270 60.369 1.00 34.12 ? 368 SER A OG 1 ATOM 2840 N N . ILE A 1 369 ? 149.774 111.352 60.753 1.00 31.33 ? 369 ILE A N 1 ATOM 2841 C CA . ILE A 1 369 ? 148.447 111.843 60.364 1.00 42.18 ? 369 ILE A CA 1 ATOM 2842 C C . ILE A 1 369 ? 147.420 111.450 61.434 1.00 30.42 ? 369 ILE A C 1 ATOM 2843 O O . ILE A 1 369 ? 146.609 112.268 61.878 1.00 30.03 ? 369 ILE A O 1 ATOM 2844 C CB . ILE A 1 369 ? 147.999 111.300 58.977 1.00 28.42 ? 369 ILE A CB 1 ATOM 2845 C CG1 . ILE A 1 369 ? 148.962 111.764 57.876 1.00 32.47 ? 369 ILE A CG1 1 ATOM 2846 C CG2 . ILE A 1 369 ? 146.571 111.762 58.642 1.00 26.98 ? 369 ILE A CG2 1 ATOM 2847 C CD1 . ILE A 1 369 ? 148.663 111.182 56.504 1.00 32.21 ? 369 ILE A CD1 1 ATOM 2848 N N . LEU A 1 370 ? 147.486 110.198 61.871 1.00 32.00 ? 370 LEU A N 1 ATOM 2849 C CA . LEU A 1 370 ? 146.552 109.700 62.858 1.00 38.83 ? 370 LEU A CA 1 ATOM 2850 C C . LEU A 1 370 ? 146.710 110.432 64.184 1.00 34.67 ? 370 LEU A C 1 ATOM 2851 O O . LEU A 1 370 ? 145.716 110.777 64.821 1.00 38.06 ? 370 LEU A O 1 ATOM 2852 C CB . LEU A 1 370 ? 146.728 108.192 63.054 1.00 40.80 ? 370 LEU A CB 1 ATOM 2853 C CG . LEU A 1 370 ? 145.810 107.568 64.106 1.00 42.46 ? 370 LEU A CG 1 ATOM 2854 C CD1 . LEU A 1 370 ? 145.295 106.225 63.628 1.00 48.46 ? 370 LEU A CD1 1 ATOM 2855 C CD2 . LEU A 1 370 ? 146.549 107.405 65.421 1.00 44.11 ? 370 LEU A CD2 1 ATOM 2856 N N . PHE A 1 371 ? 147.953 110.654 64.602 1.00 35.73 ? 371 PHE A N 1 ATOM 2857 C CA . PHE A 1 371 ? 148.216 111.385 65.838 1.00 37.41 ? 371 PHE A CA 1 ATOM 2858 C C . PHE A 1 371 ? 147.576 112.769 65.810 1.00 36.22 ? 371 PHE A C 1 ATOM 2859 O O . PHE A 1 371 ? 147.004 113.216 66.801 1.00 37.65 ? 371 PHE A O 1 ATOM 2860 C CB . PHE A 1 371 ? 149.716 111.549 66.067 1.00 38.61 ? 371 PHE A CB 1 ATOM 2861 C CG . PHE A 1 371 ? 150.059 112.212 67.370 1.00 48.85 ? 371 PHE A CG 1 ATOM 2862 C CD1 . PHE A 1 371 ? 150.062 111.480 68.555 1.00 51.95 ? 371 PHE A CD1 1 ATOM 2863 C CD2 . PHE A 1 371 ? 150.398 113.563 67.414 1.00 45.20 ? 371 PHE A CD2 1 ATOM 2864 C CE1 . PHE A 1 371 ? 150.385 112.085 69.767 1.00 57.81 ? 371 PHE A CE1 1 ATOM 2865 C CE2 . PHE A 1 371 ? 150.724 114.176 68.623 1.00 47.20 ? 371 PHE A CE2 1 ATOM 2866 C CZ . PHE A 1 371 ? 150.718 113.435 69.803 1.00 50.80 ? 371 PHE A CZ 1 ATOM 2867 N N . HIS A 1 372 ? 147.682 113.447 64.674 1.00 33.99 ? 372 HIS A N 1 ATOM 2868 C CA . HIS A 1 372 ? 147.232 114.836 64.600 1.00 37.83 ? 372 HIS A CA 1 ATOM 2869 C C . HIS A 1 372 ? 145.707 114.955 64.523 1.00 37.15 ? 372 HIS A C 1 ATOM 2870 O O . HIS A 1 372 ? 145.130 115.909 65.048 1.00 36.32 ? 372 HIS A O 1 ATOM 2871 C CB . HIS A 1 372 ? 147.887 115.561 63.422 1.00 38.21 ? 372 HIS A CB 1 ATOM 2872 C CG . HIS A 1 372 ? 147.713 117.050 63.458 1.00 56.34 ? 372 HIS A CG 1 ATOM 2873 N ND1 . HIS A 1 372 ? 148.581 117.885 64.132 1.00 62.57 ? 372 HIS A ND1 1 ATOM 2874 C CD2 . HIS A 1 372 ? 146.766 117.851 62.913 1.00 57.99 ? 372 HIS A CD2 1 ATOM 2875 C CE1 . HIS A 1 372 ? 148.177 119.137 63.996 1.00 58.82 ? 372 HIS A CE1 1 ATOM 2876 N NE2 . HIS A 1 372 ? 147.077 119.143 63.265 1.00 57.97 ? 372 HIS A NE2 1 ATOM 2877 N N . TYR A 1 373 ? 145.054 113.987 63.886 1.00 31.62 ? 373 TYR A N 1 ATOM 2878 C CA . TYR A 1 373 ? 143.611 114.080 63.657 1.00 36.32 ? 373 TYR A CA 1 ATOM 2879 C C . TYR A 1 373 ? 142.746 113.250 64.606 1.00 39.52 ? 373 TYR A C 1 ATOM 2880 O O . TYR A 1 373 ? 141.518 113.276 64.498 1.00 41.55 ? 373 TYR A O 1 ATOM 2881 C CB . TYR A 1 373 ? 143.274 113.712 62.204 1.00 28.97 ? 373 TYR A CB 1 ATOM 2882 C CG . TYR A 1 373 ? 143.463 114.866 61.244 1.00 31.45 ? 373 TYR A CG 1 ATOM 2883 C CD1 . TYR A 1 373 ? 144.721 115.162 60.724 1.00 27.44 ? 373 TYR A CD1 1 ATOM 2884 C CD2 . TYR A 1 373 ? 142.384 115.672 60.868 1.00 28.64 ? 373 TYR A CD2 1 ATOM 2885 C CE1 . TYR A 1 373 ? 144.902 116.222 59.850 1.00 30.05 ? 373 TYR A CE1 1 ATOM 2886 C CE2 . TYR A 1 373 ? 142.554 116.739 59.991 1.00 25.62 ? 373 TYR A CE2 1 ATOM 2887 C CZ . TYR A 1 373 ? 143.818 117.008 59.487 1.00 29.45 ? 373 TYR A CZ 1 ATOM 2888 O OH . TYR A 1 373 ? 144.017 118.067 58.624 1.00 24.91 ? 373 TYR A OH 1 ATOM 2889 N N . THR A 1 374 ? 143.365 112.513 65.528 1.00 36.81 ? 374 THR A N 1 ATOM 2890 C CA . THR A 1 374 ? 142.585 111.604 66.376 1.00 48.03 ? 374 THR A CA 1 ATOM 2891 C C . THR A 1 374 ? 142.744 111.812 67.874 1.00 55.09 ? 374 THR A C 1 ATOM 2892 O O . THR A 1 374 ? 142.406 110.928 68.656 1.00 54.81 ? 374 THR A O 1 ATOM 2893 C CB . THR A 1 374 ? 142.847 110.100 66.065 1.00 54.31 ? 374 THR A CB 1 ATOM 2894 O OG1 . THR A 1 374 ? 144.233 109.796 66.269 1.00 57.43 ? 374 THR A OG1 1 ATOM 2895 C CG2 . THR A 1 374 ? 142.458 109.772 64.636 1.00 55.12 ? 374 THR A CG2 1 ATOM 2896 N N . ASP A 1 375 ? 143.253 112.962 68.293 1.00 61.71 ? 375 ASP A N 1 ATOM 2897 C CA . ASP A 1 375 ? 143.116 113.286 69.702 1.00 69.06 ? 375 ASP A CA 1 ATOM 2898 C C . ASP A 1 375 ? 141.733 113.877 69.933 1.00 75.31 ? 375 ASP A C 1 ATOM 2899 O O . ASP A 1 375 ? 141.535 115.088 69.792 1.00 73.64 ? 375 ASP A O 1 ATOM 2900 C CB . ASP A 1 375 ? 144.178 114.257 70.190 1.00 69.90 ? 375 ASP A CB 1 ATOM 2901 C CG . ASP A 1 375 ? 144.045 114.543 71.669 1.00 80.95 ? 375 ASP A CG 1 ATOM 2902 O OD1 . ASP A 1 375 ? 143.306 115.486 72.025 1.00 84.51 ? 375 ASP A OD1 1 ATOM 2903 O OD2 . ASP A 1 375 ? 144.655 113.807 72.476 1.00 84.69 ? 375 ASP A OD2 1 ATOM 2904 N N . TRP A 1 376 ? 140.775 113.017 70.268 1.00 78.76 ? 376 TRP A N 1 ATOM 2905 C CA . TRP A 1 376 ? 139.432 113.480 70.578 1.00 80.90 ? 376 TRP A CA 1 ATOM 2906 C C . TRP A 1 376 ? 139.401 114.086 71.969 1.00 91.83 ? 376 TRP A C 1 ATOM 2907 O O . TRP A 1 376 ? 140.283 113.838 72.800 1.00 91.06 ? 376 TRP A O 1 ATOM 2908 C CB . TRP A 1 376 ? 138.412 112.343 70.526 1.00 76.82 ? 376 TRP A CB 1 ATOM 2909 C CG . TRP A 1 376 ? 138.763 111.229 69.614 1.00 71.23 ? 376 TRP A CG 1 ATOM 2910 C CD1 . TRP A 1 376 ? 139.117 109.958 69.970 1.00 72.52 ? 376 TRP A CD1 1 ATOM 2911 C CD2 . TRP A 1 376 ? 138.786 111.270 68.185 1.00 64.67 ? 376 TRP A CD2 1 ATOM 2912 N NE1 . TRP A 1 376 ? 139.362 109.206 68.846 1.00 69.98 ? 376 TRP A NE1 1 ATOM 2913 C CE2 . TRP A 1 376 ? 139.165 109.989 67.738 1.00 63.76 ? 376 TRP A CE2 1 ATOM 2914 C CE3 . TRP A 1 376 ? 138.526 112.266 67.240 1.00 62.75 ? 376 TRP A CE3 1 ATOM 2915 C CZ2 . TRP A 1 376 ? 139.289 109.680 66.385 1.00 60.87 ? 376 TRP A CZ2 1 ATOM 2916 C CZ3 . TRP A 1 376 ? 138.653 111.958 65.898 1.00 58.84 ? 376 TRP A CZ3 1 ATOM 2917 C CH2 . TRP A 1 376 ? 139.030 110.677 65.483 1.00 58.83 ? 376 TRP A CH2 1 ATOM 2918 N N . VAL A 1 377 ? 138.364 114.878 72.210 1.00 96.87 ? 377 VAL A N 1 ATOM 2919 C CA . VAL A 1 377 ? 138.111 115.461 73.515 1.00 100.44 ? 377 VAL A CA 1 ATOM 2920 C C . VAL A 1 377 ? 137.633 114.388 74.490 1.00 101.63 ? 377 VAL A C 1 ATOM 2921 O O . VAL A 1 377 ? 138.420 113.562 74.956 1.00 100.10 ? 377 VAL A O 1 ATOM 2922 C CB . VAL A 1 377 ? 137.052 116.568 73.406 1.00 101.47 ? 377 VAL A CB 1 ATOM 2923 C CG1 . VAL A 1 377 ? 137.654 117.811 72.775 1.00 98.64 ? 377 VAL A CG1 1 ATOM 2924 C CG2 . VAL A 1 377 ? 135.867 116.077 72.587 1.00 100.01 ? 377 VAL A CG2 1 ATOM 2925 N N . GLN A 1 380 ? 134.784 108.285 72.230 1.00 88.82 ? 380 GLN A N 1 ATOM 2926 C CA . GLN A 1 380 ? 133.619 109.099 72.567 1.00 94.02 ? 380 GLN A CA 1 ATOM 2927 C C . GLN A 1 380 ? 132.546 109.018 71.476 1.00 87.85 ? 380 GLN A C 1 ATOM 2928 O O . GLN A 1 380 ? 131.785 108.050 71.412 1.00 83.37 ? 380 GLN A O 1 ATOM 2929 C CB . GLN A 1 380 ? 134.038 110.555 72.786 1.00 97.35 ? 380 GLN A CB 1 ATOM 2930 C CG . GLN A 1 380 ? 133.009 111.410 73.507 1.00 100.03 ? 380 GLN A CG 1 ATOM 2931 C CD . GLN A 1 380 ? 133.331 112.886 73.413 1.00 98.00 ? 380 GLN A CD 1 ATOM 2932 O OE1 . GLN A 1 380 ? 134.495 113.284 73.478 1.00 99.28 ? 380 GLN A OE1 1 ATOM 2933 N NE2 . GLN A 1 380 ? 132.303 113.705 73.242 1.00 96.37 ? 380 GLN A NE2 1 ATOM 2934 N N . ARG A 1 381 ? 132.500 110.039 70.622 1.00 85.02 ? 381 ARG A N 1 ATOM 2935 C CA . ARG A 1 381 ? 131.516 110.127 69.540 1.00 78.76 ? 381 ARG A CA 1 ATOM 2936 C C . ARG A 1 381 ? 131.790 109.116 68.422 1.00 68.24 ? 381 ARG A C 1 ATOM 2937 O O . ARG A 1 381 ? 132.930 108.969 67.979 1.00 66.12 ? 381 ARG A O 1 ATOM 2938 C CB . ARG A 1 381 ? 131.500 111.545 68.964 1.00 80.90 ? 381 ARG A CB 1 ATOM 2939 C CG . ARG A 1 381 ? 131.120 112.624 69.967 1.00 88.71 ? 381 ARG A CG 1 ATOM 2940 C CD . ARG A 1 381 ? 131.426 114.026 69.436 1.00 93.45 ? 381 ARG A CD 1 ATOM 2941 N NE . ARG A 1 381 ? 130.675 114.368 68.225 1.00 95.74 ? 381 ARG A NE 1 ATOM 2942 C CZ . ARG A 1 381 ? 131.220 114.534 67.021 1.00 92.62 ? 381 ARG A CZ 1 ATOM 2943 N NH1 . ARG A 1 381 ? 132.529 114.389 66.850 1.00 90.44 ? 381 ARG A NH1 1 ATOM 2944 N NH2 . ARG A 1 381 ? 130.456 114.848 65.982 1.00 89.41 ? 381 ARG A NH2 1 ATOM 2945 N N . PRO A 1 382 ? 130.735 108.427 67.954 1.00 65.66 ? 382 PRO A N 1 ATOM 2946 C CA . PRO A 1 382 ? 130.837 107.342 66.966 1.00 60.53 ? 382 PRO A CA 1 ATOM 2947 C C . PRO A 1 382 ? 131.292 107.815 65.585 1.00 53.81 ? 382 PRO A C 1 ATOM 2948 O O . PRO A 1 382 ? 131.901 107.038 64.853 1.00 54.09 ? 382 PRO A O 1 ATOM 2949 C CB . PRO A 1 382 ? 129.400 106.806 66.880 1.00 62.46 ? 382 PRO A CB 1 ATOM 2950 C CG . PRO A 1 382 ? 128.689 107.357 68.080 1.00 65.87 ? 382 PRO A CG 1 ATOM 2951 C CD . PRO A 1 382 ? 129.340 108.670 68.354 1.00 67.91 ? 382 PRO A CD 1 ATOM 2952 N N . GLU A 1 383 ? 130.995 109.061 65.230 1.00 44.96 ? 383 GLU A N 1 ATOM 2953 C CA . GLU A 1 383 ? 131.385 109.582 63.921 1.00 45.65 ? 383 GLU A CA 1 ATOM 2954 C C . GLU A 1 383 ? 132.752 110.276 63.935 1.00 44.99 ? 383 GLU A C 1 ATOM 2955 O O . GLU A 1 383 ? 133.134 110.938 62.957 1.00 39.94 ? 383 GLU A O 1 ATOM 2956 C CB . GLU A 1 383 ? 130.308 110.515 63.354 1.00 48.88 ? 383 GLU A CB 1 ATOM 2957 C CG . GLU A 1 383 ? 130.085 111.787 64.150 1.00 59.52 ? 383 GLU A CG 1 ATOM 2958 C CD . GLU A 1 383 ? 129.077 111.612 65.270 1.00 72.23 ? 383 GLU A CD 1 ATOM 2959 O OE1 . GLU A 1 383 ? 128.203 110.725 65.161 1.00 79.89 ? 383 GLU A OE1 1 ATOM 2960 O OE2 . GLU A 1 383 ? 129.150 112.375 66.255 1.00 76.33 ? 383 GLU A OE2 1 ATOM 2961 N N . ASN A 1 384 ? 133.482 110.118 65.040 1.00 47.98 ? 384 ASN A N 1 ATOM 2962 C CA . ASN A 1 384 ? 134.820 110.699 65.175 1.00 45.70 ? 384 ASN A CA 1 ATOM 2963 C C . ASN A 1 384 ? 135.734 110.336 64.011 1.00 36.57 ? 384 ASN A C 1 ATOM 2964 O O . ASN A 1 384 ? 136.285 111.221 63.354 1.00 34.39 ? 384 ASN A O 1 ATOM 2965 C CB . ASN A 1 384 ? 135.483 110.262 66.488 1.00 49.20 ? 384 ASN A CB 1 ATOM 2966 C CG . ASN A 1 384 ? 135.052 111.103 67.678 1.00 57.75 ? 384 ASN A CG 1 ATOM 2967 O OD1 . ASN A 1 384 ? 134.662 112.266 67.532 1.00 56.35 ? 384 ASN A OD1 1 ATOM 2968 N ND2 . ASN A 1 384 ? 135.132 110.515 68.873 1.00 62.01 ? 384 ASN A ND2 1 ATOM 2969 N N . TYR A 1 385 ? 135.886 109.039 63.752 1.00 37.07 ? 385 TYR A N 1 ATOM 2970 C CA . TYR A 1 385 ? 136.797 108.581 62.703 1.00 39.68 ? 385 TYR A CA 1 ATOM 2971 C C . TYR A 1 385 ? 136.302 108.913 61.291 1.00 35.51 ? 385 TYR A C 1 ATOM 2972 O O . TYR A 1 385 ? 137.095 109.329 60.432 1.00 31.04 ? 385 TYR A O 1 ATOM 2973 C CB . TYR A 1 385 ? 137.114 107.087 62.852 1.00 40.39 ? 385 TYR A CB 1 ATOM 2974 C CG . TYR A 1 385 ? 138.008 106.777 64.037 1.00 45.57 ? 385 TYR A CG 1 ATOM 2975 C CD1 . TYR A 1 385 ? 139.377 107.039 63.989 1.00 42.30 ? 385 TYR A CD1 1 ATOM 2976 C CD2 . TYR A 1 385 ? 137.488 106.220 65.201 1.00 41.77 ? 385 TYR A CD2 1 ATOM 2977 C CE1 . TYR A 1 385 ? 140.196 106.761 65.066 1.00 42.91 ? 385 TYR A CE1 1 ATOM 2978 C CE2 . TYR A 1 385 ? 138.301 105.936 66.282 1.00 43.81 ? 385 TYR A CE2 1 ATOM 2979 C CZ . TYR A 1 385 ? 139.652 106.209 66.206 1.00 42.69 ? 385 TYR A CZ 1 ATOM 2980 O OH . TYR A 1 385 ? 140.463 105.932 67.273 1.00 45.21 ? 385 TYR A OH 1 ATOM 2981 N N . ARG A 1 386 ? 135.000 108.753 61.061 1.00 36.62 ? 386 ARG A N 1 ATOM 2982 C CA . ARG A 1 386 ? 134.387 109.148 59.788 1.00 33.31 ? 386 ARG A CA 1 ATOM 2983 C C . ARG A 1 386 ? 134.715 110.612 59.431 1.00 30.36 ? 386 ARG A C 1 ATOM 2984 O O . ARG A 1 386 ? 135.140 110.910 58.315 1.00 28.60 ? 386 ARG A O 1 ATOM 2985 C CB . ARG A 1 386 ? 132.865 108.948 59.847 1.00 33.94 ? 386 ARG A CB 1 ATOM 2986 C CG . ARG A 1 386 ? 132.125 109.392 58.590 1.00 33.41 ? 386 ARG A CG 1 ATOM 2987 C CD . ARG A 1 386 ? 130.610 109.426 58.803 1.00 36.04 ? 386 ARG A CD 1 ATOM 2988 N NE . ARG A 1 386 ? 130.175 110.681 59.418 1.00 36.71 ? 386 ARG A NE 1 ATOM 2989 C CZ . ARG A 1 386 ? 128.993 110.853 60.007 1.00 41.54 ? 386 ARG A CZ 1 ATOM 2990 N NH1 . ARG A 1 386 ? 128.124 109.855 60.066 1.00 45.35 ? 386 ARG A NH1 1 ATOM 2991 N NH2 . ARG A 1 386 ? 128.674 112.022 60.542 1.00 37.95 ? 386 ARG A NH2 1 ATOM 2992 N N . GLU A 1 387 ? 134.535 111.515 60.391 1.00 31.11 ? 387 GLU A N 1 ATOM 2993 C CA . GLU A 1 387 ? 134.763 112.943 60.144 1.00 34.12 ? 387 GLU A CA 1 ATOM 2994 C C . GLU A 1 387 ? 136.234 113.287 60.020 1.00 34.73 ? 387 GLU A C 1 ATOM 2995 O O . GLU A 1 387 ? 136.613 114.181 59.243 1.00 26.98 ? 387 GLU A O 1 ATOM 2996 C CB . GLU A 1 387 ? 134.126 113.791 61.247 1.00 34.85 ? 387 GLU A CB 1 ATOM 2997 C CG . GLU A 1 387 ? 132.642 113.535 61.382 1.00 49.72 ? 387 GLU A CG 1 ATOM 2998 C CD . GLU A 1 387 ? 131.887 114.709 61.952 1.00 63.89 ? 387 GLU A CD 1 ATOM 2999 O OE1 . GLU A 1 387 ? 132.436 115.406 62.832 1.00 69.34 ? 387 GLU A OE1 1 ATOM 3000 O OE2 . GLU A 1 387 ? 130.734 114.923 61.522 1.00 70.41 ? 387 GLU A OE2 1 ATOM 3001 N N . ALA A 1 388 ? 137.060 112.587 60.797 1.00 30.38 ? 388 ALA A N 1 ATOM 3002 C CA . ALA A 1 388 ? 138.505 112.803 60.752 1.00 28.33 ? 388 ALA A CA 1 ATOM 3003 C C . ALA A 1 388 ? 139.056 112.499 59.361 1.00 26.60 ? 388 ALA A C 1 ATOM 3004 O O . ALA A 1 388 ? 139.866 113.263 58.829 1.00 25.44 ? 388 ALA A O 1 ATOM 3005 C CB . ALA A 1 388 ? 139.218 111.953 61.809 1.00 29.92 ? 388 ALA A CB 1 ATOM 3006 N N . LEU A 1 389 ? 138.618 111.392 58.764 1.00 26.80 ? 389 LEU A N 1 ATOM 3007 C CA . LEU A 1 389 ? 139.134 111.015 57.448 1.00 26.73 ? 389 LEU A CA 1 ATOM 3008 C C . LEU A 1 389 ? 138.753 112.023 56.358 1.00 27.57 ? 389 LEU A C 1 ATOM 3009 O O . LEU A 1 389 ? 139.596 112.394 55.531 1.00 29.64 ? 389 LEU A O 1 ATOM 3010 C CB . LEU A 1 389 ? 138.711 109.590 57.062 1.00 26.75 ? 389 LEU A CB 1 ATOM 3011 C CG . LEU A 1 389 ? 139.482 108.959 55.901 1.00 26.44 ? 389 LEU A CG 1 ATOM 3012 C CD1 . LEU A 1 389 ? 140.965 108.896 56.221 1.00 29.53 ? 389 LEU A CD1 1 ATOM 3013 C CD2 . LEU A 1 389 ? 138.945 107.552 55.568 1.00 34.46 ? 389 LEU A CD2 1 ATOM 3014 N N . GLY A 1 390 ? 137.498 112.472 56.355 1.00 30.29 ? 390 GLY A N 1 ATOM 3015 C CA . GLY A 1 390 ? 137.089 113.526 55.438 1.00 28.21 ? 390 GLY A CA 1 ATOM 3016 C C . GLY A 1 390 ? 137.958 114.770 55.594 1.00 26.51 ? 390 GLY A C 1 ATOM 3017 O O . GLY A 1 390 ? 138.414 115.353 54.604 1.00 22.13 ? 390 GLY A O 1 ATOM 3018 N N . ASP A 1 391 ? 138.199 115.178 56.836 1.00 24.32 ? 391 ASP A N 1 ATOM 3019 C CA . ASP A 1 391 ? 138.992 116.384 57.081 1.00 23.41 ? 391 ASP A CA 1 ATOM 3020 C C . ASP A 1 391 ? 140.450 116.209 56.661 1.00 29.80 ? 391 ASP A C 1 ATOM 3021 O O . ASP A 1 391 ? 141.050 117.124 56.073 1.00 22.25 ? 391 ASP A O 1 ATOM 3022 C CB . ASP A 1 391 ? 138.896 116.804 58.546 1.00 24.79 ? 391 ASP A CB 1 ATOM 3023 C CG . ASP A 1 391 ? 137.572 117.463 58.861 1.00 33.75 ? 391 ASP A CG 1 ATOM 3024 O OD1 . ASP A 1 391 ? 137.052 118.185 57.977 1.00 34.41 ? 391 ASP A OD1 1 ATOM 3025 O OD2 . ASP A 1 391 ? 137.053 117.268 59.980 1.00 36.91 ? 391 ASP A OD2 1 ATOM 3026 N N . VAL A 1 392 ? 141.015 115.040 56.958 1.00 29.42 ? 392 VAL A N 1 ATOM 3027 C CA . VAL A 1 392 ? 142.338 114.689 56.451 1.00 30.85 ? 392 VAL A CA 1 ATOM 3028 C C . VAL A 1 392 ? 142.425 114.901 54.930 1.00 30.95 ? 392 VAL A C 1 ATOM 3029 O O . VAL A 1 392 ? 143.311 115.608 54.442 1.00 21.70 ? 392 VAL A O 1 ATOM 3030 C CB . VAL A 1 392 ? 142.707 113.224 56.795 1.00 28.01 ? 392 VAL A CB 1 ATOM 3031 C CG1 . VAL A 1 392 ? 143.812 112.719 55.873 1.00 23.51 ? 392 VAL A CG1 1 ATOM 3032 C CG2 . VAL A 1 392 ? 143.143 113.117 58.254 1.00 24.77 ? 392 VAL A CG2 1 ATOM 3033 N N . VAL A 1 393 ? 141.492 114.314 54.186 1.00 21.76 ? 393 VAL A N 1 ATOM 3034 C CA . VAL A 1 393 ? 141.544 114.387 52.724 1.00 21.95 ? 393 VAL A CA 1 ATOM 3035 C C . VAL A 1 393 ? 141.334 115.824 52.206 1.00 21.89 ? 393 VAL A C 1 ATOM 3036 O O . VAL A 1 393 ? 142.008 116.263 51.263 1.00 24.42 ? 393 VAL A O 1 ATOM 3037 C CB . VAL A 1 393 ? 140.534 113.398 52.083 1.00 21.77 ? 393 VAL A CB 1 ATOM 3038 C CG1 . VAL A 1 393 ? 140.386 113.644 50.594 1.00 22.70 ? 393 VAL A CG1 1 ATOM 3039 C CG2 . VAL A 1 393 ? 140.981 111.945 52.344 1.00 22.64 ? 393 VAL A CG2 1 ATOM 3040 N N . GLY A 1 394 ? 140.413 116.557 52.834 1.00 21.23 ? 394 GLY A N 1 ATOM 3041 C CA . GLY A 1 394 ? 140.074 117.895 52.383 1.00 23.31 ? 394 GLY A CA 1 ATOM 3042 C C . GLY A 1 394 ? 141.168 118.903 52.737 1.00 27.70 ? 394 GLY A C 1 ATOM 3043 O O . GLY A 1 394 ? 141.455 119.826 51.960 1.00 21.39 ? 394 GLY A O 1 ATOM 3044 N N . ASP A 1 395 ? 141.779 118.739 53.908 1.00 21.44 ? 395 ASP A N 1 ATOM 3045 C CA . ASP A 1 395 ? 142.799 119.696 54.359 1.00 23.16 ? 395 ASP A CA 1 ATOM 3046 C C . ASP A 1 395 ? 144.092 119.541 53.554 1.00 21.90 ? 395 ASP A C 1 ATOM 3047 O O . ASP A 1 395 ? 144.692 120.530 53.146 1.00 22.39 ? 395 ASP A O 1 ATOM 3048 C CB . ASP A 1 395 ? 143.120 119.532 55.852 1.00 22.64 ? 395 ASP A CB 1 ATOM 3049 C CG . ASP A 1 395 ? 141.950 119.908 56.762 1.00 29.82 ? 395 ASP A CG 1 ATOM 3050 O OD1 . ASP A 1 395 ? 141.029 120.634 56.313 1.00 24.03 ? 395 ASP A OD1 1 ATOM 3051 O OD2 . ASP A 1 395 ? 141.966 119.482 57.943 1.00 28.67 ? 395 ASP A OD2 1 ATOM 3052 N N . TYR A 1 396 ? 144.506 118.291 53.341 1.00 25.23 ? 396 TYR A N 1 ATOM 3053 C CA . TYR A 1 396 ? 145.739 117.985 52.606 1.00 24.85 ? 396 TYR A CA 1 ATOM 3054 C C . TYR A 1 396 ? 145.619 118.393 51.140 1.00 27.46 ? 396 TYR A C 1 ATOM 3055 O O . TYR A 1 396 ? 146.508 119.048 50.603 1.00 22.86 ? 396 TYR A O 1 ATOM 3056 C CB . TYR A 1 396 ? 146.069 116.485 52.716 1.00 23.52 ? 396 TYR A CB 1 ATOM 3057 C CG . TYR A 1 396 ? 147.226 116.003 51.859 1.00 23.09 ? 396 TYR A CG 1 ATOM 3058 C CD1 . TYR A 1 396 ? 148.491 116.590 51.951 1.00 29.17 ? 396 TYR A CD1 1 ATOM 3059 C CD2 . TYR A 1 396 ? 147.061 114.934 50.978 1.00 25.70 ? 396 TYR A CD2 1 ATOM 3060 C CE1 . TYR A 1 396 ? 149.564 116.128 51.168 1.00 25.11 ? 396 TYR A CE1 1 ATOM 3061 C CE2 . TYR A 1 396 ? 148.124 114.461 50.202 1.00 25.64 ? 396 TYR A CE2 1 ATOM 3062 C CZ . TYR A 1 396 ? 149.367 115.065 50.305 1.00 29.73 ? 396 TYR A CZ 1 ATOM 3063 O OH . TYR A 1 396 ? 150.408 114.604 49.532 1.00 28.87 ? 396 TYR A OH 1 ATOM 3064 N N . ASN A 1 397 ? 144.509 118.025 50.507 1.00 19.70 ? 397 ASN A N 1 ATOM 3065 C CA . ASN A 1 397 ? 144.352 118.211 49.062 1.00 22.80 ? 397 ASN A CA 1 ATOM 3066 C C . ASN A 1 397 ? 143.835 119.577 48.592 1.00 21.37 ? 397 ASN A C 1 ATOM 3067 O O . ASN A 1 397 ? 144.129 119.985 47.460 1.00 20.94 ? 397 ASN A O 1 ATOM 3068 C CB . ASN A 1 397 ? 143.472 117.097 48.471 1.00 21.85 ? 397 ASN A CB 1 ATOM 3069 C CG . ASN A 1 397 ? 144.180 115.750 48.450 1.00 30.38 ? 397 ASN A CG 1 ATOM 3070 O OD1 . ASN A 1 397 ? 145.095 115.532 47.642 1.00 23.15 ? 397 ASN A OD1 1 ATOM 3071 N ND2 . ASN A 1 397 ? 143.777 114.846 49.347 1.00 21.64 ? 397 ASN A ND2 1 ATOM 3072 N N . PHE A 1 398 ? 143.079 120.288 49.430 1.00 17.67 ? 398 PHE A N 1 ATOM 3073 C CA . PHE A 1 398 ? 142.443 121.529 48.965 1.00 17.95 ? 398 PHE A CA 1 ATOM 3074 C C . PHE A 1 398 ? 142.627 122.767 49.847 1.00 22.22 ? 398 PHE A C 1 ATOM 3075 O O . PHE A 1 398 ? 143.072 123.817 49.371 1.00 22.02 ? 398 PHE A O 1 ATOM 3076 C CB . PHE A 1 398 ? 140.950 121.284 48.700 1.00 16.79 ? 398 PHE A CB 1 ATOM 3077 C CG . PHE A 1 398 ? 140.700 120.171 47.712 1.00 20.00 ? 398 PHE A CG 1 ATOM 3078 C CD1 . PHE A 1 398 ? 140.804 120.403 46.351 1.00 17.42 ? 398 PHE A CD1 1 ATOM 3079 C CD2 . PHE A 1 398 ? 140.398 118.888 48.151 1.00 19.49 ? 398 PHE A CD2 1 ATOM 3080 C CE1 . PHE A 1 398 ? 140.584 119.369 45.431 1.00 21.09 ? 398 PHE A CE1 1 ATOM 3081 C CE2 . PHE A 1 398 ? 140.177 117.844 47.244 1.00 18.83 ? 398 PHE A CE2 1 ATOM 3082 C CZ . PHE A 1 398 ? 140.273 118.081 45.890 1.00 18.86 ? 398 PHE A CZ 1 ATOM 3083 N N . ILE A 1 399 ? 142.277 122.651 51.122 1.00 17.02 ? 399 ILE A N 1 ATOM 3084 C CA . ILE A 1 399 ? 142.201 123.824 51.985 1.00 21.58 ? 399 ILE A CA 1 ATOM 3085 C C . ILE A 1 399 ? 143.576 124.396 52.337 1.00 25.34 ? 399 ILE A C 1 ATOM 3086 O O . ILE A 1 399 ? 143.843 125.560 52.067 1.00 23.26 ? 399 ILE A O 1 ATOM 3087 C CB . ILE A 1 399 ? 141.371 123.539 53.256 1.00 20.26 ? 399 ILE A CB 1 ATOM 3088 C CG1 . ILE A 1 399 ? 139.919 123.203 52.865 1.00 20.44 ? 399 ILE A CG1 1 ATOM 3089 C CG2 . ILE A 1 399 ? 141.409 124.716 54.202 1.00 17.68 ? 399 ILE A CG2 1 ATOM 3090 C CD1 . ILE A 1 399 ? 139.004 123.023 54.060 1.00 25.12 ? 399 ILE A CD1 1 ATOM 3091 N N . CYS A 1 400 ? 144.445 123.585 52.931 1.00 22.55 ? 400 CYS A N 1 ATOM 3092 C CA . CYS A 1 400 ? 145.788 124.053 53.252 1.00 20.78 ? 400 CYS A CA 1 ATOM 3093 C C . CYS A 1 400 ? 146.603 124.588 52.043 1.00 21.63 ? 400 CYS A C 1 ATOM 3094 O O . CYS A 1 400 ? 147.254 125.620 52.170 1.00 20.37 ? 400 CYS A O 1 ATOM 3095 C CB . CYS A 1 400 ? 146.546 122.996 54.065 1.00 23.38 ? 400 CYS A CB 1 ATOM 3096 S SG . CYS A 1 400 ? 145.689 122.631 55.638 1.00 27.78 ? 400 CYS A SG 1 ATOM 3097 N N . PRO A 1 401 ? 146.554 123.918 50.871 1.00 20.94 ? 401 PRO A N 1 ATOM 3098 C CA . PRO A 1 401 ? 147.239 124.522 49.716 1.00 23.34 ? 401 PRO A CA 1 ATOM 3099 C C . PRO A 1 401 ? 146.611 125.857 49.285 1.00 22.36 ? 401 PRO A C 1 ATOM 3100 O O . PRO A 1 401 ? 147.355 126.788 48.917 1.00 17.79 ? 401 PRO A O 1 ATOM 3101 C CB . PRO A 1 401 ? 147.045 123.473 48.604 1.00 20.70 ? 401 PRO A CB 1 ATOM 3102 C CG . PRO A 1 401 ? 146.950 122.151 49.361 1.00 19.44 ? 401 PRO A CG 1 ATOM 3103 C CD . PRO A 1 401 ? 146.129 122.531 50.587 1.00 22.06 ? 401 PRO A CD 1 ATOM 3104 N N . ALA A 1 402 ? 145.281 125.960 49.321 1.00 15.96 ? 402 ALA A N 1 ATOM 3105 C CA . ALA A 1 402 ? 144.620 127.221 48.929 1.00 18.56 ? 402 ALA A CA 1 ATOM 3106 C C . ALA A 1 402 ? 145.033 128.349 49.861 1.00 18.31 ? 402 ALA A C 1 ATOM 3107 O O . ALA A 1 402 ? 145.338 129.463 49.409 1.00 18.97 ? 402 ALA A O 1 ATOM 3108 C CB . ALA A 1 402 ? 143.080 127.079 48.891 1.00 15.19 ? 402 ALA A CB 1 ATOM 3109 N N . LEU A 1 403 ? 145.052 128.067 51.162 1.00 19.47 ? 403 LEU A N 1 ATOM 3110 C CA . LEU A 1 403 ? 145.484 129.071 52.136 1.00 16.55 ? 403 LEU A CA 1 ATOM 3111 C C . LEU A 1 403 ? 146.958 129.457 51.968 1.00 25.29 ? 403 LEU A C 1 ATOM 3112 O O . LEU A 1 403 ? 147.302 130.641 52.100 1.00 19.35 ? 403 LEU A O 1 ATOM 3113 C CB . LEU A 1 403 ? 145.216 128.604 53.571 1.00 26.26 ? 403 LEU A CB 1 ATOM 3114 C CG . LEU A 1 403 ? 143.739 128.641 53.981 1.00 29.07 ? 403 LEU A CG 1 ATOM 3115 C CD1 . LEU A 1 403 ? 143.483 127.696 55.143 1.00 24.38 ? 403 LEU A CD1 1 ATOM 3116 C CD2 . LEU A 1 403 ? 143.329 130.074 54.355 1.00 17.15 ? 403 LEU A CD2 1 ATOM 3117 N N A GLU A 1 404 ? 147.825 128.474 51.695 0.46 21.36 ? 404 GLU A N 1 ATOM 3118 N N B GLU A 1 404 ? 147.824 128.486 51.689 0.54 21.18 ? 404 GLU A N 1 ATOM 3119 C CA A GLU A 1 404 ? 149.259 128.749 51.489 0.46 23.38 ? 404 GLU A CA 1 ATOM 3120 C CA B GLU A 1 404 ? 149.242 128.813 51.529 0.54 23.02 ? 404 GLU A CA 1 ATOM 3121 C C A GLU A 1 404 ? 149.452 129.631 50.261 0.46 21.24 ? 404 GLU A C 1 ATOM 3122 C C B GLU A 1 404 ? 149.467 129.632 50.254 0.54 21.21 ? 404 GLU A C 1 ATOM 3123 O O A GLU A 1 404 ? 150.233 130.583 50.282 0.46 20.94 ? 404 GLU A O 1 ATOM 3124 O O B GLU A 1 404 ? 150.283 130.553 50.241 0.54 21.05 ? 404 GLU A O 1 ATOM 3125 C CB A GLU A 1 404 ? 150.081 127.456 51.329 0.46 26.16 ? 404 GLU A CB 1 ATOM 3126 C CB B GLU A 1 404 ? 150.109 127.553 51.540 0.54 24.79 ? 404 GLU A CB 1 ATOM 3127 C CG A GLU A 1 404 ? 151.514 127.703 50.801 0.46 28.50 ? 404 GLU A CG 1 ATOM 3128 C CG B GLU A 1 404 ? 151.585 127.818 51.281 0.54 27.97 ? 404 GLU A CG 1 ATOM 3129 C CD A GLU A 1 404 ? 152.324 126.425 50.545 0.46 27.98 ? 404 GLU A CD 1 ATOM 3130 C CD B GLU A 1 404 ? 152.335 128.333 52.500 0.54 29.56 ? 404 GLU A CD 1 ATOM 3131 O OE1 A GLU A 1 404 ? 152.099 125.751 49.512 0.46 26.11 ? 404 GLU A OE1 1 ATOM 3132 O OE1 B GLU A 1 404 ? 151.692 128.751 53.491 0.54 27.26 ? 404 GLU A OE1 1 ATOM 3133 O OE2 A GLU A 1 404 ? 153.208 126.106 51.369 0.46 28.66 ? 404 GLU A OE2 1 ATOM 3134 O OE2 B GLU A 1 404 ? 153.582 128.304 52.465 0.54 38.76 ? 404 GLU A OE2 1 ATOM 3135 N N . PHE A 1 405 ? 148.728 129.301 49.194 1.00 19.64 ? 405 PHE A N 1 ATOM 3136 C CA . PHE A 1 405 ? 148.793 130.061 47.958 1.00 19.29 ? 405 PHE A CA 1 ATOM 3137 C C . PHE A 1 405 ? 148.397 131.516 48.218 1.00 21.91 ? 405 PHE A C 1 ATOM 3138 O O . PHE A 1 405 ? 149.072 132.448 47.768 1.00 20.59 ? 405 PHE A O 1 ATOM 3139 C CB . PHE A 1 405 ? 147.867 129.479 46.875 1.00 17.28 ? 405 PHE A CB 1 ATOM 3140 C CG . PHE A 1 405 ? 147.895 130.279 45.598 1.00 23.05 ? 405 PHE A CG 1 ATOM 3141 C CD1 . PHE A 1 405 ? 147.035 131.365 45.411 1.00 26.43 ? 405 PHE A CD1 1 ATOM 3142 C CD2 . PHE A 1 405 ? 148.831 129.987 44.606 1.00 26.82 ? 405 PHE A CD2 1 ATOM 3143 C CE1 . PHE A 1 405 ? 147.093 132.130 44.255 1.00 17.24 ? 405 PHE A CE1 1 ATOM 3144 C CE2 . PHE A 1 405 ? 148.889 130.745 43.438 1.00 24.61 ? 405 PHE A CE2 1 ATOM 3145 C CZ . PHE A 1 405 ? 148.025 131.807 43.261 1.00 19.62 ? 405 PHE A CZ 1 ATOM 3146 N N . THR A 1 406 ? 147.296 131.708 48.944 1.00 21.28 ? 406 THR A N 1 ATOM 3147 C CA . THR A 1 406 ? 146.809 133.054 49.204 1.00 16.39 ? 406 THR A CA 1 ATOM 3148 C C . THR A 1 406 ? 147.801 133.890 50.029 1.00 19.87 ? 406 THR A C 1 ATOM 3149 O O . THR A 1 406 ? 148.006 135.072 49.742 1.00 23.95 ? 406 THR A O 1 ATOM 3150 C CB . THR A 1 406 ? 145.424 133.036 49.859 1.00 16.10 ? 406 THR A CB 1 ATOM 3151 O OG1 . THR A 1 406 ? 144.537 132.208 49.080 1.00 18.11 ? 406 THR A OG1 1 ATOM 3152 C CG2 . THR A 1 406 ? 144.863 134.460 49.926 1.00 17.10 ? 406 THR A CG2 1 ATOM 3153 N N . LYS A 1 407 ? 148.419 133.289 51.043 1.00 22.32 ? 407 LYS A N 1 ATOM 3154 C CA . LYS A 1 407 ? 149.415 134.006 51.847 1.00 30.63 ? 407 LYS A CA 1 ATOM 3155 C C . LYS A 1 407 ? 150.614 134.430 51.008 1.00 25.90 ? 407 LYS A C 1 ATOM 3156 O O . LYS A 1 407 ? 151.011 135.611 51.015 1.00 21.20 ? 407 LYS A O 1 ATOM 3157 C CB . LYS A 1 407 ? 149.927 133.134 52.990 1.00 32.12 ? 407 LYS A CB 1 ATOM 3158 C CG . LYS A 1 407 ? 148.866 132.630 53.939 1.00 46.14 ? 407 LYS A CG 1 ATOM 3159 C CD . LYS A 1 407 ? 149.473 131.662 54.956 1.00 53.81 ? 407 LYS A CD 1 ATOM 3160 C CE . LYS A 1 407 ? 148.421 131.152 55.943 1.00 54.43 ? 407 LYS A CE 1 ATOM 3161 N NZ . LYS A 1 407 ? 149.012 130.288 57.015 1.00 52.33 ? 407 LYS A NZ 1 ATOM 3162 N N . LYS A 1 408 ? 151.199 133.460 50.305 1.00 22.12 ? 408 LYS A N 1 ATOM 3163 C CA . LYS A 1 408 ? 152.407 133.720 49.514 1.00 27.64 ? 408 LYS A CA 1 ATOM 3164 C C . LYS A 1 408 ? 152.126 134.759 48.438 1.00 26.68 ? 408 LYS A C 1 ATOM 3165 O O . LYS A 1 408 ? 152.955 135.626 48.169 1.00 28.49 ? 408 LYS A O 1 ATOM 3166 C CB . LYS A 1 408 ? 152.927 132.436 48.854 1.00 21.86 ? 408 LYS A CB 1 ATOM 3167 C CG . LYS A 1 408 ? 153.453 131.374 49.811 1.00 30.02 ? 408 LYS A CG 1 ATOM 3168 C CD . LYS A 1 408 ? 154.684 131.858 50.542 1.00 46.90 ? 408 LYS A CD 1 ATOM 3169 C CE . LYS A 1 408 ? 155.306 130.750 51.383 1.00 52.53 ? 408 LYS A CE 1 ATOM 3170 N NZ . LYS A 1 408 ? 156.446 131.290 52.179 1.00 57.94 ? 408 LYS A NZ 1 ATOM 3171 N N . PHE A 1 409 ? 150.960 134.661 47.809 1.00 24.48 ? 409 PHE A N 1 ATOM 3172 C CA . PHE A 1 409 ? 150.607 135.609 46.760 1.00 21.23 ? 409 PHE A CA 1 ATOM 3173 C C . PHE A 1 409 ? 150.474 137.029 47.321 1.00 28.47 ? 409 PHE A C 1 ATOM 3174 O O . PHE A 1 409 ? 150.995 137.984 46.742 1.00 30.47 ? 409 PHE A O 1 ATOM 3175 C CB . PHE A 1 409 ? 149.308 135.195 46.062 1.00 23.33 ? 409 PHE A CB 1 ATOM 3176 C CG . PHE A 1 409 ? 149.056 135.939 44.787 1.00 27.14 ? 409 PHE A CG 1 ATOM 3177 C CD1 . PHE A 1 409 ? 148.491 137.206 44.806 1.00 27.21 ? 409 PHE A CD1 1 ATOM 3178 C CD2 . PHE A 1 409 ? 149.406 135.382 43.568 1.00 26.91 ? 409 PHE A CD2 1 ATOM 3179 C CE1 . PHE A 1 409 ? 148.261 137.897 43.624 1.00 18.40 ? 409 PHE A CE1 1 ATOM 3180 C CE2 . PHE A 1 409 ? 149.181 136.069 42.390 1.00 25.91 ? 409 PHE A CE2 1 ATOM 3181 C CZ . PHE A 1 409 ? 148.618 137.332 42.421 1.00 26.59 ? 409 PHE A CZ 1 ATOM 3182 N N . SER A 1 410 ? 149.782 137.167 48.450 1.00 27.05 ? 410 SER A N 1 ATOM 3183 C CA . SER A 1 410 ? 149.517 138.488 49.027 1.00 26.84 ? 410 SER A CA 1 ATOM 3184 C C . SER A 1 410 ? 150.763 139.161 49.611 1.00 32.23 ? 410 SER A C 1 ATOM 3185 O O . SER A 1 410 ? 150.788 140.386 49.823 1.00 21.54 ? 410 SER A O 1 ATOM 3186 C CB . SER A 1 410 ? 148.423 138.381 50.098 1.00 26.38 ? 410 SER A CB 1 ATOM 3187 O OG . SER A 1 410 ? 148.935 137.776 51.271 1.00 35.03 ? 410 SER A OG 1 ATOM 3188 N N . GLU A 1 411 ? 151.804 138.378 49.875 1.00 28.60 ? 411 GLU A N 1 ATOM 3189 C CA . GLU A 1 411 ? 153.026 138.950 50.442 1.00 30.80 ? 411 GLU A CA 1 ATOM 3190 C C . GLU A 1 411 ? 153.752 139.874 49.467 1.00 31.38 ? 411 GLU A C 1 ATOM 3191 O O . GLU A 1 411 ? 154.628 140.632 49.866 1.00 29.45 ? 411 GLU A O 1 ATOM 3192 C CB . GLU A 1 411 ? 153.969 137.856 50.944 1.00 32.39 ? 411 GLU A CB 1 ATOM 3193 C CG . GLU A 1 411 ? 153.658 137.404 52.368 1.00 44.52 ? 411 GLU A CG 1 ATOM 3194 C CD . GLU A 1 411 ? 154.292 136.067 52.710 1.00 58.98 ? 411 GLU A CD 1 ATOM 3195 O OE1 . GLU A 1 411 ? 155.111 135.564 51.907 1.00 63.44 ? 411 GLU A OE1 1 ATOM 3196 O OE2 . GLU A 1 411 ? 153.965 135.518 53.785 1.00 63.74 ? 411 GLU A OE2 1 ATOM 3197 N N . TRP A 1 412 ? 153.383 139.821 48.193 1.00 31.02 ? 412 TRP A N 1 ATOM 3198 C CA . TRP A 1 412 ? 154.027 140.670 47.198 1.00 31.60 ? 412 TRP A CA 1 ATOM 3199 C C . TRP A 1 412 ? 153.188 141.915 46.904 1.00 34.01 ? 412 TRP A C 1 ATOM 3200 O O . TRP A 1 412 ? 153.395 142.608 45.906 1.00 34.04 ? 412 TRP A O 1 ATOM 3201 C CB . TRP A 1 412 ? 154.365 139.852 45.941 1.00 30.24 ? 412 TRP A CB 1 ATOM 3202 C CG . TRP A 1 412 ? 155.472 138.869 46.241 1.00 36.04 ? 412 TRP A CG 1 ATOM 3203 C CD1 . TRP A 1 412 ? 155.333 137.583 46.701 1.00 32.95 ? 412 TRP A CD1 1 ATOM 3204 C CD2 . TRP A 1 412 ? 156.889 139.114 46.157 1.00 35.76 ? 412 TRP A CD2 1 ATOM 3205 N NE1 . TRP A 1 412 ? 156.575 137.015 46.894 1.00 35.15 ? 412 TRP A NE1 1 ATOM 3206 C CE2 . TRP A 1 412 ? 157.544 137.930 46.568 1.00 32.93 ? 412 TRP A CE2 1 ATOM 3207 C CE3 . TRP A 1 412 ? 157.663 140.213 45.761 1.00 40.29 ? 412 TRP A CE3 1 ATOM 3208 C CZ2 . TRP A 1 412 ? 158.940 137.813 46.583 1.00 31.11 ? 412 TRP A CZ2 1 ATOM 3209 C CZ3 . TRP A 1 412 ? 159.059 140.101 45.786 1.00 36.03 ? 412 TRP A CZ3 1 ATOM 3210 C CH2 . TRP A 1 412 ? 159.680 138.910 46.196 1.00 35.18 ? 412 TRP A CH2 1 ATOM 3211 N N . GLY A 1 413 ? 152.235 142.198 47.786 1.00 34.88 ? 413 GLY A N 1 ATOM 3212 C CA . GLY A 1 413 ? 151.639 143.523 47.828 1.00 29.84 ? 413 GLY A CA 1 ATOM 3213 C C . GLY A 1 413 ? 150.253 143.652 47.224 1.00 34.20 ? 413 GLY A C 1 ATOM 3214 O O . GLY A 1 413 ? 149.668 144.733 47.265 1.00 36.99 ? 413 GLY A O 1 ATOM 3215 N N . ASN A 1 414 ? 149.715 142.570 46.665 1.00 29.47 ? 414 ASN A N 1 ATOM 3216 C CA . ASN A 1 414 ? 148.394 142.651 46.040 1.00 33.05 ? 414 ASN A CA 1 ATOM 3217 C C . ASN A 1 414 ? 147.235 142.338 46.974 1.00 29.42 ? 414 ASN A C 1 ATOM 3218 O O . ASN A 1 414 ? 147.372 141.552 47.920 1.00 28.55 ? 414 ASN A O 1 ATOM 3219 C CB . ASN A 1 414 ? 148.309 141.736 44.816 1.00 36.99 ? 414 ASN A CB 1 ATOM 3220 C CG . ASN A 1 414 ? 149.118 142.260 43.650 1.00 37.57 ? 414 ASN A CG 1 ATOM 3221 O OD1 . ASN A 1 414 ? 150.071 141.616 43.216 1.00 24.22 ? 414 ASN A OD1 1 ATOM 3222 N ND2 . ASN A 1 414 ? 148.749 143.454 43.144 1.00 34.65 ? 414 ASN A ND2 1 ATOM 3223 N N . ASN A 1 415 ? 146.092 142.958 46.696 1.00 29.37 ? 415 ASN A N 1 ATOM 3224 C CA . ASN A 1 415 ? 144.849 142.614 47.371 1.00 27.80 ? 415 ASN A CA 1 ATOM 3225 C C . ASN A 1 415 ? 144.388 141.184 47.073 1.00 24.54 ? 415 ASN A C 1 ATOM 3226 O O . ASN A 1 415 ? 144.299 140.763 45.911 1.00 27.36 ? 415 ASN A O 1 ATOM 3227 C CB . ASN A 1 415 ? 143.743 143.619 47.002 1.00 29.91 ? 415 ASN A CB 1 ATOM 3228 C CG . ASN A 1 415 ? 143.865 144.926 47.782 1.00 31.84 ? 415 ASN A CG 1 ATOM 3229 O OD1 . ASN A 1 415 ? 144.738 145.059 48.640 1.00 33.33 ? 415 ASN A OD1 1 ATOM 3230 N ND2 . ASN A 1 415 ? 142.988 145.888 47.491 1.00 25.20 ? 415 ASN A ND2 1 ATOM 3231 N N . ALA A 1 416 ? 144.089 140.444 48.134 1.00 22.82 ? 416 ALA A N 1 ATOM 3232 C CA . ALA A 1 416 ? 143.532 139.107 48.012 1.00 23.24 ? 416 ALA A CA 1 ATOM 3233 C C . ALA A 1 416 ? 142.337 139.022 48.947 1.00 25.11 ? 416 ALA A C 1 ATOM 3234 O O . ALA A 1 416 ? 142.330 139.655 50.018 1.00 23.33 ? 416 ALA A O 1 ATOM 3235 C CB . ALA A 1 416 ? 144.574 138.051 48.383 1.00 20.78 ? 416 ALA A CB 1 ATOM 3236 N N . PHE A 1 417 ? 141.338 138.244 48.538 1.00 18.64 ? 417 PHE A N 1 ATOM 3237 C CA . PHE A 1 417 ? 140.124 138.037 49.321 1.00 19.47 ? 417 PHE A CA 1 ATOM 3238 C C . PHE A 1 417 ? 139.875 136.525 49.449 1.00 19.55 ? 417 PHE A C 1 ATOM 3239 O O . PHE A 1 417 ? 139.918 135.800 48.442 1.00 20.56 ? 417 PHE A O 1 ATOM 3240 C CB . PHE A 1 417 ? 138.938 138.743 48.635 1.00 17.66 ? 417 PHE A CB 1 ATOM 3241 C CG . PHE A 1 417 ? 139.187 140.218 48.362 1.00 21.40 ? 417 PHE A CG 1 ATOM 3242 C CD1 . PHE A 1 417 ? 138.882 141.178 49.318 1.00 19.37 ? 417 PHE A CD1 1 ATOM 3243 C CD2 . PHE A 1 417 ? 139.764 140.634 47.166 1.00 20.42 ? 417 PHE A CD2 1 ATOM 3244 C CE1 . PHE A 1 417 ? 139.123 142.538 49.083 1.00 25.38 ? 417 PHE A CE1 1 ATOM 3245 C CE2 . PHE A 1 417 ? 140.015 141.997 46.924 1.00 19.41 ? 417 PHE A CE2 1 ATOM 3246 C CZ . PHE A 1 417 ? 139.691 142.943 47.888 1.00 24.34 ? 417 PHE A CZ 1 ATOM 3247 N N . PHE A 1 418 ? 139.628 136.041 50.669 1.00 21.40 ? 418 PHE A N 1 ATOM 3248 C CA . PHE A 1 418 ? 139.413 134.595 50.888 1.00 21.98 ? 418 PHE A CA 1 ATOM 3249 C C . PHE A 1 418 ? 138.017 134.303 51.465 1.00 24.52 ? 418 PHE A C 1 ATOM 3250 O O . PHE A 1 418 ? 137.551 135.031 52.372 1.00 18.45 ? 418 PHE A O 1 ATOM 3251 C CB . PHE A 1 418 ? 140.501 134.022 51.812 1.00 16.98 ? 418 PHE A CB 1 ATOM 3252 C CG . PHE A 1 418 ? 140.634 132.516 51.753 1.00 19.61 ? 418 PHE A CG 1 ATOM 3253 C CD1 . PHE A 1 418 ? 139.787 131.696 52.498 1.00 16.34 ? 418 PHE A CD1 1 ATOM 3254 C CD2 . PHE A 1 418 ? 141.626 131.915 50.963 1.00 16.41 ? 418 PHE A CD2 1 ATOM 3255 C CE1 . PHE A 1 418 ? 139.910 130.284 52.442 1.00 19.49 ? 418 PHE A CE1 1 ATOM 3256 C CE2 . PHE A 1 418 ? 141.756 130.506 50.908 1.00 21.66 ? 418 PHE A CE2 1 ATOM 3257 C CZ . PHE A 1 418 ? 140.898 129.699 51.655 1.00 17.73 ? 418 PHE A CZ 1 ATOM 3258 N N . TYR A 1 419 ? 137.355 133.252 50.954 1.00 21.65 ? 419 TYR A N 1 ATOM 3259 C CA . TYR A 1 419 ? 136.029 132.840 51.466 1.00 23.02 ? 419 TYR A CA 1 ATOM 3260 C C . TYR A 1 419 ? 136.005 131.385 51.961 1.00 24.36 ? 419 TYR A C 1 ATOM 3261 O O . TYR A 1 419 ? 136.768 130.527 51.493 1.00 19.10 ? 419 TYR A O 1 ATOM 3262 C CB . TYR A 1 419 ? 134.899 133.036 50.420 1.00 17.10 ? 419 TYR A CB 1 ATOM 3263 C CG . TYR A 1 419 ? 134.962 132.062 49.265 1.00 16.52 ? 419 TYR A CG 1 ATOM 3264 C CD1 . TYR A 1 419 ? 134.451 130.765 49.384 1.00 16.60 ? 419 TYR A CD1 1 ATOM 3265 C CD2 . TYR A 1 419 ? 135.534 132.428 48.056 1.00 18.70 ? 419 TYR A CD2 1 ATOM 3266 C CE1 . TYR A 1 419 ? 134.516 129.866 48.327 1.00 17.66 ? 419 TYR A CE1 1 ATOM 3267 C CE2 . TYR A 1 419 ? 135.604 131.528 46.980 1.00 17.24 ? 419 TYR A CE2 1 ATOM 3268 C CZ . TYR A 1 419 ? 135.103 130.248 47.132 1.00 21.03 ? 419 TYR A CZ 1 ATOM 3269 O OH . TYR A 1 419 ? 135.197 129.339 46.092 1.00 16.79 ? 419 TYR A OH 1 ATOM 3270 N N . TYR A 1 420 ? 135.086 131.107 52.879 1.00 21.76 ? 420 TYR A N 1 ATOM 3271 C CA . TYR A 1 420 ? 134.844 129.752 53.349 1.00 17.96 ? 420 TYR A CA 1 ATOM 3272 C C . TYR A 1 420 ? 133.356 129.477 53.113 1.00 23.81 ? 420 TYR A C 1 ATOM 3273 O O . TYR A 1 420 ? 132.506 130.050 53.799 1.00 22.91 ? 420 TYR A O 1 ATOM 3274 C CB . TYR A 1 420 ? 135.160 129.669 54.834 1.00 18.64 ? 420 TYR A CB 1 ATOM 3275 C CG . TYR A 1 420 ? 135.139 128.281 55.454 1.00 23.71 ? 420 TYR A CG 1 ATOM 3276 C CD1 . TYR A 1 420 ? 135.988 127.279 55.002 1.00 18.56 ? 420 TYR A CD1 1 ATOM 3277 C CD2 . TYR A 1 420 ? 134.306 127.998 56.537 1.00 23.12 ? 420 TYR A CD2 1 ATOM 3278 C CE1 . TYR A 1 420 ? 136.001 126.011 55.601 1.00 24.49 ? 420 TYR A CE1 1 ATOM 3279 C CE2 . TYR A 1 420 ? 134.304 126.747 57.139 1.00 29.80 ? 420 TYR A CE2 1 ATOM 3280 C CZ . TYR A 1 420 ? 135.157 125.756 56.670 1.00 28.43 ? 420 TYR A CZ 1 ATOM 3281 O OH . TYR A 1 420 ? 135.150 124.514 57.275 1.00 28.08 ? 420 TYR A OH 1 ATOM 3282 N N . PHE A 1 421 ? 133.048 128.614 52.146 1.00 22.07 ? 421 PHE A N 1 ATOM 3283 C CA . PHE A 1 421 ? 131.655 128.322 51.770 1.00 25.81 ? 421 PHE A CA 1 ATOM 3284 C C . PHE A 1 421 ? 131.097 127.162 52.604 1.00 24.43 ? 421 PHE A C 1 ATOM 3285 O O . PHE A 1 421 ? 131.628 126.035 52.578 1.00 24.86 ? 421 PHE A O 1 ATOM 3286 C CB . PHE A 1 421 ? 131.587 128.034 50.266 1.00 18.40 ? 421 PHE A CB 1 ATOM 3287 C CG . PHE A 1 421 ? 130.196 127.761 49.733 1.00 25.81 ? 421 PHE A CG 1 ATOM 3288 C CD1 . PHE A 1 421 ? 129.374 128.803 49.307 1.00 21.57 ? 421 PHE A CD1 1 ATOM 3289 C CD2 . PHE A 1 421 ? 129.738 126.456 49.604 1.00 21.95 ? 421 PHE A CD2 1 ATOM 3290 C CE1 . PHE A 1 421 ? 128.103 128.546 48.792 1.00 32.25 ? 421 PHE A CE1 1 ATOM 3291 C CE2 . PHE A 1 421 ? 128.480 126.187 49.087 1.00 26.01 ? 421 PHE A CE2 1 ATOM 3292 C CZ . PHE A 1 421 ? 127.655 127.228 48.685 1.00 29.57 ? 421 PHE A CZ 1 ATOM 3293 N N . GLU A 1 422 ? 130.038 127.435 53.362 1.00 24.49 ? 422 GLU A N 1 ATOM 3294 C CA . GLU A 1 422 ? 129.530 126.425 54.290 1.00 26.94 ? 422 GLU A CA 1 ATOM 3295 C C . GLU A 1 422 ? 128.027 126.169 54.178 1.00 30.64 ? 422 GLU A C 1 ATOM 3296 O O . GLU A 1 422 ? 127.398 125.723 55.137 1.00 28.96 ? 422 GLU A O 1 ATOM 3297 C CB . GLU A 1 422 ? 129.948 126.752 55.741 1.00 37.61 ? 422 GLU A CB 1 ATOM 3298 C CG . GLU A 1 422 ? 129.396 128.063 56.290 1.00 44.40 ? 422 GLU A CG 1 ATOM 3299 C CD . GLU A 1 422 ? 130.108 128.548 57.562 1.00 46.40 ? 422 GLU A CD 1 ATOM 3300 O OE1 . GLU A 1 422 ? 131.099 127.926 57.989 1.00 38.45 ? 422 GLU A OE1 1 ATOM 3301 O OE2 . GLU A 1 422 ? 129.667 129.566 58.138 1.00 52.03 ? 422 GLU A OE2 1 ATOM 3302 N N . HIS A 1 423 ? 127.442 126.433 53.012 1.00 31.11 ? 423 HIS A N 1 ATOM 3303 C CA . HIS A 1 423 ? 126.036 126.084 52.820 1.00 31.55 ? 423 HIS A CA 1 ATOM 3304 C C . HIS A 1 423 ? 125.836 124.780 52.033 1.00 30.47 ? 423 HIS A C 1 ATOM 3305 O O . HIS A 1 423 ? 126.302 124.645 50.898 1.00 27.59 ? 423 HIS A O 1 ATOM 3306 C CB . HIS A 1 423 ? 125.257 127.203 52.135 1.00 29.37 ? 423 HIS A CB 1 ATOM 3307 C CG . HIS A 1 423 ? 123.837 126.829 51.841 1.00 33.12 ? 423 HIS A CG 1 ATOM 3308 N ND1 . HIS A 1 423 ? 122.897 126.642 52.833 1.00 35.56 ? 423 HIS A ND1 1 ATOM 3309 C CD2 . HIS A 1 423 ? 123.209 126.551 50.674 1.00 33.80 ? 423 HIS A CD2 1 ATOM 3310 C CE1 . HIS A 1 423 ? 121.746 126.288 52.288 1.00 36.44 ? 423 HIS A CE1 1 ATOM 3311 N NE2 . HIS A 1 423 ? 121.907 126.228 50.978 1.00 38.19 ? 423 HIS A NE2 1 ATOM 3312 N N . ARG A 1 424 ? 125.121 123.834 52.633 1.00 31.92 ? 424 ARG A N 1 ATOM 3313 C CA . ARG A 1 424 ? 124.761 122.600 51.944 1.00 33.52 ? 424 ARG A CA 1 ATOM 3314 C C . ARG A 1 424 ? 123.439 122.741 51.174 1.00 32.06 ? 424 ARG A C 1 ATOM 3315 O O . ARG A 1 424 ? 122.392 123.001 51.770 1.00 30.43 ? 424 ARG A O 1 ATOM 3316 C CB . ARG A 1 424 ? 124.647 121.454 52.944 1.00 30.17 ? 424 ARG A CB 1 ATOM 3317 C CG . ARG A 1 424 ? 124.034 120.201 52.341 1.00 34.97 ? 424 ARG A CG 1 ATOM 3318 C CD . ARG A 1 424 ? 123.950 119.091 53.356 1.00 29.55 ? 424 ARG A CD 1 ATOM 3319 N NE . ARG A 1 424 ? 123.071 118.020 52.898 1.00 49.52 ? 424 ARG A NE 1 ATOM 3320 C CZ . ARG A 1 424 ? 123.499 116.910 52.307 1.00 54.05 ? 424 ARG A CZ 1 ATOM 3321 N NH1 . ARG A 1 424 ? 124.808 116.723 52.116 1.00 48.16 ? 424 ARG A NH1 1 ATOM 3322 N NH2 . ARG A 1 424 ? 122.623 115.981 51.918 1.00 49.36 ? 424 ARG A NH2 1 ATOM 3323 N N . SER A 1 425 ? 123.507 122.572 49.854 1.00 29.19 ? 425 SER A N 1 ATOM 3324 C CA . SER A 1 425 ? 122.351 122.693 48.965 1.00 33.64 ? 425 SER A CA 1 ATOM 3325 C C . SER A 1 425 ? 121.170 121.857 49.450 1.00 37.69 ? 425 SER A C 1 ATOM 3326 O O . SER A 1 425 ? 121.345 120.716 49.871 1.00 37.03 ? 425 SER A O 1 ATOM 3327 C CB . SER A 1 425 ? 122.758 122.268 47.551 1.00 37.34 ? 425 SER A CB 1 ATOM 3328 O OG . SER A 1 425 ? 121.670 122.299 46.647 1.00 39.11 ? 425 SER A OG 1 ATOM 3329 N N . SER A 1 426 ? 119.967 122.421 49.405 1.00 37.83 ? 426 SER A N 1 ATOM 3330 C CA . SER A 1 426 ? 118.787 121.671 49.814 1.00 33.25 ? 426 SER A CA 1 ATOM 3331 C C . SER A 1 426 ? 118.456 120.572 48.798 1.00 38.35 ? 426 SER A C 1 ATOM 3332 O O . SER A 1 426 ? 117.711 119.649 49.097 1.00 35.54 ? 426 SER A O 1 ATOM 3333 C CB . SER A 1 426 ? 117.586 122.606 50.010 1.00 50.07 ? 426 SER A CB 1 ATOM 3334 O OG . SER A 1 426 ? 117.274 123.305 48.815 1.00 34.60 ? 426 SER A OG 1 ATOM 3335 N N . LYS A 1 427 ? 119.015 120.669 47.597 1.00 45.46 ? 427 LYS A N 1 ATOM 3336 C CA . LYS A 1 427 ? 118.736 119.678 46.557 1.00 51.55 ? 427 LYS A CA 1 ATOM 3337 C C . LYS A 1 427 ? 119.830 118.603 46.452 1.00 48.47 ? 427 LYS A C 1 ATOM 3338 O O . LYS A 1 427 ? 119.742 117.712 45.605 1.00 44.91 ? 427 LYS A O 1 ATOM 3339 C CB . LYS A 1 427 ? 118.552 120.367 45.199 1.00 56.95 ? 427 LYS A CB 1 ATOM 3340 C CG . LYS A 1 427 ? 117.416 121.381 45.156 1.00 64.62 ? 427 LYS A CG 1 ATOM 3341 C CD . LYS A 1 427 ? 117.357 122.106 43.812 1.00 66.65 ? 427 LYS A CD 1 ATOM 3342 C CE . LYS A 1 427 ? 117.103 121.140 42.661 1.00 67.77 ? 427 LYS A CE 1 ATOM 3343 N NZ . LYS A 1 427 ? 116.941 121.845 41.355 1.00 66.77 ? 427 LYS A NZ 1 ATOM 3344 N N . LEU A 1 428 ? 120.854 118.698 47.302 1.00 41.83 ? 428 LEU A N 1 ATOM 3345 C CA . LEU A 1 428 ? 121.981 117.754 47.296 1.00 36.57 ? 428 LEU A CA 1 ATOM 3346 C C . LEU A 1 428 ? 121.513 116.296 47.367 1.00 37.86 ? 428 LEU A C 1 ATOM 3347 O O . LEU A 1 428 ? 120.839 115.893 48.318 1.00 45.98 ? 428 LEU A O 1 ATOM 3348 C CB . LEU A 1 428 ? 122.917 118.059 48.470 1.00 38.28 ? 428 LEU A CB 1 ATOM 3349 C CG . LEU A 1 428 ? 124.445 118.099 48.291 1.00 43.64 ? 428 LEU A CG 1 ATOM 3350 C CD1 . LEU A 1 428 ? 125.123 116.891 48.911 1.00 44.34 ? 428 LEU A CD1 1 ATOM 3351 C CD2 . LEU A 1 428 ? 124.844 118.220 46.843 1.00 39.61 ? 428 LEU A CD2 1 ATOM 3352 N N . PRO A 1 429 ? 121.845 115.502 46.340 1.00 37.78 ? 429 PRO A N 1 ATOM 3353 C CA . PRO A 1 429 ? 121.408 114.098 46.285 1.00 40.31 ? 429 PRO A CA 1 ATOM 3354 C C . PRO A 1 429 ? 122.295 113.162 47.125 1.00 33.25 ? 429 PRO A C 1 ATOM 3355 O O . PRO A 1 429 ? 121.857 112.064 47.492 1.00 35.77 ? 429 PRO A O 1 ATOM 3356 C CB . PRO A 1 429 ? 121.484 113.763 44.792 1.00 33.23 ? 429 PRO A CB 1 ATOM 3357 C CG . PRO A 1 429 ? 122.479 114.714 44.226 1.00 35.79 ? 429 PRO A CG 1 ATOM 3358 C CD . PRO A 1 429 ? 122.559 115.926 45.124 1.00 35.03 ? 429 PRO A CD 1 ATOM 3359 N N . TRP A 1 430 ? 123.512 113.605 47.441 1.00 31.51 ? 430 TRP A N 1 ATOM 3360 C CA . TRP A 1 430 ? 124.384 112.896 48.376 1.00 40.11 ? 430 TRP A CA 1 ATOM 3361 C C . TRP A 1 430 ? 123.864 113.032 49.817 1.00 38.39 ? 430 TRP A C 1 ATOM 3362 O O . TRP A 1 430 ? 123.214 114.026 50.153 1.00 39.91 ? 430 TRP A O 1 ATOM 3363 C CB . TRP A 1 430 ? 125.804 113.469 48.307 1.00 29.48 ? 430 TRP A CB 1 ATOM 3364 C CG . TRP A 1 430 ? 126.464 113.422 46.946 1.00 28.50 ? 430 TRP A CG 1 ATOM 3365 C CD1 . TRP A 1 430 ? 126.529 114.435 46.024 1.00 34.05 ? 430 TRP A CD1 1 ATOM 3366 C CD2 . TRP A 1 430 ? 127.174 112.314 46.373 1.00 28.77 ? 430 TRP A CD2 1 ATOM 3367 N NE1 . TRP A 1 430 ? 127.230 114.020 44.909 1.00 27.12 ? 430 TRP A NE1 1 ATOM 3368 C CE2 . TRP A 1 430 ? 127.639 112.723 45.101 1.00 28.37 ? 430 TRP A CE2 1 ATOM 3369 C CE3 . TRP A 1 430 ? 127.467 111.019 46.816 1.00 29.93 ? 430 TRP A CE3 1 ATOM 3370 C CZ2 . TRP A 1 430 ? 128.374 111.877 44.267 1.00 27.88 ? 430 TRP A CZ2 1 ATOM 3371 C CZ3 . TRP A 1 430 ? 128.199 110.183 45.989 1.00 39.82 ? 430 TRP A CZ3 1 ATOM 3372 C CH2 . TRP A 1 430 ? 128.649 110.614 44.732 1.00 29.02 ? 430 TRP A CH2 1 ATOM 3373 N N . PRO A 1 431 ? 124.172 112.050 50.682 1.00 35.98 ? 431 PRO A N 1 ATOM 3374 C CA . PRO A 1 431 ? 123.689 112.037 52.075 1.00 40.74 ? 431 PRO A CA 1 ATOM 3375 C C . PRO A 1 431 ? 124.248 113.188 52.930 1.00 38.42 ? 431 PRO A C 1 ATOM 3376 O O . PRO A 1 431 ? 125.303 113.755 52.608 1.00 31.62 ? 431 PRO A O 1 ATOM 3377 C CB . PRO A 1 431 ? 124.204 110.694 52.604 1.00 44.52 ? 431 PRO A CB 1 ATOM 3378 C CG . PRO A 1 431 ? 125.433 110.417 51.761 1.00 39.91 ? 431 PRO A CG 1 ATOM 3379 C CD . PRO A 1 431 ? 125.029 110.885 50.391 1.00 35.04 ? 431 PRO A CD 1 ATOM 3380 N N . GLU A 1 432 ? 123.554 113.521 54.015 1.00 34.59 ? 432 GLU A N 1 ATOM 3381 C CA . GLU A 1 432 ? 123.914 114.701 54.806 1.00 46.22 ? 432 GLU A CA 1 ATOM 3382 C C . GLU A 1 432 ? 125.250 114.592 55.557 1.00 37.06 ? 432 GLU A C 1 ATOM 3383 O O . GLU A 1 432 ? 125.875 115.616 55.858 1.00 35.48 ? 432 GLU A O 1 ATOM 3384 C CB . GLU A 1 432 ? 122.772 115.126 55.746 1.00 56.09 ? 432 GLU A CB 1 ATOM 3385 C CG . GLU A 1 432 ? 122.740 114.416 57.085 1.00 73.66 ? 432 GLU A CG 1 ATOM 3386 C CD . GLU A 1 432 ? 121.475 114.728 57.873 1.00 90.19 ? 432 GLU A CD 1 ATOM 3387 O OE1 . GLU A 1 432 ? 120.545 115.329 57.290 1.00 92.42 ? 432 GLU A OE1 1 ATOM 3388 O OE2 . GLU A 1 432 ? 121.411 114.372 59.072 1.00 95.81 ? 432 GLU A OE2 1 ATOM 3389 N N . TRP A 1 433 ? 125.703 113.373 55.841 1.00 37.58 ? 433 TRP A N 1 ATOM 3390 C CA . TRP A 1 433 ? 127.018 113.218 56.474 1.00 39.88 ? 433 TRP A CA 1 ATOM 3391 C C . TRP A 1 433 ? 128.149 113.742 55.595 1.00 34.08 ? 433 TRP A C 1 ATOM 3392 O O . TRP A 1 433 ? 129.217 114.073 56.106 1.00 30.69 ? 433 TRP A O 1 ATOM 3393 C CB . TRP A 1 433 ? 127.299 111.773 56.928 1.00 36.85 ? 433 TRP A CB 1 ATOM 3394 C CG . TRP A 1 433 ? 127.634 110.766 55.840 1.00 34.47 ? 433 TRP A CG 1 ATOM 3395 C CD1 . TRP A 1 433 ? 126.800 109.812 55.330 1.00 39.27 ? 433 TRP A CD1 1 ATOM 3396 C CD2 . TRP A 1 433 ? 128.903 110.580 55.181 1.00 33.13 ? 433 TRP A CD2 1 ATOM 3397 N NE1 . TRP A 1 433 ? 127.460 109.059 54.384 1.00 35.55 ? 433 TRP A NE1 1 ATOM 3398 C CE2 . TRP A 1 433 ? 128.747 109.514 54.268 1.00 33.85 ? 433 TRP A CE2 1 ATOM 3399 C CE3 . TRP A 1 433 ? 130.149 111.223 55.264 1.00 31.60 ? 433 TRP A CE3 1 ATOM 3400 C CZ2 . TRP A 1 433 ? 129.790 109.070 53.447 1.00 36.45 ? 433 TRP A CZ2 1 ATOM 3401 C CZ3 . TRP A 1 433 ? 131.190 110.783 54.439 1.00 30.77 ? 433 TRP A CZ3 1 ATOM 3402 C CH2 . TRP A 1 433 ? 131.003 109.717 53.546 1.00 36.21 ? 433 TRP A CH2 1 ATOM 3403 N N . MET A 1 434 ? 127.928 113.831 54.282 1.00 34.16 ? 434 MET A N 1 ATOM 3404 C CA . MET A 1 434 ? 128.981 114.355 53.396 1.00 30.11 ? 434 MET A CA 1 ATOM 3405 C C . MET A 1 434 ? 129.039 115.879 53.372 1.00 26.84 ? 434 MET A C 1 ATOM 3406 O O . MET A 1 434 ? 129.995 116.458 52.829 1.00 25.37 ? 434 MET A O 1 ATOM 3407 C CB . MET A 1 434 ? 128.872 113.783 51.975 1.00 35.50 ? 434 MET A CB 1 ATOM 3408 C CG . MET A 1 434 ? 128.982 112.252 51.936 1.00 41.18 ? 434 MET A CG 1 ATOM 3409 S SD . MET A 1 434 ? 128.723 111.494 50.318 1.00 35.93 ? 434 MET A SD 1 ATOM 3410 C CE . MET A 1 434 ? 130.209 111.960 49.469 1.00 33.11 ? 434 MET A CE 1 ATOM 3411 N N . GLY A 1 435 ? 128.038 116.529 53.967 1.00 27.53 ? 435 GLY A N 1 ATOM 3412 C CA . GLY A 1 435 ? 128.107 117.966 54.216 1.00 26.61 ? 435 GLY A CA 1 ATOM 3413 C C . GLY A 1 435 ? 128.207 118.848 52.980 1.00 26.67 ? 435 GLY A C 1 ATOM 3414 O O . GLY A 1 435 ? 127.523 118.598 51.980 1.00 26.26 ? 435 GLY A O 1 ATOM 3415 N N . VAL A 1 436 ? 129.062 119.871 53.055 1.00 25.37 ? 436 VAL A N 1 ATOM 3416 C CA . VAL A 1 436 ? 129.190 120.900 52.017 1.00 24.40 ? 436 VAL A CA 1 ATOM 3417 C C . VAL A 1 436 ? 130.302 120.476 51.048 1.00 27.81 ? 436 VAL A C 1 ATOM 3418 O O . VAL A 1 436 ? 131.489 120.782 51.261 1.00 24.74 ? 436 VAL A O 1 ATOM 3419 C CB . VAL A 1 436 ? 129.526 122.275 52.670 1.00 24.69 ? 436 VAL A CB 1 ATOM 3420 C CG1 . VAL A 1 436 ? 129.696 123.373 51.620 1.00 21.21 ? 436 VAL A CG1 1 ATOM 3421 C CG2 . VAL A 1 436 ? 128.454 122.668 53.695 1.00 24.91 ? 436 VAL A CG2 1 ATOM 3422 N N . MET A 1 437 ? 129.915 119.763 49.992 1.00 22.77 ? 437 MET A N 1 ATOM 3423 C CA . MET A 1 437 ? 130.858 118.969 49.208 1.00 21.48 ? 437 MET A CA 1 ATOM 3424 C C . MET A 1 437 ? 131.671 119.727 48.172 1.00 26.67 ? 437 MET A C 1 ATOM 3425 O O . MET A 1 437 ? 131.297 120.825 47.734 1.00 19.78 ? 437 MET A O 1 ATOM 3426 C CB . MET A 1 437 ? 130.130 117.807 48.509 1.00 22.49 ? 437 MET A CB 1 ATOM 3427 C CG . MET A 1 437 ? 129.692 116.700 49.453 1.00 32.89 ? 437 MET A CG 1 ATOM 3428 S SD . MET A 1 437 ? 128.600 115.503 48.662 1.00 27.42 ? 437 MET A SD 1 ATOM 3429 C CE . MET A 1 437 ? 129.639 114.841 47.349 1.00 24.74 ? 437 MET A CE 1 ATOM 3430 N N . HIS A 1 438 ? 132.772 119.095 47.764 1.00 21.81 ? 438 HIS A N 1 ATOM 3431 C CA . HIS A 1 438 ? 133.638 119.580 46.683 1.00 20.43 ? 438 HIS A CA 1 ATOM 3432 C C . HIS A 1 438 ? 132.826 119.769 45.411 1.00 23.02 ? 438 HIS A C 1 ATOM 3433 O O . HIS A 1 438 ? 132.244 118.806 44.903 1.00 20.91 ? 438 HIS A O 1 ATOM 3434 C CB . HIS A 1 438 ? 134.737 118.539 46.433 1.00 20.15 ? 438 HIS A CB 1 ATOM 3435 C CG . HIS A 1 438 ? 135.774 118.963 45.436 1.00 21.38 ? 438 HIS A CG 1 ATOM 3436 N ND1 . HIS A 1 438 ? 136.629 120.023 45.656 1.00 24.32 ? 438 HIS A ND1 1 ATOM 3437 C CD2 . HIS A 1 438 ? 136.110 118.452 44.227 1.00 20.77 ? 438 HIS A CD2 1 ATOM 3438 C CE1 . HIS A 1 438 ? 137.443 120.151 44.621 1.00 24.79 ? 438 HIS A CE1 1 ATOM 3439 N NE2 . HIS A 1 438 ? 137.152 119.210 43.741 1.00 20.36 ? 438 HIS A NE2 1 ATOM 3440 N N . GLY A 1 439 ? 132.759 121.002 44.908 1.00 19.66 ? 439 GLY A N 1 ATOM 3441 C CA . GLY A 1 439 ? 132.061 121.270 43.654 1.00 18.59 ? 439 GLY A CA 1 ATOM 3442 C C . GLY A 1 439 ? 130.667 121.867 43.828 1.00 25.78 ? 439 GLY A C 1 ATOM 3443 O O . GLY A 1 439 ? 130.013 122.259 42.850 1.00 19.96 ? 439 GLY A O 1 ATOM 3444 N N . TYR A 1 440 ? 130.186 121.953 45.064 1.00 25.11 ? 440 TYR A N 1 ATOM 3445 C CA . TYR A 1 440 ? 128.788 122.347 45.237 1.00 23.21 ? 440 TYR A CA 1 ATOM 3446 C C . TYR A 1 440 ? 128.542 123.814 45.630 1.00 23.75 ? 440 TYR A C 1 ATOM 3447 O O . TYR A 1 440 ? 127.427 124.182 46.031 1.00 22.70 ? 440 TYR A O 1 ATOM 3448 C CB . TYR A 1 440 ? 128.028 121.326 46.097 1.00 21.62 ? 440 TYR A CB 1 ATOM 3449 C CG . TYR A 1 440 ? 127.810 120.033 45.328 1.00 23.96 ? 440 TYR A CG 1 ATOM 3450 C CD1 . TYR A 1 440 ? 128.759 119.011 45.354 1.00 22.73 ? 440 TYR A CD1 1 ATOM 3451 C CD2 . TYR A 1 440 ? 126.682 119.863 44.526 1.00 25.35 ? 440 TYR A CD2 1 ATOM 3452 C CE1 . TYR A 1 440 ? 128.559 117.822 44.621 1.00 24.48 ? 440 TYR A CE1 1 ATOM 3453 C CE2 . TYR A 1 440 ? 126.476 118.696 43.790 1.00 26.81 ? 440 TYR A CE2 1 ATOM 3454 C CZ . TYR A 1 440 ? 127.419 117.679 43.845 1.00 27.11 ? 440 TYR A CZ 1 ATOM 3455 O OH . TYR A 1 440 ? 127.224 116.528 43.111 1.00 25.84 ? 440 TYR A OH 1 ATOM 3456 N N . GLU A 1 441 ? 129.569 124.649 45.474 1.00 20.63 ? 441 GLU A N 1 ATOM 3457 C CA . GLU A 1 441 ? 129.365 126.107 45.469 1.00 20.10 ? 441 GLU A CA 1 ATOM 3458 C C . GLU A 1 441 ? 129.105 126.588 44.041 1.00 26.43 ? 441 GLU A C 1 ATOM 3459 O O . GLU A 1 441 ? 128.575 127.690 43.820 1.00 23.93 ? 441 GLU A O 1 ATOM 3460 C CB . GLU A 1 441 ? 130.586 126.834 46.051 1.00 18.12 ? 441 GLU A CB 1 ATOM 3461 C CG . GLU A 1 441 ? 131.708 127.165 45.054 1.00 21.72 ? 441 GLU A CG 1 ATOM 3462 C CD . GLU A 1 441 ? 132.442 125.930 44.517 1.00 26.35 ? 441 GLU A CD 1 ATOM 3463 O OE1 . GLU A 1 441 ? 132.209 124.799 45.015 1.00 28.34 ? 441 GLU A OE1 1 ATOM 3464 O OE2 . GLU A 1 441 ? 133.261 126.095 43.581 1.00 23.49 ? 441 GLU A OE2 1 ATOM 3465 N N . ILE A 1 442 ? 129.480 125.755 43.068 1.00 18.90 ? 442 ILE A N 1 ATOM 3466 C CA . ILE A 1 442 ? 129.496 126.179 41.664 1.00 22.15 ? 442 ILE A CA 1 ATOM 3467 C C . ILE A 1 442 ? 128.124 126.665 41.172 1.00 25.19 ? 442 ILE A C 1 ATOM 3468 O O . ILE A 1 442 ? 128.014 127.728 40.554 1.00 24.23 ? 442 ILE A O 1 ATOM 3469 C CB . ILE A 1 442 ? 130.025 125.063 40.731 1.00 18.84 ? 442 ILE A CB 1 ATOM 3470 C CG1 . ILE A 1 442 ? 131.499 124.761 41.016 1.00 23.28 ? 442 ILE A CG1 1 ATOM 3471 C CG2 . ILE A 1 442 ? 129.860 125.469 39.271 1.00 19.16 ? 442 ILE A CG2 1 ATOM 3472 C CD1 . ILE A 1 442 ? 132.030 123.508 40.297 1.00 19.54 ? 442 ILE A CD1 1 ATOM 3473 N N . GLU A 1 443 ? 127.080 125.890 41.453 1.00 22.47 ? 443 GLU A N 1 ATOM 3474 C CA . GLU A 1 443 ? 125.734 126.264 41.052 1.00 24.68 ? 443 GLU A CA 1 ATOM 3475 C C . GLU A 1 443 ? 125.264 127.589 41.677 1.00 22.51 ? 443 GLU A C 1 ATOM 3476 O O . GLU A 1 443 ? 124.385 128.263 41.132 1.00 31.53 ? 443 GLU A O 1 ATOM 3477 C CB . GLU A 1 443 ? 124.754 125.131 41.360 1.00 25.11 ? 443 GLU A CB 1 ATOM 3478 C CG . GLU A 1 443 ? 124.643 124.731 42.823 1.00 28.83 ? 443 GLU A CG 1 ATOM 3479 C CD . GLU A 1 443 ? 124.056 123.324 42.989 1.00 33.76 ? 443 GLU A CD 1 ATOM 3480 O OE1 . GLU A 1 443 ? 124.844 122.350 42.939 1.00 30.05 ? 443 GLU A OE1 1 ATOM 3481 O OE2 . GLU A 1 443 ? 122.815 123.195 43.151 1.00 36.76 ? 443 GLU A OE2 1 ATOM 3482 N N . PHE A 1 444 ? 125.837 127.964 42.817 1.00 21.85 ? 444 PHE A N 1 ATOM 3483 C CA . PHE A 1 444 ? 125.498 129.260 43.407 1.00 31.68 ? 444 PHE A CA 1 ATOM 3484 C C . PHE A 1 444 ? 126.163 130.427 42.666 1.00 25.98 ? 444 PHE A C 1 ATOM 3485 O O . PHE A 1 444 ? 125.536 131.467 42.422 1.00 26.28 ? 444 PHE A O 1 ATOM 3486 C CB . PHE A 1 444 ? 125.795 129.263 44.913 1.00 24.00 ? 444 PHE A CB 1 ATOM 3487 C CG . PHE A 1 444 ? 124.788 128.461 45.709 1.00 25.19 ? 444 PHE A CG 1 ATOM 3488 C CD1 . PHE A 1 444 ? 124.897 127.075 45.804 1.00 24.21 ? 444 PHE A CD1 1 ATOM 3489 C CD2 . PHE A 1 444 ? 123.708 129.085 46.315 1.00 32.27 ? 444 PHE A CD2 1 ATOM 3490 C CE1 . PHE A 1 444 ? 123.956 126.334 46.504 1.00 29.07 ? 444 PHE A CE1 1 ATOM 3491 C CE2 . PHE A 1 444 ? 122.758 128.346 47.021 1.00 29.90 ? 444 PHE A CE2 1 ATOM 3492 C CZ . PHE A 1 444 ? 122.883 126.975 47.118 1.00 28.30 ? 444 PHE A CZ 1 ATOM 3493 N N . VAL A 1 445 ? 127.418 130.225 42.286 1.00 23.87 ? 445 VAL A N 1 ATOM 3494 C CA . VAL A 1 445 ? 128.192 131.196 41.503 1.00 20.01 ? 445 VAL A CA 1 ATOM 3495 C C . VAL A 1 445 ? 127.545 131.486 40.149 1.00 24.21 ? 445 VAL A C 1 ATOM 3496 O O . VAL A 1 445 ? 127.464 132.646 39.733 1.00 24.02 ? 445 VAL A O 1 ATOM 3497 C CB . VAL A 1 445 ? 129.627 130.673 41.277 1.00 19.60 ? 445 VAL A CB 1 ATOM 3498 C CG1 . VAL A 1 445 ? 130.427 131.625 40.366 1.00 19.62 ? 445 VAL A CG1 1 ATOM 3499 C CG2 . VAL A 1 445 ? 130.329 130.500 42.621 1.00 20.81 ? 445 VAL A CG2 1 ATOM 3500 N N . PHE A 1 446 ? 127.065 130.436 39.473 1.00 21.23 ? 446 PHE A N 1 ATOM 3501 C CA . PHE A 1 446 ? 126.449 130.597 38.154 1.00 22.16 ? 446 PHE A CA 1 ATOM 3502 C C . PHE A 1 446 ? 124.973 130.991 38.283 1.00 23.64 ? 446 PHE A C 1 ATOM 3503 O O . PHE A 1 446 ? 124.274 131.181 37.276 1.00 26.44 ? 446 PHE A O 1 ATOM 3504 C CB . PHE A 1 446 ? 126.621 129.320 37.305 1.00 22.14 ? 446 PHE A CB 1 ATOM 3505 C CG . PHE A 1 446 ? 127.978 129.197 36.651 1.00 21.18 ? 446 PHE A CG 1 ATOM 3506 C CD1 . PHE A 1 446 ? 129.053 128.641 37.344 1.00 20.45 ? 446 PHE A CD1 1 ATOM 3507 C CD2 . PHE A 1 446 ? 128.181 129.642 35.344 1.00 21.60 ? 446 PHE A CD2 1 ATOM 3508 C CE1 . PHE A 1 446 ? 130.317 128.531 36.750 1.00 23.90 ? 446 PHE A CE1 1 ATOM 3509 C CE2 . PHE A 1 446 ? 129.437 129.536 34.739 1.00 27.62 ? 446 PHE A CE2 1 ATOM 3510 C CZ . PHE A 1 446 ? 130.511 128.980 35.442 1.00 25.39 ? 446 PHE A CZ 1 ATOM 3511 N N . GLY A 1 447 ? 124.492 131.123 39.519 1.00 25.77 ? 447 GLY A N 1 ATOM 3512 C CA . GLY A 1 447 ? 123.171 131.712 39.739 1.00 26.07 ? 447 GLY A CA 1 ATOM 3513 C C . GLY A 1 447 ? 121.988 130.813 39.426 1.00 26.73 ? 447 GLY A C 1 ATOM 3514 O O . GLY A 1 447 ? 120.889 131.301 39.122 1.00 28.31 ? 447 GLY A O 1 ATOM 3515 N N . LEU A 1 448 ? 122.196 129.498 39.497 1.00 26.52 ? 448 LEU A N 1 ATOM 3516 C CA . LEU A 1 448 ? 121.092 128.558 39.282 1.00 28.26 ? 448 LEU A CA 1 ATOM 3517 C C . LEU A 1 448 ? 119.892 128.773 40.225 1.00 31.75 ? 448 LEU A C 1 ATOM 3518 O O . LEU A 1 448 ? 118.738 128.733 39.778 1.00 32.64 ? 448 LEU A O 1 ATOM 3519 C CB . LEU A 1 448 ? 121.570 127.095 39.303 1.00 30.02 ? 448 LEU A CB 1 ATOM 3520 C CG . LEU A 1 448 ? 121.946 126.520 37.929 1.00 31.88 ? 448 LEU A CG 1 ATOM 3521 C CD1 . LEU A 1 448 ? 123.209 127.195 37.393 1.00 32.28 ? 448 LEU A CD1 1 ATOM 3522 C CD2 . LEU A 1 448 ? 122.133 124.998 37.972 1.00 32.59 ? 448 LEU A CD2 1 ATOM 3523 N N . PRO A 1 449 ? 120.152 129.014 41.527 1.00 32.99 ? 449 PRO A N 1 ATOM 3524 C CA . PRO A 1 449 ? 118.996 129.197 42.415 1.00 35.18 ? 449 PRO A CA 1 ATOM 3525 C C . PRO A 1 449 ? 118.193 130.488 42.172 1.00 35.33 ? 449 PRO A C 1 ATOM 3526 O O . PRO A 1 449 ? 117.149 130.649 42.803 1.00 37.69 ? 449 PRO A O 1 ATOM 3527 C CB . PRO A 1 449 ? 119.625 129.211 43.815 1.00 29.35 ? 449 PRO A CB 1 ATOM 3528 C CG . PRO A 1 449 ? 120.936 128.486 43.652 1.00 34.85 ? 449 PRO A CG 1 ATOM 3529 C CD . PRO A 1 449 ? 121.413 128.879 42.291 1.00 26.91 ? 449 PRO A CD 1 ATOM 3530 N N . LEU A 1 450 ? 118.649 131.379 41.294 1.00 31.09 ? 450 LEU A N 1 ATOM 3531 C CA . LEU A 1 450 ? 117.834 132.549 40.932 1.00 32.62 ? 450 LEU A CA 1 ATOM 3532 C C . LEU A 1 450 ? 116.575 132.128 40.181 1.00 34.58 ? 450 LEU A C 1 ATOM 3533 O O . LEU A 1 450 ? 115.568 132.843 40.194 1.00 38.70 ? 450 LEU A O 1 ATOM 3534 C CB . LEU A 1 450 ? 118.633 133.560 40.108 1.00 37.47 ? 450 LEU A CB 1 ATOM 3535 C CG . LEU A 1 450 ? 119.951 134.009 40.749 1.00 35.98 ? 450 LEU A CG 1 ATOM 3536 C CD1 . LEU A 1 450 ? 120.681 135.003 39.867 1.00 35.87 ? 450 LEU A CD1 1 ATOM 3537 C CD2 . LEU A 1 450 ? 119.687 134.609 42.126 1.00 38.55 ? 450 LEU A CD2 1 ATOM 3538 N N . GLU A 1 451 ? 116.627 130.969 39.527 1.00 42.93 ? 451 GLU A N 1 ATOM 3539 C CA . GLU A 1 451 ? 115.444 130.441 38.849 1.00 48.42 ? 451 GLU A CA 1 ATOM 3540 C C . GLU A 1 451 ? 114.494 129.823 39.877 1.00 49.50 ? 451 GLU A C 1 ATOM 3541 O O . GLU A 1 451 ? 114.744 128.734 40.408 1.00 44.24 ? 451 GLU A O 1 ATOM 3542 C CB . GLU A 1 451 ? 115.830 129.427 37.767 1.00 50.09 ? 451 GLU A CB 1 ATOM 3543 C CG . GLU A 1 451 ? 114.646 128.809 37.030 1.00 62.59 ? 451 GLU A CG 1 ATOM 3544 C CD . GLU A 1 451 ? 113.999 129.750 36.016 1.00 74.33 ? 451 GLU A CD 1 ATOM 3545 O OE1 . GLU A 1 451 ? 113.085 130.516 36.402 1.00 79.32 ? 451 GLU A OE1 1 ATOM 3546 O OE2 . GLU A 1 451 ? 114.394 129.710 34.827 1.00 75.05 ? 451 GLU A OE2 1 ATOM 3547 N N . ARG A 1 452 ? 113.407 130.538 40.153 1.00 56.89 ? 452 ARG A N 1 ATOM 3548 C CA . ARG A 1 452 ? 112.456 130.160 41.194 1.00 67.58 ? 452 ARG A CA 1 ATOM 3549 C C . ARG A 1 452 ? 111.725 128.858 40.878 1.00 70.22 ? 452 ARG A C 1 ATOM 3550 O O . ARG A 1 452 ? 111.090 128.271 41.754 1.00 68.83 ? 452 ARG A O 1 ATOM 3551 C CB . ARG A 1 452 ? 111.426 131.276 41.402 1.00 74.05 ? 452 ARG A CB 1 ATOM 3552 C CG . ARG A 1 452 ? 111.952 132.677 41.127 1.00 84.90 ? 452 ARG A CG 1 ATOM 3553 C CD . ARG A 1 452 ? 111.056 133.406 40.128 1.00 99.44 ? 452 ARG A CD 1 ATOM 3554 N NE . ARG A 1 452 ? 111.755 133.722 38.883 1.00 105.38 ? 452 ARG A NE 1 ATOM 3555 C CZ . ARG A 1 452 ? 112.057 134.955 38.485 1.00 107.63 ? 452 ARG A CZ 1 ATOM 3556 N NH1 . ARG A 1 452 ? 111.717 136.002 39.226 1.00 107.52 ? 452 ARG A NH1 1 ATOM 3557 N NH2 . ARG A 1 452 ? 112.694 135.143 37.338 1.00 107.53 ? 452 ARG A NH2 1 ATOM 3558 N N . ARG A 1 453 ? 111.809 128.409 39.630 1.00 70.82 ? 453 ARG A N 1 ATOM 3559 C CA . ARG A 1 453 ? 111.093 127.209 39.216 1.00 78.92 ? 453 ARG A CA 1 ATOM 3560 C C . ARG A 1 453 ? 111.859 125.925 39.529 1.00 79.16 ? 453 ARG A C 1 ATOM 3561 O O . ARG A 1 453 ? 111.386 124.833 39.218 1.00 81.36 ? 453 ARG A O 1 ATOM 3562 C CB . ARG A 1 453 ? 110.787 127.257 37.716 1.00 83.46 ? 453 ARG A CB 1 ATOM 3563 C CG . ARG A 1 453 ? 110.549 128.651 37.161 1.00 89.54 ? 453 ARG A CG 1 ATOM 3564 C CD . ARG A 1 453 ? 109.604 128.612 35.967 1.00 93.71 ? 453 ARG A CD 1 ATOM 3565 N NE . ARG A 1 453 ? 108.291 129.156 36.302 1.00 101.17 ? 453 ARG A NE 1 ATOM 3566 C CZ . ARG A 1 453 ? 107.166 128.867 35.653 1.00 107.70 ? 453 ARG A CZ 1 ATOM 3567 N NH1 . ARG A 1 453 ? 107.181 128.024 34.628 1.00 108.05 ? 453 ARG A NH1 1 ATOM 3568 N NH2 . ARG A 1 453 ? 106.020 129.418 36.035 1.00 112.04 ? 453 ARG A NH2 1 ATOM 3569 N N . ASP A 1 454 ? 113.030 126.045 40.148 1.00 76.16 ? 454 ASP A N 1 ATOM 3570 C CA . ASP A 1 454 ? 113.937 124.900 40.245 1.00 80.97 ? 454 ASP A CA 1 ATOM 3571 C C . ASP A 1 454 ? 114.217 124.329 41.641 1.00 75.68 ? 454 ASP A C 1 ATOM 3572 O O . ASP A 1 454 ? 115.301 123.791 41.873 1.00 77.40 ? 454 ASP A O 1 ATOM 3573 C CB . ASP A 1 454 ? 115.259 125.197 39.524 1.00 88.78 ? 454 ASP A CB 1 ATOM 3574 C CG . ASP A 1 454 ? 115.235 124.768 38.069 1.00 100.80 ? 454 ASP A CG 1 ATOM 3575 O OD1 . ASP A 1 454 ? 115.398 123.556 37.805 1.00 104.78 ? 454 ASP A OD1 1 ATOM 3576 O OD2 . ASP A 1 454 ? 115.051 125.638 37.190 1.00 104.98 ? 454 ASP A OD2 1 ATOM 3577 N N . GLN A 1 455 ? 113.248 124.449 42.548 1.00 71.81 ? 455 GLN A N 1 ATOM 3578 C CA . GLN A 1 455 ? 113.267 123.753 43.849 1.00 71.14 ? 455 GLN A CA 1 ATOM 3579 C C . GLN A 1 455 ? 114.145 124.332 44.978 1.00 63.67 ? 455 GLN A C 1 ATOM 3580 O O . GLN A 1 455 ? 114.050 123.876 46.118 1.00 66.61 ? 455 GLN A O 1 ATOM 3581 C CB . GLN A 1 455 ? 113.563 122.250 43.682 1.00 73.91 ? 455 GLN A CB 1 ATOM 3582 C CG . GLN A 1 455 ? 112.333 121.360 43.670 1.00 78.07 ? 455 GLN A CG 1 ATOM 3583 C CD . GLN A 1 455 ? 111.515 121.516 42.407 1.00 81.57 ? 455 GLN A CD 1 ATOM 3584 O OE1 . GLN A 1 455 ? 112.061 121.544 41.302 1.00 85.13 ? 455 GLN A OE1 1 ATOM 3585 N NE2 . GLN A 1 455 ? 110.200 121.627 42.561 1.00 77.16 ? 455 GLN A NE2 1 ATOM 3586 N N . TYR A 1 456 ? 114.994 125.313 44.689 1.00 49.79 ? 456 TYR A N 1 ATOM 3587 C CA . TYR A 1 456 ? 115.782 125.925 45.756 1.00 44.50 ? 456 TYR A CA 1 ATOM 3588 C C . TYR A 1 456 ? 114.896 126.743 46.699 1.00 42.44 ? 456 TYR A C 1 ATOM 3589 O O . TYR A 1 456 ? 113.821 127.201 46.317 1.00 43.43 ? 456 TYR A O 1 ATOM 3590 C CB . TYR A 1 456 ? 116.889 126.815 45.193 1.00 33.94 ? 456 TYR A CB 1 ATOM 3591 C CG . TYR A 1 456 ? 117.935 126.105 44.357 1.00 33.18 ? 456 TYR A CG 1 ATOM 3592 C CD1 . TYR A 1 456 ? 119.073 125.570 44.948 1.00 35.14 ? 456 TYR A CD1 1 ATOM 3593 C CD2 . TYR A 1 456 ? 117.796 125.995 42.972 1.00 32.12 ? 456 TYR A CD2 1 ATOM 3594 C CE1 . TYR A 1 456 ? 120.046 124.940 44.193 1.00 40.74 ? 456 TYR A CE1 1 ATOM 3595 C CE2 . TYR A 1 456 ? 118.768 125.367 42.204 1.00 36.99 ? 456 TYR A CE2 1 ATOM 3596 C CZ . TYR A 1 456 ? 119.892 124.841 42.824 1.00 42.41 ? 456 TYR A CZ 1 ATOM 3597 O OH . TYR A 1 456 ? 120.872 124.217 42.084 1.00 41.34 ? 456 TYR A OH 1 ATOM 3598 N N . THR A 1 457 ? 115.352 126.924 47.935 1.00 40.31 ? 457 THR A N 1 ATOM 3599 C CA . THR A 1 457 ? 114.623 127.729 48.917 1.00 39.48 ? 457 THR A CA 1 ATOM 3600 C C . THR A 1 457 ? 114.822 129.220 48.661 1.00 40.88 ? 457 THR A C 1 ATOM 3601 O O . THR A 1 457 ? 115.688 129.623 47.874 1.00 36.18 ? 457 THR A O 1 ATOM 3602 C CB . THR A 1 457 ? 115.133 127.468 50.341 1.00 38.57 ? 457 THR A CB 1 ATOM 3603 O OG1 . THR A 1 457 ? 116.493 127.917 50.444 1.00 35.73 ? 457 THR A OG1 1 ATOM 3604 C CG2 . THR A 1 457 ? 115.059 125.987 50.680 1.00 38.58 ? 457 THR A CG2 1 ATOM 3605 N N . LYS A 1 458 ? 114.029 130.033 49.354 1.00 39.62 ? 458 LYS A N 1 ATOM 3606 C CA . LYS A 1 458 ? 114.150 131.486 49.292 1.00 42.66 ? 458 LYS A CA 1 ATOM 3607 C C . LYS A 1 458 ? 115.518 131.947 49.793 1.00 37.47 ? 458 LYS A C 1 ATOM 3608 O O . LYS A 1 458 ? 116.172 132.802 49.185 1.00 38.13 ? 458 LYS A O 1 ATOM 3609 C CB . LYS A 1 458 ? 113.041 132.139 50.133 1.00 49.56 ? 458 LYS A CB 1 ATOM 3610 C CG . LYS A 1 458 ? 113.011 133.645 50.005 1.00 53.17 ? 458 LYS A CG 1 ATOM 3611 C CD . LYS A 1 458 ? 112.674 134.036 48.572 1.00 64.22 ? 458 LYS A CD 1 ATOM 3612 C CE . LYS A 1 458 ? 112.917 135.514 48.311 1.00 68.25 ? 458 LYS A CE 1 ATOM 3613 N NZ . LYS A 1 458 ? 112.354 135.920 46.989 1.00 71.29 ? 458 LYS A NZ 1 ATOM 3614 N N . ALA A 1 459 ? 115.955 131.368 50.903 1.00 37.25 ? 459 ALA A N 1 ATOM 3615 C CA . ALA A 1 459 ? 117.241 131.706 51.476 1.00 35.28 ? 459 ALA A CA 1 ATOM 3616 C C . ALA A 1 459 ? 118.363 131.450 50.469 1.00 36.03 ? 459 ALA A C 1 ATOM 3617 O O . ALA A 1 459 ? 119.349 132.191 50.428 1.00 32.99 ? 459 ALA A O 1 ATOM 3618 C CB . ALA A 1 459 ? 117.465 130.924 52.766 1.00 35.45 ? 459 ALA A CB 1 ATOM 3619 N N . GLU A 1 460 ? 118.207 130.417 49.643 1.00 35.78 ? 460 GLU A N 1 ATOM 3620 C CA . GLU A 1 460 ? 119.252 130.065 48.676 1.00 36.18 ? 460 GLU A CA 1 ATOM 3621 C C . GLU A 1 460 ? 119.245 131.000 47.465 1.00 35.01 ? 460 GLU A C 1 ATOM 3622 O O . GLU A 1 460 ? 120.297 131.305 46.894 1.00 35.80 ? 460 GLU A O 1 ATOM 3623 C CB . GLU A 1 460 ? 119.117 128.604 48.240 1.00 37.47 ? 460 GLU A CB 1 ATOM 3624 C CG . GLU A 1 460 ? 119.534 127.618 49.319 1.00 36.05 ? 460 GLU A CG 1 ATOM 3625 C CD . GLU A 1 460 ? 119.213 126.180 48.958 1.00 37.98 ? 460 GLU A CD 1 ATOM 3626 O OE1 . GLU A 1 460 ? 118.118 125.929 48.409 1.00 39.08 ? 460 GLU A OE1 1 ATOM 3627 O OE2 . GLU A 1 460 ? 120.057 125.301 49.235 1.00 34.43 ? 460 GLU A OE2 1 ATOM 3628 N N . GLU A 1 461 ? 118.058 131.439 47.067 1.00 33.66 ? 461 GLU A N 1 ATOM 3629 C CA . GLU A 1 461 ? 117.950 132.486 46.063 1.00 32.58 ? 461 GLU A CA 1 ATOM 3630 C C . GLU A 1 461 ? 118.742 133.703 46.537 1.00 41.08 ? 461 GLU A C 1 ATOM 3631 O O . GLU A 1 461 ? 119.570 134.248 45.799 1.00 36.98 ? 461 GLU A O 1 ATOM 3632 C CB . GLU A 1 461 ? 116.487 132.864 45.847 1.00 34.97 ? 461 GLU A CB 1 ATOM 3633 C CG . GLU A 1 461 ? 116.298 134.035 44.911 1.00 51.10 ? 461 GLU A CG 1 ATOM 3634 C CD . GLU A 1 461 ? 114.832 134.392 44.695 1.00 57.34 ? 461 GLU A CD 1 ATOM 3635 O OE1 . GLU A 1 461 ? 113.944 133.627 45.133 1.00 63.29 ? 461 GLU A OE1 1 ATOM 3636 O OE2 . GLU A 1 461 ? 114.572 135.441 44.075 1.00 52.36 ? 461 GLU A OE2 1 ATOM 3637 N N . ILE A 1 462 ? 118.504 134.103 47.786 1.00 41.45 ? 462 ILE A N 1 ATOM 3638 C CA . ILE A 1 462 ? 119.177 135.263 48.371 1.00 41.07 ? 462 ILE A CA 1 ATOM 3639 C C . ILE A 1 462 ? 120.706 135.098 48.411 1.00 39.65 ? 462 ILE A C 1 ATOM 3640 O O . ILE A 1 462 ? 121.443 136.023 48.065 1.00 36.10 ? 462 ILE A O 1 ATOM 3641 C CB . ILE A 1 462 ? 118.658 135.560 49.799 1.00 43.43 ? 462 ILE A CB 1 ATOM 3642 C CG1 . ILE A 1 462 ? 117.145 135.799 49.794 1.00 50.34 ? 462 ILE A CG1 1 ATOM 3643 C CG2 . ILE A 1 462 ? 119.381 136.760 50.393 1.00 41.22 ? 462 ILE A CG2 1 ATOM 3644 C CD1 . ILE A 1 462 ? 116.700 136.846 48.808 1.00 57.48 ? 462 ILE A CD1 1 ATOM 3645 N N . LEU A 1 463 ? 121.176 133.926 48.837 1.00 29.00 ? 463 LEU A N 1 ATOM 3646 C CA . LEU A 1 463 ? 122.612 133.661 48.922 1.00 32.73 ? 463 LEU A CA 1 ATOM 3647 C C . LEU A 1 463 ? 123.285 133.747 47.549 1.00 30.47 ? 463 LEU A C 1 ATOM 3648 O O . LEU A 1 463 ? 124.326 134.386 47.403 1.00 29.53 ? 463 LEU A O 1 ATOM 3649 C CB . LEU A 1 463 ? 122.880 132.293 49.573 1.00 26.61 ? 463 LEU A CB 1 ATOM 3650 C CG . LEU A 1 463 ? 124.343 131.836 49.641 1.00 29.93 ? 463 LEU A CG 1 ATOM 3651 C CD1 . LEU A 1 463 ? 125.230 132.863 50.360 1.00 24.32 ? 463 LEU A CD1 1 ATOM 3652 C CD2 . LEU A 1 463 ? 124.443 130.478 50.324 1.00 30.48 ? 463 LEU A CD2 1 ATOM 3653 N N . SER A 1 464 ? 122.677 133.116 46.547 1.00 26.27 ? 464 SER A N 1 ATOM 3654 C CA . SER A 1 464 ? 123.222 133.114 45.186 1.00 27.26 ? 464 SER A CA 1 ATOM 3655 C C . SER A 1 464 ? 123.237 134.522 44.586 1.00 27.15 ? 464 SER A C 1 ATOM 3656 O O . SER A 1 464 ? 124.206 134.912 43.934 1.00 28.26 ? 464 SER A O 1 ATOM 3657 C CB . SER A 1 464 ? 122.399 132.181 44.282 1.00 33.11 ? 464 SER A CB 1 ATOM 3658 O OG . SER A 1 464 ? 122.885 132.196 42.949 1.00 25.51 ? 464 SER A OG 1 ATOM 3659 N N . ARG A 1 465 ? 122.156 135.271 44.796 1.00 27.44 ? 465 ARG A N 1 ATOM 3660 C CA . ARG A 1 465 ? 122.069 136.629 44.272 1.00 33.26 ? 465 ARG A CA 1 ATOM 3661 C C . ARG A 1 465 ? 123.255 137.472 44.756 1.00 33.90 ? 465 ARG A C 1 ATOM 3662 O O . ARG A 1 465 ? 123.877 138.200 43.975 1.00 34.78 ? 465 ARG A O 1 ATOM 3663 C CB . ARG A 1 465 ? 120.739 137.295 44.670 1.00 30.24 ? 465 ARG A CB 1 ATOM 3664 C CG . ARG A 1 465 ? 120.578 138.706 44.114 1.00 31.71 ? 465 ARG A CG 1 ATOM 3665 C CD . ARG A 1 465 ? 120.374 138.667 42.591 1.00 37.51 ? 465 ARG A CD 1 ATOM 3666 N NE . ARG A 1 465 ? 120.619 139.960 41.943 1.00 44.56 ? 465 ARG A NE 1 ATOM 3667 C CZ . ARG A 1 465 ? 121.820 140.406 41.566 1.00 45.96 ? 465 ARG A CZ 1 ATOM 3668 N NH1 . ARG A 1 465 ? 122.921 139.675 41.773 1.00 28.94 ? 465 ARG A NH1 1 ATOM 3669 N NH2 . ARG A 1 465 ? 121.924 141.591 40.977 1.00 44.30 ? 465 ARG A NH2 1 ATOM 3670 N N A SER A 1 466 ? 123.562 137.356 46.045 0.66 31.01 ? 466 SER A N 1 ATOM 3671 N N B SER A 1 466 ? 123.589 137.367 46.035 0.34 31.33 ? 466 SER A N 1 ATOM 3672 C CA A SER A 1 466 ? 124.657 138.110 46.649 0.66 30.38 ? 466 SER A CA 1 ATOM 3673 C CA B SER A 1 466 ? 124.682 138.174 46.564 0.34 30.50 ? 466 SER A CA 1 ATOM 3674 C C A SER A 1 466 ? 126.029 137.627 46.155 0.66 29.58 ? 466 SER A C 1 ATOM 3675 C C B SER A 1 466 ? 126.053 137.634 46.143 0.34 28.65 ? 466 SER A C 1 ATOM 3676 O O A SER A 1 466 ? 126.931 138.430 45.886 0.66 25.47 ? 466 SER A O 1 ATOM 3677 O O B SER A 1 466 ? 126.984 138.411 45.916 0.34 26.31 ? 466 SER A O 1 ATOM 3678 C CB A SER A 1 466 ? 124.566 138.028 48.174 0.66 26.43 ? 466 SER A CB 1 ATOM 3679 C CB B SER A 1 466 ? 124.583 138.304 48.082 0.34 31.08 ? 466 SER A CB 1 ATOM 3680 O OG A SER A 1 466 ? 125.775 138.452 48.781 0.66 27.97 ? 466 SER A OG 1 ATOM 3681 O OG B SER A 1 466 ? 124.671 137.040 48.704 0.34 32.98 ? 466 SER A OG 1 ATOM 3682 N N . ILE A 1 467 ? 126.176 136.312 46.034 1.00 24.64 ? 467 ILE A N 1 ATOM 3683 C CA . ILE A 1 467 ? 127.418 135.711 45.539 1.00 25.26 ? 467 ILE A CA 1 ATOM 3684 C C . ILE A 1 467 ? 127.688 136.169 44.097 1.00 21.83 ? 467 ILE A C 1 ATOM 3685 O O . ILE A 1 467 ? 128.804 136.600 43.762 1.00 22.81 ? 467 ILE A O 1 ATOM 3686 C CB . ILE A 1 467 ? 127.387 134.157 45.644 1.00 30.07 ? 467 ILE A CB 1 ATOM 3687 C CG1 . ILE A 1 467 ? 127.572 133.725 47.107 1.00 30.75 ? 467 ILE A CG1 1 ATOM 3688 C CG2 . ILE A 1 467 ? 128.464 133.521 44.770 1.00 21.29 ? 467 ILE A CG2 1 ATOM 3689 C CD1 . ILE A 1 467 ? 127.664 132.198 47.325 1.00 20.89 ? 467 ILE A CD1 1 ATOM 3690 N N . VAL A 1 468 ? 126.648 136.108 43.268 1.00 22.77 ? 468 VAL A N 1 ATOM 3691 C CA . VAL A 1 468 ? 126.715 136.575 41.889 1.00 31.02 ? 468 VAL A CA 1 ATOM 3692 C C . VAL A 1 468 ? 127.152 138.038 41.832 1.00 30.61 ? 468 VAL A C 1 ATOM 3693 O O . VAL A 1 468 ? 128.061 138.390 41.070 1.00 26.24 ? 468 VAL A O 1 ATOM 3694 C CB . VAL A 1 468 ? 125.354 136.371 41.173 1.00 24.37 ? 468 VAL A CB 1 ATOM 3695 C CG1 . VAL A 1 468 ? 125.241 137.240 39.949 1.00 26.25 ? 468 VAL A CG1 1 ATOM 3696 C CG2 . VAL A 1 468 ? 125.155 134.881 40.817 1.00 23.98 ? 468 VAL A CG2 1 ATOM 3697 N N . LYS A 1 469 ? 126.528 138.886 42.651 1.00 24.41 ? 469 LYS A N 1 ATOM 3698 C CA . LYS A 1 469 ? 126.922 140.304 42.721 1.00 25.05 ? 469 LYS A CA 1 ATOM 3699 C C . LYS A 1 469 ? 128.398 140.488 43.146 1.00 26.73 ? 469 LYS A C 1 ATOM 3700 O O . LYS A 1 469 ? 129.140 141.256 42.521 1.00 27.35 ? 469 LYS A O 1 ATOM 3701 C CB . LYS A 1 469 ? 125.999 141.081 43.662 1.00 26.39 ? 469 LYS A CB 1 ATOM 3702 C CG . LYS A 1 469 ? 126.421 142.540 43.899 1.00 27.12 ? 469 LYS A CG 1 ATOM 3703 C CD . LYS A 1 469 ? 126.466 143.343 42.593 1.00 29.52 ? 469 LYS A CD 1 ATOM 3704 C CE . LYS A 1 469 ? 125.058 143.634 42.054 1.00 30.11 ? 469 LYS A CE 1 ATOM 3705 N NZ . LYS A 1 469 ? 125.091 144.388 40.763 1.00 30.47 ? 469 LYS A NZ 1 ATOM 3706 N N . ARG A 1 470 ? 128.824 139.781 44.191 1.00 23.97 ? 470 ARG A N 1 ATOM 3707 C CA . ARG A 1 470 ? 130.215 139.875 44.668 1.00 29.51 ? 470 ARG A CA 1 ATOM 3708 C C . ARG A 1 470 ? 131.249 139.463 43.598 1.00 29.81 ? 470 ARG A C 1 ATOM 3709 O O . ARG A 1 470 ? 132.274 140.133 43.409 1.00 22.15 ? 470 ARG A O 1 ATOM 3710 C CB . ARG A 1 470 ? 130.425 139.042 45.945 1.00 28.23 ? 470 ARG A CB 1 ATOM 3711 C CG . ARG A 1 470 ? 129.752 139.590 47.226 1.00 30.29 ? 470 ARG A CG 1 ATOM 3712 C CD . ARG A 1 470 ? 130.184 138.742 48.440 1.00 28.01 ? 470 ARG A CD 1 ATOM 3713 N NE . ARG A 1 470 ? 129.490 139.073 49.684 1.00 24.99 ? 470 ARG A NE 1 ATOM 3714 C CZ . ARG A 1 470 ? 129.826 140.074 50.498 1.00 30.16 ? 470 ARG A CZ 1 ATOM 3715 N NH1 . ARG A 1 470 ? 130.853 140.870 50.207 1.00 27.59 ? 470 ARG A NH1 1 ATOM 3716 N NH2 . ARG A 1 470 ? 129.128 140.293 51.606 1.00 26.56 ? 470 ARG A NH2 1 ATOM 3717 N N . TRP A 1 471 ? 130.981 138.359 42.907 1.00 24.69 ? 471 TRP A N 1 ATOM 3718 C CA . TRP A 1 471 ? 131.868 137.880 41.846 1.00 27.69 ? 471 TRP A CA 1 ATOM 3719 C C . TRP A 1 471 ? 131.934 138.892 40.696 1.00 22.39 ? 471 TRP A C 1 ATOM 3720 O O . TRP A 1 471 ? 133.019 139.181 40.174 1.00 23.62 ? 471 TRP A O 1 ATOM 3721 C CB . TRP A 1 471 ? 131.371 136.526 41.325 1.00 19.38 ? 471 TRP A CB 1 ATOM 3722 C CG . TRP A 1 471 ? 132.061 135.247 41.888 1.00 18.33 ? 471 TRP A CG 1 ATOM 3723 C CD1 . TRP A 1 471 ? 132.587 134.218 41.147 1.00 19.08 ? 471 TRP A CD1 1 ATOM 3724 C CD2 . TRP A 1 471 ? 132.235 134.866 43.271 1.00 23.04 ? 471 TRP A CD2 1 ATOM 3725 N NE1 . TRP A 1 471 ? 133.088 133.231 41.977 1.00 18.58 ? 471 TRP A NE1 1 ATOM 3726 C CE2 . TRP A 1 471 ? 132.887 133.604 43.280 1.00 22.78 ? 471 TRP A CE2 1 ATOM 3727 C CE3 . TRP A 1 471 ? 131.918 135.472 44.499 1.00 18.93 ? 471 TRP A CE3 1 ATOM 3728 C CZ2 . TRP A 1 471 ? 133.216 132.936 44.472 1.00 16.81 ? 471 TRP A CZ2 1 ATOM 3729 C CZ3 . TRP A 1 471 ? 132.241 134.809 45.680 1.00 18.75 ? 471 TRP A CZ3 1 ATOM 3730 C CH2 . TRP A 1 471 ? 132.895 133.558 45.657 1.00 18.14 ? 471 TRP A CH2 1 ATOM 3731 N N . ALA A 1 472 ? 130.768 139.411 40.298 1.00 22.68 ? 472 ALA A N 1 ATOM 3732 C CA . ALA A 1 472 ? 130.669 140.441 39.262 1.00 25.61 ? 472 ALA A CA 1 ATOM 3733 C C . ALA A 1 472 ? 131.423 141.730 39.628 1.00 28.21 ? 472 ALA A C 1 ATOM 3734 O O . ALA A 1 472 ? 132.136 142.303 38.794 1.00 28.29 ? 472 ALA A O 1 ATOM 3735 C CB . ALA A 1 472 ? 129.202 140.761 38.971 1.00 24.19 ? 472 ALA A CB 1 ATOM 3736 N N . ASN A 1 473 ? 131.237 142.208 40.856 1.00 26.22 ? 473 ASN A N 1 ATOM 3737 C CA . ASN A 1 473 ? 131.998 143.368 41.326 1.00 28.58 ? 473 ASN A CA 1 ATOM 3738 C C . ASN A 1 473 ? 133.512 143.107 41.394 1.00 31.62 ? 473 ASN A C 1 ATOM 3739 O O . ASN A 1 473 ? 134.312 144.001 41.088 1.00 22.98 ? 473 ASN A O 1 ATOM 3740 C CB . ASN A 1 473 ? 131.479 143.877 42.676 1.00 30.76 ? 473 ASN A CB 1 ATOM 3741 C CG . ASN A 1 473 ? 130.198 144.712 42.546 1.00 33.50 ? 473 ASN A CG 1 ATOM 3742 O OD1 . ASN A 1 473 ? 129.759 145.046 41.442 1.00 28.06 ? 473 ASN A OD1 1 ATOM 3743 N ND2 . ASN A 1 473 ? 129.609 145.067 43.686 1.00 26.58 ? 473 ASN A ND2 1 ATOM 3744 N N . PHE A 1 474 ? 133.919 141.899 41.789 1.00 22.61 ? 474 PHE A N 1 ATOM 3745 C CA . PHE A 1 474 ? 135.346 141.562 41.718 1.00 21.33 ? 474 PHE A CA 1 ATOM 3746 C C . PHE A 1 474 ? 135.868 141.679 40.283 1.00 28.37 ? 474 PHE A C 1 ATOM 3747 O O . PHE A 1 474 ? 136.874 142.333 40.038 1.00 25.83 ? 474 PHE A O 1 ATOM 3748 C CB . PHE A 1 474 ? 135.667 140.155 42.247 1.00 22.38 ? 474 PHE A CB 1 ATOM 3749 C CG . PHE A 1 474 ? 137.150 139.846 42.248 1.00 20.95 ? 474 PHE A CG 1 ATOM 3750 C CD1 . PHE A 1 474 ? 138.002 140.462 43.170 1.00 18.61 ? 474 PHE A CD1 1 ATOM 3751 C CD2 . PHE A 1 474 ? 137.696 138.987 41.318 1.00 18.00 ? 474 PHE A CD2 1 ATOM 3752 C CE1 . PHE A 1 474 ? 139.380 140.201 43.171 1.00 18.83 ? 474 PHE A CE1 1 ATOM 3753 C CE2 . PHE A 1 474 ? 139.080 138.710 41.308 1.00 19.02 ? 474 PHE A CE2 1 ATOM 3754 C CZ . PHE A 1 474 ? 139.923 139.321 42.236 1.00 17.71 ? 474 PHE A CZ 1 ATOM 3755 N N . ALA A 1 475 ? 135.185 141.046 39.335 1.00 20.63 ? 475 ALA A N 1 ATOM 3756 C CA . ALA A 1 475 ? 135.639 141.097 37.946 1.00 22.17 ? 475 ALA A CA 1 ATOM 3757 C C . ALA A 1 475 ? 135.701 142.538 37.409 1.00 25.60 ? 475 ALA A C 1 ATOM 3758 O O . ALA A 1 475 ? 136.712 142.959 36.818 1.00 23.46 ? 475 ALA A O 1 ATOM 3759 C CB . ALA A 1 475 ? 134.772 140.243 37.081 1.00 21.02 ? 475 ALA A CB 1 ATOM 3760 N N . LYS A 1 476 ? 134.630 143.294 37.631 1.00 24.38 ? 476 LYS A N 1 ATOM 3761 C CA . LYS A 1 476 ? 134.547 144.666 37.128 1.00 28.42 ? 476 LYS A CA 1 ATOM 3762 C C . LYS A 1 476 ? 135.492 145.628 37.832 1.00 30.74 ? 476 LYS A C 1 ATOM 3763 O O . LYS A 1 476 ? 136.136 146.450 37.180 1.00 27.98 ? 476 LYS A O 1 ATOM 3764 C CB . LYS A 1 476 ? 133.122 145.216 37.272 1.00 28.90 ? 476 LYS A CB 1 ATOM 3765 C CG . LYS A 1 476 ? 132.074 144.515 36.412 1.00 30.28 ? 476 LYS A CG 1 ATOM 3766 C CD . LYS A 1 476 ? 130.678 145.128 36.634 1.00 29.99 ? 476 LYS A CD 1 ATOM 3767 C CE . LYS A 1 476 ? 129.658 144.466 35.699 1.00 35.80 ? 476 LYS A CE 1 ATOM 3768 N NZ . LYS A 1 476 ? 128.251 144.531 36.213 1.00 41.65 ? 476 LYS A NZ 1 ATOM 3769 N N . TYR A 1 477 ? 135.549 145.543 39.161 1.00 25.98 ? 477 TYR A N 1 ATOM 3770 C CA . TYR A 1 477 ? 136.144 146.609 39.970 1.00 31.93 ? 477 TYR A CA 1 ATOM 3771 C C . TYR A 1 477 ? 137.268 146.128 40.893 1.00 30.82 ? 477 TYR A C 1 ATOM 3772 O O . TYR A 1 477 ? 137.910 146.943 41.556 1.00 28.65 ? 477 TYR A O 1 ATOM 3773 C CB . TYR A 1 477 ? 135.056 147.316 40.796 1.00 28.21 ? 477 TYR A CB 1 ATOM 3774 C CG . TYR A 1 477 ? 133.833 147.701 39.988 1.00 31.01 ? 477 TYR A CG 1 ATOM 3775 C CD1 . TYR A 1 477 ? 133.951 148.461 38.830 1.00 28.45 ? 477 TYR A CD1 1 ATOM 3776 C CD2 . TYR A 1 477 ? 132.559 147.287 40.375 1.00 28.85 ? 477 TYR A CD2 1 ATOM 3777 C CE1 . TYR A 1 477 ? 132.824 148.812 38.082 1.00 30.79 ? 477 TYR A CE1 1 ATOM 3778 C CE2 . TYR A 1 477 ? 131.437 147.624 39.639 1.00 28.65 ? 477 TYR A CE2 1 ATOM 3779 C CZ . TYR A 1 477 ? 131.574 148.384 38.490 1.00 32.14 ? 477 TYR A CZ 1 ATOM 3780 O OH . TYR A 1 477 ? 130.459 148.732 37.744 1.00 32.87 ? 477 TYR A OH 1 ATOM 3781 N N . GLY A 1 478 ? 137.502 144.817 40.929 1.00 29.87 ? 478 GLY A N 1 ATOM 3782 C CA . GLY A 1 478 ? 138.566 144.251 41.740 1.00 28.22 ? 478 GLY A CA 1 ATOM 3783 C C . GLY A 1 478 ? 138.283 144.199 43.235 1.00 28.66 ? 478 GLY A C 1 ATOM 3784 O O . GLY A 1 478 ? 139.216 144.093 44.043 1.00 26.53 ? 478 GLY A O 1 ATOM 3785 N N . ASN A 1 479 ? 137.006 144.249 43.613 1.00 22.59 ? 479 ASN A N 1 ATOM 3786 C CA . ASN A 1 479 ? 136.628 144.351 45.023 1.00 21.99 ? 479 ASN A CA 1 ATOM 3787 C C . ASN A 1 479 ? 135.260 143.697 45.263 1.00 21.91 ? 479 ASN A C 1 ATOM 3788 O O . ASN A 1 479 ? 134.235 144.254 44.865 1.00 24.55 ? 479 ASN A O 1 ATOM 3789 C CB . ASN A 1 479 ? 136.581 145.828 45.409 1.00 23.42 ? 479 ASN A CB 1 ATOM 3790 C CG . ASN A 1 479 ? 136.679 146.047 46.905 1.00 33.95 ? 479 ASN A CG 1 ATOM 3791 O OD1 . ASN A 1 479 ? 136.613 145.103 47.689 1.00 37.12 ? 479 ASN A OD1 1 ATOM 3792 N ND2 . ASN A 1 479 ? 136.828 147.301 47.307 1.00 38.62 ? 479 ASN A ND2 1 ATOM 3793 N N . PRO A 1 480 ? 135.234 142.521 45.924 1.00 20.96 ? 480 PRO A N 1 ATOM 3794 C CA . PRO A 1 480 ? 134.027 141.676 45.926 1.00 20.84 ? 480 PRO A CA 1 ATOM 3795 C C . PRO A 1 480 ? 133.023 142.072 46.999 1.00 25.20 ? 480 PRO A C 1 ATOM 3796 O O . PRO A 1 480 ? 132.585 141.225 47.794 1.00 25.80 ? 480 PRO A O 1 ATOM 3797 C CB . PRO A 1 480 ? 134.583 140.262 46.210 1.00 19.59 ? 480 PRO A CB 1 ATOM 3798 C CG . PRO A 1 480 ? 135.791 140.516 47.094 1.00 19.36 ? 480 PRO A CG 1 ATOM 3799 C CD . PRO A 1 480 ? 136.353 141.899 46.669 1.00 21.26 ? 480 PRO A CD 1 ATOM 3800 N N . GLN A 1 481 ? 132.649 143.344 47.014 1.00 29.99 ? 481 GLN A N 1 ATOM 3801 C CA . GLN A 1 481 ? 131.666 143.827 47.972 1.00 27.54 ? 481 GLN A CA 1 ATOM 3802 C C . GLN A 1 481 ? 130.242 143.684 47.419 1.00 31.19 ? 481 GLN A C 1 ATOM 3803 O O . GLN A 1 481 ? 130.037 143.558 46.202 1.00 28.13 ? 481 GLN A O 1 ATOM 3804 C CB . GLN A 1 481 ? 131.941 145.298 48.334 1.00 25.49 ? 481 GLN A CB 1 ATOM 3805 C CG . GLN A 1 481 ? 133.395 145.599 48.772 1.00 27.32 ? 481 GLN A CG 1 ATOM 3806 C CD . GLN A 1 481 ? 133.869 144.730 49.934 1.00 25.31 ? 481 GLN A CD 1 ATOM 3807 O OE1 . GLN A 1 481 ? 133.076 144.332 50.792 1.00 28.96 ? 481 GLN A OE1 1 ATOM 3808 N NE2 . GLN A 1 481 ? 135.167 144.428 49.963 1.00 23.30 ? 481 GLN A NE2 1 ATOM 3809 N N . GLU A 1 482 ? 129.260 143.675 48.314 1.00 31.05 ? 482 GLU A N 1 ATOM 3810 C CA . GLU A 1 482 ? 127.871 143.886 47.911 1.00 32.92 ? 482 GLU A CA 1 ATOM 3811 C C . GLU A 1 482 ? 127.513 145.162 48.633 1.00 33.51 ? 482 GLU A C 1 ATOM 3812 O O . GLU A 1 482 ? 127.347 145.153 49.846 1.00 40.04 ? 482 GLU A O 1 ATOM 3813 C CB . GLU A 1 482 ? 126.963 142.718 48.331 1.00 28.71 ? 482 GLU A CB 1 ATOM 3814 C CG . GLU A 1 482 ? 125.518 142.794 47.776 1.00 34.33 ? 482 GLU A CG 1 ATOM 3815 C CD . GLU A 1 482 ? 124.724 143.922 48.385 1.00 40.51 ? 482 GLU A CD 1 ATOM 3816 O OE1 . GLU A 1 482 ? 124.599 143.954 49.629 1.00 47.77 ? 482 GLU A OE1 1 ATOM 3817 O OE2 . GLU A 1 482 ? 124.242 144.799 47.631 1.00 48.47 ? 482 GLU A OE2 1 ATOM 3818 N N . THR A 1 483 ? 127.429 146.264 47.893 1.00 33.34 ? 483 THR A N 1 ATOM 3819 C CA . THR A 1 483 ? 127.443 147.593 48.509 1.00 38.52 ? 483 THR A CA 1 ATOM 3820 C C . THR A 1 483 ? 126.063 148.124 48.889 1.00 39.32 ? 483 THR A C 1 ATOM 3821 O O . THR A 1 483 ? 125.956 149.136 49.591 1.00 38.12 ? 483 THR A O 1 ATOM 3822 C CB . THR A 1 483 ? 128.113 148.638 47.576 1.00 36.81 ? 483 THR A CB 1 ATOM 3823 O OG1 . THR A 1 483 ? 127.330 148.798 46.378 1.00 34.40 ? 483 THR A OG1 1 ATOM 3824 C CG2 . THR A 1 483 ? 129.526 148.194 47.206 1.00 30.14 ? 483 THR A CG2 1 ATOM 3825 N N . GLN A 1 484 ? 125.009 147.454 48.429 1.00 39.37 ? 484 GLN A N 1 ATOM 3826 C CA . GLN A 1 484 ? 123.664 148.031 48.516 1.00 43.58 ? 484 GLN A CA 1 ATOM 3827 C C . GLN A 1 484 ? 122.783 147.558 49.675 1.00 47.69 ? 484 GLN A C 1 ATOM 3828 O O . GLN A 1 484 ? 121.985 148.330 50.198 1.00 54.83 ? 484 GLN A O 1 ATOM 3829 C CB . GLN A 1 484 ? 122.921 147.827 47.193 1.00 48.94 ? 484 GLN A CB 1 ATOM 3830 C CG . GLN A 1 484 ? 123.499 148.625 46.032 1.00 54.20 ? 484 GLN A CG 1 ATOM 3831 C CD . GLN A 1 484 ? 122.826 148.312 44.708 1.00 60.46 ? 484 GLN A CD 1 ATOM 3832 O OE1 . GLN A 1 484 ? 122.536 147.152 44.393 1.00 57.93 ? 484 GLN A OE1 1 ATOM 3833 N NE2 . GLN A 1 484 ? 122.578 149.349 43.920 1.00 64.96 ? 484 GLN A NE2 1 ATOM 3834 N N . ASN A 1 485 ? 122.911 146.295 50.068 1.00 55.50 ? 485 ASN A N 1 ATOM 3835 C CA . ASN A 1 485 ? 121.939 145.701 50.987 1.00 61.19 ? 485 ASN A CA 1 ATOM 3836 C C . ASN A 1 485 ? 122.444 145.435 52.414 1.00 63.18 ? 485 ASN A C 1 ATOM 3837 O O . ASN A 1 485 ? 122.225 144.350 52.959 1.00 68.23 ? 485 ASN A O 1 ATOM 3838 C CB . ASN A 1 485 ? 121.345 144.422 50.375 1.00 60.02 ? 485 ASN A CB 1 ATOM 3839 C CG . ASN A 1 485 ? 120.551 144.691 49.095 1.00 66.07 ? 485 ASN A CG 1 ATOM 3840 O OD1 . ASN A 1 485 ? 120.157 145.828 48.818 1.00 61.26 ? 485 ASN A OD1 1 ATOM 3841 N ND2 . ASN A 1 485 ? 120.312 143.635 48.312 1.00 79.15 ? 485 ASN A ND2 1 ATOM 3842 N N . GLN A 1 486 ? 123.088 146.439 53.014 1.00 58.88 ? 486 GLN A N 1 ATOM 3843 C CA . GLN A 1 486 ? 123.680 146.327 54.354 1.00 59.04 ? 486 GLN A CA 1 ATOM 3844 C C . GLN A 1 486 ? 124.467 145.031 54.555 1.00 59.09 ? 486 GLN A C 1 ATOM 3845 O O . GLN A 1 486 ? 124.296 144.338 55.560 1.00 63.29 ? 486 GLN A O 1 ATOM 3846 C CB . GLN A 1 486 ? 122.618 146.478 55.431 1.00 58.16 ? 486 GLN A CB 1 ATOM 3847 N N . SER A 1 487 ? 125.322 144.704 53.593 1.00 49.22 ? 487 SER A N 1 ATOM 3848 C CA . SER A 1 487 ? 126.093 143.469 53.655 1.00 49.85 ? 487 SER A CA 1 ATOM 3849 C C . SER A 1 487 ? 127.354 143.617 54.501 1.00 50.05 ? 487 SER A C 1 ATOM 3850 O O . SER A 1 487 ? 127.889 144.720 54.661 1.00 45.02 ? 487 SER A O 1 ATOM 3851 C CB . SER A 1 487 ? 126.484 143.007 52.250 1.00 47.84 ? 487 SER A CB 1 ATOM 3852 O OG . SER A 1 487 ? 125.351 142.590 51.511 1.00 52.25 ? 487 SER A OG 1 ATOM 3853 N N . THR A 1 488 ? 127.818 142.494 55.041 1.00 46.70 ? 488 THR A N 1 ATOM 3854 C CA . THR A 1 488 ? 129.116 142.435 55.694 1.00 42.45 ? 488 THR A CA 1 ATOM 3855 C C . THR A 1 488 ? 130.182 142.797 54.669 1.00 37.05 ? 488 THR A C 1 ATOM 3856 O O . THR A 1 488 ? 130.171 142.297 53.538 1.00 38.08 ? 488 THR A O 1 ATOM 3857 C CB . THR A 1 488 ? 129.405 141.015 56.229 1.00 44.66 ? 488 THR A CB 1 ATOM 3858 O OG1 . THR A 1 488 ? 128.424 140.660 57.214 1.00 52.05 ? 488 THR A OG1 1 ATOM 3859 C CG2 . THR A 1 488 ? 130.794 140.935 56.849 1.00 44.35 ? 488 THR A CG2 1 ATOM 3860 N N . SER A 1 489 ? 131.090 143.679 55.062 1.00 31.88 ? 489 SER A N 1 ATOM 3861 C CA . SER A 1 489 ? 132.216 144.056 54.217 1.00 38.07 ? 489 SER A CA 1 ATOM 3862 C C . SER A 1 489 ? 133.228 142.907 54.173 1.00 38.13 ? 489 SER A C 1 ATOM 3863 O O . SER A 1 489 ? 133.525 142.299 55.201 1.00 34.18 ? 489 SER A O 1 ATOM 3864 C CB . SER A 1 489 ? 132.866 145.317 54.785 1.00 44.27 ? 489 SER A CB 1 ATOM 3865 O OG . SER A 1 489 ? 133.477 146.073 53.763 1.00 56.00 ? 489 SER A OG 1 ATOM 3866 N N . TRP A 1 490 ? 133.730 142.593 52.980 1.00 27.72 ? 490 TRP A N 1 ATOM 3867 C CA . TRP A 1 490 ? 134.731 141.552 52.805 1.00 25.02 ? 490 TRP A CA 1 ATOM 3868 C C . TRP A 1 490 ? 136.112 142.198 52.950 1.00 24.57 ? 490 TRP A C 1 ATOM 3869 O O . TRP A 1 490 ? 136.533 142.968 52.090 1.00 25.50 ? 490 TRP A O 1 ATOM 3870 C CB . TRP A 1 490 ? 134.568 140.905 51.416 1.00 22.18 ? 490 TRP A CB 1 ATOM 3871 C CG . TRP A 1 490 ? 135.300 139.594 51.202 1.00 24.63 ? 490 TRP A CG 1 ATOM 3872 C CD1 . TRP A 1 490 ? 136.416 139.140 51.868 1.00 23.01 ? 490 TRP A CD1 1 ATOM 3873 C CD2 . TRP A 1 490 ? 134.952 138.567 50.257 1.00 19.19 ? 490 TRP A CD2 1 ATOM 3874 N NE1 . TRP A 1 490 ? 136.780 137.892 51.383 1.00 20.36 ? 490 TRP A NE1 1 ATOM 3875 C CE2 . TRP A 1 490 ? 135.899 137.523 50.398 1.00 21.93 ? 490 TRP A CE2 1 ATOM 3876 C CE3 . TRP A 1 490 ? 133.935 138.434 49.301 1.00 21.14 ? 490 TRP A CE3 1 ATOM 3877 C CZ2 . TRP A 1 490 ? 135.859 136.363 49.613 1.00 19.74 ? 490 TRP A CZ2 1 ATOM 3878 C CZ3 . TRP A 1 490 ? 133.892 137.280 48.526 1.00 27.75 ? 490 TRP A CZ3 1 ATOM 3879 C CH2 . TRP A 1 490 ? 134.853 136.260 48.684 1.00 25.06 ? 490 TRP A CH2 1 ATOM 3880 N N . PRO A 1 491 ? 136.813 141.906 54.056 1.00 27.58 ? 491 PRO A N 1 ATOM 3881 C CA . PRO A 1 491 ? 138.111 142.524 54.323 1.00 26.57 ? 491 PRO A CA 1 ATOM 3882 C C . PRO A 1 491 ? 139.214 141.855 53.517 1.00 25.93 ? 491 PRO A C 1 ATOM 3883 O O . PRO A 1 491 ? 139.125 140.669 53.180 1.00 23.31 ? 491 PRO A O 1 ATOM 3884 C CB . PRO A 1 491 ? 138.320 142.238 55.808 1.00 31.17 ? 491 PRO A CB 1 ATOM 3885 C CG . PRO A 1 491 ? 137.663 140.905 55.994 1.00 30.82 ? 491 PRO A CG 1 ATOM 3886 C CD . PRO A 1 491 ? 136.443 140.940 55.105 1.00 28.53 ? 491 PRO A CD 1 ATOM 3887 N N . VAL A 1 492 ? 140.251 142.617 53.192 1.00 22.51 ? 492 VAL A N 1 ATOM 3888 C CA . VAL A 1 492 ? 141.379 142.071 52.440 1.00 22.51 ? 492 VAL A CA 1 ATOM 3889 C C . VAL A 1 492 ? 142.105 140.995 53.280 1.00 26.47 ? 492 VAL A C 1 ATOM 3890 O O . VAL A 1 492 ? 142.227 141.133 54.499 1.00 24.50 ? 492 VAL A O 1 ATOM 3891 C CB . VAL A 1 492 ? 142.358 143.215 52.041 1.00 35.38 ? 492 VAL A CB 1 ATOM 3892 C CG1 . VAL A 1 492 ? 143.778 142.714 51.931 1.00 34.37 ? 492 VAL A CG1 1 ATOM 3893 C CG2 . VAL A 1 492 ? 141.908 143.895 50.733 1.00 33.99 ? 492 VAL A CG2 1 ATOM 3894 N N . PHE A 1 493 ? 142.569 139.927 52.638 1.00 23.39 ? 493 PHE A N 1 ATOM 3895 C CA . PHE A 1 493 ? 143.377 138.900 53.324 1.00 27.12 ? 493 PHE A CA 1 ATOM 3896 C C . PHE A 1 493 ? 144.850 139.294 53.338 1.00 29.63 ? 493 PHE A C 1 ATOM 3897 O O . PHE A 1 493 ? 145.462 139.454 52.277 1.00 33.57 ? 493 PHE A O 1 ATOM 3898 C CB . PHE A 1 493 ? 143.219 137.564 52.590 1.00 24.72 ? 493 PHE A CB 1 ATOM 3899 C CG . PHE A 1 493 ? 143.963 136.394 53.208 1.00 24.16 ? 493 PHE A CG 1 ATOM 3900 C CD1 . PHE A 1 493 ? 145.338 136.238 53.035 1.00 22.36 ? 493 PHE A CD1 1 ATOM 3901 C CD2 . PHE A 1 493 ? 143.263 135.396 53.875 1.00 22.52 ? 493 PHE A CD2 1 ATOM 3902 C CE1 . PHE A 1 493 ? 146.006 135.128 53.561 1.00 28.74 ? 493 PHE A CE1 1 ATOM 3903 C CE2 . PHE A 1 493 ? 143.920 134.274 54.393 1.00 26.84 ? 493 PHE A CE2 1 ATOM 3904 C CZ . PHE A 1 493 ? 145.288 134.144 54.240 1.00 28.04 ? 493 PHE A CZ 1 ATOM 3905 N N . LYS A 1 494 ? 145.417 139.422 54.536 1.00 28.51 ? 494 LYS A N 1 ATOM 3906 C CA . LYS A 1 494 ? 146.835 139.737 54.718 1.00 37.10 ? 494 LYS A CA 1 ATOM 3907 C C . LYS A 1 494 ? 147.516 138.609 55.482 1.00 41.04 ? 494 LYS A C 1 ATOM 3908 O O . LYS A 1 494 ? 146.864 137.907 56.264 1.00 35.61 ? 494 LYS A O 1 ATOM 3909 C CB . LYS A 1 494 ? 146.992 141.055 55.491 1.00 37.60 ? 494 LYS A CB 1 ATOM 3910 C CG . LYS A 1 494 ? 146.562 142.284 54.706 1.00 47.65 ? 494 LYS A CG 1 ATOM 3911 C CD . LYS A 1 494 ? 145.974 143.369 55.613 1.00 59.09 ? 494 LYS A CD 1 ATOM 3912 C CE . LYS A 1 494 ? 145.658 144.639 54.813 1.00 62.76 ? 494 LYS A CE 1 ATOM 3913 N NZ . LYS A 1 494 ? 144.642 145.529 55.461 1.00 58.69 ? 494 LYS A NZ 1 ATOM 3914 N N . SER A 1 495 ? 148.824 138.446 55.273 1.00 44.86 ? 495 SER A N 1 ATOM 3915 C CA . SER A 1 495 ? 149.560 137.304 55.830 1.00 50.47 ? 495 SER A CA 1 ATOM 3916 C C . SER A 1 495 ? 149.618 137.311 57.357 1.00 41.71 ? 495 SER A C 1 ATOM 3917 O O . SER A 1 495 ? 149.777 136.258 57.979 1.00 43.81 ? 495 SER A O 1 ATOM 3918 C CB . SER A 1 495 ? 150.982 137.236 55.260 1.00 60.27 ? 495 SER A CB 1 ATOM 3919 O OG . SER A 1 495 ? 151.757 138.345 55.697 1.00 67.37 ? 495 SER A OG 1 ATOM 3920 N N . THR A 1 496 ? 149.489 138.491 57.955 1.00 33.36 ? 496 THR A N 1 ATOM 3921 C CA . THR A 1 496 ? 149.461 138.605 59.411 1.00 39.33 ? 496 THR A CA 1 ATOM 3922 C C . THR A 1 496 ? 148.113 138.178 60.004 1.00 37.47 ? 496 THR A C 1 ATOM 3923 O O . THR A 1 496 ? 148.041 137.193 60.735 1.00 42.78 ? 496 THR A O 1 ATOM 3924 C CB . THR A 1 496 ? 149.793 140.035 59.886 1.00 52.00 ? 496 THR A CB 1 ATOM 3925 O OG1 . THR A 1 496 ? 151.165 140.334 59.592 1.00 61.79 ? 496 THR A OG1 1 ATOM 3926 C CG2 . THR A 1 496 ? 149.574 140.164 61.389 1.00 49.77 ? 496 THR A CG2 1 ATOM 3927 N N . GLU A 1 497 ? 147.047 138.910 59.687 1.00 35.98 ? 497 GLU A N 1 ATOM 3928 C CA . GLU A 1 497 ? 145.754 138.662 60.326 1.00 36.90 ? 497 GLU A CA 1 ATOM 3929 C C . GLU A 1 497 ? 144.927 137.555 59.691 1.00 29.44 ? 497 GLU A C 1 ATOM 3930 O O . GLU A 1 497 ? 144.139 136.893 60.381 1.00 30.01 ? 497 GLU A O 1 ATOM 3931 C CB . GLU A 1 497 ? 144.937 139.943 60.390 1.00 36.42 ? 497 GLU A CB 1 ATOM 3932 C CG . GLU A 1 497 ? 145.481 140.928 61.384 1.00 49.28 ? 497 GLU A CG 1 ATOM 3933 C CD . GLU A 1 497 ? 145.220 142.345 60.959 1.00 63.56 ? 497 GLU A CD 1 ATOM 3934 O OE1 . GLU A 1 497 ? 145.970 142.841 60.089 1.00 71.74 ? 497 GLU A OE1 1 ATOM 3935 O OE2 . GLU A 1 497 ? 144.261 142.953 61.482 1.00 67.85 ? 497 GLU A OE2 1 ATOM 3936 N N . GLN A 1 498 ? 145.077 137.382 58.382 1.00 21.63 ? 498 GLN A N 1 ATOM 3937 C CA . GLN A 1 498 ? 144.438 136.272 57.674 1.00 20.56 ? 498 GLN A CA 1 ATOM 3938 C C . GLN A 1 498 ? 142.908 136.234 57.835 1.00 25.45 ? 498 GLN A C 1 ATOM 3939 O O . GLN A 1 498 ? 142.318 135.173 58.097 1.00 26.62 ? 498 GLN A O 1 ATOM 3940 C CB . GLN A 1 498 ? 145.082 134.939 58.112 1.00 30.23 ? 498 GLN A CB 1 ATOM 3941 C CG . GLN A 1 498 ? 146.595 134.858 57.852 1.00 33.60 ? 498 GLN A CG 1 ATOM 3942 C CD . GLN A 1 498 ? 147.299 133.772 58.677 1.00 40.28 ? 498 GLN A CD 1 ATOM 3943 O OE1 . GLN A 1 498 ? 146.860 132.621 58.736 1.00 36.54 ? 498 GLN A OE1 1 ATOM 3944 N NE2 . GLN A 1 498 ? 148.392 134.149 59.326 1.00 46.78 ? 498 GLN A NE2 1 ATOM 3945 N N . LYS A 1 499 ? 142.268 137.385 57.654 1.00 22.45 ? 499 LYS A N 1 ATOM 3946 C CA . LYS A 1 499 ? 140.810 137.468 57.751 1.00 22.80 ? 499 LYS A CA 1 ATOM 3947 C C . LYS A 1 499 ? 140.178 136.792 56.551 1.00 19.90 ? 499 LYS A C 1 ATOM 3948 O O . LYS A 1 499 ? 140.695 136.906 55.431 1.00 23.28 ? 499 LYS A O 1 ATOM 3949 C CB . LYS A 1 499 ? 140.358 138.939 57.827 1.00 21.78 ? 499 LYS A CB 1 ATOM 3950 C CG . LYS A 1 499 ? 140.912 139.666 59.045 1.00 23.03 ? 499 LYS A CG 1 ATOM 3951 C CD . LYS A 1 499 ? 140.447 141.130 59.108 1.00 24.04 ? 499 LYS A CD 1 ATOM 3952 C CE . LYS A 1 499 ? 141.001 141.813 60.351 1.00 28.89 ? 499 LYS A CE 1 ATOM 3953 N NZ . LYS A 1 499 ? 140.506 143.211 60.443 1.00 29.20 ? 499 LYS A NZ 1 ATOM 3954 N N . TYR A 1 500 ? 139.066 136.091 56.780 1.00 19.93 ? 500 TYR A N 1 ATOM 3955 C CA . TYR A 1 500 ? 138.266 135.536 55.685 1.00 22.40 ? 500 TYR A CA 1 ATOM 3956 C C . TYR A 1 500 ? 136.768 135.702 55.938 1.00 21.74 ? 500 TYR A C 1 ATOM 3957 O O . TYR A 1 500 ? 136.348 135.933 57.070 1.00 20.89 ? 500 TYR A O 1 ATOM 3958 C CB . TYR A 1 500 ? 138.602 134.059 55.447 1.00 20.12 ? 500 TYR A CB 1 ATOM 3959 C CG . TYR A 1 500 ? 138.255 133.132 56.597 1.00 21.11 ? 500 TYR A CG 1 ATOM 3960 C CD1 . TYR A 1 500 ? 139.102 133.006 57.699 1.00 19.68 ? 500 TYR A CD1 1 ATOM 3961 C CD2 . TYR A 1 500 ? 137.096 132.352 56.561 1.00 19.26 ? 500 TYR A CD2 1 ATOM 3962 C CE1 . TYR A 1 500 ? 138.792 132.132 58.755 1.00 21.19 ? 500 TYR A CE1 1 ATOM 3963 C CE2 . TYR A 1 500 ? 136.779 131.485 57.597 1.00 23.01 ? 500 TYR A CE2 1 ATOM 3964 C CZ . TYR A 1 500 ? 137.625 131.376 58.689 1.00 26.44 ? 500 TYR A CZ 1 ATOM 3965 O OH . TYR A 1 500 ? 137.292 130.512 59.719 1.00 21.42 ? 500 TYR A OH 1 ATOM 3966 N N . LEU A 1 501 ? 135.973 135.558 54.880 1.00 22.65 ? 501 LEU A N 1 ATOM 3967 C CA . LEU A 1 501 ? 134.528 135.745 54.936 1.00 24.26 ? 501 LEU A CA 1 ATOM 3968 C C . LEU A 1 501 ? 133.795 134.403 54.781 1.00 23.92 ? 501 LEU A C 1 ATOM 3969 O O . LEU A 1 501 ? 134.080 133.622 53.858 1.00 20.94 ? 501 LEU A O 1 ATOM 3970 C CB . LEU A 1 501 ? 134.085 136.697 53.814 1.00 21.97 ? 501 LEU A CB 1 ATOM 3971 C CG . LEU A 1 501 ? 132.588 137.041 53.763 1.00 27.50 ? 501 LEU A CG 1 ATOM 3972 C CD1 . LEU A 1 501 ? 132.201 137.866 54.969 1.00 31.22 ? 501 LEU A CD1 1 ATOM 3973 C CD2 . LEU A 1 501 ? 132.202 137.786 52.488 1.00 30.51 ? 501 LEU A CD2 1 ATOM 3974 N N . THR A 1 502 ? 132.860 134.119 55.680 1.00 21.71 ? 502 THR A N 1 ATOM 3975 C CA . THR A 1 502 ? 132.091 132.882 55.562 1.00 24.47 ? 502 THR A CA 1 ATOM 3976 C C . THR A 1 502 ? 130.837 133.143 54.740 1.00 26.13 ? 502 THR A C 1 ATOM 3977 O O . THR A 1 502 ? 130.158 134.158 54.941 1.00 23.91 ? 502 THR A O 1 ATOM 3978 C CB . THR A 1 502 ? 131.704 132.296 56.938 1.00 25.37 ? 502 THR A CB 1 ATOM 3979 O OG1 . THR A 1 502 ? 130.809 133.198 57.610 1.00 29.43 ? 502 THR A OG1 1 ATOM 3980 C CG2 . THR A 1 502 ? 132.969 132.068 57.791 1.00 26.13 ? 502 THR A CG2 1 ATOM 3981 N N . LEU A 1 503 ? 130.540 132.234 53.813 1.00 26.52 ? 503 LEU A N 1 ATOM 3982 C CA . LEU A 1 503 ? 129.342 132.339 52.988 1.00 27.84 ? 503 LEU A CA 1 ATOM 3983 C C . LEU A 1 503 ? 128.316 131.288 53.400 1.00 32.71 ? 503 LEU A C 1 ATOM 3984 O O . LEU A 1 503 ? 128.574 130.080 53.308 1.00 30.18 ? 503 LEU A O 1 ATOM 3985 C CB . LEU A 1 503 ? 129.696 132.182 51.505 1.00 26.70 ? 503 LEU A CB 1 ATOM 3986 C CG . LEU A 1 503 ? 130.683 133.218 50.950 1.00 26.58 ? 503 LEU A CG 1 ATOM 3987 C CD1 . LEU A 1 503 ? 131.137 132.829 49.535 1.00 18.85 ? 503 LEU A CD1 1 ATOM 3988 C CD2 . LEU A 1 503 ? 130.046 134.612 50.965 1.00 25.64 ? 503 LEU A CD2 1 ATOM 3989 N N A ASN A 1 504 ? 127.161 131.751 53.864 0.55 32.49 ? 504 ASN A N 1 ATOM 3990 N N B ASN A 1 504 ? 127.152 131.745 53.854 0.45 32.55 ? 504 ASN A N 1 ATOM 3991 C CA A ASN A 1 504 ? 126.076 130.859 54.254 0.55 33.22 ? 504 ASN A CA 1 ATOM 3992 C CA B ASN A 1 504 ? 126.069 130.850 54.256 0.45 33.18 ? 504 ASN A CA 1 ATOM 3993 C C A ASN A 1 504 ? 124.729 131.575 54.142 0.55 33.83 ? 504 ASN A C 1 ATOM 3994 C C B ASN A 1 504 ? 124.729 131.568 54.124 0.45 33.74 ? 504 ASN A C 1 ATOM 3995 O O A ASN A 1 504 ? 124.691 132.779 53.874 0.55 33.33 ? 504 ASN A O 1 ATOM 3996 O O B ASN A 1 504 ? 124.693 132.766 53.837 0.45 33.35 ? 504 ASN A O 1 ATOM 3997 C CB A ASN A 1 504 ? 126.308 130.320 55.670 0.55 32.72 ? 504 ASN A CB 1 ATOM 3998 C CB B ASN A 1 504 ? 126.278 130.377 55.697 0.45 33.24 ? 504 ASN A CB 1 ATOM 3999 C CG A ASN A 1 504 ? 126.503 131.427 56.692 0.55 36.07 ? 504 ASN A CG 1 ATOM 4000 C CG B ASN A 1 504 ? 125.597 129.049 55.992 0.45 39.78 ? 504 ASN A CG 1 ATOM 4001 O OD1 A ASN A 1 504 ? 125.532 131.994 57.188 0.55 32.35 ? 504 ASN A OD1 1 ATOM 4002 O OD1 B ASN A 1 504 ? 124.698 128.608 55.265 0.45 41.13 ? 504 ASN A OD1 1 ATOM 4003 N ND2 A ASN A 1 504 ? 127.767 131.733 57.020 0.55 30.09 ? 504 ASN A ND2 1 ATOM 4004 N ND2 B ASN A 1 504 ? 126.017 128.408 57.080 0.45 44.80 ? 504 ASN A ND2 1 ATOM 4005 N N . THR A 1 505 ? 123.629 130.846 54.332 1.00 32.32 ? 505 THR A N 1 ATOM 4006 C CA . THR A 1 505 ? 122.302 131.460 54.241 1.00 42.46 ? 505 THR A CA 1 ATOM 4007 C C . THR A 1 505 ? 121.952 132.290 55.473 1.00 51.98 ? 505 THR A C 1 ATOM 4008 O O . THR A 1 505 ? 121.206 133.263 55.381 1.00 60.37 ? 505 THR A O 1 ATOM 4009 C CB . THR A 1 505 ? 121.161 130.434 53.986 1.00 32.61 ? 505 THR A CB 1 ATOM 4010 O OG1 . THR A 1 505 ? 121.112 129.479 55.051 1.00 38.81 ? 505 THR A OG1 1 ATOM 4011 C CG2 . THR A 1 505 ? 121.359 129.711 52.657 1.00 30.73 ? 505 THR A CG2 1 ATOM 4012 N N . GLU A 1 506 ? 122.491 131.907 56.624 1.00 55.37 ? 506 GLU A N 1 ATOM 4013 C CA . GLU A 1 506 ? 122.132 132.565 57.878 1.00 67.49 ? 506 GLU A CA 1 ATOM 4014 C C . GLU A 1 506 ? 122.965 133.810 58.186 1.00 71.84 ? 506 GLU A C 1 ATOM 4015 O O . GLU A 1 506 ? 122.486 134.939 58.064 1.00 79.16 ? 506 GLU A O 1 ATOM 4016 C CB . GLU A 1 506 ? 122.244 131.573 59.035 1.00 75.31 ? 506 GLU A CB 1 ATOM 4017 C CG . GLU A 1 506 ? 123.202 130.424 58.749 1.00 83.98 ? 506 GLU A CG 1 ATOM 4018 C CD . GLU A 1 506 ? 123.588 129.656 59.997 1.00 92.07 ? 506 GLU A CD 1 ATOM 4019 O OE1 . GLU A 1 506 ? 124.514 130.108 60.707 1.00 93.57 ? 506 GLU A OE1 1 ATOM 4020 O OE2 . GLU A 1 506 ? 122.972 128.599 60.262 1.00 94.48 ? 506 GLU A OE2 1 ATOM 4021 N N . SER A 1 507 ? 124.214 133.592 58.582 1.00 64.31 ? 507 SER A N 1 ATOM 4022 C CA . SER A 1 507 ? 125.033 134.646 59.157 1.00 62.53 ? 507 SER A CA 1 ATOM 4023 C C . SER A 1 507 ? 126.386 134.712 58.468 1.00 57.19 ? 507 SER A C 1 ATOM 4024 O O . SER A 1 507 ? 127.222 133.827 58.666 1.00 63.46 ? 507 SER A O 1 ATOM 4025 C CB . SER A 1 507 ? 125.235 134.360 60.650 1.00 70.00 ? 507 SER A CB 1 ATOM 4026 O OG . SER A 1 507 ? 125.843 135.448 61.322 1.00 73.00 ? 507 SER A OG 1 ATOM 4027 N N . THR A 1 508 ? 126.609 135.744 57.656 1.00 43.81 ? 508 THR A N 1 ATOM 4028 C CA . THR A 1 508 ? 127.926 135.919 57.046 1.00 49.60 ? 508 THR A CA 1 ATOM 4029 C C . THR A 1 508 ? 128.836 136.589 58.066 1.00 44.01 ? 508 THR A C 1 ATOM 4030 O O . THR A 1 508 ? 128.476 137.614 58.648 1.00 40.75 ? 508 THR A O 1 ATOM 4031 C CB . THR A 1 508 ? 127.873 136.743 55.750 1.00 49.74 ? 508 THR A CB 1 ATOM 4032 O OG1 . THR A 1 508 ? 128.455 138.034 55.963 1.00 51.80 ? 508 THR A OG1 1 ATOM 4033 C CG2 . THR A 1 508 ? 126.445 136.902 55.303 1.00 50.04 ? 508 THR A CG2 1 ATOM 4034 N N . ARG A 1 509 ? 130.000 135.995 58.307 1.00 32.87 ? 509 ARG A N 1 ATOM 4035 C CA . ARG A 1 509 ? 130.880 136.486 59.356 1.00 32.93 ? 509 ARG A CA 1 ATOM 4036 C C . ARG A 1 509 ? 132.309 136.668 58.892 1.00 30.02 ? 509 ARG A C 1 ATOM 4037 O O . ARG A 1 509 ? 132.767 135.978 57.968 1.00 26.13 ? 509 ARG A O 1 ATOM 4038 C CB . ARG A 1 509 ? 130.854 135.530 60.551 1.00 39.22 ? 509 ARG A CB 1 ATOM 4039 C CG . ARG A 1 509 ? 129.452 135.278 61.063 1.00 45.63 ? 509 ARG A CG 1 ATOM 4040 C CD . ARG A 1 509 ? 129.430 134.397 62.281 1.00 56.74 ? 509 ARG A CD 1 ATOM 4041 N NE . ARG A 1 509 ? 128.108 134.400 62.907 1.00 69.50 ? 509 ARG A NE 1 ATOM 4042 C CZ . ARG A 1 509 ? 127.641 135.387 63.670 1.00 72.08 ? 509 ARG A CZ 1 ATOM 4043 N NH1 . ARG A 1 509 ? 128.385 136.461 63.902 1.00 68.49 ? 509 ARG A NH1 1 ATOM 4044 N NH2 . ARG A 1 509 ? 126.422 135.303 64.194 1.00 74.89 ? 509 ARG A NH2 1 ATOM 4045 N N . ILE A 1 510 ? 133.001 137.599 59.550 1.00 25.07 ? 510 ILE A N 1 ATOM 4046 C CA . ILE A 1 510 ? 134.441 137.731 59.425 1.00 24.22 ? 510 ILE A CA 1 ATOM 4047 C C . ILE A 1 510 ? 135.147 136.879 60.482 1.00 29.85 ? 510 ILE A C 1 ATOM 4048 O O . ILE A 1 510 ? 134.897 137.038 61.684 1.00 25.69 ? 510 ILE A O 1 ATOM 4049 C CB . ILE A 1 510 ? 134.918 139.185 59.629 1.00 29.50 ? 510 ILE A CB 1 ATOM 4050 C CG1 . ILE A 1 510 ? 134.164 140.145 58.708 1.00 30.31 ? 510 ILE A CG1 1 ATOM 4051 C CG2 . ILE A 1 510 ? 136.405 139.271 59.345 1.00 29.04 ? 510 ILE A CG2 1 ATOM 4052 C CD1 . ILE A 1 510 ? 134.160 139.679 57.288 1.00 27.89 ? 510 ILE A CD1 1 ATOM 4053 N N A MET A 1 511 ? 136.023 135.981 60.038 0.41 29.21 ? 511 MET A N 1 ATOM 4054 N N B MET A 1 511 ? 136.046 136.012 60.023 0.59 23.26 ? 511 MET A N 1 ATOM 4055 C CA A MET A 1 511 ? 136.801 135.141 60.947 0.41 29.49 ? 511 MET A CA 1 ATOM 4056 C CA B MET A 1 511 ? 136.804 135.112 60.888 0.59 28.82 ? 511 MET A CA 1 ATOM 4057 C C A MET A 1 511 ? 138.283 135.186 60.574 0.41 29.77 ? 511 MET A C 1 ATOM 4058 C C B MET A 1 511 ? 138.296 135.200 60.568 0.59 29.92 ? 511 MET A C 1 ATOM 4059 O O A MET A 1 511 ? 138.647 135.683 59.506 0.41 30.30 ? 511 MET A O 1 ATOM 4060 O O B MET A 1 511 ? 138.683 135.746 59.528 0.59 21.93 ? 511 MET A O 1 ATOM 4061 C CB A MET A 1 511 ? 136.285 133.696 60.926 0.41 28.29 ? 511 MET A CB 1 ATOM 4062 C CB B MET A 1 511 ? 136.317 133.679 60.683 0.59 24.50 ? 511 MET A CB 1 ATOM 4063 C CG A MET A 1 511 ? 134.798 133.568 61.258 0.41 34.68 ? 511 MET A CG 1 ATOM 4064 C CG B MET A 1 511 ? 134.820 133.527 60.878 0.59 30.42 ? 511 MET A CG 1 ATOM 4065 S SD A MET A 1 511 ? 134.163 131.873 61.319 0.41 24.48 ? 511 MET A SD 1 ATOM 4066 S SD B MET A 1 511 ? 134.358 133.664 62.620 0.59 40.98 ? 511 MET A SD 1 ATOM 4067 C CE A MET A 1 511 ? 135.118 131.191 62.660 0.41 26.69 ? 511 MET A CE 1 ATOM 4068 C CE B MET A 1 511 ? 134.753 131.997 63.157 0.59 30.41 ? 511 MET A CE 1 ATOM 4069 N N . THR A 1 512 ? 139.132 134.668 61.457 1.00 23.18 ? 512 THR A N 1 ATOM 4070 C CA . THR A 1 512 ? 140.576 134.697 61.247 1.00 22.77 ? 512 THR A CA 1 ATOM 4071 C C . THR A 1 512 ? 141.235 133.314 61.296 1.00 23.30 ? 512 THR A C 1 ATOM 4072 O O . THR A 1 512 ? 140.800 132.423 62.049 1.00 23.02 ? 512 THR A O 1 ATOM 4073 C CB . THR A 1 512 ? 141.270 135.577 62.304 1.00 26.15 ? 512 THR A CB 1 ATOM 4074 O OG1 . THR A 1 512 ? 140.835 135.180 63.611 1.00 28.72 ? 512 THR A OG1 1 ATOM 4075 C CG2 . THR A 1 512 ? 140.937 137.062 62.084 1.00 25.26 ? 512 THR A CG2 1 ATOM 4076 N N . LYS A 1 513 ? 142.281 133.154 60.481 1.00 21.67 ? 513 LYS A N 1 ATOM 4077 C CA . LYS A 1 513 ? 143.208 132.019 60.568 1.00 21.62 ? 513 LYS A CA 1 ATOM 4078 C C . LYS A 1 513 ? 142.542 130.650 60.417 1.00 21.34 ? 513 LYS A C 1 ATOM 4079 O O . LYS A 1 513 ? 142.644 129.787 61.297 1.00 22.12 ? 513 LYS A O 1 ATOM 4080 C CB . LYS A 1 513 ? 144.037 132.101 61.868 1.00 22.89 ? 513 LYS A CB 1 ATOM 4081 C CG . LYS A 1 513 ? 144.973 133.340 61.928 1.00 28.04 ? 513 LYS A CG 1 ATOM 4082 C CD . LYS A 1 513 ? 145.686 133.453 63.278 1.00 27.96 ? 513 LYS A CD 1 ATOM 4083 C CE . LYS A 1 513 ? 146.586 134.680 63.337 1.00 38.88 ? 513 LYS A CE 1 ATOM 4084 N NZ . LYS A 1 513 ? 147.285 134.809 64.653 1.00 46.49 ? 513 LYS A NZ 1 ATOM 4085 N N . LEU A 1 514 ? 141.862 130.462 59.292 1.00 23.56 ? 514 LEU A N 1 ATOM 4086 C CA . LEU A 1 514 ? 141.180 129.203 58.978 1.00 22.02 ? 514 LEU A CA 1 ATOM 4087 C C . LEU A 1 514 ? 142.080 127.955 59.144 1.00 25.38 ? 514 LEU A C 1 ATOM 4088 O O . LEU A 1 514 ? 143.199 127.923 58.631 1.00 20.45 ? 514 LEU A O 1 ATOM 4089 C CB . LEU A 1 514 ? 140.625 129.274 57.552 1.00 19.08 ? 514 LEU A CB 1 ATOM 4090 C CG . LEU A 1 514 ? 139.908 128.022 57.025 1.00 27.50 ? 514 LEU A CG 1 ATOM 4091 C CD1 . LEU A 1 514 ? 138.665 127.717 57.879 1.00 19.70 ? 514 LEU A CD1 1 ATOM 4092 C CD2 . LEU A 1 514 ? 139.528 128.205 55.557 1.00 20.80 ? 514 LEU A CD2 1 ATOM 4093 N N . ARG A 1 515 ? 141.595 126.949 59.875 1.00 21.12 ? 515 ARG A N 1 ATOM 4094 C CA . ARG A 1 515 ? 142.330 125.679 60.085 1.00 29.36 ? 515 ARG A CA 1 ATOM 4095 C C . ARG A 1 515 ? 143.800 125.881 60.467 1.00 26.05 ? 515 ARG A C 1 ATOM 4096 O O . ARG A 1 515 ? 144.672 125.160 59.966 1.00 26.17 ? 515 ARG A O 1 ATOM 4097 C CB . ARG A 1 515 ? 142.291 124.781 58.828 1.00 26.17 ? 515 ARG A CB 1 ATOM 4098 C CG . ARG A 1 515 ? 140.908 124.398 58.300 1.00 32.37 ? 515 ARG A CG 1 ATOM 4099 C CD . ARG A 1 515 ? 140.401 123.043 58.844 1.00 35.97 ? 515 ARG A CD 1 ATOM 4100 N NE . ARG A 1 515 ? 139.367 122.454 57.992 1.00 33.01 ? 515 ARG A NE 1 ATOM 4101 C CZ . ARG A 1 515 ? 138.134 122.956 57.853 1.00 43.49 ? 515 ARG A CZ 1 ATOM 4102 N NH1 . ARG A 1 515 ? 137.786 124.061 58.518 1.00 38.22 ? 515 ARG A NH1 1 ATOM 4103 N NH2 . ARG A 1 515 ? 137.238 122.362 57.048 1.00 31.09 ? 515 ARG A NH2 1 ATOM 4104 N N . ALA A 1 516 ? 144.086 126.857 61.329 1.00 34.62 ? 516 ALA A N 1 ATOM 4105 C CA . ALA A 1 516 ? 145.477 127.178 61.673 1.00 35.70 ? 516 ALA A CA 1 ATOM 4106 C C . ALA A 1 516 ? 146.309 125.934 62.061 1.00 42.68 ? 516 ALA A C 1 ATOM 4107 O O . ALA A 1 516 ? 147.347 125.660 61.464 1.00 36.23 ? 516 ALA A O 1 ATOM 4108 C CB . ALA A 1 516 ? 145.533 128.228 62.771 1.00 38.96 ? 516 ALA A CB 1 ATOM 4109 N N . GLN A 1 517 ? 145.827 125.177 63.041 1.00 44.98 ? 517 GLN A N 1 ATOM 4110 C CA . GLN A 1 517 ? 146.547 124.014 63.571 1.00 46.02 ? 517 GLN A CA 1 ATOM 4111 C C . GLN A 1 517 ? 146.719 122.879 62.550 1.00 37.75 ? 517 GLN A C 1 ATOM 4112 O O . GLN A 1 517 ? 147.802 122.305 62.421 1.00 34.09 ? 517 GLN A O 1 ATOM 4113 C CB . GLN A 1 517 ? 145.804 123.497 64.801 1.00 61.71 ? 517 GLN A CB 1 ATOM 4114 C CG . GLN A 1 517 ? 146.677 122.946 65.904 1.00 75.56 ? 517 GLN A CG 1 ATOM 4115 C CD . GLN A 1 517 ? 145.883 122.720 67.175 1.00 86.60 ? 517 GLN A CD 1 ATOM 4116 O OE1 . GLN A 1 517 ? 144.674 122.479 67.127 1.00 88.34 ? 517 GLN A OE1 1 ATOM 4117 N NE2 . GLN A 1 517 ? 146.551 122.814 68.320 1.00 91.34 ? 517 GLN A NE2 1 ATOM 4118 N N . GLN A 1 518 ? 145.648 122.546 61.834 1.00 30.72 ? 518 GLN A N 1 ATOM 4119 C CA . GLN A 1 518 ? 145.729 121.516 60.807 1.00 28.63 ? 518 GLN A CA 1 ATOM 4120 C C . GLN A 1 518 ? 146.757 121.861 59.731 1.00 29.96 ? 518 GLN A C 1 ATOM 4121 O O . GLN A 1 518 ? 147.580 121.024 59.357 1.00 27.67 ? 518 GLN A O 1 ATOM 4122 C CB . GLN A 1 518 ? 144.360 121.282 60.162 1.00 27.43 ? 518 GLN A CB 1 ATOM 4123 C CG . GLN A 1 518 ? 143.272 120.785 61.129 1.00 34.71 ? 518 GLN A CG 1 ATOM 4124 C CD . GLN A 1 518 ? 142.543 121.918 61.840 1.00 38.94 ? 518 GLN A CD 1 ATOM 4125 O OE1 . GLN A 1 518 ? 143.054 123.037 61.951 1.00 39.78 ? 518 GLN A OE1 1 ATOM 4126 N NE2 . GLN A 1 518 ? 141.335 121.630 62.321 1.00 43.22 ? 518 GLN A NE2 1 ATOM 4127 N N . CYS A 1 519 ? 146.703 123.095 59.235 1.00 28.68 ? 519 CYS A N 1 ATOM 4128 C CA . CYS A 1 519 ? 147.552 123.505 58.122 1.00 28.10 ? 519 CYS A CA 1 ATOM 4129 C C . CYS A 1 519 ? 149.025 123.625 58.512 1.00 33.85 ? 519 CYS A C 1 ATOM 4130 O O . CYS A 1 519 ? 149.897 123.365 57.685 1.00 34.26 ? 519 CYS A O 1 ATOM 4131 C CB . CYS A 1 519 ? 147.020 124.787 57.469 1.00 28.57 ? 519 CYS A CB 1 ATOM 4132 S SG . CYS A 1 519 ? 145.489 124.460 56.554 1.00 34.79 ? 519 CYS A SG 1 ATOM 4133 N N . ARG A 1 520 ? 149.310 124.000 59.759 1.00 31.11 ? 520 ARG A N 1 ATOM 4134 C CA . ARG A 1 520 ? 150.690 123.935 60.243 1.00 32.56 ? 520 ARG A CA 1 ATOM 4135 C C . ARG A 1 520 ? 151.245 122.516 60.087 1.00 31.68 ? 520 ARG A C 1 ATOM 4136 O O . ARG A 1 520 ? 152.384 122.344 59.676 1.00 32.23 ? 520 ARG A O 1 ATOM 4137 C CB . ARG A 1 520 ? 150.801 124.385 61.696 1.00 37.63 ? 520 ARG A CB 1 ATOM 4138 C CG . ARG A 1 520 ? 150.596 125.874 61.890 1.00 45.11 ? 520 ARG A CG 1 ATOM 4139 C CD . ARG A 1 520 ? 150.993 126.330 63.291 1.00 51.68 ? 520 ARG A CD 1 ATOM 4140 N NE . ARG A 1 520 ? 150.386 127.625 63.580 1.00 63.53 ? 520 ARG A NE 1 ATOM 4141 C CZ . ARG A 1 520 ? 149.290 127.790 64.315 1.00 62.09 ? 520 ARG A CZ 1 ATOM 4142 N NH1 . ARG A 1 520 ? 148.692 126.740 64.870 1.00 50.60 ? 520 ARG A NH1 1 ATOM 4143 N NH2 . ARG A 1 520 ? 148.803 129.010 64.514 1.00 69.63 ? 520 ARG A NH2 1 ATOM 4144 N N . PHE A 1 521 ? 150.435 121.504 60.386 1.00 30.63 ? 521 PHE A N 1 ATOM 4145 C CA . PHE A 1 521 ? 150.865 120.116 60.198 1.00 30.08 ? 521 PHE A CA 1 ATOM 4146 C C . PHE A 1 521 ? 151.160 119.779 58.721 1.00 31.76 ? 521 PHE A C 1 ATOM 4147 O O . PHE A 1 521 ? 152.227 119.257 58.391 1.00 29.52 ? 521 PHE A O 1 ATOM 4148 C CB . PHE A 1 521 ? 149.809 119.138 60.749 1.00 29.48 ? 521 PHE A CB 1 ATOM 4149 C CG . PHE A 1 521 ? 150.071 117.688 60.388 1.00 29.02 ? 521 PHE A CG 1 ATOM 4150 C CD1 . PHE A 1 521 ? 150.998 116.929 61.108 1.00 31.01 ? 521 PHE A CD1 1 ATOM 4151 C CD2 . PHE A 1 521 ? 149.399 117.091 59.326 1.00 27.55 ? 521 PHE A CD2 1 ATOM 4152 C CE1 . PHE A 1 521 ? 151.247 115.589 60.774 1.00 30.55 ? 521 PHE A CE1 1 ATOM 4153 C CE2 . PHE A 1 521 ? 149.643 115.750 58.979 1.00 37.35 ? 521 PHE A CE2 1 ATOM 4154 C CZ . PHE A 1 521 ? 150.571 115.001 59.705 1.00 29.04 ? 521 PHE A CZ 1 ATOM 4155 N N . TRP A 1 522 ? 150.205 120.061 57.839 1.00 27.47 ? 522 TRP A N 1 ATOM 4156 C CA . TRP A 1 522 ? 150.367 119.738 56.421 1.00 26.65 ? 522 TRP A CA 1 ATOM 4157 C C . TRP A 1 522 ? 151.414 120.595 55.709 1.00 39.86 ? 522 TRP A C 1 ATOM 4158 O O . TRP A 1 522 ? 152.144 120.110 54.848 1.00 34.44 ? 522 TRP A O 1 ATOM 4159 C CB . TRP A 1 522 ? 149.035 119.884 55.688 1.00 25.26 ? 522 TRP A CB 1 ATOM 4160 C CG . TRP A 1 522 ? 148.033 118.882 56.104 1.00 28.99 ? 522 TRP A CG 1 ATOM 4161 C CD1 . TRP A 1 522 ? 146.865 119.112 56.785 1.00 26.13 ? 522 TRP A CD1 1 ATOM 4162 C CD2 . TRP A 1 522 ? 148.098 117.470 55.877 1.00 24.21 ? 522 TRP A CD2 1 ATOM 4163 N NE1 . TRP A 1 522 ? 146.200 117.921 56.994 1.00 23.80 ? 522 TRP A NE1 1 ATOM 4164 C CE2 . TRP A 1 522 ? 146.938 116.900 56.449 1.00 24.86 ? 522 TRP A CE2 1 ATOM 4165 C CE3 . TRP A 1 522 ? 149.031 116.629 55.253 1.00 26.44 ? 522 TRP A CE3 1 ATOM 4166 C CZ2 . TRP A 1 522 ? 146.681 115.528 56.403 1.00 26.76 ? 522 TRP A CZ2 1 ATOM 4167 C CZ3 . TRP A 1 522 ? 148.777 115.262 55.216 1.00 28.54 ? 522 TRP A CZ3 1 ATOM 4168 C CH2 . TRP A 1 522 ? 147.611 114.727 55.785 1.00 26.03 ? 522 TRP A CH2 1 ATOM 4169 N N . THR A 1 523 ? 151.473 121.875 56.051 1.00 37.04 ? 523 THR A N 1 ATOM 4170 C CA . THR A 1 523 ? 152.285 122.802 55.280 1.00 37.68 ? 523 THR A CA 1 ATOM 4171 C C . THR A 1 523 ? 153.744 122.767 55.723 1.00 45.73 ? 523 THR A C 1 ATOM 4172 O O . THR A 1 523 ? 154.648 122.789 54.890 1.00 46.47 ? 523 THR A O 1 ATOM 4173 C CB . THR A 1 523 ? 151.703 124.243 55.332 1.00 40.23 ? 523 THR A CB 1 ATOM 4174 O OG1 . THR A 1 523 ? 150.378 124.231 54.787 1.00 38.13 ? 523 THR A OG1 1 ATOM 4175 C CG2 . THR A 1 523 ? 152.550 125.220 54.528 1.00 42.74 ? 523 THR A CG2 1 ATOM 4176 N N . SER A 1 524 ? 153.969 122.694 57.032 1.00 50.07 ? 524 SER A N 1 ATOM 4177 C CA . SER A 1 524 ? 155.319 122.744 57.577 1.00 50.94 ? 524 SER A CA 1 ATOM 4178 C C . SER A 1 524 ? 155.947 121.369 57.710 1.00 53.58 ? 524 SER A C 1 ATOM 4179 O O . SER A 1 524 ? 157.048 121.141 57.214 1.00 63.82 ? 524 SER A O 1 ATOM 4180 C CB . SER A 1 524 ? 155.335 123.435 58.943 1.00 52.81 ? 524 SER A CB 1 ATOM 4181 O OG . SER A 1 524 ? 154.766 124.728 58.863 1.00 54.56 ? 524 SER A OG 1 ATOM 4182 N N . PHE A 1 525 ? 155.255 120.456 58.383 1.00 48.17 ? 525 PHE A N 1 ATOM 4183 C CA . PHE A 1 525 ? 155.856 119.164 58.718 1.00 45.91 ? 525 PHE A CA 1 ATOM 4184 C C . PHE A 1 525 ? 155.750 118.073 57.644 1.00 49.14 ? 525 PHE A C 1 ATOM 4185 O O . PHE A 1 525 ? 156.764 117.519 57.214 1.00 46.74 ? 525 PHE A O 1 ATOM 4186 C CB . PHE A 1 525 ? 155.295 118.614 60.025 1.00 40.63 ? 525 PHE A CB 1 ATOM 4187 C CG . PHE A 1 525 ? 155.711 117.198 60.290 1.00 48.06 ? 525 PHE A CG 1 ATOM 4188 C CD1 . PHE A 1 525 ? 157.039 116.897 60.593 1.00 51.62 ? 525 PHE A CD1 1 ATOM 4189 C CD2 . PHE A 1 525 ? 154.796 116.165 60.205 1.00 40.61 ? 525 PHE A CD2 1 ATOM 4190 C CE1 . PHE A 1 525 ? 157.435 115.591 60.822 1.00 53.61 ? 525 PHE A CE1 1 ATOM 4191 C CE2 . PHE A 1 525 ? 155.183 114.852 60.440 1.00 41.53 ? 525 PHE A CE2 1 ATOM 4192 C CZ . PHE A 1 525 ? 156.502 114.563 60.744 1.00 45.42 ? 525 PHE A CZ 1 ATOM 4193 N N . PHE A 1 526 ? 154.525 117.757 57.231 1.00 44.96 ? 526 PHE A N 1 ATOM 4194 C CA . PHE A 1 526 ? 154.284 116.633 56.317 1.00 43.09 ? 526 PHE A CA 1 ATOM 4195 C C . PHE A 1 526 ? 155.137 116.571 55.026 1.00 39.05 ? 526 PHE A C 1 ATOM 4196 O O . PHE A 1 526 ? 155.477 115.474 54.579 1.00 39.24 ? 526 PHE A O 1 ATOM 4197 C CB . PHE A 1 526 ? 152.779 116.470 56.006 1.00 34.47 ? 526 PHE A CB 1 ATOM 4198 C CG . PHE A 1 526 ? 152.428 115.144 55.376 1.00 31.27 ? 526 PHE A CG 1 ATOM 4199 C CD1 . PHE A 1 526 ? 152.351 113.989 56.143 1.00 35.72 ? 526 PHE A CD1 1 ATOM 4200 C CD2 . PHE A 1 526 ? 152.179 115.055 54.014 1.00 30.07 ? 526 PHE A CD2 1 ATOM 4201 C CE1 . PHE A 1 526 ? 152.033 112.762 55.560 1.00 37.59 ? 526 PHE A CE1 1 ATOM 4202 C CE2 . PHE A 1 526 ? 151.858 113.840 53.425 1.00 29.96 ? 526 PHE A CE2 1 ATOM 4203 C CZ . PHE A 1 526 ? 151.784 112.691 54.198 1.00 33.07 ? 526 PHE A CZ 1 ATOM 4204 N N . PRO A 1 527 ? 155.494 117.727 54.425 1.00 43.01 ? 527 PRO A N 1 ATOM 4205 C CA . PRO A 1 527 ? 156.348 117.629 53.230 1.00 47.07 ? 527 PRO A CA 1 ATOM 4206 C C . PRO A 1 527 ? 157.734 117.013 53.476 1.00 55.46 ? 527 PRO A C 1 ATOM 4207 O O . PRO A 1 527 ? 158.471 116.797 52.509 1.00 56.91 ? 527 PRO A O 1 ATOM 4208 C CB . PRO A 1 527 ? 156.515 119.090 52.796 1.00 48.95 ? 527 PRO A CB 1 ATOM 4209 C CG . PRO A 1 527 ? 155.311 119.785 53.322 1.00 52.58 ? 527 PRO A CG 1 ATOM 4210 C CD . PRO A 1 527 ? 155.004 119.105 54.627 1.00 49.17 ? 527 PRO A CD 1 ATOM 4211 N N . LYS A 1 528 ? 158.082 116.741 54.732 1.00 53.82 ? 528 LYS A N 1 ATOM 4212 C CA . LYS A 1 528 ? 159.394 116.189 55.060 1.00 56.60 ? 528 LYS A CA 1 ATOM 4213 C C . LYS A 1 528 ? 159.413 114.661 55.069 1.00 57.78 ? 528 LYS A C 1 ATOM 4214 O O . LYS A 1 528 ? 160.450 114.052 54.797 1.00 62.08 ? 528 LYS A O 1 ATOM 4215 C CB . LYS A 1 528 ? 159.875 116.727 56.410 1.00 56.43 ? 528 LYS A CB 1 ATOM 4216 C CG . LYS A 1 528 ? 159.973 118.237 56.454 1.00 57.72 ? 528 LYS A CG 1 ATOM 4217 C CD . LYS A 1 528 ? 160.251 118.732 57.862 1.00 61.10 ? 528 LYS A CD 1 ATOM 4218 C CE . LYS A 1 528 ? 160.281 120.249 57.905 1.00 65.31 ? 528 LYS A CE 1 ATOM 4219 N NZ . LYS A 1 528 ? 160.633 120.755 59.256 1.00 74.11 ? 528 LYS A NZ 1 ATOM 4220 N N . VAL A 1 529 ? 158.273 114.044 55.384 1.00 55.06 ? 529 VAL A N 1 ATOM 4221 C CA . VAL A 1 529 ? 158.192 112.582 55.463 1.00 65.94 ? 529 VAL A CA 1 ATOM 4222 C C . VAL A 1 529 ? 158.302 111.932 54.082 1.00 67.88 ? 529 VAL A C 1 ATOM 4223 O O . VAL A 1 529 ? 158.177 112.604 53.056 1.00 64.01 ? 529 VAL A O 1 ATOM 4224 C CB . VAL A 1 529 ? 156.882 112.090 56.146 1.00 53.18 ? 529 VAL A CB 1 ATOM 4225 C CG1 . VAL A 1 529 ? 156.590 112.885 57.413 1.00 47.61 ? 529 VAL A CG1 1 ATOM 4226 C CG2 . VAL A 1 529 ? 155.708 112.166 55.188 1.00 51.61 ? 529 VAL A CG2 1 ATOM 4227 O OXT . VAL A 1 529 ? 158.509 110.721 53.960 1.00 69.60 ? 529 VAL A OXT 1 HETATM 4228 C C1 . NAG B 2 . ? 122.543 127.448 10.062 1.00 69.92 ? 601 NAG A C1 1 HETATM 4229 C C2 . NAG B 2 . ? 122.424 126.635 8.781 1.00 80.95 ? 601 NAG A C2 1 HETATM 4230 C C3 . NAG B 2 . ? 121.446 127.355 7.861 1.00 87.10 ? 601 NAG A C3 1 HETATM 4231 C C4 . NAG B 2 . ? 120.093 127.448 8.561 1.00 87.60 ? 601 NAG A C4 1 HETATM 4232 C C5 . NAG B 2 . ? 120.207 128.017 9.979 1.00 83.87 ? 601 NAG A C5 1 HETATM 4233 C C6 . NAG B 2 . ? 118.904 127.808 10.755 1.00 81.09 ? 601 NAG A C6 1 HETATM 4234 C C7 . NAG B 2 . ? 124.235 125.155 8.090 1.00 79.42 ? 601 NAG A C7 1 HETATM 4235 C C8 . NAG B 2 . ? 123.490 124.051 8.783 1.00 75.96 ? 601 NAG A C8 1 HETATM 4236 N N2 . NAG B 2 . ? 123.722 126.387 8.168 1.00 79.99 ? 601 NAG A N2 1 HETATM 4237 O O3 . NAG B 2 . ? 121.312 126.652 6.647 1.00 90.20 ? 601 NAG A O3 1 HETATM 4238 O O4 . NAG B 2 . ? 119.222 128.258 7.800 1.00 91.58 ? 601 NAG A O4 1 HETATM 4239 O O5 . NAG B 2 . ? 121.281 127.435 10.710 1.00 79.86 ? 601 NAG A O5 1 HETATM 4240 O O6 . NAG B 2 . ? 117.862 128.587 10.204 1.00 77.84 ? 601 NAG A O6 1 HETATM 4241 O O7 . NAG B 2 . ? 125.274 124.898 7.483 1.00 82.61 ? 601 NAG A O7 1 HETATM 4242 C C1 . NAG C 2 . ? 136.370 150.189 26.690 1.00 61.17 ? 611 NAG A C1 1 HETATM 4243 C C2 . NAG C 2 . ? 136.485 151.081 25.431 1.00 66.79 ? 611 NAG A C2 1 HETATM 4244 C C3 . NAG C 2 . ? 137.924 151.412 25.009 1.00 68.00 ? 611 NAG A C3 1 HETATM 4245 C C4 . NAG C 2 . ? 138.716 151.892 26.210 1.00 73.07 ? 611 NAG A C4 1 HETATM 4246 C C5 . NAG C 2 . ? 138.643 150.739 27.193 1.00 76.28 ? 611 NAG A C5 1 HETATM 4247 C C6 . NAG C 2 . ? 139.626 150.896 28.341 1.00 81.09 ? 611 NAG A C6 1 HETATM 4248 C C7 . NAG C 2 . ? 134.594 151.012 23.952 1.00 68.09 ? 611 NAG A C7 1 HETATM 4249 C C8 . NAG C 2 . ? 134.182 150.839 22.519 1.00 67.47 ? 611 NAG A C8 1 HETATM 4250 N N2 . NAG C 2 . ? 135.767 150.505 24.309 1.00 67.25 ? 611 NAG A N2 1 HETATM 4251 O O3 . NAG C 2 . ? 137.947 152.401 24.007 1.00 66.40 ? 611 NAG A O3 1 HETATM 4252 O O4 . NAG C 2 . ? 140.056 152.183 25.870 1.00 72.26 ? 611 NAG A O4 1 HETATM 4253 O O5 . NAG C 2 . ? 137.314 150.613 27.669 1.00 70.23 ? 611 NAG A O5 1 HETATM 4254 O O6 . NAG C 2 . ? 139.771 149.631 28.944 1.00 86.01 ? 611 NAG A O6 1 HETATM 4255 O O7 . NAG C 2 . ? 133.869 151.601 24.752 1.00 69.65 ? 611 NAG A O7 1 HETATM 4256 C C1 . FUC D 3 . ? 139.021 150.490 31.739 1.00 110.49 ? 612 FUC A C1 1 HETATM 4257 C C2 . FUC D 3 . ? 137.624 149.983 32.179 1.00 112.37 ? 612 FUC A C2 1 HETATM 4258 C C3 . FUC D 3 . ? 137.602 148.473 32.478 1.00 110.80 ? 612 FUC A C3 1 HETATM 4259 C C4 . FUC D 3 . ? 138.814 148.068 33.314 1.00 110.72 ? 612 FUC A C4 1 HETATM 4260 C C5 . FUC D 3 . ? 140.069 148.422 32.534 1.00 108.47 ? 612 FUC A C5 1 HETATM 4261 C C6 . FUC D 3 . ? 141.352 148.036 33.257 1.00 105.54 ? 612 FUC A C6 1 HETATM 4262 O O2 . FUC D 3 . ? 136.620 150.315 31.211 1.00 115.14 ? 612 FUC A O2 1 HETATM 4263 O O3 . FUC D 3 . ? 136.432 148.138 33.219 1.00 110.46 ? 612 FUC A O3 1 HETATM 4264 O O4 . FUC D 3 . ? 138.802 148.764 34.558 1.00 113.76 ? 612 FUC A O4 1 HETATM 4265 O O5 . FUC D 3 . ? 140.143 149.842 32.323 1.00 109.66 ? 612 FUC A O5 1 HETATM 4266 C C1 . NAG E 2 . ? 157.727 103.172 37.012 1.00 63.91 ? 621 NAG A C1 1 HETATM 4267 C C2 . NAG E 2 . ? 157.296 102.964 38.465 1.00 72.63 ? 621 NAG A C2 1 HETATM 4268 C C3 . NAG E 2 . ? 157.584 101.548 38.962 1.00 75.12 ? 621 NAG A C3 1 HETATM 4269 C C4 . NAG E 2 . ? 156.999 100.493 38.030 1.00 76.83 ? 621 NAG A C4 1 HETATM 4270 C C5 . NAG E 2 . ? 157.382 100.785 36.574 1.00 72.85 ? 621 NAG A C5 1 HETATM 4271 C C6 . NAG E 2 . ? 156.534 99.958 35.610 1.00 67.98 ? 621 NAG A C6 1 HETATM 4272 C C7 . NAG E 2 . ? 157.304 104.846 40.031 1.00 84.77 ? 621 NAG A C7 1 HETATM 4273 C C8 . NAG E 2 . ? 156.122 104.387 40.837 1.00 82.84 ? 621 NAG A C8 1 HETATM 4274 N N2 . NAG E 2 . ? 157.963 103.927 39.324 1.00 80.18 ? 621 NAG A N2 1 HETATM 4275 O O3 . NAG E 2 . ? 157.048 101.388 40.259 1.00 74.75 ? 621 NAG A O3 1 HETATM 4276 O O4 . NAG E 2 . ? 157.446 99.198 38.419 1.00 81.40 ? 621 NAG A O4 1 HETATM 4277 O O5 . NAG E 2 . ? 157.217 102.141 36.183 1.00 71.86 ? 621 NAG A O5 1 HETATM 4278 O O6 . NAG E 2 . ? 155.662 99.126 36.348 1.00 66.01 ? 621 NAG A O6 1 HETATM 4279 O O7 . NAG E 2 . ? 157.635 106.032 40.046 1.00 88.76 ? 621 NAG A O7 1 HETATM 4280 C C1 . FUL F 4 . ? 154.608 98.484 35.585 1.00 67.61 ? 622 FUL A C1 1 HETATM 4281 C C2 . FUL F 4 . ? 154.591 98.884 34.058 1.00 82.56 ? 622 FUL A C2 1 HETATM 4282 O O2 . FUL F 4 . ? 155.637 98.245 33.302 1.00 88.64 ? 622 FUL A O2 1 HETATM 4283 C C3 . FUL F 4 . ? 153.232 98.601 33.397 1.00 78.38 ? 622 FUL A C3 1 HETATM 4284 O O3 . FUL F 4 . ? 153.163 99.235 32.115 1.00 75.57 ? 622 FUL A O3 1 HETATM 4285 C C4 . FUL F 4 . ? 152.087 99.126 34.262 1.00 78.30 ? 622 FUL A C4 1 HETATM 4286 O O4 . FUL F 4 . ? 152.233 100.527 34.457 1.00 85.24 ? 622 FUL A O4 1 HETATM 4287 C C5 . FUL F 4 . ? 152.129 98.406 35.606 1.00 71.44 ? 622 FUL A C5 1 HETATM 4288 C C6 . FUL F 4 . ? 151.009 98.830 36.569 1.00 63.93 ? 622 FUL A C6 1 HETATM 4289 O O5 . FUL F 4 . ? 153.374 98.664 36.289 1.00 70.49 ? 622 FUL A O5 1 HETATM 4290 C C1 . NAG G 2 . ? 156.517 98.520 39.306 1.00 86.43 ? 623 NAG A C1 1 HETATM 4291 C C2 . NAG G 2 . ? 156.591 97.000 39.085 1.00 91.93 ? 623 NAG A C2 1 HETATM 4292 C C3 . NAG G 2 . ? 156.107 96.128 40.244 1.00 92.89 ? 623 NAG A C3 1 HETATM 4293 C C4 . NAG G 2 . ? 156.307 96.747 41.617 1.00 93.40 ? 623 NAG A C4 1 HETATM 4294 C C5 . NAG G 2 . ? 155.903 98.216 41.588 1.00 91.51 ? 623 NAG A C5 1 HETATM 4295 C C6 . NAG G 2 . ? 156.082 98.871 42.954 1.00 94.51 ? 623 NAG A C6 1 HETATM 4296 C C7 . NAG G 2 . ? 156.063 95.610 37.144 1.00 96.81 ? 623 NAG A C7 1 HETATM 4297 C C8 . NAG G 2 . ? 155.067 94.484 37.142 1.00 94.97 ? 623 NAG A C8 1 HETATM 4298 N N2 . NAG G 2 . ? 155.783 96.641 37.937 1.00 95.93 ? 623 NAG A N2 1 HETATM 4299 O O3 . NAG G 2 . ? 156.791 94.897 40.187 1.00 93.29 ? 623 NAG A O3 1 HETATM 4300 O O4 . NAG G 2 . ? 155.522 96.038 42.554 1.00 92.88 ? 623 NAG A O4 1 HETATM 4301 O O5 . NAG G 2 . ? 156.718 98.893 40.656 1.00 87.54 ? 623 NAG A O5 1 HETATM 4302 O O6 . NAG G 2 . ? 157.452 99.133 43.177 1.00 97.78 ? 623 NAG A O6 1 HETATM 4303 O O7 . NAG G 2 . ? 157.072 95.565 36.437 1.00 96.81 ? 623 NAG A O7 1 HETATM 4304 C C1 . NAG H 2 . ? 164.031 109.524 15.391 1.00 75.85 ? 631 NAG A C1 1 HETATM 4305 C C2 . NAG H 2 . ? 165.283 110.344 15.060 1.00 82.68 ? 631 NAG A C2 1 HETATM 4306 C C3 . NAG H 2 . ? 164.971 111.633 14.291 1.00 86.00 ? 631 NAG A C3 1 HETATM 4307 C C4 . NAG H 2 . ? 163.919 111.441 13.202 1.00 84.05 ? 631 NAG A C4 1 HETATM 4308 C C5 . NAG H 2 . ? 162.723 110.672 13.754 1.00 83.29 ? 631 NAG A C5 1 HETATM 4309 C C6 . NAG H 2 . ? 161.633 110.480 12.694 1.00 81.73 ? 631 NAG A C6 1 HETATM 4310 C C7 . NAG H 2 . ? 166.898 109.923 16.850 1.00 91.24 ? 631 NAG A C7 1 HETATM 4311 C C8 . NAG H 2 . ? 167.287 110.255 18.262 1.00 91.28 ? 631 NAG A C8 1 HETATM 4312 N N2 . NAG H 2 . ? 165.957 110.687 16.300 1.00 87.11 ? 631 NAG A N2 1 HETATM 4313 O O3 . NAG H 2 . ? 166.153 112.138 13.705 1.00 88.56 ? 631 NAG A O3 1 HETATM 4314 O O4 . NAG H 2 . ? 163.500 112.698 12.710 1.00 79.55 ? 631 NAG A O4 1 HETATM 4315 O O5 . NAG H 2 . ? 163.162 109.424 14.270 1.00 82.59 ? 631 NAG A O5 1 HETATM 4316 O O6 . NAG H 2 . ? 162.082 109.663 11.631 1.00 81.71 ? 631 NAG A O6 1 HETATM 4317 O O7 . NAG H 2 . ? 167.436 108.988 16.258 1.00 93.29 ? 631 NAG A O7 1 HETATM 4318 C C1 . NAG I 2 . ? 127.562 100.975 55.147 1.00 34.77 ? 641 NAG A C1 1 HETATM 4319 C C2 . NAG I 2 . ? 127.750 100.020 56.320 1.00 41.34 ? 641 NAG A C2 1 HETATM 4320 C C3 . NAG I 2 . ? 129.067 99.270 56.211 1.00 47.68 ? 641 NAG A C3 1 HETATM 4321 C C4 . NAG I 2 . ? 129.382 98.709 54.836 1.00 54.06 ? 641 NAG A C4 1 HETATM 4322 C C5 . NAG I 2 . ? 129.052 99.748 53.769 1.00 52.09 ? 641 NAG A C5 1 HETATM 4323 C C6 . NAG I 2 . ? 129.157 99.176 52.360 1.00 62.37 ? 641 NAG A C6 1 HETATM 4324 C C7 . NAG I 2 . ? 126.754 100.997 58.323 1.00 56.94 ? 641 NAG A C7 1 HETATM 4325 C C8 . NAG I 2 . ? 125.616 100.025 58.249 1.00 58.19 ? 641 NAG A C8 1 HETATM 4326 N N2 . NAG I 2 . ? 127.811 100.760 57.557 1.00 47.96 ? 641 NAG A N2 1 HETATM 4327 O O3 . NAG I 2 . ? 129.108 98.236 57.161 1.00 52.20 ? 641 NAG A O3 1 HETATM 4328 O O4 . NAG I 2 . ? 130.781 98.582 54.903 1.00 66.92 ? 641 NAG A O4 1 HETATM 4329 O O5 . NAG I 2 . ? 127.754 100.265 53.938 1.00 44.52 ? 641 NAG A O5 1 HETATM 4330 O O6 . NAG I 2 . ? 128.432 97.968 52.290 1.00 74.19 ? 641 NAG A O6 1 HETATM 4331 O O7 . NAG I 2 . ? 126.701 101.972 59.069 1.00 64.41 ? 641 NAG A O7 1 HETATM 4332 C C1 . FUL J 4 . ? 128.020 97.747 50.924 1.00 81.61 ? 642 FUL A C1 1 HETATM 4333 C C2 . FUL J 4 . ? 126.882 98.715 50.525 1.00 84.09 ? 642 FUL A C2 1 HETATM 4334 O O2 . FUL J 4 . ? 126.946 99.105 49.153 1.00 87.37 ? 642 FUL A O2 1 HETATM 4335 C C3 . FUL J 4 . ? 125.460 98.204 50.905 1.00 109.47 ? 642 FUL A C3 1 HETATM 4336 O O3 . FUL J 4 . ? 125.152 98.511 52.266 1.00 109.71 ? 642 FUL A O3 1 HETATM 4337 C C4 . FUL J 4 . ? 125.241 96.681 50.684 1.00 91.38 ? 642 FUL A C4 1 HETATM 4338 O O4 . FUL J 4 . ? 124.147 96.256 51.476 1.00 94.23 ? 642 FUL A O4 1 HETATM 4339 C C5 . FUL J 4 . ? 126.479 95.817 51.041 1.00 78.13 ? 642 FUL A C5 1 HETATM 4340 C C6 . FUL J 4 . ? 126.581 95.457 52.528 1.00 75.10 ? 642 FUL A C6 1 HETATM 4341 O O5 . FUL J 4 . ? 127.757 96.384 50.628 1.00 82.34 ? 642 FUL A O5 1 HETATM 4342 C C1 . NAG K 2 . ? 131.419 97.379 54.420 1.00 73.14 ? 643 NAG A C1 1 HETATM 4343 C C2 . NAG K 2 . ? 130.752 96.027 54.651 1.00 79.02 ? 643 NAG A C2 1 HETATM 4344 C C3 . NAG K 2 . ? 131.826 94.978 54.349 1.00 75.96 ? 643 NAG A C3 1 HETATM 4345 C C4 . NAG K 2 . ? 132.542 95.220 53.014 1.00 70.64 ? 643 NAG A C4 1 HETATM 4346 C C5 . NAG K 2 . ? 132.849 96.697 52.753 1.00 76.36 ? 643 NAG A C5 1 HETATM 4347 C C6 . NAG K 2 . ? 133.280 96.972 51.315 1.00 81.56 ? 643 NAG A C6 1 HETATM 4348 C C7 . NAG K 2 . ? 129.293 94.925 56.249 1.00 89.66 ? 643 NAG A C7 1 HETATM 4349 C C8 . NAG K 2 . ? 128.233 95.277 57.254 1.00 88.43 ? 643 NAG A C8 1 HETATM 4350 N N2 . NAG K 2 . ? 130.238 95.840 56.000 1.00 85.59 ? 643 NAG A N2 1 HETATM 4351 O O3 . NAG K 2 . ? 131.246 93.689 54.350 1.00 75.97 ? 643 NAG A O3 1 HETATM 4352 O O4 . NAG K 2 . ? 133.760 94.509 53.021 1.00 57.60 ? 643 NAG A O4 1 HETATM 4353 O O5 . NAG K 2 . ? 131.712 97.469 53.044 1.00 75.00 ? 643 NAG A O5 1 HETATM 4354 O O6 . NAG K 2 . ? 134.490 96.300 51.039 1.00 87.48 ? 643 NAG A O6 1 HETATM 4355 O O7 . NAG K 2 . ? 129.266 93.823 55.692 1.00 88.65 ? 643 NAG A O7 1 HETATM 4356 C C1 . NAG L 2 . ? 119.111 143.804 47.526 1.00 61.21 ? 651 NAG A C1 1 HETATM 4357 C C2 . NAG L 2 . ? 119.274 142.632 46.557 1.00 62.84 ? 651 NAG A C2 1 HETATM 4358 C C3 . NAG L 2 . ? 118.034 142.481 45.681 1.00 69.17 ? 651 NAG A C3 1 HETATM 4359 C C4 . NAG L 2 . ? 116.773 142.412 46.540 1.00 73.10 ? 651 NAG A C4 1 HETATM 4360 C C5 . NAG L 2 . ? 116.736 143.606 47.491 1.00 75.75 ? 651 NAG A C5 1 HETATM 4361 C C6 . NAG L 2 . ? 115.502 143.574 48.395 1.00 77.56 ? 651 NAG A C6 1 HETATM 4362 C C7 . NAG L 2 . ? 121.513 142.020 45.822 1.00 51.43 ? 651 NAG A C7 1 HETATM 4363 C C8 . NAG L 2 . ? 122.656 142.322 44.897 1.00 44.72 ? 651 NAG A C8 1 HETATM 4364 N N2 . NAG L 2 . ? 120.454 142.823 45.735 1.00 57.43 ? 651 NAG A N2 1 HETATM 4365 O O3 . NAG L 2 . ? 118.162 141.319 44.892 1.00 71.41 ? 651 NAG A O3 1 HETATM 4366 O O4 . NAG L 2 . ? 115.612 142.403 45.732 1.00 70.56 ? 651 NAG A O4 1 HETATM 4367 O O5 . NAG L 2 . ? 117.918 143.633 48.275 1.00 72.06 ? 651 NAG A O5 1 HETATM 4368 O O6 . NAG L 2 . ? 115.531 144.659 49.299 1.00 78.63 ? 651 NAG A O6 1 HETATM 4369 O O7 . NAG L 2 . ? 121.581 141.069 46.605 1.00 52.12 ? 651 NAG A O7 1 HETATM 4370 C C1 . THA M 5 . ? 131.196 114.029 43.859 1.00 29.85 ? 701 THA A C1 1 HETATM 4371 C C2 . THA M 5 . ? 131.668 115.318 43.693 1.00 33.29 ? 701 THA A C2 1 HETATM 4372 C C3 . THA M 5 . ? 132.327 115.694 42.470 1.00 32.69 ? 701 THA A C3 1 HETATM 4373 C C4 . THA M 5 . ? 132.482 114.734 41.448 1.00 33.99 ? 701 THA A C4 1 HETATM 4374 C C5 . THA M 5 . ? 131.983 113.393 41.663 1.00 31.96 ? 701 THA A C5 1 HETATM 4375 C C6 . THA M 5 . ? 131.364 113.073 42.839 1.00 30.08 ? 701 THA A C6 1 HETATM 4376 N N7 . THA M 5 . ? 132.768 117.012 42.362 1.00 31.25 ? 701 THA A N7 1 HETATM 4377 C C8 . THA M 5 . ? 133.388 117.387 41.226 1.00 26.30 ? 701 THA A C8 1 HETATM 4378 C C9 . THA M 5 . ? 133.610 116.528 40.127 1.00 32.91 ? 701 THA A C9 1 HETATM 4379 C C10 . THA M 5 . ? 133.144 115.175 40.243 1.00 36.33 ? 701 THA A C10 1 HETATM 4380 C C11 . THA M 5 . ? 133.855 118.839 41.176 1.00 29.92 ? 701 THA A C11 1 HETATM 4381 C C12 . THA M 5 . ? 134.956 119.153 40.164 1.00 33.78 ? 701 THA A C12 1 HETATM 4382 C C13 . THA M 5 . ? 134.556 118.575 38.811 1.00 35.00 ? 701 THA A C13 1 HETATM 4383 C C14 . THA M 5 . ? 134.299 117.033 38.902 1.00 30.32 ? 701 THA A C14 1 HETATM 4384 N N15 . THA M 5 . ? 133.321 114.260 39.233 1.00 31.47 ? 701 THA A N15 1 HETATM 4385 C C1 . GOL N 6 . ? 121.280 125.394 26.699 1.00 44.99 ? 702 GOL A C1 1 HETATM 4386 O O1 . GOL N 6 . ? 120.731 125.302 25.407 1.00 58.05 ? 702 GOL A O1 1 HETATM 4387 C C2 . GOL N 6 . ? 121.226 126.851 27.139 1.00 39.12 ? 702 GOL A C2 1 HETATM 4388 O O2 . GOL N 6 . ? 120.394 126.957 28.284 1.00 37.14 ? 702 GOL A O2 1 HETATM 4389 C C3 . GOL N 6 . ? 122.654 127.309 27.461 1.00 37.70 ? 702 GOL A C3 1 HETATM 4390 O O3 . GOL N 6 . ? 122.650 128.674 27.812 1.00 34.58 ? 702 GOL A O3 1 HETATM 4391 S S . SO4 O 7 . ? 146.166 146.145 44.627 0.67 34.89 ? 703 SO4 A S 1 HETATM 4392 O O1 . SO4 O 7 . ? 145.922 146.943 43.435 0.67 37.70 ? 703 SO4 A O1 1 HETATM 4393 O O2 . SO4 O 7 . ? 146.061 144.702 44.327 0.67 27.17 ? 703 SO4 A O2 1 HETATM 4394 O O3 . SO4 O 7 . ? 145.177 146.484 45.642 0.67 38.05 ? 703 SO4 A O3 1 HETATM 4395 O O4 . SO4 O 7 . ? 147.500 146.455 45.123 0.67 33.58 ? 703 SO4 A O4 1 HETATM 4396 S S . SO4 P 7 . ? 149.591 112.093 41.405 1.00 81.61 ? 704 SO4 A S 1 HETATM 4397 O O1 . SO4 P 7 . ? 150.618 112.489 40.436 1.00 71.82 ? 704 SO4 A O1 1 HETATM 4398 O O2 . SO4 P 7 . ? 148.623 111.174 40.810 1.00 75.54 ? 704 SO4 A O2 1 HETATM 4399 O O3 . SO4 P 7 . ? 150.232 111.440 42.543 1.00 87.39 ? 704 SO4 A O3 1 HETATM 4400 O O4 . SO4 P 7 . ? 148.875 113.279 41.865 1.00 85.57 ? 704 SO4 A O4 1 HETATM 4401 CL CL . CL Q 8 . ? 125.444 139.898 55.159 1.00 60.39 ? 705 CL A CL 1 HETATM 4402 CL CL . CL R 8 . ? 134.116 123.721 60.244 1.00 63.14 ? 706 CL A CL 1 HETATM 4403 C C . FPK S 9 . ? 138.932 117.420 40.915 1.00 52.49 ? 710 FPK A C 1 HETATM 4404 N N . FPK S 9 . ? 139.753 115.030 40.920 1.00 48.82 ? 710 FPK A N 1 HETATM 4405 O O . FPK S 9 . ? 137.671 117.570 41.304 1.00 55.89 ? 710 FPK A O 1 HETATM 4406 C CA . FPK S 9 . ? 139.829 116.296 41.594 1.00 43.78 ? 710 FPK A CA 1 HETATM 4407 C CB . FPK S 9 . ? 141.263 116.673 41.715 1.00 39.52 ? 710 FPK A CB 1 HETATM 4408 C CC . FPK S 9 . ? 141.971 115.444 41.657 1.00 34.70 ? 710 FPK A CC 1 HETATM 4409 C CD . FPK S 9 . ? 141.033 114.370 41.133 1.00 39.03 ? 710 FPK A CD 1 HETATM 4410 C CE . FPK S 9 . ? 138.583 114.460 40.145 1.00 53.83 ? 710 FPK A CE 1 HETATM 4411 O OE . FPK S 9 . ? 137.488 115.082 40.001 1.00 53.15 ? 710 FPK A OE 1 HETATM 4412 O OXT . FPK S 9 . ? 139.482 118.411 39.960 1.00 42.03 ? 710 FPK A OXT 1 HETATM 4413 X UNK . UNX T 10 . ? 135.605 112.912 42.092 1.00 81.23 ? 711 UNX A UNK 1 HETATM 4414 X UNK . UNX U 10 . ? 136.387 112.099 41.284 1.00 81.30 ? 712 UNX A UNK 1 HETATM 4415 X UNK . UNX V 10 . ? 136.606 110.787 42.053 1.00 77.56 ? 713 UNX A UNK 1 HETATM 4416 X UNK . UNX W 10 . ? 137.497 109.874 41.228 1.00 75.90 ? 714 UNX A UNK 1 HETATM 4417 X UNK . UNX X 10 . ? 137.769 108.543 41.912 1.00 71.14 ? 715 UNX A UNK 1 HETATM 4418 X UNK . UNX Y 10 . ? 137.971 107.436 40.861 1.00 66.51 ? 716 UNX A UNK 1 HETATM 4419 X UNK . UNX Z 10 . ? 138.384 106.315 41.564 1.00 61.45 ? 717 UNX A UNK 1 HETATM 4420 O O . HOH AA 11 . ? 119.642 137.563 12.375 1.00 66.97 ? 2001 HOH A O 1 HETATM 4421 O O . HOH AA 11 . ? 141.110 134.629 15.963 1.00 51.02 ? 2002 HOH A O 1 HETATM 4422 O O . HOH AA 11 . ? 132.416 134.060 7.154 1.00 54.78 ? 2003 HOH A O 1 HETATM 4423 O O . HOH AA 11 . ? 130.715 121.020 15.859 1.00 62.93 ? 2004 HOH A O 1 HETATM 4424 O O . HOH AA 11 . ? 117.167 132.487 18.136 1.00 50.84 ? 2005 HOH A O 1 HETATM 4425 O O . HOH AA 11 . ? 115.912 130.487 31.621 1.00 49.57 ? 2006 HOH A O 1 HETATM 4426 O O . HOH AA 11 . ? 156.049 122.169 21.230 1.00 51.34 ? 2007 HOH A O 1 HETATM 4427 O O . HOH AA 11 . ? 111.239 134.361 31.587 1.00 56.62 ? 2008 HOH A O 1 HETATM 4428 O O . HOH AA 11 . ? 113.859 132.635 33.021 1.00 50.96 ? 2009 HOH A O 1 HETATM 4429 O O . HOH AA 11 . ? 127.980 123.760 17.672 1.00 52.46 ? 2010 HOH A O 1 HETATM 4430 O O . HOH AA 11 . ? 130.239 123.829 16.457 1.00 56.41 ? 2011 HOH A O 1 HETATM 4431 O O . HOH AA 11 . ? 135.207 111.552 37.102 1.00 35.43 ? 2012 HOH A O 1 HETATM 4432 O O . HOH AA 11 . ? 138.063 123.199 16.420 1.00 28.84 ? 2013 HOH A O 1 HETATM 4433 O O . HOH AA 11 . ? 117.557 114.564 39.804 1.00 59.55 ? 2014 HOH A O 1 HETATM 4434 O O . HOH AA 11 . ? 123.220 119.580 37.128 1.00 40.52 ? 2015 HOH A O 1 HETATM 4435 O O . HOH AA 11 . ? 120.629 119.398 41.778 1.00 58.70 ? 2016 HOH A O 1 HETATM 4436 O O . HOH AA 11 . ? 145.640 121.956 16.461 1.00 34.13 ? 2017 HOH A O 1 HETATM 4437 O O . HOH AA 11 . ? 142.949 118.688 11.790 1.00 45.39 ? 2018 HOH A O 1 HETATM 4438 O O . HOH AA 11 . ? 143.770 114.686 20.203 1.00 27.82 ? 2019 HOH A O 1 HETATM 4439 O O . HOH AA 11 . ? 144.922 116.906 11.439 1.00 57.47 ? 2020 HOH A O 1 HETATM 4440 O O . HOH AA 11 . ? 143.690 111.132 16.020 1.00 39.66 ? 2021 HOH A O 1 HETATM 4441 O O . HOH AA 11 . ? 146.313 110.588 15.867 1.00 46.54 ? 2022 HOH A O 1 HETATM 4442 O O . HOH AA 11 . ? 147.131 113.490 9.500 1.00 50.29 ? 2023 HOH A O 1 HETATM 4443 O O . HOH AA 11 . ? 152.550 114.325 17.533 1.00 39.74 ? 2024 HOH A O 1 HETATM 4444 O O . HOH AA 11 . ? 147.358 119.950 17.921 1.00 29.02 ? 2025 HOH A O 1 HETATM 4445 O O . HOH AA 11 . ? 145.995 115.427 21.563 1.00 24.75 ? 2026 HOH A O 1 HETATM 4446 O O . HOH AA 11 . ? 153.759 120.920 19.985 1.00 48.82 ? 2027 HOH A O 1 HETATM 4447 O O . HOH AA 11 . ? 152.741 128.983 22.075 1.00 52.38 ? 2028 HOH A O 1 HETATM 4448 O O . HOH AA 11 . ? 154.554 126.173 18.857 1.00 51.80 ? 2029 HOH A O 1 HETATM 4449 O O . HOH AA 11 . ? 149.898 126.832 20.730 1.00 47.17 ? 2030 HOH A O 1 HETATM 4450 O O . HOH AA 11 . ? 150.068 127.366 14.584 1.00 53.92 ? 2031 HOH A O 1 HETATM 4451 O O . HOH AA 11 . ? 128.012 125.162 10.869 1.00 56.24 ? 2032 HOH A O 1 HETATM 4452 O O . HOH AA 11 . ? 123.176 122.506 22.837 1.00 41.14 ? 2033 HOH A O 1 HETATM 4453 O O . HOH AA 11 . ? 127.453 118.522 19.195 1.00 45.71 ? 2034 HOH A O 1 HETATM 4454 O O . HOH AA 11 . ? 127.195 124.845 30.126 1.00 26.63 ? 2035 HOH A O 1 HETATM 4455 O O . HOH AA 11 . ? 130.526 123.973 23.206 1.00 35.03 ? 2036 HOH A O 1 HETATM 4456 O O . HOH AA 11 . ? 130.792 120.589 24.998 1.00 27.57 ? 2037 HOH A O 1 HETATM 4457 O O . HOH AA 11 . ? 131.112 119.359 17.803 1.00 41.73 ? 2038 HOH A O 1 HETATM 4458 O O . HOH AA 11 . ? 128.277 116.480 20.114 1.00 36.60 ? 2039 HOH A O 1 HETATM 4459 O O . HOH AA 11 . ? 135.634 118.701 27.060 1.00 25.11 ? 2040 HOH A O 1 HETATM 4460 O O . HOH AA 11 . ? 140.342 114.552 23.350 1.00 30.83 ? 2041 HOH A O 1 HETATM 4461 O O . HOH AA 11 . ? 140.972 114.697 26.041 1.00 29.89 ? 2042 HOH A O 1 HETATM 4462 O O . HOH AA 11 . ? 135.156 107.308 27.268 1.00 37.78 ? 2043 HOH A O 1 HETATM 4463 O O . HOH AA 11 . ? 134.146 111.982 32.637 1.00 26.98 ? 2044 HOH A O 1 HETATM 4464 O O . HOH AA 11 . ? 132.464 115.922 31.657 1.00 39.99 ? 2045 HOH A O 1 HETATM 4465 O O . HOH AA 11 . ? 140.213 110.573 31.176 1.00 32.72 ? 2046 HOH A O 1 HETATM 4466 O O . HOH AA 11 . ? 141.994 104.136 32.335 1.00 48.33 ? 2047 HOH A O 1 HETATM 4467 O O . HOH AA 11 . ? 136.672 109.131 36.029 1.00 50.94 ? 2048 HOH A O 1 HETATM 4468 O O . HOH AA 11 . ? 135.162 105.205 31.432 1.00 45.04 ? 2049 HOH A O 1 HETATM 4469 O O . HOH AA 11 . ? 135.748 104.245 33.686 1.00 68.42 ? 2050 HOH A O 1 HETATM 4470 O O . HOH AA 11 . ? 134.041 104.800 36.952 1.00 39.30 ? 2051 HOH A O 1 HETATM 4471 O O . HOH AA 11 . ? 128.400 106.976 38.421 1.00 33.10 ? 2052 HOH A O 1 HETATM 4472 O O . HOH AA 11 . ? 126.971 106.340 35.816 1.00 45.18 ? 2053 HOH A O 1 HETATM 4473 O O . HOH AA 11 . ? 134.723 106.101 39.043 1.00 51.34 ? 2054 HOH A O 1 HETATM 4474 O O . HOH AA 11 . ? 134.720 110.107 39.357 1.00 66.97 ? 2055 HOH A O 1 HETATM 4475 O O . HOH AA 11 . ? 131.201 112.112 38.787 1.00 22.80 ? 2056 HOH A O 1 HETATM 4476 O O . HOH AA 11 . ? 119.399 110.100 40.915 1.00 42.88 ? 2057 HOH A O 1 HETATM 4477 O O . HOH AA 11 . ? 121.447 110.492 37.012 1.00 36.60 ? 2058 HOH A O 1 HETATM 4478 O O . HOH AA 11 . ? 118.349 116.454 38.257 1.00 59.71 ? 2059 HOH A O 1 HETATM 4479 O O . HOH AA 11 . ? 122.116 119.837 39.488 1.00 46.80 ? 2060 HOH A O 1 HETATM 4480 O O . HOH AA 11 . ? 125.091 111.382 32.319 1.00 58.72 ? 2061 HOH A O 1 HETATM 4481 O O . HOH AA 11 . ? 125.936 115.457 32.458 1.00 44.62 ? 2062 HOH A O 1 HETATM 4482 O O . HOH AA 11 . ? 125.616 119.566 35.521 1.00 30.93 ? 2063 HOH A O 1 HETATM 4483 O O . HOH AA 11 . ? 133.002 117.107 35.194 1.00 19.49 ? 2064 HOH A O 1 HETATM 4484 O O . HOH AA 11 . ? 133.281 112.344 35.166 1.00 30.22 ? 2065 HOH A O 1 HETATM 4485 O O . HOH AA 11 . ? 126.629 109.515 32.723 1.00 44.97 ? 2066 HOH A O 1 HETATM 4486 O O . HOH AA 11 . ? 128.299 110.496 30.021 1.00 42.14 ? 2067 HOH A O 1 HETATM 4487 O O . HOH AA 11 . ? 125.153 112.589 30.055 1.00 37.80 ? 2068 HOH A O 1 HETATM 4488 O O . HOH AA 11 . ? 129.188 109.688 20.736 1.00 38.63 ? 2069 HOH A O 1 HETATM 4489 O O . HOH AA 11 . ? 130.644 109.666 22.774 1.00 31.11 ? 2070 HOH A O 1 HETATM 4490 O O . HOH AA 11 . ? 137.638 111.402 17.738 1.00 39.00 ? 2071 HOH A O 1 HETATM 4491 O O . HOH AA 11 . ? 141.526 115.888 21.343 1.00 27.02 ? 2072 HOH A O 1 HETATM 4492 O O . HOH AA 11 . ? 139.582 110.211 16.537 1.00 35.51 ? 2073 HOH A O 1 HETATM 4493 O O . HOH AA 11 . ? 138.443 120.571 17.480 1.00 29.25 ? 2074 HOH A O 1 HETATM 4494 O O . HOH AA 11 . ? 134.639 115.264 14.025 1.00 49.62 ? 2075 HOH A O 1 HETATM 4495 O O . HOH AA 11 . ? 135.439 119.999 12.646 1.00 58.80 ? 2076 HOH A O 1 HETATM 4496 O O . HOH AA 11 . ? 136.783 123.028 14.026 1.00 43.66 ? 2077 HOH A O 1 HETATM 4497 O O . HOH AA 11 . ? 131.078 123.193 25.418 1.00 33.81 ? 2078 HOH A O 1 HETATM 4498 O O . HOH AA 11 . ? 120.649 143.733 29.660 1.00 44.42 ? 2079 HOH A O 1 HETATM 4499 O O . HOH AA 11 . ? 128.496 146.948 21.224 1.00 57.69 ? 2080 HOH A O 1 HETATM 4500 O O . HOH AA 11 . ? 126.273 148.134 27.985 1.00 44.85 ? 2081 HOH A O 1 HETATM 4501 O O . HOH AA 11 . ? 122.410 152.472 24.790 1.00 42.96 ? 2082 HOH A O 1 HETATM 4502 O O . HOH AA 11 . ? 134.324 146.834 31.192 1.00 36.79 ? 2083 HOH A O 1 HETATM 4503 O O . HOH AA 11 . ? 135.862 147.212 23.595 1.00 56.61 ? 2084 HOH A O 1 HETATM 4504 O O . HOH AA 11 . ? 139.333 110.012 36.536 1.00 53.58 ? 2085 HOH A O 1 HETATM 4505 O O . HOH AA 11 . ? 130.869 145.160 32.384 1.00 42.44 ? 2086 HOH A O 1 HETATM 4506 O O . HOH AA 11 . ? 132.767 147.316 33.462 1.00 37.87 ? 2087 HOH A O 1 HETATM 4507 O O . HOH AA 11 . ? 135.810 125.728 30.648 1.00 17.96 ? 2088 HOH A O 1 HETATM 4508 O O . HOH AA 11 . ? 134.740 122.639 37.828 1.00 16.96 ? 2089 HOH A O 1 HETATM 4509 O O . HOH AA 11 . ? 133.913 119.659 34.850 1.00 17.32 ? 2090 HOH A O 1 HETATM 4510 O O . HOH AA 11 . ? 139.982 118.820 34.267 1.00 19.71 ? 2091 HOH A O 1 HETATM 4511 O O . HOH AA 11 . ? 137.244 113.606 37.498 1.00 48.64 ? 2092 HOH A O 1 HETATM 4512 O O . HOH AA 11 . ? 134.344 114.705 36.377 1.00 26.97 ? 2093 HOH A O 1 HETATM 4513 O O . HOH AA 11 . ? 130.191 126.925 30.408 1.00 20.63 ? 2094 HOH A O 1 HETATM 4514 O O . HOH AA 11 . ? 124.895 118.629 32.862 1.00 35.00 ? 2095 HOH A O 1 HETATM 4515 O O . HOH AA 11 . ? 120.431 109.619 52.637 1.00 50.54 ? 2096 HOH A O 1 HETATM 4516 O O . HOH AA 11 . ? 118.123 106.739 48.863 1.00 63.36 ? 2097 HOH A O 1 HETATM 4517 O O . HOH AA 11 . ? 125.075 131.887 34.728 1.00 22.86 ? 2098 HOH A O 1 HETATM 4518 O O . HOH AA 11 . ? 122.407 124.352 30.303 1.00 51.97 ? 2099 HOH A O 1 HETATM 4519 O O . HOH AA 11 . ? 117.196 126.657 32.082 1.00 54.83 ? 2100 HOH A O 1 HETATM 4520 O O . HOH AA 11 . ? 120.024 141.545 31.180 1.00 44.43 ? 2101 HOH A O 1 HETATM 4521 O O . HOH AA 11 . ? 143.210 111.205 27.085 1.00 29.97 ? 2102 HOH A O 1 HETATM 4522 O O . HOH AA 11 . ? 151.805 114.539 32.488 1.00 28.17 ? 2103 HOH A O 1 HETATM 4523 O O . HOH AA 11 . ? 151.896 117.638 30.866 1.00 20.99 ? 2104 HOH A O 1 HETATM 4524 O O . HOH AA 11 . ? 140.090 148.172 45.242 1.00 47.06 ? 2105 HOH A O 1 HETATM 4525 O O . HOH AA 11 . ? 153.260 112.008 30.764 1.00 36.31 ? 2106 HOH A O 1 HETATM 4526 O O . HOH AA 11 . ? 162.496 115.480 24.831 1.00 57.34 ? 2107 HOH A O 1 HETATM 4527 O O . HOH AA 11 . ? 158.518 120.328 26.836 1.00 48.40 ? 2108 HOH A O 1 HETATM 4528 O O . HOH AA 11 . ? 161.899 112.909 23.106 1.00 55.59 ? 2109 HOH A O 1 HETATM 4529 O O . HOH AA 11 . ? 154.699 122.146 26.315 1.00 33.04 ? 2110 HOH A O 1 HETATM 4530 O O . HOH AA 11 . ? 148.075 128.155 22.438 1.00 43.60 ? 2111 HOH A O 1 HETATM 4531 O O . HOH AA 11 . ? 148.580 130.713 23.186 1.00 47.75 ? 2112 HOH A O 1 HETATM 4532 O O . HOH AA 11 . ? 153.145 130.601 27.883 1.00 46.06 ? 2113 HOH A O 1 HETATM 4533 O O . HOH AA 11 . ? 141.315 137.133 27.085 1.00 23.74 ? 2114 HOH A O 1 HETATM 4534 O O . HOH AA 11 . ? 148.076 133.081 22.041 1.00 53.53 ? 2115 HOH A O 1 HETATM 4535 O O . HOH AA 11 . ? 124.830 146.193 35.677 1.00 59.86 ? 2116 HOH A O 1 HETATM 4536 O O . HOH AA 11 . ? 138.600 142.050 20.890 1.00 36.33 ? 2117 HOH A O 1 HETATM 4537 O O . HOH AA 11 . ? 142.743 143.280 21.820 1.00 45.23 ? 2118 HOH A O 1 HETATM 4538 O O . HOH AA 11 . ? 137.324 141.992 17.690 1.00 42.80 ? 2119 HOH A O 1 HETATM 4539 O O . HOH AA 11 . ? 145.005 132.962 17.292 1.00 69.83 ? 2120 HOH A O 1 HETATM 4540 O O . HOH AA 11 . ? 142.327 133.667 17.544 1.00 52.06 ? 2121 HOH A O 1 HETATM 4541 O O . HOH AA 11 . ? 130.377 143.182 15.445 1.00 47.62 ? 2122 HOH A O 1 HETATM 4542 O O . HOH AA 11 . ? 139.780 148.008 25.079 1.00 47.33 ? 2123 HOH A O 1 HETATM 4543 O O . HOH AA 11 . ? 144.161 141.825 29.339 1.00 50.20 ? 2124 HOH A O 1 HETATM 4544 O O . HOH AA 11 . ? 144.027 143.232 31.718 1.00 40.44 ? 2125 HOH A O 1 HETATM 4545 O O . HOH AA 11 . ? 143.587 145.802 31.738 1.00 50.32 ? 2126 HOH A O 1 HETATM 4546 O O . HOH AA 11 . ? 139.985 138.441 65.966 1.00 30.81 ? 2127 HOH A O 1 HETATM 4547 O O . HOH AA 11 . ? 144.567 133.413 66.871 1.00 67.39 ? 2128 HOH A O 1 HETATM 4548 O O . HOH AA 11 . ? 140.333 140.333 63.940 0.50 29.94 ? 2129 HOH A O 1 HETATM 4549 O O . HOH AA 11 . ? 137.953 141.785 34.717 1.00 24.36 ? 2130 HOH A O 1 HETATM 4550 O O . HOH AA 11 . ? 134.415 123.132 44.826 1.00 20.03 ? 2131 HOH A O 1 HETATM 4551 O O . HOH AA 11 . ? 156.313 129.963 33.846 1.00 31.37 ? 2132 HOH A O 1 HETATM 4552 O O . HOH AA 11 . ? 156.185 133.272 36.369 1.00 30.31 ? 2133 HOH A O 1 HETATM 4553 O O . HOH AA 11 . ? 151.450 137.726 27.996 1.00 39.44 ? 2134 HOH A O 1 HETATM 4554 O O . HOH AA 11 . ? 152.895 141.651 36.728 1.00 36.46 ? 2135 HOH A O 1 HETATM 4555 O O . HOH AA 11 . ? 148.269 139.902 24.149 1.00 54.60 ? 2136 HOH A O 1 HETATM 4556 O O . HOH AA 11 . ? 146.171 143.098 33.109 1.00 33.24 ? 2137 HOH A O 1 HETATM 4557 O O . HOH AA 11 . ? 146.060 143.663 35.869 1.00 59.89 ? 2138 HOH A O 1 HETATM 4558 O O . HOH AA 11 . ? 140.958 127.609 46.008 1.00 19.72 ? 2139 HOH A O 1 HETATM 4559 O O . HOH AA 11 . ? 134.862 126.704 46.623 1.00 16.17 ? 2140 HOH A O 1 HETATM 4560 O O . HOH AA 11 . ? 144.043 124.082 46.488 1.00 21.42 ? 2141 HOH A O 1 HETATM 4561 O O . HOH AA 11 . ? 152.320 121.301 43.043 1.00 37.82 ? 2142 HOH A O 1 HETATM 4562 O O . HOH AA 11 . ? 151.566 119.275 42.450 1.00 51.85 ? 2143 HOH A O 1 HETATM 4563 O O . HOH AA 11 . ? 151.084 113.129 45.382 1.00 53.22 ? 2144 HOH A O 1 HETATM 4564 O O . HOH AA 11 . ? 149.731 114.636 39.082 1.00 36.50 ? 2145 HOH A O 1 HETATM 4565 O O . HOH AA 11 . ? 149.749 116.901 37.436 1.00 55.82 ? 2146 HOH A O 1 HETATM 4566 O O . HOH AA 11 . ? 157.237 118.376 36.221 1.00 45.05 ? 2147 HOH A O 1 HETATM 4567 O O . HOH AA 11 . ? 158.766 102.102 34.097 1.00 55.93 ? 2148 HOH A O 1 HETATM 4568 O O . HOH AA 11 . ? 158.466 101.957 26.733 1.00 47.84 ? 2149 HOH A O 1 HETATM 4569 O O . HOH AA 11 . ? 162.718 99.058 18.871 1.00 57.36 ? 2150 HOH A O 1 HETATM 4570 O O . HOH AA 11 . ? 145.437 105.130 38.483 1.00 48.90 ? 2151 HOH A O 1 HETATM 4571 O O . HOH AA 11 . ? 147.146 110.340 45.281 1.00 50.49 ? 2152 HOH A O 1 HETATM 4572 O O . HOH AA 11 . ? 141.291 110.345 40.222 1.00 59.76 ? 2153 HOH A O 1 HETATM 4573 O O . HOH AA 11 . ? 146.902 112.658 43.500 1.00 38.56 ? 2154 HOH A O 1 HETATM 4574 O O . HOH AA 11 . ? 148.648 108.695 40.937 1.00 45.28 ? 2155 HOH A O 1 HETATM 4575 O O . HOH AA 11 . ? 152.399 112.005 33.070 1.00 35.05 ? 2156 HOH A O 1 HETATM 4576 O O . HOH AA 11 . ? 156.350 123.210 24.299 1.00 31.23 ? 2157 HOH A O 1 HETATM 4577 O O . HOH AA 11 . ? 155.990 128.311 47.304 1.00 36.15 ? 2158 HOH A O 1 HETATM 4578 O O . HOH AA 11 . ? 155.529 134.388 48.093 1.00 31.25 ? 2159 HOH A O 1 HETATM 4579 O O . HOH AA 11 . ? 157.331 134.340 50.380 1.00 63.89 ? 2160 HOH A O 1 HETATM 4580 O O . HOH AA 11 . ? 160.623 135.316 36.236 1.00 50.59 ? 2161 HOH A O 1 HETATM 4581 O O . HOH AA 11 . ? 155.756 140.519 37.127 1.00 64.32 ? 2162 HOH A O 1 HETATM 4582 O O . HOH AA 11 . ? 144.739 144.566 38.073 1.00 40.08 ? 2163 HOH A O 1 HETATM 4583 O O . HOH AA 11 . ? 136.717 120.957 53.350 1.00 72.09 ? 2164 HOH A O 1 HETATM 4584 O O . HOH AA 11 . ? 134.879 120.038 57.888 1.00 38.90 ? 2165 HOH A O 1 HETATM 4585 O O . HOH AA 11 . ? 133.623 116.664 49.093 1.00 19.47 ? 2166 HOH A O 1 HETATM 4586 O O . HOH AA 11 . ? 134.835 117.353 56.010 1.00 27.90 ? 2167 HOH A O 1 HETATM 4587 O O . HOH AA 11 . ? 137.074 118.197 54.054 1.00 29.75 ? 2168 HOH A O 1 HETATM 4588 O O . HOH AA 11 . ? 134.386 103.392 49.244 1.00 42.63 ? 2169 HOH A O 1 HETATM 4589 O O . HOH AA 11 . ? 130.999 103.371 47.759 1.00 40.12 ? 2170 HOH A O 1 HETATM 4590 O O . HOH AA 11 . ? 138.278 103.906 55.449 1.00 30.31 ? 2171 HOH A O 1 HETATM 4591 O O . HOH AA 11 . ? 130.712 102.028 58.228 1.00 38.65 ? 2172 HOH A O 1 HETATM 4592 O O . HOH AA 11 . ? 128.695 104.141 48.144 1.00 37.04 ? 2173 HOH A O 1 HETATM 4593 O O . HOH AA 11 . ? 122.640 107.460 53.709 1.00 50.48 ? 2174 HOH A O 1 HETATM 4594 O O . HOH AA 11 . ? 122.571 109.102 48.181 1.00 35.57 ? 2175 HOH A O 1 HETATM 4595 O O . HOH AA 11 . ? 119.546 103.875 47.547 1.00 40.31 ? 2176 HOH A O 1 HETATM 4596 O O . HOH AA 11 . ? 123.123 104.149 58.466 1.00 54.20 ? 2177 HOH A O 1 HETATM 4597 O O . HOH AA 11 . ? 131.901 100.315 60.284 1.00 49.34 ? 2178 HOH A O 1 HETATM 4598 O O . HOH AA 11 . ? 133.493 106.903 62.770 1.00 40.09 ? 2179 HOH A O 1 HETATM 4599 O O . HOH AA 11 . ? 139.001 99.519 65.597 1.00 51.61 ? 2180 HOH A O 1 HETATM 4600 O O . HOH AA 11 . ? 136.800 101.644 66.989 1.00 51.96 ? 2181 HOH A O 1 HETATM 4601 O O . HOH AA 11 . ? 143.255 92.958 60.278 1.00 64.63 ? 2182 HOH A O 1 HETATM 4602 O O . HOH AA 11 . ? 147.749 103.500 58.079 1.00 35.88 ? 2183 HOH A O 1 HETATM 4603 O O . HOH AA 11 . ? 143.632 99.666 53.108 1.00 40.63 ? 2184 HOH A O 1 HETATM 4604 O O . HOH AA 11 . ? 144.833 112.317 50.040 1.00 38.42 ? 2185 HOH A O 1 HETATM 4605 O O . HOH AA 11 . ? 148.808 110.536 48.015 1.00 47.89 ? 2186 HOH A O 1 HETATM 4606 O O . HOH AA 11 . ? 150.673 108.776 48.052 1.00 54.35 ? 2187 HOH A O 1 HETATM 4607 O O . HOH AA 11 . ? 156.706 108.744 53.327 1.00 41.28 ? 2188 HOH A O 1 HETATM 4608 O O . HOH AA 11 . ? 158.925 109.194 56.334 1.00 52.22 ? 2189 HOH A O 1 HETATM 4609 O O . HOH AA 11 . ? 150.090 105.254 65.428 1.00 64.08 ? 2190 HOH A O 1 HETATM 4610 O O . HOH AA 11 . ? 150.897 116.552 64.847 1.00 53.27 ? 2191 HOH A O 1 HETATM 4611 O O . HOH AA 11 . ? 144.998 120.257 65.120 1.00 71.70 ? 2192 HOH A O 1 HETATM 4612 O O . HOH AA 11 . ? 146.298 112.248 71.271 1.00 71.43 ? 2193 HOH A O 1 HETATM 4613 O O . HOH AA 11 . ? 136.850 109.406 73.038 1.00 73.77 ? 2194 HOH A O 1 HETATM 4614 O O . HOH AA 11 . ? 139.130 105.469 70.004 1.00 56.69 ? 2195 HOH A O 1 HETATM 4615 O O . HOH AA 11 . ? 133.554 112.813 56.862 1.00 33.79 ? 2196 HOH A O 1 HETATM 4616 O O . HOH AA 11 . ? 131.298 113.106 58.198 1.00 37.41 ? 2197 HOH A O 1 HETATM 4617 O O . HOH AA 11 . ? 125.544 109.666 61.600 1.00 51.60 ? 2198 HOH A O 1 HETATM 4618 O O . HOH AA 11 . ? 125.726 111.857 61.959 1.00 60.66 ? 2199 HOH A O 1 HETATM 4619 O O . HOH AA 11 . ? 134.736 115.103 57.376 1.00 27.18 ? 2200 HOH A O 1 HETATM 4620 O O . HOH AA 11 . ? 138.427 119.911 56.166 1.00 24.73 ? 2201 HOH A O 1 HETATM 4621 O O . HOH AA 11 . ? 134.197 117.841 60.409 1.00 47.06 ? 2202 HOH A O 1 HETATM 4622 O O . HOH AA 11 . ? 139.825 119.993 59.739 1.00 34.55 ? 2203 HOH A O 1 HETATM 4623 O O . HOH AA 11 . ? 149.011 120.068 51.585 1.00 22.61 ? 2204 HOH A O 1 HETATM 4624 O O . HOH AA 11 . ? 149.142 112.892 46.819 1.00 59.35 ? 2205 HOH A O 1 HETATM 4625 O O . HOH AA 11 . ? 152.806 115.842 49.504 1.00 43.53 ? 2206 HOH A O 1 HETATM 4626 O O . HOH AA 11 . ? 146.715 113.442 46.735 1.00 31.61 ? 2207 HOH A O 1 HETATM 4627 O O . HOH AA 11 . ? 149.485 122.806 51.958 1.00 25.98 ? 2208 HOH A O 1 HETATM 4628 O O . HOH AA 11 . ? 148.307 126.075 54.582 1.00 25.99 ? 2209 HOH A O 1 HETATM 4629 O O . HOH AA 11 . ? 147.164 130.521 60.107 1.00 35.53 ? 2210 HOH A O 1 HETATM 4630 O O . HOH AA 11 . ? 151.030 140.351 45.218 1.00 35.34 ? 2211 HOH A O 1 HETATM 4631 O O . HOH AA 11 . ? 150.230 139.993 53.270 1.00 63.43 ? 2212 HOH A O 1 HETATM 4632 O O . HOH AA 11 . ? 152.023 143.589 43.689 1.00 44.90 ? 2213 HOH A O 1 HETATM 4633 O O . HOH AA 11 . ? 145.992 141.260 50.280 1.00 27.90 ? 2214 HOH A O 1 HETATM 4634 O O . HOH AA 11 . ? 141.029 145.575 45.375 1.00 29.06 ? 2215 HOH A O 1 HETATM 4635 O O . HOH AA 11 . ? 144.505 148.803 46.857 1.00 51.99 ? 2216 HOH A O 1 HETATM 4636 O O . HOH AA 11 . ? 139.601 137.929 52.957 1.00 21.91 ? 2217 HOH A O 1 HETATM 4637 O O . HOH AA 11 . ? 124.020 124.389 55.165 1.00 36.52 ? 2218 HOH A O 1 HETATM 4638 O O . HOH AA 11 . ? 132.523 128.992 60.055 1.00 38.20 ? 2219 HOH A O 1 HETATM 4639 O O . HOH AA 11 . ? 129.878 131.512 60.019 1.00 39.59 ? 2220 HOH A O 1 HETATM 4640 O O . HOH AA 11 . ? 126.114 122.930 48.783 1.00 34.29 ? 2221 HOH A O 1 HETATM 4641 O O . HOH AA 11 . ? 122.129 120.768 44.197 1.00 43.21 ? 2222 HOH A O 1 HETATM 4642 O O . HOH AA 11 . ? 114.808 122.691 48.340 1.00 45.11 ? 2223 HOH A O 1 HETATM 4643 O O . HOH AA 11 . ? 119.065 117.234 42.446 1.00 64.30 ? 2224 HOH A O 1 HETATM 4644 O O . HOH AA 11 . ? 119.900 113.585 49.751 1.00 44.53 ? 2225 HOH A O 1 HETATM 4645 O O . HOH AA 11 . ? 120.461 109.785 49.190 1.00 57.39 ? 2226 HOH A O 1 HETATM 4646 O O . HOH AA 11 . ? 123.766 111.172 56.487 1.00 36.06 ? 2227 HOH A O 1 HETATM 4647 O O . HOH AA 11 . ? 120.804 111.916 54.554 1.00 57.68 ? 2228 HOH A O 1 HETATM 4648 O O . HOH AA 11 . ? 127.233 123.078 41.936 1.00 26.41 ? 2229 HOH A O 1 HETATM 4649 O O . HOH AA 11 . ? 123.457 119.945 42.348 1.00 34.62 ? 2230 HOH A O 1 HETATM 4650 O O . HOH AA 11 . ? 118.063 126.707 37.653 1.00 35.29 ? 2231 HOH A O 1 HETATM 4651 O O . HOH AA 11 . ? 112.141 132.275 35.085 1.00 54.24 ? 2232 HOH A O 1 HETATM 4652 O O . HOH AA 11 . ? 116.134 128.380 33.787 1.00 51.38 ? 2233 HOH A O 1 HETATM 4653 O O . HOH AA 11 . ? 117.988 126.801 52.847 1.00 51.85 ? 2234 HOH A O 1 HETATM 4654 O O . HOH AA 11 . ? 111.567 128.450 50.724 1.00 47.50 ? 2235 HOH A O 1 HETATM 4655 O O . HOH AA 11 . ? 127.455 137.251 50.084 1.00 34.77 ? 2236 HOH A O 1 HETATM 4656 O O . HOH AA 11 . ? 122.345 145.569 40.888 1.00 52.88 ? 2237 HOH A O 1 HETATM 4657 O O . HOH AA 11 . ? 127.466 145.996 40.225 1.00 28.77 ? 2238 HOH A O 1 HETATM 4658 O O . HOH AA 11 . ? 130.271 143.832 50.844 1.00 34.61 ? 2239 HOH A O 1 HETATM 4659 O O . HOH AA 11 . ? 126.677 138.856 52.547 1.00 37.95 ? 2240 HOH A O 1 HETATM 4660 O O . HOH AA 11 . ? 127.134 146.271 44.945 1.00 26.46 ? 2241 HOH A O 1 HETATM 4661 O O . HOH AA 11 . ? 134.870 147.905 34.685 1.00 42.95 ? 2242 HOH A O 1 HETATM 4662 O O . HOH AA 11 . ? 127.806 147.165 34.870 1.00 40.31 ? 2243 HOH A O 1 HETATM 4663 O O . HOH AA 11 . ? 137.504 148.903 44.281 1.00 33.51 ? 2244 HOH A O 1 HETATM 4664 O O . HOH AA 11 . ? 137.768 145.451 51.992 1.00 36.94 ? 2245 HOH A O 1 HETATM 4665 O O . HOH AA 11 . ? 124.668 145.502 44.956 1.00 28.49 ? 2246 HOH A O 1 HETATM 4666 O O . HOH AA 11 . ? 124.448 148.687 52.392 1.00 48.96 ? 2247 HOH A O 1 HETATM 4667 O O . HOH AA 11 . ? 126.195 151.001 46.289 1.00 40.30 ? 2248 HOH A O 1 HETATM 4668 O O . HOH AA 11 . ? 140.356 145.739 54.305 1.00 42.59 ? 2249 HOH A O 1 HETATM 4669 O O . HOH AA 11 . ? 142.294 143.481 55.839 1.00 37.84 ? 2250 HOH A O 1 HETATM 4670 O O . HOH AA 11 . ? 143.544 139.903 56.724 1.00 23.86 ? 2251 HOH A O 1 HETATM 4671 O O . HOH AA 11 . ? 150.488 141.988 56.853 1.00 59.72 ? 2252 HOH A O 1 HETATM 4672 O O . HOH AA 11 . ? 144.268 137.570 63.015 1.00 32.48 ? 2253 HOH A O 1 HETATM 4673 O O . HOH AA 11 . ? 144.113 142.363 58.167 1.00 31.23 ? 2254 HOH A O 1 HETATM 4674 O O . HOH AA 11 . ? 142.104 144.599 62.534 1.00 45.23 ? 2255 HOH A O 1 HETATM 4675 O O . HOH AA 11 . ? 142.510 132.318 57.269 1.00 23.63 ? 2256 HOH A O 1 HETATM 4676 O O . HOH AA 11 . ? 145.289 131.429 57.217 1.00 26.83 ? 2257 HOH A O 1 HETATM 4677 O O . HOH AA 11 . ? 135.354 128.807 60.039 1.00 39.60 ? 2258 HOH A O 1 HETATM 4678 O O . HOH AA 11 . ? 138.888 130.411 61.920 1.00 28.45 ? 2259 HOH A O 1 HETATM 4679 O O . HOH AA 11 . ? 127.099 134.254 54.074 1.00 50.86 ? 2260 HOH A O 1 HETATM 4680 O O . HOH AA 11 . ? 130.304 137.747 63.597 1.00 50.79 ? 2261 HOH A O 1 HETATM 4681 O O . HOH AA 11 . ? 131.549 139.085 61.319 1.00 32.38 ? 2262 HOH A O 1 HETATM 4682 O O . HOH AA 11 . ? 137.954 133.502 63.971 1.00 32.72 ? 2263 HOH A O 1 HETATM 4683 O O . HOH AA 11 . ? 141.233 132.812 65.178 1.00 42.09 ? 2264 HOH A O 1 HETATM 4684 O O . HOH AA 11 . ? 142.195 130.099 63.971 1.00 33.65 ? 2265 HOH A O 1 HETATM 4685 O O . HOH AA 11 . ? 138.391 136.689 64.594 1.00 30.30 ? 2266 HOH A O 1 HETATM 4686 O O . HOH AA 11 . ? 143.046 136.149 65.402 1.00 39.04 ? 2267 HOH A O 1 HETATM 4687 O O . HOH AA 11 . ? 149.245 132.461 63.460 1.00 63.59 ? 2268 HOH A O 1 HETATM 4688 O O . HOH AA 11 . ? 145.466 129.126 58.466 1.00 34.30 ? 2269 HOH A O 1 HETATM 4689 O O . HOH AA 11 . ? 137.881 121.700 60.720 1.00 40.35 ? 2270 HOH A O 1 HETATM 4690 O O . HOH AA 11 . ? 136.239 124.946 60.818 1.00 55.87 ? 2271 HOH A O 1 HETATM 4691 O O . HOH AA 11 . ? 142.909 125.093 64.035 1.00 53.33 ? 2272 HOH A O 1 HETATM 4692 O O . HOH AA 11 . ? 148.570 127.735 59.614 1.00 45.30 ? 2273 HOH A O 1 HETATM 4693 O O . HOH AA 11 . ? 142.567 121.651 65.395 1.00 57.61 ? 2274 HOH A O 1 HETATM 4694 O O . HOH AA 11 . ? 140.238 118.503 62.515 1.00 39.23 ? 2275 HOH A O 1 HETATM 4695 O O . HOH AA 11 . ? 146.354 130.165 65.574 1.00 53.47 ? 2276 HOH A O 1 HETATM 4696 O O . HOH AA 11 . ? 151.201 118.952 52.698 1.00 35.16 ? 2277 HOH A O 1 HETATM 4697 O O . HOH AA 11 . ? 116.823 130.145 12.261 1.00 66.00 ? 2278 HOH A O 1 HETATM 4698 O O . HOH AA 11 . ? 115.662 146.999 49.351 1.00 62.16 ? 2279 HOH A O 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . ILE A 4 ? 1.0873 0.9469 0.8309 0.0164 -0.3520 0.0765 4 ILE A N 2 C CA . ILE A 4 ? 1.0755 0.9027 0.8155 0.0148 -0.3319 0.0835 4 ILE A CA 3 C C . ILE A 4 ? 1.0004 0.8150 0.7045 -0.0021 -0.3138 0.0781 4 ILE A C 4 O O . ILE A 4 ? 1.0073 0.8352 0.7137 -0.0131 -0.3046 0.0581 4 ILE A O 5 C CB . ILE A 4 ? 1.0374 0.8638 0.8235 0.0205 -0.3204 0.0714 4 ILE A CB 6 C CG1 . ILE A 4 ? 1.0129 0.8075 0.7962 0.0171 -0.3003 0.0748 4 ILE A CG1 7 C CG2 . ILE A 4 ? 1.0006 0.8529 0.8064 0.0130 -0.3146 0.0475 4 ILE A CG2 8 C CD1 . ILE A 4 ? 1.0329 0.8000 0.8132 0.0275 -0.3048 0.0978 4 ILE A CD1 9 N N . ILE A 5 ? 0.9262 0.7148 0.5989 -0.0038 -0.3079 0.0971 5 ILE A N 10 C CA . ILE A 5 ? 0.8948 0.6727 0.5292 -0.0188 -0.2918 0.0956 5 ILE A CA 11 C C . ILE A 5 ? 0.8925 0.6387 0.5288 -0.0218 -0.2717 0.1056 5 ILE A C 12 O O . ILE A 5 ? 0.9597 0.6851 0.5986 -0.0130 -0.2750 0.1265 5 ILE A O 13 C CB . ILE A 5 ? 0.8903 0.6710 0.4750 -0.0196 -0.3046 0.1102 5 ILE A CB 14 C CG1 . ILE A 5 ? 0.9668 0.7808 0.5522 -0.0181 -0.3257 0.0965 5 ILE A CG1 15 C CG2 . ILE A 5 ? 0.9097 0.6784 0.4532 -0.0340 -0.2857 0.1099 5 ILE A CG2 16 C CD1 . ILE A 5 ? 0.9859 0.8093 0.5381 -0.0115 -0.3435 0.1116 5 ILE A CD1 17 N N . ILE A 6 ? 0.8521 0.5949 0.4903 -0.0342 -0.2512 0.0905 6 ILE A N 18 C CA . ILE A 6 ? 0.8200 0.5362 0.4665 -0.0386 -0.2320 0.0963 6 ILE A CA 19 C C . ILE A 6 ? 0.9481 0.6556 0.5582 -0.0530 -0.2147 0.0991 6 ILE A C 20 O O . ILE A 6 ? 0.8264 0.5498 0.4240 -0.0623 -0.2084 0.0821 6 ILE A O 21 C CB . ILE A 6 ? 0.7703 0.4900 0.4589 -0.0389 -0.2217 0.0754 6 ILE A CB 22 C CG1 . ILE A 6 ? 0.8347 0.5595 0.5602 -0.0234 -0.2353 0.0741 6 ILE A CG1 23 C CG2 . ILE A 6 ? 0.7714 0.4669 0.4675 -0.0461 -0.2019 0.0774 6 ILE A CG2 24 C CD1 . ILE A 6 ? 0.8309 0.5298 0.5658 -0.0134 -0.2395 0.0946 6 ILE A CD1 25 N N . ALA A 7 ? 0.8784 0.5601 0.4731 -0.0547 -0.2059 0.1209 7 ALA A N 26 C CA . ALA A 7 ? 1.0035 0.6755 0.5673 -0.0683 -0.1860 0.1254 7 ALA A CA 27 C C . ALA A 7 ? 0.9559 0.6227 0.5485 -0.0781 -0.1648 0.1091 7 ALA A C 28 O O . ALA A 7 ? 0.9730 0.6236 0.5992 -0.0753 -0.1605 0.1112 7 ALA A O 29 C CB . ALA A 7 ? 1.0260 0.6723 0.5643 -0.0666 -0.1831 0.1571 7 ALA A CB 30 N N . THR A 8 ? 0.8924 0.5733 0.4731 -0.0888 -0.1526 0.0916 8 THR A N 31 C CA . THR A 8 ? 0.8814 0.5590 0.4855 -0.0983 -0.1321 0.0774 8 THR A CA 32 C C . THR A 8 ? 0.9700 0.6382 0.5446 -0.1107 -0.1115 0.0868 8 THR A C 33 O O . THR A 8 ? 0.9386 0.6036 0.4714 -0.1114 -0.1130 0.1034 8 THR A O 34 C CB . THR A 8 ? 0.8296 0.5306 0.4499 -0.1003 -0.1313 0.0490 8 THR A CB 35 O OG1 . THR A 8 ? 0.8428 0.5570 0.4284 -0.1078 -0.1267 0.0419 8 THR A OG1 36 C CG2 . THR A 8 ? 0.7498 0.4644 0.3926 -0.0885 -0.1510 0.0407 8 THR A CG2 37 N N . LYS A 9 ? 0.9776 0.6434 0.5739 -0.1199 -0.0922 0.0757 9 LYS A N 38 C CA . LYS A 9 ? 0.9595 0.6183 0.5350 -0.1322 -0.0695 0.0832 9 LYS A CA 39 C C . LYS A 9 ? 0.9473 0.6221 0.4788 -0.1369 -0.0653 0.0771 9 LYS A C 40 O O . LYS A 9 ? 0.9760 0.6439 0.4724 -0.1431 -0.0522 0.0919 9 LYS A O 41 C CB . LYS A 9 ? 0.9217 0.5801 0.5356 -0.1404 -0.0517 0.0683 9 LYS A CB 42 C CG . LYS A 9 ? 1.0225 0.6570 0.6650 -0.1433 -0.0435 0.0828 9 LYS A CG 43 C CD . LYS A 9 ? 1.0459 0.6658 0.7023 -0.1312 -0.0627 0.0946 9 LYS A CD 44 C CE . LYS A 9 ? 1.0762 0.6688 0.7589 -0.1346 -0.0543 0.1100 9 LYS A CE 45 N NZ . LYS A 9 ? 1.1337 0.7071 0.8123 -0.1234 -0.0701 0.1315 9 LYS A NZ 46 N N . ASN A 10 ? 0.9008 0.5964 0.4344 -0.1339 -0.0757 0.0552 10 ASN A N 47 C CA . ASN A 10 ? 1.0060 0.7170 0.5032 -0.1386 -0.0722 0.0441 10 ASN A CA 48 C C . ASN A 10 ? 1.0101 0.7297 0.4739 -0.1315 -0.0943 0.0484 10 ASN A C 49 O O . ASN A 10 ? 1.0395 0.7717 0.4705 -0.1347 -0.0947 0.0382 10 ASN A O 50 C CB . ASN A 10 ? 1.0716 0.7990 0.5940 -0.1418 -0.0662 0.0155 10 ASN A CB 51 C CG . ASN A 10 ? 1.1503 0.8722 0.7077 -0.1475 -0.0472 0.0099 10 ASN A CG 52 O OD1 . ASN A 10 ? 1.1851 0.9030 0.7816 -0.1432 -0.0520 0.0074 10 ASN A OD1 53 N ND2 . ASN A 10 ? 1.1650 0.8880 0.7093 -0.1569 -0.0256 0.0073 10 ASN A ND2 54 N N . GLY A 11 ? 0.9740 0.6873 0.4477 -0.1216 -0.1131 0.0626 11 GLY A N 55 C CA . GLY A 11 ? 0.9161 0.6383 0.3614 -0.1139 -0.1359 0.0692 11 GLY A CA 56 C C . GLY A 11 ? 0.9853 0.7120 0.4635 -0.1023 -0.1581 0.0694 11 GLY A C 57 O O . GLY A 11 ? 0.9038 0.6263 0.4255 -0.0997 -0.1555 0.0636 11 GLY A O 58 N N . LYS A 12 ? 0.9135 0.6505 0.3706 -0.0948 -0.1803 0.0753 12 LYS A N 59 C CA . LYS A 12 ? 0.9871 0.7319 0.4742 -0.0829 -0.2025 0.0761 12 LYS A CA 60 C C . LYS A 12 ? 0.9288 0.6964 0.4465 -0.0835 -0.2088 0.0492 12 LYS A C 61 O O . LYS A 12 ? 0.8438 0.6261 0.3461 -0.0909 -0.2071 0.0315 12 LYS A O 62 C CB . LYS A 12 ? 0.9387 0.6884 0.3938 -0.0741 -0.2250 0.0932 12 LYS A CB 63 C CG . LYS A 12 ? 1.0286 0.7551 0.4507 -0.0718 -0.2201 0.1235 12 LYS A CG 64 C CD . LYS A 12 ? 1.1079 0.8383 0.5110 -0.0585 -0.2462 0.1426 12 LYS A CD 65 C CE . LYS A 12 ? 1.2074 0.9109 0.5829 -0.0543 -0.2406 0.1766 12 LYS A CE 66 N NZ . LYS A 12 ? 1.2695 0.9732 0.6390 -0.0382 -0.2668 0.1977 12 LYS A NZ 67 N N . VAL A 13 ? 0.8406 0.6102 0.4019 -0.0754 -0.2154 0.0463 13 VAL A N 68 C CA . VAL A 13 ? 0.7717 0.5631 0.3635 -0.0742 -0.2226 0.0248 13 VAL A CA 69 C C . VAL A 13 ? 0.7686 0.5712 0.3826 -0.0612 -0.2452 0.0311 13 VAL A C 70 O O . VAL A 13 ? 0.8427 0.6320 0.4677 -0.0515 -0.2501 0.0481 13 VAL A O 71 C CB . VAL A 13 ? 0.8487 0.6371 0.4760 -0.0770 -0.2053 0.0103 13 VAL A CB 72 C CG1 . VAL A 13 ? 0.8462 0.6273 0.4550 -0.0893 -0.1840 0.0027 13 VAL A CG1 73 C CG2 . VAL A 13 ? 0.8152 0.5873 0.4699 -0.0686 -0.2033 0.0215 13 VAL A CG2 74 N N . ARG A 14 ? 0.7567 0.5836 0.3790 -0.0612 -0.2586 0.0172 14 ARG A N 75 C CA . ARG A 14 ? 0.8409 0.6838 0.4921 -0.0495 -0.2788 0.0197 14 ARG A CA 76 C C . ARG A 14 ? 0.7644 0.6208 0.4617 -0.0482 -0.2735 0.0024 14 ARG A C 77 O O . ARG A 14 ? 0.6958 0.5611 0.3973 -0.0576 -0.2640 -0.0158 14 ARG A O 78 C CB . ARG A 14 ? 0.8538 0.7174 0.4847 -0.0497 -0.3002 0.0179 14 ARG A CB 79 C CG . ARG A 14 ? 0.8025 0.6951 0.4780 -0.0416 -0.3125 0.0098 14 ARG A CG 80 C CD . ARG A 14 ? 0.8576 0.7785 0.5262 -0.0420 -0.3229 0.0041 14 ARG A CD 81 N NE . ARG A 14 ? 0.9668 0.8846 0.6082 -0.0328 -0.3379 0.0246 14 ARG A NE 82 C CZ . ARG A 14 ? 1.0321 0.9493 0.6296 -0.0360 -0.3382 0.0292 14 ARG A CZ 83 N NH1 . ARG A 14 ? 0.8599 0.7798 0.4372 -0.0480 -0.3244 0.0132 14 ARG A NH1 84 N NH2 . ARG A 14 ? 1.0340 0.9488 0.6086 -0.0258 -0.3514 0.0499 14 ARG A NH2 85 N N . GLY A 15 ? 0.7264 0.5835 0.4575 -0.0358 -0.2788 0.0085 15 GLY A N 86 C CA . GLY A 15 ? 0.6785 0.5494 0.4518 -0.0323 -0.2737 -0.0054 15 GLY A CA 87 C C . GLY A 15 ? 0.6731 0.5704 0.4733 -0.0250 -0.2918 -0.0080 15 GLY A C 88 O O . GLY A 15 ? 0.6901 0.5996 0.4751 -0.0256 -0.3097 -0.0041 15 GLY A O 89 N N . MET A 16 ? 0.6129 0.5208 0.4534 -0.0180 -0.2872 -0.0151 16 MET A N 90 C CA . MET A 16 ? 0.6475 0.5827 0.5211 -0.0109 -0.3015 -0.0179 16 MET A CA 91 C C . MET A 16 ? 0.6638 0.6000 0.5744 0.0042 -0.2978 -0.0148 16 MET A C 92 O O . MET A 16 ? 0.5570 0.4786 0.4732 0.0060 -0.2809 -0.0183 16 MET A O 93 C CB . MET A 16 ? 0.6325 0.5885 0.5205 -0.0217 -0.2970 -0.0358 16 MET A CB 94 C CG . MET A 16 ? 0.6402 0.5920 0.5460 -0.0238 -0.2747 -0.0465 16 MET A CG 95 S SD . MET A 16 ? 0.8771 0.8476 0.7969 -0.0375 -0.2676 -0.0650 16 MET A SD 96 C CE . MET A 16 ? 0.7140 0.7174 0.6670 -0.0334 -0.2862 -0.0645 16 MET A CE 97 N N . GLN A 17 ? 0.6893 0.6442 0.6255 0.0154 -0.3139 -0.0094 17 GLN A N 98 C CA . GLN A 17 ? 0.6835 0.6418 0.6560 0.0313 -0.3113 -0.0071 17 GLN A CA 99 C C . GLN A 17 ? 0.5562 0.5392 0.5655 0.0312 -0.3016 -0.0210 17 GLN A C 100 O O . GLN A 17 ? 0.6043 0.6110 0.6250 0.0235 -0.3079 -0.0280 17 GLN A O 101 C CB . GLN A 17 ? 0.7928 0.7596 0.7778 0.0452 -0.3327 0.0066 17 GLN A CB 102 C CG . GLN A 17 ? 0.9522 0.8959 0.8998 0.0463 -0.3439 0.0238 17 GLN A CG 103 C CD . GLN A 17 ? 1.0552 0.9660 0.9972 0.0542 -0.3335 0.0333 17 GLN A CD 104 O OE1 . GLN A 17 ? 1.0846 0.9776 1.0175 0.0470 -0.3147 0.0261 17 GLN A OE1 105 N NE2 . GLN A 17 ? 1.0855 0.9878 1.0350 0.0691 -0.3463 0.0491 17 GLN A NE2 106 N N . LEU A 18 ? 0.5118 0.4888 0.5392 0.0396 -0.2862 -0.0251 18 LEU A N 107 C CA . LEU A 18 ? 0.5367 0.5359 0.5976 0.0418 -0.2747 -0.0357 18 LEU A CA 108 C C . LEU A 18 ? 0.6078 0.6162 0.7023 0.0609 -0.2757 -0.0324 18 LEU A C 109 O O . LEU A 18 ? 0.7041 0.6924 0.7928 0.0719 -0.2776 -0.0258 18 LEU A O 110 C CB . LEU A 18 ? 0.4632 0.4494 0.5129 0.0357 -0.2530 -0.0453 18 LEU A CB 111 C CG . LEU A 18 ? 0.5160 0.4912 0.5341 0.0179 -0.2482 -0.0502 18 LEU A CG 112 C CD1 . LEU A 18 ? 0.4712 0.4335 0.4817 0.0155 -0.2277 -0.0583 18 LEU A CD1 113 C CD2 . LEU A 18 ? 0.5627 0.5611 0.5909 0.0067 -0.2541 -0.0561 18 LEU A CD2 114 N N . THR A 19 ? 0.5233 0.5615 0.6546 0.0649 -0.2736 -0.0373 19 THR A N 115 C CA . THR A 19 ? 0.5387 0.5886 0.7044 0.0837 -0.2709 -0.0362 19 THR A CA 116 C C . THR A 19 ? 0.4834 0.5315 0.6555 0.0877 -0.2473 -0.0457 19 THR A C 117 O O . THR A 19 ? 0.4499 0.5097 0.6257 0.0778 -0.2351 -0.0523 19 THR A O 118 C CB . THR A 19 ? 0.5828 0.6693 0.7888 0.0874 -0.2821 -0.0350 19 THR A CB 119 O OG1 . THR A 19 ? 0.6794 0.7668 0.8783 0.0880 -0.3065 -0.0254 19 THR A OG1 120 C CG2 . THR A 19 ? 0.5496 0.6511 0.7937 0.1068 -0.2748 -0.0357 19 THR A CG2 121 N N . VAL A 20 ? 0.4426 0.4747 0.6143 0.1022 -0.2410 -0.0463 20 VAL A N 122 C CA . VAL A 20 ? 0.4803 0.5090 0.6521 0.1077 -0.2202 -0.0560 20 VAL A CA 123 C C . VAL A 20 ? 0.4945 0.5247 0.6881 0.1292 -0.2171 -0.0580 20 VAL A C 124 O O . VAL A 20 ? 0.5009 0.5086 0.6868 0.1375 -0.2249 -0.0550 20 VAL A O 125 C CB . VAL A 20 ? 0.4280 0.4257 0.5627 0.0998 -0.2132 -0.0600 20 VAL A CB 126 C CG1 . VAL A 20 ? 0.4132 0.4117 0.5474 0.1056 -0.1935 -0.0706 20 VAL A CG1 127 C CG2 . VAL A 20 ? 0.4267 0.4190 0.5367 0.0796 -0.2166 -0.0583 20 VAL A CG2 128 N N . PHE A 21 ? 0.4794 0.5355 0.7009 0.1383 -0.2048 -0.0628 21 PHE A N 129 C CA . PHE A 21 ? 0.4794 0.5403 0.7227 0.1601 -0.1989 -0.0670 21 PHE A CA 130 C C . PHE A 21 ? 0.4650 0.5224 0.7256 0.1720 -0.2168 -0.0596 21 PHE A C 131 O O . PHE A 21 ? 0.4846 0.5221 0.7433 0.1859 -0.2176 -0.0624 21 PHE A O 132 C CB . PHE A 21 ? 0.4700 0.5066 0.6899 0.1668 -0.1866 -0.0773 21 PHE A CB 133 C CG . PHE A 21 ? 0.4612 0.5011 0.6634 0.1579 -0.1695 -0.0839 21 PHE A CG 134 C CD1 . PHE A 21 ? 0.4908 0.5585 0.7085 0.1521 -0.1594 -0.0819 21 PHE A CD1 135 C CD2 . PHE A 21 ? 0.4632 0.4784 0.6353 0.1557 -0.1638 -0.0916 21 PHE A CD2 136 C CE1 . PHE A 21 ? 0.5031 0.5719 0.7045 0.1451 -0.1434 -0.0859 21 PHE A CE1 137 C CE2 . PHE A 21 ? 0.4868 0.5055 0.6427 0.1493 -0.1492 -0.0968 21 PHE A CE2 138 C CZ . PHE A 21 ? 0.5341 0.5787 0.7037 0.1445 -0.1389 -0.0931 21 PHE A CZ 139 N N . GLY A 22 ? 0.4496 0.5259 0.7275 0.1670 -0.2320 -0.0505 22 GLY A N 140 C CA . GLY A 22 ? 0.4836 0.5602 0.7801 0.1796 -0.2504 -0.0417 22 GLY A CA 141 C C . GLY A 22 ? 0.5345 0.5737 0.8001 0.1777 -0.2636 -0.0340 22 GLY A C 142 O O . GLY A 22 ? 0.5920 0.6218 0.8687 0.1913 -0.2762 -0.0264 22 GLY A O 143 N N . GLY A 23 ? 0.5495 0.5669 0.7776 0.1611 -0.2595 -0.0353 23 GLY A N 144 C CA . GLY A 23 ? 0.5704 0.5527 0.7676 0.1562 -0.2692 -0.0270 23 GLY A CA 145 C C . GLY A 23 ? 0.5733 0.5527 0.7397 0.1346 -0.2743 -0.0225 23 GLY A C 146 O O . GLY A 23 ? 0.5806 0.5861 0.7544 0.1250 -0.2750 -0.0249 23 GLY A O 147 N N . THR A 24 ? 0.5337 0.4815 0.6673 0.1268 -0.2771 -0.0166 24 THR A N 148 C CA . THR A 24 ? 0.5655 0.5088 0.6670 0.1074 -0.2814 -0.0124 24 THR A CA 149 C C . THR A 24 ? 0.5714 0.4871 0.6419 0.0959 -0.2680 -0.0174 24 THR A C 150 O O . THR A 24 ? 0.5544 0.4438 0.6200 0.1018 -0.2642 -0.0164 24 THR A O 151 C CB . THR A 24 ? 0.5923 0.5290 0.6810 0.1078 -0.3022 0.0045 24 THR A CB 152 O OG1 . THR A 24 ? 0.6911 0.6576 0.8103 0.1176 -0.3165 0.0083 24 THR A OG1 153 C CG2 . THR A 24 ? 0.6339 0.5664 0.6860 0.0885 -0.3055 0.0074 24 THR A CG2 154 N N . VAL A 25 ? 0.5330 0.4555 0.5859 0.0796 -0.2612 -0.0235 25 VAL A N 155 C CA . VAL A 25 ? 0.5278 0.4277 0.5508 0.0669 -0.2504 -0.0272 25 VAL A CA 156 C C . VAL A 25 ? 0.5752 0.4734 0.5690 0.0510 -0.2578 -0.0206 25 VAL A C 157 O O . VAL A 25 ? 0.5179 0.4387 0.5159 0.0459 -0.2655 -0.0213 25 VAL A O 158 C CB . VAL A 25 ? 0.5017 0.4104 0.5297 0.0635 -0.2326 -0.0424 25 VAL A CB 159 C CG1 . VAL A 25 ? 0.4768 0.3670 0.4759 0.0492 -0.2228 -0.0465 25 VAL A CG1 160 C CG2 . VAL A 25 ? 0.4715 0.3794 0.5216 0.0799 -0.2245 -0.0499 25 VAL A CG2 161 N N . THR A 26 ? 0.5388 0.4107 0.5039 0.0434 -0.2556 -0.0145 26 THR A N 162 C CA . THR A 26 ? 0.5544 0.4231 0.4870 0.0286 -0.2598 -0.0092 26 THR A CA 163 C C . THR A 26 ? 0.5777 0.4432 0.4948 0.0146 -0.2437 -0.0212 26 THR A C 164 O O . THR A 26 ? 0.5537 0.4021 0.4686 0.0138 -0.2310 -0.0257 26 THR A O 165 C CB . THR A 26 ? 0.5902 0.4329 0.4985 0.0286 -0.2663 0.0077 26 THR A CB 166 O OG1 . THR A 26 ? 0.6083 0.4512 0.5334 0.0439 -0.2810 0.0198 26 THR A OG1 167 C CG2 . THR A 26 ? 0.6967 0.5405 0.5693 0.0155 -0.2721 0.0137 26 THR A CG2 168 N N . ALA A 27 ? 0.5694 0.4516 0.4780 0.0039 -0.2448 -0.0274 27 ALA A N 169 C CA . ALA A 27 ? 0.5614 0.4425 0.4590 -0.0081 -0.2297 -0.0395 27 ALA A CA 170 C C . ALA A 27 ? 0.5336 0.4077 0.3962 -0.0221 -0.2310 -0.0374 27 ALA A C 171 O O . ALA A 27 ? 0.5521 0.4363 0.4035 -0.0251 -0.2448 -0.0332 27 ALA A O 172 C CB . ALA A 27 ? 0.5517 0.4566 0.4728 -0.0087 -0.2254 -0.0513 27 ALA A CB 173 N N . PHE A 28 ? 0.5320 0.3901 0.3775 -0.0301 -0.2168 -0.0411 28 PHE A N 174 C CA . PHE A 28 ? 0.6084 0.4608 0.4213 -0.0435 -0.2135 -0.0419 28 PHE A CA 175 C C . PHE A 28 ? 0.5953 0.4536 0.4129 -0.0513 -0.1987 -0.0579 28 PHE A C 176 O O . PHE A 28 ? 0.5864 0.4344 0.4079 -0.0517 -0.1850 -0.0624 28 PHE A O 177 C CB . PHE A 28 ? 0.6321 0.4600 0.4225 -0.0463 -0.2074 -0.0310 28 PHE A CB 178 C CG . PHE A 28 ? 0.6872 0.5043 0.4740 -0.0376 -0.2200 -0.0130 28 PHE A CG 179 C CD1 . PHE A 28 ? 0.6538 0.4636 0.4671 -0.0254 -0.2216 -0.0090 28 PHE A CD1 180 C CD2 . PHE A 28 ? 0.6356 0.4491 0.3918 -0.0407 -0.2301 -0.0001 28 PHE A CD2 181 C CE1 . PHE A 28 ? 0.6691 0.4667 0.4813 -0.0165 -0.2329 0.0081 28 PHE A CE1 182 C CE2 . PHE A 28 ? 0.7832 0.5855 0.5357 -0.0315 -0.2418 0.0187 28 PHE A CE2 183 C CZ . PHE A 28 ? 0.7055 0.4991 0.4877 -0.0194 -0.2431 0.0231 28 PHE A CZ 184 N N . LEU A 29 ? 0.5195 0.3945 0.3392 -0.0570 -0.2024 -0.0668 29 LEU A N 185 C CA . LEU A 29 ? 0.4980 0.3786 0.3254 -0.0634 -0.1893 -0.0811 29 LEU A CA 186 C C . LEU A 29 ? 0.5640 0.4431 0.3667 -0.0747 -0.1798 -0.0857 29 LEU A C 187 O O . LEU A 29 ? 0.5331 0.4198 0.3213 -0.0788 -0.1884 -0.0845 29 LEU A O 188 C CB . LEU A 29 ? 0.4816 0.3843 0.3374 -0.0612 -0.1933 -0.0871 29 LEU A CB 189 C CG . LEU A 29 ? 0.5057 0.4176 0.3910 -0.0482 -0.1999 -0.0820 29 LEU A CG 190 C CD1 . LEU A 29 ? 0.4541 0.3883 0.3682 -0.0484 -0.2023 -0.0883 29 LEU A CD1 191 C CD2 . LEU A 29 ? 0.4701 0.3719 0.3649 -0.0399 -0.1868 -0.0823 29 LEU A CD2 192 N N . GLY A 30 ? 0.5127 0.3843 0.3127 -0.0782 -0.1619 -0.0914 30 GLY A N 193 C CA . GLY A 30 ? 0.5113 0.3843 0.2943 -0.0868 -0.1505 -0.0977 30 GLY A CA 194 C C . GLY A 30 ? 0.6430 0.4984 0.3884 -0.0931 -0.1516 -0.0909 30 GLY A C 195 O O . GLY A 30 ? 0.5960 0.4554 0.3197 -0.0988 -0.1518 -0.0930 30 GLY A O 196 N N . ILE A 31 ? 0.5503 0.3853 0.2863 -0.0929 -0.1523 -0.0833 31 ILE A N 197 C CA . ILE A 31 ? 0.5797 0.3996 0.2857 -0.0989 -0.1467 -0.0745 31 ILE A CA 198 C C . ILE A 31 ? 0.6137 0.4294 0.3152 -0.1067 -0.1274 -0.0852 31 ILE A C 199 O O . ILE A 31 ? 0.5467 0.3620 0.2724 -0.1040 -0.1181 -0.0918 31 ILE A O 200 C CB . ILE A 31 ? 0.6015 0.4073 0.3151 -0.0924 -0.1481 -0.0592 31 ILE A CB 201 C CG1 . ILE A 31 ? 0.6140 0.4243 0.3382 -0.0822 -0.1666 -0.0493 31 ILE A CG1 202 C CG2 . ILE A 31 ? 0.6680 0.4582 0.3524 -0.0990 -0.1406 -0.0471 31 ILE A CG2 203 C CD1 . ILE A 31 ? 0.6006 0.3960 0.3395 -0.0740 -0.1679 -0.0368 31 ILE A CD1 204 N N . PRO A 32 ? 0.6002 0.4136 0.2704 -0.1156 -0.1214 -0.0873 32 PRO A N 205 C CA . PRO A 32 ? 0.6431 0.4552 0.3140 -0.1212 -0.1014 -0.0968 32 PRO A CA 206 C C . PRO A 32 ? 0.6483 0.4464 0.3225 -0.1227 -0.0907 -0.0879 32 PRO A C 207 O O . PRO A 32 ? 0.6790 0.4670 0.3428 -0.1214 -0.0957 -0.0716 32 PRO A O 208 C CB . PRO A 32 ? 0.6264 0.4420 0.2642 -0.1275 -0.0978 -0.0990 32 PRO A CB 209 C CG . PRO A 32 ? 0.7095 0.5176 0.3151 -0.1281 -0.1151 -0.0844 32 PRO A CG 210 C CD . PRO A 32 ? 0.6386 0.4523 0.2729 -0.1188 -0.1315 -0.0801 32 PRO A CD 211 N N . TYR A 33 ? 0.6667 0.4654 0.3596 -0.1243 -0.0763 -0.0976 33 TYR A N 212 C CA . TYR A 33 ? 0.5786 0.3673 0.2821 -0.1260 -0.0655 -0.0909 33 TYR A CA 213 C C . TYR A 33 ? 0.6251 0.4152 0.3244 -0.1341 -0.0459 -0.0993 33 TYR A C 214 O O . TYR A 33 ? 0.5842 0.3688 0.2963 -0.1371 -0.0348 -0.0961 33 TYR A O 215 C CB . TYR A 33 ? 0.5986 0.3877 0.3383 -0.1175 -0.0697 -0.0933 33 TYR A CB 216 C CG . TYR A 33 ? 0.5156 0.3162 0.2784 -0.1136 -0.0649 -0.1097 33 TYR A CG 217 C CD1 . TYR A 33 ? 0.5171 0.3195 0.2946 -0.1162 -0.0512 -0.1176 33 TYR A CD1 218 C CD2 . TYR A 33 ? 0.4910 0.3092 0.2720 -0.1027 -0.0716 -0.1128 33 TYR A CD2 219 C CE1 . TYR A 33 ? 0.5180 0.3420 0.3287 -0.1040 -0.0462 -0.1254 33 TYR A CE1 220 C CE2 . TYR A 33 ? 0.4584 0.2956 0.2706 -0.0928 -0.0643 -0.1207 33 TYR A CE2 221 C CZ . TYR A 33 ? 0.4890 0.3283 0.3143 -0.0925 -0.0531 -0.1263 33 TYR A CZ 222 O OH . TYR A 33 ? 0.4533 0.3079 0.3048 -0.0817 -0.0493 -0.1324 33 TYR A OH 223 N N . ALA A 34 ? 0.6728 0.4704 0.3566 -0.1375 -0.0417 -0.1109 34 ALA A N 224 C CA . ALA A 34 ? 0.6636 0.4635 0.3425 -0.1442 -0.0227 -0.1200 34 ALA A CA 225 C C . ALA A 34 ? 0.6460 0.4523 0.2992 -0.1470 -0.0202 -0.1283 34 ALA A C 226 O O . ALA A 34 ? 0.6173 0.4334 0.2725 -0.1400 -0.0331 -0.1276 34 ALA A O 227 C CB . ALA A 34 ? 0.5601 0.3689 0.2774 -0.1389 -0.0153 -0.1316 34 ALA A CB 228 N N . GLN A 35 ? 0.6727 0.4786 0.3118 -0.1541 -0.0022 -0.1348 35 GLN A N 229 C CA . GLN A 35 ? 0.6839 0.5013 0.3130 -0.1519 0.0029 -0.1426 35 GLN A CA 230 C C . GLN A 35 ? 0.6377 0.4714 0.3097 -0.1387 -0.0018 -0.1509 35 GLN A C 231 O O . GLN A 35 ? 0.5765 0.4146 0.2818 -0.1334 0.0033 -0.1536 35 GLN A O 232 C CB . GLN A 35 ? 0.8063 0.6211 0.4213 -0.1604 0.0259 -0.1493 35 GLN A CB 233 C CG . GLN A 35 ? 0.9988 0.8172 0.5796 -0.1629 0.0326 -0.1529 35 GLN A CG 234 C CD . GLN A 35 ? 1.2044 1.0113 0.7437 -0.1755 0.0513 -0.1473 35 GLN A CD 235 O OE1 . GLN A 35 ? 1.2101 1.0207 0.7617 -0.1786 0.0721 -0.1528 35 GLN A OE1 236 N NE2 . GLN A 35 ? 1.3155 1.1154 0.8232 -0.1769 0.0433 -0.1289 35 GLN A NE2 237 N N . PRO A 36 ? 0.6180 0.4598 0.2882 -0.1333 -0.0120 -0.1545 36 PRO A N 238 C CA . PRO A 36 ? 0.5819 0.4344 0.2870 -0.1229 -0.0143 -0.1624 36 PRO A CA 239 C C . PRO A 36 ? 0.5776 0.4317 0.2950 -0.1224 0.0026 -0.1707 36 PRO A C 240 O O . PRO A 36 ? 0.6241 0.4762 0.3184 -0.1287 0.0140 -0.1763 36 PRO A O 241 C CB . PRO A 36 ? 0.6132 0.4703 0.3036 -0.1221 -0.0241 -0.1680 36 PRO A CB 242 C CG . PRO A 36 ? 0.6281 0.4810 0.2864 -0.1277 -0.0344 -0.1590 36 PRO A CG 243 C CD . PRO A 36 ? 0.6438 0.4846 0.2794 -0.1366 -0.0226 -0.1515 36 PRO A CD 244 N N . PRO A 37 ? 0.5920 0.4501 0.3439 -0.1144 0.0043 -0.1711 37 PRO A N 245 C CA . PRO A 37 ? 0.5399 0.4003 0.3056 -0.1134 0.0195 -0.1777 37 PRO A CA 246 C C . PRO A 37 ? 0.5711 0.4338 0.3439 -0.1087 0.0217 -0.1869 37 PRO A C 247 O O . PRO A 37 ? 0.5730 0.4376 0.3718 -0.1007 0.0211 -0.1878 37 PRO A O 248 C CB . PRO A 37 ? 0.5059 0.3693 0.3023 -0.1057 0.0165 -0.1726 37 PRO A CB 249 C CG . PRO A 37 ? 0.5291 0.3933 0.3340 -0.0988 -0.0001 -0.1666 37 PRO A CG 250 C CD . PRO A 37 ? 0.5135 0.3747 0.2911 -0.1057 -0.0077 -0.1648 37 PRO A CD 251 N N . LEU A 38 ? 0.6522 0.5132 0.3994 -0.1139 0.0243 -0.1938 38 LEU A N 252 C CA . LEU A 38 ? 0.6523 0.5131 0.4020 -0.1106 0.0243 -0.2043 38 LEU A CA 253 C C . LEU A 38 ? 0.6520 0.5130 0.3908 -0.1141 0.0417 -0.2146 38 LEU A C 254 O O . LEU A 38 ? 0.6571 0.5186 0.3781 -0.1211 0.0532 -0.2135 38 LEU A O 255 C CB . LEU A 38 ? 0.7219 0.5817 0.4504 -0.1125 0.0109 -0.2068 38 LEU A CB 256 C CG . LEU A 38 ? 0.7914 0.6527 0.5225 -0.1112 -0.0063 -0.1979 38 LEU A CG 257 C CD1 . LEU A 38 ? 0.8190 0.6814 0.5217 -0.1148 -0.0172 -0.2019 38 LEU A CD1 258 C CD2 . LEU A 38 ? 0.7887 0.6501 0.5521 -0.1039 -0.0142 -0.1968 38 LEU A CD2 259 N N . GLY A 39 ? 0.6541 0.5137 0.4026 -0.1099 0.0445 -0.2248 39 GLY A N 260 C CA . GLY A 39 ? 0.6435 0.5037 0.3830 -0.1119 0.0607 -0.2365 39 GLY A CA 261 C C . GLY A 39 ? 0.6856 0.5505 0.4395 -0.1129 0.0770 -0.2352 39 GLY A C 262 O O . GLY A 39 ? 0.6431 0.5101 0.4275 -0.1070 0.0771 -0.2319 39 GLY A O 263 N N . ARG A 40 ? 0.7125 0.5796 0.4439 -0.1204 0.0910 -0.2378 40 ARG A N 264 C CA . ARG A 40 ? 0.7552 0.6276 0.5005 -0.1234 0.1080 -0.2378 40 ARG A CA 265 C C . ARG A 40 ? 0.7312 0.6044 0.4922 -0.1246 0.1023 -0.2263 40 ARG A C 266 O O . ARG A 40 ? 0.7174 0.5961 0.5013 -0.1245 0.1123 -0.2274 40 ARG A O 267 C CB . ARG A 40 ? 0.8384 0.7119 0.5527 -0.1327 0.1261 -0.2424 40 ARG A CB 268 C CG . ARG A 40 ? 0.9580 0.8258 0.6310 -0.1407 0.1205 -0.2342 40 ARG A CG 269 C CD . ARG A 40 ? 1.0976 0.9662 0.7397 -0.1499 0.1419 -0.2354 40 ARG A CD 270 N NE . ARG A 40 ? 1.2171 1.0901 0.8822 -0.1546 0.1600 -0.2352 40 ARG A NE 271 C CZ . ARG A 40 ? 1.2596 1.1283 0.9243 -0.1626 0.1625 -0.2257 40 ARG A CZ 272 N NH1 . ARG A 40 ? 1.2582 1.1171 0.8987 -0.1664 0.1478 -0.2141 40 ARG A NH1 273 N NH2 . ARG A 40 ? 1.2555 1.1297 0.9456 -0.1666 0.1797 -0.2287 40 ARG A NH2 274 N N . LEU A 41 ? 0.7004 0.5687 0.4508 -0.1251 0.0858 -0.2166 41 LEU A N 275 C CA . LEU A 41 ? 0.7040 0.5716 0.4671 -0.1256 0.0790 -0.2063 41 LEU A CA 276 C C . LEU A 41 ? 0.6339 0.5052 0.4323 -0.1138 0.0676 -0.2024 41 LEU A C 277 O O . LEU A 41 ? 0.5428 0.4154 0.3561 -0.1120 0.0626 -0.1957 41 LEU A O 278 C CB . LEU A 41 ? 0.7746 0.6350 0.5094 -0.1315 0.0674 -0.1972 41 LEU A CB 279 C CG . LEU A 41 ? 0.7853 0.6395 0.4784 -0.1442 0.0787 -0.1968 41 LEU A CG 280 C CD1 . LEU A 41 ? 0.7772 0.6230 0.4418 -0.1485 0.0643 -0.1858 41 LEU A CD1 281 C CD2 . LEU A 41 ? 0.7126 0.5659 0.4095 -0.1528 0.0982 -0.1983 41 LEU A CD2 282 N N . ARG A 42 ? 0.5973 0.4690 0.4070 -0.1061 0.0637 -0.2068 42 ARG A N 283 C CA . ARG A 42 ? 0.6077 0.4806 0.4453 -0.0955 0.0549 -0.2024 42 ARG A CA 284 C C . ARG A 42 ? 0.6126 0.4923 0.4745 -0.0918 0.0637 -0.2038 42 ARG A C 285 O O . ARG A 42 ? 0.5089 0.3926 0.3747 -0.0941 0.0783 -0.2126 42 ARG A O 286 C CB . ARG A 42 ? 0.5801 0.4490 0.4229 -0.0904 0.0525 -0.2081 42 ARG A CB 287 C CG . ARG A 42 ? 0.6003 0.4683 0.4684 -0.0808 0.0470 -0.2039 42 ARG A CG 288 C CD . ARG A 42 ? 0.5654 0.4270 0.4403 -0.0777 0.0493 -0.2115 42 ARG A CD 289 N NE . ARG A 42 ? 0.5414 0.3965 0.4051 -0.0804 0.0388 -0.2120 42 ARG A NE 290 C CZ . ARG A 42 ? 0.5901 0.4377 0.4583 -0.0797 0.0385 -0.2192 42 ARG A CZ 291 N NH1 . ARG A 42 ? 0.5337 0.3784 0.4166 -0.0757 0.0486 -0.2259 42 ARG A NH1 292 N NH2 . ARG A 42 ? 0.5397 0.3824 0.3992 -0.0832 0.0280 -0.2205 42 ARG A NH2 293 N N . PHE A 43 ? 0.5255 0.4074 0.4037 -0.0855 0.0547 -0.1961 43 PHE A N 294 C CA . PHE A 43 ? 0.4557 0.3455 0.3578 -0.0809 0.0594 -0.1975 43 PHE A CA 295 C C . PHE A 43 ? 0.4950 0.3894 0.3974 -0.0894 0.0665 -0.1991 43 PHE A C 296 O O . PHE A 43 ? 0.4639 0.3663 0.3886 -0.0861 0.0681 -0.2012 43 PHE A O 297 C CB . PHE A 43 ? 0.4588 0.3532 0.3782 -0.0760 0.0705 -0.2067 43 PHE A CB 298 C CG . PHE A 43 ? 0.5169 0.4049 0.4407 -0.0681 0.0655 -0.2062 43 PHE A CG 299 C CD1 . PHE A 43 ? 0.4628 0.3479 0.3948 -0.0600 0.0542 -0.1984 43 PHE A CD1 300 C CD2 . PHE A 43 ? 0.4930 0.3770 0.4131 -0.0692 0.0737 -0.2147 43 PHE A CD2 301 C CE1 . PHE A 43 ? 0.4684 0.3460 0.4053 -0.0545 0.0523 -0.1988 43 PHE A CE1 302 C CE2 . PHE A 43 ? 0.4777 0.3540 0.4041 -0.0632 0.0703 -0.2155 43 PHE A CE2 303 C CZ . PHE A 43 ? 0.4885 0.3612 0.4237 -0.0565 0.0602 -0.2073 43 PHE A CZ 304 N N . LYS A 44 ? 0.5299 0.4187 0.4076 -0.1009 0.0711 -0.1991 44 LYS A N 305 C CA . LYS A 44 ? 0.5463 0.4354 0.4221 -0.1115 0.0796 -0.2006 44 LYS A CA 306 C C . LYS A 44 ? 0.5209 0.4040 0.3935 -0.1123 0.0656 -0.1908 44 LYS A C 307 O O . LYS A 44 ? 0.4699 0.3485 0.3341 -0.1065 0.0508 -0.1829 44 LYS A O 308 C CB . LYS A 44 ? 0.5947 0.4777 0.4402 -0.1254 0.0949 -0.2055 44 LYS A CB 309 C CG . LYS A 44 ? 0.6133 0.5031 0.4628 -0.1256 0.1122 -0.2170 44 LYS A CG 310 C CD . LYS A 44 ? 0.7136 0.5988 0.5326 -0.1398 0.1308 -0.2217 44 LYS A CD 311 C CE . LYS A 44 ? 0.8733 0.7685 0.7048 -0.1401 0.1518 -0.2340 44 LYS A CE 312 N NZ . LYS A 44 ? 0.9224 0.8203 0.7603 -0.1291 0.1470 -0.2384 44 LYS A NZ 313 N N . LYS A 45 ? 0.4789 0.3619 0.3608 -0.1199 0.0709 -0.1925 45 LYS A N 314 C CA . LYS A 45 ? 0.4846 0.3586 0.3614 -0.1234 0.0598 -0.1845 45 LYS A CA 315 C C . LYS A 45 ? 0.5496 0.4097 0.3881 -0.1311 0.0563 -0.1780 45 LYS A C 316 O O . LYS A 45 ? 0.5251 0.3818 0.3381 -0.1385 0.0672 -0.1818 45 LYS A O 317 C CB . LYS A 45 ? 0.4846 0.3568 0.3759 -0.1350 0.0699 -0.1892 45 LYS A CB 318 C CG . LYS A 45 ? 0.5175 0.4062 0.4503 -0.1258 0.0683 -0.1954 45 LYS A CG 319 C CD . LYS A 45 ? 0.5576 0.4479 0.5129 -0.1388 0.0805 -0.2027 45 LYS A CD 320 C CE . LYS A 45 ? 0.6252 0.5050 0.5850 -0.1434 0.0698 -0.1939 45 LYS A CE 321 N NZ . LYS A 45 ? 0.6186 0.5053 0.6110 -0.1516 0.0785 -0.1940 45 LYS A NZ 322 N N . PRO A 46 ? 0.4935 0.3464 0.3271 -0.1283 0.0404 -0.1687 46 PRO A N 323 C CA . PRO A 46 ? 0.5166 0.3571 0.3142 -0.1350 0.0346 -0.1622 46 PRO A CA 324 C C . PRO A 46 ? 0.5537 0.3798 0.3222 -0.1522 0.0474 -0.1600 46 PRO A C 325 O O . PRO A 46 ? 0.5523 0.3782 0.3406 -0.1551 0.0529 -0.1545 46 PRO A O 326 C CB . PRO A 46 ? 0.4991 0.3365 0.3067 -0.1275 0.0162 -0.1535 46 PRO A CB 327 C CG . PRO A 46 ? 0.4790 0.3214 0.3195 -0.1232 0.0164 -0.1559 46 PRO A CG 328 C CD . PRO A 46 ? 0.4673 0.3239 0.3273 -0.1181 0.0269 -0.1645 46 PRO A CD 329 N N . GLN A 47 ? 0.6171 0.4387 0.3484 -0.1576 0.0511 -0.1575 47 GLN A N 330 C CA . GLN A 47 ? 0.6644 0.4799 0.3715 -0.1667 0.0630 -0.1452 47 GLN A CA 331 C C . GLN A 47 ? 0.7581 0.5616 0.4442 -0.1669 0.0484 -0.1272 47 GLN A C 332 O O . GLN A 47 ? 0.6728 0.4748 0.3504 -0.1614 0.0305 -0.1274 47 GLN A O 333 C CB . GLN A 47 ? 0.6490 0.4673 0.3229 -0.1712 0.0762 -0.1532 47 GLN A CB 334 C CG . GLN A 47 ? 0.9076 0.7371 0.6018 -0.1700 0.0918 -0.1716 47 GLN A CG 335 C CD . GLN A 47 ? 0.9185 0.7546 0.6459 -0.1730 0.1073 -0.1699 47 GLN A CD 336 O OE1 . GLN A 47 ? 0.9856 0.8184 0.7048 -0.1808 0.1189 -0.1571 47 GLN A OE1 337 N NE2 . GLN A 47 ? 0.8085 0.6546 0.5751 -0.1668 0.1073 -0.1820 47 GLN A NE2 338 N N . SER A 48 ? 0.8313 0.6264 0.5114 -0.1731 0.0564 -0.1110 48 SER A N 339 C CA . SER A 48 ? 0.9004 0.6822 0.5632 -0.1726 0.0435 -0.0916 48 SER A CA 340 C C . SER A 48 ? 0.9242 0.7038 0.5412 -0.1718 0.0343 -0.0874 48 SER A C 341 O O . SER A 48 ? 0.9892 0.7751 0.5808 -0.1747 0.0429 -0.0970 48 SER A O 342 C CB . SER A 48 ? 0.9835 0.7547 0.6490 -0.1802 0.0567 -0.0738 48 SER A CB 343 O OG . SER A 48 ? 1.0277 0.7932 0.7318 -0.1778 0.0493 -0.0702 48 SER A OG 344 N N . LEU A 49 ? 0.9582 0.7295 0.5658 -0.1673 0.0160 -0.0740 49 LEU A N 345 C CA . LEU A 49 ? 1.0554 0.8274 0.6250 -0.1649 0.0021 -0.0713 49 LEU A CA 346 C C . LEU A 49 ? 1.2165 0.9807 0.7412 -0.1700 0.0097 -0.0545 49 LEU A C 347 O O . LEU A 49 ? 1.2617 1.0161 0.7875 -0.1747 0.0233 -0.0389 49 LEU A O 348 C CB . LEU A 49 ? 1.0248 0.7942 0.6064 -0.1565 -0.0217 -0.0649 49 LEU A CB 349 C CG . LEU A 49 ? 1.0238 0.8011 0.5844 -0.1525 -0.0401 -0.0709 49 LEU A CG 350 C CD1 . LEU A 49 ? 0.9902 0.7792 0.5486 -0.1552 -0.0339 -0.0937 49 LEU A CD1 351 C CD2 . LEU A 49 ? 1.0263 0.8052 0.6144 -0.1437 -0.0597 -0.0691 49 LEU A CD2 352 N N . THR A 50 ? 1.3111 1.0802 0.7967 -0.1690 0.0007 -0.0580 50 THR A N 353 C CA . THR A 50 ? 1.4487 1.2130 0.8834 -0.1720 0.0054 -0.0437 50 THR A CA 354 C C . THR A 50 ? 1.4864 1.2364 0.9118 -0.1687 -0.0045 -0.0155 50 THR A C 355 O O . THR A 50 ? 1.5315 1.2698 0.9801 -0.1709 0.0053 -0.0013 50 THR A O 356 C CB . THR A 50 ? 1.5027 1.2771 0.9008 -0.1698 -0.0088 -0.0566 50 THR A CB 357 O OG1 . THR A 50 ? 1.5157 1.2907 0.9180 -0.1626 -0.0359 -0.0508 50 THR A OG1 358 C CG2 . THR A 50 ? 1.4488 1.2350 0.8640 -0.1715 -0.0034 -0.0857 50 THR A CG2 359 N N . LYS A 51 ? 1.4696 1.2207 0.8615 -0.1634 -0.0242 -0.0084 51 LYS A N 360 C CA . LYS A 51 ? 1.4010 1.1400 0.7801 -0.1575 -0.0388 0.0179 51 LYS A CA 361 C C . LYS A 51 ? 1.3864 1.1349 0.7231 -0.1525 -0.0595 0.0163 51 LYS A C 362 O O . LYS A 51 ? 1.4412 1.1956 0.7345 -0.1560 -0.0523 0.0113 51 LYS A O 363 C CB . LYS A 51 ? 1.3903 1.1124 0.7507 -0.1620 -0.0199 0.0440 51 LYS A CB 364 C CG . LYS A 51 ? 1.4244 1.1500 0.7526 -0.1707 0.0062 0.0407 51 LYS A CG 365 C CD . LYS A 51 ? 1.3591 1.0721 0.7098 -0.1785 0.0323 0.0546 51 LYS A CD 366 C CE . LYS A 51 ? 1.2701 0.9933 0.6173 -0.1872 0.0598 0.0393 51 LYS A CE 367 N NZ . LYS A 51 ? 1.2089 0.9375 0.4939 -0.1884 0.0686 0.0413 51 LYS A NZ 368 N N . TRP A 52 ? 1.2959 1.0480 0.6464 -0.1441 -0.0852 0.0186 52 TRP A N 369 C CA . TRP A 52 ? 1.2431 1.0074 0.5594 -0.1392 -0.1079 0.0153 52 TRP A CA 370 C C . TRP A 52 ? 1.2405 0.9963 0.5335 -0.1306 -0.1251 0.0436 52 TRP A C 371 O O . TRP A 52 ? 1.1586 0.9003 0.4774 -0.1261 -0.1263 0.0622 52 TRP A O 372 C CB . TRP A 52 ? 1.1650 0.9459 0.5134 -0.1368 -0.1253 -0.0087 52 TRP A CB 373 C CG . TRP A 52 ? 1.1264 0.9052 0.5223 -0.1296 -0.1379 -0.0030 52 TRP A CG 374 C CD1 . TRP A 52 ? 1.1351 0.9166 0.5353 -0.1202 -0.1618 0.0090 52 TRP A CD1 375 C CD2 . TRP A 52 ? 1.0715 0.8463 0.5166 -0.1302 -0.1274 -0.0100 52 TRP A CD2 376 N NE1 . TRP A 52 ? 1.0603 0.8392 0.5095 -0.1150 -0.1653 0.0095 52 TRP A NE1 377 C CE2 . TRP A 52 ? 1.0192 0.7939 0.4948 -0.1209 -0.1449 -0.0022 52 TRP A CE2 378 C CE3 . TRP A 52 ? 1.0797 0.8521 0.5459 -0.1368 -0.1056 -0.0224 52 TRP A CE3 379 C CZ2 . TRP A 52 ? 1.0149 0.7867 0.5377 -0.1181 -0.1407 -0.0070 52 TRP A CZ2 380 C CZ3 . TRP A 52 ? 1.0488 0.8190 0.5625 -0.1339 -0.1031 -0.0266 52 TRP A CZ3 381 C CH2 . TRP A 52 ? 1.0037 0.7733 0.5434 -0.1246 -0.1203 -0.0193 52 TRP A CH2 382 N N . SER A 53 ? 1.3131 1.0779 0.5582 -0.1274 -0.1389 0.0458 53 SER A N 383 C CA . SER A 53 ? 1.3400 1.0994 0.5580 -0.1175 -0.1521 0.0742 53 SER A CA 384 C C . SER A 53 ? 1.3393 1.1155 0.5811 -0.1051 -0.1825 0.0726 53 SER A C 385 O O . SER A 53 ? 1.3621 1.1315 0.5944 -0.0953 -0.1965 0.0971 53 SER A O 386 C CB . SER A 53 ? 1.3673 1.1382 0.5401 -0.1147 -0.1431 0.0774 53 SER A CB 387 O OG . SER A 53 ? 1.4114 1.2133 0.5890 -0.1092 -0.1558 0.0516 53 SER A OG 388 N N . ASP A 54 ? 1.3083 1.1075 0.5841 -0.1050 -0.1911 0.0441 54 ASP A N 389 C CA . ASP A 54 ? 1.3114 1.1304 0.6162 -0.0945 -0.2172 0.0398 54 ASP A CA 390 C C . ASP A 54 ? 1.1921 1.0018 0.5423 -0.0943 -0.2241 0.0395 54 ASP A C 391 O O . ASP A 54 ? 1.1073 0.8929 0.4629 -0.1000 -0.2112 0.0475 54 ASP A O 392 C CB . ASP A 54 ? 1.3905 1.2416 0.7079 -0.0938 -0.2224 0.0105 54 ASP A CB 393 C CG . ASP A 54 ? 1.4455 1.2974 0.7748 -0.1043 -0.2013 -0.0139 54 ASP A CG 394 O OD1 . ASP A 54 ? 1.4702 1.3011 0.7838 -0.1125 -0.1805 -0.0078 54 ASP A OD1 395 O OD2 . ASP A 54 ? 1.4498 1.3235 0.8058 -0.1041 -0.2050 -0.0387 54 ASP A OD2 396 N N . ILE A 55 ? 1.1346 0.9658 0.5206 -0.0867 -0.2432 0.0297 55 ILE A N 397 C CA . ILE A 55 ? 1.0527 0.8798 0.4840 -0.0840 -0.2505 0.0283 55 ILE A CA 398 C C . ILE A 55 ? 1.0073 0.8499 0.4771 -0.0902 -0.2418 -0.0002 55 ILE A C 399 O O . ILE A 55 ? 0.9762 0.8449 0.4587 -0.0897 -0.2458 -0.0181 55 ILE A O 400 C CB . ILE A 55 ? 1.0547 0.8966 0.5070 -0.0706 -0.2751 0.0377 55 ILE A CB 401 C CG1 . ILE A 55 ? 1.0880 0.9126 0.5082 -0.0619 -0.2833 0.0689 55 ILE A CG1 402 C CG2 . ILE A 55 ? 1.0030 0.8452 0.5057 -0.0669 -0.2810 0.0325 55 ILE A CG2 403 C CD1 . ILE A 55 ? 0.9828 0.8213 0.4254 -0.0470 -0.3067 0.0798 55 ILE A CD1 404 N N . TRP A 56 ? 0.9079 0.7344 0.3970 -0.0955 -0.2298 -0.0039 56 TRP A N 405 C CA . TRP A 56 ? 0.8529 0.6929 0.3818 -0.0993 -0.2197 -0.0277 56 TRP A CA 406 C C . TRP A 56 ? 0.8479 0.7024 0.4222 -0.0912 -0.2335 -0.0310 56 TRP A C 407 O O . TRP A 56 ? 0.9029 0.7448 0.4909 -0.0852 -0.2406 -0.0188 56 TRP A O 408 C CB . TRP A 56 ? 0.8658 0.6871 0.4014 -0.1063 -0.1990 -0.0312 56 TRP A CB 409 C CG . TRP A 56 ? 0.8558 0.6904 0.4302 -0.1084 -0.1889 -0.0531 56 TRP A CG 410 C CD1 . TRP A 56 ? 0.7678 0.6107 0.3858 -0.1027 -0.1929 -0.0585 56 TRP A CD1 411 C CD2 . TRP A 56 ? 0.9030 0.7462 0.4806 -0.1142 -0.1707 -0.0705 56 TRP A CD2 412 N NE1 . TRP A 56 ? 0.7837 0.6393 0.4298 -0.1048 -0.1778 -0.0764 56 TRP A NE1 413 C CE2 . TRP A 56 ? 0.8428 0.6984 0.4664 -0.1114 -0.1649 -0.0841 56 TRP A CE2 414 C CE3 . TRP A 56 ? 0.9798 0.8214 0.5259 -0.1203 -0.1585 -0.0754 56 TRP A CE3 415 C CZ2 . TRP A 56 ? 0.8478 0.7127 0.4877 -0.1138 -0.1487 -0.1008 56 TRP A CZ2 416 C CZ3 . TRP A 56 ? 0.9648 0.8162 0.5289 -0.1227 -0.1427 -0.0940 56 TRP A CZ3 417 C CH2 . TRP A 56 ? 0.8888 0.7510 0.4998 -0.1190 -0.1387 -0.1059 56 TRP A CH2 418 N N . ASN A 57 ? 0.8280 0.7091 0.4280 -0.0906 -0.2358 -0.0479 57 ASN A N 419 C CA . ASN A 57 ? 0.8327 0.7298 0.4775 -0.0845 -0.2454 -0.0523 57 ASN A CA 420 C C . ASN A 57 ? 0.7350 0.6271 0.4129 -0.0863 -0.2306 -0.0616 57 ASN A C 421 O O . ASN A 57 ? 0.6763 0.5751 0.3655 -0.0920 -0.2150 -0.0771 57 ASN A O 422 C CB . ASN A 57 ? 0.9589 0.8858 0.6185 -0.0849 -0.2537 -0.0661 57 ASN A CB 423 C CG . ASN A 57 ? 1.1729 1.1100 0.8097 -0.0791 -0.2736 -0.0556 57 ASN A CG 424 O OD1 . ASN A 57 ? 1.1809 1.1028 0.7958 -0.0729 -0.2823 -0.0353 57 ASN A OD1 425 N ND2 . ASN A 57 ? 1.3940 1.3571 1.0368 -0.0807 -0.2815 -0.0691 57 ASN A ND2 426 N N . ALA A 58 ? 0.6828 0.5633 0.3762 -0.0797 -0.2356 -0.0517 58 ALA A N 427 C CA . ALA A 58 ? 0.6134 0.4907 0.3379 -0.0788 -0.2232 -0.0597 58 ALA A CA 428 C C . ALA A 58 ? 0.5896 0.4845 0.3540 -0.0705 -0.2329 -0.0617 58 ALA A C 429 O O . ALA A 58 ? 0.6141 0.5026 0.3966 -0.0614 -0.2366 -0.0547 58 ALA A O 430 C CB . ALA A 58 ? 0.6130 0.4666 0.3323 -0.0759 -0.2147 -0.0493 58 ALA A CB 431 N N . THR A 59 ? 0.6169 0.5355 0.3983 -0.0731 -0.2345 -0.0717 59 THR A N 432 C CA . THR A 59 ? 0.5959 0.5342 0.4133 -0.0668 -0.2455 -0.0727 59 THR A CA 433 C C . THR A 59 ? 0.5872 0.5394 0.4353 -0.0716 -0.2329 -0.0871 59 THR A C 434 O O . THR A 59 ? 0.5772 0.5490 0.4549 -0.0700 -0.2408 -0.0904 59 THR A O 435 C CB . THR A 59 ? 0.6636 0.6202 0.4765 -0.0656 -0.2640 -0.0696 59 THR A CB 436 O OG1 . THR A 59 ? 0.6729 0.6369 0.4664 -0.0755 -0.2587 -0.0805 59 THR A OG1 437 C CG2 . THR A 59 ? 0.6581 0.6018 0.4455 -0.0577 -0.2788 -0.0515 59 THR A CG2 438 N N . LYS A 60 ? 0.5701 0.5123 0.4125 -0.0774 -0.2136 -0.0949 60 LYS A N 439 C CA . LYS A 60 ? 0.4998 0.4507 0.3684 -0.0814 -0.2004 -0.1063 60 LYS A CA 440 C C . LYS A 60 ? 0.6590 0.5947 0.5203 -0.0829 -0.1802 -0.1099 60 LYS A C 441 O O . LYS A 60 ? 0.4981 0.4213 0.3329 -0.0852 -0.1744 -0.1083 60 LYS A O 442 C CB . LYS A 60 ? 0.5096 0.4773 0.3834 -0.0908 -0.2017 -0.1178 60 LYS A CB 443 C CG . LYS A 60 ? 0.8946 0.8575 0.7450 -0.0983 -0.1901 -0.1274 60 LYS A CG 444 C CD . LYS A 60 ? 0.9792 0.9596 0.8397 -0.1069 -0.1931 -0.1413 60 LYS A CD 445 C CE . LYS A 60 ? 1.0371 1.0136 0.8831 -0.1121 -0.1802 -0.1550 60 LYS A CE 446 N NZ . LYS A 60 ? 1.0495 1.0181 0.8570 -0.1096 -0.1839 -0.1520 60 LYS A NZ 447 N N . TYR A 61 ? 0.4603 0.3974 0.3453 -0.0810 -0.1700 -0.1141 61 TYR A N 448 C CA . TYR A 61 ? 0.5025 0.4289 0.3846 -0.0813 -0.1512 -0.1179 61 TYR A CA 449 C C . TYR A 61 ? 0.4828 0.4100 0.3519 -0.0897 -0.1408 -0.1270 61 TYR A C 450 O O . TYR A 61 ? 0.4657 0.4038 0.3381 -0.0959 -0.1451 -0.1342 61 TYR A O 451 C CB . TYR A 61 ? 0.4810 0.4109 0.3897 -0.0781 -0.1442 -0.1213 61 TYR A CB 452 C CG . TYR A 61 ? 0.4500 0.3788 0.3732 -0.0662 -0.1509 -0.1157 61 TYR A CG 453 C CD1 . TYR A 61 ? 0.4325 0.3488 0.3454 -0.0587 -0.1472 -0.1116 61 TYR A CD1 454 C CD2 . TYR A 61 ? 0.4477 0.3910 0.3995 -0.0618 -0.1583 -0.1155 61 TYR A CD2 455 C CE1 . TYR A 61 ? 0.4460 0.3643 0.3740 -0.0460 -0.1494 -0.1074 61 TYR A CE1 456 C CE2 . TYR A 61 ? 0.3905 0.3391 0.3586 -0.0480 -0.1562 -0.1085 61 TYR A CE2 457 C CZ . TYR A 61 ? 0.4299 0.3654 0.3848 -0.0399 -0.1521 -0.1052 61 TYR A CZ 458 O OH . TYR A 61 ? 0.4228 0.3629 0.3928 -0.0257 -0.1503 -0.1008 61 TYR A OH 459 N N . ALA A 62 ? 0.4528 0.3697 0.3096 -0.0889 -0.1283 -0.1279 62 ALA A N 460 C CA . ALA A 62 ? 0.6164 0.5331 0.4633 -0.0931 -0.1197 -0.1371 62 ALA A CA 461 C C . ALA A 62 ? 0.6040 0.5231 0.4736 -0.0919 -0.1071 -0.1465 62 ALA A C 462 O O . ALA A 62 ? 0.4253 0.3458 0.3127 -0.0903 -0.1031 -0.1446 62 ALA A O 463 C CB . ALA A 62 ? 0.4738 0.3767 0.2964 -0.0926 -0.1143 -0.1323 62 ALA A CB 464 N N . ASN A 63 ? 0.4532 0.3678 0.3186 -0.0919 -0.1026 -0.1549 63 ASN A N 465 C CA . ASN A 63 ? 0.4845 0.3895 0.3652 -0.0878 -0.0950 -0.1593 63 ASN A CA 466 C C . ASN A 63 ? 0.4376 0.3369 0.3260 -0.0810 -0.0853 -0.1529 63 ASN A C 467 O O . ASN A 63 ? 0.4187 0.3182 0.2972 -0.0796 -0.0819 -0.1487 63 ASN A O 468 C CB . ASN A 63 ? 0.4632 0.3575 0.3271 -0.0895 -0.0907 -0.1644 63 ASN A CB 469 C CG . ASN A 63 ? 0.5024 0.4007 0.3560 -0.0951 -0.1006 -0.1728 63 ASN A CG 470 O OD1 . ASN A 63 ? 0.5450 0.4509 0.4120 -0.0975 -0.1110 -0.1757 63 ASN A OD1 471 N ND2 . ASN A 63 ? 0.5373 0.4313 0.3672 -0.0974 -0.0971 -0.1770 63 ASN A ND2 472 N N . SER A 64 ? 0.4136 0.3028 0.3139 -0.0783 -0.0817 -0.1499 64 SER A N 473 C CA . SER A 64 ? 0.4423 0.3234 0.3438 -0.0721 -0.0732 -0.1443 64 SER A CA 474 C C . SER A 64 ? 0.4825 0.3549 0.3773 -0.0718 -0.0640 -0.1479 64 SER A C 475 O O . SER A 64 ? 0.4199 0.2896 0.3122 -0.0769 -0.0630 -0.1533 64 SER A O 476 C CB . SER A 64 ? 0.3952 0.2692 0.3034 -0.0754 -0.0689 -0.1409 64 SER A CB 477 O OG . SER A 64 ? 0.4747 0.3588 0.3873 -0.0815 -0.0729 -0.1390 64 SER A OG 478 N N . CYS A 65 ? 0.3961 0.2663 0.2898 -0.0660 -0.0566 -0.1450 65 CYS A N 479 C CA . CYS A 65 ? 0.4272 0.2936 0.3184 -0.0658 -0.0463 -0.1482 65 CYS A CA 480 C C . CYS A 65 ? 0.4710 0.3318 0.3727 -0.0663 -0.0386 -0.1510 65 CYS A C 481 O O . CYS A 65 ? 0.4133 0.2733 0.3254 -0.0653 -0.0378 -0.1491 65 CYS A O 482 C CB . CYS A 65 ? 0.3917 0.2590 0.2816 -0.0604 -0.0414 -0.1455 65 CYS A CB 483 S SG . CYS A 65 ? 0.4014 0.2746 0.2828 -0.0621 -0.0472 -0.1436 65 CYS A SG 484 N N . CYS A 66 ? 0.4191 0.2716 0.4128 -0.0612 -0.0448 -0.1068 66 CYS A N 485 C CA . CYS A 66 ? 0.5091 0.3360 0.4977 -0.0612 -0.0334 -0.1073 66 CYS A CA 486 C C . CYS A 66 ? 0.4877 0.3237 0.4961 -0.0507 -0.0338 -0.0960 66 CYS A C 487 O O . CYS A 66 ? 0.4412 0.2943 0.4647 -0.0396 -0.0359 -0.0874 66 CYS A O 488 C CB . CYS A 66 ? 0.4710 0.2703 0.4477 -0.0553 -0.0167 -0.1103 66 CYS A CB 489 S SG . CYS A 66 ? 0.6766 0.4580 0.6243 -0.0703 -0.0130 -0.1249 66 CYS A SG 490 N N . GLN A 67 ? 0.4361 0.2618 0.4434 -0.0555 -0.0320 -0.0957 67 GLN A N 491 C CA . GLN A 67 ? 0.5368 0.3724 0.5623 -0.0471 -0.0330 -0.0847 67 GLN A CA 492 C C . GLN A 67 ? 0.6219 0.4381 0.6419 -0.0530 -0.0274 -0.0856 67 GLN A C 493 O O . GLN A 67 ? 0.4582 0.2616 0.4617 -0.0674 -0.0283 -0.0950 67 GLN A O 494 C CB . GLN A 67 ? 0.3895 0.2566 0.4280 -0.0484 -0.0484 -0.0807 67 GLN A CB 495 C CG . GLN A 67 ? 0.3864 0.2610 0.4171 -0.0620 -0.0582 -0.0876 67 GLN A CG 496 C CD . GLN A 67 ? 0.4248 0.3277 0.4663 -0.0606 -0.0705 -0.0835 67 GLN A CD 497 O OE1 . GLN A 67 ? 0.3456 0.2595 0.3967 -0.0599 -0.0752 -0.0781 67 GLN A OE1 498 N NE2 . GLN A 67 ? 0.3503 0.2628 0.3887 -0.0600 -0.0745 -0.0859 67 GLN A NE2 499 N N . ASN A 68 ? 0.4392 0.2550 0.4729 -0.0429 -0.0220 -0.0748 68 ASN A N 500 C CA . ASN A 68 ? 0.4908 0.2923 0.5223 -0.0481 -0.0185 -0.0738 68 ASN A CA 501 C C . ASN A 68 ? 0.4301 0.2555 0.4681 -0.0575 -0.0342 -0.0741 68 ASN A C 502 O O . ASN A 68 ? 0.4620 0.3152 0.5114 -0.0549 -0.0453 -0.0708 68 ASN A O 503 C CB . ASN A 68 ? 0.4591 0.2543 0.5039 -0.0334 -0.0072 -0.0604 68 ASN A CB 504 C CG . ASN A 68 ? 0.5700 0.3359 0.6060 -0.0233 0.0121 -0.0594 68 ASN A CG 505 O OD1 . ASN A 68 ? 0.5707 0.3013 0.5855 -0.0302 0.0237 -0.0687 68 ASN A OD1 506 N ND2 . ASN A 68 ? 0.5429 0.3233 0.5938 -0.0076 0.0164 -0.0479 68 ASN A ND2 507 N N . ILE A 69 ? 0.4450 0.2580 0.4743 -0.0688 -0.0339 -0.0780 69 ILE A N 508 C CA . ILE A 69 ? 0.4350 0.2700 0.4690 -0.0784 -0.0474 -0.0781 69 ILE A CA 509 C C . ILE A 69 ? 0.4335 0.2701 0.4795 -0.0750 -0.0463 -0.0691 69 ILE A C 510 O O . ILE A 69 ? 0.4449 0.2580 0.4888 -0.0704 -0.0340 -0.0656 69 ILE A O 511 C CB . ILE A 69 ? 0.6925 0.5184 0.7065 -0.0974 -0.0500 -0.0890 69 ILE A CB 512 C CG1 . ILE A 69 ? 0.6867 0.5298 0.6961 -0.1013 -0.0581 -0.0943 69 ILE A CG1 513 C CG2 . ILE A 69 ? 0.7041 0.5421 0.7207 -0.1082 -0.0580 -0.0871 69 ILE A CG2 514 C CD1 . ILE A 69 ? 0.6943 0.5193 0.6927 -0.0974 -0.0492 -0.0997 69 ILE A CD1 515 N N . ASP A 70 ? 0.4141 0.2775 0.4720 -0.0763 -0.0579 -0.0647 70 ASP A N 516 C CA . ASP A 70 ? 0.4698 0.3378 0.5381 -0.0753 -0.0586 -0.0567 70 ASP A CA 517 C C . ASP A 70 ? 0.4850 0.3374 0.5409 -0.0898 -0.0572 -0.0618 70 ASP A C 518 O O . ASP A 70 ? 0.4109 0.2762 0.4613 -0.1015 -0.0661 -0.0668 70 ASP A O 519 C CB . ASP A 70 ? 0.4151 0.3155 0.4969 -0.0732 -0.0707 -0.0516 70 ASP A CB 520 C CG . ASP A 70 ? 0.4427 0.3511 0.5356 -0.0721 -0.0721 -0.0429 70 ASP A CG 521 O OD1 . ASP A 70 ? 0.5246 0.4151 0.6149 -0.0746 -0.0652 -0.0410 70 ASP A OD1 522 O OD2 . ASP A 70 ? 0.3671 0.2985 0.4699 -0.0691 -0.0795 -0.0380 70 ASP A OD2 523 N N . GLN A 71 ? 0.4407 0.2663 0.4920 -0.0892 -0.0455 -0.0595 71 GLN A N 524 C CA . GLN A 71 ? 0.5371 0.3432 0.5737 -0.1046 -0.0426 -0.0645 71 GLN A CA 525 C C . GLN A 71 ? 0.5147 0.3247 0.5629 -0.1027 -0.0425 -0.0550 71 GLN A C 526 O O . GLN A 71 ? 0.4961 0.2855 0.5330 -0.1136 -0.0374 -0.0571 71 GLN A O 527 C CB . GLN A 71 ? 0.5083 0.2711 0.5238 -0.1082 -0.0261 -0.0711 71 GLN A CB 528 C CG . GLN A 71 ? 0.8205 0.5733 0.8228 -0.1084 -0.0225 -0.0800 71 GLN A CG 529 C CD . GLN A 71 ? 0.8620 0.5694 0.8465 -0.1053 -0.0021 -0.0836 71 GLN A CD 530 O OE1 . GLN A 71 ? 0.9017 0.6017 0.8872 -0.0925 0.0060 -0.0826 71 GLN A OE1 531 N NE2 . GLN A 71 ? 0.7831 0.4585 0.7500 -0.1171 0.0073 -0.0872 71 GLN A NE2 532 N N . SER A 72 ? 0.4618 0.2976 0.5308 -0.0905 -0.0481 -0.0448 72 SER A N 533 C CA . SER A 72 ? 0.4914 0.3327 0.5724 -0.0876 -0.0477 -0.0345 72 SER A CA 534 C C . SER A 72 ? 0.4333 0.2873 0.5128 -0.1014 -0.0571 -0.0362 72 SER A C 535 O O . SER A 72 ? 0.4360 0.2821 0.5174 -0.1043 -0.0537 -0.0309 72 SER A O 536 C CB . SER A 72 ? 0.4252 0.2926 0.5266 -0.0732 -0.0516 -0.0230 72 SER A CB 537 O OG . SER A 72 ? 0.4619 0.3206 0.5656 -0.0609 -0.0428 -0.0195 72 SER A OG 538 N N . PHE A 73 ? 0.4108 0.2854 0.4874 -0.1095 -0.0681 -0.0423 73 PHE A N 539 C CA . PHE A 73 ? 0.4692 0.3608 0.5459 -0.1218 -0.0769 -0.0422 73 PHE A CA 540 C C . PHE A 73 ? 0.4134 0.3092 0.4756 -0.1369 -0.0823 -0.0511 73 PHE A C 541 O O . PHE A 73 ? 0.4467 0.3712 0.5146 -0.1374 -0.0919 -0.0504 73 PHE A O 542 C CB . PHE A 73 ? 0.4502 0.3754 0.5440 -0.1140 -0.0862 -0.0350 73 PHE A CB 543 C CG . PHE A 73 ? 0.4311 0.3589 0.5387 -0.1012 -0.0828 -0.0254 73 PHE A CG 544 C CD1 . PHE A 73 ? 0.3972 0.3195 0.5098 -0.1023 -0.0795 -0.0182 73 PHE A CD1 545 C CD2 . PHE A 73 ? 0.4604 0.3981 0.5756 -0.0893 -0.0834 -0.0227 73 PHE A CD2 546 C CE1 . PHE A 73 ? 0.3777 0.3065 0.5037 -0.0913 -0.0769 -0.0075 73 PHE A CE1 547 C CE2 . PHE A 73 ? 0.3713 0.3158 0.4987 -0.0798 -0.0811 -0.0124 73 PHE A CE2 548 C CZ . PHE A 73 ? 0.3547 0.2961 0.4881 -0.0806 -0.0780 -0.0043 73 PHE A CZ 549 N N . PRO A 74 ? 0.4580 0.3254 0.5005 -0.1498 -0.0752 -0.0587 74 PRO A N 550 C CA . PRO A 74 ? 0.5046 0.3776 0.5313 -0.1673 -0.0806 -0.0664 74 PRO A CA 551 C C . PRO A 74 ? 0.5024 0.4096 0.5356 -0.1776 -0.0925 -0.0616 74 PRO A C 552 O O . PRO A 74 ? 0.4422 0.3523 0.4814 -0.1801 -0.0931 -0.0560 74 PRO A O 553 C CB . PRO A 74 ? 0.5006 0.3334 0.5031 -0.1827 -0.0696 -0.0739 74 PRO A CB 554 C CG . PRO A 74 ? 0.5121 0.3144 0.5179 -0.1676 -0.0559 -0.0709 74 PRO A CG 555 C CD . PRO A 74 ? 0.4775 0.3059 0.5101 -0.1500 -0.0612 -0.0593 74 PRO A CD 556 N N . GLY A 75 ? 0.4304 0.3644 0.4632 -0.1824 -0.1012 -0.0624 75 GLY A N 557 C CA . GLY A 75 ? 0.5532 0.5232 0.5934 -0.1904 -0.1115 -0.0556 75 GLY A CA 558 C C . GLY A 75 ? 0.4866 0.4851 0.5489 -0.1734 -0.1164 -0.0464 75 GLY A C 559 O O . GLY A 75 ? 0.3721 0.4021 0.4419 -0.1768 -0.1235 -0.0393 75 GLY A O 560 N N . PHE A 76 ? 0.3971 0.3850 0.4685 -0.1558 -0.1120 -0.0457 76 PHE A N 561 C CA . PHE A 76 ? 0.4104 0.4192 0.4988 -0.1411 -0.1150 -0.0382 76 PHE A CA 562 C C . PHE A 76 ? 0.3427 0.3635 0.4351 -0.1290 -0.1167 -0.0387 76 PHE A C 563 O O . PHE A 76 ? 0.4140 0.4185 0.5034 -0.1221 -0.1127 -0.0433 76 PHE A O 564 C CB . PHE A 76 ? 0.3438 0.3360 0.4390 -0.1323 -0.1094 -0.0354 76 PHE A CB 565 C CG . PHE A 76 ? 0.3207 0.3314 0.4298 -0.1197 -0.1118 -0.0286 76 PHE A CG 566 C CD1 . PHE A 76 ? 0.3102 0.3449 0.4259 -0.1212 -0.1165 -0.0226 76 PHE A CD1 567 C CD2 . PHE A 76 ? 0.3123 0.3161 0.4262 -0.1075 -0.1085 -0.0277 76 PHE A CD2 568 C CE1 . PHE A 76 ? 0.2938 0.3413 0.4184 -0.1108 -0.1170 -0.0175 76 PHE A CE1 569 C CE2 . PHE A 76 ? 0.2957 0.3142 0.4182 -0.0992 -0.1102 -0.0222 76 PHE A CE2 570 C CZ . PHE A 76 ? 0.2876 0.3258 0.4143 -0.1008 -0.1139 -0.0179 76 PHE A CZ 571 N N . HIS A 77 ? 0.3209 0.3694 0.4200 -0.1258 -0.1216 -0.0331 77 HIS A N 572 C CA . HIS A 77 ? 0.3609 0.4198 0.4621 -0.1150 -0.1223 -0.0329 77 HIS A CA 573 C C . HIS A 77 ? 0.3564 0.4037 0.4614 -0.1013 -0.1184 -0.0339 77 HIS A C 574 O O . HIS A 77 ? 0.3197 0.3647 0.4224 -0.0943 -0.1174 -0.0365 77 HIS A O 575 C CB . HIS A 77 ? 0.2897 0.3792 0.3979 -0.1120 -0.1257 -0.0245 77 HIS A CB 576 C CG . HIS A 77 ? 0.5316 0.6298 0.6403 -0.1011 -0.1248 -0.0233 77 HIS A CG 577 N ND1 . HIS A 77 ? 0.4598 0.5592 0.5620 -0.1045 -0.1263 -0.0265 77 HIS A ND1 578 C CD2 . HIS A 77 ? 0.5401 0.6441 0.6531 -0.0875 -0.1217 -0.0194 77 HIS A CD2 579 C CE1 . HIS A 77 ? 0.4039 0.5106 0.5082 -0.0925 -0.1244 -0.0238 77 HIS A CE1 580 N NE2 . HIS A 77 ? 0.4958 0.6036 0.6057 -0.0821 -0.1210 -0.0198 77 HIS A NE2 581 N N . GLY A 78 ? 0.2876 0.3294 0.3981 -0.0986 -0.1166 -0.0310 78 GLY A N 582 C CA . GLY A 78 ? 0.2788 0.3150 0.3926 -0.0883 -0.1139 -0.0301 78 GLY A CA 583 C C . GLY A 78 ? 0.3450 0.3631 0.4550 -0.0853 -0.1106 -0.0348 78 GLY A C 584 O O . GLY A 78 ? 0.2931 0.3108 0.4030 -0.0779 -0.1095 -0.0351 78 GLY A O 585 N N . SER A 79 ? 0.2980 0.3003 0.4036 -0.0915 -0.1081 -0.0381 79 SER A N 586 C CA . SER A 79 ? 0.3819 0.3660 0.4834 -0.0879 -0.1032 -0.0420 79 SER A CA 587 C C . SER A 79 ? 0.4114 0.3924 0.5030 -0.0921 -0.1039 -0.0490 79 SER A C 588 O O . SER A 79 ? 0.3205 0.2968 0.4098 -0.0863 -0.1022 -0.0518 79 SER A O 589 C CB . SER A 79 ? 0.3405 0.3041 0.4409 -0.0905 -0.0968 -0.0411 79 SER A CB 590 O OG . SER A 79 ? 0.4095 0.3666 0.5023 -0.1029 -0.0970 -0.0441 79 SER A OG 591 N N . GLU A 80 ? 0.3209 0.3070 0.4065 -0.1033 -0.1069 -0.0511 80 GLU A N 592 C CA . GLU A 80 ? 0.3305 0.3150 0.4052 -0.1103 -0.1079 -0.0571 80 GLU A CA 593 C C . GLU A 80 ? 0.3155 0.3182 0.3926 -0.1034 -0.1119 -0.0561 80 GLU A C 594 O O . GLU A 80 ? 0.3489 0.3477 0.4183 -0.1051 -0.1115 -0.0608 80 GLU A O 595 C CB . GLU A 80 ? 0.3468 0.3339 0.4126 -0.1274 -0.1105 -0.0587 80 GLU A CB 596 C CG . GLU A 80 ? 0.3718 0.3290 0.4276 -0.1358 -0.1033 -0.0630 80 GLU A CG 597 C CD . GLU A 80 ? 0.4888 0.4439 0.5304 -0.1566 -0.1051 -0.0662 80 GLU A CD 598 O OE1 . GLU A 80 ? 0.4653 0.4485 0.5083 -0.1648 -0.1132 -0.0627 80 GLU A OE1 599 O OE2 . GLU A 80 ? 0.4311 0.3562 0.4594 -0.1653 -0.0975 -0.0715 80 GLU A OE2 600 N N . MET A 81 ? 0.2991 0.3190 0.3855 -0.0954 -0.1144 -0.0499 81 MET A N 601 C CA . MET A 81 ? 0.2884 0.3214 0.3758 -0.0875 -0.1159 -0.0482 81 MET A CA 602 C C . MET A 81 ? 0.3104 0.3297 0.3946 -0.0801 -0.1127 -0.0525 81 MET A C 603 O O . MET A 81 ? 0.3449 0.3704 0.4268 -0.0756 -0.1133 -0.0527 81 MET A O 604 C CB . MET A 81 ? 0.2765 0.3238 0.3714 -0.0798 -0.1161 -0.0413 81 MET A CB 605 C CG . MET A 81 ? 0.3098 0.3465 0.4081 -0.0739 -0.1132 -0.0407 81 MET A CG 606 S SD . MET A 81 ? 0.4183 0.4681 0.5209 -0.0672 -0.1120 -0.0339 81 MET A SD 607 C CE . MET A 81 ? 0.3543 0.4028 0.4504 -0.0579 -0.1089 -0.0349 81 MET A CE 608 N N . TRP A 82 ? 0.2900 0.2925 0.3749 -0.0783 -0.1090 -0.0544 82 TRP A N 609 C CA . TRP A 82 ? 0.3202 0.3125 0.4035 -0.0715 -0.1058 -0.0566 82 TRP A CA 610 C C . TRP A 82 ? 0.3548 0.3320 0.4299 -0.0753 -0.1026 -0.0629 82 TRP A C 611 O O . TRP A 82 ? 0.3017 0.2734 0.3745 -0.0702 -0.1003 -0.0650 82 TRP A O 612 C CB . TRP A 82 ? 0.2844 0.2719 0.3745 -0.0664 -0.1031 -0.0524 82 TRP A CB 613 C CG . TRP A 82 ? 0.2818 0.2817 0.3767 -0.0642 -0.1055 -0.0472 82 TRP A CG 614 C CD1 . TRP A 82 ? 0.2858 0.2900 0.3861 -0.0665 -0.1062 -0.0430 82 TRP A CD1 615 C CD2 . TRP A 82 ? 0.2663 0.2735 0.3588 -0.0597 -0.1063 -0.0461 82 TRP A CD2 616 N NE1 . TRP A 82 ? 0.2650 0.2793 0.3662 -0.0638 -0.1073 -0.0396 82 TRP A NE1 617 C CE2 . TRP A 82 ? 0.3386 0.3531 0.4339 -0.0597 -0.1067 -0.0417 82 TRP A CE2 618 C CE3 . TRP A 82 ? 0.2649 0.2710 0.3514 -0.0560 -0.1057 -0.0486 82 TRP A CE3 619 C CZ2 . TRP A 82 ? 0.2997 0.3176 0.3900 -0.0565 -0.1054 -0.0404 82 TRP A CZ2 620 C CZ3 . TRP A 82 ? 0.2622 0.2715 0.3443 -0.0528 -0.1046 -0.0468 82 TRP A CZ3 621 C CH2 . TRP A 82 ? 0.2610 0.2749 0.3441 -0.0532 -0.1040 -0.0431 82 TRP A CH2 622 N N . ASN A 83 ? 0.3171 0.2867 0.3863 -0.0851 -0.1016 -0.0659 83 ASN A N 623 C CA . ASN A 83 ? 0.3359 0.2880 0.3929 -0.0911 -0.0973 -0.0730 83 ASN A CA 624 C C . ASN A 83 ? 0.3851 0.3477 0.4351 -0.0942 -0.1011 -0.0764 83 ASN A C 625 O O . ASN A 83 ? 0.3373 0.3216 0.3908 -0.0954 -0.1074 -0.0727 83 ASN A O 626 C CB . ASN A 83 ? 0.3570 0.2958 0.4053 -0.1039 -0.0947 -0.0761 83 ASN A CB 627 C CG . ASN A 83 ? 0.4513 0.3717 0.5038 -0.0996 -0.0874 -0.0732 83 ASN A CG 628 O OD1 . ASN A 83 ? 0.3642 0.2801 0.4246 -0.0876 -0.0831 -0.0695 83 ASN A OD1 629 N ND2 . ASN A 83 ? 0.3799 0.2916 0.4276 -0.1097 -0.0860 -0.0736 83 ASN A ND2 630 N N . PRO A 84 ? 0.3985 0.3464 0.4389 -0.0949 -0.0965 -0.0824 84 PRO A N 631 C CA . PRO A 84 ? 0.3720 0.3296 0.4052 -0.0980 -0.0999 -0.0853 84 PRO A CA 632 C C . PRO A 84 ? 0.3531 0.3270 0.3801 -0.1120 -0.1060 -0.0851 84 PRO A C 633 O O . PRO A 84 ? 0.3698 0.3353 0.3888 -0.1244 -0.1050 -0.0877 84 PRO A O 634 C CB . PRO A 84 ? 0.4794 0.4129 0.5001 -0.0999 -0.0920 -0.0929 84 PRO A CB 635 C CG . PRO A 84 ? 0.4703 0.3850 0.4967 -0.0911 -0.0840 -0.0911 84 PRO A CG 636 C CD . PRO A 84 ? 0.4416 0.3623 0.4765 -0.0928 -0.0867 -0.0860 84 PRO A CD 637 N N . ASN A 85 ? 0.3474 0.3450 0.3776 -0.1105 -0.1119 -0.0807 85 ASN A N 638 C CA . ASN A 85 ? 0.3619 0.3821 0.3882 -0.1233 -0.1182 -0.0773 85 ASN A CA 639 C C . ASN A 85 ? 0.3574 0.3826 0.3715 -0.1317 -0.1197 -0.0808 85 ASN A C 640 O O . ASN A 85 ? 0.3835 0.4357 0.3973 -0.1390 -0.1258 -0.0748 85 ASN A O 641 C CB . ASN A 85 ? 0.3274 0.3763 0.3681 -0.1151 -0.1231 -0.0661 85 ASN A CB 642 C CG . ASN A 85 ? 0.3483 0.4030 0.3956 -0.0996 -0.1222 -0.0624 85 ASN A CG 643 O OD1 . ASN A 85 ? 0.3119 0.3486 0.3564 -0.0930 -0.1183 -0.0679 85 ASN A OD1 644 N ND2 . ASN A 85 ? 0.3095 0.3891 0.3651 -0.0935 -0.1247 -0.0523 85 ASN A ND2 645 N N . THR A 86 ? 0.5780 0.5787 0.5820 -0.1310 -0.1138 -0.0895 86 THR A N 646 C CA . THR A 86 ? 0.3790 0.3820 0.3707 -0.1377 -0.1143 -0.0935 86 THR A CA 647 C C . THR A 86 ? 0.4526 0.4201 0.4277 -0.1433 -0.1050 -0.1051 86 THR A C 648 O O . THR A 86 ? 0.4034 0.3490 0.3830 -0.1338 -0.0981 -0.1070 86 THR A O 649 C CB . THR A 86 ? 0.6142 0.6285 0.6166 -0.1214 -0.1154 -0.0886 86 THR A CB 650 O OG1 . THR A 86 ? 0.5041 0.5485 0.5081 -0.1246 -0.1220 -0.0812 86 THR A OG1 651 C CG2 . THR A 86 ? 0.3659 0.3585 0.3606 -0.1171 -0.1093 -0.0961 86 THR A CG2 652 N N . ASP A 87 ? 0.4263 0.3878 0.3817 -0.1584 -0.1038 -0.1120 87 ASP A N 653 C CA . ASP A 87 ? 0.4923 0.4162 0.4287 -0.1631 -0.0924 -0.1235 87 ASP A CA 654 C C . ASP A 87 ? 0.4450 0.3513 0.3908 -0.1428 -0.0844 -0.1239 87 ASP A C 655 O O . ASP A 87 ? 0.4215 0.3445 0.3808 -0.1297 -0.0884 -0.1185 87 ASP A O 656 C CB . ASP A 87 ? 0.5408 0.4646 0.4578 -0.1752 -0.0909 -0.1288 87 ASP A CB 657 C CG . ASP A 87 ? 0.5892 0.5298 0.4970 -0.1911 -0.0945 -0.1253 87 ASP A CG 658 O OD1 . ASP A 87 ? 0.5968 0.5139 0.4872 -0.2024 -0.0867 -0.1310 87 ASP A OD1 659 O OD2 . ASP A 87 ? 0.7120 0.6893 0.6289 -0.1928 -0.1043 -0.1160 87 ASP A OD2 660 N N . LEU A 88 ? 0.4652 0.3381 0.4034 -0.1406 -0.0725 -0.1292 88 LEU A N 661 C CA . LEU A 88 ? 0.5688 0.4256 0.5145 -0.1226 -0.0633 -0.1282 88 LEU A CA 662 C C . LEU A 88 ? 0.6297 0.4706 0.5583 -0.1251 -0.0558 -0.1359 88 LEU A C 663 O O . LEU A 88 ? 0.5121 0.3356 0.4170 -0.1415 -0.0511 -0.1448 88 LEU A O 664 C CB . LEU A 88 ? 0.5761 0.4053 0.5220 -0.1179 -0.0522 -0.1280 88 LEU A CB 665 C CG . LEU A 88 ? 0.5339 0.3751 0.4957 -0.1155 -0.0579 -0.1206 88 LEU A CG 666 C CD1 . LEU A 88 ? 0.5070 0.3219 0.4713 -0.1072 -0.0457 -0.1183 88 LEU A CD1 667 C CD2 . LEU A 88 ? 0.4661 0.3391 0.4502 -0.1034 -0.0685 -0.1116 88 LEU A CD2 668 N N . SER A 89 ? 0.5862 0.4324 0.5248 -0.1101 -0.0542 -0.1326 89 SER A N 669 C CA . SER A 89 ? 0.5550 0.3873 0.4784 -0.1111 -0.0466 -0.1392 89 SER A CA 670 C C . SER A 89 ? 0.5668 0.4038 0.5055 -0.0918 -0.0433 -0.1331 89 SER A C 671 O O . SER A 89 ? 0.4368 0.2957 0.3957 -0.0820 -0.0513 -0.1245 89 SER A O 672 C CB . SER A 89 ? 0.4988 0.3517 0.4123 -0.1246 -0.0565 -0.1422 89 SER A CB 673 O OG . SER A 89 ? 0.5514 0.3949 0.4522 -0.1243 -0.0503 -0.1476 89 SER A OG 674 N N . GLU A 90 ? 0.5181 0.3350 0.4463 -0.0872 -0.0312 -0.1371 90 GLU A N 675 C CA . GLU A 90 ? 0.5391 0.3663 0.4820 -0.0706 -0.0295 -0.1301 90 GLU A CA 676 C C . GLU A 90 ? 0.4689 0.3229 0.4153 -0.0730 -0.0417 -0.1291 90 GLU A C 677 O O . GLU A 90 ? 0.4255 0.2955 0.3862 -0.0619 -0.0451 -0.1221 90 GLU A O 678 C CB . GLU A 90 ? 0.5466 0.3477 0.4784 -0.0636 -0.0124 -0.1330 90 GLU A CB 679 C CG . GLU A 90 ? 0.5421 0.3138 0.4709 -0.0575 0.0033 -0.1319 90 GLU A CG 680 C CD . GLU A 90 ? 0.5851 0.3331 0.5052 -0.0466 0.0219 -0.1322 90 GLU A CD 681 O OE1 . GLU A 90 ? 0.5478 0.3103 0.4861 -0.0303 0.0242 -0.1215 90 GLU A OE1 682 O OE2 . GLU A 90 ? 0.5966 0.3117 0.4906 -0.0552 0.0349 -0.1427 90 GLU A OE2 683 N N . ASP A 91 ? 0.4832 0.3422 0.4152 -0.0883 -0.0478 -0.1354 91 ASP A N 684 C CA . ASP A 91 ? 0.4645 0.3494 0.3991 -0.0910 -0.0588 -0.1332 91 ASP A CA 685 C C . ASP A 91 ? 0.4210 0.3299 0.3727 -0.0888 -0.0705 -0.1251 91 ASP A C 686 O O . ASP A 91 ? 0.4668 0.3877 0.4148 -0.0999 -0.0777 -0.1252 91 ASP A O 687 C CB . ASP A 91 ? 0.5247 0.4084 0.4371 -0.1092 -0.0601 -0.1413 91 ASP A CB 688 C CG . ASP A 91 ? 0.5460 0.4587 0.4614 -0.1118 -0.0710 -0.1372 91 ASP A CG 689 O OD1 . ASP A 91 ? 0.4670 0.3966 0.3998 -0.0991 -0.0763 -0.1291 91 ASP A OD1 690 O OD2 . ASP A 91 ? 0.5522 0.4703 0.4510 -0.1274 -0.0738 -0.1416 91 ASP A OD2 691 N N . CYS A 92 ? 0.4636 0.3125 0.2875 -0.0678 -0.0693 -0.1393 92 CYS A N 692 C CA . CYS A 92 ? 0.4664 0.3233 0.3129 -0.0711 -0.0742 -0.1255 92 CYS A CA 693 C C . CYS A 92 ? 0.5184 0.3788 0.3582 -0.0727 -0.0663 -0.1168 92 CYS A C 694 O O . CYS A 92 ? 0.4357 0.3035 0.2958 -0.0738 -0.0681 -0.1070 92 CYS A O 695 C CB . CYS A 92 ? 0.4236 0.2837 0.3016 -0.0697 -0.0733 -0.1257 92 CYS A CB 696 S SG . CYS A 92 ? 0.4358 0.2949 0.3200 -0.0634 -0.0582 -0.1335 92 CYS A SG 697 N N . LEU A 93 ? 0.4285 0.2857 0.2415 -0.0731 -0.0561 -0.1198 93 LEU A N 698 C CA . LEU A 93 ? 0.4457 0.3118 0.2607 -0.0734 -0.0455 -0.1090 93 LEU A CA 699 C C . LEU A 93 ? 0.4612 0.3250 0.2630 -0.0765 -0.0549 -0.0968 93 LEU A C 700 O O . LEU A 93 ? 0.5097 0.3668 0.2812 -0.0788 -0.0539 -0.0952 93 LEU A O 701 C CB . LEU A 93 ? 0.4286 0.2973 0.2285 -0.0725 -0.0279 -0.1151 93 LEU A CB 702 C CG . LEU A 93 ? 0.5340 0.4084 0.3528 -0.0673 -0.0180 -0.1264 93 LEU A CG 703 C CD1 . LEU A 93 ? 0.4288 0.3125 0.2392 -0.0665 0.0010 -0.1310 93 LEU A CD1 704 C CD2 . LEU A 93 ? 0.4629 0.3448 0.3171 -0.0652 -0.0206 -0.1204 93 LEU A CD2 705 N N . TYR A 94 ? 0.4452 0.3145 0.2694 -0.0759 -0.0645 -0.0881 94 TYR A N 706 C CA . TYR A 94 ? 0.4218 0.2902 0.2394 -0.0766 -0.0760 -0.0774 94 TYR A CA 707 C C . TYR A 94 ? 0.4360 0.3140 0.2796 -0.0737 -0.0749 -0.0675 94 TYR A C 708 O O . TYR A 94 ? 0.4166 0.3024 0.2843 -0.0721 -0.0690 -0.0694 94 TYR A O 709 C CB . TYR A 94 ? 0.4157 0.2824 0.2334 -0.0784 -0.0937 -0.0800 94 TYR A CB 710 C CG . TYR A 94 ? 0.5561 0.4110 0.3449 -0.0809 -0.0971 -0.0913 94 TYR A CG 711 C CD1 . TYR A 94 ? 0.4490 0.3042 0.2475 -0.0791 -0.0924 -0.1029 94 TYR A CD1 712 C CD2 . TYR A 94 ? 0.4797 0.3269 0.2364 -0.0821 -0.1031 -0.0887 94 TYR A CD2 713 C CE1 . TYR A 94 ? 0.4788 0.3272 0.2560 -0.0782 -0.0932 -0.1133 94 TYR A CE1 714 C CE2 . TYR A 94 ? 0.5094 0.3509 0.2438 -0.0817 -0.1033 -0.0982 94 TYR A CE2 715 C CZ . TYR A 94 ? 0.5085 0.3509 0.2536 -0.0796 -0.0982 -0.1112 94 TYR A CZ 716 O OH . TYR A 94 ? 0.5641 0.4005 0.2868 -0.0783 -0.0987 -0.1223 94 TYR A OH 717 N N . LEU A 95 ? 0.3818 0.2581 0.2189 -0.0724 -0.0806 -0.0572 95 LEU A N 718 C CA . LEU A 95 ? 0.4016 0.2854 0.2605 -0.0681 -0.0807 -0.0489 95 LEU A CA 719 C C . LEU A 95 ? 0.4423 0.3288 0.3044 -0.0646 -0.0960 -0.0414 95 LEU A C 720 O O . LEU A 95 ? 0.4029 0.2835 0.2465 -0.0663 -0.1069 -0.0410 95 LEU A O 721 C CB . LEU A 95 ? 0.4085 0.2863 0.2598 -0.0682 -0.0691 -0.0442 95 LEU A CB 722 C CG . LEU A 95 ? 0.4915 0.3549 0.3112 -0.0713 -0.0685 -0.0383 95 LEU A CG 723 C CD1 . LEU A 95 ? 0.4475 0.3043 0.2617 -0.0671 -0.0819 -0.0279 95 LEU A CD1 724 C CD2 . LEU A 95 ? 0.4716 0.3313 0.2875 -0.0748 -0.0535 -0.0366 95 LEU A CD2 725 N N . ASN A 96 ? 0.3449 0.2413 0.2304 -0.0592 -0.0970 -0.0360 96 ASN A N 726 C CA . ASN A 96 ? 0.3792 0.2833 0.2755 -0.0537 -0.1103 -0.0296 96 ASN A CA 727 C C . ASN A 96 ? 0.4163 0.3155 0.3133 -0.0467 -0.1085 -0.0222 96 ASN A C 728 O O . ASN A 96 ? 0.3426 0.2395 0.2447 -0.0460 -0.0971 -0.0228 96 ASN A O 729 C CB . ASN A 96 ? 0.3515 0.2760 0.2800 -0.0526 -0.1131 -0.0311 96 ASN A CB 730 C CG . ASN A 96 ? 0.4176 0.3441 0.3486 -0.0602 -0.1146 -0.0385 96 ASN A CG 731 O OD1 . ASN A 96 ? 0.4423 0.3622 0.3575 -0.0644 -0.1238 -0.0417 96 ASN A OD1 732 N ND2 . ASN A 96 ? 0.3523 0.2862 0.3018 -0.0618 -0.1064 -0.0415 96 ASN A ND2 733 N N . VAL A 97 ? 0.3823 0.2793 0.2752 -0.0409 -0.1210 -0.0156 97 VAL A N 734 C CA . VAL A 97 ? 0.4467 0.3357 0.3400 -0.0327 -0.1215 -0.0090 97 VAL A CA 735 C C . VAL A 97 ? 0.4571 0.3605 0.3711 -0.0223 -0.1343 -0.0053 97 VAL A C 736 O O . VAL A 97 ? 0.4165 0.3245 0.3278 -0.0217 -0.1482 -0.0031 97 VAL A O 737 C CB . VAL A 97 ? 0.4527 0.3162 0.3123 -0.0350 -0.1236 -0.0025 97 VAL A CB 738 C CG1 . VAL A 97 ? 0.4308 0.2816 0.2914 -0.0276 -0.1233 0.0037 97 VAL A CG1 739 C CG2 . VAL A 97 ? 0.4634 0.3169 0.3022 -0.0459 -0.1107 -0.0062 97 VAL A CG2 740 N N . TRP A 98 ? 0.3642 0.2765 0.2995 -0.0136 -0.1299 -0.0053 98 TRP A N 741 C CA . TRP A 98 ? 0.3478 0.2748 0.3036 -0.0014 -0.1403 -0.0023 98 TRP A CA 742 C C . TRP A 98 ? 0.4859 0.3936 0.4326 0.0089 -0.1421 0.0021 98 TRP A C 743 O O . TRP A 98 ? 0.4637 0.3586 0.4052 0.0084 -0.1314 0.0003 98 TRP A O 744 C CB . TRP A 98 ? 0.3195 0.2747 0.3083 0.0022 -0.1338 -0.0064 98 TRP A CB 745 C CG . TRP A 98 ? 0.4012 0.3770 0.4047 -0.0070 -0.1348 -0.0092 98 TRP A CG 746 C CD1 . TRP A 98 ? 0.3819 0.3794 0.4042 -0.0065 -0.1463 -0.0077 98 TRP A CD1 747 C CD2 . TRP A 98 ? 0.3500 0.3258 0.3522 -0.0182 -0.1249 -0.0139 98 TRP A CD2 748 N NE1 . TRP A 98 ? 0.4042 0.4130 0.4358 -0.0180 -0.1441 -0.0109 98 TRP A NE1 749 C CE2 . TRP A 98 ? 0.3944 0.3891 0.4133 -0.0245 -0.1312 -0.0148 98 TRP A CE2 750 C CE3 . TRP A 98 ? 0.2850 0.2468 0.2749 -0.0234 -0.1122 -0.0174 98 TRP A CE3 751 C CZ2 . TRP A 98 ? 0.2749 0.2711 0.2966 -0.0352 -0.1254 -0.0190 98 TRP A CZ2 752 C CZ3 . TRP A 98 ? 0.2915 0.2575 0.2854 -0.0327 -0.1063 -0.0219 98 TRP A CZ3 753 C CH2 . TRP A 98 ? 0.3249 0.3063 0.3337 -0.0382 -0.1131 -0.0225 98 TRP A CH2 754 N N . ILE A 99 ? 0.4152 0.3206 0.3613 0.0184 -0.1569 0.0076 99 ILE A N 755 C CA . ILE A 99 ? 0.4957 0.3775 0.4300 0.0286 -0.1622 0.0129 99 ILE A CA 756 C C . ILE A 99 ? 0.4884 0.3861 0.4470 0.0461 -0.1736 0.0138 99 ILE A C 757 O O . ILE A 99 ? 0.5171 0.4378 0.4912 0.0484 -0.1840 0.0146 99 ILE A O 758 C CB . ILE A 99 ? 0.6215 0.4745 0.5197 0.0219 -0.1704 0.0210 99 ILE A CB 759 C CG1 . ILE A 99 ? 0.6728 0.5046 0.5481 0.0091 -0.1561 0.0207 99 ILE A CG1 760 C CG2 . ILE A 99 ? 0.7044 0.5374 0.5936 0.0344 -0.1847 0.0293 99 ILE A CG2 761 C CD1 . ILE A 99 ? 0.7772 0.5986 0.6236 -0.0036 -0.1570 0.0238 99 ILE A CD1 762 N N . PRO A 100 ? 0.5107 0.3977 0.4745 0.0589 -0.1717 0.0128 100 PRO A N 763 C CA . PRO A 100 ? 0.5328 0.4337 0.5198 0.0785 -0.1818 0.0126 100 PRO A CA 764 C C . PRO A 100 ? 0.5449 0.4334 0.5201 0.0845 -0.2018 0.0215 100 PRO A C 765 O O . PRO A 100 ? 0.5470 0.4041 0.4890 0.0760 -0.2064 0.0287 100 PRO A O 766 C CB . PRO A 100 ? 0.5123 0.3909 0.4955 0.0889 -0.1760 0.0094 100 PRO A CB 767 C CG . PRO A 100 ? 0.5396 0.4068 0.5090 0.0735 -0.1597 0.0057 100 PRO A CG 768 C CD . PRO A 100 ? 0.4722 0.3341 0.4216 0.0557 -0.1601 0.0107 100 PRO A CD 769 N N . ALA A 101 ? 0.5380 0.4527 0.5401 0.0986 -0.2135 0.0215 101 ALA A N 770 C CA . ALA A 101 ? 0.5952 0.4985 0.5904 0.1096 -0.2348 0.0296 101 ALA A CA 771 C C . ALA A 101 ? 0.6495 0.5545 0.6659 0.1335 -0.2390 0.0269 101 ALA A C 772 O O . ALA A 101 ? 0.6430 0.5814 0.6930 0.1427 -0.2307 0.0186 101 ALA A O 773 C CB . ALA A 101 ? 0.5720 0.5064 0.5831 0.1066 -0.2477 0.0315 101 ALA A CB 774 N N . PRO A 102 ? 0.6688 0.5367 0.6645 0.1439 -0.2514 0.0338 102 PRO A N 775 C CA . PRO A 102 ? 0.7021 0.5285 0.6556 0.1333 -0.2606 0.0454 102 PRO A CA 776 C C . PRO A 102 ? 0.6984 0.4987 0.6240 0.1145 -0.2436 0.0450 102 PRO A C 777 O O . PRO A 102 ? 0.6166 0.4198 0.5532 0.1148 -0.2280 0.0363 102 PRO A O 778 C CB . PRO A 102 ? 0.7764 0.5772 0.7248 0.1483 -0.2674 0.0489 102 PRO A CB 779 C CG . PRO A 102 ? 0.7565 0.5916 0.7470 0.1685 -0.2652 0.0392 102 PRO A CG 780 C CD . PRO A 102 ? 0.7162 0.5807 0.7284 0.1652 -0.2515 0.0292 102 PRO A CD 781 N N . LYS A 103 ? 0.6749 0.4532 0.5657 0.0983 -0.2464 0.0538 103 LYS A N 782 C CA . LYS A 103 ? 0.6832 0.4383 0.5466 0.0795 -0.2311 0.0549 103 LYS A CA 783 C C . LYS A 103 ? 0.6824 0.4096 0.5428 0.0846 -0.2241 0.0534 103 LYS A C 784 O O . LYS A 103 ? 0.6515 0.3515 0.5046 0.0971 -0.2365 0.0595 103 LYS A O 785 C CB . LYS A 103 ? 0.7762 0.5041 0.5989 0.0677 -0.2399 0.0675 103 LYS A CB 786 C CG . LYS A 103 ? 0.7906 0.4994 0.5839 0.0466 -0.2240 0.0697 103 LYS A CG 787 C CD . LYS A 103 ? 0.9053 0.5799 0.6555 0.0392 -0.2343 0.0849 103 LYS A CD 788 C CE . LYS A 103 ? 0.9508 0.6097 0.6713 0.0178 -0.2177 0.0879 103 LYS A CE 789 N NZ . LYS A 103 ? 0.9133 0.5918 0.6214 0.0056 -0.2135 0.0845 103 LYS A NZ 790 N N . PRO A 104 ? 0.6394 0.3727 0.5062 0.0752 -0.2053 0.0448 104 PRO A N 791 C CA . PRO A 104 ? 0.6190 0.3274 0.4843 0.0788 -0.1989 0.0414 104 PRO A CA 792 C C . PRO A 104 ? 0.7516 0.4165 0.5807 0.0654 -0.2000 0.0528 104 PRO A C 793 O O . PRO A 104 ? 0.7493 0.4085 0.5549 0.0529 -0.2024 0.0620 104 PRO A O 794 C CB . PRO A 104 ? 0.5456 0.2783 0.4270 0.0700 -0.1797 0.0297 104 PRO A CB 795 C CG . PRO A 104 ? 0.5815 0.3337 0.4566 0.0539 -0.1741 0.0312 104 PRO A CG 796 C CD . PRO A 104 ? 0.5322 0.2922 0.4048 0.0598 -0.1906 0.0383 104 PRO A CD 797 N N . LYS A 105 ? 0.7433 0.3780 0.5670 0.0673 -0.1982 0.0522 105 LYS A N 798 C CA . LYS A 105 ? 0.7986 0.3915 0.5894 0.0529 -0.1991 0.0644 105 LYS A CA 799 C C . LYS A 105 ? 0.8684 0.4605 0.6531 0.0320 -0.1806 0.0610 105 LYS A C 800 O O . LYS A 105 ? 1.0020 0.5804 0.7615 0.0139 -0.1759 0.0709 105 LYS A O 801 C CB . LYS A 105 ? 0.7605 0.3162 0.5459 0.0653 -0.2113 0.0684 105 LYS A CB 802 C CG . LYS A 105 ? 0.7756 0.3372 0.5660 0.0822 -0.2272 0.0725 105 LYS A CG 803 C CD . LYS A 105 ? 0.8490 0.3767 0.6242 0.0841 -0.2352 0.0804 105 LYS A CD 804 C CE . LYS A 105 ? 0.9535 0.4857 0.7270 0.0959 -0.2510 0.0879 105 LYS A CE 805 N NZ . LYS A 105 ? 0.9323 0.5011 0.7397 0.1170 -0.2563 0.0772 105 LYS A NZ 806 N N . ASN A 106 ? 0.7301 0.3386 0.5375 0.0348 -0.1700 0.0473 106 ASN A N 807 C CA . ASN A 106 ? 0.7138 0.3231 0.5191 0.0166 -0.1541 0.0433 106 ASN A CA 808 C C . ASN A 106 ? 0.5832 0.2279 0.4168 0.0215 -0.1433 0.0276 106 ASN A C 809 O O . ASN A 106 ? 0.5842 0.2233 0.4257 0.0209 -0.1375 0.0195 106 ASN A O 810 C CB . ASN A 106 ? 0.7898 0.3577 0.5828 0.0117 -0.1566 0.0470 106 ASN A CB 811 C CG . ASN A 106 ? 0.9748 0.5353 0.7549 -0.0128 -0.1437 0.0512 106 ASN A CG 812 O OD1 . ASN A 106 ? 0.8813 0.4568 0.6511 -0.0263 -0.1358 0.0565 106 ASN A OD1 813 N ND2 . ASN A 106 ? 1.1824 0.7209 0.9643 -0.0184 -0.1416 0.0478 106 ASN A ND2 814 N N . ALA A 107 ? 0.5330 0.2129 0.3805 0.0258 -0.1416 0.0239 107 ALA A N 815 C CA . ALA A 107 ? 0.4941 0.2083 0.3682 0.0320 -0.1331 0.0111 107 ALA A CA 816 C C . ALA A 107 ? 0.5307 0.2569 0.4074 0.0164 -0.1178 0.0055 107 ALA A C 817 O O . ALA A 107 ? 0.5180 0.2442 0.3819 0.0009 -0.1120 0.0104 107 ALA A O 818 C CB . ALA A 107 ? 0.4747 0.2213 0.3631 0.0390 -0.1370 0.0106 107 ALA A CB 819 N N . THR A 108 ? 0.4791 0.2170 0.3725 0.0217 -0.1115 -0.0052 108 THR A N 820 C CA . THR A 108 ? 0.4339 0.1893 0.3347 0.0104 -0.0985 -0.0117 108 THR A CA 821 C C . THR A 108 ? 0.4461 0.2319 0.3549 0.0057 -0.0937 -0.0116 108 THR A C 822 O O . THR A 108 ? 0.4264 0.2292 0.3450 0.0151 -0.0992 -0.0111 108 THR A O 823 C CB . THR A 108 ? 0.4101 0.1740 0.3261 0.0203 -0.0951 -0.0230 108 THR A CB 824 O OG1 . THR A 108 ? 0.4977 0.2300 0.4039 0.0201 -0.0985 -0.0246 108 THR A OG1 825 C CG2 . THR A 108 ? 0.4075 0.1964 0.3345 0.0119 -0.0836 -0.0293 108 THR A CG2 826 N N . VAL A 109 ? 0.4337 0.2265 0.3398 -0.0087 -0.0841 -0.0125 109 VAL A N 827 C CA . VAL A 109 ? 0.4182 0.2343 0.3290 -0.0141 -0.0800 -0.0129 109 VAL A CA 828 C C . VAL A 109 ? 0.4480 0.2868 0.3761 -0.0161 -0.0707 -0.0211 109 VAL A C 829 O O . VAL A 109 ? 0.4264 0.2611 0.3554 -0.0219 -0.0642 -0.0248 109 VAL A O 830 C CB . VAL A 109 ? 0.4454 0.2516 0.3367 -0.0283 -0.0767 -0.0073 109 VAL A CB 831 C CG1 . VAL A 109 ? 0.4090 0.2364 0.3037 -0.0323 -0.0740 -0.0095 109 VAL A CG1 832 C CG2 . VAL A 109 ? 0.4921 0.2735 0.3623 -0.0274 -0.0863 0.0027 109 VAL A CG2 833 N N A LEU A 110 ? 0.3775 0.2398 0.3194 -0.0119 -0.0712 -0.0231 110 LEU A N 834 N N B LEU A 110 ? 0.3849 0.2472 0.3267 -0.0120 -0.0711 -0.0231 110 LEU A N 835 C CA A LEU A 110 ? 0.3750 0.2578 0.3316 -0.0143 -0.0635 -0.0289 110 LEU A CA 836 C CA B LEU A 110 ? 0.3732 0.2558 0.3297 -0.0143 -0.0634 -0.0289 110 LEU A CA 837 C C A LEU A 110 ? 0.3777 0.2696 0.3327 -0.0237 -0.0608 -0.0284 110 LEU A C 838 C C B LEU A 110 ? 0.3758 0.2676 0.3308 -0.0237 -0.0607 -0.0284 110 LEU A C 839 O O A LEU A 110 ? 0.3650 0.2627 0.3193 -0.0231 -0.0666 -0.0257 110 LEU A O 840 O O B LEU A 110 ? 0.3677 0.2653 0.3220 -0.0230 -0.0666 -0.0257 110 LEU A O 841 C CB A LEU A 110 ? 0.3446 0.2473 0.3190 -0.0031 -0.0651 -0.0312 110 LEU A CB 842 C CB B LEU A 110 ? 0.3587 0.2613 0.3331 -0.0032 -0.0649 -0.0313 110 LEU A CB 843 C CG A LEU A 110 ? 0.3854 0.2868 0.3648 0.0053 -0.0625 -0.0363 110 LEU A CG 844 C CG B LEU A 110 ? 0.3969 0.2972 0.3759 0.0064 -0.0633 -0.0361 110 LEU A CG 845 C CD1 A LEU A 110 ? 0.3899 0.3094 0.3837 0.0187 -0.0648 -0.0375 110 LEU A CD1 846 C CD1 B LEU A 110 ? 0.3768 0.2517 0.3439 0.0123 -0.0697 -0.0348 110 LEU A CD1 847 C CD2 A LEU A 110 ? 0.2599 0.1689 0.2435 -0.0008 -0.0543 -0.0410 110 LEU A CD2 848 C CD2 B LEU A 110 ? 0.3898 0.3148 0.3862 0.0168 -0.0627 -0.0380 110 LEU A CD2 849 N N . ILE A 111 ? 0.3791 0.2722 0.3340 -0.0318 -0.0527 -0.0319 111 ILE A N 850 C CA . ILE A 111 ? 0.3542 0.2542 0.3074 -0.0393 -0.0496 -0.0334 111 ILE A CA 851 C C . ILE A 111 ? 0.3269 0.2440 0.2969 -0.0392 -0.0458 -0.0378 111 ILE A C 852 O O . ILE A 111 ? 0.2775 0.1968 0.2535 -0.0402 -0.0402 -0.0411 111 ILE A O 853 C CB . ILE A 111 ? 0.3618 0.2507 0.3014 -0.0486 -0.0431 -0.0339 111 ILE A CB 854 C CG1 . ILE A 111 ? 0.3379 0.2076 0.2580 -0.0506 -0.0468 -0.0274 111 ILE A CG1 855 C CG2 . ILE A 111 ? 0.3560 0.2523 0.2935 -0.0541 -0.0395 -0.0375 111 ILE A CG2 856 C CD1 . ILE A 111 ? 0.3757 0.2367 0.2818 -0.0614 -0.0387 -0.0265 111 ILE A CD1 857 N N . TRP A 112 ? 0.2442 0.1723 0.2213 -0.0385 -0.0498 -0.0373 112 TRP A N 858 C CA . TRP A 112 ? 0.2712 0.2136 0.2638 -0.0391 -0.0476 -0.0394 112 TRP A CA 859 C C . TRP A 112 ? 0.3056 0.2459 0.2960 -0.0458 -0.0440 -0.0436 112 TRP A C 860 O O . TRP A 112 ? 0.2711 0.2051 0.2507 -0.0497 -0.0461 -0.0449 112 TRP A O 861 C CB . TRP A 112 ? 0.2388 0.1944 0.2424 -0.0368 -0.0540 -0.0362 112 TRP A CB 862 C CG . TRP A 112 ? 0.2403 0.2089 0.2589 -0.0393 -0.0522 -0.0362 112 TRP A CG 863 C CD1 . TRP A 112 ? 0.2724 0.2431 0.2951 -0.0454 -0.0554 -0.0367 112 TRP A CD1 864 C CD2 . TRP A 112 ? 0.2052 0.1839 0.2344 -0.0361 -0.0474 -0.0353 112 TRP A CD2 865 N NE1 . TRP A 112 ? 0.2525 0.2331 0.2887 -0.0467 -0.0530 -0.0349 112 TRP A NE1 866 C CE2 . TRP A 112 ? 0.2694 0.2559 0.3088 -0.0410 -0.0478 -0.0336 112 TRP A CE2 867 C CE3 . TRP A 112 ? 0.2904 0.2710 0.3196 -0.0296 -0.0435 -0.0359 112 TRP A CE3 868 C CZ2 . TRP A 112 ? 0.2070 0.2036 0.2555 -0.0400 -0.0439 -0.0310 112 TRP A CZ2 869 C CZ3 . TRP A 112 ? 0.2397 0.2314 0.2772 -0.0280 -0.0396 -0.0348 112 TRP A CZ3 870 C CH2 . TRP A 112 ? 0.1930 0.1930 0.2396 -0.0333 -0.0395 -0.0316 112 TRP A CH2 871 N N . ILE A 113 ? 0.2376 0.1831 0.2376 -0.0461 -0.0393 -0.0462 113 ILE A N 872 C CA . ILE A 113 ? 0.2798 0.2243 0.2815 -0.0500 -0.0367 -0.0507 113 ILE A CA 873 C C . ILE A 113 ? 0.2877 0.2407 0.3036 -0.0494 -0.0388 -0.0493 113 ILE A C 874 O O . ILE A 113 ? 0.2427 0.2017 0.2665 -0.0466 -0.0366 -0.0477 113 ILE A O 875 C CB . ILE A 113 ? 0.3318 0.2739 0.3330 -0.0510 -0.0296 -0.0549 113 ILE A CB 876 C CG1 . ILE A 113 ? 0.2164 0.1500 0.2042 -0.0535 -0.0266 -0.0545 113 ILE A CG1 877 C CG2 . ILE A 113 ? 0.2469 0.1890 0.2515 -0.0528 -0.0269 -0.0608 113 ILE A CG2 878 C CD1 . ILE A 113 ? 0.2715 0.2056 0.2617 -0.0565 -0.0193 -0.0581 113 ILE A CD1 879 N N . TYR A 114 ? 0.2561 0.2085 0.2740 -0.0526 -0.0437 -0.0494 114 TYR A N 880 C CA . TYR A 114 ? 0.1984 0.1570 0.2297 -0.0540 -0.0465 -0.0460 114 TYR A CA 881 C C . TYR A 114 ? 0.2300 0.1851 0.2665 -0.0535 -0.0436 -0.0487 114 TYR A C 882 O O . TYR A 114 ? 0.2468 0.1952 0.2783 -0.0526 -0.0400 -0.0552 114 TYR A O 883 C CB . TYR A 114 ? 0.2042 0.1609 0.2368 -0.0591 -0.0540 -0.0457 114 TYR A CB 884 C CG . TYR A 114 ? 0.2232 0.1661 0.2442 -0.0617 -0.0555 -0.0539 114 TYR A CG 885 C CD1 . TYR A 114 ? 0.2975 0.2320 0.3207 -0.0620 -0.0542 -0.0593 114 TYR A CD1 886 C CD2 . TYR A 114 ? 0.2598 0.1977 0.2666 -0.0629 -0.0585 -0.0564 114 TYR A CD2 887 C CE1 . TYR A 114 ? 0.2537 0.1762 0.2654 -0.0628 -0.0546 -0.0686 114 TYR A CE1 888 C CE2 . TYR A 114 ? 0.2847 0.2106 0.2776 -0.0648 -0.0589 -0.0646 114 TYR A CE2 889 C CZ . TYR A 114 ? 0.3251 0.2439 0.3208 -0.0645 -0.0564 -0.0714 114 TYR A CZ 890 O OH . TYR A 114 ? 0.3174 0.2250 0.2984 -0.0649 -0.0560 -0.0812 114 TYR A OH 891 N N . GLY A 115 ? 0.2339 0.1947 0.2807 -0.0539 -0.0451 -0.0431 115 GLY A N 892 C CA . GLY A 115 ? 0.2303 0.1863 0.2823 -0.0531 -0.0448 -0.0440 115 GLY A CA 893 C C . GLY A 115 ? 0.2755 0.2222 0.3319 -0.0577 -0.0508 -0.0438 115 GLY A C 894 O O . GLY A 115 ? 0.2549 0.1984 0.3091 -0.0621 -0.0551 -0.0450 115 GLY A O 895 N N . GLY A 116 ? 0.3282 0.2688 0.3903 -0.0568 -0.0525 -0.0423 116 GLY A N 896 C CA . GLY A 116 ? 0.3103 0.2370 0.3760 -0.0606 -0.0591 -0.0431 116 GLY A CA 897 C C . GLY A 116 ? 0.3445 0.2595 0.4118 -0.0548 -0.0595 -0.0496 116 GLY A C 898 O O . GLY A 116 ? 0.2870 0.1868 0.3538 -0.0547 -0.0637 -0.0564 116 GLY A O 899 N N . GLY A 117 ? 0.3334 0.2555 0.4031 -0.0490 -0.0556 -0.0486 117 GLY A N 900 C CA . GLY A 117 ? 0.3490 0.2637 0.4240 -0.0424 -0.0569 -0.0537 117 GLY A CA 901 C C . GLY A 117 ? 0.3133 0.2238 0.3865 -0.0379 -0.0535 -0.0673 117 GLY A C 902 O O . GLY A 117 ? 0.3432 0.2457 0.4225 -0.0316 -0.0555 -0.0733 117 GLY A O 903 N N . PHE A 118 ? 0.2639 0.1799 0.3282 -0.0404 -0.0481 -0.0721 118 PHE A N 904 C CA . PHE A 118 ? 0.3339 0.2467 0.3927 -0.0375 -0.0434 -0.0845 118 PHE A CA 905 C C . PHE A 118 ? 0.3882 0.2834 0.4442 -0.0370 -0.0490 -0.0913 118 PHE A C 906 O O . PHE A 118 ? 0.3744 0.2663 0.4258 -0.0322 -0.0448 -0.1026 118 PHE A O 907 C CB . PHE A 118 ? 0.2396 0.1613 0.3065 -0.0304 -0.0372 -0.0910 118 PHE A CB 908 C CG . PHE A 118 ? 0.2628 0.1998 0.3317 -0.0316 -0.0322 -0.0863 118 PHE A CG 909 C CD1 . PHE A 118 ? 0.2764 0.2197 0.3355 -0.0358 -0.0257 -0.0874 118 PHE A CD1 910 C CD2 . PHE A 118 ? 0.2064 0.1497 0.2858 -0.0286 -0.0352 -0.0809 118 PHE A CD2 911 C CE1 . PHE A 118 ? 0.2839 0.2378 0.3446 -0.0374 -0.0222 -0.0836 118 PHE A CE1 912 C CE2 . PHE A 118 ? 0.2551 0.2107 0.3354 -0.0299 -0.0318 -0.0781 118 PHE A CE2 913 C CZ . PHE A 118 ? 0.2333 0.1933 0.3049 -0.0344 -0.0254 -0.0797 118 PHE A CZ 914 N N . GLN A 119 ? 0.3547 0.2407 0.4115 -0.0414 -0.0568 -0.0831 119 GLN A N 915 C CA . GLN A 119 ? 0.3458 0.2156 0.3970 -0.0414 -0.0615 -0.0872 119 GLN A CA 916 C C . GLN A 119 ? 0.4055 0.2739 0.4477 -0.0505 -0.0651 -0.0828 119 GLN A C 917 O O . GLN A 119 ? 0.3540 0.2106 0.3883 -0.0516 -0.0682 -0.0885 119 GLN A O 918 C CB . GLN A 119 ? 0.3506 0.2071 0.4121 -0.0389 -0.0688 -0.0826 119 GLN A CB 919 C CG . GLN A 119 ? 0.4481 0.3067 0.5224 -0.0303 -0.0687 -0.0837 119 GLN A CG 920 C CD . GLN A 119 ? 0.4817 0.3462 0.5574 -0.0207 -0.0614 -0.0982 119 GLN A CD 921 O OE1 . GLN A 119 ? 0.4702 0.3250 0.5426 -0.0147 -0.0609 -0.1084 119 GLN A OE1 922 N NE2 . GLN A 119 ? 0.4634 0.3457 0.5441 -0.0196 -0.0548 -0.0989 119 GLN A NE2 923 N N . THR A 120 ? 0.3247 0.2058 0.3697 -0.0565 -0.0653 -0.0735 120 THR A N 924 C CA . THR A 120 ? 0.3222 0.2061 0.3641 -0.0646 -0.0698 -0.0687 120 THR A CA 925 C C . THR A 120 ? 0.2763 0.1757 0.3159 -0.0666 -0.0669 -0.0655 120 THR A C 926 O O . THR A 120 ? 0.2785 0.1844 0.3178 -0.0624 -0.0613 -0.0670 120 THR A O 927 C CB . THR A 120 ? 0.3526 0.2363 0.4067 -0.0710 -0.0759 -0.0569 120 THR A CB 928 O OG1 . THR A 120 ? 0.3177 0.2123 0.3813 -0.0708 -0.0737 -0.0482 120 THR A OG1 929 C CG2 . THR A 120 ? 0.2985 0.1631 0.3548 -0.0699 -0.0808 -0.0584 120 THR A CG2 930 N N . GLY A 121 ? 0.2880 0.1932 0.3275 -0.0727 -0.0717 -0.0612 121 GLY A N 931 C CA . GLY A 121 ? 0.2625 0.1817 0.3024 -0.0739 -0.0714 -0.0570 121 GLY A CA 932 C C . GLY A 121 ? 0.3023 0.2201 0.3284 -0.0751 -0.0742 -0.0624 121 GLY A C 933 O O . GLY A 121 ? 0.3252 0.2315 0.3382 -0.0739 -0.0738 -0.0714 121 GLY A O 934 N N . THR A 122 ? 0.2885 0.2177 0.3172 -0.0771 -0.0780 -0.0569 122 THR A N 935 C CA . THR A 122 ? 0.3348 0.2622 0.3491 -0.0777 -0.0827 -0.0604 122 THR A CA 936 C C . THR A 122 ? 0.3953 0.3372 0.4135 -0.0753 -0.0829 -0.0529 122 THR A C 937 O O . THR A 122 ? 0.2827 0.2388 0.3178 -0.0748 -0.0814 -0.0452 122 THR A O 938 C CB . THR A 122 ? 0.3678 0.2928 0.3815 -0.0826 -0.0910 -0.0619 122 THR A CB 939 O OG1 . THR A 122 ? 0.4252 0.3472 0.4219 -0.0826 -0.0963 -0.0657 122 THR A OG1 940 C CG2 . THR A 122 ? 0.3307 0.2704 0.3659 -0.0880 -0.0967 -0.0522 122 THR A CG2 941 N N . SER A 123 ? 0.2562 0.1951 0.2581 -0.0726 -0.0835 -0.0545 123 SER A N 942 C CA . SER A 123 ? 0.3057 0.2558 0.3105 -0.0678 -0.0830 -0.0475 123 SER A CA 943 C C . SER A 123 ? 0.2973 0.2602 0.3135 -0.0697 -0.0941 -0.0423 123 SER A C 944 O O . SER A 123 ? 0.3455 0.3196 0.3675 -0.0643 -0.0951 -0.0368 123 SER A O 945 C CB . SER A 123 ? 0.2841 0.2240 0.2671 -0.0643 -0.0794 -0.0493 123 SER A CB 946 O OG . SER A 123 ? 0.3509 0.2813 0.3159 -0.0676 -0.0872 -0.0530 123 SER A OG 947 N N . SER A 124 ? 0.3247 0.2864 0.3456 -0.0771 -0.1032 -0.0445 124 SER A N 948 C CA . SER A 124 ? 0.3701 0.3456 0.4031 -0.0803 -0.1154 -0.0403 124 SER A CA 949 C C . SER A 124 ? 0.3242 0.3210 0.3869 -0.0838 -0.1154 -0.0329 124 SER A C 950 O O . SER A 124 ? 0.3559 0.3684 0.4339 -0.0874 -0.1249 -0.0290 124 SER A O 951 C CB . SER A 124 ? 0.3824 0.3462 0.4032 -0.0868 -0.1261 -0.0466 124 SER A CB 952 O OG . SER A 124 ? 0.3848 0.3371 0.4037 -0.0898 -0.1200 -0.0518 124 SER A OG 953 N N . LEU A 125 ? 0.2755 0.2742 0.3464 -0.0832 -0.1050 -0.0304 125 LEU A N 954 C CA . LEU A 125 ? 0.2667 0.2862 0.3629 -0.0871 -0.1030 -0.0221 125 LEU A CA 955 C C . LEU A 125 ? 0.2817 0.3265 0.3921 -0.0802 -0.1021 -0.0161 125 LEU A C 956 O O . LEU A 125 ? 0.2423 0.2854 0.3422 -0.0699 -0.0988 -0.0177 125 LEU A O 957 C CB . LEU A 125 ? 0.2717 0.2870 0.3691 -0.0861 -0.0918 -0.0201 125 LEU A CB 958 C CG . LEU A 125 ? 0.3007 0.2928 0.3889 -0.0911 -0.0923 -0.0254 125 LEU A CG 959 C CD1 . LEU A 125 ? 0.2559 0.2475 0.3483 -0.0895 -0.0832 -0.0211 125 LEU A CD1 960 C CD2 . LEU A 125 ? 0.2590 0.2464 0.3519 -0.0999 -0.1002 -0.0256 125 LEU A CD2 961 N N . HIS A 126 ? 0.2528 0.3210 0.3878 -0.0860 -0.1050 -0.0094 126 HIS A N 962 C CA . HIS A 126 ? 0.2867 0.3842 0.4408 -0.0795 -0.1041 -0.0040 126 HIS A CA 963 C C . HIS A 126 ? 0.3134 0.4161 0.4636 -0.0672 -0.0907 -0.0031 126 HIS A C 964 O O . HIS A 126 ? 0.2741 0.3868 0.4261 -0.0558 -0.0903 -0.0036 126 HIS A O 965 C CB . HIS A 126 ? 0.3051 0.4282 0.4884 -0.0907 -0.1062 0.0039 126 HIS A CB 966 C CG . HIS A 126 ? 0.4444 0.6037 0.6523 -0.0845 -0.1037 0.0095 126 HIS A CG 967 N ND1 . HIS A 126 ? 0.5876 0.7569 0.7987 -0.0743 -0.1109 0.0071 126 HIS A ND1 968 C CD2 . HIS A 126 ? 0.4634 0.6524 0.6947 -0.0867 -0.0947 0.0173 126 HIS A CD2 969 C CE1 . HIS A 126 ? 0.5642 0.7686 0.8014 -0.0691 -0.1065 0.0122 126 HIS A CE1 970 N NE2 . HIS A 126 ? 0.4855 0.7038 0.7352 -0.0768 -0.0958 0.0184 126 HIS A NE2 971 N N . VAL A 127 ? 0.2211 0.3154 0.3653 -0.0690 -0.0810 -0.0023 127 VAL A N 972 C CA . VAL A 127 ? 0.2985 0.3965 0.4375 -0.0584 -0.0693 -0.0023 127 VAL A CA 973 C C . VAL A 127 ? 0.2585 0.3350 0.3751 -0.0489 -0.0682 -0.0095 127 VAL A C 974 O O . VAL A 127 ? 0.2573 0.3348 0.3687 -0.0398 -0.0605 -0.0107 127 VAL A O 975 C CB . VAL A 127 ? 0.2387 0.3352 0.3775 -0.0634 -0.0606 0.0016 127 VAL A CB 976 C CG1 . VAL A 127 ? 0.2676 0.3898 0.4291 -0.0718 -0.0589 0.0110 127 VAL A CG1 977 C CG2 . VAL A 127 ? 0.2200 0.2890 0.3450 -0.0705 -0.0638 -0.0020 127 VAL A CG2 978 N N . TYR A 128 ? 0.2257 0.2829 0.3284 -0.0517 -0.0759 -0.0140 128 TYR A N 979 C CA . TYR A 128 ? 0.2186 0.2560 0.3001 -0.0449 -0.0749 -0.0192 128 TYR A CA 980 C C . TYR A 128 ? 0.2385 0.2755 0.3160 -0.0397 -0.0839 -0.0192 128 TYR A C 981 O O . TYR A 128 ? 0.2273 0.2448 0.2847 -0.0373 -0.0855 -0.0222 128 TYR A O 982 C CB . TYR A 128 ? 0.2201 0.2340 0.2841 -0.0511 -0.0748 -0.0245 128 TYR A CB 983 C CG . TYR A 128 ? 0.2337 0.2437 0.3004 -0.0560 -0.0687 -0.0250 128 TYR A CG 984 C CD1 . TYR A 128 ? 0.1949 0.2151 0.2697 -0.0528 -0.0609 -0.0216 128 TYR A CD1 985 C CD2 . TYR A 128 ? 0.2256 0.2204 0.2852 -0.0629 -0.0714 -0.0293 128 TYR A CD2 986 C CE1 . TYR A 128 ? 0.1840 0.1989 0.2597 -0.0569 -0.0571 -0.0210 128 TYR A CE1 987 C CE2 . TYR A 128 ? 0.2267 0.2159 0.2892 -0.0659 -0.0673 -0.0297 128 TYR A CE2 988 C CZ . TYR A 128 ? 0.2339 0.2330 0.3045 -0.0632 -0.0607 -0.0248 128 TYR A CZ 989 O OH . TYR A 128 ? 0.2290 0.2214 0.3015 -0.0658 -0.0583 -0.0241 128 TYR A OH 990 N N . ASP A 129 ? 0.2371 0.2960 0.3338 -0.0385 -0.0902 -0.0152 129 ASP A N 991 C CA . ASP A 129 ? 0.3138 0.3744 0.4092 -0.0326 -0.1010 -0.0144 129 ASP A CA 992 C C . ASP A 129 ? 0.3162 0.3716 0.4046 -0.0187 -0.0981 -0.0149 129 ASP A C 993 O O . ASP A 129 ? 0.2330 0.3069 0.3374 -0.0098 -0.0932 -0.0137 129 ASP A O 994 C CB . ASP A 129 ? 0.2820 0.3722 0.4052 -0.0343 -0.1083 -0.0101 129 ASP A CB 995 C CG . ASP A 129 ? 0.3511 0.4428 0.4735 -0.0306 -0.1234 -0.0093 129 ASP A CG 996 O OD1 . ASP A 129 ? 0.3385 0.4113 0.4408 -0.0226 -0.1267 -0.0105 129 ASP A OD1 997 O OD2 . ASP A 129 ? 0.3311 0.4430 0.4736 -0.0362 -0.1327 -0.0068 129 ASP A OD2 998 N N . GLY A 130 ? 0.2353 0.2654 0.2995 -0.0167 -0.1013 -0.0166 130 GLY A N 999 C CA . GLY A 130 ? 0.2423 0.2608 0.2971 -0.0052 -0.0990 -0.0169 130 GLY A CA 1000 C C . GLY A 130 ? 0.3541 0.3811 0.4178 0.0071 -0.1086 -0.0141 130 GLY A C 1001 O O . GLY A 130 ? 0.3158 0.3302 0.3717 0.0177 -0.1082 -0.0145 130 GLY A O 1002 N N . LYS A 131 ? 0.2538 0.3019 0.3352 0.0061 -0.1180 -0.0114 131 LYS A N 1003 C CA . LYS A 131 ? 0.2969 0.3543 0.3882 0.0185 -0.1294 -0.0086 131 LYS A CA 1004 C C . LYS A 131 ? 0.3519 0.4262 0.4620 0.0340 -0.1230 -0.0101 131 LYS A C 1005 O O . LYS A 131 ? 0.3364 0.4058 0.4464 0.0481 -0.1302 -0.0095 131 LYS A O 1006 C CB . LYS A 131 ? 0.3339 0.4132 0.4429 0.0131 -0.1422 -0.0058 131 LYS A CB 1007 C CG . LYS A 131 ? 0.3363 0.4541 0.4807 0.0110 -0.1374 -0.0050 131 LYS A CG 1008 C CD . LYS A 131 ? 0.4063 0.5426 0.5669 0.0011 -0.1510 -0.0024 131 LYS A CD 1009 C CE . LYS A 131 ? 0.3229 0.4998 0.5215 -0.0023 -0.1461 0.0000 131 LYS A CE 1010 N NZ . LYS A 131 ? 0.3969 0.5909 0.6127 -0.0147 -0.1601 0.0024 131 LYS A NZ 1011 N N . PHE A 132 ? 0.2866 0.3795 0.4111 0.0322 -0.1099 -0.0122 132 PHE A N 1012 C CA . PHE A 132 ? 0.3018 0.4122 0.4418 0.0473 -0.1024 -0.0149 132 PHE A CA 1013 C C . PHE A 132 ? 0.3022 0.3832 0.4203 0.0568 -0.0980 -0.0195 132 PHE A C 1014 O O . PHE A 132 ? 0.3419 0.4230 0.4646 0.0734 -0.1002 -0.0221 132 PHE A O 1015 C CB . PHE A 132 ? 0.3273 0.4661 0.4858 0.0419 -0.0893 -0.0150 132 PHE A CB 1016 C CG . PHE A 132 ? 0.3399 0.5078 0.5224 0.0308 -0.0934 -0.0098 132 PHE A CG 1017 C CD1 . PHE A 132 ? 0.3114 0.5090 0.5208 0.0380 -0.1013 -0.0075 132 PHE A CD1 1018 C CD2 . PHE A 132 ? 0.3101 0.4755 0.4897 0.0132 -0.0901 -0.0074 132 PHE A CD2 1019 C CE1 . PHE A 132 ? 0.3168 0.5420 0.5503 0.0259 -0.1060 -0.0025 132 PHE A CE1 1020 C CE2 . PHE A 132 ? 0.3256 0.5147 0.5271 0.0016 -0.0950 -0.0026 132 PHE A CE2 1021 C CZ . PHE A 132 ? 0.2901 0.5097 0.5190 0.0070 -0.1030 0.0000 132 PHE A CZ 1022 N N . LEU A 133 ? 0.2774 0.3335 0.3733 0.0466 -0.0922 -0.0210 133 LEU A N 1023 C CA . LEU A 133 ? 0.3125 0.3388 0.3875 0.0521 -0.0892 -0.0249 133 LEU A CA 1024 C C . LEU A 133 ? 0.3850 0.3873 0.4469 0.0598 -0.1014 -0.0225 133 LEU A C 1025 O O . LEU A 133 ? 0.3411 0.3291 0.3982 0.0728 -0.1027 -0.0256 133 LEU A O 1026 C CB . LEU A 133 ? 0.2628 0.2695 0.3190 0.0377 -0.0827 -0.0258 133 LEU A CB 1027 C CG . LEU A 133 ? 0.3251 0.3466 0.3885 0.0331 -0.0707 -0.0287 133 LEU A CG 1028 C CD1 . LEU A 133 ? 0.2757 0.2834 0.3261 0.0181 -0.0668 -0.0285 133 LEU A CD1 1029 C CD2 . LEU A 133 ? 0.3547 0.3719 0.4151 0.0447 -0.0645 -0.0347 133 LEU A CD2 1030 N N . ALA A 134 ? 0.2914 0.2876 0.3460 0.0519 -0.1112 -0.0171 134 ALA A N 1031 C CA . ALA A 134 ? 0.4263 0.3990 0.4656 0.0577 -0.1242 -0.0127 134 ALA A CA 1032 C C . ALA A 134 ? 0.4568 0.4436 0.5151 0.0766 -0.1328 -0.0126 134 ALA A C 1033 O O . ALA A 134 ? 0.4024 0.3660 0.4502 0.0883 -0.1395 -0.0120 134 ALA A O 1034 C CB . ALA A 134 ? 0.4083 0.3761 0.4355 0.0454 -0.1330 -0.0073 134 ALA A CB 1035 N N . ARG A 135 ? 0.3927 0.4177 0.4801 0.0797 -0.1327 -0.0132 135 ARG A N 1036 C CA . ARG A 135 ? 0.3799 0.4260 0.4911 0.0983 -0.1401 -0.0138 135 ARG A CA 1037 C C . ARG A 135 ? 0.4088 0.4547 0.5258 0.1150 -0.1312 -0.0212 135 ARG A C 1038 O O . ARG A 135 ? 0.4113 0.4464 0.5292 0.1326 -0.1392 -0.0226 135 ARG A O 1039 C CB . ARG A 135 ? 0.3220 0.4135 0.4661 0.0952 -0.1403 -0.0125 135 ARG A CB 1040 C CG . ARG A 135 ? 0.3183 0.4415 0.4942 0.1151 -0.1446 -0.0142 135 ARG A CG 1041 C CD . ARG A 135 ? 0.3480 0.4568 0.5200 0.1274 -0.1641 -0.0103 135 ARG A CD 1042 N NE . ARG A 135 ? 0.4612 0.6054 0.6684 0.1465 -0.1696 -0.0119 135 ARG A NE 1043 C CZ . ARG A 135 ? 0.5206 0.6583 0.7323 0.1693 -0.1713 -0.0165 135 ARG A CZ 1044 N NH1 . ARG A 135 ? 0.5931 0.6878 0.7754 0.1744 -0.1689 -0.0195 135 ARG A NH1 1045 N NH2 . ARG A 135 ? 0.4937 0.6678 0.7405 0.1872 -0.1758 -0.0186 135 ARG A NH2 1046 N N . VAL A 136 ? 0.3521 0.4087 0.4717 0.1099 -0.1154 -0.0263 136 VAL A N 1047 C CA . VAL A 136 ? 0.3890 0.4523 0.5155 0.1254 -0.1058 -0.0347 136 VAL A CA 1048 C C . VAL A 136 ? 0.4553 0.4758 0.5545 0.1298 -0.1054 -0.0395 136 VAL A C 1049 O O . VAL A 136 ? 0.3488 0.3614 0.4495 0.1482 -0.1070 -0.0459 136 VAL A O 1050 C CB . VAL A 136 ? 0.3721 0.4667 0.5118 0.1182 -0.0894 -0.0375 136 VAL A CB 1051 C CG1 . VAL A 136 ? 0.3964 0.4954 0.5369 0.1337 -0.0786 -0.0472 136 VAL A CG1 1052 C CG2 . VAL A 136 ? 0.3361 0.4750 0.5070 0.1151 -0.0900 -0.0326 136 VAL A CG2 1053 N N . GLU A 137 ? 0.4351 0.4285 0.5105 0.1131 -0.1035 -0.0370 137 GLU A N 1054 C CA . GLU A 137 ? 0.4439 0.3986 0.4955 0.1140 -0.1028 -0.0411 137 GLU A CA 1055 C C . GLU A 137 ? 0.4431 0.3593 0.4724 0.1093 -0.1148 -0.0342 137 GLU A C 1056 O O . GLU A 137 ? 0.4729 0.3551 0.4830 0.1084 -0.1154 -0.0362 137 GLU A O 1057 C CB . GLU A 137 ? 0.3360 0.2885 0.3779 0.0995 -0.0904 -0.0443 137 GLU A CB 1058 C CG . GLU A 137 ? 0.3274 0.3083 0.3832 0.1058 -0.0783 -0.0517 137 GLU A CG 1059 C CD . GLU A 137 ? 0.3915 0.3646 0.4462 0.1251 -0.0773 -0.0616 137 GLU A CD 1060 O OE1 . GLU A 137 ? 0.4786 0.4150 0.5163 0.1295 -0.0843 -0.0642 137 GLU A OE1 1061 O OE2 . GLU A 137 ? 0.4373 0.4407 0.5078 0.1360 -0.0693 -0.0670 137 GLU A OE2 1062 N N . ARG A 138 ? 0.3884 0.3099 0.4194 0.1053 -0.1246 -0.0258 138 ARG A N 1063 C CA . ARG A 138 ? 0.3955 0.2825 0.4026 0.0998 -0.1359 -0.0175 138 ARG A CA 1064 C C . ARG A 138 ? 0.4806 0.3418 0.4633 0.0813 -0.1290 -0.0157 138 ARG A C 1065 O O . ARG A 138 ? 0.4465 0.2722 0.4075 0.0786 -0.1340 -0.0115 138 ARG A O 1066 C CB . ARG A 138 ? 0.4298 0.2902 0.4313 0.1174 -0.1474 -0.0170 138 ARG A CB 1067 C CG . ARG A 138 ? 0.7598 0.6446 0.7859 0.1373 -0.1570 -0.0176 138 ARG A CG 1068 C CD . ARG A 138 ? 0.9055 0.7570 0.9207 0.1524 -0.1730 -0.0134 138 ARG A CD 1069 N NE . ARG A 138 ? 0.9944 0.8420 1.0024 0.1490 -0.1882 -0.0018 138 ARG A NE 1070 C CZ . ARG A 138 ? 0.9921 0.8006 0.9699 0.1411 -0.1978 0.0083 138 ARG A CZ 1071 N NH1 . ARG A 138 ? 0.9717 0.7413 0.9258 0.1347 -0.1938 0.0088 138 ARG A NH1 1072 N NH2 . ARG A 138 ? 0.9551 0.7640 0.9259 0.1388 -0.2118 0.0183 138 ARG A NH2 1073 N N . VAL A 139 ? 0.3877 0.2671 0.3749 0.0685 -0.1176 -0.0186 139 VAL A N 1074 C CA . VAL A 139 ? 0.3807 0.2418 0.3483 0.0509 -0.1115 -0.0166 139 VAL A CA 1075 C C . VAL A 139 ? 0.3759 0.2449 0.3379 0.0395 -0.1147 -0.0106 139 VAL A C 1076 O O . VAL A 139 ? 0.3762 0.2674 0.3522 0.0438 -0.1206 -0.0092 139 VAL A O 1077 C CB . VAL A 139 ? 0.3571 0.2302 0.3316 0.0447 -0.0980 -0.0240 139 VAL A CB 1078 C CG1 . VAL A 139 ? 0.3827 0.2440 0.3577 0.0551 -0.0957 -0.0311 139 VAL A CG1 1079 C CG2 . VAL A 139 ? 0.3157 0.2257 0.3117 0.0448 -0.0930 -0.0263 139 VAL A CG2 1080 N N . ILE A 140 ? 0.4207 0.2720 0.3621 0.0250 -0.1111 -0.0075 140 ILE A N 1081 C CA . ILE A 140 ? 0.3636 0.2222 0.2973 0.0136 -0.1119 -0.0043 140 ILE A CA 1082 C C . ILE A 140 ? 0.4101 0.2868 0.3538 0.0041 -0.0997 -0.0106 140 ILE A C 1083 O O . ILE A 140 ? 0.4451 0.3164 0.3884 0.0005 -0.0903 -0.0145 140 ILE A O 1084 C CB . ILE A 140 ? 0.4626 0.2926 0.3664 0.0042 -0.1143 0.0028 140 ILE A CB 1085 C CG1 . ILE A 140 ? 0.4567 0.2690 0.3503 0.0140 -0.1292 0.0107 140 ILE A CG1 1086 C CG2 . ILE A 140 ? 0.4913 0.3281 0.3841 -0.0087 -0.1113 0.0031 140 ILE A CG2 1087 C CD1 . ILE A 140 ? 0.5474 0.3302 0.4086 0.0049 -0.1328 0.0202 140 ILE A CD1 1088 N N . VAL A 141 ? 0.3698 0.2672 0.3233 0.0005 -0.1011 -0.0116 141 VAL A N 1089 C CA . VAL A 141 ? 0.3666 0.2787 0.3293 -0.0079 -0.0914 -0.0168 141 VAL A CA 1090 C C . VAL A 141 ? 0.3945 0.3006 0.3414 -0.0196 -0.0912 -0.0166 141 VAL A C 1091 O O . VAL A 141 ? 0.3791 0.2851 0.3187 -0.0206 -0.1008 -0.0137 141 VAL A O 1092 C CB . VAL A 141 ? 0.3770 0.3180 0.3662 -0.0032 -0.0919 -0.0187 141 VAL A CB 1093 C CG1 . VAL A 141 ? 0.2884 0.2410 0.2859 -0.0120 -0.0829 -0.0227 141 VAL A CG1 1094 C CG2 . VAL A 141 ? 0.2913 0.2394 0.2939 0.0099 -0.0907 -0.0200 141 VAL A CG2 1095 N N . VAL A 142 ? 0.3534 0.2545 0.2943 -0.0278 -0.0809 -0.0203 142 VAL A N 1096 C CA . VAL A 142 ? 0.3756 0.2725 0.3023 -0.0376 -0.0785 -0.0224 142 VAL A CA 1097 C C . VAL A 142 ? 0.4266 0.3375 0.3685 -0.0415 -0.0713 -0.0287 142 VAL A C 1098 O O . VAL A 142 ? 0.3256 0.2421 0.2803 -0.0395 -0.0645 -0.0309 142 VAL A O 1099 C CB . VAL A 142 ? 0.4336 0.3114 0.3383 -0.0440 -0.0718 -0.0208 142 VAL A CB 1100 C CG1 . VAL A 142 ? 0.3285 0.2046 0.2181 -0.0529 -0.0673 -0.0245 142 VAL A CG1 1101 C CG2 . VAL A 142 ? 0.3944 0.2543 0.2823 -0.0408 -0.0796 -0.0127 142 VAL A CG2 1102 N N . SER A 143 ? 0.4094 0.3244 0.3491 -0.0465 -0.0740 -0.0318 143 SER A N 1103 C CA . SER A 143 ? 0.2950 0.2174 0.2453 -0.0507 -0.0679 -0.0378 143 SER A CA 1104 C C . SER A 143 ? 0.3657 0.2798 0.2991 -0.0571 -0.0674 -0.0430 143 SER A C 1105 O O . SER A 143 ? 0.3717 0.2788 0.2882 -0.0585 -0.0747 -0.0416 143 SER A O 1106 C CB . SER A 143 ? 0.2945 0.2338 0.2677 -0.0489 -0.0724 -0.0370 143 SER A CB 1107 O OG . SER A 143 ? 0.3037 0.2472 0.2774 -0.0508 -0.0834 -0.0359 143 SER A OG 1108 N N . MET A 144 ? 0.3343 0.2487 0.2709 -0.0599 -0.0592 -0.0493 144 MET A N 1109 C CA . MET A 144 ? 0.3645 0.2712 0.2849 -0.0643 -0.0568 -0.0564 144 MET A CA 1110 C C . MET A 144 ? 0.4233 0.3335 0.3566 -0.0653 -0.0561 -0.0637 144 MET A C 1111 O O . MET A 144 ? 0.3594 0.2771 0.3125 -0.0633 -0.0533 -0.0628 144 MET A O 1112 C CB . MET A 144 ? 0.3110 0.2116 0.2174 -0.0663 -0.0452 -0.0579 144 MET A CB 1113 C CG . MET A 144 ? 0.3305 0.2371 0.2509 -0.0660 -0.0346 -0.0636 144 MET A CG 1114 S SD . MET A 144 ? 0.3090 0.2250 0.2545 -0.0621 -0.0330 -0.0594 144 MET A SD 1115 C CE . MET A 144 ? 0.2688 0.1780 0.2036 -0.0635 -0.0292 -0.0529 144 MET A CE 1116 N N . ASN A 145 ? 0.3335 0.2365 0.2543 -0.0680 -0.0596 -0.0708 145 ASN A N 1117 C CA . ASN A 145 ? 0.3472 0.2483 0.2767 -0.0683 -0.0580 -0.0793 145 ASN A CA 1118 C C . ASN A 145 ? 0.4176 0.3164 0.3401 -0.0665 -0.0452 -0.0866 145 ASN A C 1119 O O . ASN A 145 ? 0.3810 0.2759 0.2826 -0.0677 -0.0396 -0.0886 145 ASN A O 1120 C CB . ASN A 145 ? 0.3716 0.2644 0.2926 -0.0716 -0.0689 -0.0854 145 ASN A CB 1121 C CG . ASN A 145 ? 0.3978 0.2971 0.3332 -0.0744 -0.0816 -0.0785 145 ASN A CG 1122 O OD1 . ASN A 145 ? 0.3163 0.2274 0.2703 -0.0728 -0.0808 -0.0700 145 ASN A OD1 1123 N ND2 . ASN A 145 ? 0.3733 0.2687 0.3020 -0.0776 -0.0918 -0.0817 145 ASN A ND2 1124 N N . TYR A 146 ? 0.3407 0.2433 0.2813 -0.0637 -0.0405 -0.0898 146 TYR A N 1125 C CA . TYR A 146 ? 0.3181 0.2219 0.2579 -0.0608 -0.0292 -0.0980 146 TYR A CA 1126 C C . TYR A 146 ? 0.3705 0.2684 0.3194 -0.0575 -0.0317 -0.1073 146 TYR A C 1127 O O . TYR A 146 ? 0.3086 0.2038 0.2711 -0.0581 -0.0404 -0.1040 146 TYR A O 1128 C CB . TYR A 146 ? 0.2769 0.1914 0.2312 -0.0593 -0.0213 -0.0929 146 TYR A CB 1129 C CG . TYR A 146 ? 0.2724 0.1919 0.2491 -0.0569 -0.0259 -0.0879 146 TYR A CG 1130 C CD1 . TYR A 146 ? 0.2798 0.2028 0.2618 -0.0581 -0.0316 -0.0783 146 TYR A CD1 1131 C CD2 . TYR A 146 ? 0.2918 0.2129 0.2835 -0.0529 -0.0243 -0.0926 146 TYR A CD2 1132 C CE1 . TYR A 146 ? 0.2771 0.2059 0.2765 -0.0561 -0.0343 -0.0734 146 TYR A CE1 1133 C CE2 . TYR A 146 ? 0.2487 0.1735 0.2572 -0.0512 -0.0286 -0.0867 146 TYR A CE2 1134 C CZ . TYR A 146 ? 0.3021 0.2311 0.3134 -0.0533 -0.0330 -0.0771 146 TYR A CZ 1135 O OH . TYR A 146 ? 0.2945 0.2282 0.3198 -0.0519 -0.0359 -0.0712 146 TYR A OH 1136 N N . ARG A 147 ? 0.3733 0.2690 0.3148 -0.0539 -0.0240 -0.1187 147 ARG A N 1137 C CA . ARG A 147 ? 0.3372 0.2244 0.2866 -0.0488 -0.0266 -0.1292 147 ARG A CA 1138 C C . ARG A 147 ? 0.3860 0.2777 0.3617 -0.0449 -0.0278 -0.1252 147 ARG A C 1139 O O . ARG A 147 ? 0.2893 0.1939 0.2762 -0.0435 -0.0211 -0.1201 147 ARG A O 1140 C CB . ARG A 147 ? 0.3457 0.2334 0.2837 -0.0436 -0.0158 -0.1430 147 ARG A CB 1141 C CG . ARG A 147 ? 0.4903 0.3688 0.3981 -0.0462 -0.0164 -0.1501 147 ARG A CG 1142 C CD . ARG A 147 ? 0.4978 0.3815 0.3935 -0.0408 -0.0020 -0.1631 147 ARG A CD 1143 N NE . ARG A 147 ? 0.4350 0.3350 0.3262 -0.0445 0.0112 -0.1562 147 ARG A NE 1144 C CZ . ARG A 147 ? 0.4523 0.3635 0.3361 -0.0420 0.0268 -0.1639 147 ARG A CZ 1145 N NH1 . ARG A 147 ? 0.4222 0.3310 0.3020 -0.0337 0.0316 -0.1804 147 ARG A NH1 1146 N NH2 . ARG A 147 ? 0.3961 0.3209 0.2767 -0.0479 0.0376 -0.1553 147 ARG A NH2 1147 N N . VAL A 148 ? 0.3304 0.2107 0.3132 -0.0432 -0.0366 -0.1246 148 VAL A N 1148 C CA . VAL A 148 ? 0.3343 0.2163 0.3382 -0.0399 -0.0391 -0.1186 148 VAL A CA 1149 C C . VAL A 148 ? 0.3792 0.2488 0.3867 -0.0326 -0.0410 -0.1267 148 VAL A C 1150 O O . VAL A 148 ? 0.3414 0.2006 0.3342 -0.0309 -0.0408 -0.1363 148 VAL A O 1151 C CB . VAL A 148 ? 0.3635 0.2456 0.3741 -0.0467 -0.0478 -0.1046 148 VAL A CB 1152 C CG1 . VAL A 148 ? 0.3104 0.2054 0.3205 -0.0510 -0.0458 -0.0976 148 VAL A CG1 1153 C CG2 . VAL A 148 ? 0.3284 0.1993 0.3295 -0.0521 -0.0556 -0.1042 148 VAL A CG2 1154 N N . GLY A 149 ? 0.3112 0.1806 0.3368 -0.0278 -0.0435 -0.1233 149 GLY A N 1155 C CA . GLY A 149 ? 0.3306 0.1870 0.3613 -0.0196 -0.0464 -0.1305 149 GLY A CA 1156 C C . GLY A 149 ? 0.4034 0.2659 0.4336 -0.0097 -0.0368 -0.1458 149 GLY A C 1157 O O . GLY A 149 ? 0.3442 0.2242 0.3761 -0.0096 -0.0270 -0.1493 149 GLY A O 1158 N N . ALA A 150 ? 0.3649 0.2141 0.3937 -0.0016 -0.0386 -0.1551 150 ALA A N 1159 C CA . ALA A 150 ? 0.4287 0.2853 0.4575 0.0091 -0.0285 -0.1706 150 ALA A CA 1160 C C . ALA A 150 ? 0.4800 0.3447 0.4877 0.0048 -0.0186 -0.1775 150 ALA A C 1161 O O . ALA A 150 ? 0.4901 0.3726 0.5004 0.0096 -0.0058 -0.1864 150 ALA A O 1162 C CB . ALA A 150 ? 0.4331 0.2710 0.4608 0.0187 -0.0332 -0.1793 150 ALA A CB 1163 N N . LEU A 151 ? 0.4630 0.3156 0.4500 -0.0046 -0.0244 -0.1731 151 LEU A N 1164 C CA . LEU A 151 ? 0.4683 0.3252 0.4314 -0.0087 -0.0172 -0.1790 151 LEU A CA 1165 C C . LEU A 151 ? 0.4638 0.3425 0.4309 -0.0139 -0.0076 -0.1747 151 LEU A C 1166 O O . LEU A 151 ? 0.4499 0.3379 0.4011 -0.0155 0.0032 -0.1810 151 LEU A O 1167 C CB . LEU A 151 ? 0.4583 0.2985 0.4007 -0.0183 -0.0278 -0.1741 151 LEU A CB 1168 C CG . LEU A 151 ? 0.4475 0.2654 0.3803 -0.0163 -0.0352 -0.1809 151 LEU A CG 1169 C CD1 . LEU A 151 ? 0.5050 0.3127 0.4268 -0.0285 -0.0459 -0.1741 151 LEU A CD1 1170 C CD2 . LEU A 151 ? 0.4786 0.2928 0.3925 -0.0077 -0.0265 -0.1975 151 LEU A CD2 1171 N N . GLY A 152 ? 0.4077 0.2940 0.3945 -0.0172 -0.0111 -0.1636 152 GLY A N 1172 C CA . GLY A 152 ? 0.3902 0.2949 0.3804 -0.0230 -0.0031 -0.1563 152 GLY A CA 1173 C C . GLY A 152 ? 0.4203 0.3435 0.4335 -0.0174 0.0049 -0.1560 152 GLY A C 1174 O O . GLY A 152 ? 0.3250 0.2650 0.3402 -0.0217 0.0136 -0.1507 152 GLY A O 1175 N N . PHE A 153 ? 0.3166 0.2362 0.3481 -0.0081 0.0006 -0.1614 153 PHE A N 1176 C CA . PHE A 153 ? 0.3318 0.2696 0.3876 -0.0027 0.0049 -0.1598 153 PHE A CA 1177 C C . PHE A 153 ? 0.3741 0.3165 0.4460 0.0110 0.0085 -0.1734 153 PHE A C 1178 O O . PHE A 153 ? 0.3233 0.2822 0.4182 0.0164 0.0103 -0.1724 153 PHE A O 1179 C CB . PHE A 153 ? 0.2814 0.2167 0.3493 -0.0058 -0.0057 -0.1458 153 PHE A CB 1180 C CG . PHE A 153 ? 0.3531 0.2924 0.4107 -0.0170 -0.0056 -0.1335 153 PHE A CG 1181 C CD1 . PHE A 153 ? 0.3323 0.2896 0.3954 -0.0207 0.0018 -0.1290 153 PHE A CD1 1182 C CD2 . PHE A 153 ? 0.3050 0.2300 0.3489 -0.0236 -0.0136 -0.1268 153 PHE A CD2 1183 C CE1 . PHE A 153 ? 0.3319 0.2900 0.3853 -0.0296 0.0010 -0.1184 153 PHE A CE1 1184 C CE2 . PHE A 153 ? 0.2872 0.2165 0.3232 -0.0317 -0.0139 -0.1163 153 PHE A CE2 1185 C CZ . PHE A 153 ? 0.3334 0.2777 0.3732 -0.0342 -0.0066 -0.1124 153 PHE A CZ 1186 N N . LEU A 154 ? 0.3532 0.3688 0.4771 -0.0383 -0.0049 -0.1649 154 LEU A N 1187 C CA . LEU A 154 ? 0.3660 0.4014 0.5031 -0.0229 0.0040 -0.1783 154 LEU A CA 1188 C C . LEU A 154 ? 0.3858 0.4667 0.5339 -0.0303 0.0145 -0.1861 154 LEU A C 1189 O O . LEU A 154 ? 0.3652 0.4469 0.4940 -0.0513 0.0219 -0.1874 154 LEU A O 1190 C CB . LEU A 154 ? 0.3941 0.4068 0.5133 -0.0221 0.0104 -0.1908 154 LEU A CB 1191 C CG . LEU A 154 ? 0.4587 0.4829 0.5898 -0.0011 0.0207 -0.2058 154 LEU A CG 1192 C CD1 . LEU A 154 ? 0.5012 0.5018 0.6415 0.0217 0.0134 -0.2006 154 LEU A CD1 1193 C CD2 . LEU A 154 ? 0.4693 0.4727 0.5757 -0.0058 0.0305 -0.2207 154 LEU A CD2 1194 N N . ALA A 155 ? 0.3549 0.4732 0.5323 -0.0132 0.0154 -0.1920 155 ALA A N 1195 C CA . ALA A 155 ? 0.5155 0.6885 0.7123 -0.0228 0.0250 -0.2021 155 ALA A CA 1196 C C . ALA A 155 ? 0.5866 0.8028 0.8113 -0.0032 0.0350 -0.2211 155 ALA A C 1197 O O . ALA A 155 ? 0.3663 0.5852 0.6079 0.0277 0.0270 -0.2222 155 ALA A O 1198 C CB . ALA A 155 ? 0.3266 0.5225 0.5387 -0.0260 0.0139 -0.1929 155 ALA A CB 1199 N N . LEU A 156 ? 0.3695 0.6151 0.5946 -0.0208 0.0541 -0.2360 156 LEU A N 1200 C CA . LEU A 156 ? 0.5407 0.8495 0.8024 -0.0089 0.0673 -0.2573 156 LEU A CA 1201 C C . LEU A 156 ? 0.5720 0.9275 0.8433 -0.0425 0.0808 -0.2652 156 LEU A C 1202 O O . LEU A 156 ? 0.5900 0.9367 0.8362 -0.0693 0.1012 -0.2721 156 LEU A O 1203 C CB . LEU A 156 ? 0.5586 0.8535 0.8068 -0.0024 0.0851 -0.2722 156 LEU A CB 1204 C CG . LEU A 156 ? 0.5783 0.8365 0.8228 0.0328 0.0777 -0.2726 156 LEU A CG 1205 C CD1 . LEU A 156 ? 0.6199 0.8718 0.8516 0.0363 0.0990 -0.2918 156 LEU A CD1 1206 C CD2 . LEU A 156 ? 0.5388 0.8326 0.8230 0.0695 0.0650 -0.2741 156 LEU A CD2 1207 N N . PRO A 157 ? 0.5863 0.9868 0.8882 -0.0432 0.0698 -0.2644 157 PRO A N 1208 C CA . PRO A 157 ? 0.5932 1.0283 0.8989 -0.0806 0.0803 -0.2701 157 PRO A CA 1209 C C . PRO A 157 ? 0.5249 1.0016 0.8388 -0.1045 0.1107 -0.2928 157 PRO A C 1210 O O . PRO A 157 ? 0.5461 1.0837 0.9025 -0.0859 0.1188 -0.3131 157 PRO A O 1211 C CB . PRO A 157 ? 0.6171 1.1129 0.9681 -0.0656 0.0623 -0.2741 157 PRO A CB 1212 C CG . PRO A 157 ? 0.5952 1.0530 0.9418 -0.0263 0.0381 -0.2578 157 PRO A CG 1213 C CD . PRO A 157 ? 0.5731 0.9916 0.9036 -0.0076 0.0468 -0.2593 157 PRO A CD 1214 N N . GLY A 158 ? 0.4938 0.9344 0.7640 -0.1438 0.1284 -0.2894 158 GLY A N 1215 C CA . GLY A 158 ? 0.5474 1.0167 0.8138 -0.1738 0.1615 -0.3094 158 GLY A CA 1216 C C . GLY A 158 ? 0.6477 1.0699 0.8721 -0.1731 0.1784 -0.3110 158 GLY A C 1217 O O . GLY A 158 ? 0.7344 1.1560 0.9337 -0.2037 0.2079 -0.3225 158 GLY A O 1218 N N . ASN A 159 ? 0.5745 0.9542 0.7872 -0.1405 0.1607 -0.3001 159 ASN A N 1219 C CA . ASN A 159 ? 0.5379 0.8730 0.7114 -0.1359 0.1722 -0.3032 159 ASN A CA 1220 C C . ASN A 159 ? 0.5786 0.8292 0.6850 -0.1500 0.1623 -0.2814 159 ASN A C 1221 O O . ASN A 159 ? 0.5202 0.7350 0.6213 -0.1330 0.1362 -0.2640 159 ASN A O 1222 C CB . ASN A 159 ? 0.5156 0.8546 0.7161 -0.0926 0.1593 -0.3076 159 ASN A CB 1223 C CG . ASN A 159 ? 0.5660 0.8633 0.7289 -0.0872 0.1718 -0.3152 159 ASN A CG 1224 O OD1 . ASN A 159 ? 0.5724 0.8217 0.6795 -0.1118 0.1807 -0.3100 159 ASN A OD1 1225 N ND2 . ASN A 159 ? 0.6221 0.9329 0.8105 -0.0532 0.1718 -0.3276 159 ASN A ND2 1226 N N . PRO A 160 ? 0.6211 0.8393 0.6743 -0.1797 0.1835 -0.2831 160 PRO A N 1227 C CA . PRO A 160 ? 0.6079 0.7484 0.5950 -0.1903 0.1717 -0.2622 160 PRO A CA 1228 C C . PRO A 160 ? 0.6320 0.7278 0.5954 -0.1668 0.1537 -0.2564 160 PRO A C 1229 O O . PRO A 160 ? 0.6372 0.6768 0.5531 -0.1703 0.1387 -0.2402 160 PRO A O 1230 C CB . PRO A 160 ? 0.6209 0.7385 0.5530 -0.2260 0.2020 -0.2677 160 PRO A CB 1231 C CG . PRO A 160 ? 0.6467 0.8245 0.6128 -0.2298 0.2315 -0.2948 160 PRO A CG 1232 C CD . PRO A 160 ? 0.6096 0.8617 0.6597 -0.2048 0.2198 -0.3044 160 PRO A CD 1233 N N . GLU A 161 ? 0.6531 0.7734 0.6488 -0.1429 0.1546 -0.2705 161 GLU A N 1234 C CA . GLU A 161 ? 0.6610 0.7404 0.6393 -0.1226 0.1372 -0.2674 161 GLU A CA 1235 C C . GLU A 161 ? 0.6191 0.6907 0.6254 -0.1040 0.1080 -0.2518 161 GLU A C 1236 O O . GLU A 161 ? 0.5850 0.6172 0.5728 -0.0952 0.0904 -0.2452 161 GLU A O 1237 C CB . GLU A 161 ? 0.7006 0.7989 0.6964 -0.1040 0.1515 -0.2891 161 GLU A CB 1238 C CG . GLU A 161 ? 0.8336 0.9455 0.8060 -0.1215 0.1849 -0.3080 161 GLU A CG 1239 C CD . GLU A 161 ? 1.0082 1.0599 0.9025 -0.1437 0.1885 -0.3020 161 GLU A CD 1240 O OE1 . GLU A 161 ? 1.0833 1.0889 0.9459 -0.1342 0.1699 -0.2972 161 GLU A OE1 1241 O OE2 . GLU A 161 ? 1.0878 1.1368 0.9496 -0.1714 0.2096 -0.3026 161 GLU A OE2 1242 N N . ALA A 162 ? 0.5778 0.6885 0.6276 -0.0999 0.1039 -0.2475 162 ALA A N 1243 C CA . ALA A 162 ? 0.5942 0.6969 0.6665 -0.0852 0.0796 -0.2321 162 ALA A CA 1244 C C . ALA A 162 ? 0.5440 0.6888 0.6499 -0.0900 0.0786 -0.2282 162 ALA A C 1245 O O . ALA A 162 ? 0.4019 0.5827 0.5500 -0.0698 0.0731 -0.2323 162 ALA A O 1246 C CB . ALA A 162 ? 0.5977 0.6972 0.6935 -0.0558 0.0714 -0.2373 162 ALA A CB 1247 N N . PRO A 163 ? 0.4770 0.6131 0.5595 -0.1161 0.0831 -0.2205 163 PRO A N 1248 C CA . PRO A 163 ? 0.4114 0.5895 0.5206 -0.1286 0.0872 -0.2221 163 PRO A CA 1249 C C . PRO A 163 ? 0.4611 0.6335 0.5862 -0.1184 0.0652 -0.2066 163 PRO A C 1250 O O . PRO A 163 ? 0.3661 0.5754 0.5156 -0.1255 0.0647 -0.2089 163 PRO A O 1251 C CB . PRO A 163 ? 0.4446 0.5965 0.5077 -0.1628 0.1033 -0.2195 163 PRO A CB 1252 C CG . PRO A 163 ? 0.4846 0.5698 0.4981 -0.1594 0.0916 -0.2044 163 PRO A CG 1253 C CD . PRO A 163 ? 0.4847 0.5676 0.5098 -0.1347 0.0842 -0.2107 163 PRO A CD 1254 N N . GLY A 164 ? 0.3219 0.3625 0.4055 0.0051 0.0722 -0.1912 164 GLY A N 1255 C CA . GLY A 164 ? 0.3069 0.3348 0.3974 0.0011 0.0566 -0.1781 164 GLY A CA 1256 C C . GLY A 164 ? 0.3268 0.3493 0.3994 -0.0140 0.0556 -0.1640 164 GLY A C 1257 O O . GLY A 164 ? 0.3078 0.3388 0.3663 -0.0224 0.0671 -0.1625 164 GLY A O 1258 N N . ASN A 165 ? 0.3022 0.3101 0.3747 -0.0170 0.0418 -0.1536 165 ASN A N 1259 C CA . ASN A 165 ? 0.3023 0.3055 0.3622 -0.0288 0.0393 -0.1405 165 ASN A CA 1260 C C . ASN A 165 ? 0.2849 0.2749 0.3138 -0.0360 0.0415 -0.1384 165 ASN A C 1261 O O . ASN A 165 ? 0.2848 0.2731 0.3029 -0.0452 0.0418 -0.1285 165 ASN A O 1262 C CB . ASN A 165 ? 0.2849 0.3085 0.3589 -0.0355 0.0464 -0.1354 165 ASN A CB 1263 C CG . ASN A 165 ? 0.2883 0.3209 0.3892 -0.0308 0.0388 -0.1333 165 ASN A CG 1264 O OD1 . ASN A 165 ? 0.2790 0.3012 0.3860 -0.0232 0.0280 -0.1335 165 ASN A OD1 1265 N ND2 . ASN A 165 ? 0.2745 0.3259 0.3911 -0.0362 0.0436 -0.1309 165 ASN A ND2 1266 N N . MET A 166 ? 0.3088 0.2885 0.3229 -0.0313 0.0419 -0.1479 166 MET A N 1267 C CA . MET A 166 ? 0.3453 0.3129 0.3285 -0.0376 0.0428 -0.1466 166 MET A CA 1268 C C . MET A 166 ? 0.3434 0.2966 0.3169 -0.0442 0.0303 -0.1341 166 MET A C 1269 O O . MET A 166 ? 0.3212 0.2713 0.2759 -0.0520 0.0318 -0.1268 166 MET A O 1270 C CB . MET A 166 ? 0.3572 0.3135 0.3257 -0.0308 0.0424 -0.1604 166 MET A CB 1271 C CG . MET A 166 ? 0.4154 0.3869 0.3905 -0.0228 0.0565 -0.1745 166 MET A CG 1272 S SD . MET A 166 ? 0.3809 0.3599 0.3933 -0.0090 0.0529 -0.1824 166 MET A SD 1273 C CE . MET A 166 ? 0.3635 0.3120 0.3645 -0.0012 0.0386 -0.1922 166 MET A CE 1274 N N . GLY A 167 ? 0.3525 0.2976 0.3389 -0.0409 0.0182 -0.1311 167 GLY A N 1275 C CA . GLY A 167 ? 0.2956 0.2315 0.2768 -0.0462 0.0076 -0.1198 167 GLY A CA 1276 C C . GLY A 167 ? 0.3965 0.3405 0.3806 -0.0517 0.0104 -0.1093 167 GLY A C 1277 O O . GLY A 167 ? 0.3022 0.2399 0.2746 -0.0564 0.0055 -0.1010 167 GLY A O 1278 N N . LEU A 168 ? 0.3525 0.3102 0.3533 -0.0507 0.0172 -0.1100 168 LEU A N 1279 C CA . LEU A 168 ? 0.3587 0.3223 0.3622 -0.0566 0.0195 -0.1014 168 LEU A CA 1280 C C . LEU A 168 ? 0.3710 0.3341 0.3549 -0.0641 0.0283 -0.0994 168 LEU A C 1281 O O . LEU A 168 ? 0.3511 0.3081 0.3255 -0.0699 0.0262 -0.0905 168 LEU A O 1282 C CB . LEU A 168 ? 0.2811 0.2597 0.3089 -0.0545 0.0225 -0.1031 168 LEU A CB 1283 C CG . LEU A 168 ? 0.3074 0.2852 0.3515 -0.0487 0.0125 -0.1009 168 LEU A CG 1284 C CD1 . LEU A 168 ? 0.2135 0.2072 0.2811 -0.0452 0.0148 -0.1047 168 LEU A CD1 1285 C CD2 . LEU A 168 ? 0.2652 0.2360 0.3042 -0.0519 0.0053 -0.0912 168 LEU A CD2 1286 N N . PHE A 169 ? 0.3103 0.2790 0.2869 -0.0636 0.0381 -0.1076 169 PHE A N 1287 C CA . PHE A 169 ? 0.3160 0.2836 0.2697 -0.0713 0.0470 -0.1048 169 PHE A CA 1288 C C . PHE A 169 ? 0.3506 0.2996 0.2768 -0.0734 0.0387 -0.1000 169 PHE A C 1289 O O . PHE A 169 ? 0.3586 0.3013 0.2656 -0.0807 0.0405 -0.0918 169 PHE A O 1290 C CB . PHE A 169 ? 0.3205 0.3016 0.2723 -0.0697 0.0614 -0.1154 169 PHE A CB 1291 C CG . PHE A 169 ? 0.3929 0.3960 0.3673 -0.0728 0.0726 -0.1159 169 PHE A CG 1292 C CD1 . PHE A 169 ? 0.3767 0.3832 0.3475 -0.0844 0.0782 -0.1057 169 PHE A CD1 1293 C CD2 . PHE A 169 ? 0.3709 0.3908 0.3711 -0.0643 0.0767 -0.1262 169 PHE A CD2 1294 C CE1 . PHE A 169 ? 0.4291 0.4572 0.4229 -0.0892 0.0878 -0.1059 169 PHE A CE1 1295 C CE2 . PHE A 169 ? 0.3987 0.4422 0.4228 -0.0674 0.0861 -0.1267 169 PHE A CE2 1296 C CZ . PHE A 169 ? 0.4422 0.4906 0.4636 -0.0806 0.0918 -0.1166 169 PHE A CZ 1297 N N . ASP A 170 ? 0.3158 0.2558 0.2410 -0.0676 0.0284 -0.1043 170 ASP A N 1298 C CA . ASP A 170 ? 0.3794 0.3044 0.2843 -0.0694 0.0177 -0.0994 170 ASP A CA 1299 C C . ASP A 170 ? 0.3920 0.3131 0.3001 -0.0726 0.0108 -0.0867 170 ASP A C 1300 O O . ASP A 170 ? 0.3596 0.2721 0.2478 -0.0770 0.0085 -0.0793 170 ASP A O 1301 C CB . ASP A 170 ? 0.3229 0.2408 0.2332 -0.0640 0.0067 -0.1054 170 ASP A CB 1302 C CG . ASP A 170 ? 0.4227 0.3386 0.3252 -0.0597 0.0110 -0.1196 170 ASP A CG 1303 O OD1 . ASP A 170 ? 0.4798 0.4001 0.3672 -0.0609 0.0226 -0.1248 170 ASP A OD1 1304 O OD2 . ASP A 170 ? 0.3908 0.2998 0.3016 -0.0553 0.0027 -0.1257 170 ASP A OD2 1305 N N . GLN A 171 ? 0.3233 0.2498 0.2550 -0.0696 0.0071 -0.0844 171 GLN A N 1306 C CA . GLN A 171 ? 0.3348 0.2588 0.2712 -0.0709 0.0020 -0.0746 171 GLN A CA 1307 C C . GLN A 171 ? 0.3397 0.2611 0.2652 -0.0776 0.0087 -0.0687 171 GLN A C 1308 O O . GLN A 171 ? 0.3210 0.2320 0.2355 -0.0795 0.0032 -0.0604 171 GLN A O 1309 C CB . GLN A 171 ? 0.3395 0.2718 0.3010 -0.0669 0.0002 -0.0749 171 GLN A CB 1310 C CG . GLN A 171 ? 0.3685 0.3012 0.3410 -0.0617 -0.0079 -0.0770 171 GLN A CG 1311 C CD . GLN A 171 ? 0.3612 0.3021 0.3549 -0.0581 -0.0085 -0.0770 171 GLN A CD 1312 O OE1 . GLN A 171 ? 0.3123 0.2578 0.3122 -0.0592 -0.0056 -0.0747 171 GLN A OE1 1313 N NE2 . GLN A 171 ? 0.2853 0.2266 0.2890 -0.0543 -0.0132 -0.0794 171 GLN A NE2 1314 N N . GLN A 172 ? 0.3383 0.2691 0.2681 -0.0813 0.0204 -0.0725 172 GLN A N 1315 C CA . GLN A 172 ? 0.3613 0.2903 0.2839 -0.0899 0.0271 -0.0657 172 GLN A CA 1316 C C . GLN A 172 ? 0.4905 0.4071 0.3823 -0.0950 0.0280 -0.0601 172 GLN A C 1317 O O . GLN A 172 ? 0.4244 0.3290 0.3042 -0.1006 0.0259 -0.0502 172 GLN A O 1318 C CB . GLN A 172 ? 0.3717 0.3181 0.3088 -0.0937 0.0401 -0.0711 172 GLN A CB 1319 C CG . GLN A 172 ? 0.3353 0.2822 0.2732 -0.1043 0.0462 -0.0636 172 GLN A CG 1320 C CD . GLN A 172 ? 0.3503 0.3197 0.3071 -0.1082 0.0592 -0.0696 172 GLN A CD 1321 O OE1 . GLN A 172 ? 0.3816 0.3607 0.3300 -0.1103 0.0708 -0.0737 172 GLN A OE1 1322 N NE2 . GLN A 172 ? 0.3170 0.2964 0.2999 -0.1083 0.0570 -0.0709 172 GLN A NE2 1323 N N . LEU A 173 ? 0.4280 0.3454 0.3056 -0.0928 0.0302 -0.0666 173 LEU A N 1324 C CA . LEU A 173 ? 0.4727 0.3786 0.3175 -0.0975 0.0307 -0.0618 173 LEU A CA 1325 C C . LEU A 173 ? 0.3809 0.2702 0.2147 -0.0955 0.0153 -0.0529 173 LEU A C 1326 O O . LEU A 173 ? 0.4818 0.3581 0.2929 -0.1006 0.0133 -0.0432 173 LEU A O 1327 C CB . LEU A 173 ? 0.4480 0.3575 0.2785 -0.0945 0.0350 -0.0728 173 LEU A CB 1328 C CG . LEU A 173 ? 0.5070 0.4069 0.2996 -0.0999 0.0380 -0.0692 173 LEU A CG 1329 C CD1 . LEU A 173 ? 0.4871 0.3904 0.2695 -0.1104 0.0520 -0.0608 173 LEU A CD1 1330 C CD2 . LEU A 173 ? 0.4992 0.4023 0.2780 -0.0955 0.0417 -0.0830 173 LEU A CD2 1331 N N . ALA A 174 ? 0.3987 0.2891 0.2496 -0.0881 0.0044 -0.0554 174 ALA A N 1332 C CA . ALA A 174 ? 0.4118 0.2915 0.2587 -0.0848 -0.0097 -0.0477 174 ALA A CA 1333 C C . ALA A 174 ? 0.4237 0.2957 0.2746 -0.0865 -0.0111 -0.0380 174 ALA A C 1334 O O . ALA A 174 ? 0.4723 0.3306 0.3081 -0.0862 -0.0194 -0.0294 174 ALA A O 1335 C CB . ALA A 174 ? 0.3697 0.2559 0.2366 -0.0776 -0.0191 -0.0522 174 ALA A CB 1336 N N . LEU A 175 ? 0.4277 0.3071 0.2983 -0.0878 -0.0044 -0.0399 175 LEU A N 1337 C CA . LEU A 175 ? 0.4655 0.3354 0.3390 -0.0903 -0.0057 -0.0324 175 LEU A CA 1338 C C . LEU A 175 ? 0.4783 0.3344 0.3275 -0.0998 -0.0014 -0.0237 175 LEU A C 1339 O O . LEU A 175 ? 0.5057 0.3445 0.3459 -0.1007 -0.0079 -0.0146 175 LEU A O 1340 C CB . LEU A 175 ? 0.4100 0.2911 0.3075 -0.0916 0.0005 -0.0370 175 LEU A CB 1341 C CG . LEU A 175 ? 0.4516 0.3469 0.3723 -0.0838 -0.0019 -0.0449 175 LEU A CG 1342 C CD1 . LEU A 175 ? 0.3481 0.2508 0.2885 -0.0852 0.0014 -0.0475 175 LEU A CD1 1343 C CD2 . LEU A 175 ? 0.4414 0.3333 0.3645 -0.0751 -0.0134 -0.0431 175 LEU A CD2 1344 N N . GLN A 176 ? 0.4649 0.3283 0.3029 -0.1063 0.0098 -0.0263 176 GLN A N 1345 C CA . GLN A 176 ? 0.4986 0.3512 0.3107 -0.1167 0.0161 -0.0174 176 GLN A CA 1346 C C . GLN A 176 ? 0.5224 0.3572 0.3059 -0.1142 0.0050 -0.0099 176 GLN A C 1347 O O . GLN A 176 ? 0.5125 0.3288 0.2754 -0.1200 0.0024 0.0021 176 GLN A O 1348 C CB . GLN A 176 ? 0.5741 0.4434 0.3818 -0.1227 0.0323 -0.0239 176 GLN A CB 1349 C CG . GLN A 176 ? 0.7947 0.6572 0.5764 -0.1351 0.0423 -0.0144 176 GLN A CG 1350 C CD . GLN A 176 ? 0.9995 0.8541 0.7895 -0.1451 0.0445 -0.0044 176 GLN A CD 1351 O OE1 . GLN A 176 ? 1.0845 0.9156 0.8595 -0.1477 0.0352 0.0074 176 GLN A OE1 1352 N NE2 . GLN A 176 ? 1.0185 0.8920 0.8333 -0.1505 0.0558 -0.0095 176 GLN A NE2 1353 N N . TRP A 177 ? 0.5445 0.3840 0.3271 -0.1058 -0.0028 -0.0165 177 TRP A N 1354 C CA . TRP A 177 ? 0.5503 0.3758 0.3089 -0.1025 -0.0159 -0.0105 177 TRP A CA 1355 C C . TRP A 177 ? 0.5054 0.3154 0.2680 -0.0980 -0.0287 -0.0006 177 TRP A C 1356 O O . TRP A 177 ? 0.5468 0.3381 0.2855 -0.0999 -0.0357 0.0105 177 TRP A O 1357 C CB . TRP A 177 ? 0.5285 0.3635 0.2918 -0.0951 -0.0235 -0.0203 177 TRP A CB 1358 C CG . TRP A 177 ? 0.5794 0.4024 0.3188 -0.0924 -0.0381 -0.0149 177 TRP A CG 1359 C CD1 . TRP A 177 ? 0.5880 0.4052 0.2950 -0.0961 -0.0385 -0.0153 177 TRP A CD1 1360 C CD2 . TRP A 177 ? 0.5196 0.3359 0.2653 -0.0851 -0.0548 -0.0084 177 TRP A CD2 1361 N NE1 . TRP A 177 ? 0.5468 0.3535 0.2397 -0.0920 -0.0561 -0.0090 177 TRP A NE1 1362 C CE2 . TRP A 177 ? 0.5533 0.3603 0.2713 -0.0849 -0.0661 -0.0046 177 TRP A CE2 1363 C CE3 . TRP A 177 ? 0.4926 0.3109 0.2645 -0.0779 -0.0612 -0.0060 177 TRP A CE3 1364 C CZ2 . TRP A 177 ? 0.5171 0.3184 0.2362 -0.0776 -0.0842 0.0019 177 TRP A CZ2 1365 C CZ3 . TRP A 177 ? 0.4923 0.3056 0.2651 -0.0701 -0.0775 -0.0003 177 TRP A CZ3 1366 C CH2 . TRP A 177 ? 0.5203 0.3259 0.2684 -0.0700 -0.0892 0.0038 177 TRP A CH2 1367 N N . VAL A 178 ? 0.4730 0.2901 0.2648 -0.0913 -0.0319 -0.0046 178 VAL A N 1368 C CA . VAL A 178 ? 0.4871 0.2910 0.2855 -0.0854 -0.0422 0.0023 178 VAL A CA 1369 C C . VAL A 178 ? 0.4772 0.2611 0.2629 -0.0936 -0.0389 0.0122 178 VAL A C 1370 O O . VAL A 178 ? 0.5098 0.2728 0.2822 -0.0908 -0.0494 0.0219 178 VAL A O 1371 C CB . VAL A 178 ? 0.4424 0.2597 0.2729 -0.0773 -0.0435 -0.0053 178 VAL A CB 1372 C CG1 . VAL A 178 ? 0.4041 0.2072 0.2401 -0.0707 -0.0522 0.0000 178 VAL A CG1 1373 C CG2 . VAL A 178 ? 0.3957 0.2294 0.2381 -0.0699 -0.0493 -0.0119 178 VAL A CG2 1374 N N . GLN A 179 ? 0.4871 0.2768 0.2778 -0.1039 -0.0251 0.0103 179 GLN A N 1375 C CA . GLN A 179 ? 0.5094 0.2803 0.2891 -0.1144 -0.0217 0.0204 179 GLN A CA 1376 C C . GLN A 179 ? 0.5584 0.3102 0.3023 -0.1205 -0.0243 0.0331 179 GLN A C 1377 O O . GLN A 179 ? 0.6139 0.3400 0.3442 -0.1231 -0.0315 0.0448 179 GLN A O 1378 C CB . GLN A 179 ? 0.5785 0.3637 0.3709 -0.1262 -0.0057 0.0164 179 GLN A CB 1379 C CG . GLN A 179 ? 0.4917 0.2880 0.3163 -0.1226 -0.0052 0.0076 179 GLN A CG 1380 C CD . GLN A 179 ? 0.4651 0.2394 0.2938 -0.1183 -0.0168 0.0119 179 GLN A CD 1381 O OE1 . GLN A 179 ? 0.5041 0.2577 0.3224 -0.1275 -0.0174 0.0210 179 GLN A OE1 1382 N NE2 . GLN A 179 ? 0.5060 0.2843 0.3491 -0.1044 -0.0258 0.0054 179 GLN A NE2 1383 N N . LYS A 180 ? 0.5955 0.3578 0.3224 -0.1223 -0.0195 0.0306 180 LYS A N 1384 C CA . LYS A 180 ? 0.6946 0.4403 0.3833 -0.1290 -0.0209 0.0423 180 LYS A CA 1385 C C . LYS A 180 ? 0.6589 0.3882 0.3306 -0.1188 -0.0401 0.0487 180 LYS A C 1386 O O . LYS A 180 ? 0.6809 0.3876 0.3224 -0.1231 -0.0461 0.0624 180 LYS A O 1387 C CB . LYS A 180 ? 0.7104 0.4736 0.3839 -0.1359 -0.0063 0.0364 180 LYS A CB 1388 C CG . LYS A 180 ? 0.8631 0.6360 0.5414 -0.1499 0.0132 0.0374 180 LYS A CG 1389 C CD . LYS A 180 ? 0.9202 0.7228 0.6117 -0.1497 0.0283 0.0223 180 LYS A CD 1390 C CE . LYS A 180 ? 0.9884 0.7945 0.6460 -0.1524 0.0351 0.0210 180 LYS A CE 1391 N NZ . LYS A 180 ? 1.0098 0.8435 0.6797 -0.1531 0.0525 0.0067 180 LYS A NZ 1392 N N . ASN A 181 ? 0.5886 0.3296 0.2805 -0.1057 -0.0503 0.0396 181 ASN A N 1393 C CA . ASN A 181 ? 0.6573 0.3907 0.3363 -0.0963 -0.0680 0.0434 181 ASN A CA 1394 C C . ASN A 181 ? 0.6206 0.3486 0.3207 -0.0827 -0.0835 0.0448 181 ASN A C 1395 O O . ASN A 181 ? 0.5880 0.3061 0.2767 -0.0752 -0.0994 0.0511 181 ASN A O 1396 C CB . ASN A 181 ? 0.6464 0.4003 0.3264 -0.0931 -0.0686 0.0318 181 ASN A CB 1397 C CG . ASN A 181 ? 0.6402 0.3965 0.2913 -0.1036 -0.0565 0.0302 181 ASN A CG 1398 O OD1 . ASN A 181 ? 0.6523 0.3930 0.2677 -0.1083 -0.0602 0.0401 181 ASN A OD1 1399 N ND2 . ASN A 181 ? 0.6067 0.3829 0.2722 -0.1063 -0.0423 0.0175 181 ASN A ND2 1400 N N . ILE A 182 ? 0.5329 0.2690 0.2636 -0.0787 -0.0793 0.0382 182 ILE A N 1401 C CA . ILE A 182 ? 0.5744 0.3124 0.3277 -0.0641 -0.0918 0.0361 182 ILE A CA 1402 C C . ILE A 182 ? 0.6252 0.3354 0.3675 -0.0576 -0.1052 0.0477 182 ILE A C 1403 O O . ILE A 182 ? 0.6016 0.3135 0.3558 -0.0435 -0.1187 0.0474 182 ILE A O 1404 C CB . ILE A 182 ? 0.4996 0.2543 0.2859 -0.0606 -0.0838 0.0253 182 ILE A CB 1405 C CG1 . ILE A 182 ? 0.4690 0.2398 0.2795 -0.0461 -0.0934 0.0196 182 ILE A CG1 1406 C CG2 . ILE A 182 ? 0.4887 0.2251 0.2777 -0.0636 -0.0803 0.0287 182 ILE A CG2 1407 C CD1 . ILE A 182 ? 0.4899 0.2835 0.3063 -0.0454 -0.0949 0.0135 182 ILE A CD1 1408 N N . ALA A 183 ? 0.6378 0.3223 0.3580 -0.0676 -0.1019 0.0582 183 ALA A N 1409 C CA . ALA A 183 ? 0.6162 0.2692 0.3230 -0.0618 -0.1160 0.0703 183 ALA A CA 1410 C C . ALA A 183 ? 0.7493 0.3976 0.4376 -0.0542 -0.1319 0.0775 183 ALA A C 1411 O O . ALA A 183 ? 0.7370 0.3706 0.4271 -0.0411 -0.1480 0.0828 183 ALA A O 1412 C CB . ALA A 183 ? 0.6508 0.2760 0.3344 -0.0771 -0.1094 0.0820 183 ALA A CB 1413 N N . ALA A 184 ? 0.7178 0.3789 0.3888 -0.0614 -0.1283 0.0768 184 ALA A N 1414 C CA . ALA A 184 ? 0.7570 0.4136 0.4069 -0.0559 -0.1444 0.0835 184 ALA A CA 1415 C C . ALA A 184 ? 0.7681 0.4442 0.4472 -0.0389 -0.1583 0.0759 184 ALA A C 1416 O O . ALA A 184 ? 0.7986 0.4687 0.4694 -0.0297 -0.1765 0.0823 184 ALA A O 1417 C CB . ALA A 184 ? 0.7559 0.4235 0.3813 -0.0673 -0.1366 0.0813 184 ALA A CB 1418 N N . PHE A 185 ? 0.6784 0.3788 0.3922 -0.0352 -0.1496 0.0628 185 PHE A N 1419 C CA . PHE A 185 ? 0.6256 0.3500 0.3717 -0.0211 -0.1585 0.0547 185 PHE A CA 1420 C C . PHE A 185 ? 0.7241 0.4412 0.4921 -0.0077 -0.1628 0.0546 185 PHE A C 1421 O O . PHE A 185 ? 0.7079 0.4466 0.5057 0.0049 -0.1675 0.0476 185 PHE A O 1422 C CB . PHE A 185 ? 0.6258 0.3802 0.3949 -0.0257 -0.1454 0.0412 185 PHE A CB 1423 C CG . PHE A 185 ? 0.6282 0.3931 0.3815 -0.0353 -0.1431 0.0377 185 PHE A CG 1424 C CD1 . PHE A 185 ? 0.6226 0.3795 0.3522 -0.0490 -0.1295 0.0377 185 PHE A CD1 1425 C CD2 . PHE A 185 ? 0.6003 0.3844 0.3640 -0.0307 -0.1544 0.0333 185 PHE A CD2 1426 C CE1 . PHE A 185 ? 0.6271 0.3929 0.3410 -0.0562 -0.1270 0.0325 185 PHE A CE1 1427 C CE2 . PHE A 185 ? 0.6204 0.4115 0.3686 -0.0393 -0.1535 0.0283 185 PHE A CE2 1428 C CZ . PHE A 185 ? 0.6357 0.4168 0.3578 -0.0512 -0.1397 0.0273 185 PHE A CZ 1429 N N . GLY A 186 ? 0.7130 0.4002 0.4666 -0.0109 -0.1605 0.0618 186 GLY A N 1430 C CA . GLY A 186 ? 0.6464 0.3211 0.4166 0.0016 -0.1647 0.0605 186 GLY A CA 1431 C C . GLY A 186 ? 0.6439 0.3295 0.4363 -0.0007 -0.1498 0.0492 186 GLY A C 1432 O O . GLY A 186 ? 0.5936 0.2771 0.4046 0.0120 -0.1526 0.0439 186 GLY A O 1433 N N . GLY A 187 ? 0.5679 0.2653 0.3580 -0.0158 -0.1344 0.0449 187 GLY A N 1434 C CA . GLY A 187 ? 0.5305 0.2389 0.3404 -0.0187 -0.1214 0.0346 187 GLY A CA 1435 C C . GLY A 187 ? 0.6133 0.2962 0.4108 -0.0304 -0.1144 0.0386 187 GLY A C 1436 O O . GLY A 187 ? 0.6344 0.2944 0.4059 -0.0406 -0.1156 0.0500 187 GLY A O 1437 N N . ASN A 188 ? 0.6277 0.3150 0.4434 -0.0297 -0.1074 0.0297 188 ASN A N 1438 C CA . ASN A 188 ? 0.5918 0.2588 0.4011 -0.0421 -0.1008 0.0315 188 ASN A CA 1439 C C . ASN A 188 ? 0.5437 0.2331 0.3610 -0.0562 -0.0849 0.0254 188 ASN A C 1440 O O . ASN A 188 ? 0.5054 0.2162 0.3442 -0.0521 -0.0795 0.0143 188 ASN A O 1441 C CB . ASN A 188 ? 0.5585 0.2123 0.3814 -0.0313 -0.1059 0.0248 188 ASN A CB 1442 C CG . ASN A 188 ? 0.5681 0.1953 0.3836 -0.0444 -0.1028 0.0273 188 ASN A CG 1443 O OD1 . ASN A 188 ? 0.6283 0.2493 0.4305 -0.0623 -0.0956 0.0351 188 ASN A OD1 1444 N ND2 . ASN A 188 ? 0.5606 0.1725 0.3849 -0.0357 -0.1083 0.0204 188 ASN A ND2 1445 N N . PRO A 189 ? 0.5650 0.2499 0.3646 -0.0723 -0.0771 0.0329 189 PRO A N 1446 C CA . PRO A 189 ? 0.5748 0.2820 0.3832 -0.0846 -0.0619 0.0268 189 PRO A CA 1447 C C . PRO A 189 ? 0.5947 0.3007 0.4204 -0.0895 -0.0569 0.0206 189 PRO A C 1448 O O . PRO A 189 ? 0.5337 0.2625 0.3743 -0.0953 -0.0465 0.0129 189 PRO A O 1449 C CB . PRO A 189 ? 0.5751 0.2724 0.3580 -0.1000 -0.0555 0.0379 189 PRO A CB 1450 C CG . PRO A 189 ? 0.6356 0.2966 0.3976 -0.0998 -0.0671 0.0511 189 PRO A CG 1451 C CD . PRO A 189 ? 0.6499 0.3075 0.4201 -0.0799 -0.0820 0.0478 189 PRO A CD 1452 N N . LYS A 190 ? 0.5344 0.2133 0.3579 -0.0867 -0.0656 0.0234 190 LYS A N 1453 C CA . LYS A 190 ? 0.5556 0.2300 0.3937 -0.0912 -0.0636 0.0167 190 LYS A CA 1454 C C . LYS A 190 ? 0.5278 0.2147 0.3854 -0.0751 -0.0678 0.0037 190 LYS A C 1455 O O . LYS A 190 ? 0.5750 0.2573 0.4431 -0.0761 -0.0683 -0.0035 190 LYS A O 1456 C CB . LYS A 190 ? 0.5816 0.2167 0.4061 -0.0977 -0.0712 0.0253 190 LYS A CB 1457 C CG . LYS A 190 ? 0.6165 0.2390 0.4224 -0.1175 -0.0650 0.0392 190 LYS A CG 1458 C CD . LYS A 190 ? 0.7490 0.3401 0.5458 -0.1208 -0.0725 0.0478 190 LYS A CD 1459 C CE . LYS A 190 ? 0.9722 0.5578 0.7525 -0.1403 -0.0644 0.0621 190 LYS A CE 1460 N NZ . LYS A 190 ? 1.0548 0.6703 0.8482 -0.1557 -0.0480 0.0580 190 LYS A NZ 1461 N N . SER A 191 ? 0.5043 0.2074 0.3664 -0.0608 -0.0710 0.0007 191 SER A N 1462 C CA . SER A 191 ? 0.4937 0.2121 0.3736 -0.0460 -0.0733 -0.0106 191 SER A CA 1463 C C . SER A 191 ? 0.5479 0.2992 0.4388 -0.0412 -0.0685 -0.0143 191 SER A C 1464 O O . SER A 191 ? 0.5684 0.3278 0.4624 -0.0288 -0.0741 -0.0142 191 SER A O 1465 C CB . SER A 191 ? 0.4813 0.1803 0.3584 -0.0296 -0.0853 -0.0108 191 SER A CB 1466 O OG . SER A 191 ? 0.4424 0.1591 0.3359 -0.0154 -0.0854 -0.0220 191 SER A OG 1467 N N . VAL A 192 ? 0.3849 0.1550 0.2829 -0.0514 -0.0585 -0.0176 192 VAL A N 1468 C CA . VAL A 192 ? 0.3574 0.1554 0.2650 -0.0494 -0.0537 -0.0211 192 VAL A CA 1469 C C . VAL A 192 ? 0.3511 0.1681 0.2772 -0.0470 -0.0490 -0.0305 192 VAL A C 1470 O O . VAL A 192 ? 0.3930 0.2093 0.3234 -0.0551 -0.0444 -0.0336 192 VAL A O 1471 C CB . VAL A 192 ? 0.4312 0.2344 0.3299 -0.0623 -0.0460 -0.0172 192 VAL A CB 1472 C CG1 . VAL A 192 ? 0.3807 0.2096 0.2898 -0.0605 -0.0415 -0.0225 192 VAL A CG1 1473 C CG2 . VAL A 192 ? 0.4319 0.2165 0.3082 -0.0651 -0.0508 -0.0070 192 VAL A CG2 1474 N N . THR A 193 ? 0.3797 0.2142 0.3167 -0.0365 -0.0505 -0.0342 193 THR A N 1475 C CA . THR A 193 ? 0.3375 0.1904 0.2893 -0.0341 -0.0463 -0.0415 193 THR A CA 1476 C C . THR A 193 ? 0.4014 0.2757 0.3609 -0.0361 -0.0422 -0.0416 193 THR A C 1477 O O . THR A 193 ? 0.3224 0.2032 0.2821 -0.0317 -0.0454 -0.0388 193 THR A O 1478 C CB . THR A 193 ? 0.2903 0.1461 0.2479 -0.0204 -0.0505 -0.0456 193 THR A CB 1479 O OG1 . THR A 193 ? 0.3395 0.1728 0.2897 -0.0182 -0.0548 -0.0476 193 THR A OG1 1480 C CG2 . THR A 193 ? 0.2906 0.1666 0.2604 -0.0181 -0.0462 -0.0515 193 THR A CG2 1481 N N . LEU A 194 ? 0.3390 0.2233 0.3056 -0.0428 -0.0361 -0.0451 194 LEU A N 1482 C CA . LEU A 194 ? 0.2988 0.2002 0.2732 -0.0437 -0.0332 -0.0462 194 LEU A CA 1483 C C . LEU A 194 ? 0.3238 0.2389 0.3098 -0.0359 -0.0345 -0.0485 194 LEU A C 1484 O O . LEU A 194 ? 0.2629 0.1775 0.2517 -0.0327 -0.0346 -0.0517 194 LEU A O 1485 C CB . LEU A 194 ? 0.3101 0.2170 0.2889 -0.0520 -0.0266 -0.0494 194 LEU A CB 1486 C CG . LEU A 194 ? 0.3348 0.2317 0.3041 -0.0615 -0.0223 -0.0477 194 LEU A CG 1487 C CD1 . LEU A 194 ? 0.3198 0.2283 0.2988 -0.0679 -0.0149 -0.0521 194 LEU A CD1 1488 C CD2 . LEU A 194 ? 0.2678 0.1570 0.2216 -0.0633 -0.0233 -0.0428 194 LEU A CD2 1489 N N . PHE A 195 ? 0.3075 0.2343 0.2990 -0.0334 -0.0357 -0.0466 195 PHE A N 1490 C CA . PHE A 195 ? 0.2460 0.1879 0.2488 -0.0289 -0.0350 -0.0473 195 PHE A CA 1491 C C . PHE A 195 ? 0.3414 0.2933 0.3513 -0.0328 -0.0344 -0.0460 195 PHE A C 1492 O O . PHE A 195 ? 0.3366 0.2854 0.3427 -0.0366 -0.0360 -0.0449 195 PHE A O 1493 C CB . PHE A 195 ? 0.2435 0.1909 0.2488 -0.0193 -0.0376 -0.0462 195 PHE A CB 1494 C CG . PHE A 195 ? 0.2259 0.1794 0.2342 -0.0164 -0.0417 -0.0420 195 PHE A CG 1495 C CD1 . PHE A 195 ? 0.2530 0.1962 0.2532 -0.0198 -0.0456 -0.0396 195 PHE A CD1 1496 C CD2 . PHE A 195 ? 0.2270 0.1984 0.2466 -0.0102 -0.0418 -0.0401 195 PHE A CD2 1497 C CE1 . PHE A 195 ? 0.2737 0.2237 0.2774 -0.0168 -0.0515 -0.0358 195 PHE A CE1 1498 C CE2 . PHE A 195 ? 0.2363 0.2170 0.2625 -0.0076 -0.0464 -0.0363 195 PHE A CE2 1499 C CZ . PHE A 195 ? 0.2751 0.2446 0.2936 -0.0108 -0.0522 -0.0344 195 PHE A CZ 1500 N N . GLY A 196 ? 0.2318 0.1936 0.2501 -0.0321 -0.0327 -0.0463 196 GLY A N 1501 C CA . GLY A 196 ? 0.1804 0.1479 0.2056 -0.0360 -0.0329 -0.0450 196 GLY A CA 1502 C C . GLY A 196 ? 0.2881 0.2655 0.3209 -0.0342 -0.0321 -0.0427 196 GLY A C 1503 O O . GLY A 196 ? 0.2077 0.1879 0.2389 -0.0299 -0.0307 -0.0436 196 GLY A O 1504 N N . GLU A 197 ? 0.2138 0.1949 0.2534 -0.0376 -0.0336 -0.0397 197 GLU A N 1505 C CA . GLU A 197 ? 0.2378 0.2272 0.2832 -0.0371 -0.0333 -0.0350 197 GLU A CA 1506 C C . GLU A 197 ? 0.2631 0.2461 0.3124 -0.0407 -0.0352 -0.0352 197 GLU A C 1507 O O . GLU A 197 ? 0.1851 0.1607 0.2354 -0.0442 -0.0371 -0.0379 197 GLU A O 1508 C CB . GLU A 197 ? 0.1809 0.1827 0.2326 -0.0379 -0.0337 -0.0281 197 GLU A CB 1509 C CG . GLU A 197 ? 0.1708 0.1825 0.2265 -0.0385 -0.0320 -0.0212 197 GLU A CG 1510 C CD . GLU A 197 ? 0.2675 0.2749 0.3299 -0.0459 -0.0355 -0.0163 197 GLU A CD 1511 O OE1 . GLU A 197 ? 0.2311 0.2283 0.2950 -0.0496 -0.0393 -0.0199 197 GLU A OE1 1512 O OE2 . GLU A 197 ? 0.2221 0.2347 0.2867 -0.0480 -0.0348 -0.0087 197 GLU A OE2 1513 N N A SER A 198 ? 0.2244 0.2095 0.2749 -0.0390 -0.0353 -0.0329 198 SER A N 1514 N N B SER A 198 ? 0.2250 0.2102 0.2756 -0.0390 -0.0353 -0.0329 198 SER A N 1515 C CA A SER A 198 ? 0.2128 0.1909 0.2679 -0.0404 -0.0383 -0.0328 198 SER A CA 1516 C CA B SER A 198 ? 0.2165 0.1947 0.2716 -0.0403 -0.0383 -0.0330 198 SER A CA 1517 C C A SER A 198 ? 0.2470 0.2175 0.3029 -0.0398 -0.0378 -0.0417 198 SER A C 1518 C C B SER A 198 ? 0.2503 0.2207 0.3062 -0.0398 -0.0377 -0.0418 198 SER A C 1519 O O A SER A 198 ? 0.2412 0.2134 0.2950 -0.0377 -0.0355 -0.0464 198 SER A O 1520 O O B SER A 198 ? 0.2437 0.2158 0.2976 -0.0377 -0.0354 -0.0467 198 SER A O 1521 C CB A SER A 198 ? 0.2628 0.2382 0.3233 -0.0456 -0.0416 -0.0267 198 SER A CB 1522 C CB B SER A 198 ? 0.2594 0.2350 0.3199 -0.0452 -0.0417 -0.0263 198 SER A CB 1523 O OG A SER A 198 ? 0.2850 0.2559 0.3484 -0.0459 -0.0450 -0.0216 198 SER A OG 1524 O OG B SER A 198 ? 0.2502 0.2220 0.3119 -0.0491 -0.0429 -0.0288 198 SER A OG 1525 N N . ALA A 199 ? 0.2370 0.1994 0.2959 -0.0421 -0.0396 -0.0445 199 ALA A N 1526 C CA . ALA A 199 ? 0.2470 0.2047 0.3063 -0.0409 -0.0372 -0.0536 199 ALA A CA 1527 C C . ALA A 199 ? 0.2572 0.2162 0.3083 -0.0426 -0.0326 -0.0574 199 ALA A C 1528 O O . ALA A 199 ? 0.2562 0.2155 0.3068 -0.0423 -0.0284 -0.0634 199 ALA A O 1529 C CB . ALA A 199 ? 0.2561 0.2035 0.3180 -0.0416 -0.0400 -0.0575 199 ALA A CB 1530 N N . GLY A 200 ? 0.2158 0.1762 0.2613 -0.0445 -0.0335 -0.0531 200 GLY A N 1531 C CA . GLY A 200 ? 0.2145 0.1738 0.2511 -0.0453 -0.0308 -0.0546 200 GLY A CA 1532 C C . GLY A 200 ? 0.1974 0.1598 0.2333 -0.0431 -0.0284 -0.0550 200 GLY A C 1533 O O . GLY A 200 ? 0.2149 0.1737 0.2456 -0.0448 -0.0253 -0.0581 200 GLY A O 1534 N N . ALA A 201 ? 0.1837 0.1519 0.2237 -0.0400 -0.0300 -0.0518 201 ALA A N 1535 C CA . ALA A 201 ? 0.2456 0.2154 0.2841 -0.0378 -0.0292 -0.0536 201 ALA A CA 1536 C C . ALA A 201 ? 0.2668 0.2371 0.3114 -0.0390 -0.0282 -0.0587 201 ALA A C 1537 O O . ALA A 201 ? 0.2474 0.2168 0.2910 -0.0405 -0.0270 -0.0621 201 ALA A O 1538 C CB . ALA A 201 ? 0.1771 0.1534 0.2152 -0.0337 -0.0310 -0.0496 201 ALA A CB 1539 N N . ALA A 202 ? 0.2285 0.2006 0.2810 -0.0383 -0.0295 -0.0592 202 ALA A N 1540 C CA . ALA A 202 ? 0.2585 0.2339 0.3203 -0.0382 -0.0284 -0.0648 202 ALA A CA 1541 C C . ALA A 202 ? 0.2448 0.2189 0.3045 -0.0424 -0.0224 -0.0697 202 ALA A C 1542 O O . ALA A 202 ? 0.2753 0.2543 0.3402 -0.0448 -0.0198 -0.0733 202 ALA A O 1543 C CB . ALA A 202 ? 0.2518 0.2266 0.3222 -0.0350 -0.0313 -0.0650 202 ALA A CB 1544 N N . SER A 203 ? 0.2505 0.2185 0.3020 -0.0443 -0.0204 -0.0692 203 SER A N 1545 C CA . SER A 203 ? 0.2511 0.2163 0.2952 -0.0489 -0.0145 -0.0722 203 SER A CA 1546 C C . SER A 203 ? 0.2486 0.2114 0.2865 -0.0525 -0.0132 -0.0700 203 SER A C 1547 O O . SER A 203 ? 0.2948 0.2596 0.3337 -0.0573 -0.0081 -0.0724 203 SER A O 1548 C CB . SER A 203 ? 0.3025 0.2600 0.3352 -0.0499 -0.0153 -0.0711 203 SER A CB 1549 O OG . SER A 203 ? 0.3043 0.2606 0.3418 -0.0474 -0.0173 -0.0740 203 SER A OG 1550 N N . VAL A 204 ? 0.2641 0.2225 0.2963 -0.0504 -0.0177 -0.0655 204 VAL A N 1551 C CA . VAL A 204 ? 0.2629 0.2151 0.2886 -0.0525 -0.0180 -0.0641 204 VAL A CA 1552 C C . VAL A 204 ? 0.2483 0.2053 0.2832 -0.0550 -0.0174 -0.0677 204 VAL A C 1553 O O . VAL A 204 ? 0.2475 0.2005 0.2804 -0.0613 -0.0147 -0.0684 204 VAL A O 1554 C CB . VAL A 204 ? 0.2923 0.2412 0.3128 -0.0470 -0.0229 -0.0606 204 VAL A CB 1555 C CG1 . VAL A 204 ? 0.3115 0.2515 0.3262 -0.0475 -0.0244 -0.0612 204 VAL A CG1 1556 C CG2 . VAL A 204 ? 0.2819 0.2274 0.2953 -0.0456 -0.0243 -0.0568 204 VAL A CG2 1557 N N . SER A 205 ? 0.2196 0.1853 0.2647 -0.0511 -0.0206 -0.0695 205 SER A N 1558 C CA . SER A 205 ? 0.2802 0.2520 0.3353 -0.0533 -0.0222 -0.0732 205 SER A CA 1559 C C . SER A 205 ? 0.2492 0.2291 0.3150 -0.0592 -0.0162 -0.0768 205 SER A C 1560 O O . SER A 205 ? 0.2616 0.2451 0.3343 -0.0650 -0.0159 -0.0790 205 SER A O 1561 C CB . SER A 205 ? 0.2749 0.2543 0.3372 -0.0472 -0.0281 -0.0736 205 SER A CB 1562 O OG . SER A 205 ? 0.2815 0.2675 0.3529 -0.0442 -0.0275 -0.0739 205 SER A OG 1563 N N . LEU A 206 ? 0.2175 0.2008 0.2848 -0.0580 -0.0114 -0.0778 206 LEU A N 1564 C CA . LEU A 206 ? 0.2829 0.2767 0.3601 -0.0620 -0.0038 -0.0821 206 LEU A CA 1565 C C . LEU A 206 ? 0.2712 0.2592 0.3376 -0.0711 0.0031 -0.0800 206 LEU A C 1566 O O . LEU A 206 ? 0.2781 0.2761 0.3535 -0.0778 0.0095 -0.0821 206 LEU A O 1567 C CB . LEU A 206 ? 0.2442 0.2413 0.3243 -0.0562 -0.0012 -0.0855 206 LEU A CB 1568 C CG . LEU A 206 ? 0.2596 0.2644 0.3554 -0.0482 -0.0069 -0.0882 206 LEU A CG 1569 C CD1 . LEU A 206 ? 0.2533 0.2562 0.3504 -0.0423 -0.0054 -0.0921 206 LEU A CD1 1570 C CD2 . LEU A 206 ? 0.1772 0.1986 0.2932 -0.0491 -0.0067 -0.0923 206 LEU A CD2 1571 N N . HIS A 207 ? 0.2259 0.1986 0.2735 -0.0716 0.0017 -0.0751 207 HIS A N 1572 C CA . HIS A 207 ? 0.2193 0.1822 0.2535 -0.0800 0.0059 -0.0710 207 HIS A CA 1573 C C . HIS A 207 ? 0.2298 0.1891 0.2688 -0.0863 0.0031 -0.0697 207 HIS A C 1574 O O . HIS A 207 ? 0.2478 0.2038 0.2835 -0.0963 0.0080 -0.0670 207 HIS A O 1575 C CB . HIS A 207 ? 0.2845 0.2314 0.2988 -0.0774 0.0022 -0.0658 207 HIS A CB 1576 C CG . HIS A 207 ? 0.2370 0.1848 0.2432 -0.0751 0.0052 -0.0670 207 HIS A CG 1577 N ND1 . HIS A 207 ? 0.2558 0.2050 0.2530 -0.0807 0.0136 -0.0678 207 HIS A ND1 1578 C CD2 . HIS A 207 ? 0.2497 0.1970 0.2547 -0.0684 0.0006 -0.0679 207 HIS A CD2 1579 C CE1 . HIS A 207 ? 0.2978 0.2462 0.2874 -0.0766 0.0134 -0.0704 207 HIS A CE1 1580 N NE2 . HIS A 207 ? 0.2310 0.1777 0.2262 -0.0697 0.0050 -0.0703 207 HIS A NE2 1581 N N . LEU A 208 ? 0.2476 0.2066 0.2931 -0.0813 -0.0050 -0.0715 208 LEU A N 1582 C CA . LEU A 208 ? 0.2728 0.2283 0.3235 -0.0869 -0.0092 -0.0725 208 LEU A CA 1583 C C . LEU A 208 ? 0.3045 0.2780 0.3752 -0.0945 -0.0049 -0.0761 208 LEU A C 1584 O O . LEU A 208 ? 0.3140 0.2852 0.3897 -0.1041 -0.0060 -0.0759 208 LEU A O 1585 C CB . LEU A 208 ? 0.2458 0.1986 0.2969 -0.0788 -0.0188 -0.0750 208 LEU A CB 1586 C CG . LEU A 208 ? 0.2967 0.2321 0.3305 -0.0724 -0.0236 -0.0724 208 LEU A CG 1587 C CD1 . LEU A 208 ? 0.2645 0.2035 0.2990 -0.0633 -0.0303 -0.0754 208 LEU A CD1 1588 C CD2 . LEU A 208 ? 0.2432 0.1592 0.2671 -0.0786 -0.0260 -0.0708 208 LEU A CD2 1589 N N . LEU A 209 ? 0.2697 0.2613 0.3534 -0.0902 -0.0005 -0.0797 209 LEU A N 1590 C CA . LEU A 209 ? 0.3375 0.3507 0.4441 -0.0954 0.0039 -0.0839 209 LEU A CA 1591 C C . LEU A 209 ? 0.3634 0.3857 0.4708 -0.1031 0.0174 -0.0831 209 LEU A C 1592 O O . LEU A 209 ? 0.4363 0.4771 0.5624 -0.1106 0.0230 -0.0853 209 LEU A O 1593 C CB . LEU A 209 ? 0.4094 0.4387 0.5329 -0.0849 0.0002 -0.0892 209 LEU A CB 1594 C CG . LEU A 209 ? 0.4549 0.4803 0.5788 -0.0766 -0.0122 -0.0898 209 LEU A CG 1595 C CD1 . LEU A 209 ? 0.4750 0.5180 0.6187 -0.0685 -0.0154 -0.0941 209 LEU A CD1 1596 C CD2 . LEU A 209 ? 0.4358 0.4559 0.5598 -0.0825 -0.0200 -0.0901 209 LEU A CD2 1597 N N . SER A 210 ? 0.2826 0.2940 0.3702 -0.1012 0.0227 -0.0802 210 SER A N 1598 C CA . SER A 210 ? 0.2970 0.3179 0.3818 -0.1071 0.0361 -0.0804 210 SER A CA 1599 C C . SER A 210 ? 0.2984 0.3098 0.3713 -0.1216 0.0414 -0.0728 210 SER A C 1600 O O . SER A 210 ? 0.3303 0.3181 0.3810 -0.1232 0.0368 -0.0663 210 SER A O 1601 C CB . SER A 210 ? 0.3031 0.3162 0.3700 -0.0991 0.0386 -0.0814 210 SER A CB 1602 O OG . SER A 210 ? 0.3454 0.3699 0.4090 -0.1028 0.0519 -0.0838 210 SER A OG 1603 N N . PRO A 211 ? 0.4050 0.4348 0.4931 -0.1325 0.0510 -0.0730 211 PRO A N 1604 C CA . PRO A 211 ? 0.4883 0.5073 0.5653 -0.1486 0.0556 -0.0640 211 PRO A CA 1605 C C . PRO A 211 ? 0.4461 0.4481 0.4915 -0.1504 0.0617 -0.0573 211 PRO A C 1606 O O . PRO A 211 ? 0.4754 0.4552 0.5027 -0.1593 0.0591 -0.0479 211 PRO A O 1607 C CB . PRO A 211 ? 0.4828 0.5321 0.5854 -0.1592 0.0673 -0.0663 211 PRO A CB 1608 C CG . PRO A 211 ? 0.4977 0.5692 0.6295 -0.1485 0.0619 -0.0764 211 PRO A CG 1609 C CD . PRO A 211 ? 0.4086 0.4700 0.5272 -0.1311 0.0566 -0.0808 211 PRO A CD 1610 N N . GLY A 212 ? 0.3621 0.3723 0.4000 -0.1416 0.0681 -0.0622 212 GLY A N 1611 C CA . GLY A 212 ? 0.4268 0.4213 0.4331 -0.1419 0.0719 -0.0571 212 GLY A CA 1612 C C . GLY A 212 ? 0.4815 0.4474 0.4672 -0.1355 0.0581 -0.0521 212 GLY A C 1613 O O . GLY A 212 ? 0.4934 0.4422 0.4522 -0.1382 0.0582 -0.0451 212 GLY A O 1614 N N . SER A 213 ? 0.3832 0.3451 0.3812 -0.1266 0.0462 -0.0555 213 SER A N 1615 C CA . SER A 213 ? 0.3602 0.2990 0.3422 -0.1201 0.0341 -0.0512 213 SER A CA 1616 C C . SER A 213 ? 0.3985 0.3188 0.3782 -0.1255 0.0262 -0.0450 213 SER A C 1617 O O . SER A 213 ? 0.4332 0.3341 0.3995 -0.1198 0.0169 -0.0411 213 SER A O 1618 C CB . SER A 213 ? 0.3279 0.2720 0.3205 -0.1064 0.0262 -0.0579 213 SER A CB 1619 O OG . SER A 213 ? 0.3438 0.2987 0.3359 -0.1008 0.0311 -0.0638 213 SER A OG 1620 N N . HIS A 214 ? 0.3789 0.3052 0.3727 -0.1361 0.0294 -0.0445 214 HIS A N 1621 C CA A HIS A 214 ? 0.4155 0.3237 0.4101 -0.1412 0.0205 -0.0411 214 HIS A CA 1622 C CA B HIS A 214 ? 0.4079 0.3158 0.4021 -0.1401 0.0200 -0.0414 214 HIS A CA 1623 C C . HIS A 214 ? 0.4276 0.3054 0.3965 -0.1440 0.0156 -0.0312 214 HIS A C 1624 O O . HIS A 214 ? 0.4653 0.3234 0.4286 -0.1376 0.0044 -0.0308 214 HIS A O 1625 C CB A HIS A 214 ? 0.4436 0.3640 0.4570 -0.1560 0.0259 -0.0411 214 HIS A CB 1626 C CB B HIS A 214 ? 0.4353 0.3559 0.4514 -0.1521 0.0227 -0.0434 214 HIS A CB 1627 C CG A HIS A 214 ? 0.4826 0.3841 0.4988 -0.1622 0.0156 -0.0396 214 HIS A CG 1628 C CG B HIS A 214 ? 0.3876 0.3304 0.4288 -0.1448 0.0196 -0.0535 214 HIS A CG 1629 N ND1 A HIS A 214 ? 0.5045 0.3769 0.5020 -0.1686 0.0113 -0.0303 214 HIS A ND1 1630 N ND1 B HIS A 214 ? 0.3129 0.2693 0.3771 -0.1531 0.0184 -0.0570 214 HIS A ND1 1631 C CD2 A HIS A 214 ? 0.4634 0.3719 0.4988 -0.1592 0.0073 -0.0455 214 HIS A CD2 1632 C CD2 B HIS A 214 ? 0.3137 0.2664 0.3602 -0.1304 0.0163 -0.0600 214 HIS A CD2 1633 C CE1 A HIS A 214 ? 0.4356 0.2988 0.4423 -0.1673 0.0011 -0.0315 214 HIS A CE1 1634 C CE1 B HIS A 214 ? 0.2750 0.2486 0.3562 -0.1430 0.0140 -0.0653 214 HIS A CE1 1635 N NE2 A HIS A 214 ? 0.4006 0.2854 0.4294 -0.1623 -0.0015 -0.0407 214 HIS A NE2 1636 N NE2 B HIS A 214 ? 0.4299 0.4006 0.5002 -0.1294 0.0131 -0.0667 214 HIS A NE2 1637 N N . SER A 215 ? 0.4211 0.2949 0.3734 -0.1530 0.0239 -0.0233 215 SER A N 1638 C CA . SER A 215 ? 0.5563 0.3996 0.4828 -0.1565 0.0185 -0.0121 215 SER A CA 1639 C C . SER A 215 ? 0.5116 0.3448 0.4203 -0.1425 0.0114 -0.0112 215 SER A C 1640 O O . SER A 215 ? 0.5149 0.3235 0.4022 -0.1424 0.0050 -0.0023 215 SER A O 1641 C CB . SER A 215 ? 0.6840 0.5260 0.5965 -0.1729 0.0300 -0.0021 215 SER A CB 1642 O OG . SER A 215 ? 0.7814 0.6398 0.6839 -0.1698 0.0396 -0.0039 215 SER A OG 1643 N N . LEU A 216 ? 0.4193 0.2713 0.3377 -0.1310 0.0117 -0.0201 216 LEU A N 1644 C CA . LEU A 216 ? 0.3928 0.2401 0.2968 -0.1202 0.0062 -0.0195 216 LEU A CA 1645 C C . LEU A 216 ? 0.4613 0.3006 0.3705 -0.1068 -0.0063 -0.0219 216 LEU A C 1646 O O . LEU A 216 ? 0.4413 0.2787 0.3422 -0.0978 -0.0122 -0.0212 216 LEU A O 1647 C CB . LEU A 216 ? 0.4047 0.2747 0.3138 -0.1164 0.0135 -0.0270 216 LEU A CB 1648 C CG . LEU A 216 ? 0.4792 0.3626 0.3844 -0.1266 0.0279 -0.0274 216 LEU A CG 1649 C CD1 . LEU A 216 ? 0.3481 0.2484 0.2547 -0.1194 0.0324 -0.0363 216 LEU A CD1 1650 C CD2 . LEU A 216 ? 0.4938 0.3600 0.3714 -0.1365 0.0307 -0.0159 216 LEU A CD2 1651 N N . PHE A 217 ? 0.4033 0.2399 0.3265 -0.1054 -0.0104 -0.0255 217 PHE A N 1652 C CA . PHE A 217 ? 0.3670 0.1980 0.2944 -0.0921 -0.0206 -0.0286 217 PHE A CA 1653 C C . PHE A 217 ? 0.4008 0.2192 0.3345 -0.0929 -0.0258 -0.0310 217 PHE A C 1654 O O . PHE A 217 ? 0.4141 0.2312 0.3532 -0.1045 -0.0221 -0.0309 217 PHE A O 1655 C CB . PHE A 217 ? 0.3115 0.1650 0.2531 -0.0827 -0.0200 -0.0361 217 PHE A CB 1656 C CG . PHE A 217 ? 0.3783 0.2491 0.3390 -0.0850 -0.0156 -0.0434 217 PHE A CG 1657 C CD1 . PHE A 217 ? 0.3485 0.2339 0.3162 -0.0930 -0.0065 -0.0453 217 PHE A CD1 1658 C CD2 . PHE A 217 ? 0.3505 0.2241 0.3218 -0.0778 -0.0209 -0.0487 217 PHE A CD2 1659 C CE1 . PHE A 217 ? 0.3062 0.2088 0.2936 -0.0938 -0.0040 -0.0520 217 PHE A CE1 1660 C CE2 . PHE A 217 ? 0.3144 0.2036 0.3021 -0.0794 -0.0188 -0.0548 217 PHE A CE2 1661 C CZ . PHE A 217 ? 0.3024 0.2062 0.2993 -0.0872 -0.0110 -0.0562 217 PHE A CZ 1662 N N . THR A 218 ? 0.3736 0.1833 0.3070 -0.0806 -0.0345 -0.0336 218 THR A N 1663 C CA . THR A 218 ? 0.4127 0.2056 0.3479 -0.0793 -0.0410 -0.0370 218 THR A CA 1664 C C . THR A 218 ? 0.3707 0.1795 0.3206 -0.0719 -0.0420 -0.0473 218 THR A C 1665 O O . THR A 218 ? 0.4131 0.2200 0.3699 -0.0776 -0.0432 -0.0522 218 THR A O 1666 C CB . THR A 218 ? 0.4849 0.2543 0.4075 -0.0684 -0.0505 -0.0340 218 THR A CB 1667 O OG1 . THR A 218 ? 0.4985 0.2544 0.4052 -0.0728 -0.0511 -0.0234 218 THR A OG1 1668 C CG2 . THR A 218 ? 0.5133 0.2581 0.4338 -0.0684 -0.0578 -0.0377 218 THR A CG2 1669 N N . ARG A 219 ? 0.3286 0.1531 0.2826 -0.0599 -0.0422 -0.0499 219 ARG A N 1670 C CA . ARG A 219 ? 0.3574 0.1951 0.3210 -0.0514 -0.0436 -0.0580 219 ARG A CA 1671 C C . ARG A 219 ? 0.3716 0.2342 0.3438 -0.0474 -0.0390 -0.0580 219 ARG A C 1672 O O . ARG A 219 ? 0.3239 0.1911 0.2938 -0.0495 -0.0362 -0.0530 219 ARG A O 1673 C CB . ARG A 219 ? 0.3584 0.1840 0.3158 -0.0379 -0.0503 -0.0612 219 ARG A CB 1674 C CG . ARG A 219 ? 0.6117 0.4162 0.5644 -0.0387 -0.0562 -0.0667 219 ARG A CG 1675 C CD . ARG A 219 ? 0.5990 0.3937 0.5457 -0.0224 -0.0619 -0.0721 219 ARG A CD 1676 N NE . ARG A 219 ? 0.5673 0.3450 0.5057 -0.0170 -0.0659 -0.0659 219 ARG A NE 1677 C CZ . ARG A 219 ? 0.5430 0.2899 0.4712 -0.0208 -0.0721 -0.0633 219 ARG A CZ 1678 N NH1 . ARG A 219 ? 0.5062 0.2419 0.4341 -0.0309 -0.0728 -0.0655 219 ARG A NH1 1679 N NH2 . ARG A 219 ? 0.5218 0.2537 0.4420 -0.0145 -0.0769 -0.0567 219 ARG A NH2 1680 N N . ALA A 220 ? 0.2626 0.1396 0.2431 -0.0420 -0.0391 -0.0633 220 ALA A N 1681 C CA . ALA A 220 ? 0.2419 0.1397 0.2308 -0.0398 -0.0354 -0.0624 220 ALA A CA 1682 C C . ALA A 220 ? 0.2650 0.1743 0.2568 -0.0295 -0.0368 -0.0648 220 ALA A C 1683 O O . ALA A 220 ? 0.2479 0.1540 0.2372 -0.0252 -0.0395 -0.0700 220 ALA A O 1684 C CB . ALA A 220 ? 0.2818 0.1903 0.2805 -0.0484 -0.0315 -0.0641 220 ALA A CB 1685 N N . ILE A 221 ? 0.2214 0.1442 0.2178 -0.0265 -0.0347 -0.0611 221 ILE A N 1686 C CA . ILE A 221 ? 0.2553 0.1922 0.2553 -0.0188 -0.0344 -0.0612 221 ILE A CA 1687 C C . ILE A 221 ? 0.3215 0.2723 0.3300 -0.0226 -0.0320 -0.0585 221 ILE A C 1688 O O . ILE A 221 ? 0.2785 0.2309 0.2904 -0.0270 -0.0309 -0.0554 221 ILE A O 1689 C CB . ILE A 221 ? 0.2748 0.2155 0.2746 -0.0114 -0.0351 -0.0578 221 ILE A CB 1690 C CG1 . ILE A 221 ? 0.2338 0.1592 0.2254 -0.0047 -0.0385 -0.0608 221 ILE A CG1 1691 C CG2 . ILE A 221 ? 0.2144 0.1747 0.2206 -0.0058 -0.0326 -0.0560 221 ILE A CG2 1692 C CD1 . ILE A 221 ? 0.2366 0.1691 0.2312 0.0051 -0.0399 -0.0582 221 ILE A CD1 1693 N N . LEU A 222 ? 0.1965 0.1558 0.2070 -0.0205 -0.0320 -0.0598 222 LEU A N 1694 C CA . LEU A 222 ? 0.1866 0.1555 0.2048 -0.0238 -0.0313 -0.0568 222 LEU A CA 1695 C C . LEU A 222 ? 0.2264 0.2077 0.2454 -0.0195 -0.0304 -0.0520 222 LEU A C 1696 O O . LEU A 222 ? 0.2317 0.2172 0.2454 -0.0154 -0.0308 -0.0532 222 LEU A O 1697 C CB . LEU A 222 ? 0.1871 0.1548 0.2081 -0.0268 -0.0333 -0.0608 222 LEU A CB 1698 C CG . LEU A 222 ? 0.3195 0.2811 0.3450 -0.0335 -0.0327 -0.0644 222 LEU A CG 1699 C CD1 . LEU A 222 ? 0.4337 0.3828 0.4516 -0.0350 -0.0332 -0.0672 222 LEU A CD1 1700 C CD2 . LEU A 222 ? 0.2746 0.2417 0.3079 -0.0355 -0.0353 -0.0677 222 LEU A CD2 1701 N N . GLN A 223 ? 0.2224 0.2100 0.2470 -0.0210 -0.0291 -0.0464 223 GLN A N 1702 C CA . GLN A 223 ? 0.2442 0.2452 0.2714 -0.0192 -0.0274 -0.0402 223 GLN A CA 1703 C C . GLN A 223 ? 0.2638 0.2663 0.2959 -0.0241 -0.0288 -0.0353 223 GLN A C 1704 O O . GLN A 223 ? 0.1971 0.1952 0.2356 -0.0291 -0.0304 -0.0339 223 GLN A O 1705 C CB . GLN A 223 ? 0.2043 0.2129 0.2374 -0.0189 -0.0263 -0.0362 223 GLN A CB 1706 C CG . GLN A 223 ? 0.1927 0.1997 0.2216 -0.0118 -0.0259 -0.0404 223 GLN A CG 1707 C CD . GLN A 223 ? 0.2628 0.2761 0.2992 -0.0113 -0.0272 -0.0371 223 GLN A CD 1708 O OE1 . GLN A 223 ? 0.2760 0.2817 0.3091 -0.0072 -0.0295 -0.0400 223 GLN A OE1 1709 N NE2 . GLN A 223 ? 0.1903 0.2169 0.2370 -0.0157 -0.0268 -0.0306 223 GLN A NE2 1710 N N . SER A 224 ? 0.2214 0.2282 0.2488 -0.0221 -0.0291 -0.0330 224 SER A N 1711 C CA . SER A 224 ? 0.2397 0.2458 0.2708 -0.0258 -0.0319 -0.0269 224 SER A CA 1712 C C . SER A 224 ? 0.2610 0.2564 0.2990 -0.0287 -0.0358 -0.0308 224 SER A C 1713 O O . SER A 224 ? 0.2081 0.1995 0.2528 -0.0323 -0.0378 -0.0269 224 SER A O 1714 C CB . SER A 224 ? 0.1899 0.2029 0.2269 -0.0303 -0.0303 -0.0173 224 SER A CB 1715 O OG . SER A 224 ? 0.2032 0.2308 0.2363 -0.0278 -0.0251 -0.0129 224 SER A OG 1716 N N . GLY A 225 ? 0.2165 0.2074 0.2538 -0.0272 -0.0367 -0.0387 225 GLY A N 1717 C CA . GLY A 225 ? 0.2592 0.2446 0.3050 -0.0290 -0.0390 -0.0428 225 GLY A CA 1718 C C . GLY A 225 ? 0.2679 0.2522 0.3149 -0.0289 -0.0391 -0.0508 225 GLY A C 1719 O O . GLY A 225 ? 0.2537 0.2366 0.2944 -0.0288 -0.0372 -0.0539 225 GLY A O 1720 N N . SER A 226 ? 0.2231 0.2081 0.2794 -0.0288 -0.0416 -0.0542 226 SER A N 1721 C CA . SER A 226 ? 0.2079 0.1948 0.2696 -0.0306 -0.0412 -0.0614 226 SER A CA 1722 C C . SER A 226 ? 0.2828 0.2735 0.3592 -0.0298 -0.0424 -0.0646 226 SER A C 1723 O O . SER A 226 ? 0.2445 0.2342 0.3246 -0.0263 -0.0461 -0.0610 226 SER A O 1724 C CB . SER A 226 ? 0.2001 0.1894 0.2565 -0.0291 -0.0458 -0.0633 226 SER A CB 1725 O OG . SER A 226 ? 0.2081 0.2011 0.2636 -0.0249 -0.0520 -0.0595 226 SER A OG 1726 N N . PHE A 227 ? 0.2355 0.2308 0.3209 -0.0329 -0.0391 -0.0710 227 PHE A N 1727 C CA . PHE A 227 ? 0.2597 0.2613 0.3608 -0.0307 -0.0383 -0.0752 227 PHE A CA 1728 C C . PHE A 227 ? 0.3273 0.3353 0.4393 -0.0249 -0.0468 -0.0749 227 PHE A C 1729 O O . PHE A 227 ? 0.3620 0.3725 0.4862 -0.0200 -0.0483 -0.0769 227 PHE A O 1730 C CB . PHE A 227 ? 0.3072 0.3167 0.4171 -0.0358 -0.0315 -0.0817 227 PHE A CB 1731 C CG . PHE A 227 ? 0.3664 0.3851 0.4848 -0.0388 -0.0349 -0.0844 227 PHE A CG 1732 C CD1 . PHE A 227 ? 0.4593 0.4909 0.5959 -0.0349 -0.0405 -0.0875 227 PHE A CD1 1733 C CD2 . PHE A 227 ? 0.3643 0.3779 0.4733 -0.0453 -0.0339 -0.0840 227 PHE A CD2 1734 C CE1 . PHE A 227 ? 0.4984 0.5391 0.6436 -0.0387 -0.0453 -0.0903 227 PHE A CE1 1735 C CE2 . PHE A 227 ? 0.4504 0.4704 0.5670 -0.0493 -0.0383 -0.0871 227 PHE A CE2 1736 C CZ . PHE A 227 ? 0.4574 0.4918 0.5924 -0.0465 -0.0441 -0.0903 227 PHE A CZ 1737 N N . ASN A 228 ? 0.2072 0.2174 0.3144 -0.0248 -0.0531 -0.0730 228 ASN A N 1738 C CA . ASN A 228 ? 0.2170 0.2332 0.3325 -0.0193 -0.0629 -0.0721 228 ASN A CA 1739 C C . ASN A 228 ? 0.2457 0.2530 0.3526 -0.0141 -0.0683 -0.0636 228 ASN A C 1740 O O . ASN A 228 ? 0.2159 0.2251 0.3258 -0.0091 -0.0776 -0.0607 228 ASN A O 1741 C CB . ASN A 228 ? 0.1852 0.2064 0.2969 -0.0215 -0.0690 -0.0742 228 ASN A CB 1742 C CG . ASN A 228 ? 0.2556 0.2673 0.3443 -0.0230 -0.0682 -0.0706 228 ASN A CG 1743 O OD1 . ASN A 228 ? 0.2972 0.3020 0.3771 -0.0255 -0.0605 -0.0691 228 ASN A OD1 1744 N ND2 . ASN A 228 ? 0.1991 0.2114 0.2779 -0.0206 -0.0763 -0.0696 228 ASN A ND2 1745 N N . ALA A 229 ? 0.2210 0.2187 0.3174 -0.0159 -0.0632 -0.0588 229 ALA A N 1746 C CA . ALA A 229 ? 0.2857 0.2746 0.3762 -0.0132 -0.0675 -0.0498 229 ALA A CA 1747 C C . ALA A 229 ? 0.3031 0.2888 0.4090 -0.0078 -0.0718 -0.0518 229 ALA A C 1748 O O . ALA A 229 ? 0.2812 0.2703 0.3992 -0.0073 -0.0669 -0.0602 229 ALA A O 1749 C CB . ALA A 229 ? 0.2391 0.2208 0.3194 -0.0178 -0.0612 -0.0452 229 ALA A CB 1750 N N . PRO A 230 ? 0.2549 0.2336 0.3595 -0.0033 -0.0808 -0.0440 230 PRO A N 1751 C CA . PRO A 230 ? 0.3091 0.2834 0.4297 0.0041 -0.0866 -0.0468 230 PRO A CA 1752 C C . PRO A 230 ? 0.3700 0.3336 0.4954 0.0039 -0.0814 -0.0509 230 PRO A C 1753 O O . PRO A 230 ? 0.3103 0.2733 0.4510 0.0111 -0.0834 -0.0580 230 PRO A O 1754 C CB . PRO A 230 ? 0.3242 0.2883 0.4371 0.0077 -0.0979 -0.0347 230 PRO A CB 1755 C CG . PRO A 230 ? 0.3810 0.3416 0.4727 0.0002 -0.0944 -0.0247 230 PRO A CG 1756 C CD . PRO A 230 ? 0.3092 0.2827 0.3970 -0.0045 -0.0855 -0.0321 230 PRO A CD 1757 N N . TRP A 231 ? 0.3118 0.2680 0.4251 -0.0034 -0.0755 -0.0475 231 TRP A N 1758 C CA . TRP A 231 ? 0.2678 0.2126 0.3830 -0.0045 -0.0720 -0.0520 231 TRP A CA 1759 C C . TRP A 231 ? 0.2628 0.2163 0.3804 -0.0068 -0.0618 -0.0633 231 TRP A C 1760 O O . TRP A 231 ? 0.2898 0.2351 0.4076 -0.0068 -0.0588 -0.0693 231 TRP A O 1761 C CB . TRP A 231 ? 0.2671 0.2004 0.3697 -0.0122 -0.0722 -0.0422 231 TRP A CB 1762 C CG . TRP A 231 ? 0.3115 0.2558 0.4025 -0.0186 -0.0668 -0.0371 231 TRP A CG 1763 C CD1 . TRP A 231 ? 0.3029 0.2517 0.3852 -0.0198 -0.0692 -0.0274 231 TRP A CD1 1764 C CD2 . TRP A 231 ? 0.2482 0.1996 0.3346 -0.0232 -0.0586 -0.0421 231 TRP A CD2 1765 N NE1 . TRP A 231 ? 0.2841 0.2428 0.3578 -0.0240 -0.0625 -0.0272 231 TRP A NE1 1766 C CE2 . TRP A 231 ? 0.2635 0.2231 0.3401 -0.0261 -0.0566 -0.0356 231 TRP A CE2 1767 C CE3 . TRP A 231 ? 0.2636 0.2146 0.3515 -0.0248 -0.0529 -0.0510 231 TRP A CE3 1768 C CZ2 . TRP A 231 ? 0.2662 0.2323 0.3368 -0.0294 -0.0502 -0.0382 231 TRP A CZ2 1769 C CZ3 . TRP A 231 ? 0.2608 0.2179 0.3408 -0.0294 -0.0469 -0.0520 231 TRP A CZ3 1770 C CH2 . TRP A 231 ? 0.2281 0.1921 0.3007 -0.0312 -0.0460 -0.0457 231 TRP A CH2 1771 N N . ALA A 232 ? 0.3318 0.2965 0.4104 -0.0380 -0.0502 -0.0656 232 ALA A N 1772 C CA . ALA A 232 ? 0.3118 0.2893 0.4011 -0.0533 -0.0446 -0.0726 232 ALA A CA 1773 C C . ALA A 232 ? 0.3341 0.3491 0.4410 -0.0551 -0.0473 -0.0841 232 ALA A C 1774 O O . ALA A 232 ? 0.3184 0.3336 0.4302 -0.0633 -0.0412 -0.0884 232 ALA A O 1775 C CB . ALA A 232 ? 0.3747 0.3433 0.4464 -0.0695 -0.0400 -0.0719 232 ALA A CB 1776 N N . VAL A 233 ? 0.3063 0.3552 0.4217 -0.0477 -0.0562 -0.0902 233 VAL A N 1777 C CA . VAL A 233 ? 0.3539 0.4464 0.4911 -0.0503 -0.0559 -0.1039 233 VAL A CA 1778 C C . VAL A 233 ? 0.4049 0.5192 0.5596 -0.0235 -0.0649 -0.1074 233 VAL A C 1779 O O . VAL A 233 ? 0.3346 0.4523 0.4839 -0.0067 -0.0768 -0.1032 233 VAL A O 1780 C CB . VAL A 233 ? 0.3270 0.4565 0.4662 -0.0701 -0.0570 -0.1143 233 VAL A CB 1781 C CG1 . VAL A 233 ? 0.2933 0.4738 0.4591 -0.0753 -0.0532 -0.1308 233 VAL A CG1 1782 C CG2 . VAL A 233 ? 0.3044 0.4016 0.4183 -0.0951 -0.0466 -0.1107 233 VAL A CG2 1783 N N . THR A 234 ? 0.2989 0.4234 0.4694 -0.0177 -0.0591 -0.1150 234 THR A N 1784 C CA . THR A 234 ? 0.4094 0.5512 0.5957 0.0106 -0.0651 -0.1203 234 THR A CA 1785 C C . THR A 234 ? 0.3749 0.5863 0.5911 0.0116 -0.0680 -0.1376 234 THR A C 1786 O O . THR A 234 ? 0.3878 0.6252 0.6138 -0.0128 -0.0568 -0.1483 234 THR A O 1787 C CB . THR A 234 ? 0.4249 0.5405 0.6116 0.0160 -0.0554 -0.1223 234 THR A CB 1788 O OG1 . THR A 234 ? 0.4813 0.5423 0.6465 0.0093 -0.0517 -0.1100 234 THR A OG1 1789 C CG2 . THR A 234 ? 0.5003 0.6203 0.6963 0.0485 -0.0601 -0.1269 234 THR A CG2 1790 N N . SER A 235 ? 0.3957 0.6376 0.6251 0.0393 -0.0825 -0.1409 235 SER A N 1791 C CA . SER A 235 ? 0.4155 0.7365 0.6823 0.0430 -0.0868 -0.1606 235 SER A CA 1792 C C . SER A 235 ? 0.3264 0.6713 0.6182 0.0516 -0.0739 -0.1749 235 SER A C 1793 O O . SER A 235 ? 0.3595 0.6575 0.6374 0.0651 -0.0675 -0.1688 235 SER A O 1794 C CB . SER A 235 ? 0.4697 0.8194 0.7435 0.0768 -0.1100 -0.1603 235 SER A CB 1795 O OG . SER A 235 ? 0.5048 0.8272 0.7737 0.1166 -0.1145 -0.1552 235 SER A OG 1796 N N . LEU A 236 ? 0.3097 0.7280 0.6375 0.0414 -0.0685 -0.1957 236 LEU A N 1797 C CA . LEU A 236 ? 0.4307 0.8773 0.7830 0.0487 -0.0532 -0.2120 236 LEU A CA 1798 C C . LEU A 236 ? 0.4145 0.8545 0.7746 0.0976 -0.0625 -0.2118 236 LEU A C 1799 O O . LEU A 236 ? 0.3984 0.8107 0.7532 0.1075 -0.0497 -0.2149 236 LEU A O 1800 C CB . LEU A 236 ? 0.4252 0.9605 0.8190 0.0285 -0.0442 -0.2367 236 LEU A CB 1801 C CG . LEU A 236 ? 0.4546 0.9839 0.8387 -0.0148 -0.0171 -0.2446 236 LEU A CG 1802 C CD1 . LEU A 236 ? 0.3608 0.8055 0.6935 -0.0378 -0.0132 -0.2233 236 LEU A CD1 1803 C CD2 . LEU A 236 ? 0.4882 1.0919 0.9013 -0.0480 -0.0090 -0.2650 236 LEU A CD2 1804 N N . TYR A 237 ? 0.4605 0.9202 0.8273 0.1284 -0.0853 -0.2082 237 TYR A N 1805 C CA . TYR A 237 ? 0.5994 1.0396 0.9626 0.1796 -0.0971 -0.2044 237 TYR A CA 1806 C C . TYR A 237 ? 0.5796 0.9171 0.8948 0.1860 -0.0909 -0.1847 237 TYR A C 1807 O O . TYR A 237 ? 0.4978 0.8071 0.8088 0.2072 -0.0818 -0.1887 237 TYR A O 1808 C CB . TYR A 237 ? 0.7621 1.2325 1.1286 0.2089 -0.1257 -0.2004 237 TYR A CB 1809 C CG . TYR A 237 ? 0.9839 1.4075 1.3257 0.2632 -0.1409 -0.1886 237 TYR A CG 1810 C CD1 . TYR A 237 ? 1.0776 1.5302 1.4447 0.3059 -0.1416 -0.2024 237 TYR A CD1 1811 C CD2 . TYR A 237 ? 1.1007 1.4474 1.3899 0.2725 -0.1528 -0.1641 237 TYR A CD2 1812 C CE1 . TYR A 237 ? 1.1769 1.5755 1.5131 0.3582 -0.1549 -0.1907 237 TYR A CE1 1813 C CE2 . TYR A 237 ? 1.2016 1.4938 1.4580 0.3208 -0.1646 -0.1521 237 TYR A CE2 1814 C CZ . TYR A 237 ? 1.2371 1.5523 1.5152 0.3644 -0.1663 -0.1648 237 TYR A CZ 1815 O OH . TYR A 237 ? 1.3354 1.5845 1.5717 0.4126 -0.1764 -0.1513 237 TYR A OH 1816 N N . GLU A 238 ? 0.3967 0.6800 0.6767 0.1658 -0.0943 -0.1656 238 GLU A N 1817 C CA . GLU A 238 ? 0.5226 0.7163 0.7618 0.1659 -0.0871 -0.1493 238 GLU A CA 1818 C C . GLU A 238 ? 0.5005 0.6758 0.7412 0.1449 -0.0665 -0.1572 238 GLU A C 1819 O O . GLU A 238 ? 0.4652 0.5905 0.6885 0.1591 -0.0596 -0.1560 238 GLU A O 1820 C CB . GLU A 238 ? 0.6244 0.7767 0.8336 0.1422 -0.0905 -0.1312 238 GLU A CB 1821 C CG . GLU A 238 ? 0.7578 0.9050 0.9485 0.1629 -0.1101 -0.1197 238 GLU A CG 1822 C CD . GLU A 238 ? 0.8083 0.9308 0.9755 0.1335 -0.1103 -0.1069 238 GLU A CD 1823 O OE1 . GLU A 238 ? 0.7100 0.8524 0.8896 0.0989 -0.1005 -0.1121 238 GLU A OE1 1824 O OE2 . GLU A 238 ? 0.8775 0.9564 1.0097 0.1460 -0.1188 -0.0916 238 GLU A OE2 1825 N N . ALA A 239 ? 0.4912 0.7021 0.7472 0.1105 -0.0566 -0.1654 239 ALA A N 1826 C CA . ALA A 239 ? 0.4511 0.6422 0.7005 0.0890 -0.0390 -0.1716 239 ALA A CA 1827 C C . ALA A 239 ? 0.4545 0.6579 0.7172 0.1105 -0.0292 -0.1879 239 ALA A C 1828 O O . ALA A 239 ? 0.4680 0.6249 0.7109 0.1089 -0.0197 -0.1888 239 ALA A O 1829 C CB . ALA A 239 ? 0.3427 0.5664 0.5988 0.0514 -0.0302 -0.1770 239 ALA A CB 1830 N N . ARG A 240 ? 0.3812 0.6502 0.6784 0.1304 -0.0313 -0.2027 240 ARG A N 1831 C CA . ARG A 240 ? 0.4051 0.6902 0.7179 0.1567 -0.0210 -0.2200 240 ARG A CA 1832 C C . ARG A 240 ? 0.4494 0.6683 0.7362 0.1936 -0.0263 -0.2121 240 ARG A C 1833 O O . ARG A 240 ? 0.5790 0.7585 0.8497 0.1968 -0.0128 -0.2188 240 ARG A O 1834 C CB . ARG A 240 ? 0.4477 0.8257 0.8096 0.1748 -0.0238 -0.2390 240 ARG A CB 1835 C CG . ARG A 240 ? 0.5309 0.9301 0.9126 0.2062 -0.0114 -0.2589 240 ARG A CG 1836 C CD . ARG A 240 ? 0.5916 1.0972 1.0312 0.2215 -0.0122 -0.2815 240 ARG A CD 1837 N NE . ARG A 240 ? 0.6219 1.1518 1.0822 0.2480 0.0045 -0.3029 240 ARG A NE 1838 C CZ . ARG A 240 ? 0.6272 1.1717 1.0921 0.2221 0.0322 -0.3197 240 ARG A CZ 1839 N NH1 . ARG A 240 ? 0.5691 1.1010 1.0149 0.1701 0.0444 -0.3153 240 ARG A NH1 1840 N NH2 . ARG A 240 ? 0.6859 1.2376 1.1559 0.2425 0.0462 -0.3320 240 ARG A NH2 1841 N N . ASN A 241 ? 0.5708 0.7721 0.8475 0.2202 -0.0450 -0.1984 241 ASN A N 1842 C CA . ASN A 241 ? 0.6694 0.7953 0.9112 0.2542 -0.0490 -0.1885 241 ASN A CA 1843 C C . ASN A 241 ? 0.6381 0.6807 0.8401 0.2280 -0.0372 -0.1791 241 ASN A C 1844 O O . ASN A 241 ? 0.6399 0.6234 0.8167 0.2445 -0.0292 -0.1813 241 ASN A O 1845 C CB . ASN A 241 ? 0.7886 0.9017 1.0151 0.2806 -0.0711 -0.1717 241 ASN A CB 1846 C CG . ASN A 241 ? 0.9526 1.0088 1.1500 0.3319 -0.0770 -0.1669 241 ASN A CG 1847 O OD1 . ASN A 241 ? 0.8648 0.9518 1.0834 0.3682 -0.0762 -0.1823 241 ASN A OD1 1848 N ND2 . ASN A 241 ? 1.2176 1.1889 1.3640 0.3357 -0.0815 -0.1457 241 ASN A ND2 1849 N N . ARG A 242 ? 0.5266 0.5664 0.7238 0.1873 -0.0360 -0.1705 242 ARG A N 1850 C CA . ARG A 242 ? 0.5155 0.4898 0.6824 0.1610 -0.0274 -0.1633 242 ARG A CA 1851 C C . ARG A 242 ? 0.5291 0.5020 0.6969 0.1442 -0.0123 -0.1792 242 ARG A C 1852 O O . ARG A 242 ? 0.5270 0.4421 0.6693 0.1406 -0.0050 -0.1811 242 ARG A O 1853 C CB . ARG A 242 ? 0.5261 0.4997 0.6885 0.1292 -0.0327 -0.1492 242 ARG A CB 1854 C CG . ARG A 242 ? 0.5587 0.5158 0.7076 0.1437 -0.0455 -0.1327 242 ARG A CG 1855 C CD . ARG A 242 ? 0.5671 0.5357 0.7161 0.1149 -0.0494 -0.1220 242 ARG A CD 1856 N NE . ARG A 242 ? 0.4583 0.4233 0.5950 0.1302 -0.0623 -0.1093 242 ARG A NE 1857 C CZ . ARG A 242 ? 0.5280 0.4882 0.6551 0.1110 -0.0655 -0.0981 242 ARG A CZ 1858 N NH1 . ARG A 242 ? 0.4214 0.3806 0.5524 0.0786 -0.0571 -0.0977 242 ARG A NH1 1859 N NH2 . ARG A 242 ? 0.5007 0.4553 0.6110 0.1264 -0.0775 -0.0875 242 ARG A NH2 1860 N N . THR A 243 ? 0.5367 0.5710 0.7301 0.1320 -0.0068 -0.1915 243 THR A N 1861 C CA . THR A 243 ? 0.5410 0.5773 0.7309 0.1190 0.0085 -0.2077 243 THR A CA 1862 C C . THR A 243 ? 0.5824 0.5958 0.7664 0.1508 0.0171 -0.2213 243 THR A C 1863 O O . THR A 243 ? 0.6224 0.5903 0.7817 0.1435 0.0266 -0.2287 243 THR A O 1864 C CB . THR A 243 ? 0.4994 0.6049 0.7144 0.1017 0.0162 -0.2188 243 THR A CB 1865 O OG1 . THR A 243 ? 0.4619 0.5691 0.6691 0.0682 0.0120 -0.2075 243 THR A OG1 1866 C CG2 . THR A 243 ? 0.4979 0.6065 0.7062 0.0956 0.0345 -0.2377 243 THR A CG2 1867 N N . LEU A 244 ? 0.5618 0.6063 0.7672 0.1877 0.0127 -0.2255 244 LEU A N 1868 C CA . LEU A 244 ? 0.6496 0.6717 0.8494 0.2252 0.0206 -0.2385 244 LEU A CA 1869 C C . LEU A 244 ? 0.6722 0.5992 0.8280 0.2374 0.0186 -0.2278 244 LEU A C 1870 O O . LEU A 244 ? 0.6845 0.5636 0.8173 0.2485 0.0309 -0.2392 244 LEU A O 1871 C CB . LEU A 244 ? 0.7097 0.7935 0.9457 0.2666 0.0128 -0.2451 244 LEU A CB 1872 C CG . LEU A 244 ? 0.6505 0.8337 0.9345 0.2547 0.0199 -0.2622 244 LEU A CG 1873 C CD1 . LEU A 244 ? 0.6312 0.8836 0.9570 0.2978 0.0092 -0.2712 244 LEU A CD1 1874 C CD2 . LEU A 244 ? 0.6583 0.8440 0.9392 0.2404 0.0444 -0.2826 244 LEU A CD2 1875 N N . ASN A 245 ? 0.6576 0.5545 0.7984 0.2334 0.0052 -0.2070 245 ASN A N 1876 C CA . ASN A 245 ? 0.7225 0.5257 0.8181 0.2366 0.0064 -0.1959 245 ASN A CA 1877 C C . ASN A 245 ? 0.7078 0.4681 0.7820 0.1976 0.0182 -0.2019 245 ASN A C 1878 O O . ASN A 245 ? 0.7883 0.4793 0.8294 0.2022 0.0280 -0.2079 245 ASN A O 1879 C CB . ASN A 245 ? 0.7252 0.5095 0.8084 0.2353 -0.0075 -0.1730 245 ASN A CB 1880 C CG . ASN A 245 ? 0.7774 0.5706 0.8606 0.2835 -0.0210 -0.1660 245 ASN A CG 1881 O OD1 . ASN A 245 ? 0.8258 0.6418 0.9225 0.3208 -0.0204 -0.1789 245 ASN A OD1 1882 N ND2 . ASN A 245 ? 0.7346 0.5121 0.8020 0.2845 -0.0338 -0.1464 245 ASN A ND2 1883 N N . LEU A 246 ? 0.6316 0.4321 0.7226 0.1603 0.0164 -0.2013 246 LEU A N 1884 C CA . LEU A 246 ? 0.7492 0.5243 0.8246 0.1253 0.0233 -0.2090 246 LEU A CA 1885 C C . LEU A 246 ? 0.7983 0.5620 0.8627 0.1321 0.0370 -0.2309 246 LEU A C 1886 O O . LEU A 246 ? 0.7824 0.4893 0.8174 0.1199 0.0438 -0.2391 246 LEU A O 1887 C CB . LEU A 246 ? 0.6521 0.4775 0.7461 0.0929 0.0174 -0.2049 246 LEU A CB 1888 C CG . LEU A 246 ? 0.6736 0.4764 0.7510 0.0595 0.0191 -0.2110 246 LEU A CG 1889 C CD1 . LEU A 246 ? 0.5959 0.3406 0.6545 0.0483 0.0175 -0.2041 246 LEU A CD1 1890 C CD2 . LEU A 246 ? 0.5182 0.3666 0.6088 0.0344 0.0122 -0.2058 246 LEU A CD2 1891 N N . ALA A 247 ? 0.6523 0.4712 0.7401 0.1496 0.0423 -0.2423 247 ALA A N 1892 C CA . ALA A 247 ? 0.6877 0.5010 0.7662 0.1592 0.0582 -0.2646 247 ALA A CA 1893 C C . ALA A 247 ? 0.8716 0.6135 0.9210 0.1888 0.0653 -0.2705 247 ALA A C 1894 O O . ALA A 247 ? 0.9286 0.6250 0.9490 0.1816 0.0773 -0.2860 247 ALA A O 1895 C CB . ALA A 247 ? 0.7382 0.6285 0.8527 0.1764 0.0648 -0.2758 247 ALA A CB 1896 N N . LYS A 248 ? 0.7809 0.5083 0.8327 0.2228 0.0577 -0.2585 248 LYS A N 1897 C CA . LYS A 248 ? 0.8966 0.5463 0.9134 0.2559 0.0646 -0.2618 248 LYS A CA 1898 C C . LYS A 248 ? 0.9013 0.4637 0.8727 0.2244 0.0696 -0.2569 248 LYS A C 1899 O O . LYS A 248 ? 0.9570 0.4687 0.8998 0.2187 0.0854 -0.2670 248 LYS A O 1900 C CB . LYS A 248 ? 0.8867 0.5395 0.9088 0.2950 0.0534 -0.2425 248 LYS A CB 1901 C CG . LYS A 248 ? 0.9671 0.5510 0.9559 0.3213 0.0629 -0.2354 248 LYS A CG 1902 C CD . LYS A 248 ? 1.1125 0.7095 1.1079 0.3619 0.0483 -0.2172 248 LYS A CD 1903 C CE . LYS A 248 ? 1.1422 0.6902 1.1149 0.3949 0.0564 -0.2168 248 LYS A CE 1904 N NZ . LYS A 248 ? 1.2049 0.6550 1.1296 0.3702 0.0685 -0.2156 248 LYS A NZ 1905 N N . LEU A 249 ? 0.8902 0.4471 0.8620 0.1969 0.0587 -0.2406 249 LEU A N 1906 C CA . LEU A 249 ? 0.9027 0.3869 0.8394 0.1640 0.0632 -0.2381 249 LEU A CA 1907 C C . LEU A 249 ? 0.9958 0.4769 0.9211 0.1283 0.0686 -0.2556 249 LEU A C 1908 O O . LEU A 249 ? 0.9570 0.3924 0.8566 0.1064 0.0679 -0.2566 249 LEU A O 1909 C CB . LEU A 249 ? 0.8561 0.3574 0.8056 0.1387 0.0517 -0.2177 249 LEU A CB 1910 C CG . LEU A 249 ? 0.8673 0.3588 0.8131 0.1688 0.0437 -0.1966 249 LEU A CG 1911 C CD1 . LEU A 249 ? 0.8413 0.3648 0.8047 0.1425 0.0334 -0.1793 249 LEU A CD1 1912 C CD2 . LEU A 249 ? 0.9486 0.3624 0.8563 0.1786 0.0524 -0.1876 249 LEU A CD2 1913 N N . THR A 250 ? 0.8569 0.4020 0.8097 0.1206 0.0690 -0.2682 250 THR A N 1914 C CA . THR A 250 ? 0.9397 0.4863 0.8772 0.0882 0.0716 -0.2831 250 THR A CA 1915 C C . THR A 250 ? 0.9894 0.5277 0.9078 0.1072 0.0847 -0.3016 250 THR A C 1916 O O . THR A 250 ? 1.0277 0.5677 0.9286 0.0845 0.0863 -0.3144 250 THR A O 1917 C CB . THR A 250 ? 0.8689 0.4853 0.8362 0.0621 0.0613 -0.2814 250 THR A CB 1918 O OG1 . THR A 250 ? 0.7485 0.4282 0.7449 0.0840 0.0619 -0.2783 250 THR A OG1 1919 C CG2 . THR A 250 ? 0.7846 0.4081 0.7656 0.0406 0.0478 -0.2624 250 THR A CG2 1920 N N . GLY A 251 ? 1.0145 0.5454 0.9349 0.1507 0.0931 -0.3024 251 GLY A N 1921 C CA . GLY A 251 ? 1.0480 0.5734 0.9522 0.1738 0.1076 -0.3196 251 GLY A CA 1922 C C . GLY A 251 ? 1.0091 0.6132 0.9461 0.1708 0.1150 -0.3333 251 GLY A C 1923 O O . GLY A 251 ? 1.0129 0.6144 0.9302 0.1706 0.1278 -0.3498 251 GLY A O 1924 N N . CYS A 252 ? 0.8639 0.5365 0.8473 0.1686 0.1058 -0.3274 252 CYS A N 1925 C CA . CYS A 252 ? 0.8495 0.5985 0.8586 0.1584 0.1113 -0.3354 252 CYS A CA 1926 C C . CYS A 252 ? 0.8676 0.6852 0.9217 0.1927 0.1146 -0.3360 252 CYS A C 1927 O O . CYS A 252 ? 0.7565 0.6440 0.8374 0.1808 0.1193 -0.3400 252 CYS A O 1928 C CB . CYS A 252 ? 0.7601 0.5394 0.7761 0.1185 0.0969 -0.3205 252 CYS A CB 1929 S SG . CYS A 252 ? 0.7810 0.5135 0.7526 0.0761 0.0934 -0.3280 252 CYS A SG 1930 N N . SER A 253 ? 0.9044 0.7020 0.9647 0.2343 0.1116 -0.3318 253 SER A N 1931 C CA . SER A 253 ? 0.9219 0.7894 1.0255 0.2701 0.1120 -0.3319 253 SER A CA 1932 C C . SER A 253 ? 0.8944 0.8045 1.0083 0.2758 0.1343 -0.3523 253 SER A C 1933 O O . SER A 253 ? 0.9638 0.8242 1.0449 0.2877 0.1494 -0.3606 253 SER A O 1934 C CB . SER A 253 ? 0.9605 0.7870 1.0543 0.3122 0.1045 -0.3161 253 SER A CB 1935 O OG . SER A 253 ? 0.9445 0.7365 1.0279 0.3058 0.0853 -0.2958 253 SER A OG 1936 N N . ARG A 254 ? 0.8912 0.8897 1.0471 0.2637 0.1387 -0.3606 254 ARG A N 1937 C CA . ARG A 254 ? 0.9263 0.9738 1.0957 0.2654 0.1621 -0.3792 254 ARG A CA 1938 C C . ARG A 254 ? 0.9178 1.0652 1.1490 0.2810 0.1596 -0.3802 254 ARG A C 1939 O O . ARG A 254 ? 0.8740 1.0457 1.1313 0.2931 0.1383 -0.3663 254 ARG A O 1940 C CB . ARG A 254 ? 0.9041 0.9543 1.0508 0.2187 0.1761 -0.3908 254 ARG A CB 1941 C CG . ARG A 254 ? 0.9208 0.8820 1.0078 0.1952 0.1733 -0.3896 254 ARG A CG 1942 C CD . ARG A 254 ? 0.9874 0.8919 1.0339 0.2118 0.1888 -0.4005 254 ARG A CD 1943 N NE . ARG A 254 ? 1.0209 0.8503 1.0108 0.1825 0.1845 -0.4008 254 ARG A NE 1944 C CZ . ARG A 254 ? 1.0098 0.7682 0.9720 0.1834 0.1704 -0.3906 254 ARG A CZ 1945 N NH1 . ARG A 254 ? 0.9953 0.7382 0.9741 0.2138 0.1614 -0.3780 254 ARG A NH1 1946 N NH2 . ARG A 254 ? 0.9680 0.6715 0.8838 0.1526 0.1647 -0.3921 254 ARG A NH2 1947 N N . GLU A 255 ? 0.9425 1.1475 1.1950 0.2784 0.1811 -0.3969 255 GLU A N 1948 C CA . GLU A 255 ? 0.9468 1.2532 1.2601 0.2856 0.1805 -0.4010 255 GLU A CA 1949 C C . GLU A 255 ? 0.8867 1.2529 1.2165 0.2367 0.1919 -0.4089 255 GLU A C 1950 O O . GLU A 255 ? 0.8465 1.2841 1.2198 0.2282 0.1827 -0.4065 255 GLU A O 1951 C CB . GLU A 255 ? 1.1028 1.4392 1.4369 0.3205 0.1963 -0.4137 255 GLU A CB 1952 C CG . GLU A 255 ? 1.2291 1.5614 1.5420 0.3026 0.2289 -0.4332 255 GLU A CG 1953 C CD . GLU A 255 ? 1.3008 1.5333 1.5442 0.2875 0.2359 -0.4332 255 GLU A CD 1954 O OE1 . GLU A 255 ? 1.3807 1.5403 1.5924 0.3174 0.2324 -0.4287 255 GLU A OE1 1955 O OE2 . GLU A 255 ? 1.2469 1.4704 1.4640 0.2438 0.2441 -0.4370 255 GLU A OE2 1956 N N . ASN A 256 ? 0.8866 1.2182 1.1754 0.2031 0.2118 -0.4175 256 ASN A N 1957 C CA . ASN A 256 ? 0.8913 1.2527 1.1761 0.1534 0.2223 -0.4199 256 ASN A CA 1958 C C . ASN A 256 ? 0.8174 1.1368 1.0814 0.1357 0.2016 -0.4045 256 ASN A C 1959 O O . ASN A 256 ? 0.7795 1.0200 0.9957 0.1320 0.1946 -0.3978 256 ASN A O 1960 C CB . ASN A 256 ? 1.0710 1.4018 1.3090 0.1262 0.2499 -0.4322 256 ASN A CB 1961 C CG . ASN A 256 ? 1.2385 1.6021 1.4685 0.0764 0.2661 -0.4344 256 ASN A CG 1962 O OD1 . ASN A 256 ? 1.1998 1.5636 1.4264 0.0517 0.2549 -0.4234 256 ASN A OD1 1963 N ND2 . ASN A 256 ? 1.4786 1.8639 1.7006 0.0614 0.2942 -0.4481 256 ASN A ND2 1964 N N . GLU A 257 ? 0.7117 1.0806 1.0091 0.1231 0.1892 -0.3956 257 GLU A N 1965 C CA . GLU A 257 ? 0.6609 0.9827 0.9337 0.1050 0.1626 -0.3670 257 GLU A CA 1966 C C . GLU A 257 ? 0.6463 0.9076 0.8598 0.0655 0.1671 -0.3583 257 GLU A C 1967 O O . GLU A 257 ? 0.6309 0.8311 0.8127 0.0596 0.1475 -0.3395 257 GLU A O 1968 C CB . GLU A 257 ? 0.6688 1.0521 0.9802 0.0918 0.1510 -0.3583 257 GLU A CB 1969 C CG . GLU A 257 ? 0.7020 1.1393 1.0671 0.1334 0.1354 -0.3614 257 GLU A CG 1970 C CD . GLU A 257 ? 0.6095 1.1004 1.0053 0.1168 0.1205 -0.3524 257 GLU A CD 1971 O OE1 . GLU A 257 ? 0.5102 1.0110 0.8944 0.0721 0.1303 -0.3502 257 GLU A OE1 1972 O OE2 . GLU A 257 ? 0.6283 1.1459 1.0544 0.1487 0.0988 -0.3474 257 GLU A OE2 1973 N N . THR A 258 ? 0.6633 0.9427 0.8608 0.0392 0.1932 -0.3728 258 THR A N 1974 C CA . THR A 258 ? 0.7464 0.9670 0.8803 0.0055 0.1971 -0.3658 258 THR A CA 1975 C C . THR A 258 ? 0.7404 0.8925 0.8341 0.0200 0.1930 -0.3695 258 THR A C 1976 O O . THR A 258 ? 0.6594 0.7540 0.7069 0.0022 0.1792 -0.3569 258 THR A O 1977 C CB . THR A 258 ? 0.8468 1.0952 0.9636 -0.0254 0.2290 -0.3809 258 THR A CB 1978 O OG1 . THR A 258 ? 0.8430 1.1625 1.0054 -0.0383 0.2361 -0.3831 258 THR A OG1 1979 C CG2 . THR A 258 ? 0.9087 1.0943 0.9543 -0.0600 0.2269 -0.3676 258 THR A CG2 1980 N N . GLU A 259 ? 0.7114 0.8705 0.8235 0.0531 0.2042 -0.3879 259 GLU A N 1981 C CA . GLU A 259 ? 0.7207 0.8107 0.7951 0.0678 0.2016 -0.3938 259 GLU A CA 1982 C C . GLU A 259 ? 0.7060 0.7468 0.7763 0.0785 0.1719 -0.3738 259 GLU A C 1983 O O . GLU A 259 ? 0.7334 0.7099 0.7611 0.0697 0.1639 -0.3722 259 GLU A O 1984 C CB . GLU A 259 ? 0.7610 0.8643 0.8530 0.1035 0.2205 -0.4146 259 GLU A CB 1985 C CG . GLU A 259 ? 1.0184 1.1369 1.0896 0.0899 0.2487 -0.4292 259 GLU A CG 1986 C CD . GLU A 259 ? 1.1067 1.2237 1.1868 0.1272 0.2620 -0.4414 259 GLU A CD 1987 O OE1 . GLU A 259 ? 1.1540 1.2228 1.2266 0.1568 0.2491 -0.4375 259 GLU A OE1 1988 O OE2 . GLU A 259 ? 1.1537 1.3135 1.2453 0.1266 0.2862 -0.4543 259 GLU A OE2 1989 N N . ILE A 260 ? 0.6680 0.7397 0.7811 0.0961 0.1567 -0.3605 260 ILE A N 1990 C CA . ILE A 260 ? 0.6971 0.7247 0.8042 0.0997 0.1309 -0.3393 260 ILE A CA 1991 C C . ILE A 260 ? 0.7248 0.7222 0.7983 0.0612 0.1182 -0.3246 260 ILE A C 1992 O O . ILE A 260 ? 0.6529 0.5936 0.6970 0.0544 0.1069 -0.3198 260 ILE A O 1993 C CB . ILE A 260 ? 0.6460 0.7168 0.7986 0.1181 0.1162 -0.3254 260 ILE A CB 1994 C CG1 . ILE A 260 ? 0.7082 0.8082 0.8939 0.1638 0.1228 -0.3390 260 ILE A CG1 1995 C CG2 . ILE A 260 ? 0.6002 0.6226 0.7399 0.1154 0.0929 -0.3028 260 ILE A CG2 1996 C CD1 . ILE A 260 ? 0.6939 0.8416 0.9223 0.1848 0.1057 -0.3273 260 ILE A CD1 1997 N N . ILE A 261 ? 0.7415 0.7773 0.8190 0.0364 0.1207 -0.3190 261 ILE A N 1998 C CA . ILE A 261 ? 0.7189 0.7292 0.7643 0.0050 0.1080 -0.3043 261 ILE A CA 1999 C C . ILE A 261 ? 0.6386 0.5999 0.6324 -0.0090 0.1104 -0.3137 261 ILE A C 2000 O O . ILE A 261 ? 0.6390 0.5636 0.6096 -0.0214 0.0919 -0.3040 261 ILE A O 2001 C CB . ILE A 261 ? 0.6719 0.7220 0.7195 -0.0187 0.1157 -0.2993 261 ILE A CB 2002 C CG1 . ILE A 261 ? 0.5432 0.6461 0.6414 -0.0090 0.1120 -0.2925 261 ILE A CG1 2003 C CG2 . ILE A 261 ? 0.5705 0.5865 0.5800 -0.0444 0.1006 -0.2830 261 ILE A CG2 2004 C CD1 . ILE A 261 ? 0.5039 0.5883 0.6163 0.0015 0.0872 -0.2734 261 ILE A CD1 2005 N N . LYS A 262 ? 0.6780 0.6425 0.6545 -0.0070 0.1332 -0.3343 262 LYS A N 2006 C CA . LYS A 262 ? 0.7284 0.6454 0.6507 -0.0195 0.1362 -0.3461 262 LYS A CA 2007 C C . LYS A 262 ? 0.7850 0.6522 0.6987 -0.0090 0.1217 -0.3483 262 LYS A C 2008 O O . LYS A 262 ? 0.7877 0.6180 0.6667 -0.0268 0.1062 -0.3464 262 LYS A O 2009 C CB . LYS A 262 ? 0.7726 0.7009 0.6793 -0.0158 0.1671 -0.3701 262 LYS A CB 2010 C CG . LYS A 262 ? 1.0639 0.9597 0.9044 -0.0419 0.1738 -0.3775 262 LYS A CG 2011 C CD . LYS A 262 ? 1.0941 0.9906 0.9155 -0.0353 0.2028 -0.3982 262 LYS A CD 2012 C CE . LYS A 262 ? 1.1535 1.0246 0.9087 -0.0614 0.2089 -0.3968 262 LYS A CE 2013 N NZ . LYS A 262 ? 1.1318 1.0341 0.8821 -0.0833 0.2231 -0.3897 262 LYS A NZ 2014 N N . CYS A 263 ? 0.7780 0.6440 0.7221 0.0196 0.1263 -0.3529 263 CYS A N 2015 C CA . CYS A 263 ? 0.8232 0.6340 0.7561 0.0289 0.1168 -0.3550 263 CYS A CA 2016 C C . CYS A 263 ? 0.7443 0.5400 0.6814 0.0121 0.0913 -0.3349 263 CYS A C 2017 O O . CYS A 263 ? 0.7698 0.5219 0.6814 -0.0021 0.0812 -0.3388 263 CYS A O 2018 C CB . CYS A 263 ? 0.7891 0.5992 0.7509 0.0672 0.1261 -0.3594 263 CYS A CB 2019 S SG . CYS A 263 ? 0.8445 0.5726 0.7841 0.0799 0.1194 -0.3603 263 CYS A SG 2020 N N . LEU A 264 ? 0.6906 0.5254 0.6610 0.0126 0.0819 -0.3156 264 LEU A N 2021 C CA . LEU A 264 ? 0.6819 0.5083 0.6602 -0.0014 0.0604 -0.2968 264 LEU A CA 2022 C C . LEU A 264 ? 0.6888 0.5088 0.6384 -0.0301 0.0476 -0.2953 264 LEU A C 2023 O O . LEU A 264 ? 0.6929 0.4957 0.6415 -0.0426 0.0309 -0.2887 264 LEU A O 2024 C CB . LEU A 264 ? 0.6069 0.4752 0.6229 0.0062 0.0549 -0.2783 264 LEU A CB 2025 C CG . LEU A 264 ? 0.8389 0.7036 0.8807 0.0357 0.0567 -0.2745 264 LEU A CG 2026 C CD1 . LEU A 264 ? 0.5646 0.4820 0.6419 0.0447 0.0536 -0.2622 264 LEU A CD1 2027 C CD2 . LEU A 264 ? 0.6205 0.4358 0.6543 0.0335 0.0458 -0.2659 264 LEU A CD2 2028 N N . ARG A 265 ? 0.7133 0.5475 0.6382 -0.0395 0.0561 -0.3023 265 ARG A N 2029 C CA . ARG A 265 ? 0.6866 0.5105 0.5746 -0.0618 0.0429 -0.3011 265 ARG A CA 2030 C C . ARG A 265 ? 0.7590 0.5429 0.6130 -0.0712 0.0360 -0.3180 265 ARG A C 2031 O O . ARG A 265 ? 0.7965 0.5730 0.6262 -0.0875 0.0171 -0.3168 265 ARG A O 2032 C CB . ARG A 265 ? 0.7002 0.5412 0.5611 -0.0698 0.0566 -0.3029 265 ARG A CB 2033 C CG . ARG A 265 ? 0.7316 0.6087 0.6167 -0.0715 0.0587 -0.2854 265 ARG A CG 2034 C CD . ARG A 265 ? 0.8020 0.6773 0.6430 -0.0891 0.0649 -0.2826 265 ARG A CD 2035 N NE . ARG A 265 ? 0.8650 0.7745 0.7219 -0.0913 0.0879 -0.2827 265 ARG A NE 2036 C CZ . ARG A 265 ? 0.9128 0.8367 0.7655 -0.0902 0.1150 -0.3005 265 ARG A CZ 2037 N NH1 . ARG A 265 ? 0.9562 0.8565 0.7839 -0.0851 0.1229 -0.3187 265 ARG A NH1 2038 N NH2 . ARG A 265 ? 0.8609 0.8247 0.7352 -0.0955 0.1355 -0.3020 265 ARG A NH2 2039 N N . ASN A 266 ? 0.7687 0.5268 0.6200 -0.0598 0.0499 -0.3339 266 ASN A N 2040 C CA . ASN A 266 ? 0.8191 0.5401 0.6380 -0.0676 0.0420 -0.3416 266 ASN A CA 2041 C C . ASN A 266 ? 0.8160 0.5151 0.6533 -0.0706 0.0289 -0.3352 266 ASN A C 2042 O O . ASN A 266 ? 1.0115 0.6814 0.8270 -0.0799 0.0216 -0.3424 266 ASN A O 2043 C CB . ASN A 266 ? 1.1104 0.8097 0.9060 -0.0543 0.0643 -0.3589 266 ASN A CB 2044 C CG . ASN A 266 ? 1.1554 0.8674 0.9162 -0.0605 0.0752 -0.3665 266 ASN A CG 2045 O OD1 . ASN A 266 ? 1.2176 0.9311 0.9486 -0.0781 0.0597 -0.3620 266 ASN A OD1 2046 N ND2 . ASN A 266 ? 1.1542 0.8763 0.9180 -0.0446 0.1023 -0.3775 266 ASN A ND2 2047 N N . LYS A 267 ? 0.7705 0.4838 0.6466 -0.0643 0.0268 -0.3223 267 LYS A N 2048 C CA . LYS A 267 ? 0.7692 0.4617 0.6608 -0.0695 0.0176 -0.3139 267 LYS A CA 2049 C C . LYS A 267 ? 0.8201 0.5359 0.7205 -0.0907 -0.0055 -0.3036 267 LYS A C 2050 O O . LYS A 267 ? 0.7823 0.5325 0.6920 -0.0931 -0.0138 -0.2960 267 LYS A O 2051 C CB . LYS A 267 ? 0.7415 0.4340 0.6661 -0.0505 0.0266 -0.3041 267 LYS A CB 2052 C CG . LYS A 267 ? 0.7596 0.4453 0.6858 -0.0216 0.0474 -0.3136 267 LYS A CG 2053 C CD . LYS A 267 ? 0.9226 0.5637 0.8130 -0.0152 0.0583 -0.3280 267 LYS A CD 2054 C CE . LYS A 267 ? 0.9913 0.5789 0.8716 -0.0122 0.0575 -0.3233 267 LYS A CE 2055 N NZ . LYS A 267 ? 1.1260 0.6674 0.9719 -0.0008 0.0689 -0.3385 267 LYS A NZ 2056 N N . ASP A 268 ? 0.9149 0.6130 0.8126 -0.1054 -0.0153 -0.3045 268 ASP A N 2057 C CA . ASP A 268 ? 0.9604 0.6869 0.8744 -0.1228 -0.0361 -0.2964 268 ASP A CA 2058 C C . ASP A 268 ? 0.8140 0.5605 0.7664 -0.1178 -0.0351 -0.2790 268 ASP A C 2059 O O . ASP A 268 ? 0.7285 0.4536 0.6915 -0.1065 -0.0207 -0.2743 268 ASP A O 2060 C CB . ASP A 268 ? 1.0962 0.8045 1.0027 -0.1414 -0.0442 -0.3051 268 ASP A CB 2061 C CG . ASP A 268 ? 1.1986 0.9248 1.1387 -0.1544 -0.0516 -0.2947 268 ASP A CG 2062 O OD1 . ASP A 268 ? 1.1811 0.9475 1.1366 -0.1636 -0.0697 -0.2912 268 ASP A OD1 2063 O OD2 . ASP A 268 ? 1.3014 1.0000 1.2503 -0.1541 -0.0385 -0.2905 268 ASP A OD2 2064 N N . PRO A 269 ? 0.7496 0.5346 0.7194 -0.1235 -0.0508 -0.2697 269 PRO A N 2065 C CA . PRO A 269 ? 0.6978 0.5037 0.7020 -0.1181 -0.0504 -0.2534 269 PRO A CA 2066 C C . PRO A 269 ? 0.7084 0.4930 0.7296 -0.1219 -0.0409 -0.2476 269 PRO A C 2067 O O . PRO A 269 ? 0.6125 0.3947 0.6508 -0.1111 -0.0325 -0.2365 269 PRO A O 2068 C CB . PRO A 269 ? 0.7056 0.5498 0.7202 -0.1260 -0.0711 -0.2483 269 PRO A CB 2069 C CG . PRO A 269 ? 0.7711 0.6144 0.7528 -0.1339 -0.0841 -0.2621 269 PRO A CG 2070 C CD . PRO A 269 ? 0.7944 0.6020 0.7457 -0.1300 -0.0691 -0.2741 269 PRO A CD 2071 N N . GLN A 270 ? 0.6457 0.4119 0.6582 -0.1377 -0.0419 -0.2556 270 GLN A N 2072 C CA . GLN A 270 ? 0.7054 0.4448 0.7262 -0.1447 -0.0313 -0.2507 270 GLN A CA 2073 C C . GLN A 270 ? 0.7337 0.4236 0.7383 -0.1271 -0.0129 -0.2483 270 GLN A C 2074 O O . GLN A 270 ? 0.6882 0.3589 0.7001 -0.1241 -0.0041 -0.2371 270 GLN A O 2075 C CB . GLN A 270 ? 0.7711 0.5029 0.7862 -0.1681 -0.0362 -0.2625 270 GLN A CB 2076 C CG . GLN A 270 ? 0.8784 0.5915 0.9055 -0.1814 -0.0256 -0.2574 270 GLN A CG 2077 C CD . GLN A 270 ? 0.9953 0.7401 1.0540 -0.1797 -0.0253 -0.2417 270 GLN A CD 2078 O OE1 . GLN A 270 ? 1.0390 0.7564 1.0972 -0.1745 -0.0114 -0.2307 270 GLN A OE1 2079 N NE2 . GLN A 270 ? 0.9804 0.7803 1.0635 -0.1823 -0.0408 -0.2408 270 GLN A NE2 2080 N N . GLU A 271 ? 0.7136 0.3819 0.6945 -0.1132 -0.0067 -0.2587 271 GLU A N 2081 C CA . GLU A 271 ? 0.7416 0.3659 0.7088 -0.0901 0.0095 -0.2575 271 GLU A CA 2082 C C . GLU A 271 ? 0.7662 0.4117 0.7560 -0.0688 0.0127 -0.2463 271 GLU A C 2083 O O . GLU A 271 ? 0.7670 0.3826 0.7550 -0.0509 0.0218 -0.2383 271 GLU A O 2084 C CB . GLU A 271 ? 0.8241 0.4222 0.7621 -0.0781 0.0173 -0.2739 271 GLU A CB 2085 C CG . GLU A 271 ? 0.9442 0.4951 0.8675 -0.0489 0.0331 -0.2732 271 GLU A CG 2086 C CD . GLU A 271 ? 1.0674 0.5879 0.9608 -0.0362 0.0422 -0.2905 271 GLU A CD 2087 O OE1 . GLU A 271 ? 1.1165 0.6497 0.9975 -0.0529 0.0369 -0.3033 271 GLU A OE1 2088 O OE2 . GLU A 271 ? 1.0654 0.5493 0.9466 -0.0072 0.0539 -0.2911 271 GLU A OE2 2089 N N . ILE A 272 ? 0.7233 0.4187 0.7320 -0.0696 0.0037 -0.2460 272 ILE A N 2090 C CA . ILE A 272 ? 0.6224 0.3466 0.6558 -0.0531 0.0032 -0.2348 272 ILE A CA 2091 C C . ILE A 272 ? 0.6228 0.3474 0.6744 -0.0601 -0.0003 -0.2188 272 ILE A C 2092 O O . ILE A 272 ? 0.6409 0.3560 0.6961 -0.0422 0.0045 -0.2052 272 ILE A O 2093 C CB . ILE A 272 ? 0.6265 0.4008 0.6662 -0.0558 -0.0059 -0.2327 272 ILE A CB 2094 C CG1 . ILE A 272 ? 0.6631 0.4374 0.6829 -0.0462 0.0027 -0.2469 272 ILE A CG1 2095 C CG2 . ILE A 272 ? 0.6283 0.4368 0.6899 -0.0446 -0.0085 -0.2136 272 ILE A CG2 2096 C CD1 . ILE A 272 ? 0.7066 0.5077 0.7129 -0.0592 -0.0049 -0.2514 272 ILE A CD1 2097 N N . LEU A 273 ? 0.5699 0.3111 0.6282 -0.0832 -0.0091 -0.2160 273 LEU A N 2098 C CA . LEU A 273 ? 0.6093 0.3565 0.6847 -0.0918 -0.0099 -0.2018 273 LEU A CA 2099 C C . LEU A 273 ? 0.6536 0.3483 0.7124 -0.0900 0.0037 -0.1966 273 LEU A C 2100 O O . LEU A 273 ? 0.6403 0.3261 0.7051 -0.0850 0.0083 -0.1834 273 LEU A O 2101 C CB . LEU A 273 ? 0.5805 0.3585 0.6672 -0.1142 -0.0205 -0.2033 273 LEU A CB 2102 C CG . LEU A 273 ? 0.5766 0.4034 0.6781 -0.1135 -0.0358 -0.2020 273 LEU A CG 2103 C CD1 . LEU A 273 ? 0.5923 0.4456 0.7019 -0.1309 -0.0479 -0.2082 273 LEU A CD1 2104 C CD2 . LEU A 273 ? 0.4591 0.3055 0.5812 -0.1044 -0.0364 -0.1874 273 LEU A CD2 2105 N N . LEU A 274 ? 0.6492 0.3043 0.6814 -0.0935 0.0099 -0.2066 274 LEU A N 2106 C CA . LEU A 274 ? 0.7560 0.3527 0.7640 -0.0921 0.0220 -0.2015 274 LEU A CA 2107 C C . LEU A 274 ? 0.7852 0.3484 0.7808 -0.0604 0.0296 -0.1920 274 LEU A C 2108 O O . LEU A 274 ? 0.7973 0.3237 0.7786 -0.0564 0.0364 -0.1793 274 LEU A O 2109 C CB . LEU A 274 ? 0.8525 0.4128 0.8343 -0.1004 0.0257 -0.2156 274 LEU A CB 2110 C CG . LEU A 274 ? 0.9849 0.5321 0.9655 -0.1295 0.0292 -0.2167 274 LEU A CG 2111 C CD1 . LEU A 274 ? 1.0117 0.5874 0.9989 -0.1528 0.0196 -0.2335 274 LEU A CD1 2112 C CD2 . LEU A 274 ? 1.1123 0.5891 1.0602 -0.1239 0.0441 -0.2143 274 LEU A CD2 2113 N N . ASN A 275 ? 0.7890 0.3689 0.7914 -0.0368 0.0281 -0.1988 275 ASN A N 2114 C CA . ASN A 275 ? 0.8418 0.4000 0.8368 -0.0003 0.0327 -0.1920 275 ASN A CA 2115 C C . ASN A 275 ? 0.7666 0.3768 0.7859 0.0140 0.0222 -0.1740 275 ASN A C 2116 O O . ASN A 275 ? 0.8125 0.4175 0.8256 0.0454 0.0208 -0.1646 275 ASN A O 2117 C CB . ASN A 275 ? 0.7402 0.2948 0.7252 0.0235 0.0365 -0.2061 275 ASN A CB 2118 C CG . ASN A 275 ? 0.8160 0.3047 0.7612 0.0223 0.0457 -0.2146 275 ASN A CG 2119 O OD1 . ASN A 275 ? 0.9197 0.3608 0.8421 0.0478 0.0508 -0.2085 275 ASN A OD1 2120 N ND2 . ASN A 275 ? 0.8227 0.3165 0.7620 -0.0062 0.0435 -0.2264 275 ASN A ND2 2121 N N . GLU A 276 ? 0.6357 0.2943 0.6805 -0.0076 0.0139 -0.1703 276 GLU A N 2122 C CA . GLU A 276 ? 0.6387 0.3421 0.7029 0.0008 0.0052 -0.1550 276 GLU A CA 2123 C C . GLU A 276 ? 0.6113 0.2820 0.6608 0.0126 0.0077 -0.1381 276 GLU A C 2124 O O . GLU A 276 ? 0.6051 0.2975 0.6584 0.0345 0.0009 -0.1278 276 GLU A O 2125 C CB . GLU A 276 ? 0.6103 0.3570 0.6971 -0.0245 -0.0022 -0.1540 276 GLU A CB 2126 C CG . GLU A 276 ? 0.6544 0.4406 0.7505 -0.0304 -0.0084 -0.1652 276 GLU A CG 2127 C CD . GLU A 276 ? 0.7282 0.5503 0.8402 -0.0485 -0.0175 -0.1613 276 GLU A CD 2128 O OE1 . GLU A 276 ? 0.7677 0.5868 0.8888 -0.0590 -0.0178 -0.1538 276 GLU A OE1 2129 O OE2 . GLU A 276 ? 0.6717 0.5221 0.7841 -0.0510 -0.0232 -0.1661 276 GLU A OE2 2130 N N . ALA A 277 ? 0.6612 0.2797 0.6913 -0.0035 0.0178 -0.1362 277 ALA A N 2131 C CA . ALA A 277 ? 0.8276 0.4057 0.8345 0.0036 0.0230 -0.1195 277 ALA A CA 2132 C C . ALA A 277 ? 0.8934 0.4325 0.8696 0.0426 0.0218 -0.1117 277 ALA A C 2133 O O . ALA A 277 ? 0.9169 0.4393 0.8745 0.0582 0.0189 -0.0955 277 ALA A O 2134 C CB . ALA A 277 ? 0.8891 0.4153 0.8786 -0.0265 0.0388 -0.1218 277 ALA A CB 2135 N N . PHE A 278 ? 0.8514 0.3768 0.8206 0.0606 0.0232 -0.1238 278 PHE A N 2136 C CA . PHE A 278 ? 0.9090 0.3917 0.8475 0.1018 0.0226 -0.1184 278 PHE A CA 2137 C C . PHE A 278 ? 0.8622 0.4078 0.8268 0.1371 0.0084 -0.1205 278 PHE A C 2138 O O . PHE A 278 ? 0.8491 0.3699 0.7948 0.1764 0.0057 -0.1191 278 PHE A O 2139 C CB . PHE A 278 ? 1.0034 0.4142 0.9087 0.1044 0.0368 -0.1309 278 PHE A CB 2140 C CG . PHE A 278 ? 1.0713 0.4549 0.9683 0.0616 0.0472 -0.1312 278 PHE A CG 2141 C CD1 . PHE A 278 ? 1.2054 0.5429 1.0724 0.0550 0.0541 -0.1148 278 PHE A CD1 2142 C CD2 . PHE A 278 ? 1.0850 0.4935 1.0015 0.0287 0.0485 -0.1480 278 PHE A CD2 2143 C CE1 . PHE A 278 ? 1.2970 0.6163 1.1576 0.0158 0.0646 -0.1169 278 PHE A CE1 2144 C CE2 . PHE A 278 ? 1.1930 0.5873 1.1039 -0.0079 0.0546 -0.1492 278 PHE A CE2 2145 C CZ . PHE A 278 ? 1.2811 0.6321 1.1665 -0.0149 0.0641 -0.1346 278 PHE A CZ 2146 N N . VAL A 279 ? 0.7499 0.3757 0.7565 0.1242 -0.0001 -0.1247 279 VAL A N 2147 C CA . VAL A 279 ? 0.7480 0.4372 0.7816 0.1526 -0.0107 -0.1294 279 VAL A CA 2148 C C . VAL A 279 ? 0.7569 0.4584 0.7857 0.1797 -0.0245 -0.1143 279 VAL A C 2149 O O . VAL A 279 ? 0.7745 0.5305 0.8265 0.2063 -0.0350 -0.1191 279 VAL A O 2150 C CB . VAL A 279 ? 0.7479 0.5121 0.8208 0.1295 -0.0125 -0.1401 279 VAL A CB 2151 C CG1 . VAL A 279 ? 0.7339 0.4845 0.8044 0.1120 -0.0014 -0.1567 279 VAL A CG1 2152 C CG2 . VAL A 279 ? 0.6764 0.4633 0.7595 0.1000 -0.0174 -0.1291 279 VAL A CG2 2153 N N . VAL A 280 ? 0.8264 0.4780 0.8240 0.1720 -0.0240 -0.0976 280 VAL A N 2154 C CA . VAL A 280 ? 0.8579 0.5058 0.8373 0.1972 -0.0373 -0.0819 280 VAL A CA 2155 C C . VAL A 280 ? 0.9864 0.5349 0.9059 0.2159 -0.0307 -0.0691 280 VAL A C 2156 O O . VAL A 280 ? 1.0298 0.5151 0.9244 0.1911 -0.0132 -0.0692 280 VAL A O 2157 C CB . VAL A 280 ? 0.7636 0.4420 0.7529 0.1690 -0.0417 -0.0718 280 VAL A CB 2158 C CG1 . VAL A 280 ? 0.6914 0.4583 0.7307 0.1532 -0.0479 -0.0831 280 VAL A CG1 2159 C CG2 . VAL A 280 ? 0.7348 0.3645 0.7071 0.1317 -0.0254 -0.0669 280 VAL A CG2 2160 N N . PRO A 281 ? 1.0710 0.6042 0.9647 0.2591 -0.0449 -0.0588 281 PRO A N 2161 C CA . PRO A 281 ? 1.1960 0.6265 1.0226 0.2816 -0.0389 -0.0446 281 PRO A CA 2162 C C . PRO A 281 ? 1.2204 0.5936 1.0088 0.2462 -0.0256 -0.0285 281 PRO A C 2163 O O . PRO A 281 ? 1.2362 0.5477 0.9942 0.2237 -0.0054 -0.0245 281 PRO A O 2164 C CB . PRO A 281 ? 1.2238 0.6823 1.0426 0.3302 -0.0623 -0.0357 281 PRO A CB 2165 C CG . PRO A 281 ? 1.1590 0.7165 1.0291 0.3261 -0.0806 -0.0419 281 PRO A CG 2166 C CD . PRO A 281 ? 1.0926 0.7062 1.0169 0.2872 -0.0680 -0.0600 281 PRO A CD 2167 N N . TYR A 282 ? 1.1737 0.5861 0.9727 0.2345 -0.0354 -0.0206 282 TYR A N 2168 C CA . TYR A 282 ? 1.2536 0.6218 1.0233 0.1993 -0.0207 -0.0084 282 TYR A CA 2169 C C . TYR A 282 ? 1.1845 0.6308 1.0078 0.1611 -0.0204 -0.0155 282 TYR A C 2170 O O . TYR A 282 ? 1.2098 0.7358 1.0730 0.1688 -0.0376 -0.0208 282 TYR A O 2171 C CB . TYR A 282 ? 1.4288 0.7499 1.1397 0.2233 -0.0296 0.0129 282 TYR A CB 2172 C CG . TYR A 282 ? 1.5102 0.8931 1.2344 0.2646 -0.0606 0.0150 282 TYR A CG 2173 C CD1 . TYR A 282 ? 1.4644 0.9399 1.2375 0.2494 -0.0737 0.0091 282 TYR A CD1 2174 C CD2 . TYR A 282 ? 1.5792 0.9419 1.2731 0.3122 -0.0754 0.0212 282 TYR A CD2 2175 C CE1 . TYR A 282 ? 1.4633 1.0023 1.2522 0.2815 -0.1017 0.0077 282 TYR A CE1 2176 C CE2 . TYR A 282 ? 1.5865 1.0122 1.2964 0.3517 -0.1063 0.0203 282 TYR A CE2 2177 C CZ . TYR A 282 ? 1.5336 1.0496 1.2926 0.3344 -0.1194 0.0127 282 TYR A CZ 2178 O OH . TYR A 282 ? 1.5308 1.1209 1.3117 0.3663 -0.1494 0.0085 282 TYR A OH 2179 N N . GLY A 283 ? 1.0841 0.5070 0.9083 0.1199 0.0001 -0.0171 283 GLY A N 2180 C CA . GLY A 283 ? 0.9293 0.4152 0.7970 0.0871 0.0014 -0.0223 283 GLY A CA 2181 C C . GLY A 283 ? 0.9001 0.3533 0.7369 0.0694 0.0121 -0.0087 283 GLY A C 2182 O O . GLY A 283 ? 0.9631 0.3418 0.7420 0.0797 0.0197 0.0048 283 GLY A O 2183 N N . THR A 284 ? 0.7330 0.2383 0.6041 0.0443 0.0136 -0.0121 284 THR A N 2184 C CA . THR A 284 ? 0.7486 0.2316 0.5984 0.0235 0.0275 -0.0029 284 THR A CA 2185 C C . THR A 284 ? 0.6934 0.2156 0.5907 -0.0121 0.0404 -0.0158 284 THR A C 2186 O O . THR A 284 ? 0.6455 0.2115 0.5847 -0.0158 0.0335 -0.0290 284 THR A O 2187 C CB . THR A 284 ? 0.7303 0.2474 0.5736 0.0368 0.0114 0.0055 284 THR A CB 2188 O OG1 . THR A 284 ? 0.6501 0.2440 0.5471 0.0260 0.0024 -0.0056 284 THR A OG1 2189 C CG2 . THR A 284 ? 0.7671 0.2762 0.5819 0.0775 -0.0109 0.0130 284 THR A CG2 2190 N N . PRO A 285 ? 0.7618 0.2696 0.6518 -0.0368 0.0591 -0.0127 285 PRO A N 2191 C CA . PRO A 285 ? 0.6501 0.2063 0.5907 -0.0649 0.0678 -0.0260 285 PRO A CA 2192 C C . PRO A 285 ? 0.7037 0.3319 0.6854 -0.0587 0.0497 -0.0312 285 PRO A C 2193 O O . PRO A 285 ? 0.6494 0.3188 0.6728 -0.0746 0.0515 -0.0427 285 PRO A O 2194 C CB . PRO A 285 ? 0.6815 0.2112 0.6021 -0.0855 0.0909 -0.0204 285 PRO A CB 2195 C CG . PRO A 285 ? 0.7661 0.2185 0.6253 -0.0795 0.1016 -0.0082 285 PRO A CG 2196 C CD . PRO A 285 ? 0.8270 0.2641 0.6595 -0.0421 0.0775 0.0006 285 PRO A CD 2197 N N . LEU A 286 ? 0.5692 0.2111 0.5373 -0.0366 0.0325 -0.0237 286 LEU A N 2198 C CA . LEU A 286 ? 0.5102 0.2123 0.5101 -0.0340 0.0178 -0.0290 286 LEU A CA 2199 C C . LEU A 286 ? 0.4862 0.2186 0.5036 -0.0178 0.0004 -0.0356 286 LEU A C 2200 O O . LEU A 286 ? 0.4646 0.2413 0.5007 -0.0157 -0.0108 -0.0395 286 LEU A O 2201 C CB . LEU A 286 ? 0.5564 0.2620 0.5335 -0.0282 0.0129 -0.0202 286 LEU A CB 2202 C CG . LEU A 286 ? 0.6305 0.3182 0.5976 -0.0466 0.0324 -0.0170 286 LEU A CG 2203 C CD1 . LEU A 286 ? 0.6610 0.2902 0.5740 -0.0426 0.0423 -0.0041 286 LEU A CD1 2204 C CD2 . LEU A 286 ? 0.5448 0.2682 0.5240 -0.0507 0.0283 -0.0194 286 LEU A CD2 2205 N N . SER A 287 ? 0.5726 0.2787 0.5819 -0.0079 0.0008 -0.0379 287 SER A N 2206 C CA . SER A 287 ? 0.5697 0.3039 0.5955 0.0086 -0.0124 -0.0459 287 SER A CA 2207 C C . SER A 287 ? 0.5147 0.2986 0.5787 -0.0049 -0.0156 -0.0580 287 SER A C 2208 O O . SER A 287 ? 0.4827 0.2676 0.5617 -0.0242 -0.0077 -0.0635 287 SER A O 2209 C CB . SER A 287 ? 0.5512 0.2411 0.5600 0.0200 -0.0076 -0.0484 287 SER A CB 2210 O OG . SER A 287 ? 0.6346 0.2820 0.6031 0.0442 -0.0109 -0.0368 287 SER A OG 2211 N N . VAL A 288 ? 0.4173 0.2425 0.4947 0.0053 -0.0274 -0.0624 288 VAL A N 2212 C CA . VAL A 288 ? 0.3782 0.2425 0.4812 -0.0054 -0.0299 -0.0729 288 VAL A CA 2213 C C . VAL A 288 ? 0.3819 0.2635 0.4922 0.0107 -0.0350 -0.0818 288 VAL A C 2214 O O . VAL A 288 ? 0.4331 0.3496 0.5508 0.0205 -0.0426 -0.0843 288 VAL A O 2215 C CB . VAL A 288 ? 0.3825 0.2794 0.4912 -0.0141 -0.0342 -0.0709 288 VAL A CB 2216 C CG1 . VAL A 288 ? 0.3220 0.2511 0.4467 -0.0233 -0.0359 -0.0804 288 VAL A CG1 2217 C CG2 . VAL A 288 ? 0.3487 0.2283 0.4511 -0.0277 -0.0270 -0.0637 288 VAL A CG2 2218 N N . ASN A 289 ? 0.4000 0.2588 0.5090 0.0128 -0.0298 -0.0886 289 ASN A N 2219 C CA . ASN A 289 ? 0.5728 0.4406 0.6852 0.0320 -0.0318 -0.0979 289 ASN A CA 2220 C C . ASN A 289 ? 0.4538 0.3708 0.5869 0.0263 -0.0334 -0.1093 289 ASN A C 2221 O O . ASN A 289 ? 0.4525 0.3989 0.5956 0.0426 -0.0361 -0.1163 289 ASN A O 2222 C CB . ASN A 289 ? 0.6576 0.4792 0.7566 0.0342 -0.0237 -0.1035 289 ASN A CB 2223 C CG . ASN A 289 ? 0.7646 0.5290 0.8347 0.0434 -0.0193 -0.0926 289 ASN A CG 2224 O OD1 . ASN A 289 ? 0.8227 0.5822 0.8792 0.0632 -0.0256 -0.0825 289 ASN A OD1 2225 N ND2 . ASN A 289 ? 0.8211 0.5408 0.8785 0.0274 -0.0083 -0.0951 289 ASN A ND2 2226 N N . PHE A 290 ? 0.4551 0.2726 0.4593 0.0569 -0.0574 -0.1556 290 PHE A N 2227 C CA . PHE A 290 ? 0.4967 0.3324 0.4944 0.0567 -0.0448 -0.1630 290 PHE A CA 2228 C C . PHE A 290 ? 0.4461 0.3033 0.4438 0.0451 -0.0444 -0.1523 290 PHE A C 2229 O O . PHE A 290 ? 0.4544 0.3050 0.4368 0.0338 -0.0496 -0.1485 290 PHE A O 2230 C CB . PHE A 290 ? 0.4346 0.2522 0.4064 0.0532 -0.0411 -0.1729 290 PHE A CB 2231 C CG . PHE A 290 ? 0.5174 0.3176 0.4875 0.0642 -0.0373 -0.1815 290 PHE A CG 2232 C CD1 . PHE A 290 ? 0.4761 0.2877 0.4536 0.0774 -0.0246 -0.1924 290 PHE A CD1 2233 C CD2 . PHE A 290 ? 0.5291 0.3028 0.4917 0.0612 -0.0459 -0.1787 290 PHE A CD2 2234 C CE1 . PHE A 290 ? 0.5489 0.3445 0.5254 0.0888 -0.0208 -0.2004 290 PHE A CE1 2235 C CE2 . PHE A 290 ? 0.5439 0.2991 0.5043 0.0717 -0.0426 -0.1869 290 PHE A CE2 2236 C CZ . PHE A 290 ? 0.5874 0.3529 0.5543 0.0861 -0.0302 -0.1978 290 PHE A CZ 2237 N N . GLY A 291 ? 0.3570 0.2398 0.3728 0.0482 -0.0389 -0.1479 291 GLY A N 2238 C CA . GLY A 291 ? 0.4043 0.3052 0.4204 0.0381 -0.0384 -0.1385 291 GLY A CA 2239 C C . GLY A 291 ? 0.3805 0.3054 0.4037 0.0391 -0.0258 -0.1414 291 GLY A C 2240 O O . GLY A 291 ? 0.3394 0.2687 0.3654 0.0469 -0.0159 -0.1516 291 GLY A O 2241 N N . PRO A 292 ? 0.3247 0.2648 0.3502 0.0307 -0.0253 -0.1329 292 PRO A N 2242 C CA . PRO A 292 ? 0.3284 0.2908 0.3612 0.0289 -0.0137 -0.1344 292 PRO A CA 2243 C C . PRO A 292 ? 0.3209 0.3016 0.3798 0.0396 -0.0083 -0.1397 292 PRO A C 2244 O O . PRO A 292 ? 0.3134 0.2935 0.3885 0.0472 -0.0169 -0.1373 292 PRO A O 2245 C CB . PRO A 292 ? 0.2771 0.2483 0.3131 0.0198 -0.0188 -0.1232 292 PRO A CB 2246 C CG . PRO A 292 ? 0.2921 0.2444 0.3123 0.0148 -0.0295 -0.1177 292 PRO A CG 2247 C CD . PRO A 292 ? 0.3000 0.2361 0.3208 0.0221 -0.0352 -0.1222 292 PRO A CD 2248 N N . THR A 293 ? 0.3055 0.3027 0.3682 0.0404 0.0058 -0.1468 293 THR A N 2249 C CA . THR A 293 ? 0.3039 0.3253 0.3954 0.0500 0.0121 -0.1521 293 THR A CA 2250 C C . THR A 293 ? 0.3405 0.3886 0.4411 0.0409 0.0233 -0.1508 293 THR A C 2251 O O . THR A 293 ? 0.3231 0.3661 0.4033 0.0284 0.0277 -0.1468 293 THR A O 2252 C CB . THR A 293 ? 0.3721 0.3901 0.4637 0.0624 0.0216 -0.1659 293 THR A CB 2253 O OG1 . THR A 293 ? 0.3926 0.4009 0.4562 0.0555 0.0324 -0.1714 293 THR A OG1 2254 C CG2 . THR A 293 ? 0.4582 0.4508 0.5475 0.0734 0.0102 -0.1683 293 THR A CG2 2255 N N . VAL A 294 ? 0.2892 0.3654 0.4205 0.0469 0.0273 -0.1538 294 VAL A N 2256 C CA . VAL A 294 ? 0.2850 0.3894 0.4286 0.0378 0.0399 -0.1543 294 VAL A CA 2257 C C . VAL A 294 ? 0.3071 0.4181 0.4440 0.0404 0.0586 -0.1655 294 VAL A C 2258 O O . VAL A 294 ? 0.3146 0.4439 0.4739 0.0528 0.0656 -0.1749 294 VAL A O 2259 C CB . VAL A 294 ? 0.3140 0.4497 0.4962 0.0424 0.0357 -0.1534 294 VAL A CB 2260 C CG1 . VAL A 294 ? 0.2682 0.4352 0.4656 0.0312 0.0495 -0.1548 294 VAL A CG1 2261 C CG2 . VAL A 294 ? 0.2521 0.3794 0.4358 0.0392 0.0175 -0.1425 294 VAL A CG2 2262 N N . ASP A 295 ? 0.3230 0.4188 0.4280 0.0295 0.0665 -0.1645 295 ASP A N 2263 C CA . ASP A 295 ? 0.3746 0.4699 0.4637 0.0316 0.0837 -0.1751 295 ASP A CA 2264 C C . ASP A 295 ? 0.3527 0.4765 0.4496 0.0214 0.1030 -0.1766 295 ASP A C 2265 O O . ASP A 295 ? 0.4061 0.5351 0.4926 0.0231 0.1200 -0.1860 295 ASP A O 2266 C CB . ASP A 295 ? 0.3618 0.4234 0.4080 0.0251 0.0807 -0.1730 295 ASP A CB 2267 C CG . ASP A 295 ? 0.4110 0.4659 0.4395 0.0081 0.0777 -0.1604 295 ASP A CG 2268 O OD1 . ASP A 295 ? 0.3331 0.4030 0.3822 0.0022 0.0731 -0.1526 295 ASP A OD1 2269 O OD2 . ASP A 295 ? 0.3711 0.4051 0.3649 0.0010 0.0791 -0.1584 295 ASP A OD2 2270 N N . GLY A 296 ? 0.3598 0.5006 0.4727 0.0097 0.1009 -0.1677 296 GLY A N 2271 C CA . GLY A 296 ? 0.3997 0.5659 0.5197 -0.0033 0.1184 -0.1675 296 GLY A CA 2272 C C . GLY A 296 ? 0.4772 0.6224 0.5563 -0.0189 0.1267 -0.1617 296 GLY A C 2273 O O . GLY A 296 ? 0.3770 0.5377 0.4533 -0.0303 0.1444 -0.1620 296 GLY A O 2274 N N . ASP A 297 ? 0.4595 0.5697 0.5070 -0.0196 0.1138 -0.1559 297 ASP A N 2275 C CA . ASP A 297 ? 0.4044 0.4911 0.4108 -0.0322 0.1181 -0.1495 297 ASP A CA 2276 C C . ASP A 297 ? 0.4344 0.4982 0.4280 -0.0386 0.1001 -0.1371 297 ASP A C 2277 O O . ASP A 297 ? 0.3992 0.4642 0.3918 -0.0518 0.1007 -0.1281 297 ASP A O 2278 C CB . ASP A 297 ? 0.4231 0.4899 0.3982 -0.0247 0.1225 -0.1578 297 ASP A CB 2279 C CG . ASP A 297 ? 0.4900 0.5367 0.4216 -0.0374 0.1297 -0.1523 297 ASP A CG 2280 O OD1 . ASP A 297 ? 0.4973 0.5402 0.4217 -0.0512 0.1285 -0.1405 297 ASP A OD1 2281 O OD2 . ASP A 297 ? 0.5054 0.5382 0.4085 -0.0334 0.1356 -0.1596 297 ASP A OD2 2282 N N . PHE A 298 ? 0.3624 0.4051 0.3466 -0.0296 0.0845 -0.1369 298 PHE A N 2283 C CA . PHE A 298 ? 0.3471 0.3724 0.3244 -0.0336 0.0677 -0.1263 298 PHE A CA 2284 C C . PHE A 298 ? 0.3867 0.4295 0.3976 -0.0333 0.0600 -0.1228 298 PHE A C 2285 O O . PHE A 298 ? 0.3690 0.4060 0.3779 -0.0415 0.0530 -0.1141 298 PHE A O 2286 C CB . PHE A 298 ? 0.3466 0.3492 0.3092 -0.0248 0.0539 -0.1277 298 PHE A CB 2287 C CG . PHE A 298 ? 0.3347 0.3204 0.2877 -0.0286 0.0383 -0.1174 298 PHE A CG 2288 C CD1 . PHE A 298 ? 0.3278 0.3187 0.3032 -0.0250 0.0265 -0.1138 298 PHE A CD1 2289 C CD2 . PHE A 298 ? 0.4031 0.3684 0.3244 -0.0351 0.0356 -0.1117 298 PHE A CD2 2290 C CE1 . PHE A 298 ? 0.3311 0.3083 0.2983 -0.0277 0.0138 -0.1055 298 PHE A CE1 2291 C CE2 . PHE A 298 ? 0.4137 0.3658 0.3290 -0.0368 0.0217 -0.1031 298 PHE A CE2 2292 C CZ . PHE A 298 ? 0.3539 0.3127 0.2927 -0.0331 0.0116 -0.1004 298 PHE A CZ 2293 N N . LEU A 299 ? 0.3421 0.4055 0.3828 -0.0232 0.0609 -0.1301 299 LEU A N 2294 C CA . LEU A 299 ? 0.3315 0.4123 0.4038 -0.0210 0.0519 -0.1276 299 LEU A CA 2295 C C . LEU A 299 ? 0.4069 0.5219 0.5105 -0.0198 0.0637 -0.1343 299 LEU A C 2296 O O . LEU A 299 ? 0.2920 0.4177 0.4083 -0.0075 0.0692 -0.1435 299 LEU A O 2297 C CB . LEU A 299 ? 0.3762 0.4480 0.4561 -0.0074 0.0379 -0.1290 299 LEU A CB 2298 C CG . LEU A 299 ? 0.5177 0.5797 0.5996 -0.0080 0.0212 -0.1207 299 LEU A CG 2299 C CD1 . LEU A 299 ? 0.4670 0.5231 0.5585 0.0053 0.0103 -0.1227 299 LEU A CD1 2300 C CD2 . LEU A 299 ? 0.5346 0.6159 0.6368 -0.0152 0.0191 -0.1166 299 LEU A CD2 2301 N N . THR A 300 ? 0.3605 0.4930 0.4778 -0.0321 0.0673 -0.1302 300 THR A N 2302 C CA . THR A 300 ? 0.3650 0.5333 0.5119 -0.0345 0.0807 -0.1363 300 THR A CA 2303 C C . THR A 300 ? 0.3391 0.5355 0.5267 -0.0245 0.0723 -0.1400 300 THR A C 2304 O O . THR A 300 ? 0.3567 0.5861 0.5732 -0.0227 0.0826 -0.1467 300 THR A O 2305 C CB . THR A 300 ? 0.3874 0.5636 0.5319 -0.0549 0.0896 -0.1306 300 THR A CB 2306 O OG1 . THR A 300 ? 0.3398 0.5080 0.4870 -0.0619 0.0747 -0.1227 300 THR A OG1 2307 C CG2 . THR A 300 ? 0.4711 0.6217 0.5753 -0.0643 0.0997 -0.1267 300 THR A CG2 2308 N N . ASP A 301 ? 0.3240 0.5085 0.5140 -0.0182 0.0538 -0.1354 301 ASP A N 2309 C CA . ASP A 301 ? 0.3411 0.5492 0.5659 -0.0091 0.0431 -0.1371 301 ASP A CA 2310 C C . ASP A 301 ? 0.2745 0.4581 0.4883 -0.0001 0.0246 -0.1318 301 ASP A C 2311 O O . ASP A 301 ? 0.2288 0.3824 0.4125 -0.0034 0.0211 -0.1270 301 ASP A O 2312 C CB . ASP A 301 ? 0.3171 0.5481 0.5615 -0.0236 0.0414 -0.1338 301 ASP A CB 2313 C CG . ASP A 301 ? 0.3424 0.6072 0.6277 -0.0151 0.0329 -0.1373 301 ASP A CG 2314 O OD1 . ASP A 301 ? 0.2750 0.5453 0.5744 0.0033 0.0284 -0.1418 301 ASP A OD1 2315 O OD2 . ASP A 301 ? 0.3578 0.6433 0.6612 -0.0271 0.0299 -0.1356 301 ASP A OD2 2316 N N . MET A 302 ? 0.2715 0.4683 0.5094 0.0108 0.0127 -0.1322 302 MET A N 2317 C CA . MET A 302 ? 0.2447 0.4188 0.4712 0.0174 -0.0042 -0.1259 302 MET A CA 2318 C C . MET A 302 ? 0.2462 0.4052 0.4533 0.0035 -0.0110 -0.1177 302 MET A C 2319 O O . MET A 302 ? 0.2758 0.4501 0.4929 -0.0073 -0.0117 -0.1161 302 MET A O 2320 C CB . MET A 302 ? 0.2333 0.4254 0.4881 0.0301 -0.0163 -0.1265 302 MET A CB 2321 C CG . MET A 302 ? 0.2376 0.4480 0.5158 0.0451 -0.0086 -0.1359 302 MET A CG 2322 S SD . MET A 302 ? 0.5969 0.8250 0.9074 0.0634 -0.0251 -0.1357 302 MET A SD 2323 C CE . MET A 302 ? 0.8769 1.0614 1.1569 0.0687 -0.0408 -0.1265 302 MET A CE 2324 N N . PRO A 303 ? 0.2798 0.4087 0.4593 0.0036 -0.0155 -0.1130 303 PRO A N 2325 C CA . PRO A 303 ? 0.2574 0.3705 0.4167 -0.0082 -0.0196 -0.1064 303 PRO A CA 2326 C C . PRO A 303 ? 0.3009 0.4200 0.4683 -0.0106 -0.0325 -0.1018 303 PRO A C 2327 O O . PRO A 303 ? 0.2321 0.3461 0.3898 -0.0219 -0.0334 -0.0988 303 PRO A O 2328 C CB . PRO A 303 ? 0.3171 0.4013 0.4505 -0.0044 -0.0221 -0.1036 303 PRO A CB 2329 C CG . PRO A 303 ? 0.2909 0.3738 0.4323 0.0094 -0.0236 -0.1078 303 PRO A CG 2330 C CD . PRO A 303 ? 0.2487 0.3574 0.4140 0.0134 -0.0145 -0.1152 303 PRO A CD 2331 N N . ASP A 304 ? 0.1881 0.3160 0.3711 -0.0002 -0.0425 -0.1015 304 ASP A N 2332 C CA . ASP A 304 ? 0.3421 0.4778 0.5321 -0.0024 -0.0550 -0.0978 304 ASP A CA 2333 C C . ASP A 304 ? 0.3221 0.4826 0.5304 -0.0129 -0.0524 -0.1011 304 ASP A C 2334 O O . ASP A 304 ? 0.2734 0.4339 0.4777 -0.0217 -0.0594 -0.0988 304 ASP A O 2335 C CB . ASP A 304 ? 0.4262 0.5677 0.6298 0.0114 -0.0665 -0.0963 304 ASP A CB 2336 C CG . ASP A 304 ? 0.6053 0.7645 0.8328 0.0226 -0.0613 -0.1027 304 ASP A CG 2337 O OD1 . ASP A 304 ? 0.7139 0.8651 0.9353 0.0251 -0.0499 -0.1069 304 ASP A OD1 2338 O OD2 . ASP A 304 ? 0.5761 0.7576 0.8284 0.0296 -0.0689 -0.1040 304 ASP A OD2 2339 N N . ILE A 305 ? 0.2579 0.4398 0.4864 -0.0124 -0.0420 -0.1070 305 ILE A N 2340 C CA . ILE A 305 ? 0.2871 0.4958 0.5363 -0.0240 -0.0378 -0.1105 305 ILE A CA 2341 C C . ILE A 305 ? 0.2667 0.4602 0.4953 -0.0412 -0.0297 -0.1085 305 ILE A C 2342 O O . ILE A 305 ? 0.2289 0.4274 0.4602 -0.0532 -0.0343 -0.1078 305 ILE A O 2343 C CB . ILE A 305 ? 0.1877 0.4255 0.4649 -0.0189 -0.0263 -0.1177 305 ILE A CB 2344 C CG1 . ILE A 305 ? 0.1867 0.4340 0.4822 0.0011 -0.0345 -0.1197 305 ILE A CG1 2345 C CG2 . ILE A 305 ? 0.1880 0.4586 0.4918 -0.0319 -0.0232 -0.1210 305 ILE A CG2 2346 C CD1 . ILE A 305 ? 0.1900 0.4735 0.5214 0.0089 -0.0258 -0.1280 305 ILE A CD1 2347 N N . LEU A 306 ? 0.1950 0.3683 0.4016 -0.0420 -0.0189 -0.1077 306 LEU A N 2348 C CA . LEU A 306 ? 0.3077 0.4619 0.4911 -0.0563 -0.0118 -0.1046 306 LEU A CA 2349 C C . LEU A 306 ? 0.3037 0.4369 0.4693 -0.0605 -0.0234 -0.0997 306 LEU A C 2350 O O . LEU A 306 ? 0.2635 0.3913 0.4231 -0.0740 -0.0228 -0.0986 306 LEU A O 2351 C CB . LEU A 306 ? 0.2335 0.3674 0.3936 -0.0532 -0.0016 -0.1039 306 LEU A CB 2352 C CG . LEU A 306 ? 0.2291 0.3803 0.4008 -0.0494 0.0125 -0.1098 306 LEU A CG 2353 C CD1 . LEU A 306 ? 0.2285 0.3560 0.3725 -0.0452 0.0196 -0.1095 306 LEU A CD1 2354 C CD2 . LEU A 306 ? 0.2272 0.3998 0.4126 -0.0638 0.0250 -0.1119 306 LEU A CD2 2355 N N . LEU A 307 ? 0.3276 0.4484 0.4844 -0.0493 -0.0335 -0.0971 307 LEU A N 2356 C CA . LEU A 307 ? 0.3224 0.4257 0.4629 -0.0512 -0.0437 -0.0933 307 LEU A CA 2357 C C . LEU A 307 ? 0.2751 0.3935 0.4294 -0.0576 -0.0525 -0.0951 307 LEU A C 2358 O O . LEU A 307 ? 0.2854 0.3926 0.4283 -0.0678 -0.0546 -0.0948 307 LEU A O 2359 C CB . LEU A 307 ? 0.2930 0.3847 0.4245 -0.0386 -0.0516 -0.0901 307 LEU A CB 2360 C CG . LEU A 307 ? 0.3486 0.4239 0.4626 -0.0397 -0.0601 -0.0865 307 LEU A CG 2361 C CD1 . LEU A 307 ? 0.3992 0.4537 0.4922 -0.0468 -0.0546 -0.0850 307 LEU A CD1 2362 C CD2 . LEU A 307 ? 0.2554 0.3225 0.3627 -0.0290 -0.0666 -0.0827 307 LEU A CD2 2363 N N . GLU A 308 ? 0.2329 0.3757 0.4113 -0.0513 -0.0585 -0.0974 308 GLU A N 2364 C CA . GLU A 308 ? 0.2240 0.3839 0.4167 -0.0567 -0.0690 -0.0994 308 GLU A CA 2365 C C . GLU A 308 ? 0.2985 0.4671 0.4988 -0.0739 -0.0630 -0.1028 308 GLU A C 2366 O O . GLU A 308 ? 0.2582 0.4234 0.4539 -0.0835 -0.0706 -0.1040 308 GLU A O 2367 C CB . GLU A 308 ? 0.2242 0.4112 0.4444 -0.0458 -0.0763 -0.1010 308 GLU A CB 2368 C CG . GLU A 308 ? 0.2629 0.4722 0.5010 -0.0511 -0.0888 -0.1035 308 GLU A CG 2369 C CD . GLU A 308 ? 0.3788 0.5686 0.5923 -0.0505 -0.1012 -0.0985 308 GLU A CD 2370 O OE1 . GLU A 308 ? 0.4147 0.5826 0.6075 -0.0442 -0.1027 -0.0957 308 GLU A OE1 2371 O OE2 . GLU A 308 ? 0.4606 0.6571 0.6742 -0.0564 -0.1086 -0.0972 308 GLU A OE2 2372 N N . LEU A 309 ? 0.2000 0.3774 0.4092 -0.0787 -0.0489 -0.1045 309 LEU A N 2373 C CA . LEU A 309 ? 0.2141 0.4030 0.4338 -0.0966 -0.0418 -0.1072 309 LEU A CA 2374 C C . LEU A 309 ? 0.2330 0.3913 0.4244 -0.1083 -0.0330 -0.1039 309 LEU A C 2375 O O . LEU A 309 ? 0.2356 0.3984 0.4316 -0.1239 -0.0241 -0.1047 309 LEU A O 2376 C CB . LEU A 309 ? 0.2083 0.4309 0.4583 -0.0969 -0.0308 -0.1112 309 LEU A CB 2377 C CG . LEU A 309 ? 0.1983 0.4537 0.4804 -0.0848 -0.0406 -0.1148 309 LEU A CG 2378 C CD1 . LEU A 309 ? 0.1979 0.4896 0.5130 -0.0841 -0.0285 -0.1200 309 LEU A CD1 2379 C CD2 . LEU A 309 ? 0.2015 0.4648 0.4905 -0.0911 -0.0565 -0.1148 309 LEU A CD2 2380 N N . GLY A 310 ? 0.3106 0.4381 0.4736 -0.1010 -0.0358 -0.0999 310 GLY A N 2381 C CA . GLY A 310 ? 0.3597 0.4556 0.4949 -0.1094 -0.0309 -0.0964 310 GLY A CA 2382 C C . GLY A 310 ? 0.3815 0.4700 0.5072 -0.1143 -0.0158 -0.0938 310 GLY A C 2383 O O . GLY A 310 ? 0.3276 0.3963 0.4367 -0.1265 -0.0106 -0.0909 310 GLY A O 2384 N N . GLN A 311 ? 0.2392 0.3411 0.3728 -0.1047 -0.0090 -0.0947 311 GLN A N 2385 C CA . GLN A 311 ? 0.2513 0.3474 0.3736 -0.1087 0.0058 -0.0930 311 GLN A CA 2386 C C . GLN A 311 ? 0.3520 0.4209 0.4464 -0.0984 0.0051 -0.0891 311 GLN A C 2387 O O . GLN A 311 ? 0.3417 0.4161 0.4378 -0.0870 0.0076 -0.0910 311 GLN A O 2388 C CB . GLN A 311 ? 0.2987 0.4277 0.4469 -0.1052 0.0154 -0.0982 311 GLN A CB 2389 C CG . GLN A 311 ? 0.3215 0.4830 0.5025 -0.1142 0.0146 -0.1025 311 GLN A CG 2390 C CD . GLN A 311 ? 0.3948 0.5520 0.5715 -0.1359 0.0221 -0.1003 311 GLN A CD 2391 O OE1 . GLN A 311 ? 0.3969 0.5540 0.5795 -0.1462 0.0135 -0.1006 311 GLN A OE1 2392 N NE2 . GLN A 311 ? 0.3138 0.4657 0.4781 -0.1437 0.0382 -0.0980 311 GLN A NE2 2393 N N . PHE A 312 ? 0.2627 0.3022 0.3324 -0.1022 0.0010 -0.0843 312 PHE A N 2394 C CA . PHE A 312 ? 0.2699 0.2845 0.3142 -0.0933 -0.0012 -0.0803 312 PHE A CA 2395 C C . PHE A 312 ? 0.3717 0.3560 0.3904 -0.1012 -0.0018 -0.0746 312 PHE A C 2396 O O . PHE A 312 ? 0.3071 0.2865 0.3272 -0.1125 -0.0025 -0.0743 312 PHE A O 2397 C CB . PHE A 312 ? 0.3120 0.3261 0.3594 -0.0798 -0.0132 -0.0811 312 PHE A CB 2398 C CG . PHE A 312 ? 0.3372 0.3542 0.3931 -0.0816 -0.0230 -0.0824 312 PHE A CG 2399 C CD1 . PHE A 312 ? 0.3324 0.3268 0.3714 -0.0851 -0.0278 -0.0801 312 PHE A CD1 2400 C CD2 . PHE A 312 ? 0.3531 0.3946 0.4329 -0.0792 -0.0277 -0.0864 312 PHE A CD2 2401 C CE1 . PHE A 312 ? 0.3794 0.3753 0.4236 -0.0869 -0.0364 -0.0826 312 PHE A CE1 2402 C CE2 . PHE A 312 ? 0.2871 0.3309 0.3718 -0.0814 -0.0374 -0.0879 312 PHE A CE2 2403 C CZ . PHE A 312 ? 0.3402 0.3608 0.4061 -0.0857 -0.0414 -0.0865 312 PHE A CZ 2404 N N . LYS A 313 ? 0.2932 0.2564 0.2887 -0.0950 -0.0024 -0.0704 313 LYS A N 2405 C CA . LYS A 313 ? 0.4052 0.3376 0.3752 -0.0989 -0.0045 -0.0644 313 LYS A CA 2406 C C . LYS A 313 ? 0.3734 0.2957 0.3450 -0.0974 -0.0148 -0.0653 313 LYS A C 2407 O O . LYS A 313 ? 0.3599 0.2897 0.3399 -0.0869 -0.0228 -0.0680 313 LYS A O 2408 C CB . LYS A 313 ? 0.3963 0.3129 0.3456 -0.0886 -0.0072 -0.0606 313 LYS A CB 2409 C CG . LYS A 313 ? 0.4386 0.3229 0.3611 -0.0898 -0.0109 -0.0537 313 LYS A CG 2410 C CD . LYS A 313 ? 0.4914 0.3649 0.3966 -0.0793 -0.0153 -0.0505 313 LYS A CD 2411 C CE . LYS A 313 ? 0.5266 0.3685 0.4062 -0.0784 -0.0207 -0.0431 313 LYS A CE 2412 N NZ . LYS A 313 ? 0.4507 0.2747 0.3086 -0.0904 -0.0124 -0.0367 313 LYS A NZ 2413 N N . LYS A 314 ? 0.3330 0.2370 0.2951 -0.1084 -0.0142 -0.0631 314 LYS A N 2414 C CA . LYS A 314 ? 0.4480 0.3390 0.4084 -0.1074 -0.0232 -0.0653 314 LYS A CA 2415 C C . LYS A 314 ? 0.4322 0.2942 0.3697 -0.0977 -0.0288 -0.0609 314 LYS A C 2416 O O . LYS A 314 ? 0.4109 0.2472 0.3281 -0.1026 -0.0264 -0.0552 314 LYS A O 2417 C CB . LYS A 314 ? 0.4843 0.3679 0.4462 -0.1245 -0.0207 -0.0663 314 LYS A CB 2418 C CG . LYS A 314 ? 0.4790 0.3957 0.4681 -0.1347 -0.0161 -0.0712 314 LYS A CG 2419 C CD . LYS A 314 ? 0.4858 0.4296 0.4957 -0.1232 -0.0232 -0.0769 314 LYS A CD 2420 C CE . LYS A 314 ? 0.5163 0.4935 0.5549 -0.1314 -0.0214 -0.0819 314 LYS A CE 2421 N NZ . LYS A 314 ? 0.4933 0.4890 0.5423 -0.1363 -0.0090 -0.0807 314 LYS A NZ 2422 N N . THR A 315 ? 0.4468 0.3136 0.3876 -0.0837 -0.0361 -0.0632 315 THR A N 2423 C CA . THR A 315 ? 0.3403 0.1862 0.2647 -0.0724 -0.0418 -0.0599 315 THR A CA 2424 C C . THR A 315 ? 0.4007 0.2573 0.3348 -0.0608 -0.0487 -0.0646 315 THR A C 2425 O O . THR A 315 ? 0.3825 0.2591 0.3323 -0.0623 -0.0495 -0.0693 315 THR A O 2426 C CB . THR A 315 ? 0.4291 0.2732 0.3433 -0.0672 -0.0400 -0.0545 315 THR A CB 2427 O OG1 . THR A 315 ? 0.4007 0.2231 0.2988 -0.0576 -0.0464 -0.0506 315 THR A OG1 2428 C CG2 . THR A 315 ? 0.3133 0.1841 0.2431 -0.0600 -0.0404 -0.0574 315 THR A CG2 2429 N N . GLN A 316 ? 0.3758 0.2202 0.3007 -0.0492 -0.0538 -0.0629 316 GLN A N 2430 C CA . GLN A 316 ? 0.4047 0.2602 0.3380 -0.0388 -0.0586 -0.0671 316 GLN A CA 2431 C C . GLN A 316 ? 0.3655 0.2432 0.3097 -0.0329 -0.0589 -0.0659 316 GLN A C 2432 O O . GLN A 316 ? 0.3755 0.2527 0.3155 -0.0324 -0.0576 -0.0618 316 GLN A O 2433 C CB . GLN A 316 ? 0.3379 0.1737 0.2597 -0.0280 -0.0631 -0.0667 316 GLN A CB 2434 C CG . GLN A 316 ? 0.4453 0.2525 0.3535 -0.0322 -0.0639 -0.0684 316 GLN A CG 2435 C CD . GLN A 316 ? 0.4494 0.2339 0.3425 -0.0402 -0.0617 -0.0617 316 GLN A CD 2436 O OE1 . GLN A 316 ? 0.4003 0.1819 0.2864 -0.0363 -0.0621 -0.0553 316 GLN A OE1 2437 N NE2 . GLN A 316 ? 0.5505 0.3187 0.4374 -0.0527 -0.0594 -0.0629 316 GLN A NE2 2438 N N . ILE A 317 ? 0.2857 0.1811 0.2419 -0.0291 -0.0607 -0.0693 317 ILE A N 2439 C CA . ILE A 317 ? 0.2771 0.1898 0.2425 -0.0235 -0.0617 -0.0678 317 ILE A CA 2440 C C . ILE A 317 ? 0.3202 0.2402 0.2895 -0.0151 -0.0649 -0.0693 317 ILE A C 2441 O O . ILE A 317 ? 0.3044 0.2219 0.2719 -0.0142 -0.0655 -0.0731 317 ILE A O 2442 C CB . ILE A 317 ? 0.3252 0.2561 0.3037 -0.0285 -0.0598 -0.0690 317 ILE A CB 2443 C CG1 . ILE A 317 ? 0.2816 0.2197 0.2662 -0.0315 -0.0614 -0.0729 317 ILE A CG1 2444 C CG2 . ILE A 317 ? 0.2788 0.2083 0.2565 -0.0358 -0.0548 -0.0680 317 ILE A CG2 2445 C CD1 . ILE A 317 ? 0.3227 0.2797 0.3216 -0.0340 -0.0615 -0.0736 317 ILE A CD1 2446 N N . LEU A 318 ? 0.2940 0.2235 0.2682 -0.0097 -0.0664 -0.0667 318 LEU A N 2447 C CA . LEU A 318 ? 0.2866 0.2279 0.2673 -0.0033 -0.0679 -0.0673 318 LEU A CA 2448 C C . LEU A 318 ? 0.3326 0.2893 0.3232 -0.0058 -0.0679 -0.0654 318 LEU A C 2449 O O . LEU A 318 ? 0.2399 0.1974 0.2320 -0.0071 -0.0687 -0.0631 318 LEU A O 2450 C CB . LEU A 318 ? 0.2321 0.1705 0.2112 0.0048 -0.0705 -0.0656 318 LEU A CB 2451 C CG . LEU A 318 ? 0.3365 0.2879 0.3234 0.0123 -0.0707 -0.0669 318 LEU A CG 2452 C CD1 . LEU A 318 ? 0.3794 0.3263 0.3656 0.0214 -0.0741 -0.0660 318 LEU A CD1 2453 C CD2 . LEU A 318 ? 0.3102 0.2806 0.3084 0.0096 -0.0705 -0.0645 318 LEU A CD2 2454 N N . VAL A 319 ? 0.2045 0.1714 0.1998 -0.0066 -0.0676 -0.0663 319 VAL A N 2455 C CA . VAL A 319 ? 0.1940 0.1719 0.1972 -0.0089 -0.0683 -0.0637 319 VAL A CA 2456 C C . VAL A 319 ? 0.2558 0.2442 0.2619 -0.0067 -0.0682 -0.0620 319 VAL A C 2457 O O . VAL A 319 ? 0.2248 0.2142 0.2264 -0.0044 -0.0667 -0.0644 319 VAL A O 2458 C CB . VAL A 319 ? 0.2438 0.2239 0.2493 -0.0133 -0.0687 -0.0649 319 VAL A CB 2459 C CG1 . VAL A 319 ? 0.2382 0.2257 0.2517 -0.0141 -0.0702 -0.0620 319 VAL A CG1 2460 C CG2 . VAL A 319 ? 0.2702 0.2421 0.2733 -0.0172 -0.0670 -0.0674 319 VAL A CG2 2461 N N . GLY A 320 ? 0.2055 0.2009 0.2180 -0.0081 -0.0691 -0.0581 320 GLY A N 2462 C CA . GLY A 320 ? 0.2431 0.2486 0.2577 -0.0083 -0.0680 -0.0553 320 GLY A CA 2463 C C . GLY A 320 ? 0.2898 0.2985 0.3101 -0.0121 -0.0697 -0.0503 320 GLY A C 2464 O O . GLY A 320 ? 0.2442 0.2469 0.2672 -0.0135 -0.0721 -0.0501 320 GLY A O 2465 N N . VAL A 321 ? 0.2421 0.2587 0.2627 -0.0142 -0.0680 -0.0463 321 VAL A N 2466 C CA . VAL A 321 ? 0.2161 0.2327 0.2401 -0.0191 -0.0697 -0.0405 321 VAL A CA 2467 C C . VAL A 321 ? 0.2934 0.3218 0.3203 -0.0222 -0.0658 -0.0368 321 VAL A C 2468 O O . VAL A 321 ? 0.2333 0.2711 0.2591 -0.0191 -0.0613 -0.0393 321 VAL A O 2469 C CB . VAL A 321 ? 0.2262 0.2375 0.2443 -0.0201 -0.0722 -0.0372 321 VAL A CB 2470 C CG1 . VAL A 321 ? 0.2060 0.2099 0.2254 -0.0173 -0.0756 -0.0411 321 VAL A CG1 2471 C CG2 . VAL A 321 ? 0.1999 0.2172 0.2085 -0.0195 -0.0695 -0.0369 321 VAL A CG2 2472 N N . ASN A 322 ? 0.2015 0.2291 0.2325 -0.0284 -0.0670 -0.0311 322 ASN A N 2473 C CA . ASN A 322 ? 0.2207 0.2610 0.2565 -0.0340 -0.0627 -0.0266 322 ASN A CA 2474 C C . ASN A 322 ? 0.2776 0.3157 0.3034 -0.0388 -0.0605 -0.0194 322 ASN A C 2475 O O . ASN A 322 ? 0.2241 0.2486 0.2420 -0.0383 -0.0651 -0.0167 322 ASN A O 2476 C CB . ASN A 322 ? 0.2603 0.3004 0.3069 -0.0402 -0.0659 -0.0249 322 ASN A CB 2477 C CG . ASN A 322 ? 0.2959 0.3393 0.3502 -0.0357 -0.0689 -0.0313 322 ASN A CG 2478 O OD1 . ASN A 322 ? 0.2436 0.2899 0.2960 -0.0281 -0.0677 -0.0361 322 ASN A OD1 2479 N ND2 . ASN A 322 ? 0.2611 0.3023 0.3226 -0.0409 -0.0736 -0.0311 322 ASN A ND2 2480 N N . LYS A 323 ? 0.3235 0.3756 0.3494 -0.0432 -0.0536 -0.0158 323 LYS A N 2481 C CA . LYS A 323 ? 0.2820 0.3317 0.2944 -0.0484 -0.0507 -0.0080 323 LYS A CA 2482 C C . LYS A 323 ? 0.3517 0.3848 0.3606 -0.0558 -0.0561 0.0011 323 LYS A C 2483 O O . LYS A 323 ? 0.2667 0.2889 0.2609 -0.0564 -0.0584 0.0071 323 LYS A O 2484 C CB . LYS A 323 ? 0.3314 0.4016 0.3456 -0.0528 -0.0402 -0.0060 323 LYS A CB 2485 C CG . LYS A 323 ? 0.4004 0.4689 0.3976 -0.0596 -0.0355 0.0030 323 LYS A CG 2486 C CD . LYS A 323 ? 0.5263 0.6186 0.5261 -0.0630 -0.0227 0.0029 323 LYS A CD 2487 C CE . LYS A 323 ? 0.6295 0.7205 0.6108 -0.0722 -0.0166 0.0134 323 LYS A CE 2488 N NZ . LYS A 323 ? 0.7770 0.8941 0.7614 -0.0753 -0.0020 0.0123 323 LYS A NZ 2489 N N . ASP A 324 ? 0.2463 0.2758 0.2672 -0.0613 -0.0588 0.0021 324 ASP A N 2490 C CA . ASP A 324 ? 0.2619 0.2721 0.2788 -0.0683 -0.0640 0.0101 324 ASP A CA 2491 C C . ASP A 324 ? 0.3055 0.2998 0.3292 -0.0651 -0.0721 0.0051 324 ASP A C 2492 O O . ASP A 324 ? 0.2845 0.2705 0.3140 -0.0727 -0.0748 0.0072 324 ASP A O 2493 C CB . ASP A 324 ? 0.2755 0.2926 0.2968 -0.0822 -0.0587 0.0179 324 ASP A CB 2494 C CG . ASP A 324 ? 0.3709 0.4038 0.3832 -0.0860 -0.0488 0.0234 324 ASP A CG 2495 O OD1 . ASP A 324 ? 0.3779 0.3987 0.3718 -0.0873 -0.0492 0.0312 324 ASP A OD1 2496 O OD2 . ASP A 324 ? 0.3357 0.3933 0.3587 -0.0873 -0.0406 0.0196 324 ASP A OD2 2497 N N . GLU A 325 ? 0.2599 0.2499 0.2820 -0.0547 -0.0756 -0.0016 325 GLU A N 2498 C CA . GLU A 325 ? 0.2932 0.2697 0.3200 -0.0505 -0.0816 -0.0073 325 GLU A CA 2499 C C . GLU A 325 ? 0.3189 0.2732 0.3428 -0.0544 -0.0870 -0.0020 325 GLU A C 2500 O O . GLU A 325 ? 0.3295 0.2735 0.3582 -0.0558 -0.0903 -0.0062 325 GLU A O 2501 C CB . GLU A 325 ? 0.2759 0.2508 0.3001 -0.0399 -0.0835 -0.0131 325 GLU A CB 2502 C CG . GLU A 325 ? 0.2930 0.2834 0.3185 -0.0353 -0.0794 -0.0195 325 GLU A CG 2503 C CD . GLU A 325 ? 0.2636 0.2574 0.2967 -0.0344 -0.0791 -0.0263 325 GLU A CD 2504 O OE1 . GLU A 325 ? 0.2603 0.2465 0.2973 -0.0379 -0.0820 -0.0268 325 GLU A OE1 2505 O OE2 . GLU A 325 ? 0.2473 0.2499 0.2808 -0.0302 -0.0766 -0.0311 325 GLU A OE2 2506 N N . GLY A 326 ? 0.2765 0.2215 0.2906 -0.0559 -0.0883 0.0070 326 GLY A N 2507 C CA . GLY A 326 ? 0.2976 0.2174 0.3072 -0.0565 -0.0948 0.0120 326 GLY A CA 2508 C C . GLY A 326 ? 0.5032 0.4102 0.5127 -0.0693 -0.0953 0.0184 326 GLY A C 2509 O O . GLY A 326 ? 0.3344 0.2170 0.3420 -0.0693 -0.1012 0.0193 326 GLY A O 2510 N N . THR A 327 ? 0.2902 0.2461 0.3381 -0.0586 -0.1068 0.0238 327 THR A N 2511 C CA . THR A 327 ? 0.3005 0.2615 0.3507 -0.0714 -0.1135 0.0351 327 THR A CA 2512 C C . THR A 327 ? 0.3106 0.2628 0.3588 -0.0826 -0.1267 0.0364 327 THR A C 2513 O O . THR A 327 ? 0.3273 0.2661 0.3716 -0.0937 -0.1369 0.0394 327 THR A O 2514 C CB . THR A 327 ? 0.2974 0.2904 0.3657 -0.0725 -0.1056 0.0474 327 THR A CB 2515 O OG1 . THR A 327 ? 0.2876 0.2970 0.3738 -0.0659 -0.1029 0.0486 327 THR A OG1 2516 C CG2 . THR A 327 ? 0.2990 0.3009 0.3612 -0.0641 -0.0931 0.0441 327 THR A CG2 2517 N N . ALA A 328 ? 0.3389 0.2968 0.3883 -0.0806 -0.1283 0.0345 328 ALA A N 2518 C CA . ALA A 328 ? 0.3228 0.2754 0.3641 -0.0920 -0.1419 0.0339 328 ALA A CA 2519 C C . ALA A 328 ? 0.3431 0.2653 0.3643 -0.0955 -0.1496 0.0191 328 ALA A C 2520 O O . ALA A 328 ? 0.3715 0.2825 0.3874 -0.1077 -0.1635 0.0172 328 ALA A O 2521 C CB . ALA A 328 ? 0.3205 0.2826 0.3585 -0.0883 -0.1418 0.0344 328 ALA A CB 2522 N N . PHE A 329 ? 0.3679 0.2763 0.3812 -0.0842 -0.1417 0.0076 329 PHE A N 2523 C CA . PHE A 329 ? 0.4428 0.3252 0.4422 -0.0820 -0.1466 -0.0096 329 PHE A CA 2524 C C . PHE A 329 ? 0.3750 0.2348 0.3791 -0.0869 -0.1566 -0.0077 329 PHE A C 2525 O O . PHE A 329 ? 0.4470 0.2803 0.4441 -0.0873 -0.1661 -0.0215 329 PHE A O 2526 C CB . PHE A 329 ? 0.3932 0.2760 0.3896 -0.0679 -0.1348 -0.0205 329 PHE A CB 2527 C CG . PHE A 329 ? 0.4076 0.3098 0.3998 -0.0660 -0.1268 -0.0191 329 PHE A CG 2528 C CD1 . PHE A 329 ? 0.3910 0.2947 0.3650 -0.0685 -0.1276 -0.0291 329 PHE A CD1 2529 C CD2 . PHE A 329 ? 0.4061 0.3243 0.4116 -0.0625 -0.1194 -0.0072 329 PHE A CD2 2530 C CE1 . PHE A 329 ? 0.4101 0.3333 0.3786 -0.0696 -0.1216 -0.0222 329 PHE A CE1 2531 C CE2 . PHE A 329 ? 0.3145 0.2466 0.3197 -0.0623 -0.1150 -0.0016 329 PHE A CE2 2532 C CZ . PHE A 329 ? 0.3463 0.2822 0.3327 -0.0670 -0.1164 -0.0065 329 PHE A CZ 2533 N N . LEU A 330 ? 0.4189 0.2890 0.4347 -0.0905 -0.1545 0.0094 330 LEU A N 2534 C CA . LEU A 330 ? 0.4902 0.3414 0.5103 -0.0973 -0.1641 0.0181 330 LEU A CA 2535 C C . LEU A 330 ? 0.4685 0.3016 0.4921 -0.1141 -0.1816 0.0214 330 LEU A C 2536 O O . LEU A 330 ? 0.4729 0.2763 0.4984 -0.1174 -0.1935 0.0215 330 LEU A O 2537 C CB . LEU A 330 ? 0.4718 0.3463 0.4988 -0.0996 -0.1556 0.0373 330 LEU A CB 2538 C CG . LEU A 330 ? 0.4831 0.3724 0.5058 -0.0844 -0.1410 0.0315 330 LEU A CG 2539 C CD1 . LEU A 330 ? 0.3457 0.2582 0.3691 -0.0865 -0.1325 0.0461 330 LEU A CD1 2540 C CD2 . LEU A 330 ? 0.4377 0.3044 0.4542 -0.0732 -0.1441 0.0183 330 LEU A CD2 2541 N N . VAL A 331 ? 0.4296 0.2800 0.4559 -0.1243 -0.1848 0.0248 331 VAL A N 2542 C CA . VAL A 331 ? 0.5058 0.3445 0.5351 -0.1380 -0.1988 0.0285 331 VAL A CA 2543 C C . VAL A 331 ? 0.5401 0.3539 0.5510 -0.1317 -0.2043 0.0032 331 VAL A C 2544 O O . VAL A 331 ? 0.5315 0.3353 0.5415 -0.1412 -0.2153 0.0013 331 VAL A O 2545 C CB . VAL A 331 ? 0.5157 0.3890 0.5607 -0.1525 -0.2008 0.0467 331 VAL A CB 2546 C CG1 . VAL A 331 ? 0.4706 0.3741 0.5368 -0.1586 -0.1925 0.0701 331 VAL A CG1 2547 C CG2 . VAL A 331 ? 0.4166 0.3105 0.4550 -0.1479 -0.1980 0.0385 331 VAL A CG2 2548 N N . TYR A 332 ? 0.4765 0.2825 0.4736 -0.1165 -0.1965 -0.0171 332 TYR A N 2549 C CA . TYR A 332 ? 0.5170 0.3040 0.4956 -0.1099 -0.1989 -0.0441 332 TYR A CA 2550 C C . TYR A 332 ? 0.6282 0.3851 0.6106 -0.0956 -0.1986 -0.0586 332 TYR A C 2551 O O . TYR A 332 ? 0.6359 0.3842 0.6064 -0.0829 -0.1934 -0.0839 332 TYR A O 2552 C CB . TYR A 332 ? 0.4816 0.2877 0.4412 -0.1048 -0.1907 -0.0568 332 TYR A CB 2553 C CG . TYR A 332 ? 0.4765 0.3092 0.4307 -0.1179 -0.1954 -0.0451 332 TYR A CG 2554 C CD1 . TYR A 332 ? 0.4416 0.3025 0.4122 -0.1220 -0.1921 -0.0221 332 TYR A CD1 2555 C CD2 . TYR A 332 ? 0.5106 0.3416 0.4450 -0.1254 -0.2043 -0.0575 332 TYR A CD2 2556 C CE1 . TYR A 332 ? 0.4386 0.3260 0.4108 -0.1318 -0.1979 -0.0091 332 TYR A CE1 2557 C CE2 . TYR A 332 ? 0.5087 0.3660 0.4401 -0.1370 -0.2110 -0.0439 332 TYR A CE2 2558 C CZ . TYR A 332 ? 0.4715 0.3571 0.4240 -0.1394 -0.2079 -0.0185 332 TYR A CZ 2559 O OH . TYR A 332 ? 0.4713 0.3844 0.4269 -0.1485 -0.2155 -0.0031 332 TYR A OH 2560 N N . GLY A 333 ? 0.6384 0.3821 0.6381 -0.0976 -0.2047 -0.0415 333 GLY A N 2561 C CA . GLY A 333 ? 0.6900 0.4047 0.6982 -0.0845 -0.2090 -0.0508 333 GLY A CA 2562 C C . GLY A 333 ? 0.6638 0.3723 0.6883 -0.0837 -0.2136 -0.0287 333 GLY A C 2563 O O . GLY A 333 ? 0.7706 0.4526 0.8063 -0.0779 -0.2241 -0.0292 333 GLY A O 2564 N N . ALA A 334 ? 0.5627 0.2949 0.5883 -0.0894 -0.2072 -0.0096 334 ALA A N 2565 C CA . ALA A 334 ? 0.5189 0.2465 0.5539 -0.0911 -0.2125 0.0116 334 ALA A CA 2566 C C . ALA A 334 ? 0.6095 0.3277 0.6530 -0.1088 -0.2263 0.0367 334 ALA A C 2567 O O . ALA A 334 ? 0.6168 0.3507 0.6611 -0.1252 -0.2265 0.0481 334 ALA A O 2568 C CB . ALA A 334 ? 0.5041 0.2598 0.5348 -0.0935 -0.2014 0.0219 334 ALA A CB 2569 N N . PRO A 335 ? 0.6021 0.2970 0.6551 -0.1060 -0.2390 0.0469 335 PRO A N 2570 C CA . PRO A 335 ? 0.5839 0.2686 0.6466 -0.1235 -0.2539 0.0715 335 PRO A CA 2571 C C . PRO A 335 ? 0.5746 0.2901 0.6351 -0.1441 -0.2493 0.1044 335 PRO A C 2572 O O . PRO A 335 ? 0.5454 0.2785 0.5973 -0.1423 -0.2394 0.1117 335 PRO A O 2573 C CB . PRO A 335 ? 0.6233 0.2795 0.6974 -0.1131 -0.2683 0.0748 335 PRO A CB 2574 C CG . PRO A 335 ? 0.6474 0.2966 0.7214 -0.0880 -0.2609 0.0450 335 PRO A CG 2575 C CD . PRO A 335 ? 0.5804 0.2592 0.6394 -0.0866 -0.2420 0.0366 335 PRO A CD 2576 N N . GLY A 336 ? 0.5886 0.3125 0.6574 -0.1639 -0.2555 0.1236 336 GLY A N 2577 C CA . GLY A 336 ? 0.6673 0.4294 0.7376 -0.1843 -0.2476 0.1549 336 GLY A CA 2578 C C . GLY A 336 ? 0.6282 0.4275 0.6993 -0.1899 -0.2319 0.1508 336 GLY A C 2579 O O . GLY A 336 ? 0.6517 0.4893 0.7311 -0.2071 -0.2240 0.1750 336 GLY A O 2580 N N . PHE A 337 ? 0.5223 0.3158 0.5870 -0.1751 -0.2266 0.1211 337 PHE A N 2581 C CA . PHE A 337 ? 0.5121 0.3422 0.5798 -0.1782 -0.2136 0.1172 337 PHE A CA 2582 C C . PHE A 337 ? 0.5797 0.4158 0.6566 -0.1869 -0.2205 0.1145 337 PHE A C 2583 O O . PHE A 337 ? 0.6884 0.4920 0.7619 -0.1849 -0.2338 0.1017 337 PHE A O 2584 C CB . PHE A 337 ? 0.4596 0.2893 0.5148 -0.1587 -0.2033 0.0911 337 PHE A CB 2585 C CG . PHE A 337 ? 0.5775 0.4242 0.6217 -0.1439 -0.1873 0.0936 337 PHE A CG 2586 C CD1 . PHE A 337 ? 0.5533 0.3715 0.5898 -0.1344 -0.1941 0.0901 337 PHE A CD1 2587 C CD2 . PHE A 337 ? 0.4134 0.3041 0.4566 -0.1385 -0.1673 0.0977 337 PHE A CD2 2588 C CE1 . PHE A 337 ? 0.4411 0.2759 0.4660 -0.1226 -0.1826 0.0917 337 PHE A CE1 2589 C CE2 . PHE A 337 ? 0.6297 0.5330 0.6596 -0.1257 -0.1547 0.0960 337 PHE A CE2 2590 C CZ . PHE A 337 ? 0.4168 0.2929 0.4360 -0.1190 -0.1631 0.0935 337 PHE A CZ 2591 N N . SER A 338 ? 0.5179 0.3975 0.6085 -0.1966 -0.2119 0.1266 338 SER A N 2592 C CA . SER A 338 ? 0.5441 0.4364 0.6461 -0.2060 -0.2191 0.1278 338 SER A CA 2593 C C . SER A 338 ? 0.4562 0.4014 0.5759 -0.2082 -0.2062 0.1366 338 SER A C 2594 O O . SER A 338 ? 0.4852 0.4673 0.6195 -0.2127 -0.1926 0.1547 338 SER A O 2595 C CB . SER A 338 ? 0.5262 0.4164 0.6434 -0.2248 -0.2311 0.1505 338 SER A CB 2596 O OG . SER A 338 ? 0.5325 0.4466 0.6662 -0.2363 -0.2365 0.1567 338 SER A OG 2597 N N . LYS A 339 ? 0.5530 0.5053 0.6729 -0.2047 -0.2102 0.1245 339 LYS A N 2598 C CA . LYS A 339 ? 0.4951 0.4989 0.6390 -0.2050 -0.2011 0.1349 339 LYS A CA 2599 C C . LYS A 339 ? 0.4600 0.5007 0.6349 -0.2220 -0.2013 0.1617 339 LYS A C 2600 O O . LYS A 339 ? 0.4714 0.5639 0.6753 -0.2214 -0.1906 0.1742 339 LYS A O 2601 C CB . LYS A 339 ? 0.4228 0.4239 0.5578 -0.1985 -0.2087 0.1194 339 LYS A CB 2602 C CG . LYS A 339 ? 0.4573 0.4524 0.5955 -0.2123 -0.2257 0.1228 339 LYS A CG 2603 C CD . LYS A 339 ? 0.4616 0.4577 0.5870 -0.2080 -0.2337 0.1097 339 LYS A CD 2604 C CE . LYS A 339 ? 0.4980 0.4949 0.6299 -0.2240 -0.2517 0.1147 339 LYS A CE 2605 N NZ . LYS A 339 ? 0.4903 0.5345 0.6639 -0.2344 -0.2506 0.1423 339 LYS A NZ 2606 N N . ASP A 340 ? 0.4709 0.4870 0.6429 -0.2357 -0.2135 0.1705 340 ASP A N 2607 C CA . ASP A 340 ? 0.5303 0.5788 0.7311 -0.2538 -0.2166 0.1962 340 ASP A CA 2608 C C . ASP A 340 ? 0.5904 0.6609 0.8020 -0.2641 -0.2056 0.2219 340 ASP A C 2609 O O . ASP A 340 ? 0.5179 0.6144 0.7520 -0.2804 -0.2079 0.2450 340 ASP A O 2610 C CB . ASP A 340 ? 0.5335 0.5467 0.7297 -0.2659 -0.2405 0.1921 340 ASP A CB 2611 C CG . ASP A 340 ? 0.5624 0.5679 0.7495 -0.2604 -0.2504 0.1721 340 ASP A CG 2612 O OD1 . ASP A 340 ? 0.5094 0.5569 0.7139 -0.2564 -0.2433 0.1769 340 ASP A OD1 2613 O OD2 . ASP A 340 ? 0.5657 0.5247 0.7284 -0.2595 -0.2652 0.1513 340 ASP A OD2 2614 N N . ASN A 341 ? 0.4821 0.5433 0.6763 -0.2559 -0.1943 0.2190 341 ASN A N 2615 C CA . ASN A 341 ? 0.6549 0.7502 0.8552 -0.2645 -0.1783 0.2443 341 ASN A CA 2616 C C . ASN A 341 ? 0.6052 0.7146 0.7924 -0.2514 -0.1582 0.2368 341 ASN A C 2617 O O . ASN A 341 ? 0.4302 0.5218 0.6054 -0.2325 -0.1573 0.2106 341 ASN A O 2618 C CB . ASN A 341 ? 0.5293 0.5903 0.7186 -0.2778 -0.1931 0.2601 341 ASN A CB 2619 C CG . ASN A 341 ? 0.5744 0.5691 0.7348 -0.2669 -0.2078 0.2402 341 ASN A CG 2620 O OD1 . ASN A 341 ? 0.5299 0.5114 0.6730 -0.2510 -0.2003 0.2212 341 ASN A OD1 2621 N ND2 . ASN A 341 ? 0.7231 0.6769 0.8819 -0.2747 -0.2292 0.2442 341 ASN A ND2 2622 N N . ASN A 342 ? 0.4602 0.6011 0.6423 -0.2563 -0.1403 0.2564 342 ASN A N 2623 C CA . ASN A 342 ? 0.4692 0.6243 0.6247 -0.2285 -0.1162 0.2383 342 ASN A CA 2624 C C . ASN A 342 ? 0.4459 0.5442 0.5632 -0.2146 -0.1250 0.2200 342 ASN A C 2625 O O . ASN A 342 ? 0.4342 0.5392 0.5287 -0.1936 -0.1091 0.2041 342 ASN A O 2626 C CB . ASN A 342 ? 0.4861 0.7016 0.6417 -0.2327 -0.0903 0.2591 342 ASN A CB 2627 C CG . ASN A 342 ? 0.6452 0.8515 0.7883 -0.2581 -0.0989 0.2914 342 ASN A CG 2628 O OD1 . ASN A 342 ? 0.7052 0.8528 0.8388 -0.2685 -0.1250 0.2953 342 ASN A OD1 2629 N ND2 . ASN A 342 ? 0.7889 1.0544 0.9327 -0.2680 -0.0770 0.3155 342 ASN A ND2 2630 N N . SER A 343 ? 0.4723 0.5159 0.5860 -0.2261 -0.1511 0.2217 343 SER A N 2631 C CA . SER A 343 ? 0.4815 0.4717 0.5683 -0.2115 -0.1617 0.2032 343 SER A CA 2632 C C . SER A 343 ? 0.5361 0.5315 0.5954 -0.2036 -0.1518 0.2099 343 SER A C 2633 O O . SER A 343 ? 0.5233 0.5003 0.5629 -0.1826 -0.1490 0.1876 343 SER A O 2634 C CB . SER A 343 ? 0.4607 0.4351 0.5414 -0.1883 -0.1594 0.1683 343 SER A CB 2635 O OG . SER A 343 ? 0.4824 0.4479 0.5809 -0.1963 -0.1724 0.1615 343 SER A OG 2636 N N . ILE A 344 ? 0.5068 0.5295 0.5644 -0.2220 -0.1473 0.2420 344 ILE A N 2637 C CA . ILE A 344 ? 0.5263 0.5529 0.5527 -0.2185 -0.1423 0.2522 344 ILE A CA 2638 C C . ILE A 344 ? 0.5506 0.5150 0.5694 -0.2196 -0.1699 0.2553 344 ILE A C 2639 O O . ILE A 344 ? 0.6439 0.5834 0.6759 -0.2409 -0.1899 0.2814 344 ILE A O 2640 C CB . ILE A 344 ? 0.6718 0.7468 0.6952 -0.2413 -0.1309 0.2904 344 ILE A CB 2641 C CG1 . ILE A 344 ? 0.6032 0.7465 0.6403 -0.2379 -0.1011 0.2867 344 ILE A CG1 2642 C CG2 . ILE A 344 ? 0.6795 0.7573 0.6633 -0.2391 -0.1288 0.3019 344 ILE A CG2 2643 C CD1 . ILE A 344 ? 0.5161 0.6840 0.5288 -0.2093 -0.0774 0.2558 344 ILE A CD1 2644 N N . ILE A 345 ? 0.5365 0.4757 0.5388 -0.1965 -0.1722 0.2291 345 ILE A N 2645 C CA . ILE A 345 ? 0.5584 0.4422 0.5604 -0.1929 -0.1974 0.2291 345 ILE A CA 2646 C C . ILE A 345 ? 0.6664 0.5521 0.6428 -0.1923 -0.2023 0.2473 345 ILE A C 2647 O O . ILE A 345 ? 0.6686 0.5969 0.6198 -0.1896 -0.1838 0.2495 345 ILE A O 2648 C CB . ILE A 345 ? 0.6174 0.4714 0.6241 -0.1688 -0.2002 0.1903 345 ILE A CB 2649 C CG1 . ILE A 345 ? 0.4989 0.3849 0.4883 -0.1491 -0.1783 0.1673 345 ILE A CG1 2650 C CG2 . ILE A 345 ? 0.5205 0.3592 0.5493 -0.1728 -0.2049 0.1760 345 ILE A CG2 2651 C CD1 . ILE A 345 ? 0.4783 0.3375 0.4688 -0.1271 -0.1827 0.1373 345 ILE A CD1 2652 N N . THR A 346 ? 0.7188 0.5576 0.7019 -0.1940 -0.2287 0.2591 346 THR A N 2653 C CA . THR A 346 ? 0.7560 0.5958 0.7192 -0.1918 -0.2377 0.2749 346 THR A CA 2654 C C . THR A 346 ? 0.7553 0.5758 0.7110 -0.1663 -0.2434 0.2491 346 THR A C 2655 O O . THR A 346 ? 0.5949 0.3992 0.5672 -0.1490 -0.2399 0.2154 346 THR A O 2656 C CB . THR A 346 ? 0.7179 0.5334 0.7030 -0.2016 -0.2595 0.2918 346 THR A CB 2657 O OG1 . THR A 346 ? 0.7011 0.4706 0.7167 -0.1894 -0.2753 0.2677 346 THR A OG1 2658 C CG2 . THR A 346 ? 0.7251 0.5696 0.7170 -0.2272 -0.2543 0.3195 346 THR A CG2 2659 N N . ARG A 347 ? 0.7484 0.5779 0.6812 -0.1643 -0.2507 0.2627 347 ARG A N 2660 C CA . ARG A 347 ? 0.7355 0.5511 0.6675 -0.1421 -0.2598 0.2413 347 ARG A CA 2661 C C . ARG A 347 ? 0.6886 0.4566 0.6605 -0.1284 -0.2764 0.2241 347 ARG A C 2662 O O . ARG A 347 ? 0.6469 0.4066 0.6313 -0.1085 -0.2721 0.1925 347 ARG A O 2663 C CB . ARG A 347 ? 0.6749 0.5035 0.5857 -0.1461 -0.2704 0.2614 347 ARG A CB 2664 C CG . ARG A 347 ? 0.7308 0.5460 0.6485 -0.1255 -0.2842 0.2436 347 ARG A CG 2665 C CD . ARG A 347 ? 0.8191 0.6537 0.7118 -0.1316 -0.2928 0.2629 347 ARG A CD 2666 N NE . ARG A 347 ? 0.8921 0.7229 0.7907 -0.1135 -0.3046 0.2455 347 ARG A NE 2667 C CZ . ARG A 347 ? 0.9052 0.7595 0.7808 -0.1048 -0.2972 0.2241 347 ARG A CZ 2668 N NH1 . ARG A 347 ? 0.8404 0.7220 0.6833 -0.1106 -0.2779 0.2157 347 ARG A NH1 2669 N NH2 . ARG A 347 ? 0.9387 0.7909 0.8272 -0.0906 -0.3096 0.2097 347 ARG A NH2 2670 N N . LYS A 348 ? 0.7107 0.4581 0.7052 -0.1383 -0.2898 0.2378 348 LYS A N 2671 C CA . LYS A 348 ? 0.7173 0.4251 0.7485 -0.1249 -0.3044 0.2182 348 LYS A CA 2672 C C . LYS A 348 ? 0.7033 0.3995 0.7458 -0.1158 -0.2935 0.1872 348 LYS A C 2673 O O . LYS A 348 ? 0.6907 0.3684 0.7513 -0.0947 -0.2956 0.1583 348 LYS A O 2674 C CB . LYS A 348 ? 0.7879 0.4791 0.8374 -0.1398 -0.3209 0.2397 348 LYS A CB 2675 C CG . LYS A 348 ? 0.8611 0.5127 0.9461 -0.1234 -0.3380 0.2201 348 LYS A CG 2676 C CD . LYS A 348 ? 0.9570 0.5959 1.0557 -0.1212 -0.3588 0.2385 348 LYS A CD 2677 C CE . LYS A 348 ? 1.0015 0.6200 1.1185 -0.1375 -0.3767 0.2605 348 LYS A CE 2678 N NZ . LYS A 348 ? 1.0719 0.6674 1.2127 -0.1302 -0.4002 0.2719 348 LYS A NZ 2679 N N . GLU A 349 ? 0.7056 0.4180 0.7380 -0.1318 -0.2805 0.1929 349 GLU A N 2680 C CA . GLU A 349 ? 0.6021 0.3087 0.6423 -0.1263 -0.2699 0.1650 349 GLU A CA 2681 C C . GLU A 349 ? 0.6425 0.3646 0.6725 -0.1086 -0.2532 0.1386 349 GLU A C 2682 O O . GLU A 349 ? 0.6274 0.3383 0.6684 -0.0949 -0.2485 0.1082 349 GLU A O 2683 C CB . GLU A 349 ? 0.5999 0.3279 0.6369 -0.1490 -0.2609 0.1797 349 GLU A CB 2684 C CG . GLU A 349 ? 0.7863 0.4999 0.8419 -0.1623 -0.2766 0.1930 349 GLU A CG 2685 C CD . GLU A 349 ? 0.7320 0.4759 0.7880 -0.1867 -0.2689 0.2147 349 GLU A CD 2686 O OE1 . GLU A 349 ? 0.6898 0.4724 0.7298 -0.1974 -0.2528 0.2333 349 GLU A OE1 2687 O OE2 . GLU A 349 ? 0.7800 0.5113 0.8528 -0.1946 -0.2788 0.2134 349 GLU A OE2 2688 N N . PHE A 350 ? 0.5925 0.3518 0.6006 -0.1078 -0.2407 0.1457 350 PHE A N 2689 C CA . PHE A 350 ? 0.5780 0.3597 0.5792 -0.0900 -0.2250 0.1188 350 PHE A CA 2690 C C . PHE A 350 ? 0.5967 0.3526 0.6179 -0.0706 -0.2372 0.1012 350 PHE A C 2691 O O . PHE A 350 ? 0.5329 0.2904 0.5643 -0.0571 -0.2272 0.0734 350 PHE A O 2692 C CB . PHE A 350 ? 0.5461 0.3630 0.5199 -0.0930 -0.2164 0.1295 350 PHE A CB 2693 C CG . PHE A 350 ? 0.5819 0.4187 0.5498 -0.0775 -0.2031 0.1030 350 PHE A CG 2694 C CD1 . PHE A 350 ? 0.4500 0.3119 0.4117 -0.0763 -0.1815 0.0879 350 PHE A CD1 2695 C CD2 . PHE A 350 ? 0.5675 0.3980 0.5400 -0.0651 -0.2142 0.0953 350 PHE A CD2 2696 C CE1 . PHE A 350 ? 0.5379 0.4131 0.4971 -0.0640 -0.1717 0.0654 350 PHE A CE1 2697 C CE2 . PHE A 350 ? 0.5551 0.4032 0.5256 -0.0542 -0.2040 0.0728 350 PHE A CE2 2698 C CZ . PHE A 350 ? 0.4309 0.2989 0.3939 -0.0543 -0.1831 0.0580 350 PHE A CZ 2699 N N . GLN A 351 ? 0.6012 0.3354 0.6306 -0.0695 -0.2591 0.1192 351 GLN A N 2700 C CA . GLN A 351 ? 0.6251 0.3382 0.6810 -0.0490 -0.2717 0.1042 351 GLN A CA 2701 C C . GLN A 351 ? 0.6224 0.3073 0.7029 -0.0380 -0.2710 0.0779 351 GLN A C 2702 O O . GLN A 351 ? 0.5327 0.2246 0.6273 -0.0197 -0.2620 0.0503 351 GLN A O 2703 C CB . GLN A 351 ? 0.6459 0.3434 0.7103 -0.0505 -0.2962 0.1301 351 GLN A CB 2704 C CG . GLN A 351 ? 0.6818 0.4076 0.7207 -0.0546 -0.3003 0.1490 351 GLN A CG 2705 C CD . GLN A 351 ? 0.7044 0.4260 0.7468 -0.0623 -0.3177 0.1743 351 GLN A CD 2706 O OE1 . GLN A 351 ? 0.7319 0.4408 0.7760 -0.0776 -0.3236 0.1938 351 GLN A OE1 2707 N NE2 . GLN A 351 ? 0.6436 0.3772 0.6895 -0.0528 -0.3273 0.1748 351 GLN A NE2 2708 N N . GLU A 352 ? 0.6224 0.2917 0.7055 -0.0498 -0.2751 0.0828 352 GLU A N 2709 C CA . GLU A 352 ? 0.6190 0.2751 0.7154 -0.0408 -0.2701 0.0546 352 GLU A CA 2710 C C . GLU A 352 ? 0.5415 0.2146 0.6249 -0.0388 -0.2495 0.0316 352 GLU A C 2711 O O . GLU A 352 ? 0.6046 0.2761 0.6954 -0.0246 -0.2412 0.0029 352 GLU A O 2712 C CB . GLU A 352 ? 0.6647 0.3040 0.7630 -0.0567 -0.2801 0.0670 352 GLU A CB 2713 C CG . GLU A 352 ? 0.8324 0.4526 0.9471 -0.0597 -0.3018 0.0886 352 GLU A CG 2714 C CD . GLU A 352 ? 0.9611 0.5625 1.1031 -0.0356 -0.3099 0.0677 352 GLU A CD 2715 O OE1 . GLU A 352 ? 1.0159 0.6103 1.1650 -0.0207 -0.3008 0.0354 352 GLU A OE1 2716 O OE2 . GLU A 352 ? 1.0053 0.6016 1.1616 -0.0319 -0.3246 0.0837 352 GLU A OE2 2717 N N . GLY A 353 ? 0.5176 0.2112 0.5812 -0.0537 -0.2402 0.0447 353 GLY A N 2718 C CA . GLY A 353 ? 0.5638 0.2867 0.6158 -0.0518 -0.2185 0.0261 353 GLY A CA 2719 C C . GLY A 353 ? 0.5741 0.3145 0.6316 -0.0327 -0.2069 0.0049 353 GLY A C 2720 O O . GLY A 353 ? 0.5196 0.2684 0.5766 -0.0264 -0.1947 -0.0166 353 GLY A O 2721 N N . LEU A 354 ? 0.5395 0.2883 0.6023 -0.0254 -0.2116 0.0130 354 LEU A N 2722 C CA . LEU A 354 ? 0.4925 0.2608 0.5668 -0.0096 -0.2028 -0.0042 354 LEU A CA 2723 C C . LEU A 354 ? 0.5089 0.2609 0.6073 0.0072 -0.2049 -0.0263 354 LEU A C 2724 O O . LEU A 354 ? 0.4409 0.2132 0.5469 0.0173 -0.1905 -0.0456 354 LEU A O 2725 C CB . LEU A 354 ? 0.4617 0.2414 0.5385 -0.0068 -0.2124 0.0095 354 LEU A CB 2726 C CG . LEU A 354 ? 0.5162 0.3186 0.5659 -0.0196 -0.2070 0.0240 354 LEU A CG 2727 C CD1 . LEU A 354 ? 0.4468 0.2599 0.4961 -0.0164 -0.2193 0.0331 354 LEU A CD1 2728 C CD2 . LEU A 354 ? 0.4945 0.3202 0.5351 -0.0211 -0.1859 0.0094 354 LEU A CD2 2729 N N . LYS A 355 ? 0.4863 0.2022 0.5978 0.0101 -0.2226 -0.0236 355 LYS A N 2730 C CA . LYS A 355 ? 0.5829 0.2842 0.7176 0.0288 -0.2230 -0.0488 355 LYS A CA 2731 C C . LYS A 355 ? 0.5838 0.2899 0.7030 0.0274 -0.2063 -0.0731 355 LYS A C 2732 O O . LYS A 355 ? 0.6102 0.3259 0.7398 0.0432 -0.1948 -0.0993 355 LYS A O 2733 C CB . LYS A 355 ? 0.5811 0.2558 0.7305 0.0307 -0.2413 -0.0391 355 LYS A CB 2734 C CG . LYS A 355 ? 0.7695 0.4434 0.9399 0.0369 -0.2586 -0.0197 355 LYS A CG 2735 C CD . LYS A 355 ? 0.8975 0.5437 1.0798 0.0330 -0.2786 -0.0048 355 LYS A CD 2736 C CE . LYS A 355 ? 0.9611 0.5873 1.1569 0.0445 -0.2759 -0.0313 355 LYS A CE 2737 N NZ . LYS A 355 ? 0.9936 0.6342 1.2123 0.0699 -0.2630 -0.0623 355 LYS A NZ 2738 N N . ILE A 356 ? 0.5230 0.2258 0.6179 0.0081 -0.2055 -0.0630 356 ILE A N 2739 C CA . ILE A 356 ? 0.5359 0.2463 0.6113 0.0025 -0.1930 -0.0803 356 ILE A CA 2740 C C . ILE A 356 ? 0.4796 0.2256 0.5470 0.0057 -0.1733 -0.0901 356 ILE A C 2741 O O . ILE A 356 ? 0.5226 0.2787 0.5837 0.0125 -0.1615 -0.1125 356 ILE A O 2742 C CB . ILE A 356 ? 0.5821 0.2904 0.6391 -0.0199 -0.1973 -0.0614 356 ILE A CB 2743 C CG1 . ILE A 356 ? 0.6538 0.3341 0.7184 -0.0260 -0.2141 -0.0500 356 ILE A CG1 2744 C CG2 . ILE A 356 ? 0.6418 0.3631 0.6789 -0.0268 -0.1867 -0.0758 356 ILE A CG2 2745 C CD1 . ILE A 356 ? 0.6778 0.3369 0.7462 -0.0164 -0.2167 -0.0752 356 ILE A CD1 2746 N N . PHE A 357 ? 0.4312 0.2022 0.4968 0.0005 -0.1676 -0.0717 357 PHE A N 2747 C CA . PHE A 357 ? 0.4010 0.2075 0.4612 0.0012 -0.1491 -0.0756 357 PHE A CA 2748 C C . PHE A 357 ? 0.4872 0.3134 0.5694 0.0161 -0.1420 -0.0844 357 PHE A C 2749 O O . PHE A 357 ? 0.4500 0.3046 0.5320 0.0161 -0.1269 -0.0884 357 PHE A O 2750 C CB . PHE A 357 ? 0.4923 0.3145 0.5406 -0.0118 -0.1461 -0.0555 357 PHE A CB 2751 C CG . PHE A 357 ? 0.4640 0.2832 0.4955 -0.0261 -0.1468 -0.0481 357 PHE A CG 2752 C CD1 . PHE A 357 ? 0.4421 0.2772 0.4628 -0.0301 -0.1365 -0.0536 357 PHE A CD1 2753 C CD2 . PHE A 357 ? 0.5082 0.3117 0.5370 -0.0367 -0.1587 -0.0326 357 PHE A CD2 2754 C CE1 . PHE A 357 ? 0.4759 0.3116 0.4857 -0.0433 -0.1399 -0.0454 357 PHE A CE1 2755 C CE2 . PHE A 357 ? 0.5072 0.3132 0.5270 -0.0510 -0.1601 -0.0244 357 PHE A CE2 2756 C CZ . PHE A 357 ? 0.4768 0.2991 0.4882 -0.0535 -0.1514 -0.0316 357 PHE A CZ 2757 N N . PHE A 358 ? 0.4367 0.2497 0.5414 0.0275 -0.1542 -0.0844 358 PHE A N 2758 C CA . PHE A 358 ? 0.4469 0.2827 0.5804 0.0420 -0.1499 -0.0913 358 PHE A CA 2759 C C . PHE A 358 ? 0.5825 0.4011 0.7442 0.0616 -0.1580 -0.1067 358 PHE A C 2760 O O . PHE A 358 ? 0.5858 0.4012 0.7743 0.0711 -0.1720 -0.0989 358 PHE A O 2761 C CB . PHE A 358 ? 0.3839 0.2303 0.5233 0.0370 -0.1592 -0.0719 358 PHE A CB 2762 C CG . PHE A 358 ? 0.4525 0.3141 0.5684 0.0216 -0.1508 -0.0617 358 PHE A CG 2763 C CD1 . PHE A 358 ? 0.4177 0.2656 0.5083 0.0087 -0.1556 -0.0480 358 PHE A CD1 2764 C CD2 . PHE A 358 ? 0.4247 0.3152 0.5481 0.0202 -0.1380 -0.0656 358 PHE A CD2 2765 C CE1 . PHE A 358 ? 0.3405 0.2029 0.4144 -0.0018 -0.1470 -0.0418 358 PHE A CE1 2766 C CE2 . PHE A 358 ? 0.3209 0.2199 0.4272 0.0080 -0.1322 -0.0578 358 PHE A CE2 2767 C CZ . PHE A 358 ? 0.3662 0.2510 0.4483 -0.0011 -0.1363 -0.0476 358 PHE A CZ 2768 N N . PRO A 359 ? 0.6266 0.4345 0.7827 0.0686 -0.1504 -0.1299 359 PRO A N 2769 C CA . PRO A 359 ? 0.6951 0.4770 0.8761 0.0886 -0.1594 -0.1490 359 PRO A CA 2770 C C . PRO A 359 ? 0.7091 0.5188 0.9328 0.1116 -0.1527 -0.1613 359 PRO A C 2771 O O . PRO A 359 ? 0.7668 0.5542 1.0230 0.1294 -0.1679 -0.1663 359 PRO A O 2772 C CB . PRO A 359 ? 0.7547 0.5258 0.9105 0.0881 -0.1490 -0.1751 359 PRO A CB 2773 C CG . PRO A 359 ? 0.6451 0.4547 0.7737 0.0741 -0.1284 -0.1715 359 PRO A CG 2774 C CD . PRO A 359 ? 0.6043 0.4232 0.7289 0.0584 -0.1342 -0.1403 359 PRO A CD 2775 N N . GLY A 360 ? 0.7098 0.5679 0.9381 0.1113 -0.1317 -0.1643 360 GLY A N 2776 C CA . GLY A 360 ? 0.7510 0.6439 1.0254 0.1316 -0.1238 -0.1744 360 GLY A CA 2777 C C . GLY A 360 ? 0.7249 0.6378 1.0264 0.1281 -0.1362 -0.1501 360 GLY A C 2778 O O . GLY A 360 ? 0.7040 0.6533 1.0480 0.1416 -0.1308 -0.1543 360 GLY A O 2779 N N . VAL A 361 ? 0.6568 0.5489 0.9339 0.1098 -0.1527 -0.1255 361 VAL A N 2780 C CA . VAL A 361 ? 0.5433 0.4526 0.8342 0.1028 -0.1658 -0.1040 361 VAL A CA 2781 C C . VAL A 361 ? 0.5322 0.4198 0.8508 0.1146 -0.1936 -0.0924 361 VAL A C 2782 O O . VAL A 361 ? 0.5038 0.3494 0.8136 0.1174 -0.2078 -0.0895 361 VAL A O 2783 C CB . VAL A 361 ? 0.4710 0.3726 0.7181 0.0780 -0.1678 -0.0858 361 VAL A CB 2784 C CG1 . VAL A 361 ? 0.4451 0.3545 0.6978 0.0710 -0.1863 -0.0663 361 VAL A CG1 2785 C CG2 . VAL A 361 ? 0.3655 0.2927 0.5950 0.0669 -0.1441 -0.0923 361 VAL A CG2 2786 N N . SER A 362 ? 0.4270 0.3431 0.7811 0.1202 -0.2038 -0.0836 362 SER A N 2787 C CA . SER A 362 ? 0.4648 0.3648 0.8470 0.1306 -0.2337 -0.0680 362 SER A CA 2788 C C . SER A 362 ? 0.4789 0.3429 0.8196 0.1127 -0.2550 -0.0424 362 SER A C 2789 O O . SER A 362 ? 0.4712 0.3341 0.7662 0.0917 -0.2466 -0.0360 362 SER A O 2790 C CB . SER A 362 ? 0.4397 0.3827 0.8620 0.1341 -0.2427 -0.0600 362 SER A CB 2791 O OG . SER A 362 ? 0.4601 0.4136 0.8488 0.1103 -0.2475 -0.0448 362 SER A OG 2792 N N . GLU A 363 ? 0.4991 0.3413 0.8484 0.1151 -0.2753 -0.0276 363 GLU A N 2793 C CA . GLU A 363 ? 0.6248 0.4410 0.9371 0.0964 -0.2946 0.0004 363 GLU A CA 2794 C C . GLU A 363 ? 0.5003 0.3406 0.7894 0.0813 -0.3027 0.0166 363 GLU A C 2795 O O . GLU A 363 ? 0.5592 0.3884 0.8039 0.0638 -0.3065 0.0315 363 GLU A O 2796 C CB . GLU A 363 ? 0.6530 0.4491 0.9844 0.1008 -0.3141 0.0147 363 GLU A CB 2797 C CG . GLU A 363 ? 0.8541 0.6090 1.1593 0.0886 -0.3228 0.0287 363 GLU A CG 2798 C CD . GLU A 363 ? 0.9781 0.7129 1.2788 0.0931 -0.3062 0.0053 363 GLU A CD 2799 O OE1 . GLU A 363 ? 1.0087 0.7567 1.3343 0.1113 -0.2897 -0.0234 363 GLU A OE1 2800 O OE2 . GLU A 363 ? 1.0136 0.7225 1.2848 0.0773 -0.3089 0.0159 363 GLU A OE2 2801 N N . PHE A 364 ? 0.4891 0.3647 0.8070 0.0869 -0.3041 0.0122 364 PHE A N 2802 C CA . PHE A 364 ? 0.4772 0.3768 0.7721 0.0710 -0.3109 0.0215 364 PHE A CA 2803 C C . PHE A 364 ? 0.4445 0.3517 0.7070 0.0588 -0.2916 0.0099 364 PHE A C 2804 O O . PHE A 364 ? 0.4459 0.3526 0.6649 0.0415 -0.2942 0.0181 364 PHE A O 2805 C CB . PHE A 364 ? 0.4735 0.4100 0.8099 0.0772 -0.3144 0.0170 364 PHE A CB 2806 C CG . PHE A 364 ? 0.5778 0.5374 0.8912 0.0596 -0.3191 0.0201 364 PHE A CG 2807 C CD1 . PHE A 364 ? 0.4928 0.4443 0.7667 0.0454 -0.3368 0.0384 364 PHE A CD1 2808 C CD2 . PHE A 364 ? 0.4318 0.4208 0.7618 0.0562 -0.3050 0.0040 364 PHE A CD2 2809 C CE1 . PHE A 364 ? 0.6161 0.5857 0.8650 0.0300 -0.3401 0.0362 364 PHE A CE1 2810 C CE2 . PHE A 364 ? 0.4304 0.4341 0.7385 0.0386 -0.3094 0.0042 364 PHE A CE2 2811 C CZ . PHE A 364 ? 0.4613 0.4539 0.7278 0.0267 -0.3268 0.0180 364 PHE A CZ 2812 N N . GLY A 365 ? 0.4309 0.3453 0.7081 0.0657 -0.2659 -0.0110 365 GLY A N 2813 C CA . GLY A 365 ? 0.3966 0.3163 0.6418 0.0524 -0.2416 -0.0217 365 GLY A CA 2814 C C . GLY A 365 ? 0.4248 0.3160 0.6214 0.0400 -0.2388 -0.0133 365 GLY A C 2815 O O . GLY A 365 ? 0.3921 0.2881 0.5555 0.0258 -0.2311 -0.0124 365 GLY A O 2816 N N . LYS A 366 ? 0.4242 0.2862 0.6202 0.0455 -0.2458 -0.0072 366 LYS A N 2817 C CA . LYS A 366 ? 0.4560 0.2948 0.6122 0.0319 -0.2433 0.0031 366 LYS A CA 2818 C C . LYS A 366 ? 0.4741 0.3134 0.5989 0.0181 -0.2586 0.0257 366 LYS A C 2819 O O . LYS A 366 ? 0.4464 0.2884 0.5344 0.0040 -0.2483 0.0298 366 LYS A O 2820 C CB . LYS A 366 ? 0.4558 0.2602 0.6221 0.0385 -0.2492 0.0040 366 LYS A CB 2821 C CG . LYS A 366 ? 0.6049 0.4077 0.7867 0.0492 -0.2304 -0.0222 366 LYS A CG 2822 C CD . LYS A 366 ? 0.6739 0.4371 0.8587 0.0528 -0.2378 -0.0250 366 LYS A CD 2823 C CE . LYS A 366 ? 0.7759 0.5217 1.0043 0.0747 -0.2539 -0.0309 366 LYS A CE 2824 N NZ . LYS A 366 ? 0.7473 0.5249 1.0079 0.0938 -0.2384 -0.0557 366 LYS A NZ 2825 N N . GLU A 367 ? 0.4722 0.3124 0.6121 0.0228 -0.2828 0.0401 367 GLU A N 2826 C CA . GLU A 367 ? 0.5818 0.4275 0.6884 0.0095 -0.2997 0.0619 367 GLU A CA 2827 C C . GLU A 367 ? 0.4790 0.3510 0.5579 -0.0003 -0.2885 0.0501 367 GLU A C 2828 O O . GLU A 367 ? 0.5797 0.4556 0.6150 -0.0139 -0.2858 0.0581 367 GLU A O 2829 C CB . GLU A 367 ? 0.5256 0.3726 0.6558 0.0159 -0.3253 0.0770 367 GLU A CB 2830 C CG . GLU A 367 ? 0.9684 0.7856 1.1161 0.0200 -0.3360 0.0928 367 GLU A CG 2831 C CD . GLU A 367 ? 1.0654 0.8872 1.2262 0.0208 -0.3561 0.1102 367 GLU A CD 2832 O OE1 . GLU A 367 ? 1.0419 0.8796 1.2423 0.0345 -0.3605 0.0995 367 GLU A OE1 2833 O OE2 . GLU A 367 ? 1.1495 0.9622 1.2822 0.0070 -0.3673 0.1360 367 GLU A OE2 2834 N N . SER A 368 ? 0.4548 0.3454 0.5610 0.0064 -0.2818 0.0308 368 SER A N 2835 C CA . SER A 368 ? 0.4438 0.3534 0.5300 -0.0029 -0.2743 0.0180 368 SER A CA 2836 C C . SER A 368 ? 0.4273 0.3320 0.4830 -0.0104 -0.2492 0.0085 368 SER A C 2837 O O . SER A 368 ? 0.4341 0.3458 0.4576 -0.0194 -0.2454 0.0033 368 SER A O 2838 C CB . SER A 368 ? 0.4401 0.3704 0.5687 0.0032 -0.2735 0.0029 368 SER A CB 2839 O OG . SER A 368 ? 0.4066 0.3387 0.5510 0.0068 -0.2483 -0.0120 368 SER A OG 2840 N N . ILE A 369 ? 0.4105 0.3033 0.4765 -0.0060 -0.2335 0.0054 369 ILE A N 2841 C CA . ILE A 369 ? 0.5574 0.4468 0.5983 -0.0129 -0.2133 0.0009 369 ILE A CA 2842 C C . ILE A 369 ? 0.4225 0.3082 0.4251 -0.0230 -0.2172 0.0174 369 ILE A C 2843 O O . ILE A 369 ? 0.4234 0.3190 0.3984 -0.0296 -0.2060 0.0129 369 ILE A O 2844 C CB . ILE A 369 ? 0.3816 0.2595 0.4388 -0.0079 -0.1999 -0.0041 369 ILE A CB 2845 C CG1 . ILE A 369 ? 0.4183 0.3073 0.5083 0.0009 -0.1914 -0.0201 369 ILE A CG1 2846 C CG2 . ILE A 369 ? 0.3713 0.2485 0.4052 -0.0160 -0.1829 -0.0050 369 ILE A CG2 2847 C CD1 . ILE A 369 ? 0.4141 0.2944 0.5151 0.0065 -0.1793 -0.0278 369 ILE A CD1 2848 N N . LEU A 370 ? 0.4466 0.3195 0.4498 -0.0239 -0.2333 0.0372 370 LEU A N 2849 C CA . LEU A 370 ? 0.5448 0.4172 0.5135 -0.0361 -0.2373 0.0585 370 LEU A CA 2850 C C . LEU A 370 ? 0.4969 0.3895 0.4309 -0.0427 -0.2432 0.0600 370 LEU A C 2851 O O . LEU A 370 ? 0.5473 0.4530 0.4458 -0.0519 -0.2319 0.0635 370 LEU A O 2852 C CB . LEU A 370 ? 0.5729 0.4234 0.5540 -0.0368 -0.2576 0.0830 370 LEU A CB 2853 C CG . LEU A 370 ? 0.6048 0.4565 0.5518 -0.0530 -0.2637 0.1124 370 LEU A CG 2854 C CD1 . LEU A 370 ? 0.6844 0.5072 0.6495 -0.0570 -0.2715 0.1310 370 LEU A CD1 2855 C CD2 . LEU A 370 ? 0.6291 0.4897 0.5571 -0.0569 -0.2866 0.1307 370 LEU A CD2 2856 N N . PHE A 371 ? 0.5052 0.4027 0.4498 -0.0381 -0.2611 0.0561 371 PHE A N 2857 C CA . PHE A 371 ? 0.5322 0.4477 0.4417 -0.0450 -0.2704 0.0535 371 PHE A CA 2858 C C . PHE A 371 ? 0.5202 0.4472 0.4087 -0.0467 -0.2487 0.0280 371 PHE A C 2859 O O . PHE A 371 ? 0.5484 0.4889 0.3933 -0.0540 -0.2450 0.0258 371 PHE A O 2860 C CB . PHE A 371 ? 0.5375 0.4580 0.4716 -0.0398 -0.2938 0.0494 371 PHE A CB 2861 C CG . PHE A 371 ? 0.6740 0.6114 0.5708 -0.0482 -0.3057 0.0459 371 PHE A CG 2862 C CD1 . PHE A 371 ? 0.7212 0.6650 0.5877 -0.0555 -0.3181 0.0695 371 PHE A CD1 2863 C CD2 . PHE A 371 ? 0.6256 0.5722 0.5194 -0.0490 -0.3009 0.0182 371 PHE A CD2 2864 C CE1 . PHE A 371 ? 0.8016 0.7640 0.6309 -0.0626 -0.3257 0.0637 371 PHE A CE1 2865 C CE2 . PHE A 371 ? 0.6577 0.6187 0.5169 -0.0561 -0.3093 0.0108 371 PHE A CE2 2866 C CZ . PHE A 371 ? 0.7115 0.6823 0.5364 -0.0625 -0.3219 0.0326 371 PHE A CZ 2867 N N . HIS A 372 ? 0.4832 0.4053 0.4029 -0.0395 -0.2346 0.0088 372 HIS A N 2868 C CA . HIS A 372 ? 0.5335 0.4615 0.4421 -0.0395 -0.2183 -0.0151 372 HIS A CA 2869 C C . HIS A 372 ? 0.5308 0.4627 0.4180 -0.0412 -0.1955 -0.0148 372 HIS A C 2870 O O . HIS A 372 ? 0.5252 0.4662 0.3886 -0.0415 -0.1848 -0.0306 372 HIS A O 2871 C CB . HIS A 372 ? 0.5263 0.4491 0.4766 -0.0335 -0.2127 -0.0307 372 HIS A CB 2872 C CG . HIS A 372 ? 0.7574 0.6809 0.7024 -0.0343 -0.2040 -0.0536 372 HIS A CG 2873 N ND1 . HIS A 372 ? 0.8364 0.7623 0.7787 -0.0380 -0.2189 -0.0677 372 HIS A ND1 2874 C CD2 . HIS A 372 ? 0.7796 0.6994 0.7245 -0.0318 -0.1843 -0.0645 372 HIS A CD2 2875 C CE1 . HIS A 372 ? 0.7917 0.7111 0.7323 -0.0377 -0.2086 -0.0878 372 HIS A CE1 2876 N NE2 . HIS A 372 ? 0.7811 0.6973 0.7242 -0.0329 -0.1874 -0.0854 372 HIS A NE2 2877 N N . TYR A 373 ? 0.4590 0.3850 0.3574 -0.0420 -0.1890 0.0020 373 TYR A N 2878 C CA . TYR A 373 ? 0.5193 0.4530 0.4077 -0.0443 -0.1683 0.0040 373 TYR A CA 2879 C C . TYR A 373 ? 0.5658 0.5125 0.4234 -0.0544 -0.1673 0.0263 373 TYR A C 2880 O O . TYR A 373 ? 0.5888 0.5485 0.4414 -0.0576 -0.1499 0.0304 373 TYR A O 2881 C CB . TYR A 373 ? 0.4194 0.3407 0.3406 -0.0411 -0.1603 0.0059 373 TYR A CB 2882 C CG . TYR A 373 ? 0.4445 0.3634 0.3872 -0.0339 -0.1503 -0.0146 373 TYR A CG 2883 C CD1 . TYR A 373 ? 0.3884 0.2998 0.3543 -0.0293 -0.1588 -0.0237 373 TYR A CD1 2884 C CD2 . TYR A 373 ? 0.4062 0.3328 0.3492 -0.0321 -0.1329 -0.0223 373 TYR A CD2 2885 C CE1 . TYR A 373 ? 0.4152 0.3257 0.4009 -0.0257 -0.1501 -0.0376 373 TYR A CE1 2886 C CE2 . TYR A 373 ? 0.3626 0.2845 0.3263 -0.0266 -0.1264 -0.0366 373 TYR A CE2 2887 C CZ . TYR A 373 ? 0.4074 0.3207 0.3907 -0.0248 -0.1351 -0.0430 373 TYR A CZ 2888 O OH . TYR A 373 ? 0.3442 0.2540 0.3481 -0.0224 -0.1293 -0.0525 373 TYR A OH 2889 N N . THR A 374 ? 0.5375 0.4839 0.3771 -0.0606 -0.1866 0.0436 374 THR A N 2890 C CA . THR A 374 ? 0.6848 0.6436 0.4967 -0.0734 -0.1873 0.0719 374 THR A CA 2891 C C . THR A 374 ? 0.7830 0.7636 0.5465 -0.0806 -0.1939 0.0769 374 THR A C 2892 O O . THR A 374 ? 0.7842 0.7746 0.5237 -0.0933 -0.2007 0.1067 374 THR A O 2893 C CB . THR A 374 ? 0.7648 0.7005 0.5981 -0.0790 -0.2061 0.1013 374 THR A CB 2894 O OG1 . THR A 374 ? 0.8056 0.7265 0.6502 -0.0734 -0.2312 0.1034 374 THR A OG1 2895 C CG2 . THR A 374 ? 0.7686 0.6851 0.6407 -0.0744 -0.1981 0.0960 374 THR A CG2 2896 N N . ASP A 375 ? 0.8698 0.8578 0.6169 -0.0741 -0.1934 0.0490 375 ASP A N 2897 C CA . ASP A 375 ? 0.9729 0.9863 0.6649 -0.0812 -0.1941 0.0477 375 ASP A CA 2898 C C . ASP A 375 ? 1.0500 1.0907 0.7207 -0.0805 -0.1625 0.0362 375 ASP A C 2899 O O . ASP A 375 ? 1.0277 1.0713 0.6990 -0.0695 -0.1479 0.0020 375 ASP A O 2900 C CB . ASP A 375 ? 0.9890 0.9994 0.6674 -0.0764 -0.2087 0.0203 375 ASP A CB 2901 C CG . ASP A 375 ? 1.1417 1.1784 0.7557 -0.0844 -0.2112 0.0167 375 ASP A CG 2902 O OD1 . ASP A 375 ? 1.1899 1.2435 0.7777 -0.0798 -0.1890 -0.0105 375 ASP A OD1 2903 O OD2 . ASP A 375 ? 1.1957 1.2373 0.7849 -0.0948 -0.2354 0.0412 375 ASP A OD2 2904 N N . TRP A 376 ? 1.0915 1.1526 0.7484 -0.0920 -0.1526 0.0656 376 TRP A N 2905 C CA . TRP A 376 ? 1.1125 1.2091 0.7521 -0.0917 -0.1214 0.0582 376 TRP A CA 2906 C C . TRP A 376 ? 1.2607 1.3889 0.8394 -0.0934 -0.1151 0.0436 376 TRP A C 2907 O O . TRP A 376 ? 1.2634 1.3891 0.8072 -0.1009 -0.1377 0.0513 376 TRP A O 2908 C CB . TRP A 376 ? 1.0526 1.1666 0.6996 -0.1069 -0.1128 0.0974 376 TRP A CB 2909 C CG . TRP A 376 ? 0.9799 1.0585 0.6680 -0.1128 -0.1327 0.1234 376 TRP A CG 2910 C CD1 . TRP A 376 ? 1.0019 1.0680 0.6855 -0.1278 -0.1553 0.1618 376 TRP A CD1 2911 C CD2 . TRP A 376 ? 0.8894 0.9391 0.6288 -0.1035 -0.1327 0.1120 376 TRP A CD2 2912 N NE1 . TRP A 376 ? 0.9665 0.9951 0.6975 -0.1264 -0.1687 0.1708 376 TRP A NE1 2913 C CE2 . TRP A 376 ? 0.8800 0.9002 0.6425 -0.1121 -0.1543 0.1401 376 TRP A CE2 2914 C CE3 . TRP A 376 ? 0.8574 0.9027 0.6242 -0.0888 -0.1175 0.0815 376 TRP A CE3 2915 C CZ2 . TRP A 376 ? 0.8387 0.8279 0.6461 -0.1060 -0.1591 0.1343 376 TRP A CZ2 2916 C CZ3 . TRP A 376 ? 0.8029 0.8198 0.6129 -0.0848 -0.1232 0.0807 376 TRP A CZ3 2917 C CH2 . TRP A 376 ? 0.8058 0.7962 0.6333 -0.0932 -0.1428 0.1049 376 TRP A CH2 2918 N N . VAL A 377 ? 1.3182 1.4776 0.8848 -0.0855 -0.0845 0.0214 377 VAL A N 2919 C CA . VAL A 377 ? 1.3715 1.5674 0.8773 -0.0853 -0.0716 0.0030 377 VAL A CA 2920 C C . VAL A 377 ? 1.3880 1.6225 0.8512 -0.1064 -0.0688 0.0449 377 VAL A C 2921 O O . VAL A 377 ? 1.3793 1.6029 0.8210 -0.1211 -0.0965 0.0744 377 VAL A O 2922 C CB . VAL A 377 ? 1.3738 1.5938 0.8878 -0.0675 -0.0370 -0.0334 377 VAL A CB 2923 C CG1 . VAL A 377 ? 1.3416 1.5234 0.8828 -0.0483 -0.0434 -0.0774 377 VAL A CG1 2924 C CG2 . VAL A 377 ? 1.3339 1.5713 0.8947 -0.0688 -0.0162 -0.0106 377 VAL A CG2 2925 N N . GLN A 380 ? 1.1774 1.3990 0.7984 -0.1937 -0.0891 0.2681 380 GLN A N 2926 C CA . GLN A 380 ? 1.2271 1.5082 0.8372 -0.1896 -0.0503 0.2516 380 GLN A CA 2927 C C . GLN A 380 ? 1.1273 1.4144 0.7961 -0.1895 -0.0353 0.2529 380 GLN A C 2928 O O . GLN A 380 ? 1.0594 1.3605 0.7480 -0.2121 -0.0356 0.2928 380 GLN A O 2929 C CB . GLN A 380 ? 1.2751 1.5622 0.8613 -0.1635 -0.0370 0.1976 380 GLN A CB 2930 C CG . GLN A 380 ? 1.2962 1.6478 0.8566 -0.1567 0.0020 0.1777 380 GLN A CG 2931 C CD . GLN A 380 ? 1.2749 1.6191 0.8294 -0.1279 0.0129 0.1194 380 GLN A CD 2932 O OE1 . GLN A 380 ? 1.3098 1.6155 0.8468 -0.1195 -0.0090 0.0979 380 GLN A OE1 2933 N NE2 . GLN A 380 ? 1.2358 1.6160 0.8099 -0.1129 0.0454 0.0944 380 GLN A NE2 2934 N N . ARG A 381 ? 1.0858 1.3616 0.7830 -0.1656 -0.0247 0.2109 381 ARG A N 2935 C CA . ARG A 381 ? 0.9860 1.2688 0.7379 -0.1629 -0.0124 0.2080 381 ARG A CA 2936 C C . ARG A 381 ? 0.8565 1.0873 0.6491 -0.1735 -0.0401 0.2279 381 ARG A C 2937 O O . ARG A 381 ? 0.8468 1.0252 0.6403 -0.1660 -0.0644 0.2176 381 ARG A O 2938 C CB . ARG A 381 ? 1.0083 1.2892 0.7764 -0.1339 0.0027 0.1595 381 ARG A CB 2939 C CG . ARG A 381 ? 1.1024 1.4315 0.8368 -0.1195 0.0316 0.1321 381 ARG A CG 2940 C CD . ARG A 381 ? 1.1642 1.4734 0.9130 -0.0903 0.0374 0.0829 381 ARG A CD 2941 N NE . ARG A 381 ? 1.1745 1.4817 0.9817 -0.0808 0.0442 0.0766 381 ARG A NE 2942 C CZ . ARG A 381 ? 1.1405 1.3990 0.9797 -0.0737 0.0257 0.0670 381 ARG A CZ 2943 N NH1 . ARG A 381 ? 1.1344 1.3439 0.9580 -0.0738 0.0012 0.0615 381 ARG A NH1 2944 N NH2 . ARG A 381 ? 1.0824 1.3451 0.9698 -0.0667 0.0315 0.0641 381 ARG A NH2 2945 N N . PRO A 382 ? 0.8064 1.0536 0.6346 -0.1907 -0.0365 0.2543 382 PRO A N 2946 C CA . PRO A 382 ? 0.7452 0.9450 0.6096 -0.2044 -0.0632 0.2741 382 PRO A CA 2947 C C . PRO A 382 ? 0.6645 0.8211 0.5591 -0.1850 -0.0728 0.2405 382 PRO A C 2948 O O . PRO A 382 ? 0.6800 0.7851 0.5902 -0.1888 -0.0983 0.2450 382 PRO A O 2949 C CB . PRO A 382 ? 0.7453 0.9874 0.6404 -0.2267 -0.0513 0.3044 382 PRO A CB 2950 C CG . PRO A 382 ? 0.7735 1.0882 0.6412 -0.2285 -0.0191 0.3103 382 PRO A CG 2951 C CD . PRO A 382 ? 0.8086 1.1247 0.6470 -0.1981 -0.0059 0.2651 382 PRO A CD 2952 N N . GLU A 383 ? 0.5426 0.7202 0.4455 -0.1643 -0.0528 0.2079 383 GLU A N 2953 C CA . GLU A 383 ? 0.5546 0.6964 0.4835 -0.1477 -0.0608 0.1798 383 GLU A CA 2954 C C . GLU A 383 ? 0.5643 0.6730 0.4719 -0.1280 -0.0685 0.1507 383 GLU A C 2955 O O . GLU A 383 ? 0.5021 0.5884 0.4272 -0.1129 -0.0709 0.1259 383 GLU A O 2956 C CB . GLU A 383 ? 0.5737 0.7512 0.5324 -0.1373 -0.0401 0.1649 383 GLU A CB 2957 C CG . GLU A 383 ? 0.7009 0.9175 0.6432 -0.1185 -0.0140 0.1417 383 GLU A CG 2958 C CD . GLU A 383 ? 0.8446 1.1230 0.7767 -0.1293 0.0087 0.1611 383 GLU A CD 2959 O OE1 . GLU A 383 ? 0.9266 1.2276 0.8812 -0.1508 0.0082 0.1930 383 GLU A OE1 2960 O OE2 . GLU A 383 ? 0.8975 1.2038 0.7989 -0.1170 0.0275 0.1437 383 GLU A OE2 2961 N N . ASN A 384 ? 0.6147 0.7229 0.4854 -0.1301 -0.0735 0.1563 384 ASN A N 2962 C CA . ASN A 384 ? 0.6013 0.6816 0.4534 -0.1147 -0.0840 0.1322 384 ASN A CA 2963 C C . ASN A 384 ? 0.4937 0.5245 0.3712 -0.1091 -0.1047 0.1242 384 ASN A C 2964 O O . ASN A 384 ? 0.4673 0.4844 0.3550 -0.0931 -0.1030 0.0966 384 ASN A O 2965 C CB . ASN A 384 ? 0.6581 0.7425 0.4687 -0.1229 -0.0941 0.1478 384 ASN A CB 2966 C CG . ASN A 384 ? 0.7638 0.8943 0.5360 -0.1196 -0.0723 0.1373 384 ASN A CG 2967 O OD1 . ASN A 384 ? 0.7388 0.8868 0.5156 -0.1038 -0.0527 0.1070 384 ASN A OD1 2968 N ND2 . ASN A 384 ? 0.8244 0.9742 0.5574 -0.1341 -0.0765 0.1620 384 ASN A ND2 2969 N N . TYR A 385 ? 0.5050 0.5099 0.3937 -0.1222 -0.1238 0.1483 385 TYR A N 2970 C CA . TYR A 385 ? 0.5455 0.5052 0.4568 -0.1152 -0.1425 0.1386 385 TYR A CA 2971 C C . TYR A 385 ? 0.4854 0.4383 0.4254 -0.1098 -0.1360 0.1219 385 TYR A C 2972 O O . TYR A 385 ? 0.4323 0.3643 0.3829 -0.0963 -0.1395 0.0996 385 TYR A O 2973 C CB . TYR A 385 ? 0.5628 0.4920 0.4799 -0.1284 -0.1665 0.1661 385 TYR A CB 2974 C CG . TYR A 385 ? 0.6379 0.5637 0.5298 -0.1296 -0.1805 0.1806 385 TYR A CG 2975 C CD1 . TYR A 385 ? 0.6030 0.5086 0.4958 -0.1139 -0.1929 0.1632 385 TYR A CD1 2976 C CD2 . TYR A 385 ? 0.5907 0.5376 0.4590 -0.1479 -0.1822 0.2141 385 TYR A CD2 2977 C CE1 . TYR A 385 ? 0.6180 0.5227 0.4897 -0.1155 -0.2092 0.1779 385 TYR A CE1 2978 C CE2 . TYR A 385 ? 0.6258 0.5711 0.4676 -0.1503 -0.1978 0.2301 385 TYR A CE2 2979 C CZ . TYR A 385 ? 0.6182 0.5414 0.4624 -0.1336 -0.2125 0.2114 385 TYR A CZ 2980 O OH . TYR A 385 ? 0.6581 0.5817 0.4780 -0.1364 -0.2312 0.2285 385 TYR A OH 2981 N N . ARG A 386 ? 0.4880 0.4628 0.4405 -0.1214 -0.1267 0.1343 386 ARG A N 2982 C CA . ARG A 386 ? 0.4377 0.4130 0.4151 -0.1178 -0.1215 0.1211 386 ARG A CA 2983 C C . ARG A 386 ? 0.3973 0.3820 0.3744 -0.0980 -0.1080 0.0929 386 ARG A C 2984 O O . ARG A 386 ? 0.3774 0.3424 0.3667 -0.0899 -0.1123 0.0770 386 ARG A O 2985 C CB . ARG A 386 ? 0.4289 0.4392 0.4216 -0.1330 -0.1119 0.1403 386 ARG A CB 2986 C CG . ARG A 386 ? 0.4111 0.4278 0.4304 -0.1304 -0.1089 0.1298 386 ARG A CG 2987 C CD . ARG A 386 ? 0.4222 0.4855 0.4617 -0.1426 -0.0967 0.1480 386 ARG A CD 2988 N NE . ARG A 386 ? 0.4170 0.5228 0.4552 -0.1276 -0.0724 0.1373 386 ARG A NE 2989 C CZ . ARG A 386 ? 0.4563 0.6138 0.5084 -0.1332 -0.0550 0.1510 386 ARG A CZ 2990 N NH1 . ARG A 386 ? 0.4928 0.6680 0.5621 -0.1567 -0.0600 0.1797 386 ARG A NH1 2991 N NH2 . ARG A 386 ? 0.3993 0.5918 0.4508 -0.1154 -0.0325 0.1355 386 ARG A NH2 2992 N N . GLU A 387 ? 0.4020 0.4157 0.3641 -0.0910 -0.0923 0.0869 387 GLU A N 2993 C CA . GLU A 387 ? 0.4374 0.4565 0.4024 -0.0731 -0.0811 0.0609 387 GLU A CA 2994 C C . GLU A 387 ? 0.4579 0.4474 0.4142 -0.0633 -0.0915 0.0439 387 GLU A C 2995 O O . GLU A 387 ? 0.3588 0.3387 0.3277 -0.0526 -0.0896 0.0264 387 GLU A O 2996 C CB . GLU A 387 ? 0.4386 0.4951 0.3904 -0.0670 -0.0616 0.0548 387 GLU A CB 2997 C CG . GLU A 387 ? 0.6087 0.7046 0.5757 -0.0755 -0.0478 0.0717 387 GLU A CG 2998 C CD . GLU A 387 ? 0.7747 0.9086 0.7443 -0.0612 -0.0246 0.0560 387 GLU A CD 2999 O OE1 . GLU A 387 ? 0.8521 0.9875 0.7952 -0.0506 -0.0182 0.0372 387 GLU A OE1 3000 O OE2 . GLU A 387 ? 0.8375 1.0003 0.8376 -0.0601 -0.0138 0.0613 387 GLU A OE2 3001 N N . ALA A 388 ? 0.4131 0.3907 0.3504 -0.0679 -0.1035 0.0519 388 ALA A N 3002 C CA . ALA A 388 ? 0.3959 0.3503 0.3301 -0.0596 -0.1153 0.0385 388 ALA A CA 3003 C C . ALA A 388 ? 0.3743 0.3037 0.3328 -0.0560 -0.1232 0.0324 388 ALA A C 3004 O O . ALA A 388 ? 0.3591 0.2810 0.3265 -0.0467 -0.1229 0.0155 388 ALA A O 3005 C CB . ALA A 388 ? 0.4249 0.3730 0.3389 -0.0658 -0.1303 0.0529 388 ALA A CB 3006 N N . LEU A 389 ? 0.3774 0.2948 0.3460 -0.0645 -0.1302 0.0455 389 LEU A N 3007 C CA . LEU A 389 ? 0.3783 0.2729 0.3644 -0.0606 -0.1370 0.0363 389 LEU A CA 3008 C C . LEU A 389 ? 0.3824 0.2862 0.3790 -0.0556 -0.1256 0.0230 389 LEU A C 3009 O O . LEU A 389 ? 0.4090 0.3038 0.4132 -0.0479 -0.1259 0.0095 389 LEU A O 3010 C CB . LEU A 389 ? 0.3827 0.2578 0.3758 -0.0712 -0.1494 0.0497 389 LEU A CB 3011 C CG . LEU A 389 ? 0.3838 0.2308 0.3899 -0.0650 -0.1588 0.0363 389 LEU A CG 3012 C CD1 . LEU A 389 ? 0.4254 0.2614 0.4353 -0.0526 -0.1656 0.0279 389 LEU A CD1 3013 C CD2 . LEU A 389 ? 0.4913 0.3135 0.5044 -0.0763 -0.1732 0.0468 389 LEU A CD2 3014 N N . GLY A 390 ? 0.4091 0.3336 0.4083 -0.0599 -0.1158 0.0289 390 GLY A N 3015 C CA . GLY A 390 ? 0.3756 0.3099 0.3865 -0.0545 -0.1073 0.0201 390 GLY A CA 3016 C C . GLY A 390 ? 0.3542 0.2880 0.3649 -0.0429 -0.1019 0.0052 390 GLY A C 3017 O O . GLY A 390 ? 0.2977 0.2254 0.3176 -0.0389 -0.1016 -0.0024 390 GLY A O 3018 N N . ASP A 391 ? 0.3281 0.2689 0.3272 -0.0393 -0.0988 0.0015 391 ASP A N 3019 C CA . ASP A 391 ? 0.3173 0.2548 0.3172 -0.0304 -0.0966 -0.0141 391 ASP A CA 3020 C C . ASP A 391 ? 0.4023 0.3232 0.4068 -0.0291 -0.1062 -0.0199 391 ASP A C 3021 O O . ASP A 391 ? 0.3038 0.2208 0.3208 -0.0252 -0.1049 -0.0286 391 ASP A O 3022 C CB . ASP A 391 ? 0.3373 0.2861 0.3186 -0.0276 -0.0926 -0.0200 391 ASP A CB 3023 C CG . ASP A 391 ? 0.4425 0.4131 0.4268 -0.0233 -0.0780 -0.0220 391 ASP A CG 3024 O OD1 . ASP A 391 ? 0.4432 0.4147 0.4496 -0.0181 -0.0731 -0.0246 391 ASP A OD1 3025 O OD2 . ASP A 391 ? 0.4824 0.4718 0.4482 -0.0246 -0.0713 -0.0199 391 ASP A OD2 3026 N N . VAL A 392 ? 0.4023 0.3149 0.4005 -0.0323 -0.1161 -0.0134 392 VAL A N 3027 C CA . VAL A 392 ? 0.4204 0.3216 0.4300 -0.0290 -0.1243 -0.0185 392 VAL A CA 3028 C C . VAL A 392 ? 0.4173 0.3169 0.4416 -0.0276 -0.1186 -0.0232 392 VAL A C 3029 O O . VAL A 392 ? 0.2952 0.1976 0.3316 -0.0244 -0.1165 -0.0307 392 VAL A O 3030 C CB . VAL A 392 ? 0.3893 0.2785 0.3963 -0.0308 -0.1368 -0.0093 392 VAL A CB 3031 C CG1 . VAL A 392 ? 0.3293 0.2088 0.3553 -0.0243 -0.1415 -0.0169 392 VAL A CG1 3032 C CG2 . VAL A 392 ? 0.3520 0.2443 0.3447 -0.0318 -0.1462 -0.0037 392 VAL A CG2 3033 N N . VAL A 393 ? 0.3024 0.1998 0.3246 -0.0320 -0.1168 -0.0176 393 VAL A N 3034 C CA . VAL A 393 ? 0.3027 0.2000 0.3311 -0.0322 -0.1130 -0.0219 393 VAL A CA 3035 C C . VAL A 393 ? 0.2960 0.2047 0.3310 -0.0317 -0.1047 -0.0223 393 VAL A C 3036 O O . VAL A 393 ? 0.3247 0.2370 0.3662 -0.0311 -0.1012 -0.0257 393 VAL A O 3037 C CB . VAL A 393 ? 0.3045 0.1956 0.3269 -0.0391 -0.1168 -0.0167 393 VAL A CB 3038 C CG1 . VAL A 393 ? 0.3153 0.2105 0.3368 -0.0409 -0.1133 -0.0210 393 VAL A CG1 3039 C CG2 . VAL A 393 ? 0.3225 0.1943 0.3436 -0.0389 -0.1276 -0.0178 393 VAL A CG2 3040 N N . GLY A 394 ? 0.2854 0.2007 0.3206 -0.0317 -0.1014 -0.0181 394 GLY A N 3041 C CA . GLY A 394 ? 0.3061 0.2272 0.3523 -0.0298 -0.0963 -0.0171 394 GLY A CA 3042 C C . GLY A 394 ? 0.3603 0.2768 0.4153 -0.0264 -0.0963 -0.0249 394 GLY A C 3043 O O . GLY A 394 ? 0.2762 0.1929 0.3437 -0.0277 -0.0948 -0.0223 394 GLY A O 3044 N N . ASP A 395 ? 0.2841 0.1971 0.3332 -0.0241 -0.1000 -0.0324 395 ASP A N 3045 C CA . ASP A 395 ? 0.3043 0.2128 0.3628 -0.0230 -0.1034 -0.0410 395 ASP A CA 3046 C C . ASP A 395 ? 0.2829 0.1944 0.3549 -0.0262 -0.1054 -0.0400 395 ASP A C 3047 O O . ASP A 395 ? 0.2835 0.1954 0.3720 -0.0294 -0.1052 -0.0398 395 ASP A O 3048 C CB . ASP A 395 ? 0.3029 0.2095 0.3477 -0.0211 -0.1096 -0.0495 395 ASP A CB 3049 C CG . ASP A 395 ? 0.3975 0.3073 0.4283 -0.0170 -0.1042 -0.0539 395 ASP A CG 3050 O OD1 . ASP A 395 ? 0.3204 0.2315 0.3612 -0.0135 -0.0968 -0.0534 395 ASP A OD1 3051 O OD2 . ASP A 395 ? 0.3884 0.3021 0.3989 -0.0170 -0.1072 -0.0574 395 ASP A OD2 3052 N N . TYR A 396 ? 0.3256 0.2399 0.3931 -0.0253 -0.1071 -0.0391 396 TYR A N 3053 C CA . TYR A 396 ? 0.3129 0.2359 0.3954 -0.0251 -0.1062 -0.0408 396 TYR A CA 3054 C C . TYR A 396 ? 0.3415 0.2736 0.4283 -0.0291 -0.0966 -0.0355 396 TYR A C 3055 O O . TYR A 396 ? 0.2737 0.2177 0.3771 -0.0327 -0.0928 -0.0336 396 TYR A O 3056 C CB . TYR A 396 ? 0.2983 0.2185 0.3769 -0.0197 -0.1107 -0.0435 396 TYR A CB 3057 C CG . TYR A 396 ? 0.2829 0.2153 0.3790 -0.0154 -0.1068 -0.0487 396 TYR A CG 3058 C CD1 . TYR A 396 ? 0.3465 0.2949 0.4670 -0.0153 -0.1071 -0.0506 396 TYR A CD1 3059 C CD2 . TYR A 396 ? 0.3190 0.2485 0.4090 -0.0111 -0.1030 -0.0535 396 TYR A CD2 3060 C CE1 . TYR A 396 ? 0.2819 0.2494 0.4230 -0.0098 -0.1005 -0.0558 396 TYR A CE1 3061 C CE2 . TYR A 396 ? 0.3080 0.2518 0.4142 -0.0040 -0.0967 -0.0626 396 TYR A CE2 3062 C CZ . TYR A 396 ? 0.3437 0.3094 0.4765 -0.0027 -0.0941 -0.0630 396 TYR A CZ 3063 O OH . TYR A 396 ? 0.3190 0.3063 0.4718 0.0055 -0.0849 -0.0721 396 TYR A OH 3064 N N . ASN A 397 ? 0.2585 0.1972 0.2929 0.0017 -0.1107 -0.0180 397 ASN A N 3065 C CA . ASN A 397 ? 0.2955 0.2342 0.3367 0.0016 -0.1052 -0.0272 397 ASN A CA 3066 C C . ASN A 397 ? 0.2726 0.2257 0.3135 -0.0031 -0.0985 -0.0326 397 ASN A C 3067 O O . ASN A 397 ? 0.2646 0.2206 0.3105 -0.0013 -0.0946 -0.0405 397 ASN A O 3068 C CB . ASN A 397 ? 0.2910 0.2108 0.3284 -0.0025 -0.1056 -0.0256 397 ASN A CB 3069 C CG . ASN A 397 ? 0.4049 0.3054 0.4441 0.0047 -0.1117 -0.0239 397 ASN A CG 3070 O OD1 . ASN A 397 ? 0.3110 0.2101 0.3586 0.0135 -0.1114 -0.0318 397 ASN A OD1 3071 N ND2 . ASN A 397 ? 0.3020 0.1873 0.3329 0.0015 -0.1168 -0.0134 397 ASN A ND2 3072 N N . PHE A 398 ? 0.2255 0.1865 0.2595 -0.0085 -0.0968 -0.0286 398 PHE A N 3073 C CA . PHE A 398 ? 0.2258 0.1971 0.2592 -0.0119 -0.0910 -0.0334 398 PHE A CA 3074 C C . PHE A 398 ? 0.2772 0.2605 0.3066 -0.0121 -0.0897 -0.0341 398 PHE A C 3075 O O . PHE A 398 ? 0.2718 0.2612 0.3038 -0.0110 -0.0872 -0.0402 398 PHE A O 3076 C CB . PHE A 398 ? 0.2128 0.1819 0.2434 -0.0184 -0.0886 -0.0310 398 PHE A CB 3077 C CG . PHE A 398 ? 0.2569 0.2129 0.2900 -0.0196 -0.0904 -0.0321 398 PHE A CG 3078 C CD1 . PHE A 398 ? 0.2241 0.1781 0.2596 -0.0180 -0.0888 -0.0397 398 PHE A CD1 3079 C CD2 . PHE A 398 ? 0.2555 0.1986 0.2863 -0.0229 -0.0940 -0.0256 398 PHE A CD2 3080 C CE1 . PHE A 398 ? 0.2751 0.2155 0.3106 -0.0192 -0.0909 -0.0422 398 PHE A CE1 3081 C CE2 . PHE A 398 ? 0.2520 0.1798 0.2839 -0.0245 -0.0963 -0.0277 398 PHE A CE2 3082 C CZ . PHE A 398 ? 0.2519 0.1786 0.2860 -0.0225 -0.0949 -0.0367 398 PHE A CZ 3083 N N . ILE A 399 ? 0.2134 0.1984 0.2348 -0.0143 -0.0912 -0.0279 399 ILE A N 3084 C CA . ILE A 399 ? 0.2703 0.2648 0.2847 -0.0152 -0.0893 -0.0295 399 ILE A CA 3085 C C . ILE A 399 ? 0.3157 0.3150 0.3320 -0.0118 -0.0936 -0.0332 399 ILE A C 3086 O O . ILE A 399 ? 0.2873 0.2918 0.3049 -0.0121 -0.0911 -0.0397 399 ILE A O 3087 C CB . ILE A 399 ? 0.2573 0.2528 0.2598 -0.0191 -0.0883 -0.0223 399 ILE A CB 3088 C CG1 . ILE A 399 ? 0.2587 0.2549 0.2630 -0.0240 -0.0827 -0.0198 399 ILE A CG1 3089 C CG2 . ILE A 399 ? 0.2250 0.2287 0.2179 -0.0190 -0.0865 -0.0255 399 ILE A CG2 3090 C CD1 . ILE A 399 ? 0.3199 0.3207 0.3137 -0.0290 -0.0789 -0.0132 399 ILE A CD1 3091 N N . CYS A 400 ? 0.2809 0.2780 0.2978 -0.0088 -0.1006 -0.0290 400 CYS A N 3092 C CA . CYS A 400 ? 0.2540 0.2592 0.2764 -0.0058 -0.1061 -0.0327 400 CYS A CA 3093 C C . CYS A 400 ? 0.2579 0.2687 0.2952 -0.0042 -0.1032 -0.0410 400 CYS A C 3094 O O . CYS A 400 ? 0.2383 0.2577 0.2781 -0.0060 -0.1035 -0.0462 400 CYS A O 3095 C CB . CYS A 400 ? 0.2880 0.2904 0.3098 -0.0013 -0.1156 -0.0259 400 CYS A CB 3096 S SG . CYS A 400 ? 0.3536 0.3496 0.3522 -0.0052 -0.1182 -0.0156 400 CYS A SG 3097 N N . PRO A 401 ? 0.2482 0.2536 0.2938 -0.0019 -0.1001 -0.0424 401 PRO A N 3098 C CA . PRO A 401 ? 0.2732 0.2844 0.3294 -0.0016 -0.0953 -0.0500 401 PRO A CA 3099 C C . PRO A 401 ? 0.2629 0.2743 0.3124 -0.0071 -0.0890 -0.0539 401 PRO A C 3100 O O . PRO A 401 ? 0.2012 0.2190 0.2556 -0.0094 -0.0867 -0.0591 401 PRO A O 3101 C CB . PRO A 401 ? 0.2412 0.2434 0.3019 0.0017 -0.0928 -0.0507 401 PRO A CB 3102 C CG . PRO A 401 ? 0.2287 0.2222 0.2875 0.0056 -0.0996 -0.0437 401 PRO A CG 3103 C CD . PRO A 401 ? 0.2664 0.2598 0.3120 0.0007 -0.1015 -0.0376 401 PRO A CD 3104 N N . ALA A 402 ? 0.1874 0.1922 0.2269 -0.0093 -0.0864 -0.0514 402 ALA A N 3105 C CA . ALA A 402 ? 0.2227 0.2263 0.2561 -0.0124 -0.0815 -0.0548 402 ALA A CA 3106 C C . ALA A 402 ? 0.2197 0.2277 0.2484 -0.0145 -0.0828 -0.0573 402 ALA A C 3107 O O . ALA A 402 ? 0.2286 0.2355 0.2567 -0.0170 -0.0801 -0.0620 402 ALA A O 3108 C CB . ALA A 402 ? 0.1836 0.1832 0.2105 -0.0131 -0.0793 -0.0517 402 ALA A CB 3109 N N . LEU A 403 ? 0.2351 0.2462 0.2585 -0.0142 -0.0873 -0.0542 403 LEU A N 3110 C CA . LEU A 403 ? 0.1993 0.2136 0.2160 -0.0164 -0.0897 -0.0576 403 LEU A CA 3111 C C . LEU A 403 ? 0.3043 0.3255 0.3313 -0.0184 -0.0933 -0.0619 403 LEU A C 3112 O O . LEU A 403 ? 0.2301 0.2509 0.2542 -0.0226 -0.0928 -0.0673 403 LEU A O 3113 C CB . LEU A 403 ? 0.3254 0.3413 0.3310 -0.0159 -0.0941 -0.0530 403 LEU A CB 3114 C CG . LEU A 403 ? 0.3658 0.3785 0.3600 -0.0159 -0.0886 -0.0504 403 LEU A CG 3115 C CD1 . LEU A 403 ? 0.3095 0.3231 0.2939 -0.0161 -0.0917 -0.0430 403 LEU A CD1 3116 C CD2 . LEU A 403 ? 0.2186 0.2298 0.2031 -0.0167 -0.0850 -0.0572 403 LEU A CD2 3117 N N A GLU A 404 ? 0.2481 0.2756 0.2880 -0.0154 -0.0968 -0.0600 404 GLU A N 3118 N N B GLU A 404 ? 0.2457 0.2733 0.2856 -0.0155 -0.0967 -0.0601 404 GLU A N 3119 C CA A GLU A 404 ? 0.2649 0.3041 0.3195 -0.0169 -0.0996 -0.0643 404 GLU A CA 3120 C CA B GLU A 404 ? 0.2606 0.2996 0.3145 -0.0172 -0.0996 -0.0645 404 GLU A CA 3121 C C A GLU A 404 ? 0.2366 0.2744 0.2960 -0.0215 -0.0916 -0.0694 404 GLU A C 3122 C C B GLU A 404 ? 0.2361 0.2741 0.2958 -0.0215 -0.0916 -0.0695 404 GLU A C 3123 O O A GLU A 404 ? 0.2295 0.2729 0.2934 -0.0275 -0.0917 -0.0740 404 GLU A O 3124 O O B GLU A 404 ? 0.2303 0.2743 0.2951 -0.0274 -0.0916 -0.0741 404 GLU A O 3125 C CB A GLU A 404 ? 0.2924 0.3393 0.3620 -0.0104 -0.1039 -0.0618 404 GLU A CB 3126 C CB B GLU A 404 ? 0.2754 0.3229 0.3437 -0.0109 -0.1051 -0.0617 404 GLU A CB 3127 C CG A GLU A 404 ? 0.3099 0.3729 0.4000 -0.0113 -0.1040 -0.0672 404 GLU A CG 3128 C CG B GLU A 404 ? 0.3034 0.3679 0.3913 -0.0119 -0.1072 -0.0668 404 GLU A CG 3129 C CD A GLU A 404 ? 0.2948 0.3662 0.4021 -0.0024 -0.1074 -0.0660 404 GLU A CD 3130 C CD B GLU A 404 ? 0.3197 0.3950 0.4084 -0.0150 -0.1171 -0.0681 404 GLU A CD 3131 O OE1 A GLU A 404 ? 0.2719 0.3374 0.3828 0.0017 -0.1011 -0.0665 404 GLU A OE1 3132 O OE1 B GLU A 404 ? 0.2993 0.3668 0.3695 -0.0176 -0.1206 -0.0665 404 GLU A OE1 3133 O OE2 A GLU A 404 ? 0.2960 0.3798 0.4132 0.0011 -0.1171 -0.0651 404 GLU A OE2 3134 O OE2 B GLU A 404 ? 0.4239 0.5169 0.5320 -0.0148 -0.1214 -0.0712 404 GLU A OE2 3135 N N . PHE A 405 ? 0.2199 0.2493 0.2771 -0.0196 -0.0851 -0.0683 405 PHE A N 3136 C CA . PHE A 405 ? 0.2167 0.2420 0.2741 -0.0236 -0.0776 -0.0716 405 PHE A CA 3137 C C . PHE A 405 ? 0.2566 0.2735 0.3022 -0.0293 -0.0763 -0.0739 405 PHE A C 3138 O O . PHE A 405 ? 0.2393 0.2561 0.2871 -0.0357 -0.0732 -0.0772 405 PHE A O 3139 C CB . PHE A 405 ? 0.1961 0.2118 0.2484 -0.0203 -0.0728 -0.0697 405 PHE A CB 3140 C CG . PHE A 405 ? 0.2726 0.2822 0.3208 -0.0244 -0.0657 -0.0722 405 PHE A CG 3141 C CD1 . PHE A 405 ? 0.3239 0.3215 0.3587 -0.0271 -0.0640 -0.0717 405 PHE A CD1 3142 C CD2 . PHE A 405 ? 0.3154 0.3311 0.3724 -0.0253 -0.0605 -0.0749 405 PHE A CD2 3143 C CE1 . PHE A 405 ? 0.2125 0.2018 0.2408 -0.0310 -0.0584 -0.0726 405 PHE A CE1 3144 C CE2 . PHE A 405 ? 0.2920 0.3011 0.3419 -0.0302 -0.0533 -0.0762 405 PHE A CE2 3145 C CZ . PHE A 405 ? 0.2387 0.2335 0.2734 -0.0333 -0.0529 -0.0744 405 PHE A CZ 3146 N N . THR A 406 ? 0.2554 0.2646 0.2886 -0.0270 -0.0780 -0.0721 406 THR A N 3147 C CA . THR A 406 ? 0.2009 0.1997 0.2222 -0.0300 -0.0767 -0.0751 406 THR A CA 3148 C C . THR A 406 ? 0.2438 0.2457 0.2654 -0.0362 -0.0807 -0.0797 406 THR A C 3149 O O . THR A 406 ? 0.3001 0.2928 0.3170 -0.0418 -0.0786 -0.0833 406 THR A O 3150 C CB . THR A 406 ? 0.2029 0.1962 0.2128 -0.0251 -0.0768 -0.0732 406 THR A CB 3151 O OG1 . THR A 406 ? 0.2279 0.2203 0.2398 -0.0209 -0.0742 -0.0691 406 THR A OG1 3152 C CG2 . THR A 406 ? 0.2237 0.2040 0.2219 -0.0258 -0.0746 -0.0772 406 THR A CG2 3153 N N . LYS A 407 ? 0.2693 0.2830 0.2958 -0.0356 -0.0874 -0.0794 407 LYS A N 3154 C CA . LYS A 407 ? 0.3723 0.3914 0.4002 -0.0420 -0.0932 -0.0843 407 LYS A CA 3155 C C . LYS A 407 ? 0.3047 0.3312 0.3479 -0.0495 -0.0911 -0.0872 407 LYS A C 3156 O O . LYS A 407 ? 0.2488 0.2688 0.2878 -0.0579 -0.0896 -0.0907 407 LYS A O 3157 C CB . LYS A 407 ? 0.3858 0.4179 0.4168 -0.0391 -0.1019 -0.0820 407 LYS A CB 3158 C CG . LYS A 407 ? 0.5704 0.5970 0.5856 -0.0334 -0.1039 -0.0785 407 LYS A CG 3159 C CD . LYS A 407 ? 0.6633 0.7010 0.6803 -0.0306 -0.1136 -0.0746 407 LYS A CD 3160 C CE . LYS A 407 ? 0.6793 0.7109 0.6777 -0.0266 -0.1142 -0.0696 407 LYS A CE 3161 N NZ . LYS A 407 ? 0.6513 0.6903 0.6466 -0.0243 -0.1247 -0.0647 407 LYS A NZ 3162 N N . LYS A 408 ? 0.2471 0.2866 0.3068 -0.0466 -0.0893 -0.0848 408 LYS A N 3163 C CA . LYS A 408 ? 0.3071 0.3589 0.3842 -0.0533 -0.0857 -0.0877 408 LYS A CA 3164 C C . LYS A 408 ? 0.3027 0.3395 0.3714 -0.0603 -0.0766 -0.0886 408 LYS A C 3165 O O . LYS A 408 ? 0.3228 0.3623 0.3973 -0.0708 -0.0743 -0.0918 408 LYS A O 3166 C CB . LYS A 408 ? 0.2231 0.2898 0.3177 -0.0464 -0.0835 -0.0857 408 LYS A CB 3167 C CG . LYS A 408 ? 0.3176 0.3993 0.4235 -0.0391 -0.0934 -0.0841 408 LYS A CG 3168 C CD . LYS A 408 ? 0.5205 0.6207 0.6408 -0.0454 -0.1010 -0.0881 408 LYS A CD 3169 C CE . LYS A 408 ? 0.5825 0.6985 0.7151 -0.0366 -0.1118 -0.0855 408 LYS A CE 3170 N NZ . LYS A 408 ? 0.6430 0.7745 0.7840 -0.0425 -0.1180 -0.0865 408 LYS A NZ 3171 N N . PHE A 409 ? 0.2847 0.3056 0.3397 -0.0550 -0.0718 -0.0853 409 PHE A N 3172 C CA . PHE A 409 ? 0.2529 0.2570 0.2969 -0.0601 -0.0645 -0.0849 409 PHE A CA 3173 C C . PHE A 409 ? 0.3540 0.3421 0.3855 -0.0671 -0.0667 -0.0879 409 PHE A C 3174 O O . PHE A 409 ? 0.3827 0.3628 0.4123 -0.0769 -0.0627 -0.0889 409 PHE A O 3175 C CB . PHE A 409 ? 0.2876 0.2790 0.3197 -0.0519 -0.0615 -0.0808 409 PHE A CB 3176 C CG . PHE A 409 ? 0.3445 0.3206 0.3659 -0.0558 -0.0547 -0.0791 409 PHE A CG 3177 C CD1 . PHE A 409 ? 0.3576 0.3130 0.3635 -0.0586 -0.0550 -0.0790 409 PHE A CD1 3178 C CD2 . PHE A 409 ? 0.3389 0.3196 0.3639 -0.0563 -0.0483 -0.0777 409 PHE A CD2 3179 C CE1 . PHE A 409 ? 0.2557 0.1943 0.2493 -0.0619 -0.0499 -0.0760 409 PHE A CE1 3180 C CE2 . PHE A 409 ? 0.3360 0.3012 0.3474 -0.0604 -0.0424 -0.0752 409 PHE A CE2 3181 C CZ . PHE A 409 ? 0.3570 0.3008 0.3525 -0.0634 -0.0437 -0.0737 409 PHE A CZ 3182 N N . SER A 410 ? 0.3412 0.3236 0.3631 -0.0623 -0.0727 -0.0894 410 SER A N 3183 C CA . SER A 410 ? 0.3494 0.3134 0.3568 -0.0668 -0.0748 -0.0936 410 SER A CA 3184 C C . SER A 410 ? 0.4139 0.3836 0.4270 -0.0785 -0.0783 -0.0979 410 SER A C 3185 O O . SER A 410 ? 0.2885 0.2403 0.2895 -0.0853 -0.0780 -0.1008 410 SER A O 3186 C CB . SER A 410 ? 0.3495 0.3082 0.3445 -0.0576 -0.0786 -0.0948 410 SER A CB 3187 O OG . SER A 410 ? 0.4524 0.4272 0.4515 -0.0571 -0.0839 -0.0950 410 SER A OG 3188 N N . GLU A 411 ? 0.3538 0.3479 0.3850 -0.0806 -0.0813 -0.0974 411 GLU A N 3189 C CA . GLU A 411 ? 0.3763 0.3792 0.4147 -0.0914 -0.0854 -0.0997 411 GLU A CA 3190 C C . GLU A 411 ? 0.3836 0.3808 0.4279 -0.1046 -0.0800 -0.1010 411 GLU A C 3191 O O . GLU A 411 ? 0.3577 0.3558 0.4056 -0.1150 -0.0836 -0.1027 411 GLU A O 3192 C CB . GLU A 411 ? 0.3800 0.4121 0.4386 -0.0886 -0.0910 -0.0985 411 GLU A CB 3193 C CG . GLU A 411 ? 0.5360 0.5710 0.5847 -0.0816 -0.0992 -0.0977 411 GLU A CG 3194 C CD . GLU A 411 ? 0.7051 0.7646 0.7714 -0.0747 -0.1049 -0.0947 411 GLU A CD 3195 O OE1 . GLU A 411 ? 0.7482 0.8251 0.8371 -0.0754 -0.1027 -0.0946 411 GLU A OE1 3196 O OE2 . GLU A 411 ? 0.7679 0.8288 0.8251 -0.0682 -0.1115 -0.0927 411 GLU A OE2 3197 N N . TRP A 412 ? 0.3812 0.3717 0.4257 -0.1050 -0.0715 -0.0998 412 TRP A N 3198 C CA . TRP A 412 ? 0.3900 0.3739 0.4366 -0.1189 -0.0639 -0.0994 412 TRP A CA 3199 C C . TRP A 412 ? 0.4412 0.3883 0.4626 -0.1214 -0.0618 -0.0982 412 TRP A C 3200 O O . TRP A 412 ? 0.4484 0.3815 0.4637 -0.1311 -0.0545 -0.0953 412 TRP A O 3201 C CB . TRP A 412 ? 0.3637 0.3629 0.4223 -0.1173 -0.0541 -0.0952 412 TRP A CB 3202 C CG . TRP A 412 ? 0.4157 0.4510 0.5027 -0.1166 -0.0561 -0.0978 412 TRP A CG 3203 C CD1 . TRP A 412 ? 0.3677 0.4198 0.4645 -0.1030 -0.0611 -0.0974 412 TRP A CD1 3204 C CD2 . TRP A 412 ? 0.3964 0.4554 0.5067 -0.1298 -0.0541 -0.1011 412 TRP A CD2 3205 N NE1 . TRP A 412 ? 0.3758 0.4595 0.5002 -0.1052 -0.0629 -0.1002 412 TRP A NE1 3206 C CE2 . TRP A 412 ? 0.3419 0.4329 0.4766 -0.1215 -0.0586 -0.1029 412 TRP A CE2 3207 C CE3 . TRP A 412 ? 0.4542 0.5099 0.5669 -0.1471 -0.0489 -0.1012 412 TRP A CE3 3208 C CZ2 . TRP A 412 ? 0.2990 0.4211 0.4619 -0.1284 -0.0579 -0.1051 412 TRP A CZ2 3209 C CZ3 . TRP A 412 ? 0.3805 0.4675 0.5210 -0.1551 -0.0476 -0.1027 412 TRP A CZ3 3210 C CH2 . TRP A 412 ? 0.3499 0.4709 0.5159 -0.1453 -0.0521 -0.1049 412 TRP A CH2 3211 N N . GLY A 413 ? 0.4625 0.3937 0.4688 -0.1119 -0.0681 -0.1003 413 GLY A N 3212 C CA . GLY A 413 ? 0.4153 0.3154 0.4030 -0.1122 -0.0673 -0.1013 413 GLY A CA 3213 C C . GLY A 413 ? 0.4848 0.3615 0.4531 -0.1018 -0.0645 -0.0976 413 GLY A C 3214 O O . GLY A 413 ? 0.5340 0.3846 0.4869 -0.0995 -0.0641 -0.0980 413 GLY A O 3215 N N . ASN A 414 ? 0.4200 0.3079 0.3916 -0.0929 -0.0625 -0.0932 414 ASN A N 3216 C CA . ASN A 414 ? 0.4760 0.3464 0.4333 -0.0812 -0.0608 -0.0886 414 ASN A CA 3217 C C . ASN A 414 ? 0.4312 0.3026 0.3839 -0.0670 -0.0652 -0.0913 414 ASN A C 3218 O O . ASN A 414 ? 0.4105 0.3019 0.3724 -0.0641 -0.0684 -0.0942 414 ASN A O 3219 C CB . ASN A 414 ? 0.5204 0.4021 0.4830 -0.0782 -0.0553 -0.0820 414 ASN A CB 3220 C CG . ASN A 414 ? 0.5315 0.4050 0.4910 -0.0906 -0.0486 -0.0781 414 ASN A CG 3221 O OD1 . ASN A 414 ? 0.3508 0.2452 0.3245 -0.0971 -0.0437 -0.0776 414 ASN A OD1 3222 N ND2 . ASN A 414 ? 0.5112 0.3536 0.4517 -0.0939 -0.0479 -0.0751 414 ASN A ND2 3223 N N . ASN A 415 ? 0.4423 0.2925 0.3810 -0.0580 -0.0653 -0.0900 415 ASN A N 3224 C CA . ASN A 415 ? 0.4218 0.2760 0.3583 -0.0438 -0.0674 -0.0917 415 ASN A CA 3225 C C . ASN A 415 ? 0.3688 0.2467 0.3169 -0.0370 -0.0663 -0.0870 415 ASN A C 3226 O O . ASN A 415 ? 0.4034 0.2828 0.3535 -0.0369 -0.0639 -0.0812 415 ASN A O 3227 C CB . ASN A 415 ? 0.4623 0.2902 0.3842 -0.0346 -0.0679 -0.0913 415 ASN A CB 3228 C CG . ASN A 415 ? 0.4984 0.3031 0.4081 -0.0365 -0.0696 -0.0983 415 ASN A CG 3229 O OD1 . ASN A 415 ? 0.5134 0.3264 0.4267 -0.0450 -0.0693 -0.1026 415 ASN A OD1 3230 N ND2 . ASN A 415 ? 0.4268 0.2064 0.3241 -0.0276 -0.0702 -0.0982 415 ASN A ND2 3231 N N . ALA A 416 ? 0.3394 0.2343 0.2932 -0.0321 -0.0681 -0.0895 416 ALA A N 3232 C CA . ALA A 416 ? 0.3351 0.2493 0.2985 -0.0260 -0.0675 -0.0851 416 ALA A CA 3233 C C . ALA A 416 ? 0.3587 0.2767 0.3187 -0.0163 -0.0679 -0.0872 416 ALA A C 3234 O O . ALA A 416 ? 0.3404 0.2534 0.2927 -0.0157 -0.0688 -0.0932 416 ALA A O 3235 C CB . ALA A 416 ? 0.2935 0.2274 0.2689 -0.0317 -0.0687 -0.0845 416 ALA A CB 3236 N N . PHE A 417 ? 0.2717 0.1992 0.2373 -0.0095 -0.0668 -0.0829 417 PHE A N 3237 C CA . PHE A 417 ? 0.2794 0.2154 0.2452 -0.0010 -0.0656 -0.0841 417 PHE A CA 3238 C C . PHE A 417 ? 0.2702 0.2263 0.2464 -0.0015 -0.0654 -0.0791 417 PHE A C 3239 O O . PHE A 417 ? 0.2796 0.2390 0.2626 -0.0031 -0.0661 -0.0745 417 PHE A O 3240 C CB . PHE A 417 ? 0.2602 0.1870 0.2238 0.0081 -0.0652 -0.0838 417 PHE A CB 3241 C CG . PHE A 417 ? 0.3199 0.2215 0.2716 0.0089 -0.0661 -0.0874 417 PHE A CG 3242 C CD1 . PHE A 417 ? 0.3005 0.1918 0.2435 0.0141 -0.0653 -0.0947 417 PHE A CD1 3243 C CD2 . PHE A 417 ? 0.3140 0.2003 0.2614 0.0038 -0.0675 -0.0837 417 PHE A CD2 3244 C CE1 . PHE A 417 ? 0.3899 0.2536 0.3206 0.0144 -0.0668 -0.0983 417 PHE A CE1 3245 C CE2 . PHE A 417 ? 0.3144 0.1740 0.2491 0.0030 -0.0685 -0.0859 417 PHE A CE2 3246 C CZ . PHE A 417 ? 0.3837 0.2310 0.3104 0.0084 -0.0686 -0.0933 417 PHE A CZ 3247 N N . PHE A 418 ? 0.2901 0.2574 0.2655 -0.0006 -0.0644 -0.0799 418 PHE A N 3248 C CA . PHE A 418 ? 0.2897 0.2725 0.2730 -0.0022 -0.0644 -0.0742 418 PHE A CA 3249 C C . PHE A 418 ? 0.3175 0.3117 0.3025 0.0029 -0.0605 -0.0732 418 PHE A C 3250 O O . PHE A 418 ? 0.2432 0.2374 0.2206 0.0070 -0.0573 -0.0780 418 PHE A O 3251 C CB . PHE A 418 ? 0.2257 0.2131 0.2065 -0.0076 -0.0673 -0.0737 418 PHE A CB 3252 C CG . PHE A 418 ? 0.2531 0.2502 0.2418 -0.0098 -0.0690 -0.0669 418 PHE A CG 3253 C CD1 . PHE A 418 ? 0.2091 0.2151 0.1968 -0.0090 -0.0671 -0.0627 418 PHE A CD1 3254 C CD2 . PHE A 418 ? 0.2102 0.2064 0.2068 -0.0128 -0.0719 -0.0650 418 PHE A CD2 3255 C CE1 . PHE A 418 ? 0.2456 0.2561 0.2391 -0.0117 -0.0692 -0.0559 418 PHE A CE1 3256 C CE2 . PHE A 418 ? 0.2726 0.2743 0.2758 -0.0136 -0.0739 -0.0594 418 PHE A CE2 3257 C CZ . PHE A 418 ? 0.2219 0.2289 0.2228 -0.0132 -0.0732 -0.0546 418 PHE A CZ 3258 N N . TYR A 419 ? 0.2745 0.2786 0.2696 0.0023 -0.0603 -0.0676 419 TYR A N 3259 C CA . TYR A 419 ? 0.2853 0.3040 0.2854 0.0049 -0.0560 -0.0657 419 TYR A CA 3260 C C . TYR A 419 ? 0.2979 0.3264 0.3013 -0.0015 -0.0558 -0.0589 419 TYR A C 3261 O O . TYR A 419 ? 0.2321 0.2558 0.2378 -0.0060 -0.0600 -0.0551 419 TYR A O 3262 C CB . TYR A 419 ? 0.2051 0.2285 0.2161 0.0098 -0.0562 -0.0654 419 TYR A CB 3263 C CG . TYR A 419 ? 0.1951 0.2184 0.2141 0.0053 -0.0607 -0.0605 419 TYR A CG 3264 C CD1 . TYR A 419 ? 0.1896 0.2244 0.2167 0.0000 -0.0604 -0.0553 419 TYR A CD1 3265 C CD2 . TYR A 419 ? 0.2279 0.2381 0.2445 0.0056 -0.0648 -0.0612 419 TYR A CD2 3266 C CE1 . TYR A 419 ? 0.2021 0.2342 0.2348 -0.0042 -0.0648 -0.0523 419 TYR A CE1 3267 C CE2 . TYR A 419 ? 0.2083 0.2174 0.2294 0.0017 -0.0684 -0.0580 419 TYR A CE2 3268 C CZ . TYR A 419 ? 0.2501 0.2696 0.2793 -0.0029 -0.0687 -0.0541 419 TYR A CZ 3269 O OH . TYR A 419 ? 0.1968 0.2126 0.2287 -0.0068 -0.0726 -0.0523 419 TYR A OH 3270 N N . TYR A 420 ? 0.2607 0.3020 0.2639 -0.0015 -0.0504 -0.0574 420 TYR A N 3271 C CA . TYR A 420 ? 0.2093 0.2584 0.2146 -0.0084 -0.0494 -0.0497 420 TYR A CA 3272 C C . TYR A 420 ? 0.2735 0.3391 0.2921 -0.0085 -0.0446 -0.0479 420 TYR A C 3273 O O . TYR A 420 ? 0.2578 0.3359 0.2767 -0.0047 -0.0376 -0.0510 420 TYR A O 3274 C CB . TYR A 420 ? 0.2224 0.2731 0.2127 -0.0105 -0.0463 -0.0486 420 TYR A CB 3275 C CG . TYR A 420 ? 0.2868 0.3401 0.2739 -0.0183 -0.0463 -0.0391 420 TYR A CG 3276 C CD1 . TYR A 420 ? 0.2243 0.2672 0.2134 -0.0221 -0.0536 -0.0336 420 TYR A CD1 3277 C CD2 . TYR A 420 ? 0.2777 0.3425 0.2582 -0.0214 -0.0386 -0.0356 420 TYR A CD2 3278 C CE1 . TYR A 420 ? 0.3018 0.3426 0.2860 -0.0286 -0.0545 -0.0242 420 TYR A CE1 3279 C CE2 . TYR A 420 ? 0.3646 0.4284 0.3391 -0.0296 -0.0386 -0.0255 420 TYR A CE2 3280 C CZ . TYR A 420 ? 0.3513 0.4016 0.3274 -0.0329 -0.0473 -0.0195 420 TYR A CZ 3281 O OH . TYR A 420 ? 0.3510 0.3964 0.3197 -0.0404 -0.0482 -0.0089 420 TYR A OH 3282 N N . PHE A 421 ? 0.2472 0.3139 0.2774 -0.0128 -0.0484 -0.0438 421 PHE A N 3283 C CA . PHE A 421 ? 0.2834 0.3675 0.3296 -0.0142 -0.0459 -0.0424 421 PHE A CA 3284 C C . PHE A 421 ? 0.2618 0.3566 0.3099 -0.0240 -0.0411 -0.0351 421 PHE A C 3285 O O . PHE A 421 ? 0.2721 0.3562 0.3162 -0.0317 -0.0449 -0.0289 421 PHE A O 3286 C CB . PHE A 421 ? 0.1882 0.2669 0.2439 -0.0148 -0.0536 -0.0426 421 PHE A CB 3287 C CG . PHE A 421 ? 0.2700 0.3671 0.3436 -0.0166 -0.0538 -0.0418 421 PHE A CG 3288 C CD1 . PHE A 421 ? 0.2094 0.3177 0.2924 -0.0075 -0.0539 -0.0467 421 PHE A CD1 3289 C CD2 . PHE A 421 ? 0.2167 0.3190 0.2983 -0.0274 -0.0551 -0.0362 421 PHE A CD2 3290 C CE1 . PHE A 421 ? 0.3315 0.4600 0.4338 -0.0087 -0.0556 -0.0461 421 PHE A CE1 3291 C CE2 . PHE A 421 ? 0.2558 0.3769 0.3558 -0.0306 -0.0564 -0.0358 421 PHE A CE2 3292 C CZ . PHE A 421 ? 0.2920 0.4282 0.4035 -0.0212 -0.0569 -0.0409 421 PHE A CZ 3293 N N . GLU A 422 ? 0.2540 0.3691 0.3075 -0.0235 -0.0323 -0.0356 422 GLU A N 3294 C CA . GLU A 422 ? 0.2821 0.4072 0.3344 -0.0341 -0.0258 -0.0279 422 GLU A CA 3295 C C . GLU A 422 ? 0.3130 0.4650 0.3864 -0.0385 -0.0197 -0.0267 422 GLU A C 3296 O O . GLU A 422 ? 0.2869 0.4535 0.3599 -0.0457 -0.0103 -0.0220 422 GLU A O 3297 C CB . GLU A 422 ? 0.4246 0.5480 0.4565 -0.0330 -0.0187 -0.0276 422 GLU A CB 3298 C CG . GLU A 422 ? 0.5063 0.6434 0.5374 -0.0227 -0.0104 -0.0367 422 GLU A CG 3299 C CD . GLU A 422 ? 0.5429 0.6714 0.5488 -0.0202 -0.0064 -0.0390 422 GLU A CD 3300 O OE1 . GLU A 422 ? 0.4529 0.5654 0.4426 -0.0258 -0.0116 -0.0333 422 GLU A OE1 3301 O OE2 . GLU A 422 ? 0.6124 0.7499 0.6144 -0.0121 0.0012 -0.0472 422 GLU A OE2 3302 N N . HIS A 423 ? 0.3101 0.4699 0.4020 -0.0349 -0.0253 -0.0305 423 HIS A N 3303 C CA . HIS A 423 ? 0.2985 0.4863 0.4142 -0.0402 -0.0216 -0.0292 423 HIS A CA 3304 C C . HIS A 423 ? 0.2830 0.4667 0.4081 -0.0538 -0.0290 -0.0231 423 HIS A C 3305 O O . HIS A 423 ? 0.2520 0.4196 0.3768 -0.0523 -0.0399 -0.0249 423 HIS A O 3306 C CB . HIS A 423 ? 0.2593 0.4641 0.3925 -0.0274 -0.0233 -0.0373 423 HIS A CB 3307 C CG . HIS A 423 ? 0.2867 0.5234 0.4482 -0.0326 -0.0215 -0.0364 423 HIS A CG 3308 N ND1 . HIS A 423 ? 0.3042 0.5697 0.4772 -0.0377 -0.0085 -0.0347 423 HIS A ND1 3309 C CD2 . HIS A 423 ? 0.2859 0.5317 0.4668 -0.0349 -0.0313 -0.0369 423 HIS A CD2 3310 C CE1 . HIS A 423 ? 0.2968 0.5898 0.4980 -0.0430 -0.0102 -0.0342 423 HIS A CE1 3311 N NE2 . HIS A 423 ? 0.3212 0.6025 0.5275 -0.0413 -0.0249 -0.0356 423 HIS A NE2 3312 N N . ARG A 424 ? 0.2943 0.4919 0.4267 -0.0676 -0.0226 -0.0162 424 ARG A N 3313 C CA . ARG A 424 ? 0.3121 0.5066 0.4549 -0.0820 -0.0292 -0.0110 424 ARG A CA 3314 C C . ARG A 424 ? 0.2737 0.4981 0.4463 -0.0838 -0.0316 -0.0147 424 ARG A C 3315 O O . ARG A 424 ? 0.2366 0.4932 0.4263 -0.0854 -0.0218 -0.0148 424 ARG A O 3316 C CB . ARG A 424 ? 0.2732 0.4649 0.4084 -0.0982 -0.0219 -0.0005 424 ARG A CB 3317 C CG . ARG A 424 ? 0.3295 0.5210 0.4783 -0.1153 -0.0272 0.0047 424 ARG A CG 3318 C CD . ARG A 424 ? 0.2665 0.4511 0.4051 -0.1319 -0.0199 0.0164 424 ARG A CD 3319 N NE . ARG A 424 ? 0.5115 0.7027 0.6675 -0.1503 -0.0226 0.0209 424 ARG A NE 3320 C CZ . ARG A 424 ? 0.5810 0.7426 0.7300 -0.1600 -0.0327 0.0246 424 ARG A CZ 3321 N NH1 . ARG A 424 ? 0.5258 0.6516 0.6523 -0.1517 -0.0403 0.0244 424 ARG A NH1 3322 N NH2 . ARG A 424 ? 0.5141 0.6821 0.6794 -0.1781 -0.0352 0.0279 424 ARG A NH2 3323 N N . SER A 425 ? 0.2387 0.4534 0.4171 -0.0832 -0.0447 -0.0179 425 SER A N 3324 C CA . SER A 425 ? 0.2775 0.5181 0.4827 -0.0843 -0.0509 -0.0217 425 SER A CA 3325 C C . SER A 425 ? 0.3118 0.5809 0.5391 -0.1012 -0.0446 -0.0167 425 SER A C 3326 O O . SER A 425 ? 0.3105 0.5665 0.5300 -0.1173 -0.0422 -0.0092 425 SER A O 3327 C CB . SER A 425 ? 0.3332 0.5518 0.5339 -0.0860 -0.0664 -0.0243 425 SER A CB 3328 O OG . SER A 425 ? 0.3398 0.5818 0.5643 -0.0882 -0.0749 -0.0277 425 SER A OG 3329 N N . SER A 426 ? 0.2912 0.5994 0.5467 -0.0978 -0.0417 -0.0204 426 SER A N 3330 C CA . SER A 426 ? 0.2141 0.5546 0.4948 -0.1149 -0.0351 -0.0160 426 SER A CA 3331 C C . SER A 426 ? 0.2771 0.6118 0.5682 -0.1316 -0.0485 -0.0143 426 SER A C 3332 O O . SER A 426 ? 0.2310 0.5817 0.5375 -0.1511 -0.0447 -0.0090 426 SER A O 3333 C CB . SER A 426 ? 0.4009 0.7889 0.7128 -0.1051 -0.0285 -0.0215 426 SER A CB 3334 O OG . SER A 426 ? 0.1977 0.5932 0.5238 -0.0921 -0.0429 -0.0288 426 SER A OG 3335 N N . LYS A 427 ? 0.3785 0.6892 0.6597 -0.1248 -0.0640 -0.0191 427 LYS A N 3336 C CA . LYS A 427 ? 0.4562 0.7586 0.7439 -0.1395 -0.0779 -0.0194 427 LYS A CA 3337 C C . LYS A 427 ? 0.4422 0.6983 0.7012 -0.1492 -0.0816 -0.0154 427 LYS A C 3338 O O . LYS A 427 ? 0.4025 0.6430 0.6608 -0.1602 -0.0924 -0.0169 427 LYS A O 3339 C CB . LYS A 427 ? 0.5212 0.8272 0.8153 -0.1272 -0.0937 -0.0276 427 LYS A CB 3340 C CG . LYS A 427 ? 0.5941 0.9431 0.9180 -0.1156 -0.0931 -0.0316 427 LYS A CG 3341 C CD . LYS A 427 ? 0.6232 0.9648 0.9446 -0.1008 -0.1095 -0.0367 427 LYS A CD 3342 C CE . LYS A 427 ? 0.6447 0.9670 0.9634 -0.1115 -0.1236 -0.0382 427 LYS A CE 3343 N NZ . LYS A 427 ? 0.6356 0.9619 0.9392 -0.1021 -0.1359 -0.0390 427 LYS A NZ 3344 N N . LEU A 428 ? 0.3740 0.6068 0.6087 -0.1432 -0.0727 -0.0114 428 LEU A N 3345 C CA . LEU A 428 ? 0.3305 0.5201 0.5387 -0.1488 -0.0758 -0.0076 428 LEU A CA 3346 C C . LEU A 428 ? 0.3481 0.5295 0.5611 -0.1721 -0.0777 -0.0013 428 LEU A C 3347 O O . LEU A 428 ? 0.4419 0.6407 0.6646 -0.1852 -0.0674 0.0062 428 LEU A O 3348 C CB . LEU A 428 ? 0.3640 0.5395 0.5509 -0.1409 -0.0649 -0.0027 428 LEU A CB 3349 C CG . LEU A 428 ? 0.4538 0.5914 0.6131 -0.1298 -0.0692 -0.0040 428 LEU A CG 3350 C CD1 . LEU A 428 ? 0.4784 0.5862 0.6201 -0.1403 -0.0679 0.0045 428 LEU A CD1 3351 C CD2 . LEU A 428 ? 0.4087 0.5312 0.5651 -0.1231 -0.0820 -0.0122 428 LEU A CD2 3352 N N . PRO A 429 ? 0.3588 0.5127 0.5640 -0.1779 -0.0904 -0.0048 429 PRO A N 3353 C CA . PRO A 429 ? 0.3963 0.5340 0.6012 -0.1953 -0.0912 -0.0015 429 PRO A CA 3354 C C . PRO A 429 ? 0.3262 0.4285 0.5087 -0.2036 -0.0875 0.0084 429 PRO A C 3355 O O . PRO A 429 ? 0.3616 0.4535 0.5439 -0.2192 -0.0843 0.0146 429 PRO A O 3356 C CB . PRO A 429 ? 0.3150 0.4340 0.5136 -0.1902 -0.1033 -0.0123 429 PRO A CB 3357 C CG . PRO A 429 ? 0.3556 0.4644 0.5400 -0.1715 -0.1082 -0.0181 429 PRO A CG 3358 C CD . PRO A 429 ? 0.3345 0.4693 0.5273 -0.1637 -0.1016 -0.0141 429 PRO A CD 3359 N N . TRP A 430 ? 0.3174 0.4002 0.4798 -0.1898 -0.0865 0.0092 430 TRP A N 3360 C CA . TRP A 430 ? 0.4439 0.4960 0.5841 -0.1919 -0.0817 0.0186 430 TRP A CA 3361 C C . TRP A 430 ? 0.4141 0.4875 0.5569 -0.1991 -0.0674 0.0293 430 TRP A C 3362 O O . TRP A 430 ? 0.4160 0.5266 0.5736 -0.1939 -0.0595 0.0270 430 TRP A O 3363 C CB . TRP A 430 ? 0.3230 0.3540 0.4429 -0.1711 -0.0835 0.0147 430 TRP A CB 3364 C CG . TRP A 430 ? 0.3196 0.3297 0.4336 -0.1622 -0.0950 0.0041 430 TRP A CG 3365 C CD1 . TRP A 430 ? 0.3838 0.4072 0.5026 -0.1494 -0.0990 -0.0059 430 TRP A CD1 3366 C CD2 . TRP A 430 ? 0.3407 0.3117 0.4408 -0.1650 -0.1032 0.0026 430 TRP A CD2 3367 N NE1 . TRP A 430 ? 0.3087 0.3052 0.4165 -0.1451 -0.1083 -0.0135 430 TRP A NE1 3368 C CE2 . TRP A 430 ? 0.3388 0.3035 0.4357 -0.1538 -0.1109 -0.0093 430 TRP A CE2 3369 C CE3 . TRP A 430 ? 0.3699 0.3089 0.4585 -0.1754 -0.1048 0.0101 430 TRP A CE3 3370 C CZ2 . TRP A 430 ? 0.3486 0.2801 0.4308 -0.1495 -0.1162 -0.0152 430 TRP A CZ2 3371 C CZ3 . TRP A 430 ? 0.5111 0.4149 0.5868 -0.1710 -0.1124 0.0041 430 TRP A CZ3 3372 C CH2 . TRP A 430 ? 0.3760 0.2781 0.4487 -0.1573 -0.1167 -0.0089 430 TRP A CH2 3373 N N . PRO A 431 ? 0.3973 0.4459 0.5239 -0.2101 -0.0638 0.0409 431 PRO A N 3374 C CA . PRO A 431 ? 0.4529 0.5180 0.5770 -0.2193 -0.0497 0.0524 431 PRO A CA 3375 C C . PRO A 431 ? 0.4228 0.5011 0.5357 -0.2015 -0.0410 0.0518 431 PRO A C 3376 O O . PRO A 431 ? 0.3455 0.4091 0.4467 -0.1833 -0.0468 0.0454 431 PRO A O 3377 C CB . PRO A 431 ? 0.5220 0.5453 0.6241 -0.2317 -0.0519 0.0648 431 PRO A CB 3378 C CG . PRO A 431 ? 0.4813 0.4664 0.5689 -0.2178 -0.0654 0.0582 431 PRO A CG 3379 C CD . PRO A 431 ? 0.4076 0.4086 0.5150 -0.2135 -0.0731 0.0440 431 PRO A CD 3380 N N . GLU A 432 ? 0.3641 0.4700 0.4802 -0.2074 -0.0267 0.0578 432 GLU A N 3381 C CA . GLU A 432 ? 0.5090 0.6310 0.6160 -0.1912 -0.0180 0.0551 432 GLU A CA 3382 C C . GLU A 432 ? 0.4148 0.5040 0.4893 -0.1821 -0.0199 0.0608 432 GLU A C 3383 O O . GLU A 432 ? 0.3962 0.4903 0.4617 -0.1654 -0.0183 0.0550 432 GLU A O 3384 C CB . GLU A 432 ? 0.6166 0.7790 0.7356 -0.1988 -0.0011 0.0582 432 GLU A CB 3385 C CG . GLU A 432 ? 0.8492 1.0026 0.9470 -0.2128 0.0100 0.0730 432 GLU A CG 3386 C CD . GLU A 432 ? 1.0389 1.2358 1.1522 -0.2231 0.0281 0.0754 432 GLU A CD 3387 O OE1 . GLU A 432 ? 1.0442 1.2782 1.1893 -0.2209 0.0305 0.0660 432 GLU A OE1 3388 O OE2 . GLU A 432 ? 1.1174 1.3120 1.2109 -0.2329 0.0401 0.0868 432 GLU A OE2 3389 N N . TRP A 433 ? 0.4385 0.4938 0.4957 -0.1927 -0.0245 0.0718 433 TRP A N 3390 C CA . TRP A 433 ? 0.4877 0.5118 0.5160 -0.1827 -0.0290 0.0772 433 TRP A CA 3391 C C . TRP A 433 ? 0.4191 0.4291 0.4466 -0.1632 -0.0406 0.0659 433 TRP A C 3392 O O . TRP A 433 ? 0.3865 0.3836 0.3960 -0.1509 -0.0432 0.0665 433 TRP A O 3393 C CB . TRP A 433 ? 0.4678 0.4551 0.4774 -0.1963 -0.0331 0.0920 433 TRP A CB 3394 C CG . TRP A 433 ? 0.4469 0.4020 0.4607 -0.1995 -0.0465 0.0901 433 TRP A CG 3395 C CD1 . TRP A 433 ? 0.5061 0.4544 0.5315 -0.2182 -0.0483 0.0932 433 TRP A CD1 3396 C CD2 . TRP A 433 ? 0.4429 0.3677 0.4482 -0.1840 -0.0595 0.0844 433 TRP A CD2 3397 N NE1 . TRP A 433 ? 0.4716 0.3850 0.4943 -0.2147 -0.0618 0.0890 433 TRP A NE1 3398 C CE2 . TRP A 433 ? 0.4584 0.3582 0.4696 -0.1933 -0.0682 0.0834 433 TRP A CE2 3399 C CE3 . TRP A 433 ? 0.4292 0.3473 0.4239 -0.1637 -0.0643 0.0793 433 TRP A CE3 3400 C CZ2 . TRP A 433 ? 0.5036 0.3719 0.5094 -0.1814 -0.0803 0.0771 433 TRP A CZ2 3401 C CZ3 . TRP A 433 ? 0.4291 0.3188 0.4211 -0.1527 -0.0763 0.0737 433 TRP A CZ3 3402 C CH2 . TRP A 433 ? 0.5045 0.3697 0.5016 -0.1609 -0.0836 0.0725 433 TRP A CH2 3403 N N . MET A 434 ? 0.4127 0.4261 0.4590 -0.1610 -0.0475 0.0557 434 MET A N 3404 C CA . MET A 434 ? 0.3660 0.3673 0.4108 -0.1436 -0.0568 0.0451 434 MET A CA 3405 C C . MET A 434 ? 0.3139 0.3414 0.3646 -0.1292 -0.0525 0.0354 434 MET A C 3406 O O . MET A 434 ? 0.2993 0.3182 0.3463 -0.1150 -0.0583 0.0278 434 MET A O 3407 C CB . MET A 434 ? 0.4345 0.4232 0.4911 -0.1464 -0.0667 0.0380 434 MET A CB 3408 C CG . MET A 434 ? 0.5205 0.4756 0.5686 -0.1591 -0.0726 0.0461 434 MET A CG 3409 S SD . MET A 434 ? 0.4558 0.3944 0.5150 -0.1648 -0.0839 0.0368 434 MET A SD 3410 C CE . MET A 434 ? 0.4288 0.3499 0.4792 -0.1425 -0.0914 0.0256 434 MET A CE 3411 N N . GLY A 435 ? 0.3091 0.3679 0.3690 -0.1327 -0.0418 0.0357 435 GLY A N 3412 C CA . GLY A 435 ? 0.2900 0.3698 0.3512 -0.1187 -0.0365 0.0277 435 GLY A CA 3413 C C . GLY A 435 ? 0.2844 0.3704 0.3587 -0.1067 -0.0429 0.0155 435 GLY A C 3414 O O . GLY A 435 ? 0.2712 0.3641 0.3626 -0.1115 -0.0474 0.0120 435 GLY A O 3415 N N . VAL A 436 ? 0.2721 0.3548 0.3372 -0.0921 -0.0437 0.0093 436 VAL A N 3416 C CA . VAL A 436 ? 0.2551 0.3431 0.3290 -0.0803 -0.0482 -0.0013 436 VAL A CA 3417 C C . VAL A 436 ? 0.3093 0.3708 0.3765 -0.0765 -0.0587 -0.0038 436 VAL A C 3418 O O . VAL A 436 ? 0.2796 0.3268 0.3337 -0.0685 -0.0608 -0.0052 436 VAL A O 3419 C CB . VAL A 436 ? 0.2583 0.3552 0.3247 -0.0678 -0.0427 -0.0066 436 VAL A CB 3420 C CG1 . VAL A 436 ? 0.2116 0.3098 0.2844 -0.0561 -0.0475 -0.0163 436 VAL A CG1 3421 C CG2 . VAL A 436 ? 0.2508 0.3738 0.3221 -0.0704 -0.0308 -0.0052 436 VAL A CG2 3422 N N . MET A 437 ? 0.2442 0.3003 0.3207 -0.0827 -0.0650 -0.0051 437 MET A N 3423 C CA . MET A 437 ? 0.2395 0.2684 0.3083 -0.0821 -0.0734 -0.0063 437 MET A CA 3424 C C . MET A 437 ? 0.3085 0.3305 0.3746 -0.0704 -0.0781 -0.0152 437 MET A C 3425 O O . MET A 437 ? 0.2142 0.2509 0.2862 -0.0641 -0.0772 -0.0207 437 MET A O 3426 C CB . MET A 437 ? 0.2517 0.2741 0.3286 -0.0947 -0.0785 -0.0048 437 MET A CB 3427 C CG . MET A 437 ? 0.3859 0.4030 0.4606 -0.1086 -0.0752 0.0057 437 MET A CG 3428 S SD . MET A 437 ? 0.3135 0.3273 0.4009 -0.1262 -0.0808 0.0066 437 MET A SD 3429 C CE . MET A 437 ? 0.2944 0.2737 0.3718 -0.1205 -0.0922 -0.0010 437 MET A CE 3430 N N . HIS A 438 ? 0.2576 0.2564 0.3147 -0.0676 -0.0829 -0.0162 438 HIS A N 3431 C CA . HIS A 438 ? 0.2442 0.2342 0.2977 -0.0585 -0.0866 -0.0243 438 HIS A CA 3432 C C . HIS A 438 ? 0.2728 0.2685 0.3332 -0.0605 -0.0905 -0.0301 438 HIS A C 3433 O O . HIS A 438 ? 0.2470 0.2365 0.3108 -0.0691 -0.0950 -0.0299 438 HIS A O 3434 C CB . HIS A 438 ? 0.2514 0.2169 0.2972 -0.0570 -0.0906 -0.0244 438 HIS A CB 3435 C CG . HIS A 438 ? 0.2709 0.2287 0.3128 -0.0479 -0.0922 -0.0324 438 HIS A CG 3436 N ND1 . HIS A 438 ? 0.3068 0.2711 0.3462 -0.0395 -0.0892 -0.0348 438 HIS A ND1 3437 C CD2 . HIS A 438 ? 0.2687 0.2127 0.3078 -0.0467 -0.0958 -0.0388 438 HIS A CD2 3438 C CE1 . HIS A 438 ? 0.3163 0.2726 0.3528 -0.0341 -0.0901 -0.0415 438 HIS A CE1 3439 N NE2 . HIS A 438 ? 0.2646 0.2088 0.3001 -0.0377 -0.0938 -0.0443 438 HIS A NE2 3440 N N . GLY A 439 ? 0.2265 0.2327 0.2878 -0.0530 -0.0899 -0.0350 439 GLY A N 3441 C CA . GLY A 439 ? 0.2102 0.2208 0.2753 -0.0534 -0.0953 -0.0400 439 GLY A CA 3442 C C . GLY A 439 ? 0.2885 0.3236 0.3675 -0.0551 -0.0950 -0.0389 439 GLY A C 3443 O O . GLY A 439 ? 0.2111 0.2531 0.2944 -0.0538 -0.1007 -0.0426 439 GLY A O 3444 N N . TYR A 440 ? 0.2726 0.3224 0.3589 -0.0575 -0.0885 -0.0340 440 TYR A N 3445 C CA . TYR A 440 ? 0.2340 0.3105 0.3372 -0.0597 -0.0873 -0.0334 440 TYR A CA 3446 C C . TYR A 440 ? 0.2347 0.3268 0.3410 -0.0481 -0.0827 -0.0357 440 TYR A C 3447 O O . TYR A 440 ? 0.2080 0.3248 0.3298 -0.0479 -0.0795 -0.0353 440 TYR A O 3448 C CB . TYR A 440 ? 0.2073 0.2939 0.3203 -0.0728 -0.0834 -0.0270 440 TYR A CB 3449 C CG . TYR A 440 ? 0.2405 0.3146 0.3553 -0.0848 -0.0911 -0.0266 440 TYR A CG 3450 C CD1 . TYR A 440 ? 0.2389 0.2849 0.3398 -0.0887 -0.0929 -0.0245 440 TYR A CD1 3451 C CD2 . TYR A 440 ? 0.2477 0.3372 0.3780 -0.0912 -0.0976 -0.0292 440 TYR A CD2 3452 C CE1 . TYR A 440 ? 0.2662 0.2970 0.3671 -0.0993 -0.1002 -0.0255 440 TYR A CE1 3453 C CE2 . TYR A 440 ? 0.2707 0.3468 0.4011 -0.1031 -0.1056 -0.0302 440 TYR A CE2 3454 C CZ . TYR A 440 ? 0.2900 0.3353 0.4048 -0.1071 -0.1065 -0.0286 440 TYR A CZ 3455 O OH . TYR A 440 ? 0.2800 0.3085 0.3933 -0.1183 -0.1145 -0.0307 440 TYR A OH 3456 N N . GLU A 441 ? 0.2045 0.2823 0.2971 -0.0385 -0.0822 -0.0387 441 GLU A N 3457 C CA . GLU A 441 ? 0.1949 0.2806 0.2882 -0.0269 -0.0806 -0.0424 441 GLU A CA 3458 C C . GLU A 441 ? 0.2764 0.3584 0.3696 -0.0222 -0.0895 -0.0458 441 GLU A C 3459 O O . GLU A 441 ? 0.2405 0.3308 0.3378 -0.0129 -0.0908 -0.0481 441 GLU A O 3460 C CB . GLU A 441 ? 0.1799 0.2510 0.2577 -0.0205 -0.0761 -0.0436 441 GLU A CB 3461 C CG . GLU A 441 ? 0.2369 0.2869 0.3015 -0.0171 -0.0805 -0.0465 441 GLU A CG 3462 C CD . GLU A 441 ? 0.3021 0.3378 0.3614 -0.0241 -0.0837 -0.0454 441 GLU A CD 3463 O OE1 . GLU A 441 ? 0.3249 0.3628 0.3890 -0.0318 -0.0832 -0.0418 441 GLU A OE1 3464 O OE2 . GLU A 441 ? 0.2738 0.2950 0.3236 -0.0219 -0.0864 -0.0483 441 GLU A OE2 3465 N N . ILE A 442 ? 0.1877 0.2558 0.2746 -0.0280 -0.0958 -0.0464 442 ILE A N 3466 C CA . ILE A 442 ? 0.2342 0.2935 0.3138 -0.0240 -0.1040 -0.0496 442 ILE A CA 3467 C C . ILE A 442 ? 0.2615 0.3405 0.3553 -0.0206 -0.1108 -0.0502 442 ILE A C 3468 O O . ILE A 442 ? 0.2518 0.3283 0.3406 -0.0111 -0.1149 -0.0516 442 ILE A O 3469 C CB . ILE A 442 ? 0.2013 0.2434 0.2712 -0.0315 -0.1091 -0.0513 442 ILE A CB 3470 C CG1 . ILE A 442 ? 0.2685 0.2911 0.3249 -0.0313 -0.1034 -0.0516 442 ILE A CG1 3471 C CG2 . ILE A 442 ? 0.2108 0.2459 0.2713 -0.0283 -0.1179 -0.0545 442 ILE A CG2 3472 C CD1 . ILE A 442 ? 0.2293 0.2352 0.2779 -0.0378 -0.1067 -0.0540 442 ILE A CD1 3473 N N . GLU A 443 ? 0.2142 0.3132 0.3265 -0.0286 -0.1124 -0.0489 443 GLU A N 3474 C CA . GLU A 443 ? 0.2278 0.3511 0.3586 -0.0258 -0.1193 -0.0497 443 GLU A CA 3475 C C . GLU A 443 ? 0.1922 0.3310 0.3320 -0.0123 -0.1146 -0.0502 443 GLU A C 3476 O O . GLU A 443 ? 0.2979 0.4511 0.4488 -0.0043 -0.1219 -0.0515 443 GLU A O 3477 C CB . GLU A 443 ? 0.2196 0.3636 0.3709 -0.0392 -0.1202 -0.0481 443 GLU A CB 3478 C CG . GLU A 443 ? 0.2595 0.4155 0.4202 -0.0450 -0.1077 -0.0443 443 GLU A CG 3479 C CD . GLU A 443 ? 0.3153 0.4794 0.4881 -0.0626 -0.1086 -0.0414 443 GLU A CD 3480 O OE1 . GLU A 443 ? 0.2812 0.4209 0.4396 -0.0711 -0.1089 -0.0399 443 GLU A OE1 3481 O OE2 . GLU A 443 ? 0.3350 0.5294 0.5323 -0.0679 -0.1093 -0.0408 443 GLU A OE2 3482 N N . PHE A 444 ? 0.1868 0.3220 0.3215 -0.0092 -0.1032 -0.0495 444 PHE A N 3483 C CA . PHE A 444 ? 0.3065 0.4513 0.4459 0.0044 -0.0984 -0.0515 444 PHE A CA 3484 C C . PHE A 444 ? 0.2481 0.3697 0.3694 0.0159 -0.1032 -0.0533 444 PHE A C 3485 O O . PHE A 444 ? 0.2478 0.3757 0.3748 0.0282 -0.1069 -0.0550 444 PHE A O 3486 C CB . PHE A 444 ? 0.2080 0.3574 0.3465 0.0032 -0.0850 -0.0511 444 PHE A CB 3487 C CG . PHE A 444 ? 0.2066 0.3848 0.3658 -0.0054 -0.0790 -0.0489 444 PHE A CG 3488 C CD1 . PHE A 444 ? 0.1944 0.3709 0.3544 -0.0212 -0.0789 -0.0446 444 PHE A CD1 3489 C CD2 . PHE A 444 ? 0.2802 0.4871 0.4588 0.0021 -0.0734 -0.0512 444 PHE A CD2 3490 C CE1 . PHE A 444 ? 0.2415 0.4433 0.4198 -0.0312 -0.0730 -0.0416 444 PHE A CE1 3491 C CE2 . PHE A 444 ? 0.2337 0.4700 0.4326 -0.0073 -0.0664 -0.0489 444 PHE A CE2 3492 C CZ . PHE A 444 ? 0.2146 0.4480 0.4129 -0.0249 -0.0662 -0.0436 444 PHE A CZ 3493 N N . VAL A 445 ? 0.2372 0.3323 0.3373 0.0116 -0.1031 -0.0527 445 VAL A N 3494 C CA . VAL A 445 ? 0.2030 0.2738 0.2835 0.0187 -0.1067 -0.0534 445 VAL A CA 3495 C C . VAL A 445 ? 0.2569 0.3268 0.3363 0.0231 -0.1190 -0.0528 445 VAL A C 3496 O O . VAL A 445 ? 0.2601 0.3204 0.3320 0.0338 -0.1228 -0.0526 445 VAL A O 3497 C CB . VAL A 445 ? 0.2116 0.2596 0.2734 0.0110 -0.1037 -0.0530 445 VAL A CB 3498 C CG1 . VAL A 445 ? 0.2265 0.2507 0.2681 0.0159 -0.1064 -0.0532 445 VAL A CG1 3499 C CG2 . VAL A 445 ? 0.2271 0.2750 0.2886 0.0081 -0.0936 -0.0532 445 VAL A CG2 3500 N N . PHE A 446 ? 0.2143 0.2925 0.2999 0.0146 -0.1260 -0.0524 446 PHE A N 3501 C CA . PHE A 446 ? 0.2272 0.3050 0.3098 0.0175 -0.1395 -0.0521 446 PHE A CA 3502 C C . PHE A 446 ? 0.2279 0.3348 0.3357 0.0252 -0.1458 -0.0522 446 PHE A C 3503 O O . PHE A 446 ? 0.2613 0.3728 0.3706 0.0291 -0.1590 -0.0517 446 PHE A O 3504 C CB . PHE A 446 ? 0.2311 0.3031 0.3070 0.0049 -0.1453 -0.0531 446 PHE A CB 3505 C CG . PHE A 446 ? 0.2382 0.2803 0.2864 0.0016 -0.1427 -0.0537 446 PHE A CG 3506 C CD1 . PHE A 446 ? 0.2339 0.2661 0.2772 -0.0042 -0.1319 -0.0544 446 PHE A CD1 3507 C CD2 . PHE A 446 ? 0.2560 0.2814 0.2832 0.0046 -0.1508 -0.0534 446 PHE A CD2 3508 C CE1 . PHE A 446 ? 0.2927 0.3014 0.3141 -0.0065 -0.1286 -0.0557 446 PHE A CE1 3509 C CE2 . PHE A 446 ? 0.3488 0.3493 0.3512 0.0012 -0.1463 -0.0544 446 PHE A CE2 3510 C CZ . PHE A 446 ? 0.3233 0.3170 0.3246 -0.0042 -0.1348 -0.0559 446 PHE A CZ 3511 N N . GLY A 447 ? 0.2412 0.3690 0.3688 0.0278 -0.1367 -0.0531 447 GLY A N 3512 C CA . GLY A 447 ? 0.2270 0.3837 0.3798 0.0383 -0.1403 -0.0541 447 GLY A CA 3513 C C . GLY A 447 ? 0.2164 0.4044 0.3950 0.0305 -0.1482 -0.0543 447 GLY A C 3514 O O . GLY A 447 ? 0.2226 0.4329 0.4202 0.0396 -0.1558 -0.0546 447 GLY A O 3515 N N . LEU A 448 ? 0.2133 0.4020 0.3925 0.0134 -0.1462 -0.0537 448 LEU A N 3516 C CA . LEU A 448 ? 0.2194 0.4342 0.4203 0.0023 -0.1507 -0.0527 448 LEU A CA 3517 C C . LEU A 448 ? 0.2383 0.4940 0.4739 0.0059 -0.1448 -0.0532 448 LEU A C 3518 O O . LEU A 448 ? 0.2359 0.5148 0.4895 0.0059 -0.1507 -0.0515 448 LEU A O 3519 C CB . LEU A 448 ? 0.2479 0.4515 0.4411 -0.0169 -0.1480 -0.0517 448 LEU A CB 3520 C CG . LEU A 448 ? 0.2880 0.4665 0.4569 -0.0234 -0.1565 -0.0513 448 LEU A CG 3521 C CD1 . LEU A 448 ? 0.3142 0.4590 0.4532 -0.0149 -0.1570 -0.0523 448 LEU A CD1 3522 C CD2 . LEU A 448 ? 0.3004 0.4716 0.4661 -0.0416 -0.1539 -0.0513 448 LEU A CD2 3523 N N . PRO A 449 ? 0.2500 0.5127 0.4910 0.0086 -0.1305 -0.0545 449 PRO A N 3524 C CA . PRO A 449 ? 0.2531 0.5568 0.5267 0.0119 -0.1228 -0.0559 449 PRO A CA 3525 C C . PRO A 449 ? 0.2446 0.5649 0.5328 0.0328 -0.1277 -0.0586 449 PRO A C 3526 O O . PRO A 449 ? 0.2539 0.6087 0.5695 0.0365 -0.1208 -0.0595 449 PRO A O 3527 C CB . PRO A 449 ? 0.1849 0.4818 0.4485 0.0101 -0.1042 -0.0553 449 PRO A CB 3528 C CG . PRO A 449 ? 0.2770 0.5366 0.5107 -0.0011 -0.1040 -0.0523 449 PRO A CG 3529 C CD . PRO A 449 ? 0.1904 0.4253 0.4069 0.0049 -0.1183 -0.0532 449 PRO A CD 3530 N N . LEU A 450 ? 0.2068 0.5000 0.4744 0.0457 -0.1377 -0.0585 450 LEU A N 3531 C CA . LEU A 450 ? 0.2201 0.5221 0.4972 0.0647 -0.1432 -0.0588 450 LEU A CA 3532 C C . LEU A 450 ? 0.2299 0.5570 0.5272 0.0600 -0.1522 -0.0550 450 LEU A C 3533 O O . LEU A 450 ? 0.2680 0.6170 0.5856 0.0731 -0.1539 -0.0552 450 LEU A O 3534 C CB . LEU A 450 ? 0.3042 0.5678 0.5516 0.0776 -0.1523 -0.0581 450 LEU A CB 3535 C CG . LEU A 450 ? 0.3037 0.5369 0.5266 0.0803 -0.1433 -0.0604 450 LEU A CG 3536 C CD1 . LEU A 450 ? 0.3250 0.5196 0.5183 0.0907 -0.1520 -0.0583 450 LEU A CD1 3537 C CD2 . LEU A 450 ? 0.3270 0.5752 0.5626 0.0897 -0.1278 -0.0648 450 LEU A CD2 3538 N N . GLU A 451 ? 0.3387 0.6621 0.6304 0.0414 -0.1584 -0.0518 451 GLU A N 3539 C CA . GLU A 451 ? 0.3933 0.7420 0.7044 0.0342 -0.1675 -0.0485 451 GLU A CA 3540 C C . GLU A 451 ? 0.3815 0.7710 0.7281 0.0251 -0.1570 -0.0484 451 GLU A C 3541 O O . GLU A 451 ? 0.3135 0.7054 0.6620 0.0069 -0.1499 -0.0477 451 GLU A O 3542 C CB . GLU A 451 ? 0.4283 0.7569 0.7181 0.0176 -0.1775 -0.0462 451 GLU A CB 3543 C CG . GLU A 451 ? 0.5721 0.9263 0.8796 0.0082 -0.1881 -0.0435 451 GLU A CG 3544 C CD . GLU A 451 ? 0.7198 1.0773 1.0271 0.0234 -0.2020 -0.0418 451 GLU A CD 3545 O OE1 . GLU A 451 ? 0.7650 1.1498 1.0990 0.0367 -0.2014 -0.0412 451 GLU A OE1 3546 O OE2 . GLU A 451 ? 0.7461 1.0790 1.0264 0.0221 -0.2132 -0.0411 451 GLU A OE2 3547 N N . ARG A 452 ? 0.4556 0.8760 0.8300 0.0379 -0.1557 -0.0488 452 ARG A N 3548 C CA . ARG A 452 ? 0.5656 1.0268 0.9754 0.0323 -0.1433 -0.0492 452 ARG A CA 3549 C C . ARG A 452 ? 0.5865 1.0677 1.0138 0.0096 -0.1483 -0.0445 452 ARG A C 3550 O O . ARG A 452 ? 0.5505 1.0606 1.0041 -0.0010 -0.1371 -0.0437 452 ARG A O 3551 C CB . ARG A 452 ? 0.6300 1.1183 1.0652 0.0530 -0.1419 -0.0511 452 ARG A CB 3552 C CG . ARG A 452 ? 0.7831 1.2448 1.1979 0.0770 -0.1458 -0.0541 452 ARG A CG 3553 C CD . ARG A 452 ? 0.9612 1.4311 1.3861 0.0910 -0.1610 -0.0514 452 ARG A CD 3554 N NE . ARG A 452 ? 1.0602 1.4921 1.4518 0.0943 -0.1768 -0.0486 452 ARG A NE 3555 C CZ . ARG A 452 ? 1.1028 1.5097 1.4769 0.1143 -0.1825 -0.0491 452 ARG A CZ 3556 N NH1 . ARG A 452 ? 1.0947 1.5093 1.4813 0.1336 -0.1744 -0.0530 452 ARG A NH1 3557 N NH2 . ARG A 452 ? 1.1234 1.4960 1.4661 0.1146 -0.1958 -0.0457 452 ARG A NH2 3558 N N . ARG A 453 ? 0.6048 1.0698 1.0163 0.0018 -0.1645 -0.0415 453 ARG A N 3559 C CA . ARG A 453 ? 0.6970 1.1787 1.1229 -0.0197 -0.1715 -0.0375 453 ARG A CA 3560 C C . ARG A 453 ? 0.7121 1.1737 1.1220 -0.0420 -0.1661 -0.0366 453 ARG A C 3561 O O . ARG A 453 ? 0.7348 1.2039 1.1525 -0.0618 -0.1716 -0.0335 453 ARG A O 3562 C CB . ARG A 453 ? 0.7607 1.2359 1.1743 -0.0189 -0.1912 -0.0360 453 ARG A CB 3563 C CG . ARG A 453 ? 0.8386 1.3131 1.2503 0.0059 -0.1991 -0.0368 453 ARG A CG 3564 C CD . ARG A 453 ? 0.8834 1.3742 1.3030 0.0050 -0.2173 -0.0340 453 ARG A CD 3565 N NE . ARG A 453 ? 0.9500 1.4832 1.4110 0.0152 -0.2180 -0.0322 453 ARG A NE 3566 C CZ . ARG A 453 ? 1.0150 1.5783 1.4988 0.0097 -0.2309 -0.0290 453 ARG A CZ 3567 N NH1 . ARG A 453 ? 1.0278 1.5832 1.4947 -0.0066 -0.2441 -0.0280 453 ARG A NH1 3568 N NH2 . ARG A 453 ? 1.0437 1.6459 1.5673 0.0206 -0.2302 -0.0277 453 ARG A NH2 3569 N N . ASP A 454 ? 0.6901 1.1256 1.0781 -0.0390 -0.1559 -0.0393 454 ASP A N 3570 C CA . ASP A 454 ? 0.7672 1.1758 1.1335 -0.0576 -0.1533 -0.0386 454 ASP A CA 3571 C C . ASP A 454 ? 0.6954 1.1086 1.0713 -0.0677 -0.1367 -0.0379 454 ASP A C 3572 O O . ASP A 454 ? 0.7348 1.1191 1.0870 -0.0752 -0.1328 -0.0384 454 ASP A O 3573 C CB . ASP A 454 ? 0.8938 1.2597 1.2198 -0.0503 -0.1583 -0.0419 454 ASP A CB 3574 C CG . ASP A 454 ? 1.0577 1.4080 1.3641 -0.0559 -0.1729 -0.0428 454 ASP A CG 3575 O OD1 . ASP A 454 ? 1.1148 1.4551 1.4111 -0.0741 -0.1738 -0.0441 454 ASP A OD1 3576 O OD2 . ASP A 454 ? 1.1140 1.4612 1.4136 -0.0418 -0.1827 -0.0434 454 ASP A OD2 3577 N N . GLN A 455 ? 0.6233 1.0728 1.0322 -0.0676 -0.1260 -0.0374 455 GLN A N 3578 C CA . GLN A 455 ? 0.6082 1.0678 1.0269 -0.0809 -0.1085 -0.0364 455 GLN A CA 3579 C C . GLN A 455 ? 0.5203 0.9750 0.9240 -0.0720 -0.0922 -0.0391 455 GLN A C 3580 O O . GLN A 455 ? 0.5509 1.0192 0.9606 -0.0824 -0.0761 -0.0370 455 GLN A O 3581 C CB . GLN A 455 ? 0.6538 1.0904 1.0640 -0.1047 -0.1119 -0.0338 455 GLN A CB 3582 C CG . GLN A 455 ? 0.6885 1.1481 1.1297 -0.1208 -0.1128 -0.0327 455 GLN A CG 3583 C CD . GLN A 455 ? 0.7251 1.1932 1.1808 -0.1175 -0.1323 -0.0329 455 GLN A CD 3584 O OE1 . GLN A 455 ? 0.7890 1.2283 1.2172 -0.1144 -0.1469 -0.0324 455 GLN A OE1 3585 N NE2 . GLN A 455 ? 0.6438 1.1516 1.1362 -0.1185 -0.1311 -0.0321 455 GLN A NE2 3586 N N . TYR A 456 ? 0.3581 0.7929 0.7408 -0.0540 -0.0961 -0.0434 456 TYR A N 3587 C CA . TYR A 456 ? 0.2963 0.7278 0.6666 -0.0450 -0.0819 -0.0470 456 TYR A CA 3588 C C . TYR A 456 ? 0.2500 0.7187 0.6438 -0.0328 -0.0677 -0.0497 456 TYR A C 3589 O O . TYR A 456 ? 0.2470 0.7388 0.6642 -0.0241 -0.0719 -0.0503 456 TYR A O 3590 C CB . TYR A 456 ? 0.1844 0.5795 0.5255 -0.0282 -0.0896 -0.0505 456 TYR A CB 3591 C CG . TYR A 456 ? 0.1985 0.5517 0.5107 -0.0378 -0.1001 -0.0481 456 TYR A CG 3592 C CD1 . TYR A 456 ? 0.2430 0.5643 0.5277 -0.0455 -0.0918 -0.0445 456 TYR A CD1 3593 C CD2 . TYR A 456 ? 0.1895 0.5324 0.4984 -0.0379 -0.1175 -0.0486 456 TYR A CD2 3594 C CE1 . TYR A 456 ? 0.3344 0.6192 0.5945 -0.0522 -0.1003 -0.0434 456 TYR A CE1 3595 C CE2 . TYR A 456 ? 0.2728 0.5784 0.5543 -0.0455 -0.1255 -0.0478 456 TYR A CE2 3596 C CZ . TYR A 456 ? 0.3579 0.6361 0.6175 -0.0522 -0.1168 -0.0460 456 TYR A CZ 3597 O OH . TYR A 456 ? 0.3648 0.6071 0.5989 -0.0582 -0.1236 -0.0459 456 TYR A OH 3598 N N . THR A 457 ? 0.2261 0.6957 0.6097 -0.0317 -0.0505 -0.0505 457 THR A N 3599 C CA . THR A 457 ? 0.1978 0.7020 0.6003 -0.0191 -0.0348 -0.0551 457 THR A CA 3600 C C . THR A 457 ? 0.2212 0.7151 0.6170 0.0087 -0.0390 -0.0625 457 THR A C 3601 O O . THR A 457 ? 0.1825 0.6385 0.5539 0.0163 -0.0516 -0.0628 457 THR A O 3602 C CB . THR A 457 ? 0.1960 0.6916 0.5778 -0.0264 -0.0146 -0.0520 457 THR A CB 3603 O OG1 . THR A 457 ? 0.1891 0.6374 0.5311 -0.0182 -0.0163 -0.0524 457 THR A OG1 3604 C CG2 . THR A 457 ? 0.1953 0.6930 0.5774 -0.0542 -0.0100 -0.0430 457 THR A CG2 3605 N N . LYS A 458 ? 0.1892 0.7125 0.6038 0.0233 -0.0272 -0.0678 458 LYS A N 3606 C CA . LYS A 458 ? 0.2332 0.7462 0.6416 0.0503 -0.0290 -0.0755 458 LYS A CA 3607 C C . LYS A 458 ? 0.1962 0.6643 0.5630 0.0550 -0.0241 -0.0768 458 LYS A C 3608 O O . LYS A 458 ? 0.2219 0.6573 0.5694 0.0691 -0.0344 -0.0792 458 LYS A O 3609 C CB . LYS A 458 ? 0.3019 0.8483 0.7329 0.0628 -0.0137 -0.0801 458 LYS A CB 3610 C CG . LYS A 458 ? 0.3535 0.8870 0.7795 0.0912 -0.0166 -0.0878 458 LYS A CG 3611 C CD . LYS A 458 ? 0.4952 1.0174 0.9276 0.0999 -0.0384 -0.0847 458 LYS A CD 3612 C CE . LYS A 458 ? 0.5592 1.0559 0.9780 0.1263 -0.0440 -0.0905 458 LYS A CE 3613 N NZ . LYS A 458 ? 0.5965 1.0882 1.0240 0.1349 -0.0636 -0.0863 458 LYS A NZ 3614 N N . ALA A 459 ? 0.2005 0.6640 0.5510 0.0420 -0.0086 -0.0740 459 ALA A N 3615 C CA . ALA A 459 ? 0.2028 0.6243 0.5133 0.0440 -0.0040 -0.0743 459 ALA A CA 3616 C C . ALA A 459 ? 0.2347 0.6135 0.5209 0.0388 -0.0202 -0.0697 459 ALA A C 3617 O O . ALA A 459 ? 0.2168 0.5606 0.4761 0.0480 -0.0231 -0.0722 459 ALA A O 3618 C CB . ALA A 459 ? 0.2079 0.6335 0.5055 0.0282 0.0130 -0.0702 459 ALA A CB 3619 N N . GLU A 460 ? 0.2273 0.6093 0.5231 0.0236 -0.0306 -0.0636 460 GLU A N 3620 C CA . GLU A 460 ? 0.2529 0.5963 0.5256 0.0179 -0.0445 -0.0598 460 GLU A CA 3621 C C . GLU A 460 ? 0.2420 0.5735 0.5149 0.0337 -0.0597 -0.0633 460 GLU A C 3622 O O . GLU A 460 ? 0.2730 0.5676 0.5197 0.0365 -0.0670 -0.0626 460 GLU A O 3623 C CB . GLU A 460 ? 0.2657 0.6128 0.5453 -0.0038 -0.0499 -0.0531 460 GLU A CB 3624 C CG . GLU A 460 ? 0.2535 0.5954 0.5209 -0.0204 -0.0375 -0.0473 460 GLU A CG 3625 C CD . GLU A 460 ? 0.2729 0.6200 0.5502 -0.0421 -0.0421 -0.0408 460 GLU A CD 3626 O OE1 . GLU A 460 ? 0.2671 0.6442 0.5736 -0.0465 -0.0475 -0.0416 460 GLU A OE1 3627 O OE2 . GLU A 460 ? 0.2438 0.5645 0.4998 -0.0545 -0.0409 -0.0352 460 GLU A OE2 3628 N N . GLU A 461 ? 0.2044 0.5678 0.5069 0.0437 -0.0645 -0.0664 461 GLU A N 3629 C CA . GLU A 461 ? 0.1943 0.5472 0.4963 0.0618 -0.0784 -0.0694 461 GLU A CA 3630 C C . GLU A 461 ? 0.3201 0.6433 0.5974 0.0776 -0.0727 -0.0736 461 GLU A C 3631 O O . GLU A 461 ? 0.2880 0.5755 0.5415 0.0830 -0.0821 -0.0727 461 GLU A O 3632 C CB . GLU A 461 ? 0.1970 0.5937 0.5379 0.0730 -0.0824 -0.0729 461 GLU A CB 3633 C CG . GLU A 461 ? 0.4069 0.7898 0.7449 0.0937 -0.0962 -0.0745 461 GLU A CG 3634 C CD . GLU A 461 ? 0.4657 0.8799 0.8330 0.1026 -0.0980 -0.0736 461 GLU A CD 3635 O OE1 . GLU A 461 ? 0.5203 0.9706 0.9139 0.0912 -0.0907 -0.0721 461 GLU A OE1 3636 O OE2 . GLU A 461 ? 0.4080 0.8098 0.7717 0.1205 -0.1071 -0.0740 461 GLU A OE2 3637 N N . ILE A 462 ? 0.3186 0.6560 0.6003 0.0837 -0.0567 -0.0784 462 ILE A N 3638 C CA . ILE A 462 ? 0.3303 0.6409 0.5892 0.0981 -0.0505 -0.0840 462 ILE A CA 3639 C C . ILE A 462 ? 0.3391 0.6063 0.5612 0.0882 -0.0511 -0.0808 462 ILE A C 3640 O O . ILE A 462 ? 0.3120 0.5464 0.5131 0.0977 -0.0563 -0.0828 462 ILE A O 3641 C CB . ILE A 462 ? 0.3492 0.6840 0.6169 0.1039 -0.0318 -0.0905 462 ILE A CB 3642 C CG1 . ILE A 462 ? 0.4078 0.7894 0.7154 0.1156 -0.0296 -0.0948 462 ILE A CG1 3643 C CG2 . ILE A 462 ? 0.3403 0.6439 0.5819 0.1181 -0.0265 -0.0976 462 ILE A CG2 3644 C CD1 . ILE A 462 ? 0.4963 0.8733 0.8142 0.1368 -0.0442 -0.0979 462 ILE A CD1 3645 N N . LEU A 463 ? 0.2065 0.4738 0.4215 0.0692 -0.0458 -0.0757 463 LEU A N 3646 C CA . LEU A 463 ? 0.2761 0.5072 0.4602 0.0599 -0.0464 -0.0727 463 LEU A CA 3647 C C . LEU A 463 ? 0.2607 0.4643 0.4326 0.0595 -0.0613 -0.0696 463 LEU A C 3648 O O . LEU A 463 ? 0.2672 0.4391 0.4157 0.0630 -0.0633 -0.0707 463 LEU A O 3649 C CB . LEU A 463 ? 0.1973 0.4349 0.3788 0.0406 -0.0396 -0.0668 463 LEU A CB 3650 C CG . LEU A 463 ? 0.2599 0.4640 0.4134 0.0309 -0.0414 -0.0631 463 LEU A CG 3651 C CD1 . LEU A 463 ? 0.2037 0.3856 0.3347 0.0397 -0.0364 -0.0683 463 LEU A CD1 3652 C CD2 . LEU A 463 ? 0.2647 0.4761 0.4175 0.0138 -0.0354 -0.0567 463 LEU A CD2 3653 N N . SER A 464 ? 0.1982 0.4146 0.3854 0.0545 -0.0714 -0.0662 464 SER A N 3654 C CA . SER A 464 ? 0.2232 0.4154 0.3974 0.0533 -0.0852 -0.0634 464 SER A CA 3655 C C . SER A 464 ? 0.2299 0.4053 0.3962 0.0709 -0.0921 -0.0661 464 SER A C 3656 O O . SER A 464 ? 0.2626 0.4058 0.4054 0.0711 -0.0973 -0.0646 464 SER A O 3657 C CB . SER A 464 ? 0.2844 0.4965 0.4773 0.0448 -0.0953 -0.0604 464 SER A CB 3658 O OG . SER A 464 ? 0.2010 0.3897 0.3785 0.0442 -0.1084 -0.0584 464 SER A OG 3659 N N . ARG A 465 ? 0.2197 0.4169 0.4059 0.0856 -0.0920 -0.0699 465 ARG A N 3660 C CA . ARG A 465 ? 0.3015 0.4813 0.4807 0.1039 -0.0992 -0.0721 465 ARG A CA 3661 C C . ARG A 465 ? 0.3314 0.4746 0.4819 0.1070 -0.0930 -0.0744 465 ARG A C 3662 O O . ARG A 465 ? 0.3599 0.4714 0.4903 0.1115 -0.1008 -0.0725 465 ARG A O 3663 C CB . ARG A 465 ? 0.2436 0.4545 0.4509 0.1212 -0.0976 -0.0772 465 ARG A CB 3664 C CG . ARG A 465 ? 0.2712 0.4619 0.4719 0.1422 -0.1065 -0.0791 465 ARG A CG 3665 C CD . ARG A 465 ? 0.3481 0.5308 0.5465 0.1433 -0.1254 -0.0728 465 ARG A CD 3666 N NE . ARG A 465 ? 0.4549 0.6038 0.6345 0.1594 -0.1347 -0.0717 465 ARG A NE 3667 C CZ . ARG A 465 ? 0.4985 0.6037 0.6440 0.1549 -0.1358 -0.0686 465 ARG A CZ 3668 N NH1 . ARG A 465 ? 0.2932 0.3850 0.4213 0.1364 -0.1284 -0.0670 465 ARG A NH1 3669 N NH2 . ARG A 465 ? 0.4930 0.5678 0.6223 0.1691 -0.1444 -0.0667 465 ARG A NH2 3670 N N A SER A 466 ? 0.2943 0.4420 0.4420 0.1033 -0.0792 -0.0782 466 SER A N 3671 N N B SER A 466 ? 0.2988 0.4457 0.4459 0.1033 -0.0793 -0.0782 466 SER A N 3672 C CA A SER A 466 ? 0.3052 0.4217 0.4274 0.1048 -0.0734 -0.0816 466 SER A CA 3673 C CA B SER A 466 ? 0.3078 0.4222 0.4290 0.1054 -0.0743 -0.0814 466 SER A CA 3674 C C A SER A 466 ? 0.3119 0.4009 0.4113 0.0902 -0.0767 -0.0766 466 SER A C 3675 C C B SER A 466 ? 0.3004 0.3887 0.3993 0.0901 -0.0768 -0.0765 466 SER A C 3676 O O A SER A 466 ? 0.2773 0.3347 0.3557 0.0922 -0.0790 -0.0771 466 SER A O 3677 O O B SER A 466 ? 0.2884 0.3452 0.3661 0.0916 -0.0787 -0.0771 466 SER A O 3678 C CB A SER A 466 ? 0.2496 0.3808 0.3739 0.1040 -0.0586 -0.0872 466 SER A CB 3679 C CB B SER A 466 ? 0.3107 0.4370 0.4331 0.1072 -0.0598 -0.0879 466 SER A CB 3680 O OG A SER A 466 ? 0.2873 0.3897 0.3858 0.1003 -0.0542 -0.0897 466 SER A OG 3681 O OG B SER A 466 ? 0.3268 0.4721 0.4541 0.0916 -0.0527 -0.0847 466 SER A OG 3682 N N . ILE A 467 ? 0.2434 0.3447 0.3479 0.0755 -0.0765 -0.0720 467 ILE A N 3683 C CA . ILE A 467 ? 0.2646 0.3441 0.3511 0.0627 -0.0792 -0.0679 467 ILE A CA 3684 C C . ILE A 467 ? 0.2318 0.2902 0.3074 0.0655 -0.0903 -0.0649 467 ILE A C 3685 O O . ILE A 467 ? 0.2601 0.2911 0.3154 0.0627 -0.0910 -0.0641 467 ILE A O 3686 C CB . ILE A 467 ? 0.3171 0.4130 0.4124 0.0480 -0.0777 -0.0639 467 ILE A CB 3687 C CG1 . ILE A 467 ? 0.3223 0.4283 0.4177 0.0426 -0.0662 -0.0651 467 ILE A CG1 3688 C CG2 . ILE A 467 ? 0.2177 0.2929 0.2982 0.0378 -0.0829 -0.0603 467 ILE A CG2 3689 C CD1 . ILE A 467 ? 0.1924 0.3086 0.2928 0.0276 -0.0645 -0.0601 467 ILE A CD1 3690 N N . VAL A 468 ? 0.2345 0.3070 0.3238 0.0709 -0.0991 -0.0632 468 VAL A N 3691 C CA . VAL A 468 ? 0.3490 0.4031 0.4267 0.0748 -0.1108 -0.0598 468 VAL A CA 3692 C C . VAL A 468 ? 0.3589 0.3846 0.4194 0.0859 -0.1114 -0.0608 468 VAL A C 3693 O O . VAL A 468 ? 0.3204 0.3179 0.3587 0.0821 -0.1146 -0.0577 468 VAL A O 3694 C CB . VAL A 468 ? 0.2500 0.3280 0.3479 0.0810 -0.1214 -0.0584 468 VAL A CB 3695 C CG1 . VAL A 468 ? 0.2849 0.3430 0.3696 0.0905 -0.1341 -0.0551 468 VAL A CG1 3696 C CG2 . VAL A 468 ? 0.2359 0.3317 0.3436 0.0661 -0.1241 -0.0564 468 VAL A CG2 3697 N N . LYS A 469 ? 0.2751 0.3074 0.3450 0.0991 -0.1075 -0.0656 469 LYS A N 3698 C CA . LYS A 469 ? 0.2989 0.3009 0.3519 0.1098 -0.1077 -0.0676 469 LYS A CA 3699 C C . LYS A 469 ? 0.3365 0.3119 0.3670 0.0989 -0.1005 -0.0685 469 LYS A C 3700 O O . LYS A 469 ? 0.3620 0.3057 0.3717 0.0983 -0.1041 -0.0659 469 LYS A O 3701 C CB . LYS A 469 ? 0.3067 0.3216 0.3745 0.1262 -0.1032 -0.0746 469 LYS A CB 3702 C CG . LYS A 469 ? 0.3336 0.3139 0.3829 0.1372 -0.1026 -0.0783 469 LYS A CG 3703 C CD . LYS A 469 ? 0.3788 0.3299 0.4130 0.1439 -0.1154 -0.0718 469 LYS A CD 3704 C CE . LYS A 469 ? 0.3737 0.3427 0.4276 0.1618 -0.1256 -0.0708 469 LYS A CE 3705 N NZ . LYS A 469 ? 0.3942 0.3330 0.4303 0.1686 -0.1396 -0.0631 469 LYS A NZ 3706 N N . ARG A 470 ? 0.2958 0.2844 0.3304 0.0897 -0.0909 -0.0717 470 ARG A N 3707 C CA . ARG A 470 ? 0.3787 0.3471 0.3955 0.0792 -0.0852 -0.0730 470 ARG A CA 3708 C C . ARG A 470 ? 0.3926 0.3445 0.3956 0.0673 -0.0892 -0.0671 470 ARG A C 3709 O O . ARG A 470 ? 0.3100 0.2361 0.2956 0.0630 -0.0885 -0.0668 470 ARG A O 3710 C CB . ARG A 470 ? 0.3537 0.3414 0.3773 0.0717 -0.0760 -0.0762 470 ARG A CB 3711 C CG . ARG A 470 ? 0.3741 0.3729 0.4038 0.0815 -0.0687 -0.0836 470 ARG A CG 3712 C CD . ARG A 470 ? 0.3407 0.3535 0.3702 0.0715 -0.0602 -0.0852 470 ARG A CD 3713 N NE . ARG A 470 ? 0.2961 0.3234 0.3301 0.0793 -0.0516 -0.0920 470 ARG A NE 3714 C CZ . ARG A 470 ? 0.3716 0.3828 0.3917 0.0850 -0.0475 -0.0998 470 ARG A CZ 3715 N NH1 . ARG A 470 ? 0.3554 0.3352 0.3576 0.0828 -0.0518 -0.1012 470 ARG A NH1 3716 N NH2 . ARG A 470 ? 0.3198 0.3461 0.3433 0.0924 -0.0387 -0.1067 470 ARG A NH2 3717 N N . TRP A 471 ? 0.3199 0.2871 0.3310 0.0613 -0.0928 -0.0630 471 TRP A N 3718 C CA . TRP A 471 ? 0.3666 0.3207 0.3650 0.0512 -0.0957 -0.0586 471 TRP A CA 3719 C C . TRP A 471 ? 0.3134 0.2423 0.2950 0.0561 -0.1025 -0.0548 471 TRP A C 3720 O O . TRP A 471 ? 0.3420 0.2495 0.3060 0.0487 -0.1009 -0.0526 471 TRP A O 3721 C CB . TRP A 471 ? 0.2508 0.2250 0.2606 0.0455 -0.0991 -0.0563 471 TRP A CB 3722 C CG . TRP A 471 ? 0.2324 0.2169 0.2469 0.0337 -0.0932 -0.0569 471 TRP A CG 3723 C CD1 . TRP A 471 ? 0.2438 0.2267 0.2545 0.0246 -0.0948 -0.0550 471 TRP A CD1 3724 C CD2 . TRP A 471 ? 0.2856 0.2819 0.3080 0.0310 -0.0857 -0.0594 471 TRP A CD2 3725 N NE1 . TRP A 471 ? 0.2324 0.2242 0.2494 0.0173 -0.0893 -0.0559 471 TRP A NE1 3726 C CE2 . TRP A 471 ? 0.2807 0.2808 0.3041 0.0206 -0.0840 -0.0579 471 TRP A CE2 3727 C CE3 . TRP A 471 ? 0.2300 0.2327 0.2567 0.0367 -0.0802 -0.0630 471 TRP A CE3 3728 C CZ2 . TRP A 471 ? 0.2003 0.2097 0.2286 0.0158 -0.0782 -0.0585 471 TRP A CZ2 3729 C CZ3 . TRP A 471 ? 0.2231 0.2362 0.2531 0.0311 -0.0737 -0.0641 471 TRP A CZ3 3730 C CH2 . TRP A 471 ? 0.2143 0.2302 0.2449 0.0206 -0.0733 -0.0611 471 TRP A CH2 3731 N N . ALA A 472 ? 0.3140 0.2464 0.3014 0.0684 -0.1102 -0.0536 472 ALA A N 3732 C CA . ALA A 472 ? 0.3653 0.2722 0.3357 0.0754 -0.1183 -0.0489 472 ALA A CA 3733 C C . ALA A 472 ? 0.4141 0.2903 0.3676 0.0773 -0.1144 -0.0499 472 ALA A C 3734 O O . ALA A 472 ? 0.4316 0.2800 0.3633 0.0726 -0.1163 -0.0449 472 ALA A O 3735 C CB . ALA A 472 ? 0.3384 0.2584 0.3224 0.0907 -0.1281 -0.0481 472 ALA A CB 3736 N N . ASN A 473 ? 0.3847 0.2647 0.3468 0.0836 -0.1088 -0.0565 473 ASN A N 3737 C CA . ASN A 473 ? 0.4299 0.2801 0.3761 0.0835 -0.1050 -0.0591 473 ASN A CA 3738 C C . ASN A 473 ? 0.4760 0.3154 0.4101 0.0660 -0.0984 -0.0587 473 ASN A C 3739 O O . ASN A 473 ? 0.3827 0.1922 0.2984 0.0612 -0.0980 -0.0568 473 ASN A O 3740 C CB . ASN A 473 ? 0.4516 0.3089 0.4082 0.0939 -0.1001 -0.0680 473 ASN A CB 3741 C CG . ASN A 473 ? 0.4848 0.3400 0.4482 0.1142 -0.1066 -0.0691 473 ASN A CG 3742 O OD1 . ASN A 473 ? 0.4214 0.2654 0.3794 0.1207 -0.1163 -0.0625 473 ASN A OD1 3743 N ND2 . ASN A 473 ? 0.3899 0.2557 0.3644 0.1249 -0.1012 -0.0779 473 ASN A ND2 3744 N N . PHE A 474 ? 0.3503 0.2134 0.2952 0.0562 -0.0933 -0.0602 474 PHE A N 3745 C CA . PHE A 474 ? 0.3391 0.1957 0.2757 0.0409 -0.0881 -0.0595 474 PHE A CA 3746 C C . PHE A 474 ? 0.4394 0.2784 0.3600 0.0345 -0.0909 -0.0524 474 PHE A C 3747 O O . PHE A 474 ? 0.4190 0.2369 0.3254 0.0262 -0.0879 -0.0510 474 PHE A O 3748 C CB . PHE A 474 ? 0.3387 0.2223 0.2893 0.0332 -0.0838 -0.0613 474 PHE A CB 3749 C CG . PHE A 474 ? 0.3239 0.2031 0.2691 0.0196 -0.0788 -0.0614 474 PHE A CG 3750 C CD1 . PHE A 474 ? 0.2981 0.1691 0.2399 0.0149 -0.0750 -0.0658 474 PHE A CD1 3751 C CD2 . PHE A 474 ? 0.2853 0.1691 0.2293 0.0120 -0.0782 -0.0578 474 PHE A CD2 3752 C CE1 . PHE A 474 ? 0.3015 0.1722 0.2419 0.0025 -0.0712 -0.0661 474 PHE A CE1 3753 C CE2 . PHE A 474 ? 0.2992 0.1821 0.2414 0.0008 -0.0730 -0.0585 474 PHE A CE2 3754 C CZ . PHE A 474 ? 0.2844 0.1622 0.2262 -0.0040 -0.0698 -0.0624 474 PHE A CZ 3755 N N . ALA A 475 ? 0.3378 0.1860 0.2600 0.0374 -0.0964 -0.0482 475 ALA A N 3756 C CA . ALA A 475 ? 0.3688 0.2009 0.2726 0.0314 -0.0987 -0.0417 475 ALA A CA 3757 C C . ALA A 475 ? 0.4306 0.2288 0.3134 0.0348 -0.1021 -0.0368 475 ALA A C 3758 O O . ALA A 475 ? 0.4162 0.1941 0.2811 0.0243 -0.0981 -0.0330 475 ALA A O 3759 C CB . ALA A 475 ? 0.3483 0.1948 0.2557 0.0350 -0.1058 -0.0389 475 ALA A CB 3760 N N . LYS A 476 ? 0.4163 0.2083 0.3016 0.0494 -0.1091 -0.0368 476 LYS A N 3761 C CA . LYS A 476 ? 0.4862 0.2427 0.3510 0.0551 -0.1142 -0.0316 476 LYS A CA 3762 C C . LYS A 476 ? 0.5265 0.2590 0.3822 0.0485 -0.1075 -0.0345 476 LYS A C 3763 O O . LYS A 476 ? 0.5095 0.2106 0.3430 0.0417 -0.1073 -0.0286 476 LYS A O 3764 C CB . LYS A 476 ? 0.4891 0.2467 0.3624 0.0751 -0.1238 -0.0321 476 LYS A CB 3765 C CG . LYS A 476 ? 0.4976 0.2749 0.3781 0.0825 -0.1338 -0.0281 476 LYS A CG 3766 C CD . LYS A 476 ? 0.4880 0.2700 0.3814 0.1035 -0.1434 -0.0292 476 LYS A CD 3767 C CE . LYS A 476 ? 0.5524 0.3547 0.4533 0.1096 -0.1552 -0.0249 476 LYS A CE 3768 N NZ . LYS A 476 ? 0.6087 0.4368 0.5369 0.1276 -0.1617 -0.0292 476 LYS A NZ 3769 N N . TYR A 477 ? 0.4565 0.2028 0.3279 0.0499 -0.1024 -0.0436 477 TYR A N 3770 C CA . TYR A 477 ? 0.5424 0.2648 0.4059 0.0473 -0.0988 -0.0483 477 TYR A CA 3771 C C . TYR A 477 ? 0.5212 0.2573 0.3924 0.0331 -0.0900 -0.0547 477 TYR A C 3772 O O . TYR A 477 ? 0.5023 0.2197 0.3666 0.0279 -0.0874 -0.0593 477 TYR A O 3773 C CB . TYR A 477 ? 0.4942 0.2129 0.3647 0.0658 -0.1025 -0.0546 477 TYR A CB 3774 C CG . TYR A 477 ? 0.5326 0.2443 0.4012 0.0827 -0.1125 -0.0491 477 TYR A CG 3775 C CD1 . TYR A 477 ? 0.5189 0.1972 0.3648 0.0826 -0.1190 -0.0393 477 TYR A CD1 3776 C CD2 . TYR A 477 ? 0.4888 0.2288 0.3787 0.0986 -0.1157 -0.0530 477 TYR A CD2 3777 C CE1 . TYR A 477 ? 0.5514 0.2234 0.3951 0.0992 -0.1303 -0.0336 477 TYR A CE1 3778 C CE2 . TYR A 477 ? 0.4866 0.2239 0.3780 0.1147 -0.1263 -0.0482 477 TYR A CE2 3779 C CZ . TYR A 477 ? 0.5501 0.2530 0.4181 0.1156 -0.1344 -0.0384 477 TYR A CZ 3780 O OH . TYR A 477 ? 0.5601 0.2599 0.4288 0.1327 -0.1468 -0.0330 477 TYR A OH 3781 N N . GLY A 478 ? 0.4941 0.2614 0.3793 0.0270 -0.0866 -0.0552 478 GLY A N 3782 C CA . GLY A 478 ? 0.4654 0.2477 0.3590 0.0149 -0.0800 -0.0602 478 GLY A CA 3783 C C . GLY A 478 ? 0.4628 0.2585 0.3677 0.0202 -0.0783 -0.0692 478 GLY A C 3784 O O . GLY A 478 ? 0.4334 0.2338 0.3407 0.0107 -0.0745 -0.0739 478 GLY A O 3785 N N . ASN A 479 ? 0.3810 0.1846 0.2929 0.0352 -0.0810 -0.0716 479 ASN A N 3786 C CA . ASN A 479 ? 0.3676 0.1814 0.2866 0.0415 -0.0782 -0.0804 479 ASN A CA 3787 C C . ASN A 479 ? 0.3524 0.1926 0.2874 0.0543 -0.0788 -0.0811 479 ASN A C 3788 O O . ASN A 479 ? 0.3874 0.2219 0.3236 0.0677 -0.0829 -0.0802 479 ASN A O 3789 C CB . ASN A 479 ? 0.4009 0.1831 0.3060 0.0474 -0.0795 -0.0856 479 ASN A CB 3790 C CG . ASN A 479 ? 0.5326 0.3191 0.4383 0.0487 -0.0754 -0.0963 479 ASN A CG 3791 O OD1 . ASN A 479 ? 0.5597 0.3743 0.4764 0.0470 -0.0718 -0.0990 479 ASN A OD1 3792 N ND2 . ASN A 479 ? 0.6065 0.3629 0.4981 0.0515 -0.0763 -0.1025 479 ASN A ND2 3793 N N . PRO A 480 ? 0.3262 0.1957 0.2744 0.0501 -0.0749 -0.0823 480 PRO A N 3794 C CA . PRO A 480 ? 0.3099 0.2071 0.2750 0.0578 -0.0753 -0.0808 480 PRO A CA 3795 C C . PRO A 480 ? 0.3590 0.2671 0.3313 0.0702 -0.0717 -0.0879 480 PRO A C 3796 O O . PRO A 480 ? 0.3540 0.2883 0.3380 0.0695 -0.0669 -0.0896 480 PRO A O 3797 C CB . PRO A 480 ? 0.2842 0.2029 0.2573 0.0461 -0.0722 -0.0786 480 PRO A CB 3798 C CG . PRO A 480 ? 0.2875 0.1969 0.2511 0.0375 -0.0687 -0.0829 480 PRO A CG 3799 C CD . PRO A 480 ? 0.3274 0.2049 0.2754 0.0374 -0.0709 -0.0844 480 PRO A CD 3800 N N . GLN A 481 ? 0.4292 0.3164 0.3939 0.0816 -0.0734 -0.0920 481 GLN A N 3801 C CA . GLN A 481 ? 0.3929 0.2894 0.3643 0.0957 -0.0692 -0.1002 481 GLN A CA 3802 C C . GLN A 481 ? 0.4263 0.3427 0.4162 0.1096 -0.0726 -0.0977 481 GLN A C 3803 O O . GLN A 481 ? 0.3878 0.3011 0.3800 0.1101 -0.0805 -0.0902 481 GLN A O 3804 C CB . GLN A 481 ? 0.3840 0.2462 0.3381 0.1029 -0.0696 -0.1074 481 GLN A CB 3805 C CG . GLN A 481 ? 0.4208 0.2607 0.3567 0.0880 -0.0682 -0.1101 481 GLN A CG 3806 C CD . GLN A 481 ? 0.3871 0.2492 0.3254 0.0783 -0.0619 -0.1139 481 GLN A CD 3807 O OE1 . GLN A 481 ? 0.4227 0.3080 0.3697 0.0852 -0.0562 -0.1183 481 GLN A OE1 3808 N NE2 . GLN A 481 ? 0.3664 0.2220 0.2970 0.0624 -0.0628 -0.1118 481 GLN A NE2 3809 N N . GLU A 482 ? 0.4123 0.3515 0.4158 0.1203 -0.0665 -0.1043 482 GLU A N 3810 C CA . GLU A 482 ? 0.4239 0.3805 0.4465 0.1369 -0.0697 -0.1045 482 GLU A CA 3811 C C . GLU A 482 ? 0.4388 0.3793 0.4554 0.1534 -0.0662 -0.1148 482 GLU A C 3812 O O . GLU A 482 ? 0.5168 0.4698 0.5346 0.1556 -0.0560 -0.1234 482 GLU A O 3813 C CB . GLU A 482 ? 0.3473 0.3490 0.3947 0.1350 -0.0642 -0.1038 482 GLU A CB 3814 C CG . GLU A 482 ? 0.4018 0.4282 0.4744 0.1502 -0.0691 -0.1030 482 GLU A CG 3815 C CD . GLU A 482 ? 0.4784 0.5041 0.5566 0.1712 -0.0652 -0.1127 482 GLU A CD 3816 O OE1 . GLU A 482 ? 0.5662 0.6038 0.6451 0.1730 -0.0529 -0.1211 482 GLU A OE1 3817 O OE2 . GLU A 482 ? 0.5834 0.5949 0.6636 0.1867 -0.0745 -0.1121 482 GLU A OE2 3818 N N . THR A 483 ? 0.4497 0.3597 0.4572 0.1648 -0.0745 -0.1140 483 THR A N 3819 C CA . THR A 483 ? 0.5296 0.4103 0.5236 0.1779 -0.0724 -0.1239 483 THR A CA 3820 C C . THR A 483 ? 0.5278 0.4256 0.5404 0.2020 -0.0700 -0.1319 483 THR A C 3821 O O . THR A 483 ? 0.5221 0.4010 0.5251 0.2128 -0.0655 -0.1414 483 THR A O 3822 C CB . THR A 483 ? 0.5318 0.3638 0.5032 0.1781 -0.0824 -0.1191 483 THR A CB 3823 O OG1 . THR A 483 ? 0.4981 0.3304 0.4786 0.1897 -0.0934 -0.1108 483 THR A OG1 3824 C CG2 . THR A 483 ? 0.4580 0.2746 0.4124 0.1544 -0.0833 -0.1122 483 THR A CG2 3825 N N . GLN A 484 ? 0.5070 0.4422 0.5467 0.2085 -0.0725 -0.1274 484 GLN A N 3826 C CA . GLN A 484 ? 0.5474 0.5002 0.6082 0.2318 -0.0726 -0.1327 484 GLN A CA 3827 C C . GLN A 484 ? 0.5772 0.5744 0.6606 0.2373 -0.0583 -0.1417 484 GLN A C 3828 O O . GLN A 484 ? 0.6636 0.6657 0.7538 0.2508 -0.0523 -0.1478 484 GLN A O 3829 C CB . GLN A 484 ? 0.6054 0.5709 0.6830 0.2371 -0.0861 -0.1218 484 GLN A CB 3830 C CG . GLN A 484 ? 0.6952 0.6152 0.7490 0.2361 -0.0994 -0.1126 484 GLN A CG 3831 C CD . GLN A 484 ? 0.7661 0.6988 0.8323 0.2393 -0.1134 -0.1015 484 GLN A CD 3832 O OE1 . GLN A 484 ? 0.7164 0.6833 0.8012 0.2327 -0.1160 -0.0981 484 GLN A OE1 3833 N NE2 . GLN A 484 ? 0.8362 0.7411 0.8910 0.2484 -0.1228 -0.0957 484 GLN A NE2 3834 N N . ASN A 485 ? 0.6624 0.6915 0.7550 0.2213 -0.0514 -0.1394 485 ASN A N 3835 C CA . ASN A 485 ? 0.7103 0.7869 0.8276 0.2251 -0.0383 -0.1453 485 ASN A CA 3836 C C . ASN A 485 ? 0.7396 0.8195 0.8416 0.2153 -0.0225 -0.1530 485 ASN A C 3837 O O . ASN A 485 ? 0.7885 0.9025 0.9014 0.2028 -0.0136 -0.1505 485 ASN A O 3838 C CB . ASN A 485 ? 0.6730 0.7903 0.8170 0.2142 -0.0418 -0.1353 485 ASN A CB 3839 C CG . ASN A 485 ? 0.7411 0.8644 0.9047 0.2271 -0.0570 -0.1297 485 ASN A CG 3840 O OD1 . ASN A 485 ? 0.6874 0.7918 0.8485 0.2441 -0.0620 -0.1320 485 ASN A OD1 3841 N ND2 . ASN A 485 ? 0.8939 1.0406 1.0729 0.2145 -0.0643 -0.1199 485 ASN A ND2 3842 N N . GLN A 486 ? 0.7060 0.7494 0.7816 0.2208 -0.0198 -0.1624 486 GLN A N 3843 C CA . GLN A 486 ? 0.7160 0.7562 0.7712 0.2119 -0.0071 -0.1705 486 GLN A CA 3844 C C . GLN A 486 ? 0.7149 0.7667 0.7634 0.1865 -0.0054 -0.1610 486 GLN A C 3845 O O . GLN A 486 ? 0.7594 0.8368 0.8086 0.1793 0.0066 -0.1632 486 GLN A O 3846 C CB . GLN A 486 ? 0.6900 0.7616 0.7583 0.2259 0.0086 -0.1822 486 GLN A CB 3847 N N . SER A 487 ? 0.5987 0.6311 0.6402 0.1734 -0.0173 -0.1503 487 SER A N 3848 C CA . SER A 487 ? 0.6053 0.6467 0.6420 0.1512 -0.0173 -0.1412 487 SER A CA 3849 C C . SER A 487 ? 0.6259 0.6423 0.6335 0.1397 -0.0149 -0.1451 487 SER A C 3850 O O . SER A 487 ? 0.5796 0.5628 0.5682 0.1452 -0.0173 -0.1528 487 SER A O 3851 C CB . SER A 487 ? 0.5809 0.6141 0.6228 0.1427 -0.0303 -0.1291 487 SER A CB 3852 O OG . SER A 487 ? 0.6182 0.6797 0.6874 0.1493 -0.0336 -0.1243 487 SER A OG 3853 N N . THR A 488 ? 0.5794 0.6114 0.5837 0.1236 -0.0109 -0.1398 488 THR A N 3854 C CA . THR A 488 ? 0.5407 0.5522 0.5199 0.1106 -0.0118 -0.1410 488 THR A CA 3855 C C . THR A 488 ? 0.4853 0.4660 0.4562 0.1040 -0.0238 -0.1362 488 THR A C 3856 O O . THR A 488 ? 0.4931 0.4774 0.4765 0.1002 -0.0306 -0.1267 488 THR A O 3857 C CB . THR A 488 ? 0.5609 0.5949 0.5410 0.0948 -0.0081 -0.1330 488 THR A CB 3858 O OG1 . THR A 488 ? 0.6430 0.7058 0.6289 0.0988 0.0046 -0.1365 488 THR A OG1 3859 C CG2 . THR A 488 ? 0.5716 0.5858 0.5277 0.0823 -0.0113 -0.1337 488 THR A CG2 3860 N N . SER A 489 ? 0.4373 0.3877 0.3864 0.1021 -0.0262 -0.1433 489 SER A N 3861 C CA . SER A 489 ? 0.5284 0.4500 0.4682 0.0933 -0.0359 -0.1391 489 SER A CA 3862 C C . SER A 489 ? 0.5260 0.4572 0.4656 0.0754 -0.0387 -0.1306 489 SER A C 3863 O O . SER A 489 ? 0.4739 0.4177 0.4072 0.0687 -0.0346 -0.1320 489 SER A O 3864 C CB . SER A 489 ? 0.6254 0.5136 0.5429 0.0949 -0.0371 -0.1500 489 SER A CB 3865 O OG . SER A 489 ? 0.7861 0.6436 0.6979 0.0924 -0.0454 -0.1470 489 SER A OG 3866 N N . TRP A 490 ? 0.3941 0.3193 0.3399 0.0686 -0.0455 -0.1216 490 TRP A N 3867 C CA . TRP A 490 ? 0.3570 0.2894 0.3040 0.0535 -0.0484 -0.1142 490 TRP A CA 3868 C C . TRP A 490 ? 0.3645 0.2728 0.2961 0.0441 -0.0526 -0.1177 490 TRP A C 3869 O O . TRP A 490 ? 0.3853 0.2712 0.3126 0.0429 -0.0569 -0.1168 490 TRP A O 3870 C CB . TRP A 490 ? 0.3146 0.2530 0.2752 0.0514 -0.0528 -0.1044 490 TRP A CB 3871 C CG . TRP A 490 ? 0.3394 0.2908 0.3056 0.0390 -0.0544 -0.0969 490 TRP A CG 3872 C CD1 . TRP A 490 ? 0.3210 0.2727 0.2806 0.0287 -0.0549 -0.0970 490 TRP A CD1 3873 C CD2 . TRP A 490 ? 0.2616 0.2266 0.2412 0.0365 -0.0565 -0.0888 490 TRP A CD2 3874 N NE1 . TRP A 490 ? 0.2803 0.2442 0.2491 0.0213 -0.0568 -0.0893 490 TRP A NE1 3875 C CE2 . TRP A 490 ? 0.2941 0.2651 0.2742 0.0254 -0.0575 -0.0847 490 TRP A CE2 3876 C CE3 . TRP A 490 ? 0.2800 0.2522 0.2709 0.0428 -0.0587 -0.0852 490 TRP A CE3 3877 C CZ2 . TRP A 490 ? 0.2595 0.2408 0.2497 0.0208 -0.0596 -0.0778 490 TRP A CZ2 3878 C CZ3 . TRP A 490 ? 0.3567 0.3404 0.3572 0.0367 -0.0614 -0.0783 490 TRP A CZ3 3879 C CH2 . TRP A 490 ? 0.3220 0.3088 0.3214 0.0258 -0.0614 -0.0750 490 TRP A CH2 3880 N N . PRO A 491 ? 0.4042 0.3170 0.3267 0.0366 -0.0518 -0.1213 491 PRO A N 3881 C CA . PRO A 491 ? 0.4022 0.2956 0.3118 0.0268 -0.0565 -0.1257 491 PRO A CA 3882 C C . PRO A 491 ? 0.3901 0.2869 0.3081 0.0146 -0.0613 -0.1175 491 PRO A C 3883 O O . PRO A 491 ? 0.3464 0.2628 0.2765 0.0126 -0.0609 -0.1097 491 PRO A O 3884 C CB . PRO A 491 ? 0.4609 0.3640 0.3594 0.0242 -0.0547 -0.1315 491 PRO A CB 3885 C CG . PRO A 491 ? 0.4434 0.3747 0.3530 0.0256 -0.0506 -0.1238 491 PRO A CG 3886 C CD . PRO A 491 ? 0.4079 0.3447 0.3313 0.0360 -0.0470 -0.1206 491 PRO A CD 3887 N N . VAL A 492 ? 0.3554 0.2328 0.2672 0.0062 -0.0655 -0.1198 492 VAL A N 3888 C CA . VAL A 492 ? 0.3508 0.2330 0.2714 -0.0054 -0.0687 -0.1133 492 VAL A CA 3889 C C . VAL A 492 ? 0.3922 0.2959 0.3175 -0.0119 -0.0709 -0.1120 492 VAL A C 3890 O O . VAL A 492 ? 0.3701 0.2754 0.2854 -0.0125 -0.0722 -0.1181 492 VAL A O 3891 C CB . VAL A 492 ? 0.5244 0.3823 0.4376 -0.0147 -0.0717 -0.1166 492 VAL A CB 3892 C CG1 . VAL A 492 ? 0.5042 0.3749 0.4268 -0.0286 -0.0734 -0.1129 492 VAL A CG1 3893 C CG2 . VAL A 492 ? 0.5139 0.3522 0.4254 -0.0111 -0.0706 -0.1123 492 VAL A CG2 3894 N N . PHE A 493 ? 0.3437 0.2625 0.2825 -0.0161 -0.0717 -0.1043 493 PHE A N 3895 C CA . PHE A 493 ? 0.3832 0.3200 0.3274 -0.0215 -0.0753 -0.1021 493 PHE A CA 3896 C C . PHE A 493 ? 0.4148 0.3492 0.3616 -0.0325 -0.0804 -0.1051 493 PHE A C 3897 O O . PHE A 493 ? 0.4630 0.3942 0.4183 -0.0379 -0.0794 -0.1024 493 PHE A O 3898 C CB . PHE A 493 ? 0.3429 0.2951 0.3012 -0.0199 -0.0741 -0.0934 493 PHE A CB 3899 C CG . PHE A 493 ? 0.3282 0.2969 0.2928 -0.0232 -0.0782 -0.0898 493 PHE A CG 3900 C CD1 . PHE A 493 ? 0.3008 0.2747 0.2741 -0.0304 -0.0827 -0.0900 493 PHE A CD1 3901 C CD2 . PHE A 493 ? 0.3043 0.2838 0.2676 -0.0189 -0.0774 -0.0855 493 PHE A CD2 3902 C CE1 . PHE A 493 ? 0.3742 0.3630 0.3547 -0.0312 -0.0877 -0.0863 493 PHE A CE1 3903 C CE2 . PHE A 493 ? 0.3537 0.3449 0.3213 -0.0210 -0.0821 -0.0808 493 PHE A CE2 3904 C CZ . PHE A 493 ? 0.3645 0.3600 0.3408 -0.0261 -0.0878 -0.0813 493 PHE A CZ 3905 N N . LYS A 494 ? 0.4017 0.3402 0.3415 -0.0364 -0.0840 -0.1087 494 LYS A N 3906 C CA . LYS A 494 ? 0.5074 0.4500 0.4523 -0.0474 -0.0873 -0.1092 494 LYS A CA 3907 C C . LYS A 494 ? 0.5481 0.5117 0.4996 -0.0486 -0.0934 -0.1058 494 LYS A C 3908 O O . LYS A 494 ? 0.4799 0.4492 0.4238 -0.0422 -0.0952 -0.1049 494 LYS A O 3909 C CB . LYS A 494 ? 0.5239 0.4509 0.4537 -0.0519 -0.0875 -0.1170 494 LYS A CB 3910 C CG . LYS A 494 ? 0.6611 0.5644 0.5852 -0.0518 -0.0825 -0.1199 494 LYS A CG 3911 C CD . LYS A 494 ? 0.8182 0.7034 0.7236 -0.0483 -0.0812 -0.1285 494 LYS A CD 3912 C CE . LYS A 494 ? 0.8750 0.7342 0.7755 -0.0479 -0.0774 -0.1307 494 LYS A CE 3913 N NZ . LYS A 494 ? 0.8352 0.6756 0.7191 -0.0383 -0.0747 -0.1382 494 LYS A NZ 3914 N N . SER A 495 ? 0.5881 0.5631 0.5532 -0.0565 -0.0969 -0.1040 495 SER A N 3915 C CA . SER A 495 ? 0.6491 0.6445 0.6239 -0.0559 -0.1036 -0.0997 495 SER A CA 3916 C C . SER A 495 ? 0.5425 0.5404 0.5020 -0.0560 -0.1101 -0.1021 495 SER A C 3917 O O . SER A 495 ? 0.5645 0.5749 0.5252 -0.0522 -0.1159 -0.0976 495 SER A O 3918 C CB . SER A 495 ? 0.7621 0.7710 0.7568 -0.0636 -0.1061 -0.0985 495 SER A CB 3919 O OG . SER A 495 ? 0.8549 0.8598 0.8453 -0.0740 -0.1085 -0.1038 495 SER A OG 3920 N N . THR A 496 ? 0.4466 0.4309 0.3901 -0.0602 -0.1092 -0.1093 496 THR A N 3921 C CA . THR A 496 ? 0.5282 0.5128 0.4533 -0.0606 -0.1144 -0.1131 496 THR A CA 3922 C C . THR A 496 ? 0.5123 0.4916 0.4197 -0.0509 -0.1114 -0.1131 496 THR A C 3923 O O . THR A 496 ? 0.5779 0.5676 0.4798 -0.0476 -0.1163 -0.1086 496 THR A O 3924 C CB . THR A 496 ? 0.6972 0.6684 0.6103 -0.0686 -0.1141 -0.1225 496 THR A CB 3925 O OG1 . THR A 496 ? 0.8129 0.7934 0.7413 -0.0795 -0.1186 -0.1228 496 THR A OG1 3926 C CG2 . THR A 496 ? 0.6769 0.6468 0.5673 -0.0678 -0.1182 -0.1277 496 THR A CG2 3927 N N . GLU A 497 ? 0.5018 0.4652 0.4002 -0.0463 -0.1036 -0.1180 497 GLU A N 3928 C CA . GLU A 497 ? 0.5203 0.4804 0.4013 -0.0373 -0.0998 -0.1202 497 GLU A CA 3929 C C . GLU A 497 ? 0.4196 0.3888 0.3102 -0.0300 -0.0969 -0.1134 497 GLU A C 3930 O O . GLU A 497 ? 0.4279 0.4037 0.3086 -0.0253 -0.0931 -0.1094 497 GLU A O 3931 C CB . GLU A 497 ? 0.5251 0.4661 0.3927 -0.0337 -0.0926 -0.1296 497 GLU A CB 3932 C CG . GLU A 497 ? 0.6965 0.6279 0.5479 -0.0398 -0.0948 -0.1377 497 GLU A CG 3933 C CD . GLU A 497 ? 0.8858 0.7955 0.7338 -0.0397 -0.0894 -0.1454 497 GLU A CD 3934 O OE1 . GLU A 497 ? 0.9864 0.8913 0.8482 -0.0469 -0.0905 -0.1438 497 GLU A OE1 3935 O OE2 . GLU A 497 ? 0.9496 0.8473 0.7811 -0.0321 -0.0835 -0.1530 497 GLU A OE2 3936 N N . GLN A 498 ? 0.3136 0.2838 0.2244 -0.0304 -0.0948 -0.1088 498 GLN A N 3937 C CA . GLN A 498 ? 0.2926 0.2724 0.2162 -0.0256 -0.0900 -0.0989 498 GLN A CA 3938 C C . GLN A 498 ? 0.3572 0.3364 0.2736 -0.0179 -0.0807 -0.0981 498 GLN A C 3939 O O . GLN A 498 ? 0.3681 0.3579 0.2855 -0.0156 -0.0781 -0.0906 498 GLN A O 3940 C CB . GLN A 498 ? 0.4086 0.4027 0.3374 -0.0271 -0.0965 -0.0909 498 GLN A CB 3941 C CG . GLN A 498 ? 0.4448 0.4450 0.3868 -0.0331 -0.1056 -0.0914 498 GLN A CG 3942 C CD . GLN A 498 ? 0.5254 0.5377 0.4674 -0.0331 -0.1150 -0.0855 498 GLN A CD 3943 O OE1 . GLN A 498 ? 0.4762 0.4929 0.4194 -0.0288 -0.1139 -0.0767 498 GLN A OE1 3944 N NE2 . GLN A 498 ? 0.6064 0.6235 0.5475 -0.0383 -0.1219 -0.0879 498 GLN A NE2 3945 N N . LYS A 499 ? 0.3253 0.2921 0.2356 -0.0141 -0.0757 -0.1055 499 LYS A N 3946 C CA . LYS A 499 ? 0.3301 0.2990 0.2373 -0.0055 -0.0667 -0.1060 499 LYS A CA 3947 C C . LYS A 499 ? 0.2848 0.2608 0.2104 -0.0027 -0.0635 -0.0980 499 LYS A C 3948 O O . LYS A 499 ? 0.3260 0.2963 0.2623 -0.0051 -0.0663 -0.0960 499 LYS A O 3949 C CB . LYS A 499 ? 0.3262 0.2781 0.2231 -0.0002 -0.0633 -0.1169 499 LYS A CB 3950 C CG . LYS A 499 ? 0.3523 0.2946 0.2282 -0.0032 -0.0666 -0.1268 499 LYS A CG 3951 C CD . LYS A 499 ? 0.3758 0.2972 0.2405 0.0029 -0.0633 -0.1386 499 LYS A CD 3952 C CE . LYS A 499 ? 0.4485 0.3590 0.2900 -0.0009 -0.0670 -0.1497 499 LYS A CE 3953 N NZ . LYS A 499 ? 0.4631 0.3517 0.2947 0.0052 -0.0619 -0.1594 499 LYS A NZ 3954 N N . TYR A 500 ? 0.2801 0.2689 0.2085 0.0015 -0.0574 -0.0936 500 TYR A N 3955 C CA . TYR A 500 ? 0.3033 0.2992 0.2484 0.0043 -0.0547 -0.0874 500 TYR A CA 3956 C C . TYR A 500 ? 0.2911 0.2968 0.2382 0.0118 -0.0464 -0.0890 500 TYR A C 3957 O O . TYR A 500 ? 0.2827 0.2930 0.2181 0.0142 -0.0413 -0.0932 500 TYR A O 3958 C CB . TYR A 500 ? 0.2683 0.2739 0.2223 -0.0013 -0.0577 -0.0776 500 TYR A CB 3959 C CG . TYR A 500 ? 0.2796 0.2962 0.2261 -0.0036 -0.0553 -0.0727 500 TYR A CG 3960 C CD1 . TYR A 500 ? 0.2671 0.2818 0.1989 -0.0073 -0.0594 -0.0730 500 TYR A CD1 3961 C CD2 . TYR A 500 ? 0.2497 0.2787 0.2035 -0.0032 -0.0494 -0.0670 500 TYR A CD2 3962 C CE1 . TYR A 500 ? 0.2871 0.3097 0.2085 -0.0099 -0.0574 -0.0669 500 TYR A CE1 3963 C CE2 . TYR A 500 ? 0.2971 0.3347 0.2425 -0.0070 -0.0463 -0.0611 500 TYR A CE2 3964 C CZ . TYR A 500 ? 0.3479 0.3811 0.2757 -0.0100 -0.0502 -0.0606 500 TYR A CZ 3965 O OH . TYR A 500 ? 0.2861 0.3257 0.2020 -0.0141 -0.0472 -0.0535 500 TYR A OH 3966 N N . LEU A 501 ? 0.2959 0.3064 0.2582 0.0155 -0.0453 -0.0859 501 LEU A N 3967 C CA . LEU A 501 ? 0.3094 0.3329 0.2795 0.0233 -0.0383 -0.0875 501 LEU A CA 3968 C C . LEU A 501 ? 0.2940 0.3372 0.2776 0.0190 -0.0360 -0.0788 501 LEU A C 3969 O O . LEU A 501 ? 0.2535 0.2958 0.2464 0.0140 -0.0412 -0.0725 501 LEU A O 3970 C CB . LEU A 501 ? 0.2809 0.2951 0.2588 0.0315 -0.0406 -0.0907 501 LEU A CB 3971 C CG . LEU A 501 ? 0.3422 0.3709 0.3317 0.0422 -0.0350 -0.0934 501 LEU A CG 3972 C CD1 . LEU A 501 ? 0.3929 0.4221 0.3714 0.0496 -0.0275 -0.1027 501 LEU A CD1 3973 C CD2 . LEU A 501 ? 0.3808 0.3998 0.3786 0.0501 -0.0401 -0.0939 501 LEU A CD2 3974 N N . THR A 502 ? 0.2602 0.3206 0.2442 0.0200 -0.0277 -0.0787 502 THR A N 3975 C CA . THR A 502 ? 0.2846 0.3634 0.2819 0.0141 -0.0250 -0.0703 502 THR A CA 3976 C C . THR A 502 ? 0.2939 0.3872 0.3117 0.0207 -0.0230 -0.0717 502 THR A C 3977 O O . THR A 502 ? 0.2634 0.3616 0.2834 0.0312 -0.0183 -0.0792 502 THR A O 3978 C CB . THR A 502 ? 0.2947 0.3869 0.2825 0.0093 -0.0162 -0.0675 502 THR A CB 3979 O OG1 . THR A 502 ? 0.3428 0.4463 0.3290 0.0180 -0.0064 -0.0758 502 THR A OG1 3980 C CG2 . THR A 502 ? 0.3165 0.3940 0.2822 0.0037 -0.0203 -0.0659 502 THR A CG2 3981 N N . LEU A 503 ? 0.2918 0.3912 0.3245 0.0151 -0.0275 -0.0649 503 LEU A N 3982 C CA . LEU A 503 ? 0.2962 0.4118 0.3498 0.0199 -0.0279 -0.0654 503 LEU A CA 3983 C C . LEU A 503 ? 0.3447 0.4859 0.4124 0.0122 -0.0216 -0.0599 503 LEU A C 3984 O O . LEU A 503 ? 0.3131 0.4527 0.3811 0.0004 -0.0241 -0.0523 503 LEU A O 3985 C CB . LEU A 503 ? 0.2840 0.3872 0.3432 0.0189 -0.0386 -0.0630 503 LEU A CB 3986 C CG . LEU A 503 ? 0.2953 0.3734 0.3414 0.0248 -0.0442 -0.0673 503 LEU A CG 3987 C CD1 . LEU A 503 ? 0.2005 0.2670 0.2487 0.0211 -0.0533 -0.0636 503 LEU A CD1 3988 C CD2 . LEU A 503 ? 0.2830 0.3607 0.3306 0.0384 -0.0425 -0.0745 503 LEU A CD2 3989 N N A ASN A 504 ? 0.3300 0.4945 0.4099 0.0187 -0.0132 -0.0640 504 ASN A N 3990 N N B ASN A 504 ? 0.3306 0.4953 0.4108 0.0186 -0.0132 -0.0639 504 ASN A N 3991 C CA A ASN A 504 ? 0.3243 0.5173 0.4207 0.0106 -0.0057 -0.0592 504 ASN A CA 3992 C CA B ASN A 504 ? 0.3236 0.5168 0.4201 0.0105 -0.0057 -0.0591 504 ASN A CA 3993 C C A ASN A 504 ? 0.3149 0.5360 0.4345 0.0216 -0.0004 -0.0653 504 ASN A C 3994 C C B ASN A 504 ? 0.3138 0.5348 0.4335 0.0215 -0.0006 -0.0652 504 ASN A C 3995 O O A ASN A 504 ? 0.3108 0.5255 0.4300 0.0365 -0.0025 -0.0732 504 ASN A O 3996 O O B ASN A 504 ? 0.3110 0.5255 0.4305 0.0364 -0.0028 -0.0731 504 ASN A O 3997 C CB A ASN A 504 ? 0.3227 0.5182 0.4024 0.0022 0.0046 -0.0556 504 ASN A CB 3998 C CB B ASN A 504 ? 0.3291 0.5252 0.4088 0.0029 0.0051 -0.0561 504 ASN A CB 3999 C CG A ASN A 504 ? 0.3720 0.5639 0.4345 0.0126 0.0126 -0.0643 504 ASN A CG 4000 C CG B ASN A 504 ? 0.4022 0.6170 0.4924 -0.0122 0.0103 -0.0466 504 ASN A CG 4001 O OD1 A ASN A 504 ? 0.3146 0.5283 0.3863 0.0203 0.0230 -0.0703 504 ASN A OD1 4002 O OD1 B ASN A 504 ? 0.4049 0.6382 0.5195 -0.0161 0.0084 -0.0444 504 ASN A OD1 4003 N ND2 A ASN A 504 ? 0.3134 0.4784 0.3514 0.0129 0.0078 -0.0658 504 ASN A ND2 4004 N ND2 B ASN A 504 ? 0.4741 0.6833 0.5448 -0.0215 0.0164 -0.0407 504 ASN A ND2 4005 N N . THR A 505 ? 0.2785 0.5305 0.4190 0.0143 0.0061 -0.0616 505 THR A N 4006 C CA . THR A 505 ? 0.3871 0.6717 0.5545 0.0249 0.0113 -0.0675 505 THR A CA 4007 C C . THR A 505 ? 0.5057 0.8025 0.6668 0.0353 0.0265 -0.0755 505 THR A C 4008 O O . THR A 505 ? 0.6018 0.9139 0.7780 0.0514 0.0293 -0.0841 505 THR A O 4009 C CB . THR A 505 ? 0.2412 0.5599 0.4380 0.0128 0.0133 -0.0617 505 THR A CB 4010 O OG1 . THR A 505 ? 0.3193 0.6468 0.5084 -0.0029 0.0253 -0.0550 505 THR A OG1 4011 C CG2 . THR A 505 ? 0.2186 0.5260 0.4228 0.0044 -0.0026 -0.0561 505 THR A CG2 4012 N N . GLU A 506 ? 0.5589 0.8481 0.6966 0.0268 0.0358 -0.0731 506 GLU A N 4013 C CA . GLU A 506 ? 0.7113 1.0131 0.8397 0.0345 0.0517 -0.0808 506 GLU A CA 4014 C C . GLU A 506 ? 0.7845 1.0572 0.8879 0.0488 0.0496 -0.0909 506 GLU A C 4015 O O . GLU A 506 ? 0.8731 1.1499 0.9848 0.0662 0.0514 -0.1014 506 GLU A O 4016 C CB . GLU A 506 ? 0.8139 1.1217 0.9258 0.0181 0.0631 -0.0730 506 GLU A CB 4017 C CG . GLU A 506 ? 0.9365 1.2201 1.0343 0.0015 0.0526 -0.0608 506 GLU A CG 4018 C CD . GLU A 506 ? 1.0492 1.3280 1.1212 -0.0117 0.0615 -0.0534 506 GLU A CD 4019 O OE1 . GLU A 506 ? 1.0856 1.3420 1.1278 -0.0079 0.0611 -0.0566 506 GLU A OE1 4020 O OE2 . GLU A 506 ? 1.0710 1.3674 1.1516 -0.0265 0.0682 -0.0439 506 GLU A OE2 4021 N N . SER A 507 ? 0.7089 0.9519 0.7825 0.0411 0.0450 -0.0877 507 SER A N 4022 C CA . SER A 507 ? 0.7039 0.9212 0.7507 0.0505 0.0448 -0.0971 507 SER A CA 4023 C C . SER A 507 ? 0.6528 0.8351 0.6851 0.0470 0.0293 -0.0943 507 SER A C 4024 O O . SER A 507 ? 0.7403 0.9114 0.7593 0.0339 0.0249 -0.0859 507 SER A O 4025 C CB . SER A 507 ? 0.8062 1.0261 0.8273 0.0437 0.0569 -0.0973 507 SER A CB 4026 O OG . SER A 507 ? 0.8597 1.0585 0.8553 0.0533 0.0580 -0.1087 507 SER A OG 4027 N N . THR A 508 ? 0.4881 0.6533 0.5233 0.0587 0.0210 -0.1008 508 THR A N 4028 C CA . THR A 508 ? 0.5768 0.7099 0.5977 0.0550 0.0082 -0.0989 508 THR A CA 4029 C C . THR A 508 ? 0.5225 0.6349 0.5146 0.0558 0.0100 -0.1061 508 THR A C 4030 O O . THR A 508 ? 0.4845 0.5947 0.4692 0.0672 0.0164 -0.1171 508 THR A O 4031 C CB . THR A 508 ? 0.5793 0.6993 0.6114 0.0649 -0.0015 -0.1015 508 THR A CB 4032 O OG1 . THR A 508 ? 0.6197 0.7140 0.6343 0.0740 -0.0033 -0.1110 508 THR A OG1 4033 C CG2 . THR A 508 ? 0.5654 0.7116 0.6242 0.0749 0.0019 -0.1031 508 THR A CG2 4034 N N . ARG A 509 ? 0.3916 0.4895 0.3677 0.0442 0.0040 -0.1006 509 ARG A N 4035 C CA . ARG A 509 ? 0.4071 0.4884 0.3557 0.0429 0.0043 -0.1067 509 ARG A CA 4036 C C . ARG A 509 ? 0.3821 0.4377 0.3209 0.0374 -0.0083 -0.1057 509 ARG A C 4037 O O . ARG A 509 ? 0.3298 0.3831 0.2799 0.0311 -0.0159 -0.0973 509 ARG A O 4038 C CB . ARG A 509 ? 0.4870 0.5812 0.4219 0.0336 0.0113 -0.1012 509 ARG A CB 4039 C CG . ARG A 509 ? 0.5554 0.6781 0.5003 0.0366 0.0258 -0.1015 509 ARG A CG 4040 C CD . ARG A 509 ? 0.6985 0.8314 0.6257 0.0265 0.0336 -0.0954 509 ARG A CD 4041 N NE . ARG A 509 ? 0.8487 1.0094 0.7827 0.0300 0.0503 -0.0982 509 ARG A NE 4042 C CZ . ARG A 509 ? 0.8836 1.0485 0.8068 0.0410 0.0609 -0.1112 509 ARG A CZ 4043 N NH1 . ARG A 509 ? 0.8529 0.9929 0.7565 0.0486 0.0556 -0.1225 509 ARG A NH1 4044 N NH2 . ARG A 509 ? 0.9062 1.1005 0.8389 0.0440 0.0773 -0.1134 509 ARG A NH2 4045 N N . ILE A 510 ? 0.3323 0.3697 0.2505 0.0396 -0.0099 -0.1151 510 ILE A N 4046 C CA . ILE A 510 ? 0.3321 0.3491 0.2392 0.0321 -0.0208 -0.1147 510 ILE A CA 4047 C C . ILE A 510 ? 0.4075 0.4285 0.2982 0.0223 -0.0226 -0.1100 510 ILE A C 4048 O O . ILE A 510 ? 0.3598 0.3844 0.2317 0.0233 -0.0164 -0.1150 510 ILE A O 4049 C CB . ILE A 510 ? 0.4117 0.4051 0.3040 0.0372 -0.0234 -0.1275 510 ILE A CB 4050 C CG1 . ILE A 510 ? 0.4204 0.4060 0.3251 0.0489 -0.0219 -0.1324 510 ILE A CG1 4051 C CG2 . ILE A 510 ? 0.4135 0.3898 0.3001 0.0275 -0.0349 -0.1261 510 ILE A CG2 4052 C CD1 . ILE A 510 ? 0.3821 0.3700 0.3075 0.0469 -0.0274 -0.1227 510 ILE A CD1 4053 N N A MET A 511 ? 0.3978 0.4177 0.2945 0.0136 -0.0311 -0.1006 511 MET A N 4054 N N B MET A 511 ? 0.3226 0.3420 0.2192 0.0137 -0.0313 -0.1008 511 MET A N 4055 C CA A MET A 511 ? 0.4055 0.4272 0.2877 0.0054 -0.0356 -0.0948 511 MET A CA 4056 C CA B MET A 511 ? 0.3966 0.4184 0.2799 0.0053 -0.0358 -0.0944 511 MET A CA 4057 C C A MET A 511 ? 0.4131 0.4222 0.2958 -0.0002 -0.0483 -0.0943 511 MET A C 4058 C C B MET A 511 ? 0.4151 0.4239 0.2977 -0.0002 -0.0484 -0.0944 511 MET A C 4059 O O A MET A 511 ? 0.4183 0.4190 0.3141 0.0007 -0.0521 -0.0963 511 MET A O 4060 O O B MET A 511 ? 0.3127 0.3126 0.2078 0.0007 -0.0523 -0.0969 511 MET A O 4061 C CB A MET A 511 ? 0.3824 0.4192 0.2732 0.0006 -0.0326 -0.0819 511 MET A CB 4062 C CB B MET A 511 ? 0.3332 0.3695 0.2280 0.0007 -0.0335 -0.0814 511 MET A CB 4063 C CG A MET A 511 ? 0.4565 0.5104 0.3509 0.0040 -0.0193 -0.0816 511 MET A CG 4064 C CG B MET A 511 ? 0.4005 0.4538 0.3013 0.0042 -0.0208 -0.0807 511 MET A CG 4065 S SD A MET A 511 ? 0.3190 0.3890 0.2221 -0.0047 -0.0154 -0.0660 511 MET A SD 4066 S SD B MET A 511 ? 0.5412 0.6018 0.4141 0.0041 -0.0105 -0.0845 511 MET A SD 4067 C CE A MET A 511 ? 0.3593 0.4216 0.2333 -0.0124 -0.0204 -0.0597 511 MET A CE 4068 C CE B MET A 511 ? 0.4087 0.4732 0.2735 -0.0079 -0.0142 -0.0680 511 MET A CE 4069 N N . THR A 512 ? 0.3344 0.3432 0.2029 -0.0060 -0.0548 -0.0912 512 THR A N 4070 C CA . THR A 512 ? 0.3311 0.3325 0.2018 -0.0112 -0.0672 -0.0912 512 THR A CA 4071 C C . THR A 512 ? 0.3337 0.3420 0.2097 -0.0158 -0.0744 -0.0793 512 THR A C 4072 O O . THR A 512 ? 0.3315 0.3461 0.1973 -0.0170 -0.0721 -0.0716 512 THR A O 4073 C CB . THR A 512 ? 0.3843 0.3768 0.2327 -0.0134 -0.0725 -0.1012 512 THR A CB 4074 O OG1 . THR A 512 ? 0.4226 0.4204 0.2480 -0.0135 -0.0692 -0.0997 512 THR A OG1 4075 C CG2 . THR A 512 ? 0.3787 0.3579 0.2233 -0.0092 -0.0682 -0.1143 512 THR A CG2 4076 N N . LYS A 513 ? 0.3083 0.3147 0.2002 -0.0182 -0.0827 -0.0777 513 LYS A N 4077 C CA . LYS A 513 ? 0.3042 0.3154 0.2017 -0.0210 -0.0921 -0.0689 513 LYS A CA 4078 C C . LYS A 513 ? 0.2975 0.3134 0.1999 -0.0203 -0.0887 -0.0571 513 LYS A C 4079 O O . LYS A 513 ? 0.3111 0.3282 0.2013 -0.0218 -0.0925 -0.0493 513 LYS A O 4080 C CB . LYS A 513 ? 0.3269 0.3379 0.2049 -0.0238 -0.1016 -0.0705 513 LYS A CB 4081 C CG . LYS A 513 ? 0.3941 0.4004 0.2708 -0.0270 -0.1081 -0.0822 513 LYS A CG 4082 C CD . LYS A 513 ? 0.4001 0.4068 0.2553 -0.0302 -0.1185 -0.0848 513 LYS A CD 4083 C CE . LYS A 513 ? 0.5401 0.5420 0.3951 -0.0353 -0.1248 -0.0966 513 LYS A CE 4084 N NZ . LYS A 513 ? 0.6414 0.6463 0.4787 -0.0396 -0.1325 -0.0977 513 LYS A NZ 4085 N N . LEU A 514 ? 0.3198 0.3366 0.2389 -0.0186 -0.0824 -0.0555 514 LEU A N 4086 C CA . LEU A 514 ? 0.2970 0.3166 0.2231 -0.0192 -0.0793 -0.0454 514 LEU A CA 4087 C C . LEU A 514 ? 0.3397 0.3570 0.2677 -0.0205 -0.0887 -0.0363 514 LEU A C 4088 O O . LEU A 514 ? 0.2738 0.2902 0.2130 -0.0193 -0.0963 -0.0381 514 LEU A O 4089 C CB . LEU A 514 ? 0.2532 0.2732 0.1986 -0.0175 -0.0747 -0.0468 514 LEU A CB 4090 C CG . LEU A 514 ? 0.3560 0.3778 0.3109 -0.0193 -0.0723 -0.0380 514 LEU A CG 4091 C CD1 . LEU A 514 ? 0.2582 0.2869 0.2035 -0.0218 -0.0643 -0.0336 514 LEU A CD1 4092 C CD2 . LEU A 514 ? 0.2657 0.2870 0.2376 -0.0176 -0.0700 -0.0410 514 LEU A CD2 4093 N N . ARG A 515 ? 0.2896 0.3060 0.2068 -0.0229 -0.0880 -0.0265 515 ARG A N 4094 C CA . ARG A 515 ? 0.3960 0.4065 0.3130 -0.0230 -0.0973 -0.0164 515 ARG A CA 4095 C C . ARG A 515 ? 0.3544 0.3651 0.2704 -0.0203 -0.1099 -0.0189 515 ARG A C 4096 O O . ARG A 515 ? 0.3520 0.3607 0.2816 -0.0171 -0.1178 -0.0157 515 ARG A O 4097 C CB . ARG A 515 ? 0.3502 0.3564 0.2877 -0.0219 -0.0975 -0.0129 515 ARG A CB 4098 C CG . ARG A 515 ? 0.4269 0.4337 0.3695 -0.0256 -0.0876 -0.0099 515 ARG A CG 4099 C CD . ARG A 515 ? 0.4779 0.4771 0.4118 -0.0304 -0.0878 0.0029 515 ARG A CD 4100 N NE . ARG A 515 ? 0.4366 0.4352 0.3826 -0.0346 -0.0816 0.0053 515 ARG A NE 4101 C CZ . ARG A 515 ? 0.5644 0.5742 0.5140 -0.0379 -0.0715 0.0023 515 ARG A CZ 4102 N NH1 . ARG A 515 ? 0.4969 0.5175 0.4377 -0.0364 -0.0654 -0.0035 515 ARG A NH1 4103 N NH2 . ARG A 515 ? 0.4027 0.4134 0.3651 -0.0424 -0.0678 0.0045 515 ARG A NH2 4104 N N . ALA A 516 ? 0.4882 0.3104 0.5168 -0.0041 -0.1453 -0.1806 516 ALA A N 4105 C CA . ALA A 516 ? 0.5026 0.3179 0.5358 -0.0165 -0.1626 -0.1836 516 ALA A CA 4106 C C . ALA A 516 ? 0.5899 0.4264 0.6053 -0.0251 -0.1718 -0.1724 516 ALA A C 4107 O O . ALA A 516 ? 0.4976 0.3419 0.5371 -0.0342 -0.1778 -0.1548 516 ALA A O 4108 C CB . ALA A 516 ? 0.5543 0.3547 0.5712 -0.0133 -0.1670 -0.2103 516 ALA A CB 4109 N N . GLN A 517 ? 0.6281 0.4782 0.6028 -0.0210 -0.1701 -0.1789 517 GLN A N 4110 C CA . GLN A 517 ? 0.6413 0.5100 0.5972 -0.0280 -0.1809 -0.1657 517 GLN A CA 4111 C C . GLN A 517 ? 0.5252 0.4067 0.5026 -0.0295 -0.1754 -0.1367 517 GLN A C 4112 O O . GLN A 517 ? 0.4715 0.3602 0.4635 -0.0356 -0.1884 -0.1257 517 GLN A O 4113 C CB . GLN A 517 ? 0.8521 0.7354 0.7573 -0.0239 -0.1757 -0.1723 517 GLN A CB 4114 C CG . GLN A 517 ? 1.0342 0.9278 0.9091 -0.0325 -0.1962 -0.1719 517 GLN A CG 4115 C CD . GLN A 517 ? 1.1876 1.0965 1.0065 -0.0298 -0.1896 -0.1815 517 GLN A CD 4116 O OE1 . GLN A 517 ? 1.2094 1.1302 1.0167 -0.0224 -0.1672 -0.1775 517 GLN A OE1 4117 N NE2 . GLN A 517 ? 1.2580 1.1708 1.0417 -0.0369 -0.2090 -0.1937 517 GLN A NE2 4118 N N . GLN A 518 ? 0.4337 0.3189 0.4146 -0.0232 -0.1569 -0.1260 518 GLN A N 4119 C CA . GLN A 518 ? 0.3986 0.2921 0.3971 -0.0243 -0.1520 -0.1035 518 GLN A CA 4120 C C . GLN A 518 ? 0.4038 0.2941 0.4406 -0.0291 -0.1566 -0.0981 518 GLN A C 4121 O O . GLN A 518 ? 0.3671 0.2671 0.4172 -0.0313 -0.1617 -0.0870 518 GLN A O 4122 C CB . GLN A 518 ? 0.3824 0.2797 0.3800 -0.0187 -0.1339 -0.0952 518 GLN A CB 4123 C CG . GLN A 518 ? 0.4816 0.3911 0.4463 -0.0155 -0.1257 -0.0953 518 GLN A CG 4124 C CD . GLN A 518 ? 0.5396 0.4478 0.4922 -0.0081 -0.1179 -0.1169 518 GLN A CD 4125 O OE1 . GLN A 518 ? 0.5523 0.4444 0.5145 -0.0065 -0.1246 -0.1352 518 GLN A OE1 4126 N NE2 . GLN A 518 ? 0.5939 0.5197 0.5284 -0.0033 -0.1034 -0.1156 518 GLN A NE2 4127 N N . CYS A 519 ? 0.3850 0.2629 0.4416 -0.0304 -0.1544 -0.1053 519 CYS A N 4128 C CA . CYS A 519 ? 0.3652 0.2441 0.4582 -0.0374 -0.1557 -0.0959 519 CYS A CA 4129 C C . CYS A 519 ? 0.4301 0.3153 0.5407 -0.0462 -0.1725 -0.0987 519 CYS A C 4130 O O . CYS A 519 ? 0.4209 0.3211 0.5597 -0.0510 -0.1717 -0.0867 519 CYS A O 4131 C CB . CYS A 519 ? 0.3707 0.2330 0.4817 -0.0381 -0.1507 -0.0973 519 CYS A CB 4132 S SG . CYS A 519 ? 0.4507 0.3160 0.5550 -0.0294 -0.1325 -0.0850 519 CYS A SG 4133 N N . ARG A 520 ? 0.4031 0.2835 0.4953 -0.0469 -0.1831 -0.1120 520 ARG A N 4134 C CA . ARG A 520 ? 0.4131 0.3061 0.5180 -0.0537 -0.1971 -0.1100 520 ARG A CA 4135 C C . ARG A 520 ? 0.3928 0.3063 0.5044 -0.0514 -0.2018 -0.0972 520 ARG A C 4136 O O . ARG A 520 ? 0.3831 0.3137 0.5277 -0.0554 -0.2070 -0.0888 520 ARG A O 4137 C CB . ARG A 520 ? 0.4894 0.3751 0.5651 -0.0553 -0.2092 -0.1268 520 ARG A CB 4138 C CG . ARG A 520 ? 0.5905 0.4549 0.6684 -0.0578 -0.2085 -0.1421 520 ARG A CG 4139 C CD . ARG A 520 ? 0.6841 0.5437 0.7358 -0.0619 -0.2227 -0.1607 520 ARG A CD 4140 N NE . ARG A 520 ? 0.8451 0.6791 0.8897 -0.0595 -0.2194 -0.1810 520 ARG A NE 4141 C CZ . ARG A 520 ? 0.8422 0.6661 0.8506 -0.0499 -0.2125 -0.2013 520 ARG A CZ 4142 N NH1 . ARG A 520 ? 0.7038 0.5427 0.6763 -0.0444 -0.2090 -0.2020 520 ARG A NH1 4143 N NH2 . ARG A 520 ? 0.9457 0.7453 0.9546 -0.0456 -0.2095 -0.2209 520 ARG A NH2 4144 N N . PHE A 521 ? 0.3891 0.3014 0.4732 -0.0448 -0.2004 -0.0952 521 PHE A N 4145 C CA . PHE A 521 ? 0.3750 0.3018 0.4661 -0.0398 -0.2026 -0.0808 521 PHE A CA 4146 C C . PHE A 521 ? 0.3816 0.3188 0.5065 -0.0367 -0.1884 -0.0711 521 PHE A C 4147 O O . PHE A 521 ? 0.3372 0.2921 0.4924 -0.0351 -0.1934 -0.0654 521 PHE A O 4148 C CB . PHE A 521 ? 0.3817 0.3035 0.4349 -0.0339 -0.1981 -0.0748 521 PHE A CB 4149 C CG . PHE A 521 ? 0.3704 0.2983 0.4338 -0.0279 -0.1996 -0.0595 521 PHE A CG 4150 C CD1 . PHE A 521 ? 0.3911 0.3267 0.4605 -0.0269 -0.2196 -0.0520 521 PHE A CD1 4151 C CD2 . PHE A 521 ? 0.3514 0.2754 0.4199 -0.0230 -0.1834 -0.0532 521 PHE A CD2 4152 C CE1 . PHE A 521 ? 0.3802 0.3164 0.4643 -0.0190 -0.2227 -0.0390 521 PHE A CE1 4153 C CE2 . PHE A 521 ? 0.4721 0.3959 0.5512 -0.0165 -0.1863 -0.0432 521 PHE A CE2 4154 C CZ . PHE A 521 ? 0.3621 0.2905 0.4509 -0.0135 -0.2056 -0.0364 521 PHE A CZ 4155 N N . TRP A 522 ? 0.3317 0.2611 0.4510 -0.0353 -0.1706 -0.0696 522 TRP A N 4156 C CA . TRP A 522 ? 0.3103 0.2508 0.4515 -0.0333 -0.1564 -0.0615 522 TRP A CA 4157 C C . TRP A 522 ? 0.4601 0.4160 0.6384 -0.0414 -0.1551 -0.0593 522 TRP A C 4158 O O . TRP A 522 ? 0.3763 0.3536 0.5786 -0.0393 -0.1477 -0.0538 522 TRP A O 4159 C CB . TRP A 522 ? 0.3023 0.2319 0.4258 -0.0318 -0.1411 -0.0587 522 TRP A CB 4160 C CG . TRP A 522 ? 0.3617 0.2831 0.4569 -0.0259 -0.1396 -0.0567 522 TRP A CG 4161 C CD1 . TRP A 522 ? 0.3372 0.2486 0.4068 -0.0253 -0.1376 -0.0590 522 TRP A CD1 4162 C CD2 . TRP A 522 ? 0.3013 0.2246 0.3941 -0.0203 -0.1402 -0.0514 522 TRP A CD2 4163 N NE1 . TRP A 522 ? 0.3141 0.2241 0.3659 -0.0225 -0.1368 -0.0520 522 TRP A NE1 4164 C CE2 . TRP A 522 ? 0.3220 0.2351 0.3875 -0.0197 -0.1400 -0.0474 522 TRP A CE2 4165 C CE3 . TRP A 522 ? 0.3192 0.2521 0.4332 -0.0151 -0.1407 -0.0506 522 TRP A CE3 4166 C CZ2 . TRP A 522 ? 0.3502 0.2573 0.4091 -0.0168 -0.1431 -0.0404 522 TRP A CZ2 4167 C CZ3 . TRP A 522 ? 0.3510 0.2754 0.4581 -0.0087 -0.1435 -0.0476 522 TRP A CZ3 4168 C CH2 . TRP A 522 ? 0.3334 0.2426 0.4132 -0.0109 -0.1461 -0.0414 522 TRP A CH2 4169 N N . THR A 523 ? 0.4259 0.3715 0.6100 -0.0508 -0.1618 -0.0637 523 THR A N 4170 C CA . THR A 523 ? 0.4180 0.3757 0.6382 -0.0623 -0.1599 -0.0570 523 THR A CA 4171 C C . THR A 523 ? 0.5014 0.4812 0.7547 -0.0684 -0.1742 -0.0571 523 THR A C 4172 O O . THR A 523 ? 0.4895 0.4978 0.7785 -0.0735 -0.1673 -0.0473 523 THR A O 4173 C CB . THR A 523 ? 0.4590 0.3911 0.6783 -0.0708 -0.1629 -0.0598 523 THR A CB 4174 O OG1 . THR A 523 ? 0.4445 0.3629 0.6412 -0.0638 -0.1495 -0.0567 523 THR A OG1 4175 C CG2 . THR A 523 ? 0.4740 0.4167 0.7332 -0.0863 -0.1631 -0.0477 523 THR A CG2 4176 N N . SER A 524 ? 0.5640 0.5352 0.8033 -0.0674 -0.1923 -0.0667 524 SER A N 4177 C CA . SER A 524 ? 0.5599 0.5511 0.8246 -0.0722 -0.2059 -0.0648 524 SER A CA 4178 C C . SER A 524 ? 0.5802 0.5956 0.8601 -0.0621 -0.2125 -0.0610 524 SER A C 4179 O O . SER A 524 ? 0.6840 0.7320 1.0090 -0.0631 -0.2126 -0.0541 524 SER A O 4180 C CB . SER A 524 ? 0.5994 0.5708 0.8363 -0.0757 -0.2204 -0.0756 524 SER A CB 4181 O OG . SER A 524 ? 0.6329 0.5798 0.8605 -0.0820 -0.2157 -0.0817 524 SER A OG 4182 N N . PHE A 525 ? 0.5281 0.5289 0.7733 -0.0518 -0.2178 -0.0642 525 PHE A N 4183 C CA . PHE A 525 ? 0.4899 0.5067 0.7479 -0.0411 -0.2289 -0.0587 525 PHE A CA 4184 C C . PHE A 525 ? 0.5236 0.5497 0.7939 -0.0267 -0.2099 -0.0533 525 PHE A C 4185 O O . PHE A 525 ? 0.4702 0.5237 0.7821 -0.0193 -0.2097 -0.0500 525 PHE A O 4186 C CB . PHE A 525 ? 0.4449 0.4419 0.6568 -0.0374 -0.2424 -0.0588 525 PHE A CB 4187 C CG . PHE A 525 ? 0.5325 0.5382 0.7552 -0.0256 -0.2542 -0.0488 525 PHE A CG 4188 C CD1 . PHE A 525 ? 0.5579 0.5866 0.8167 -0.0227 -0.2675 -0.0423 525 PHE A CD1 4189 C CD2 . PHE A 525 ? 0.4525 0.4410 0.6494 -0.0164 -0.2476 -0.0434 525 PHE A CD2 4190 C CE1 . PHE A 525 ? 0.5769 0.6101 0.8500 -0.0094 -0.2786 -0.0320 525 PHE A CE1 4191 C CE2 . PHE A 525 ? 0.4594 0.4495 0.6689 -0.0049 -0.2595 -0.0325 525 PHE A CE2 4192 C CZ . PHE A 525 ? 0.4875 0.5000 0.7381 -0.0004 -0.2776 -0.0273 525 PHE A CZ 4193 N N . PHE A 526 ? 0.4895 0.4937 0.7251 -0.0223 -0.1948 -0.0543 526 PHE A N 4194 C CA . PHE A 526 ? 0.4643 0.4699 0.7031 -0.0092 -0.1804 -0.0527 526 PHE A CA 4195 C C . PHE A 526 ? 0.3896 0.4256 0.6684 -0.0046 -0.1637 -0.0541 526 PHE A C 4196 O O . PHE A 526 ? 0.3843 0.4281 0.6786 0.0099 -0.1593 -0.0568 526 PHE A O 4197 C CB . PHE A 526 ? 0.3777 0.3572 0.5749 -0.0092 -0.1680 -0.0532 526 PHE A CB 4198 C CG . PHE A 526 ? 0.3408 0.3129 0.5342 0.0026 -0.1610 -0.0532 526 PHE A CG 4199 C CD1 . PHE A 526 ? 0.4045 0.3622 0.5907 0.0101 -0.1757 -0.0484 526 PHE A CD1 4200 C CD2 . PHE A 526 ? 0.3229 0.3009 0.5189 0.0052 -0.1415 -0.0576 526 PHE A CD2 4201 C CE1 . PHE A 526 ? 0.4326 0.3770 0.6185 0.0203 -0.1720 -0.0497 526 PHE A CE1 4202 C CE2 . PHE A 526 ? 0.3267 0.2941 0.5176 0.0157 -0.1370 -0.0619 526 PHE A CE2 4203 C CZ . PHE A 526 ? 0.3734 0.3217 0.5613 0.0235 -0.1527 -0.0588 526 PHE A CZ 4204 N N . PRO A 527 ? 0.4280 0.4817 0.7244 -0.0168 -0.1542 -0.0522 527 PRO A N 4205 C CA . PRO A 527 ? 0.4548 0.5456 0.7879 -0.0135 -0.1361 -0.0515 527 PRO A CA 4206 C C . PRO A 527 ? 0.5333 0.6580 0.9160 -0.0035 -0.1441 -0.0522 527 PRO A C 4207 O O . PRO A 527 ? 0.5284 0.6898 0.9441 0.0027 -0.1265 -0.0539 527 PRO A O 4208 C CB . PRO A 527 ? 0.4710 0.5732 0.8157 -0.0330 -0.1300 -0.0436 527 PRO A CB 4209 C CG . PRO A 527 ? 0.5440 0.6060 0.8480 -0.0411 -0.1370 -0.0440 527 PRO A CG 4210 C CD . PRO A 527 ? 0.5156 0.5550 0.7977 -0.0331 -0.1560 -0.0504 527 PRO A CD 4211 N N . LYS A 528 ? 0.5134 0.6299 0.9018 -0.0015 -0.1699 -0.0507 528 LYS A N 4212 C CA . LYS A 528 ? 0.5202 0.6698 0.9606 0.0083 -0.1822 -0.0489 528 LYS A CA 4213 C C . LYS A 528 ? 0.5361 0.6777 0.9816 0.0323 -0.1847 -0.0533 528 LYS A C 4214 O O . LYS A 528 ? 0.5628 0.7372 1.0589 0.0472 -0.1838 -0.0554 528 LYS A O 4215 C CB . LYS A 528 ? 0.5164 0.6644 0.9633 -0.0037 -0.2132 -0.0431 528 LYS A CB 4216 C CG . LYS A 528 ? 0.5308 0.6826 0.9797 -0.0274 -0.2149 -0.0413 528 LYS A CG 4217 C CD . LYS A 528 ? 0.5870 0.7210 1.0135 -0.0375 -0.2392 -0.0396 528 LYS A CD 4218 C CE . LYS A 528 ? 0.6454 0.7712 1.0648 -0.0587 -0.2379 -0.0404 528 LYS A CE 4219 N NZ . LYS A 528 ? 0.7694 0.8801 1.1664 -0.0673 -0.2597 -0.0426 528 LYS A NZ 4220 N N . VAL A 529 ? 0.5320 0.6305 0.9295 0.0360 -0.1885 -0.0543 529 VAL A N 4221 C CA . VAL A 529 ? 0.6744 0.7556 1.0755 0.0563 -0.1951 -0.0565 529 VAL A CA 4222 C C . VAL A 529 ? 0.6895 0.7824 1.1074 0.0725 -0.1695 -0.0709 529 VAL A C 4223 O O . VAL A 529 ? 0.6363 0.7471 1.0487 0.0655 -0.1452 -0.0769 529 VAL A O 4224 C CB . VAL A 529 ? 0.5471 0.5803 0.8931 0.0523 -0.2056 -0.0508 529 VAL A CB 4225 C CG1 . VAL A 529 ? 0.4894 0.5133 0.8063 0.0351 -0.2245 -0.0408 529 VAL A CG1 4226 C CG2 . VAL A 529 ? 0.5459 0.5599 0.8551 0.0485 -0.1827 -0.0584 529 VAL A CG2 4227 O OXT . VAL A 529 ? 0.7086 0.7920 1.1441 0.0928 -0.1735 -0.0773 529 VAL A OXT # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 GLU 1 1 ? ? ? A . n A 1 2 ASP 2 2 ? ? ? A . n A 1 3 ASP 3 3 ? ? ? A . n A 1 4 ILE 4 4 4 ILE ILE A . n A 1 5 ILE 5 5 5 ILE ILE A . n A 1 6 ILE 6 6 6 ILE ILE A . n A 1 7 ALA 7 7 7 ALA ALA A . n A 1 8 THR 8 8 8 THR THR A . n A 1 9 LYS 9 9 9 LYS LYS A . n A 1 10 ASN 10 10 10 ASN ASN A . n A 1 11 GLY 11 11 11 GLY GLY A . n A 1 12 LYS 12 12 12 LYS LYS A . n A 1 13 VAL 13 13 13 VAL VAL A . n A 1 14 ARG 14 14 14 ARG ARG A . n A 1 15 GLY 15 15 15 GLY GLY A . n A 1 16 MET 16 16 16 MET MET A . n A 1 17 GLN 17 17 17 GLN GLN A . n A 1 18 LEU 18 18 18 LEU LEU A . n A 1 19 THR 19 19 19 THR THR A . n A 1 20 VAL 20 20 20 VAL VAL A . n A 1 21 PHE 21 21 21 PHE PHE A . n A 1 22 GLY 22 22 22 GLY GLY A . n A 1 23 GLY 23 23 23 GLY GLY A . n A 1 24 THR 24 24 24 THR THR A . n A 1 25 VAL 25 25 25 VAL VAL A . n A 1 26 THR 26 26 26 THR THR A . n A 1 27 ALA 27 27 27 ALA ALA A . n A 1 28 PHE 28 28 28 PHE PHE A . n A 1 29 LEU 29 29 29 LEU LEU A . n A 1 30 GLY 30 30 30 GLY GLY A . n A 1 31 ILE 31 31 31 ILE ILE A . n A 1 32 PRO 32 32 32 PRO PRO A . n A 1 33 TYR 33 33 33 TYR TYR A . n A 1 34 ALA 34 34 34 ALA ALA A . n A 1 35 GLN 35 35 35 GLN GLN A . n A 1 36 PRO 36 36 36 PRO PRO A . n A 1 37 PRO 37 37 37 PRO PRO A . n A 1 38 LEU 38 38 38 LEU LEU A . n A 1 39 GLY 39 39 39 GLY GLY A . n A 1 40 ARG 40 40 40 ARG ARG A . n A 1 41 LEU 41 41 41 LEU LEU A . n A 1 42 ARG 42 42 42 ARG ARG A . n A 1 43 PHE 43 43 43 PHE PHE A . n A 1 44 LYS 44 44 44 LYS LYS A . n A 1 45 LYS 45 45 45 LYS LYS A . n A 1 46 PRO 46 46 46 PRO PRO A . n A 1 47 GLN 47 47 47 GLN GLN A . n A 1 48 SER 48 48 48 SER SER A . n A 1 49 LEU 49 49 49 LEU LEU A . n A 1 50 THR 50 50 50 THR THR A . n A 1 51 LYS 51 51 51 LYS LYS A . n A 1 52 TRP 52 52 52 TRP TRP A . n A 1 53 SER 53 53 53 SER SER A . n A 1 54 ASP 54 54 54 ASP ASP A . n A 1 55 ILE 55 55 55 ILE ILE A . n A 1 56 TRP 56 56 56 TRP TRP A . n A 1 57 ASN 57 57 57 ASN ASN A . n A 1 58 ALA 58 58 58 ALA ALA A . n A 1 59 THR 59 59 59 THR THR A . n A 1 60 LYS 60 60 60 LYS LYS A . n A 1 61 TYR 61 61 61 TYR TYR A . n A 1 62 ALA 62 62 62 ALA ALA A . n A 1 63 ASN 63 63 63 ASN ASN A . n A 1 64 SER 64 64 64 SER SER A . n A 1 65 CYS 65 65 65 CYS CYS A . n A 1 66 CYS 66 66 66 CYS CYS A . n A 1 67 GLN 67 67 67 GLN GLN A . n A 1 68 ASN 68 68 68 ASN ASN A . n A 1 69 ILE 69 69 69 ILE ILE A . n A 1 70 ASP 70 70 70 ASP ASP A . n A 1 71 GLN 71 71 71 GLN GLN A . n A 1 72 SER 72 72 72 SER SER A . n A 1 73 PHE 73 73 73 PHE PHE A . n A 1 74 PRO 74 74 74 PRO PRO A . n A 1 75 GLY 75 75 75 GLY GLY A . n A 1 76 PHE 76 76 76 PHE PHE A . n A 1 77 HIS 77 77 77 HIS HIS A . n A 1 78 GLY 78 78 78 GLY GLY A . n A 1 79 SER 79 79 79 SER SER A . n A 1 80 GLU 80 80 80 GLU GLU A . n A 1 81 MET 81 81 81 MET MET A . n A 1 82 TRP 82 82 82 TRP TRP A . n A 1 83 ASN 83 83 83 ASN ASN A . n A 1 84 PRO 84 84 84 PRO PRO A . n A 1 85 ASN 85 85 85 ASN ASN A . n A 1 86 THR 86 86 86 THR THR A . n A 1 87 ASP 87 87 87 ASP ASP A . n A 1 88 LEU 88 88 88 LEU LEU A . n A 1 89 SER 89 89 89 SER SER A . n A 1 90 GLU 90 90 90 GLU GLU A . n A 1 91 ASP 91 91 91 ASP ASP A . n A 1 92 CYS 92 92 92 CYS CYS A . n A 1 93 LEU 93 93 93 LEU LEU A . n A 1 94 TYR 94 94 94 TYR TYR A . n A 1 95 LEU 95 95 95 LEU LEU A . n A 1 96 ASN 96 96 96 ASN ASN A . n A 1 97 VAL 97 97 97 VAL VAL A . n A 1 98 TRP 98 98 98 TRP TRP A . n A 1 99 ILE 99 99 99 ILE ILE A . n A 1 100 PRO 100 100 100 PRO PRO A . n A 1 101 ALA 101 101 101 ALA ALA A . n A 1 102 PRO 102 102 102 PRO PRO A . n A 1 103 LYS 103 103 103 LYS LYS A . n A 1 104 PRO 104 104 104 PRO PRO A . n A 1 105 LYS 105 105 105 LYS LYS A . n A 1 106 ASN 106 106 106 ASN ASN A . n A 1 107 ALA 107 107 107 ALA ALA A . n A 1 108 THR 108 108 108 THR THR A . n A 1 109 VAL 109 109 109 VAL VAL A . n A 1 110 LEU 110 110 110 LEU LEU A . n A 1 111 ILE 111 111 111 ILE ILE A . n A 1 112 TRP 112 112 112 TRP TRP A . n A 1 113 ILE 113 113 113 ILE ILE A . n A 1 114 TYR 114 114 114 TYR TYR A . n A 1 115 GLY 115 115 115 GLY GLY A . n A 1 116 GLY 116 116 116 GLY GLY A . n A 1 117 GLY 117 117 117 GLY GLY A . n A 1 118 PHE 118 118 118 PHE PHE A . n A 1 119 GLN 119 119 119 GLN GLN A . n A 1 120 THR 120 120 120 THR THR A . n A 1 121 GLY 121 121 121 GLY GLY A . n A 1 122 THR 122 122 122 THR THR A . n A 1 123 SER 123 123 123 SER SER A . n A 1 124 SER 124 124 124 SER SER A . n A 1 125 LEU 125 125 125 LEU LEU A . n A 1 126 HIS 126 126 126 HIS HIS A . n A 1 127 VAL 127 127 127 VAL VAL A . n A 1 128 TYR 128 128 128 TYR TYR A . n A 1 129 ASP 129 129 129 ASP ASP A . n A 1 130 GLY 130 130 130 GLY GLY A . n A 1 131 LYS 131 131 131 LYS LYS A . n A 1 132 PHE 132 132 132 PHE PHE A . n A 1 133 LEU 133 133 133 LEU LEU A . n A 1 134 ALA 134 134 134 ALA ALA A . n A 1 135 ARG 135 135 135 ARG ARG A . n A 1 136 VAL 136 136 136 VAL VAL A . n A 1 137 GLU 137 137 137 GLU GLU A . n A 1 138 ARG 138 138 138 ARG ARG A . n A 1 139 VAL 139 139 139 VAL VAL A . n A 1 140 ILE 140 140 140 ILE ILE A . n A 1 141 VAL 141 141 141 VAL VAL A . n A 1 142 VAL 142 142 142 VAL VAL A . n A 1 143 SER 143 143 143 SER SER A . n A 1 144 MET 144 144 144 MET MET A . n A 1 145 ASN 145 145 145 ASN ASN A . n A 1 146 TYR 146 146 146 TYR TYR A . n A 1 147 ARG 147 147 147 ARG ARG A . n A 1 148 VAL 148 148 148 VAL VAL A . n A 1 149 GLY 149 149 149 GLY GLY A . n A 1 150 ALA 150 150 150 ALA ALA A . n A 1 151 LEU 151 151 151 LEU LEU A . n A 1 152 GLY 152 152 152 GLY GLY A . n A 1 153 PHE 153 153 153 PHE PHE A . n A 1 154 LEU 154 154 154 LEU LEU A . n A 1 155 ALA 155 155 155 ALA ALA A . n A 1 156 LEU 156 156 156 LEU LEU A . n A 1 157 PRO 157 157 157 PRO PRO A . n A 1 158 GLY 158 158 158 GLY GLY A . n A 1 159 ASN 159 159 159 ASN ASN A . n A 1 160 PRO 160 160 160 PRO PRO A . n A 1 161 GLU 161 161 161 GLU GLU A . n A 1 162 ALA 162 162 162 ALA ALA A . n A 1 163 PRO 163 163 163 PRO PRO A . n A 1 164 GLY 164 164 164 GLY GLY A . n A 1 165 ASN 165 165 165 ASN ASN A . n A 1 166 MET 166 166 166 MET MET A . n A 1 167 GLY 167 167 167 GLY GLY A . n A 1 168 LEU 168 168 168 LEU LEU A . n A 1 169 PHE 169 169 169 PHE PHE A . n A 1 170 ASP 170 170 170 ASP ASP A . n A 1 171 GLN 171 171 171 GLN GLN A . n A 1 172 GLN 172 172 172 GLN GLN A . n A 1 173 LEU 173 173 173 LEU LEU A . n A 1 174 ALA 174 174 174 ALA ALA A . n A 1 175 LEU 175 175 175 LEU LEU A . n A 1 176 GLN 176 176 176 GLN GLN A . n A 1 177 TRP 177 177 177 TRP TRP A . n A 1 178 VAL 178 178 178 VAL VAL A . n A 1 179 GLN 179 179 179 GLN GLN A . n A 1 180 LYS 180 180 180 LYS LYS A . n A 1 181 ASN 181 181 181 ASN ASN A . n A 1 182 ILE 182 182 182 ILE ILE A . n A 1 183 ALA 183 183 183 ALA ALA A . n A 1 184 ALA 184 184 184 ALA ALA A . n A 1 185 PHE 185 185 185 PHE PHE A . n A 1 186 GLY 186 186 186 GLY GLY A . n A 1 187 GLY 187 187 187 GLY GLY A . n A 1 188 ASN 188 188 188 ASN ASN A . n A 1 189 PRO 189 189 189 PRO PRO A . n A 1 190 LYS 190 190 190 LYS LYS A . n A 1 191 SER 191 191 191 SER SER A . n A 1 192 VAL 192 192 192 VAL VAL A . n A 1 193 THR 193 193 193 THR THR A . n A 1 194 LEU 194 194 194 LEU LEU A . n A 1 195 PHE 195 195 195 PHE PHE A . n A 1 196 GLY 196 196 196 GLY GLY A . n A 1 197 GLU 197 197 197 GLU GLU A . n A 1 198 SER 198 198 198 SER SER A . n A 1 199 ALA 199 199 199 ALA ALA A . n A 1 200 GLY 200 200 200 GLY GLY A . n A 1 201 ALA 201 201 201 ALA ALA A . n A 1 202 ALA 202 202 202 ALA ALA A . n A 1 203 SER 203 203 203 SER SER A . n A 1 204 VAL 204 204 204 VAL VAL A . n A 1 205 SER 205 205 205 SER SER A . n A 1 206 LEU 206 206 206 LEU LEU A . n A 1 207 HIS 207 207 207 HIS HIS A . n A 1 208 LEU 208 208 208 LEU LEU A . n A 1 209 LEU 209 209 209 LEU LEU A . n A 1 210 SER 210 210 210 SER SER A . n A 1 211 PRO 211 211 211 PRO PRO A . n A 1 212 GLY 212 212 212 GLY GLY A . n A 1 213 SER 213 213 213 SER SER A . n A 1 214 HIS 214 214 214 HIS HIS A . n A 1 215 SER 215 215 215 SER SER A . n A 1 216 LEU 216 216 216 LEU LEU A . n A 1 217 PHE 217 217 217 PHE PHE A . n A 1 218 THR 218 218 218 THR THR A . n A 1 219 ARG 219 219 219 ARG ARG A . n A 1 220 ALA 220 220 220 ALA ALA A . n A 1 221 ILE 221 221 221 ILE ILE A . n A 1 222 LEU 222 222 222 LEU LEU A . n A 1 223 GLN 223 223 223 GLN GLN A . n A 1 224 SER 224 224 224 SER SER A . n A 1 225 GLY 225 225 225 GLY GLY A . n A 1 226 SER 226 226 226 SER SER A . n A 1 227 PHE 227 227 227 PHE PHE A . n A 1 228 ASN 228 228 228 ASN ASN A . n A 1 229 ALA 229 229 229 ALA ALA A . n A 1 230 PRO 230 230 230 PRO PRO A . n A 1 231 TRP 231 231 231 TRP TRP A . n A 1 232 ALA 232 232 232 ALA ALA A . n A 1 233 VAL 233 233 233 VAL VAL A . n A 1 234 THR 234 234 234 THR THR A . n A 1 235 SER 235 235 235 SER SER A . n A 1 236 LEU 236 236 236 LEU LEU A . n A 1 237 TYR 237 237 237 TYR TYR A . n A 1 238 GLU 238 238 238 GLU GLU A . n A 1 239 ALA 239 239 239 ALA ALA A . n A 1 240 ARG 240 240 240 ARG ARG A . n A 1 241 ASN 241 241 241 ASN ASN A . n A 1 242 ARG 242 242 242 ARG ARG A . n A 1 243 THR 243 243 243 THR THR A . n A 1 244 LEU 244 244 244 LEU LEU A . n A 1 245 ASN 245 245 245 ASN ASN A . n A 1 246 LEU 246 246 246 LEU LEU A . n A 1 247 ALA 247 247 247 ALA ALA A . n A 1 248 LYS 248 248 248 LYS LYS A . n A 1 249 LEU 249 249 249 LEU LEU A . n A 1 250 THR 250 250 250 THR THR A . n A 1 251 GLY 251 251 251 GLY GLY A . n A 1 252 CYS 252 252 252 CYS CYS A . n A 1 253 SER 253 253 253 SER SER A . n A 1 254 ARG 254 254 254 ARG ARG A . n A 1 255 GLU 255 255 255 GLU GLU A . n A 1 256 ASN 256 256 256 ASN ASN A . n A 1 257 GLU 257 257 257 GLU GLU A . n A 1 258 THR 258 258 258 THR THR A . n A 1 259 GLU 259 259 259 GLU GLU A . n A 1 260 ILE 260 260 260 ILE ILE A . n A 1 261 ILE 261 261 261 ILE ILE A . n A 1 262 LYS 262 262 262 LYS LYS A . n A 1 263 CYS 263 263 263 CYS CYS A . n A 1 264 LEU 264 264 264 LEU LEU A . n A 1 265 ARG 265 265 265 ARG ARG A . n A 1 266 ASN 266 266 266 ASN ASN A . n A 1 267 LYS 267 267 267 LYS LYS A . n A 1 268 ASP 268 268 268 ASP ASP A . n A 1 269 PRO 269 269 269 PRO PRO A . n A 1 270 GLN 270 270 270 GLN GLN A . n A 1 271 GLU 271 271 271 GLU GLU A . n A 1 272 ILE 272 272 272 ILE ILE A . n A 1 273 LEU 273 273 273 LEU LEU A . n A 1 274 LEU 274 274 274 LEU LEU A . n A 1 275 ASN 275 275 275 ASN ASN A . n A 1 276 GLU 276 276 276 GLU GLU A . n A 1 277 ALA 277 277 277 ALA ALA A . n A 1 278 PHE 278 278 278 PHE PHE A . n A 1 279 VAL 279 279 279 VAL VAL A . n A 1 280 VAL 280 280 280 VAL VAL A . n A 1 281 PRO 281 281 281 PRO PRO A . n A 1 282 TYR 282 282 282 TYR TYR A . n A 1 283 GLY 283 283 283 GLY GLY A . n A 1 284 THR 284 284 284 THR THR A . n A 1 285 PRO 285 285 285 PRO PRO A . n A 1 286 LEU 286 286 286 LEU LEU A . n A 1 287 SER 287 287 287 SER SER A . n A 1 288 VAL 288 288 288 VAL VAL A . n A 1 289 ASN 289 289 289 ASN ASN A . n A 1 290 PHE 290 290 290 PHE PHE A . n A 1 291 GLY 291 291 291 GLY GLY A . n A 1 292 PRO 292 292 292 PRO PRO A . n A 1 293 THR 293 293 293 THR THR A . n A 1 294 VAL 294 294 294 VAL VAL A . n A 1 295 ASP 295 295 295 ASP ASP A . n A 1 296 GLY 296 296 296 GLY GLY A . n A 1 297 ASP 297 297 297 ASP ASP A . n A 1 298 PHE 298 298 298 PHE PHE A . n A 1 299 LEU 299 299 299 LEU LEU A . n A 1 300 THR 300 300 300 THR THR A . n A 1 301 ASP 301 301 301 ASP ASP A . n A 1 302 MET 302 302 302 MET MET A . n A 1 303 PRO 303 303 303 PRO PRO A . n A 1 304 ASP 304 304 304 ASP ASP A . n A 1 305 ILE 305 305 305 ILE ILE A . n A 1 306 LEU 306 306 306 LEU LEU A . n A 1 307 LEU 307 307 307 LEU LEU A . n A 1 308 GLU 308 308 308 GLU GLU A . n A 1 309 LEU 309 309 309 LEU LEU A . n A 1 310 GLY 310 310 310 GLY GLY A . n A 1 311 GLN 311 311 311 GLN GLN A . n A 1 312 PHE 312 312 312 PHE PHE A . n A 1 313 LYS 313 313 313 LYS LYS A . n A 1 314 LYS 314 314 314 LYS LYS A . n A 1 315 THR 315 315 315 THR THR A . n A 1 316 GLN 316 316 316 GLN GLN A . n A 1 317 ILE 317 317 317 ILE ILE A . n A 1 318 LEU 318 318 318 LEU LEU A . n A 1 319 VAL 319 319 319 VAL VAL A . n A 1 320 GLY 320 320 320 GLY GLY A . n A 1 321 VAL 321 321 321 VAL VAL A . n A 1 322 ASN 322 322 322 ASN ASN A . n A 1 323 LYS 323 323 323 LYS LYS A . n A 1 324 ASP 324 324 324 ASP ASP A . n A 1 325 GLU 325 325 325 GLU GLU A . n A 1 326 GLY 326 326 326 GLY GLY A . n A 1 327 THR 327 327 327 THR THR A . n A 1 328 ALA 328 328 328 ALA ALA A . n A 1 329 PHE 329 329 329 PHE PHE A . n A 1 330 LEU 330 330 330 LEU LEU 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 GLY 333 333 333 GLY GLY A . n A 1 334 ALA 334 334 334 ALA ALA A . n A 1 335 PRO 335 335 335 PRO PRO A . n A 1 336 GLY 336 336 336 GLY GLY A . n A 1 337 PHE 337 337 337 PHE PHE A . n A 1 338 SER 338 338 338 SER SER A . n A 1 339 LYS 339 339 339 LYS LYS A . n A 1 340 ASP 340 340 340 ASP ASP A . n A 1 341 ASN 341 341 341 ASN ASN A . n A 1 342 ASN 342 342 342 ASN ASN A . n A 1 343 SER 343 343 343 SER SER A . n A 1 344 ILE 344 344 344 ILE ILE A . n A 1 345 ILE 345 345 345 ILE ILE A . n A 1 346 THR 346 346 346 THR THR A . n A 1 347 ARG 347 347 347 ARG ARG A . n A 1 348 LYS 348 348 348 LYS LYS A . n A 1 349 GLU 349 349 349 GLU GLU A . n A 1 350 PHE 350 350 350 PHE PHE A . n A 1 351 GLN 351 351 351 GLN GLN A . n A 1 352 GLU 352 352 352 GLU GLU A . n A 1 353 GLY 353 353 353 GLY GLY A . n A 1 354 LEU 354 354 354 LEU LEU A . n A 1 355 LYS 355 355 355 LYS LYS A . n A 1 356 ILE 356 356 356 ILE ILE A . n A 1 357 PHE 357 357 357 PHE PHE A . n A 1 358 PHE 358 358 358 PHE PHE A . n A 1 359 PRO 359 359 359 PRO PRO A . n A 1 360 GLY 360 360 360 GLY GLY A . n A 1 361 VAL 361 361 361 VAL VAL A . n A 1 362 SER 362 362 362 SER SER 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 GLY 365 365 365 GLY GLY A . n A 1 366 LYS 366 366 366 LYS LYS A . n A 1 367 GLU 367 367 367 GLU GLU A . n A 1 368 SER 368 368 368 SER SER A . n A 1 369 ILE 369 369 369 ILE ILE A . n A 1 370 LEU 370 370 370 LEU LEU A . n A 1 371 PHE 371 371 371 PHE PHE A . n A 1 372 HIS 372 372 372 HIS HIS A . n A 1 373 TYR 373 373 373 TYR TYR A . n A 1 374 THR 374 374 374 THR THR A . n A 1 375 ASP 375 375 375 ASP ASP A . n A 1 376 TRP 376 376 376 TRP TRP A . n A 1 377 VAL 377 377 377 VAL VAL A . n A 1 378 ASP 378 378 ? ? ? A . n A 1 379 ASP 379 379 ? ? ? A . n A 1 380 GLN 380 380 380 GLN GLN A . n A 1 381 ARG 381 381 381 ARG ARG A . n A 1 382 PRO 382 382 382 PRO PRO A . n A 1 383 GLU 383 383 383 GLU GLU A . n A 1 384 ASN 384 384 384 ASN ASN A . n A 1 385 TYR 385 385 385 TYR TYR A . n A 1 386 ARG 386 386 386 ARG ARG A . n A 1 387 GLU 387 387 387 GLU GLU A . n A 1 388 ALA 388 388 388 ALA ALA A . n A 1 389 LEU 389 389 389 LEU LEU A . n A 1 390 GLY 390 390 390 GLY GLY A . n A 1 391 ASP 391 391 391 ASP ASP A . n A 1 392 VAL 392 392 392 VAL VAL A . n A 1 393 VAL 393 393 393 VAL VAL A . n A 1 394 GLY 394 394 394 GLY GLY A . n A 1 395 ASP 395 395 395 ASP ASP A . n A 1 396 TYR 396 396 396 TYR TYR A . n A 1 397 ASN 397 397 397 ASN ASN A . n A 1 398 PHE 398 398 398 PHE PHE A . n A 1 399 ILE 399 399 399 ILE ILE A . n A 1 400 CYS 400 400 400 CYS CYS A . n A 1 401 PRO 401 401 401 PRO PRO A . n A 1 402 ALA 402 402 402 ALA ALA A . n A 1 403 LEU 403 403 403 LEU LEU A . n A 1 404 GLU 404 404 404 GLU GLU A . n A 1 405 PHE 405 405 405 PHE PHE A . n A 1 406 THR 406 406 406 THR THR A . n A 1 407 LYS 407 407 407 LYS LYS A . n A 1 408 LYS 408 408 408 LYS LYS A . n A 1 409 PHE 409 409 409 PHE PHE A . n A 1 410 SER 410 410 410 SER SER A . n A 1 411 GLU 411 411 411 GLU GLU A . n A 1 412 TRP 412 412 412 TRP TRP A . n A 1 413 GLY 413 413 413 GLY GLY A . n A 1 414 ASN 414 414 414 ASN ASN A . n A 1 415 ASN 415 415 415 ASN ASN A . n A 1 416 ALA 416 416 416 ALA ALA A . n A 1 417 PHE 417 417 417 PHE PHE A . n A 1 418 PHE 418 418 418 PHE PHE A . n A 1 419 TYR 419 419 419 TYR TYR A . n A 1 420 TYR 420 420 420 TYR TYR A . n A 1 421 PHE 421 421 421 PHE PHE A . n A 1 422 GLU 422 422 422 GLU GLU A . n A 1 423 HIS 423 423 423 HIS HIS A . n A 1 424 ARG 424 424 424 ARG ARG A . n A 1 425 SER 425 425 425 SER SER A . n A 1 426 SER 426 426 426 SER SER A . n A 1 427 LYS 427 427 427 LYS LYS A . n A 1 428 LEU 428 428 428 LEU LEU A . n A 1 429 PRO 429 429 429 PRO PRO A . n A 1 430 TRP 430 430 430 TRP TRP A . n A 1 431 PRO 431 431 431 PRO PRO A . n A 1 432 GLU 432 432 432 GLU GLU A . n A 1 433 TRP 433 433 433 TRP TRP A . n A 1 434 MET 434 434 434 MET MET A . n A 1 435 GLY 435 435 435 GLY GLY A . n A 1 436 VAL 436 436 436 VAL VAL A . n A 1 437 MET 437 437 437 MET MET A . n A 1 438 HIS 438 438 438 HIS HIS A . n A 1 439 GLY 439 439 439 GLY GLY A . n A 1 440 TYR 440 440 440 TYR TYR A . n A 1 441 GLU 441 441 441 GLU GLU A . n A 1 442 ILE 442 442 442 ILE ILE A . n A 1 443 GLU 443 443 443 GLU GLU A . n A 1 444 PHE 444 444 444 PHE PHE A . n A 1 445 VAL 445 445 445 VAL VAL A . n A 1 446 PHE 446 446 446 PHE PHE A . n A 1 447 GLY 447 447 447 GLY GLY A . n A 1 448 LEU 448 448 448 LEU LEU A . n A 1 449 PRO 449 449 449 PRO PRO A . n A 1 450 LEU 450 450 450 LEU LEU A . n A 1 451 GLU 451 451 451 GLU GLU A . n A 1 452 ARG 452 452 452 ARG ARG A . n A 1 453 ARG 453 453 453 ARG ARG A . n A 1 454 ASP 454 454 454 ASP ASP A . n A 1 455 GLN 455 455 455 GLN GLN A . n A 1 456 TYR 456 456 456 TYR TYR A . n A 1 457 THR 457 457 457 THR THR A . n A 1 458 LYS 458 458 458 LYS LYS A . n A 1 459 ALA 459 459 459 ALA ALA A . n A 1 460 GLU 460 460 460 GLU GLU A . n A 1 461 GLU 461 461 461 GLU GLU A . n A 1 462 ILE 462 462 462 ILE ILE A . n A 1 463 LEU 463 463 463 LEU LEU A . n A 1 464 SER 464 464 464 SER SER A . n A 1 465 ARG 465 465 465 ARG ARG A . n A 1 466 SER 466 466 466 SER SER A . n A 1 467 ILE 467 467 467 ILE ILE A . n A 1 468 VAL 468 468 468 VAL VAL A . n A 1 469 LYS 469 469 469 LYS LYS A . n A 1 470 ARG 470 470 470 ARG ARG A . n A 1 471 TRP 471 471 471 TRP TRP A . n A 1 472 ALA 472 472 472 ALA ALA A . n A 1 473 ASN 473 473 473 ASN ASN A . n A 1 474 PHE 474 474 474 PHE PHE A . n A 1 475 ALA 475 475 475 ALA ALA A . n A 1 476 LYS 476 476 476 LYS LYS A . n A 1 477 TYR 477 477 477 TYR TYR A . n A 1 478 GLY 478 478 478 GLY GLY A . n A 1 479 ASN 479 479 479 ASN ASN A . n A 1 480 PRO 480 480 480 PRO PRO A . n A 1 481 GLN 481 481 481 GLN GLN A . n A 1 482 GLU 482 482 482 GLU GLU A . n A 1 483 THR 483 483 483 THR THR A . n A 1 484 GLN 484 484 484 GLN GLN A . n A 1 485 ASN 485 485 485 ASN ASN A . n A 1 486 GLN 486 486 486 GLN GLN A . n A 1 487 SER 487 487 487 SER SER A . n A 1 488 THR 488 488 488 THR THR A . n A 1 489 SER 489 489 489 SER SER A . n A 1 490 TRP 490 490 490 TRP TRP A . n A 1 491 PRO 491 491 491 PRO PRO A . n A 1 492 VAL 492 492 492 VAL VAL A . n A 1 493 PHE 493 493 493 PHE PHE A . n A 1 494 LYS 494 494 494 LYS LYS A . n A 1 495 SER 495 495 495 SER SER A . n A 1 496 THR 496 496 496 THR THR A . n A 1 497 GLU 497 497 497 GLU GLU A . n A 1 498 GLN 498 498 498 GLN GLN A . n A 1 499 LYS 499 499 499 LYS LYS A . n A 1 500 TYR 500 500 500 TYR TYR A . n A 1 501 LEU 501 501 501 LEU LEU A . n A 1 502 THR 502 502 502 THR THR A . n A 1 503 LEU 503 503 503 LEU LEU A . n A 1 504 ASN 504 504 504 ASN ASN A . n A 1 505 THR 505 505 505 THR THR A . n A 1 506 GLU 506 506 506 GLU GLU A . n A 1 507 SER 507 507 507 SER SER A . n A 1 508 THR 508 508 508 THR THR A . n A 1 509 ARG 509 509 509 ARG ARG A . n A 1 510 ILE 510 510 510 ILE ILE A . n A 1 511 MET 511 511 511 MET MET A . n A 1 512 THR 512 512 512 THR THR A . n A 1 513 LYS 513 513 513 LYS LYS A . n A 1 514 LEU 514 514 514 LEU LEU A . n A 1 515 ARG 515 515 515 ARG ARG A . n A 1 516 ALA 516 516 516 ALA ALA A . n A 1 517 GLN 517 517 517 GLN GLN A . n A 1 518 GLN 518 518 518 GLN GLN A . n A 1 519 CYS 519 519 519 CYS CYS A . n A 1 520 ARG 520 520 520 ARG ARG A . n A 1 521 PHE 521 521 521 PHE PHE A . n A 1 522 TRP 522 522 522 TRP TRP 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 PHE 525 525 525 PHE PHE A . n A 1 526 PHE 526 526 526 PHE PHE A . n A 1 527 PRO 527 527 527 PRO PRO A . n A 1 528 LYS 528 528 528 LYS LYS A . n A 1 529 VAL 529 529 529 VAL VAL A . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code B 2 NAG 1 601 601 NAG NAG A . C 2 NAG 1 611 611 NAG NAG A . D 3 FUC 1 612 612 FUC FU4 A . E 2 NAG 1 621 621 NAG NAG A . F 4 FUL 2 622 622 FUL FUL A . G 2 NAG 3 623 623 NAG NAG A . H 2 NAG 1 631 631 NAG NAG A . I 2 NAG 1 641 641 NAG NAG A . J 4 FUL 2 642 642 FUL FUL A . K 2 NAG 3 643 643 NAG NAG A . L 2 NAG 1 651 651 NAG NAG A . M 5 THA 1 701 701 THA THA A . N 6 GOL 1 702 702 GOL GOL A . O 7 SO4 1 703 703 SO4 SO4 A . P 7 SO4 1 704 704 SO4 SO4 A . Q 8 CL 1 705 705 CL CL A . R 8 CL 1 706 706 CL CL A . S 9 FPK 1 710 710 FPK FPK A . T 10 UNX 1 711 711 UNX UNX A . U 10 UNX 1 712 712 UNX UNX A . V 10 UNX 1 713 713 UNX UNX A . W 10 UNX 1 714 714 UNX UNX A . X 10 UNX 1 715 715 UNX UNX A . Y 10 UNX 1 716 716 UNX UNX A . Z 10 UNX 1 717 717 UNX UNX A . AA 11 HOH 1 2001 2001 HOH HOH A . AA 11 HOH 2 2002 2002 HOH HOH A . AA 11 HOH 3 2003 2003 HOH HOH A . AA 11 HOH 4 2004 2004 HOH HOH A . AA 11 HOH 5 2005 2005 HOH HOH A . AA 11 HOH 6 2006 2006 HOH HOH A . AA 11 HOH 7 2007 2007 HOH HOH A . AA 11 HOH 8 2008 2008 HOH HOH A . AA 11 HOH 9 2009 2009 HOH HOH A . AA 11 HOH 10 2010 2010 HOH HOH A . AA 11 HOH 11 2011 2011 HOH HOH A . AA 11 HOH 12 2012 2012 HOH HOH A . AA 11 HOH 13 2013 2013 HOH HOH A . AA 11 HOH 14 2014 2014 HOH HOH A . AA 11 HOH 15 2015 2015 HOH HOH A . AA 11 HOH 16 2016 2016 HOH HOH A . AA 11 HOH 17 2017 2017 HOH HOH A . AA 11 HOH 18 2018 2018 HOH HOH A . AA 11 HOH 19 2019 2019 HOH HOH A . AA 11 HOH 20 2020 2020 HOH HOH A . AA 11 HOH 21 2021 2021 HOH HOH A . AA 11 HOH 22 2022 2022 HOH HOH A . AA 11 HOH 23 2023 2023 HOH HOH A . AA 11 HOH 24 2024 2024 HOH HOH A . AA 11 HOH 25 2025 2025 HOH HOH A . AA 11 HOH 26 2026 2026 HOH HOH A . AA 11 HOH 27 2027 2027 HOH HOH A . AA 11 HOH 28 2028 2028 HOH HOH A . AA 11 HOH 29 2029 2029 HOH HOH A . AA 11 HOH 30 2030 2030 HOH HOH A . AA 11 HOH 31 2031 2031 HOH HOH A . AA 11 HOH 32 2032 2032 HOH HOH A . AA 11 HOH 33 2033 2033 HOH HOH A . AA 11 HOH 34 2034 2034 HOH HOH A . AA 11 HOH 35 2035 2035 HOH HOH A . AA 11 HOH 36 2036 2036 HOH HOH A . AA 11 HOH 37 2037 2037 HOH HOH A . AA 11 HOH 38 2038 2038 HOH HOH A . AA 11 HOH 39 2039 2039 HOH HOH A . AA 11 HOH 40 2040 2040 HOH HOH A . AA 11 HOH 41 2041 2041 HOH HOH A . AA 11 HOH 42 2042 2042 HOH HOH A . AA 11 HOH 43 2043 2043 HOH HOH A . AA 11 HOH 44 2044 2044 HOH HOH A . AA 11 HOH 45 2045 2045 HOH HOH A . AA 11 HOH 46 2046 2046 HOH HOH A . AA 11 HOH 47 2047 2047 HOH HOH A . AA 11 HOH 48 2048 2048 HOH HOH A . AA 11 HOH 49 2049 2049 HOH HOH A . AA 11 HOH 50 2050 2050 HOH HOH A . AA 11 HOH 51 2051 2051 HOH HOH A . AA 11 HOH 52 2052 2052 HOH HOH A . AA 11 HOH 53 2053 2053 HOH HOH A . AA 11 HOH 54 2054 2054 HOH HOH A . AA 11 HOH 55 2055 2055 HOH HOH A . AA 11 HOH 56 2056 2056 HOH HOH A . AA 11 HOH 57 2057 2057 HOH HOH A . AA 11 HOH 58 2058 2058 HOH HOH A . AA 11 HOH 59 2059 2059 HOH HOH A . AA 11 HOH 60 2060 2060 HOH HOH A . AA 11 HOH 61 2061 2061 HOH HOH A . AA 11 HOH 62 2062 2062 HOH HOH A . AA 11 HOH 63 2063 2063 HOH HOH A . AA 11 HOH 64 2064 2064 HOH HOH A . AA 11 HOH 65 2065 2065 HOH HOH A . AA 11 HOH 66 2066 2066 HOH HOH A . AA 11 HOH 67 2067 2067 HOH HOH A . AA 11 HOH 68 2068 2068 HOH HOH A . AA 11 HOH 69 2069 2069 HOH HOH A . AA 11 HOH 70 2070 2070 HOH HOH A . AA 11 HOH 71 2071 2071 HOH HOH A . AA 11 HOH 72 2072 2072 HOH HOH A . AA 11 HOH 73 2073 2073 HOH HOH A . AA 11 HOH 74 2074 2074 HOH HOH A . AA 11 HOH 75 2075 2075 HOH HOH A . AA 11 HOH 76 2076 2076 HOH HOH A . AA 11 HOH 77 2077 2077 HOH HOH A . AA 11 HOH 78 2078 2078 HOH HOH A . AA 11 HOH 79 2079 2079 HOH HOH A . AA 11 HOH 80 2080 2080 HOH HOH A . AA 11 HOH 81 2081 2081 HOH HOH A . AA 11 HOH 82 2082 2082 HOH HOH A . AA 11 HOH 83 2083 2083 HOH HOH A . AA 11 HOH 84 2084 2084 HOH HOH A . AA 11 HOH 85 2085 2085 HOH HOH A . AA 11 HOH 86 2086 2086 HOH HOH A . AA 11 HOH 87 2087 2087 HOH HOH A . AA 11 HOH 88 2088 2088 HOH HOH A . AA 11 HOH 89 2089 2089 HOH HOH A . AA 11 HOH 90 2090 2090 HOH HOH A . AA 11 HOH 91 2091 2091 HOH HOH A . AA 11 HOH 92 2092 2092 HOH HOH A . AA 11 HOH 93 2093 2093 HOH HOH A . AA 11 HOH 94 2094 2094 HOH HOH A . AA 11 HOH 95 2095 2095 HOH HOH A . AA 11 HOH 96 2096 2096 HOH HOH A . AA 11 HOH 97 2097 2097 HOH HOH A . AA 11 HOH 98 2098 2098 HOH HOH A . AA 11 HOH 99 2099 2099 HOH HOH A . AA 11 HOH 100 2100 2100 HOH HOH A . AA 11 HOH 101 2101 2101 HOH HOH A . AA 11 HOH 102 2102 2102 HOH HOH A . AA 11 HOH 103 2103 2103 HOH HOH A . AA 11 HOH 104 2104 2104 HOH HOH A . AA 11 HOH 105 2105 2105 HOH HOH A . AA 11 HOH 106 2106 2106 HOH HOH A . AA 11 HOH 107 2107 2107 HOH HOH A . AA 11 HOH 108 2108 2108 HOH HOH A . AA 11 HOH 109 2109 2109 HOH HOH A . AA 11 HOH 110 2110 2110 HOH HOH A . AA 11 HOH 111 2111 2111 HOH HOH A . AA 11 HOH 112 2112 2112 HOH HOH A . AA 11 HOH 113 2113 2113 HOH HOH A . AA 11 HOH 114 2114 2114 HOH HOH A . AA 11 HOH 115 2115 2115 HOH HOH A . AA 11 HOH 116 2116 2116 HOH HOH A . AA 11 HOH 117 2117 2117 HOH HOH A . AA 11 HOH 118 2118 2118 HOH HOH A . AA 11 HOH 119 2119 2119 HOH HOH A . AA 11 HOH 120 2120 2120 HOH HOH A . AA 11 HOH 121 2121 2121 HOH HOH A . AA 11 HOH 122 2122 2122 HOH HOH A . AA 11 HOH 123 2123 2123 HOH HOH A . AA 11 HOH 124 2124 2124 HOH HOH A . AA 11 HOH 125 2125 2125 HOH HOH A . AA 11 HOH 126 2126 2126 HOH HOH A . AA 11 HOH 127 2127 2127 HOH HOH A . AA 11 HOH 128 2128 2128 HOH HOH A . AA 11 HOH 129 2129 2129 HOH HOH A . AA 11 HOH 130 2130 2130 HOH HOH A . AA 11 HOH 131 2131 2131 HOH HOH A . AA 11 HOH 132 2132 2132 HOH HOH A . AA 11 HOH 133 2133 2133 HOH HOH A . AA 11 HOH 134 2134 2134 HOH HOH A . AA 11 HOH 135 2135 2135 HOH HOH A . AA 11 HOH 136 2136 2136 HOH HOH A . AA 11 HOH 137 2137 2137 HOH HOH A . AA 11 HOH 138 2138 2138 HOH HOH A . AA 11 HOH 139 2139 2139 HOH HOH A . AA 11 HOH 140 2140 2140 HOH HOH A . AA 11 HOH 141 2141 2141 HOH HOH A . AA 11 HOH 142 2142 2142 HOH HOH A . AA 11 HOH 143 2143 2143 HOH HOH A . AA 11 HOH 144 2144 2144 HOH HOH A . AA 11 HOH 145 2145 2145 HOH HOH A . AA 11 HOH 146 2146 2146 HOH HOH A . AA 11 HOH 147 2147 2147 HOH HOH A . AA 11 HOH 148 2148 2148 HOH HOH A . AA 11 HOH 149 2149 2149 HOH HOH A . AA 11 HOH 150 2150 2150 HOH HOH A . AA 11 HOH 151 2151 2151 HOH HOH A . AA 11 HOH 152 2152 2152 HOH HOH A . AA 11 HOH 153 2153 2153 HOH HOH A . AA 11 HOH 154 2154 2154 HOH HOH A . AA 11 HOH 155 2155 2155 HOH HOH A . AA 11 HOH 156 2156 2156 HOH HOH A . AA 11 HOH 157 2157 2157 HOH HOH A . AA 11 HOH 158 2158 2158 HOH HOH A . AA 11 HOH 159 2159 2159 HOH HOH A . AA 11 HOH 160 2160 2160 HOH HOH A . AA 11 HOH 161 2161 2161 HOH HOH A . AA 11 HOH 162 2162 2162 HOH HOH A . AA 11 HOH 163 2163 2163 HOH HOH A . AA 11 HOH 164 2164 2164 HOH HOH A . AA 11 HOH 165 2165 2165 HOH HOH A . AA 11 HOH 166 2166 2166 HOH HOH A . AA 11 HOH 167 2167 2167 HOH HOH A . AA 11 HOH 168 2168 2168 HOH HOH A . AA 11 HOH 169 2169 2169 HOH HOH A . AA 11 HOH 170 2170 2170 HOH HOH A . AA 11 HOH 171 2171 2171 HOH HOH A . AA 11 HOH 172 2172 2172 HOH HOH A . AA 11 HOH 173 2173 2173 HOH HOH A . AA 11 HOH 174 2174 2174 HOH HOH A . AA 11 HOH 175 2175 2175 HOH HOH A . AA 11 HOH 176 2176 2176 HOH HOH A . AA 11 HOH 177 2177 2177 HOH HOH A . AA 11 HOH 178 2178 2178 HOH HOH A . AA 11 HOH 179 2179 2179 HOH HOH A . AA 11 HOH 180 2180 2180 HOH HOH A . AA 11 HOH 181 2181 2181 HOH HOH A . AA 11 HOH 182 2182 2182 HOH HOH A . AA 11 HOH 183 2183 2183 HOH HOH A . AA 11 HOH 184 2184 2184 HOH HOH A . AA 11 HOH 185 2185 2185 HOH HOH A . AA 11 HOH 186 2186 2186 HOH HOH A . AA 11 HOH 187 2187 2187 HOH HOH A . AA 11 HOH 188 2188 2188 HOH HOH A . AA 11 HOH 189 2189 2189 HOH HOH A . AA 11 HOH 190 2190 2190 HOH HOH A . AA 11 HOH 191 2191 2191 HOH HOH A . AA 11 HOH 192 2192 2192 HOH HOH A . AA 11 HOH 193 2193 2193 HOH HOH A . AA 11 HOH 194 2194 2194 HOH HOH A . AA 11 HOH 195 2195 2195 HOH HOH A . AA 11 HOH 196 2196 2196 HOH HOH A . AA 11 HOH 197 2197 2197 HOH HOH A . AA 11 HOH 198 2198 2198 HOH HOH A . AA 11 HOH 199 2199 2199 HOH HOH A . AA 11 HOH 200 2200 2200 HOH HOH A . AA 11 HOH 201 2201 2201 HOH HOH A . AA 11 HOH 202 2202 2202 HOH HOH A . AA 11 HOH 203 2203 2203 HOH HOH A . AA 11 HOH 204 2204 2204 HOH HOH A . AA 11 HOH 205 2205 2205 HOH HOH A . AA 11 HOH 206 2206 2206 HOH HOH A . AA 11 HOH 207 2207 2207 HOH HOH A . AA 11 HOH 208 2208 2208 HOH HOH A . AA 11 HOH 209 2209 2209 HOH HOH A . AA 11 HOH 210 2210 2210 HOH HOH A . AA 11 HOH 211 2211 2211 HOH HOH A . AA 11 HOH 212 2212 2212 HOH HOH A . AA 11 HOH 213 2213 2213 HOH HOH A . AA 11 HOH 214 2214 2214 HOH HOH A . AA 11 HOH 215 2215 2215 HOH HOH A . AA 11 HOH 216 2216 2216 HOH HOH A . AA 11 HOH 217 2217 2217 HOH HOH A . AA 11 HOH 218 2218 2218 HOH HOH A . AA 11 HOH 219 2219 2219 HOH HOH A . AA 11 HOH 220 2220 2220 HOH HOH A . AA 11 HOH 221 2221 2221 HOH HOH A . AA 11 HOH 222 2222 2222 HOH HOH A . AA 11 HOH 223 2223 2223 HOH HOH A . AA 11 HOH 224 2224 2224 HOH HOH A . AA 11 HOH 225 2225 2225 HOH HOH A . AA 11 HOH 226 2226 2226 HOH HOH A . AA 11 HOH 227 2227 2227 HOH HOH A . AA 11 HOH 228 2228 2228 HOH HOH A . AA 11 HOH 229 2229 2229 HOH HOH A . AA 11 HOH 230 2230 2230 HOH HOH A . AA 11 HOH 231 2231 2231 HOH HOH A . AA 11 HOH 232 2232 2232 HOH HOH A . AA 11 HOH 233 2233 2233 HOH HOH A . AA 11 HOH 234 2234 2234 HOH HOH A . AA 11 HOH 235 2235 2235 HOH HOH A . AA 11 HOH 236 2236 2236 HOH HOH A . AA 11 HOH 237 2237 2237 HOH HOH A . AA 11 HOH 238 2238 2238 HOH HOH A . AA 11 HOH 239 2239 2239 HOH HOH A . AA 11 HOH 240 2240 2240 HOH HOH A . AA 11 HOH 241 2241 2241 HOH HOH A . AA 11 HOH 242 2242 2242 HOH HOH A . AA 11 HOH 243 2243 2243 HOH HOH A . AA 11 HOH 244 2244 2244 HOH HOH A . AA 11 HOH 245 2245 2245 HOH HOH A . AA 11 HOH 246 2246 2246 HOH HOH A . AA 11 HOH 247 2247 2247 HOH HOH A . AA 11 HOH 248 2248 2248 HOH HOH A . AA 11 HOH 249 2249 2249 HOH HOH A . AA 11 HOH 250 2250 2250 HOH HOH A . AA 11 HOH 251 2251 2251 HOH HOH A . AA 11 HOH 252 2252 2252 HOH HOH A . AA 11 HOH 253 2253 2253 HOH HOH A . AA 11 HOH 254 2254 2254 HOH HOH A . AA 11 HOH 255 2255 2255 HOH HOH A . AA 11 HOH 256 2256 2256 HOH HOH A . AA 11 HOH 257 2257 2257 HOH HOH A . AA 11 HOH 258 2258 2258 HOH HOH A . AA 11 HOH 259 2259 2259 HOH HOH A . AA 11 HOH 260 2260 2260 HOH HOH A . AA 11 HOH 261 2261 2261 HOH HOH A . AA 11 HOH 262 2262 2262 HOH HOH A . AA 11 HOH 263 2263 2263 HOH HOH A . AA 11 HOH 264 2264 2264 HOH HOH A . AA 11 HOH 265 2265 2265 HOH HOH A . AA 11 HOH 266 2266 2266 HOH HOH A . AA 11 HOH 267 2267 2267 HOH HOH A . AA 11 HOH 268 2268 2268 HOH HOH A . AA 11 HOH 269 2269 2269 HOH HOH A . AA 11 HOH 270 2270 2270 HOH HOH A . AA 11 HOH 271 2271 2271 HOH HOH A . AA 11 HOH 272 2272 2272 HOH HOH A . AA 11 HOH 273 2273 2273 HOH HOH A . AA 11 HOH 274 2274 2274 HOH HOH A . AA 11 HOH 275 2275 2275 HOH HOH A . AA 11 HOH 276 2276 2276 HOH HOH A . AA 11 HOH 277 2277 2277 HOH HOH A . AA 11 HOH 278 2278 2278 HOH HOH A . AA 11 HOH 279 2279 2279 HOH HOH A . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 57 A ASN 57 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 106 A ASN 106 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 241 A ASN 241 ? ASN 'GLYCOSYLATION SITE' 4 A ASN 256 A ASN 256 ? ASN 'GLYCOSYLATION SITE' 5 A ASN 341 A ASN 341 ? ASN 'GLYCOSYLATION SITE' 6 A ASN 485 A ASN 485 ? 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 monomeric _pdbx_struct_assembly.oligomeric_count 1 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA # _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 # _pdbx_struct_special_symmetry.id 1 _pdbx_struct_special_symmetry.PDB_model_num 1 _pdbx_struct_special_symmetry.auth_asym_id A _pdbx_struct_special_symmetry.auth_comp_id HOH _pdbx_struct_special_symmetry.auth_seq_id 2129 _pdbx_struct_special_symmetry.PDB_ins_code ? _pdbx_struct_special_symmetry.label_asym_id AA _pdbx_struct_special_symmetry.label_comp_id HOH _pdbx_struct_special_symmetry.label_seq_id . # 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 2013-05-29 2 'Structure model' 1 1 2013-07-31 3 'Structure model' 1 2 2014-04-09 4 'Structure model' 2 0 2017-11-15 # _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' 'Database references' 2 3 'Structure model' 'Atomic model' 3 3 'Structure model' 'Derived calculations' 4 3 'Structure model' 'Non-polymer description' 5 4 'Structure model' Advisory 6 4 'Structure model' 'Atomic model' 7 4 'Structure model' 'Derived calculations' 8 4 'Structure model' 'Non-polymer description' 9 4 'Structure model' 'Structure summary' # 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' atom_site 2 4 'Structure model' entity 3 4 'Structure model' pdbx_unobs_or_zero_occ_atoms 4 4 'Structure model' pdbx_validate_close_contact 5 4 'Structure model' struct_site_gen # 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 4 'Structure model' '_atom_site.auth_comp_id' 2 4 'Structure model' '_atom_site.label_comp_id' 3 4 'Structure model' '_chem_comp.formula' 4 4 'Structure model' '_chem_comp.id' 5 4 'Structure model' '_chem_comp.name' 6 4 'Structure model' '_entity.formula_weight' 7 4 'Structure model' '_entity.pdbx_description' 8 4 'Structure model' '_pdbx_validate_close_contact.auth_comp_id_1' 9 4 'Structure model' '_struct_site_gen.auth_comp_id' 10 4 'Structure model' '_struct_site_gen.label_comp_id' # 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[1][2] _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[2][2] _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][2] _pdbx_refine_tls.S[3][3] 'X-RAY DIFFRACTION' 1 ? refined 132.9016 127.9849 17.3185 0.5993 0.4181 0.2820 -0.1051 -0.1446 -0.0754 2.6622 2.2135 1.3772 -0.5986 -0.2127 0.2219 -0.1346 0.6986 0.2149 -0.7533 0.1215 0.1332 -0.2378 -0.2138 0.0455 'X-RAY DIFFRACTION' 2 ? refined 130.2196 111.4728 32.4519 0.3708 0.2869 0.4113 -0.0999 -0.0863 -0.0810 1.1105 0.7403 2.4035 0.6579 -1.0400 -1.1745 -0.1934 0.1231 -0.3089 -0.2917 0.0851 -0.0661 0.4867 -0.2820 0.0799 'X-RAY DIFFRACTION' 3 ? refined 137.9794 130.6719 30.9152 0.2468 0.1603 0.2050 -0.0524 -0.0368 -0.0435 1.8228 1.9433 2.0755 -0.0259 0.6398 0.0432 -0.0710 0.1674 0.0410 -0.3399 0.1076 0.0360 -0.2002 -0.0484 -0.0284 'X-RAY DIFFRACTION' 4 ? refined 136.1026 131.2096 47.5354 0.1875 0.1969 0.2070 -0.0008 -0.0673 -0.0575 1.4993 1.9509 2.2119 0.1511 0.2608 0.1916 0.0169 -0.1681 0.0084 0.0286 0.0082 0.1424 -0.1279 -0.2212 -0.0426 'X-RAY DIFFRACTION' 5 ? refined 152.3616 107.5594 28.2685 0.4893 0.4291 0.6282 0.0808 0.0123 -0.2027 1.7763 3.8715 5.6974 0.0893 -0.9645 1.5885 -0.2213 0.2033 -0.6324 -0.1748 0.2905 -0.4412 0.9279 0.9187 -0.0952 'X-RAY DIFFRACTION' 6 ? refined 142.2188 110.6356 58.2482 0.3803 0.2487 0.3708 -0.0432 -0.1610 0.0248 5.2544 3.5359 3.2992 0.6090 1.4110 -0.6461 0.2434 -0.5473 -0.4980 0.3679 0.0620 -0.2191 0.3991 -0.1686 -0.2884 # 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.beg_label_asym_id _pdbx_refine_tls_group.beg_label_seq_id _pdbx_refine_tls_group.end_auth_asym_id _pdbx_refine_tls_group.end_auth_seq_id _pdbx_refine_tls_group.end_label_asym_id _pdbx_refine_tls_group.end_label_seq_id _pdbx_refine_tls_group.selection _pdbx_refine_tls_group.selection_details 'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? 'CHAIN A AND RESSEQ 1:65' 'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? 'CHAIN A AND RESSEQ 66:91' 'X-RAY DIFFRACTION' 3 3 ? ? ? ? ? ? ? ? ? '(CHAIN A AND RESSEQ 92:153) OR (CHAIN A AND RESSEQ 164:231)' 'X-RAY DIFFRACTION' 4 4 ? ? ? ? ? ? ? ? ? '(CHAIN A AND RESSEQ 290:326) OR (CHAIN A AND RESSEQ 397:515)' 'X-RAY DIFFRACTION' 5 5 ? ? ? ? ? ? ? ? ? '(CHAIN A AND RESSEQ 154:163) OR (CHAIN A AND RESSEQ 232:289)' 'X-RAY DIFFRACTION' 6 6 ? ? ? ? ? ? ? ? ? '(CHAIN A AND RESSEQ 327:396) OR (CHAIN A AND RESSEQ 516:529)' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal PHENIX refinement '(PHENIX.REFINE)' ? 1 XDS 'data reduction' . ? 2 XSCALE 'data scaling' . ? 3 MOLREP phasing . ? 4 # _pdbx_entry_details.entry_id 4BDS _pdbx_entry_details.compound_details ? _pdbx_entry_details.source_details ? _pdbx_entry_details.nonpolymer_details ;FPK IS BOUND TO THE OXYANION HOLE OF THE ENZYME, WHICH OFTEN LEADS TO THE DISTORTION OF SOME BONDS. ; _pdbx_entry_details.sequence_details ? # 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 UNK A UNX 716 ? ? UNK A UNX 717 ? ? 1.39 2 1 UNK A UNX 711 ? ? UNK A UNX 712 ? ? 1.39 3 1 UNK A UNX 713 ? ? UNK A UNX 714 ? ? 1.52 4 1 UNK A UNX 714 ? ? UNK A UNX 715 ? ? 1.52 5 1 UNK A UNX 712 ? ? UNK A UNX 713 ? ? 1.54 6 1 UNK A UNX 715 ? ? UNK A UNX 716 ? ? 1.54 7 1 O3 A FUC 612 ? ? O A HOH 2242 ? ? 2.15 8 1 OE1 A GLU 255 ? ? O A HOH 2150 ? ? 2.18 # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 PHE A 43 ? ? 79.70 -8.36 2 1 THR A 50 ? ? -64.36 -115.35 3 1 LYS A 51 ? ? 174.58 121.13 4 1 ALA A 58 ? ? -109.92 66.57 5 1 ASN A 106 ? ? -152.58 54.53 6 1 PHE A 118 ? ? 59.62 13.66 7 1 ALA A 162 ? ? -166.29 71.32 8 1 SER A 198 ? A 57.08 -121.41 9 1 SER A 198 ? B 52.62 -118.62 10 1 ASP A 297 ? ? -132.48 -75.35 11 1 PHE A 398 ? ? -130.33 -54.28 12 1 GLN A 455 ? ? 78.82 -9.54 13 1 ASN A 485 ? ? -108.79 48.21 14 1 GLU A 506 ? ? -86.50 -73.96 # loop_ _pdbx_unobs_or_zero_occ_atoms.id _pdbx_unobs_or_zero_occ_atoms.PDB_model_num _pdbx_unobs_or_zero_occ_atoms.polymer_flag _pdbx_unobs_or_zero_occ_atoms.occupancy_flag _pdbx_unobs_or_zero_occ_atoms.auth_asym_id _pdbx_unobs_or_zero_occ_atoms.auth_comp_id _pdbx_unobs_or_zero_occ_atoms.auth_seq_id _pdbx_unobs_or_zero_occ_atoms.PDB_ins_code _pdbx_unobs_or_zero_occ_atoms.auth_atom_id _pdbx_unobs_or_zero_occ_atoms.label_alt_id _pdbx_unobs_or_zero_occ_atoms.label_asym_id _pdbx_unobs_or_zero_occ_atoms.label_comp_id _pdbx_unobs_or_zero_occ_atoms.label_seq_id _pdbx_unobs_or_zero_occ_atoms.label_atom_id 1 1 Y 1 A GLN 486 ? CG ? A GLN 486 CG 2 1 Y 1 A GLN 486 ? CD ? A GLN 486 CD 3 1 Y 1 A GLN 486 ? OE1 ? A GLN 486 OE1 4 1 Y 1 A GLN 486 ? NE2 ? A GLN 486 NE2 5 1 N 1 A FUC 612 ? O1 ? D FUC 1 O1 # 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 GLU 1 ? A GLU 1 2 1 Y 1 A ASP 2 ? A ASP 2 3 1 Y 1 A ASP 3 ? A ASP 3 4 1 Y 1 A ASP 378 ? A ASP 378 5 1 Y 1 A ASP 379 ? A ASP 379 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 ALPHA-L-FUCOSE FUC 4 BETA-L-FUCOSE FUL 5 TACRINE THA 6 GLYCEROL GOL 7 'SULFATE ION' SO4 8 'CHLORIDE ION' CL 9 1-formyl-L-proline FPK 10 'UNKNOWN ATOM OR ION' UNX 11 water HOH #