data_2XQG # _entry.id 2XQG # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.279 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 2XQG PDBE EBI-45260 WWPDB D_1290045260 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.content_type _pdbx_database_related.details PDB 2WSL unspecified 'AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY TABUN ANALOGUE TA4' PDB 2XQK unspecified 'X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY PURE ENANTIOMER VX-(S)' PDB 2XMB unspecified 'G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH SULFATE' PDB 2J4C unspecified 'STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH 10MM HGCL2' PDB 2XMG unspecified 'G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH VX' PDB 2WIK unspecified 'NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY TABUN ANALOGUE TA6' PDB 1KCJ unspecified 'MODEL OF (-)-COCAINE-BOUND (-)-COCAINE HYDROLASE COMPLEX' PDB 1XLU unspecified 'X-RAY STRUCTURE OF DI-ISOPROPYL-PHOSPHORO- FLUORIDATE (DFP) INHIBITED BUTYRYLCHOLINESTERASE AFTER AGING' PDB 1P0P unspecified 'CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH THE SUBSTRATE ANALOGBUTYRYLTHIOCHOLINE' PDB 2WIJ unspecified 'NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY TABUN ANALOGUE TA5' PDB 2XMD unspecified 'G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH ECHOTHIOPHATE' PDB 1XLV unspecified 'ETHYLPHOSPHORYLATED BUTYRYLCHOLINESTERASE (AGED) OBTAINEDBY REACTION WITH ECHOTHIOPHATE' PDB 1EHO unspecified 'MODEL OF (-)-COCAINE-BOUND BCHE COMPLEX.' PDB 2XQJ unspecified 'X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY PURE ENANTIOMER VX-(R)' PDB 1P0M unspecified 'CRYSTAL STRUCTURE OF HUMAN BUTYRYL CHOLINESTERASE INCOMPLEX WITH A CHOLINE MOLECULE' PDB 1XLW unspecified 'DIETHYLPHOSPHORYLATED BUTYRYLCHOLINESTERASE (NONAGED ) OBTAINED BY REACTION WITH ECHOTHIOPHATE' PDB 1EHQ unspecified 'MODEL OF (+)-COCAINE-BOUND BCHE COMPLEX' PDB 1P0Q unspecified 'CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN BUTYRYL CHOLINESTERASE' PDB 2XMC unspecified 'G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH FLUORIDE ANION' PDB 2WID unspecified 'AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY TABUN ANALOGUE TA1' PDB 2XQF unspecified 'X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY RACEMIC VX' PDB 2WIL unspecified 'AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY TABUN ANALOGUE TA5' PDB 2WIF unspecified 'AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY TABUN ANALOGUE TA1' PDB 1P0I unspecified 'CRYSTAL STRUCTURE OF HUMAN BUTYRYL CHOLINESTERASE' PDB 2WIG unspecified 'NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY TABUN ANALOGUE TA4' PDB 2XQI unspecified 'X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY RACEMIC CVX' # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 2XQG _pdbx_database_status.deposit_site PDBE _pdbx_database_status.process_site PDBE _pdbx_database_status.SG_entry . _pdbx_database_status.recvd_initial_deposition_date 2010-09-02 _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 'Wandhammer, M.' 1 'Carletti, E.' 2 'Gillon, E.' 3 'Masson, P.' 4 'Goeldner, M.' 5 'Noort, D.' 6 'Nachon, F.' 7 # _citation.id primary _citation.title 'Structural Study of the Complex Stereoselectivity of Human Butyrylcholinesterase for the Neurotoxic V-Agents.' _citation.journal_abbrev J.Biol.Chem. _citation.journal_volume 286 _citation.page_first 16783 _citation.page_last ? _citation.year 2011 _citation.journal_id_ASTM JBCHA3 _citation.country US _citation.journal_id_ISSN 0021-9258 _citation.journal_id_CSD 0071 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 21454498 _citation.pdbx_database_id_DOI 10.1074/JBC.M110.209569 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Wandhammer, M.' 1 primary 'Carletti, E.' 2 primary 'Van Der Schans, M.' 3 primary 'Gillon, E.' 4 primary 'Nicolet, Y.' 5 primary 'Masson, P.' 6 primary 'Goeldner, M.' 7 primary 'Noort, D.' 8 primary 'Nachon, F.' 9 # _cell.entry_id 2XQG _cell.length_a 154.600 _cell.length_b 154.600 _cell.length_c 127.610 _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 2XQG _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 59469.309 1 3.1.1.8 YES 'RESIDUES 31-557' ? 2 non-polymer syn 'UNKNOWN ATOM OR ION' ? 23 ? ? ? ? 3 non-polymer syn '2-METHYLPROPYL HYDROGEN (R)-METHYLPHOSPHONATE' 152.129 1 ? ? ? ? 4 non-polymer syn GLYCINE 75.067 1 ? ? ? ? 5 non-polymer syn 'SULFATE ION' 96.063 2 ? ? ? ? 6 non-polymer syn 'CALCIUM ION' 40.078 3 ? ? ? ? 7 non-polymer syn 'BROMIDE ION' 79.904 1 ? ? ? ? 8 non-polymer syn 'SODIUM ION' 22.990 2 ? ? ? ? 9 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 8 ? ? ? ? 10 non-polymer man BETA-L-FUCOSE 164.156 2 ? ? ? ? 11 non-polymer syn 'CHLORIDE ION' 35.453 1 ? ? ? ? 12 water nat water 18.015 419 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'ACYLCHOLINE ACYLHYDROLASE, CHOLINE ESTERASE II, BUTYRYLCHOLINE ESTERASE, 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 ;DIIIATKNGKVRGMQLTVFGGTVTAFLGIPYAQPPLGRLRFKKPQSLTKWSDIWNATKYANSCCQNIDQSFPGFHGSEMW NPNTDLSEDCLYLNVWIPAPKPKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGALGFLALPGNPEA PGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAASVSLHLLSPGSHSLFTRAILQSGSFNAPWAVTSLYEARNR TLNLAKLTGCSRENETEIIKCLRNKDPQEILLNEAFVVPYGTPLSVNFGPTVDGDFLTDMPDILLELGQFKKTQILVGVN KDEGTAFLVYGAPGFSKDNNSIITRKEFQEGLKIFFPGVSEFGKESILFHYTDWVDDQRPENYREALGDVVGDYNFICPA LEFTKKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPLERRDQYTKAEEILSRSIVKRWANFAKYGNPQE TQNQSTSWPVFKSTEQKYLTLNTESTRIMTKLRAQQCRFWTSFFPKV ; _entity_poly.pdbx_seq_one_letter_code_can ;DIIIATKNGKVRGMQLTVFGGTVTAFLGIPYAQPPLGRLRFKKPQSLTKWSDIWNATKYANSCCQNIDQSFPGFHGSEMW NPNTDLSEDCLYLNVWIPAPKPKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGALGFLALPGNPEA PGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAASVSLHLLSPGSHSLFTRAILQSGSFNAPWAVTSLYEARNR TLNLAKLTGCSRENETEIIKCLRNKDPQEILLNEAFVVPYGTPLSVNFGPTVDGDFLTDMPDILLELGQFKKTQILVGVN KDEGTAFLVYGAPGFSKDNNSIITRKEFQEGLKIFFPGVSEFGKESILFHYTDWVDDQRPENYREALGDVVGDYNFICPA LEFTKKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPLERRDQYTKAEEILSRSIVKRWANFAKYGNPQE TQNQSTSWPVFKSTEQKYLTLNTESTRIMTKLRAQQCRFWTSFFPKV ; _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 ASP n 1 2 ILE n 1 3 ILE n 1 4 ILE n 1 5 ALA n 1 6 THR n 1 7 LYS n 1 8 ASN n 1 9 GLY n 1 10 LYS n 1 11 VAL n 1 12 ARG n 1 13 GLY n 1 14 MET n 1 15 GLN n 1 16 LEU n 1 17 THR n 1 18 VAL n 1 19 PHE n 1 20 GLY n 1 21 GLY n 1 22 THR n 1 23 VAL n 1 24 THR n 1 25 ALA n 1 26 PHE n 1 27 LEU n 1 28 GLY n 1 29 ILE n 1 30 PRO n 1 31 TYR n 1 32 ALA n 1 33 GLN n 1 34 PRO n 1 35 PRO n 1 36 LEU n 1 37 GLY n 1 38 ARG n 1 39 LEU n 1 40 ARG n 1 41 PHE n 1 42 LYS n 1 43 LYS n 1 44 PRO n 1 45 GLN n 1 46 SER n 1 47 LEU n 1 48 THR n 1 49 LYS n 1 50 TRP n 1 51 SER n 1 52 ASP n 1 53 ILE n 1 54 TRP n 1 55 ASN n 1 56 ALA n 1 57 THR n 1 58 LYS n 1 59 TYR n 1 60 ALA n 1 61 ASN n 1 62 SER n 1 63 CYS n 1 64 CYS n 1 65 GLN n 1 66 ASN n 1 67 ILE n 1 68 ASP n 1 69 GLN n 1 70 SER n 1 71 PHE n 1 72 PRO n 1 73 GLY n 1 74 PHE n 1 75 HIS n 1 76 GLY n 1 77 SER n 1 78 GLU n 1 79 MET n 1 80 TRP n 1 81 ASN n 1 82 PRO n 1 83 ASN n 1 84 THR n 1 85 ASP n 1 86 LEU n 1 87 SER n 1 88 GLU n 1 89 ASP n 1 90 CYS n 1 91 LEU n 1 92 TYR n 1 93 LEU n 1 94 ASN n 1 95 VAL n 1 96 TRP n 1 97 ILE n 1 98 PRO n 1 99 ALA n 1 100 PRO n 1 101 LYS n 1 102 PRO n 1 103 LYS n 1 104 ASN n 1 105 ALA n 1 106 THR n 1 107 VAL n 1 108 LEU n 1 109 ILE n 1 110 TRP n 1 111 ILE n 1 112 TYR n 1 113 GLY n 1 114 GLY n 1 115 GLY n 1 116 PHE n 1 117 GLN n 1 118 THR n 1 119 GLY n 1 120 THR n 1 121 SER n 1 122 SER n 1 123 LEU n 1 124 HIS n 1 125 VAL n 1 126 TYR n 1 127 ASP n 1 128 GLY n 1 129 LYS n 1 130 PHE n 1 131 LEU n 1 132 ALA n 1 133 ARG n 1 134 VAL n 1 135 GLU n 1 136 ARG n 1 137 VAL n 1 138 ILE n 1 139 VAL n 1 140 VAL n 1 141 SER n 1 142 MET n 1 143 ASN n 1 144 TYR n 1 145 ARG n 1 146 VAL n 1 147 GLY n 1 148 ALA n 1 149 LEU n 1 150 GLY n 1 151 PHE n 1 152 LEU n 1 153 ALA n 1 154 LEU n 1 155 PRO n 1 156 GLY n 1 157 ASN n 1 158 PRO n 1 159 GLU n 1 160 ALA n 1 161 PRO n 1 162 GLY n 1 163 ASN n 1 164 MET n 1 165 GLY n 1 166 LEU n 1 167 PHE n 1 168 ASP n 1 169 GLN n 1 170 GLN n 1 171 LEU n 1 172 ALA n 1 173 LEU n 1 174 GLN n 1 175 TRP n 1 176 VAL n 1 177 GLN n 1 178 LYS n 1 179 ASN n 1 180 ILE n 1 181 ALA n 1 182 ALA n 1 183 PHE n 1 184 GLY n 1 185 GLY n 1 186 ASN n 1 187 PRO n 1 188 LYS n 1 189 SER n 1 190 VAL n 1 191 THR n 1 192 LEU n 1 193 PHE n 1 194 GLY n 1 195 GLU n 1 196 SER n 1 197 ALA n 1 198 GLY n 1 199 ALA n 1 200 ALA n 1 201 SER n 1 202 VAL n 1 203 SER n 1 204 LEU n 1 205 HIS n 1 206 LEU n 1 207 LEU n 1 208 SER n 1 209 PRO n 1 210 GLY n 1 211 SER n 1 212 HIS n 1 213 SER n 1 214 LEU n 1 215 PHE n 1 216 THR n 1 217 ARG n 1 218 ALA n 1 219 ILE n 1 220 LEU n 1 221 GLN n 1 222 SER n 1 223 GLY n 1 224 SER n 1 225 PHE n 1 226 ASN n 1 227 ALA n 1 228 PRO n 1 229 TRP n 1 230 ALA n 1 231 VAL n 1 232 THR n 1 233 SER n 1 234 LEU n 1 235 TYR n 1 236 GLU n 1 237 ALA n 1 238 ARG n 1 239 ASN n 1 240 ARG n 1 241 THR n 1 242 LEU n 1 243 ASN n 1 244 LEU n 1 245 ALA n 1 246 LYS n 1 247 LEU n 1 248 THR n 1 249 GLY n 1 250 CYS n 1 251 SER n 1 252 ARG n 1 253 GLU n 1 254 ASN n 1 255 GLU n 1 256 THR n 1 257 GLU n 1 258 ILE n 1 259 ILE n 1 260 LYS n 1 261 CYS n 1 262 LEU n 1 263 ARG n 1 264 ASN n 1 265 LYS n 1 266 ASP n 1 267 PRO n 1 268 GLN n 1 269 GLU n 1 270 ILE n 1 271 LEU n 1 272 LEU n 1 273 ASN n 1 274 GLU n 1 275 ALA n 1 276 PHE n 1 277 VAL n 1 278 VAL n 1 279 PRO n 1 280 TYR n 1 281 GLY n 1 282 THR n 1 283 PRO n 1 284 LEU n 1 285 SER n 1 286 VAL n 1 287 ASN n 1 288 PHE n 1 289 GLY n 1 290 PRO n 1 291 THR n 1 292 VAL n 1 293 ASP n 1 294 GLY n 1 295 ASP n 1 296 PHE n 1 297 LEU n 1 298 THR n 1 299 ASP n 1 300 MET n 1 301 PRO n 1 302 ASP n 1 303 ILE n 1 304 LEU n 1 305 LEU n 1 306 GLU n 1 307 LEU n 1 308 GLY n 1 309 GLN n 1 310 PHE n 1 311 LYS n 1 312 LYS n 1 313 THR n 1 314 GLN n 1 315 ILE n 1 316 LEU n 1 317 VAL n 1 318 GLY n 1 319 VAL n 1 320 ASN n 1 321 LYS n 1 322 ASP n 1 323 GLU n 1 324 GLY n 1 325 THR n 1 326 ALA n 1 327 PHE n 1 328 LEU n 1 329 VAL n 1 330 TYR n 1 331 GLY n 1 332 ALA n 1 333 PRO n 1 334 GLY n 1 335 PHE n 1 336 SER n 1 337 LYS n 1 338 ASP n 1 339 ASN n 1 340 ASN n 1 341 SER n 1 342 ILE n 1 343 ILE n 1 344 THR n 1 345 ARG n 1 346 LYS n 1 347 GLU n 1 348 PHE n 1 349 GLN n 1 350 GLU n 1 351 GLY n 1 352 LEU n 1 353 LYS n 1 354 ILE n 1 355 PHE n 1 356 PHE n 1 357 PRO n 1 358 GLY n 1 359 VAL n 1 360 SER n 1 361 GLU n 1 362 PHE n 1 363 GLY n 1 364 LYS n 1 365 GLU n 1 366 SER n 1 367 ILE n 1 368 LEU n 1 369 PHE n 1 370 HIS n 1 371 TYR n 1 372 THR n 1 373 ASP n 1 374 TRP n 1 375 VAL n 1 376 ASP n 1 377 ASP n 1 378 GLN n 1 379 ARG n 1 380 PRO n 1 381 GLU n 1 382 ASN n 1 383 TYR n 1 384 ARG n 1 385 GLU n 1 386 ALA n 1 387 LEU n 1 388 GLY n 1 389 ASP n 1 390 VAL n 1 391 VAL n 1 392 GLY n 1 393 ASP n 1 394 TYR n 1 395 ASN n 1 396 PHE n 1 397 ILE n 1 398 CYS n 1 399 PRO n 1 400 ALA n 1 401 LEU n 1 402 GLU n 1 403 PHE n 1 404 THR n 1 405 LYS n 1 406 LYS n 1 407 PHE n 1 408 SER n 1 409 GLU n 1 410 TRP n 1 411 GLY n 1 412 ASN n 1 413 ASN n 1 414 ALA n 1 415 PHE n 1 416 PHE n 1 417 TYR n 1 418 TYR n 1 419 PHE n 1 420 GLU n 1 421 HIS n 1 422 ARG n 1 423 SER n 1 424 SER n 1 425 LYS n 1 426 LEU n 1 427 PRO n 1 428 TRP n 1 429 PRO n 1 430 GLU n 1 431 TRP n 1 432 MET n 1 433 GLY n 1 434 VAL n 1 435 MET n 1 436 HIS n 1 437 GLY n 1 438 TYR n 1 439 GLU n 1 440 ILE n 1 441 GLU n 1 442 PHE n 1 443 VAL n 1 444 PHE n 1 445 GLY n 1 446 LEU n 1 447 PRO n 1 448 LEU n 1 449 GLU n 1 450 ARG n 1 451 ARG n 1 452 ASP n 1 453 GLN n 1 454 TYR n 1 455 THR n 1 456 LYS n 1 457 ALA n 1 458 GLU n 1 459 GLU n 1 460 ILE n 1 461 LEU n 1 462 SER n 1 463 ARG n 1 464 SER n 1 465 ILE n 1 466 VAL n 1 467 LYS n 1 468 ARG n 1 469 TRP n 1 470 ALA n 1 471 ASN n 1 472 PHE n 1 473 ALA n 1 474 LYS n 1 475 TYR n 1 476 GLY n 1 477 ASN n 1 478 PRO n 1 479 GLN n 1 480 GLU n 1 481 THR n 1 482 GLN n 1 483 ASN n 1 484 GLN n 1 485 SER n 1 486 THR n 1 487 SER n 1 488 TRP n 1 489 PRO n 1 490 VAL n 1 491 PHE n 1 492 LYS n 1 493 SER n 1 494 THR n 1 495 GLU n 1 496 GLN n 1 497 LYS n 1 498 TYR n 1 499 LEU n 1 500 THR n 1 501 LEU n 1 502 ASN n 1 503 THR n 1 504 GLU n 1 505 SER n 1 506 THR n 1 507 ARG n 1 508 ILE n 1 509 MET n 1 510 THR n 1 511 LYS n 1 512 LEU n 1 513 ARG n 1 514 ALA n 1 515 GLN n 1 516 GLN n 1 517 CYS n 1 518 ARG n 1 519 PHE n 1 520 TRP n 1 521 THR n 1 522 SER n 1 523 PHE n 1 524 PHE n 1 525 PRO n 1 526 LYS n 1 527 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 ? _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 2XQG _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 527 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession P06276 _struct_ref_seq.db_align_beg 31 _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 3 _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 2XQG GLN A 15 ? UNP P06276 ASN 45 'engineered mutation' 17 1 1 2XQG GLN A 453 ? UNP P06276 ASN 483 'engineered mutation' 455 2 1 2XQG GLN A 479 ? UNP P06276 ASN 509 'engineered mutation' 481 3 1 2XQG GLN A 484 ? 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 BR non-polymer . 'BROMIDE ION' ? 'Br -1' 79.904 CA non-polymer . 'CALCIUM ION' ? 'Ca 2' 40.078 CL non-polymer . 'CHLORIDE ION' ? 'Cl -1' 35.453 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 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 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 NA non-polymer . 'SODIUM ION' ? 'Na 1' 22.990 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 SO4 non-polymer . 'SULFATE ION' ? 'O4 S -2' 96.063 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 VR non-polymer . '2-METHYLPROPYL HYDROGEN (R)-METHYLPHOSPHONATE' ? 'C5 H13 O3 P' 152.129 # _exptl.entry_id 2XQG _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.8 _exptl_crystal.density_percent_sol 5 _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 'AMMONIUM SULFATE 2.1, M 2-(N -MORPHOLINO)-ETHANESULFONIC ACID 0.1 M, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298.0K .' # _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 CCD' _diffrn_detector.pdbx_collection_date 2009-10-04 _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 0.933 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'ESRF BEAMLINE ID14-1' _diffrn_source.pdbx_synchrotron_site ESRF _diffrn_source.pdbx_synchrotron_beamline ID14-1 _diffrn_source.pdbx_wavelength 0.933 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 2XQG _reflns.observed_criterion_sigma_I -3.0 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 41.50 _reflns.d_resolution_high 2.30 _reflns.number_obs 34420 _reflns.number_all ? _reflns.percent_possible_obs 99.7 _reflns.pdbx_Rmerge_I_obs 0.07 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 27.30 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 7.3 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 2.30 _reflns_shell.d_res_low 2.50 _reflns_shell.percent_possible_all 99.6 _reflns_shell.Rmerge_I_obs 0.45 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 4.80 _reflns_shell.pdbx_redundancy 7.4 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 2XQG _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 33383 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F . _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 41.51 _refine.ls_d_res_high 2.30 _refine.ls_percent_reflns_obs 99.77 _refine.ls_R_factor_obs 0.16364 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.16207 _refine.ls_R_factor_R_free 0.21461 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 3.0 _refine.ls_number_reflns_R_free 1036 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.963 _refine.correlation_coeff_Fo_to_Fc_free 0.937 _refine.B_iso_mean 38.092 _refine.aniso_B[1][1] 0.34 _refine.aniso_B[2][2] 0.34 _refine.aniso_B[3][3] -0.68 _refine.aniso_B[1][2] 0.00 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details MASK _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.40 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.' _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 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.222 _refine.pdbx_overall_ESU_R_Free 0.190 _refine.overall_SU_ML 0.131 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 11.815 _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 4203 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 185 _refine_hist.number_atoms_solvent 419 _refine_hist.number_atoms_total 4807 _refine_hist.d_res_high 2.30 _refine_hist.d_res_low 41.51 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function r_bond_refined_d 0.023 0.022 ? 4547 'X-RAY DIFFRACTION' ? r_bond_other_d ? ? ? ? 'X-RAY DIFFRACTION' ? r_angle_refined_deg 2.051 1.982 ? 6202 'X-RAY DIFFRACTION' ? r_angle_other_deg ? ? ? ? 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 7.417 5.000 ? 543 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 36.771 24.211 ? 209 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 17.120 15.000 ? 718 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 19.721 15.000 ? 22 'X-RAY DIFFRACTION' ? r_chiral_restr 0.144 0.200 ? 675 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.011 0.021 ? 3483 'X-RAY DIFFRACTION' ? r_gen_planes_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcbond_it 1.084 1.500 ? 2655 'X-RAY DIFFRACTION' ? r_mcbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_it 1.903 2.000 ? 4295 'X-RAY DIFFRACTION' ? r_mcangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_it 3.385 3.000 ? 1892 'X-RAY DIFFRACTION' ? r_scbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_it 5.332 4.500 ? 1899 'X-RAY DIFFRACTION' ? r_scangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_rigid_bond_restr ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_free ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_bonded ? ? ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 2.300 _refine_ls_shell.d_res_low 2.360 _refine_ls_shell.number_reflns_R_work 2390 _refine_ls_shell.R_factor_R_work 0.217 _refine_ls_shell.percent_reflns_obs 99.24 _refine_ls_shell.R_factor_R_free 0.270 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 79 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? # _struct.entry_id 2XQG _struct.title 'X-ray Structure of human butyrylcholinesterase inhibited by racemic VR' _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 2XQG _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text 'HYDROLASE, NERVE AGENT, BIOSCAVENGER' # 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 2 ? E N N 2 ? F N N 2 ? G N N 2 ? H N N 2 ? I N N 2 ? J N N 2 ? K N N 2 ? L N N 2 ? M N N 2 ? N N N 2 ? O N N 2 ? P N N 2 ? Q N N 2 ? R N N 2 ? S N N 2 ? T N N 2 ? U N N 2 ? V N N 2 ? W N N 2 ? X N N 2 ? Y N N 3 ? Z N N 4 ? AA N N 5 ? BA N N 5 ? CA N N 6 ? DA N N 6 ? EA N N 6 ? FA N N 7 ? GA N N 8 ? HA N N 9 ? IA N N 9 ? JA N N 10 ? KA N N 9 ? LA N N 9 ? MA N N 9 ? NA N N 9 ? OA N N 9 ? PA N N 9 ? QA N N 10 ? RA N N 11 ? SA N N 8 ? TA N N 12 ? # _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 36 ? ARG A 40 ? LEU A 38 ARG A 42 5 ? 5 HELX_P HELX_P2 2 PHE A 74 ? MET A 79 ? PHE A 76 MET A 81 1 ? 6 HELX_P HELX_P3 3 LEU A 123 ? ASP A 127 ? LEU A 125 ASP A 129 5 ? 5 HELX_P HELX_P4 4 GLY A 128 ? ARG A 136 ? GLY A 130 ARG A 138 1 ? 9 HELX_P HELX_P5 5 VAL A 146 ? LEU A 152 ? VAL A 148 LEU A 154 1 ? 7 HELX_P HELX_P6 6 ASN A 163 ? ILE A 180 ? ASN A 165 ILE A 182 1 ? 18 HELX_P HELX_P7 7 ALA A 181 ? PHE A 183 ? ALA A 183 PHE A 185 5 ? 3 HELX_P HELX_P8 8 SER A 196 ? SER A 208 ? SER A 198 SER A 210 1 ? 13 HELX_P HELX_P9 9 PRO A 209 ? PHE A 215 ? PRO A 211 PHE A 217 5 ? 7 HELX_P HELX_P10 10 SER A 233 ? GLY A 249 ? SER A 235 GLY A 251 1 ? 17 HELX_P HELX_P11 11 ASN A 254 ? LYS A 265 ? ASN A 256 LYS A 267 1 ? 12 HELX_P HELX_P12 12 ASP A 266 ? GLU A 274 ? ASP A 268 GLU A 276 1 ? 9 HELX_P HELX_P13 13 ALA A 275 ? VAL A 278 ? ALA A 277 VAL A 280 5 ? 4 HELX_P HELX_P14 14 MET A 300 ? LEU A 307 ? MET A 302 LEU A 309 1 ? 8 HELX_P HELX_P15 15 GLY A 324 ? GLY A 331 ? GLY A 326 GLY A 333 5 ? 8 HELX_P HELX_P16 16 THR A 344 ? PHE A 356 ? THR A 346 PHE A 358 1 ? 13 HELX_P HELX_P17 17 SER A 360 ? THR A 372 ? SER A 362 THR A 374 1 ? 13 HELX_P HELX_P18 18 GLU A 381 ? PHE A 396 ? GLU A 383 PHE A 398 1 ? 16 HELX_P HELX_P19 19 PHE A 396 ? GLU A 409 ? PHE A 398 GLU A 411 1 ? 14 HELX_P HELX_P20 20 PRO A 429 ? GLY A 433 ? PRO A 431 GLY A 435 5 ? 5 HELX_P HELX_P21 21 GLU A 439 ? PHE A 444 ? GLU A 441 PHE A 446 1 ? 6 HELX_P HELX_P22 22 GLY A 445 ? GLU A 449 ? GLY A 447 GLU A 451 5 ? 5 HELX_P HELX_P23 23 GLU A 449 ? GLN A 453 ? GLU A 451 GLN A 455 5 ? 5 HELX_P HELX_P24 24 THR A 455 ? GLY A 476 ? THR A 457 GLY A 478 1 ? 22 HELX_P HELX_P25 25 ARG A 513 ? PHE A 523 ? ARG A 515 PHE A 525 1 ? 11 HELX_P HELX_P26 26 PHE A 524 ? VAL A 527 ? 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 63 SG ? ? ? 1_555 A CYS 90 SG ? ? A CYS 65 A CYS 92 1_555 ? ? ? ? ? ? ? 2.041 ? disulf2 disulf ? ? A CYS 250 SG ? ? ? 1_555 A CYS 261 SG ? ? A CYS 252 A CYS 263 1_555 ? ? ? ? ? ? ? 2.043 ? disulf3 disulf ? ? A CYS 398 SG ? ? ? 1_555 A CYS 517 SG ? ? A CYS 400 A CYS 519 1_555 ? ? ? ? ? ? ? 2.049 ? covale1 covale ? ? A ASN 55 ND2 ? ? ? 1_555 LA NAG . C1 ? ? A ASN 57 A NAG 1560 1_555 ? ? ? ? ? ? ? 1.458 ? covale2 covale ? ? A ASN 104 ND2 ? ? ? 1_555 KA NAG . C1 ? ? A ASN 106 A NAG 1559 1_555 ? ? ? ? ? ? ? 1.437 ? covale3 covale ? ? A SER 196 OG ? ? ? 1_555 Y VR . P1 ? ? A SER 198 A VR 1530 1_555 ? ? ? ? ? ? ? 1.673 ? covale4 covale ? ? A ASN 239 ND2 ? ? ? 1_555 OA NAG . C1 ? ? A ASN 241 A NAG 1563 1_555 ? ? ? ? ? ? ? 1.467 ? covale5 covale ? ? A ASN 254 ND2 ? ? ? 1_555 NA NAG . C1 ? ? A ASN 256 A NAG 1562 1_555 ? ? ? ? ? ? ? 1.456 ? covale6 covale ? ? A ASN 339 ND2 ? ? ? 1_555 HA NAG . C1 ? ? A ASN 341 A NAG 1556 1_555 ? ? ? ? ? ? ? 1.442 ? covale7 covale ? ? A ASN 483 ND2 ? ? ? 1_555 MA NAG . C1 ? ? A ASN 485 A NAG 1561 1_555 ? ? ? ? ? ? ? 1.454 ? metalc1 metalc ? ? CA CA . CA ? ? ? 1_555 TA HOH . O ? ? A CA 1551 A HOH 2040 1_555 ? ? ? ? ? ? ? 2.180 ? metalc2 metalc ? ? CA CA . CA ? ? ? 1_555 TA HOH . O ? ? A CA 1551 A HOH 2179 1_555 ? ? ? ? ? ? ? 2.829 ? metalc3 metalc ? ? DA CA . CA ? ? ? 1_555 TA HOH . O ? ? A CA 1552 A HOH 2355 1_555 ? ? ? ? ? ? ? 2.869 ? metalc4 metalc ? ? EA CA . CA ? ? ? 1_555 TA HOH . O ? ? A CA 1553 A HOH 2393 7_555 ? ? ? ? ? ? ? 3.150 ? metalc5 metalc ? ? EA CA . CA ? ? ? 1_555 A TYR 418 OH ? ? A CA 1553 A TYR 420 1_555 ? ? ? ? ? ? ? 3.172 ? covale8 covale ? ? HA NAG . O6 ? ? ? 1_555 JA FUL . C1 ? ? A NAG 1556 A FUL 1558 1_555 ? ? ? ? ? ? ? 1.454 ? covale9 covale ? ? HA NAG . O4 ? ? ? 1_555 IA NAG . C1 ? ? A NAG 1556 A NAG 1557 1_555 ? ? ? ? ? ? ? 1.446 ? covale10 covale ? ? OA NAG . O6 ? ? ? 1_555 QA FUL . C1 ? ? A NAG 1563 A FUL 1565 1_555 ? ? ? ? ? ? ? 1.446 ? covale11 covale ? ? OA NAG . O4 ? ? ? 1_555 PA NAG . C1 ? ? A NAG 1563 A NAG 1564 1_555 ? ? ? ? ? ? ? 1.459 ? metalc6 metalc ? ? SA NA . NA ? ? ? 1_555 TA HOH . O ? ? A NA 1567 A HOH 2290 1_555 ? ? ? ? ? ? ? 3.155 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? metalc ? ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 ALA 99 A . ? ALA 101 A PRO 100 A ? PRO 102 A 1 -1.97 2 TRP 374 A . ? TRP 376 A VAL 375 A ? VAL 377 A 1 7.26 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA ? 3 ? AB ? 11 ? # 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 # 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 3 ? THR A 6 ? ILE A 5 THR A 8 AA 2 GLY A 9 ? ARG A 12 ? GLY A 11 ARG A 14 AA 3 ILE A 53 ? ASN A 55 ? ILE A 55 ASN A 57 AB 1 MET A 14 ? VAL A 18 ? MET A 16 VAL A 20 AB 2 GLY A 21 ? PRO A 30 ? GLY A 23 PRO A 32 AB 3 TYR A 92 ? PRO A 98 ? TYR A 94 PRO A 100 AB 4 ILE A 138 ? MET A 142 ? ILE A 140 MET A 144 AB 5 ALA A 105 ? ILE A 111 ? ALA A 107 ILE A 113 AB 6 GLY A 185 ? GLU A 195 ? GLY A 187 GLU A 197 AB 7 ARG A 217 ? GLN A 221 ? ARG A 219 GLN A 223 AB 8 ILE A 315 ? ASN A 320 ? ILE A 317 ASN A 322 AB 9 ALA A 414 ? PHE A 419 ? ALA A 416 PHE A 421 AB 10 LYS A 497 ? LEU A 501 ? LYS A 499 LEU A 503 AB 11 ILE A 508 ? THR A 510 ? ILE A 510 THR A 512 # 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 6 ? N THR A 8 O GLY A 9 ? O GLY A 11 AA 2 3 N ARG A 12 ? N ARG A 14 O TRP A 54 ? O TRP A 56 AB 1 2 N VAL A 18 ? N VAL A 20 O GLY A 21 ? O GLY A 23 AB 2 3 N ILE A 29 ? N ILE A 31 O LEU A 93 ? O LEU A 95 AB 3 4 N TRP A 96 ? N TRP A 98 O VAL A 139 ? O VAL A 141 AB 4 5 N ILE A 138 ? N ILE A 140 O THR A 106 ? O THR A 108 AB 5 6 O ALA A 105 ? O ALA A 107 N ASN A 186 ? N ASN A 188 AB 6 7 N LEU A 192 ? N LEU A 194 O ARG A 217 ? O ARG A 219 AB 7 8 N LEU A 220 ? N LEU A 222 O LEU A 316 ? O LEU A 318 AB 8 9 N VAL A 317 ? N VAL A 319 O PHE A 415 ? O PHE A 417 AB 9 10 N TYR A 418 ? N TYR A 420 O LEU A 499 ? O LEU A 501 AB 10 11 N TYR A 498 ? N TYR A 500 O MET A 509 ? O MET A 511 # 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 ? ? ? ? 8 'BINDING SITE FOR RESIDUE VR A 1530' AC2 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE GLY A 1548' AC3 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE SO4 A 1549' AC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE SO4 A 1550' AC5 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE CL A 1566' AC6 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE CA A 1551' AC7 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE CA A 1552' AC8 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE CA A 1553' AC9 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE BR A 1554' BC1 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NA A 1567' BC2 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NA A 1555' BC3 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 1559' BC4 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 1560' BC5 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 1561' BC6 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 1562' BC7 Software ? ? ? ? 8 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 241 RESIDUES 1563 TO 1565' BC8 Software ? ? ? ? 7 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 341 RESIDUES 1556 TO 1558' # 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 8 GLY A 114 ? GLY A 116 . ? 1_555 ? 2 AC1 8 GLY A 115 ? GLY A 117 . ? 1_555 ? 3 AC1 8 SER A 196 ? SER A 198 . ? 1_555 ? 4 AC1 8 ALA A 197 ? ALA A 199 . ? 1_555 ? 5 AC1 8 TRP A 229 ? TRP A 231 . ? 1_555 ? 6 AC1 8 LEU A 284 ? LEU A 286 . ? 1_555 ? 7 AC1 8 VAL A 286 ? VAL A 288 . ? 1_555 ? 8 AC1 8 HIS A 436 ? HIS A 438 . ? 1_555 ? 9 AC2 5 LEU A 16 ? LEU A 18 . ? 1_555 ? 10 AC2 5 TYR A 59 ? TYR A 61 . ? 1_555 ? 11 AC2 5 TRP A 96 ? TRP A 98 . ? 1_555 ? 12 AC2 5 ASP A 127 ? ASP A 129 . ? 1_555 ? 13 AC2 5 LYS A 129 ? LYS A 131 . ? 1_555 ? 14 AC3 3 GLN A 314 ? GLN A 316 . ? 1_555 ? 15 AC3 3 ASN A 412 ? ASN A 414 . ? 1_555 ? 16 AC3 3 ASN A 413 ? ASN A 415 . ? 1_555 ? 17 AC4 4 HIS A 370 ? HIS A 372 . ? 1_555 ? 18 AC4 4 PHE A 519 ? PHE A 521 . ? 1_555 ? 19 AC4 4 PHE A 523 ? PHE A 525 . ? 5_555 ? 20 AC4 4 HOH TA . ? HOH A 2413 . ? 1_555 ? 21 AC5 2 THR A 510 ? THR A 512 . ? 7_555 ? 22 AC5 2 HOH TA . ? HOH A 2381 . ? 7_555 ? 23 AC6 2 HOH TA . ? HOH A 2040 . ? 1_555 ? 24 AC6 2 HOH TA . ? HOH A 2179 . ? 1_555 ? 25 AC7 2 THR A 506 ? THR A 508 . ? 1_555 ? 26 AC7 2 HOH TA . ? HOH A 2355 . ? 1_555 ? 27 AC8 1 TYR A 418 ? TYR A 420 . ? 1_555 ? 28 AC9 2 ARG A 345 ? ARG A 347 . ? 1_555 ? 29 AC9 2 GLN A 349 ? GLN A 351 . ? 1_555 ? 30 BC1 1 TYR A 383 ? TYR A 385 . ? 1_555 ? 31 BC2 2 PHE A 523 ? PHE A 525 . ? 1_555 ? 32 BC2 2 PHE A 523 ? PHE A 525 . ? 5_555 ? 33 BC3 5 ASN A 104 ? ASN A 106 . ? 1_555 ? 34 BC3 5 ASN A 186 ? ASN A 188 . ? 1_555 ? 35 BC3 5 LYS A 188 ? LYS A 190 . ? 1_555 ? 36 BC3 5 HOH TA . ? HOH A 2416 . ? 1_555 ? 37 BC3 5 HOH TA . ? HOH A 2417 . ? 1_555 ? 38 BC4 2 ASN A 55 ? ASN A 57 . ? 1_555 ? 39 BC4 2 HOH TA . ? HOH A 2050 . ? 1_555 ? 40 BC5 2 ARG A 463 ? ARG A 465 . ? 1_555 ? 41 BC5 2 ASN A 483 ? ASN A 485 . ? 1_555 ? 42 BC6 2 ASN A 254 ? ASN A 256 . ? 1_555 ? 43 BC6 2 HOH TA . ? HOH A 2419 . ? 1_555 ? 44 BC7 8 TYR A 235 ? TYR A 237 . ? 1_555 ? 45 BC7 8 GLU A 236 ? GLU A 238 . ? 1_555 ? 46 BC7 8 ASN A 239 ? ASN A 241 . ? 1_555 ? 47 BC7 8 ASN A 243 ? ASN A 245 . ? 1_555 ? 48 BC7 8 PHE A 276 ? PHE A 278 . ? 1_555 ? 49 BC7 8 VAL A 278 ? VAL A 280 . ? 1_555 ? 50 BC7 8 PRO A 279 ? PRO A 281 . ? 1_555 ? 51 BC7 8 HOH TA . ? HOH A 2200 . ? 1_555 ? 52 BC8 7 PRO A 333 ? PRO A 335 . ? 1_555 ? 53 BC8 7 GLY A 334 ? GLY A 336 . ? 1_555 ? 54 BC8 7 SER A 336 ? SER A 338 . ? 1_555 ? 55 BC8 7 ASN A 339 ? ASN A 341 . ? 1_555 ? 56 BC8 7 ASN A 340 ? ASN A 342 . ? 1_555 ? 57 BC8 7 HOH TA . ? HOH A 2414 . ? 1_555 ? 58 BC8 7 HOH TA . ? HOH A 2415 . ? 1_555 ? # _database_PDB_matrix.entry_id 2XQG _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 2XQG _atom_sites.fract_transf_matrix[1][1] 0.006468 _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] 0.006468 _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] 0.007836 _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 BR C CA CL N NA O P 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 . ASP A 1 1 ? -37.922 -17.858 -49.354 1.00 78.88 ? 3 ASP A N 1 ATOM 2 C CA . ASP A 1 1 ? -36.728 -18.629 -49.854 1.00 77.13 ? 3 ASP A CA 1 ATOM 3 C C . ASP A 1 1 ? -35.431 -17.858 -49.568 1.00 74.88 ? 3 ASP A C 1 ATOM 4 O O . ASP A 1 1 ? -35.167 -16.808 -50.178 1.00 76.70 ? 3 ASP A O 1 ATOM 5 C CB . ASP A 1 1 ? -36.856 -18.926 -51.359 1.00 79.78 ? 3 ASP A CB 1 ATOM 6 C CG . ASP A 1 1 ? -35.782 -19.896 -51.880 1.00 79.90 ? 3 ASP A CG 1 ATOM 7 O OD1 . ASP A 1 1 ? -35.092 -20.583 -51.076 1.00 80.31 ? 3 ASP A OD1 1 ATOM 8 O OD2 . ASP A 1 1 ? -35.638 -19.980 -53.118 1.00 82.61 ? 3 ASP A OD2 1 ATOM 9 N N . ILE A 1 2 ? -34.621 -18.377 -48.656 1.00 70.24 ? 4 ILE A N 1 ATOM 10 C CA . ILE A 1 2 ? -33.461 -17.609 -48.174 1.00 67.67 ? 4 ILE A CA 1 ATOM 11 C C . ILE A 1 2 ? -32.113 -18.198 -48.656 1.00 63.85 ? 4 ILE A C 1 ATOM 12 O O . ILE A 1 2 ? -31.733 -19.287 -48.217 1.00 61.19 ? 4 ILE A O 1 ATOM 13 C CB . ILE A 1 2 ? -33.486 -17.454 -46.625 1.00 66.74 ? 4 ILE A CB 1 ATOM 14 C CG1 . ILE A 1 2 ? -34.703 -18.179 -46.012 1.00 68.02 ? 4 ILE A CG1 1 ATOM 15 C CG2 . ILE A 1 2 ? -33.526 -15.931 -46.238 1.00 68.38 ? 4 ILE A CG2 1 ATOM 16 C CD1 . ILE A 1 2 ? -35.143 -19.542 -46.653 1.00 68.42 ? 4 ILE A CD1 1 ATOM 17 N N . ILE A 1 3 ? -31.435 -17.475 -49.571 1.00 61.81 ? 5 ILE A N 1 ATOM 18 C CA . ILE A 1 3 ? -30.190 -17.918 -50.224 1.00 58.50 ? 5 ILE A CA 1 ATOM 19 C C . ILE A 1 3 ? -29.003 -17.003 -49.871 1.00 57.11 ? 5 ILE A C 1 ATOM 20 O O . ILE A 1 3 ? -29.082 -15.786 -50.023 1.00 57.50 ? 5 ILE A O 1 ATOM 21 C CB . ILE A 1 3 ? -30.363 -18.012 -51.750 1.00 60.19 ? 5 ILE A CB 1 ATOM 22 C CG1 . ILE A 1 3 ? -31.200 -19.243 -52.099 1.00 61.41 ? 5 ILE A CG1 1 ATOM 23 C CG2 . ILE A 1 3 ? -29.033 -18.115 -52.476 1.00 58.06 ? 5 ILE A CG2 1 ATOM 24 C CD1 . ILE A 1 3 ? -31.930 -19.125 -53.450 1.00 64.08 ? 5 ILE A CD1 1 ATOM 25 N N . ILE A 1 4 ? -27.904 -17.606 -49.405 1.00 53.52 ? 6 ILE A N 1 ATOM 26 C CA . ILE A 1 4 ? -26.718 -16.848 -49.041 1.00 51.51 ? 6 ILE A CA 1 ATOM 27 C C . ILE A 1 4 ? -25.544 -17.175 -49.964 1.00 52.22 ? 6 ILE A C 1 ATOM 28 O O . ILE A 1 4 ? -25.260 -18.332 -50.194 1.00 51.86 ? 6 ILE A O 1 ATOM 29 C CB . ILE A 1 4 ? -26.356 -17.079 -47.558 1.00 48.50 ? 6 ILE A CB 1 ATOM 30 C CG1 . ILE A 1 4 ? -27.483 -16.611 -46.626 1.00 47.24 ? 6 ILE A CG1 1 ATOM 31 C CG2 . ILE A 1 4 ? -25.046 -16.368 -47.174 1.00 47.42 ? 6 ILE A CG2 1 ATOM 32 C CD1 . ILE A 1 4 ? -27.888 -15.141 -46.785 1.00 48.04 ? 6 ILE A CD1 1 ATOM 33 N N . ALA A 1 5 ? -24.879 -16.157 -50.513 1.00 54.01 ? 7 ALA A N 1 ATOM 34 C CA . ALA A 1 5 ? -23.666 -16.338 -51.319 1.00 54.91 ? 7 ALA A CA 1 ATOM 35 C C . ALA A 1 5 ? -22.458 -16.501 -50.412 1.00 53.46 ? 7 ALA A C 1 ATOM 36 O O . ALA A 1 5 ? -22.146 -15.578 -49.678 1.00 53.84 ? 7 ALA A O 1 ATOM 37 C CB . ALA A 1 5 ? -23.460 -15.131 -52.243 1.00 56.99 ? 7 ALA A CB 1 ATOM 38 N N . THR A 1 6 ? -21.785 -17.660 -50.446 1.00 52.77 ? 8 THR A N 1 ATOM 39 C CA . THR A 1 6 ? -20.553 -17.863 -49.659 1.00 51.86 ? 8 THR A CA 1 ATOM 40 C C . THR A 1 6 ? -19.340 -17.784 -50.570 1.00 53.68 ? 8 THR A C 1 ATOM 41 O O . THR A 1 6 ? -19.519 -17.659 -51.776 1.00 55.11 ? 8 THR A O 1 ATOM 42 C CB . THR A 1 6 ? -20.547 -19.187 -48.861 1.00 49.84 ? 8 THR A CB 1 ATOM 43 O OG1 . THR A 1 6 ? -20.248 -20.319 -49.712 1.00 51.20 ? 8 THR A OG1 1 ATOM 44 C CG2 . THR A 1 6 ? -21.877 -19.380 -48.184 1.00 50.04 ? 8 THR A CG2 1 ATOM 45 N N . LYS A 1 7 ? -18.119 -17.846 -50.019 1.00 53.06 ? 9 LYS A N 1 ATOM 46 C CA . LYS A 1 7 ? -16.904 -17.852 -50.857 1.00 54.97 ? 9 LYS A CA 1 ATOM 47 C C . LYS A 1 7 ? -16.861 -19.045 -51.810 1.00 55.63 ? 9 LYS A C 1 ATOM 48 O O . LYS A 1 7 ? -16.296 -18.938 -52.886 1.00 57.39 ? 9 LYS A O 1 ATOM 49 C CB . LYS A 1 7 ? -15.608 -17.799 -50.029 1.00 54.90 ? 9 LYS A CB 1 ATOM 50 C CG . LYS A 1 7 ? -15.351 -16.468 -49.260 1.00 56.80 ? 9 LYS A CG 1 ATOM 51 C CD . LYS A 1 7 ? -15.255 -15.306 -50.195 1.00 63.41 ? 9 LYS A CD 1 ATOM 52 C CE . LYS A 1 7 ? -16.104 -14.107 -49.692 1.00 68.98 ? 9 LYS A CE 1 ATOM 53 N NZ . LYS A 1 7 ? -15.659 -13.688 -48.319 1.00 71.02 ? 9 LYS A NZ 1 ATOM 54 N N . ASN A 1 8 ? -17.478 -20.166 -51.428 1.00 53.81 ? 10 ASN A N 1 ATOM 55 C CA . ASN A 1 8 ? -17.501 -21.367 -52.276 1.00 55.02 ? 10 ASN A CA 1 ATOM 56 C C . ASN A 1 8 ? -18.776 -21.570 -53.108 1.00 54.75 ? 10 ASN A C 1 ATOM 57 O O . ASN A 1 8 ? -18.834 -22.477 -53.933 1.00 55.57 ? 10 ASN A O 1 ATOM 58 C CB . ASN A 1 8 ? -17.224 -22.624 -51.433 1.00 54.41 ? 10 ASN A CB 1 ATOM 59 C CG . ASN A 1 8 ? -15.962 -22.476 -50.584 1.00 57.78 ? 10 ASN A CG 1 ATOM 60 O OD1 . ASN A 1 8 ? -14.901 -23.001 -50.956 1.00 63.78 ? 10 ASN A OD1 1 ATOM 61 N ND2 . ASN A 1 8 ? -16.059 -21.720 -49.455 1.00 57.79 ? 10 ASN A ND2 1 ATOM 62 N N . GLY A 1 9 ? -19.790 -20.732 -52.910 1.00 53.42 ? 11 GLY A N 1 ATOM 63 C CA . GLY A 1 9 ? -20.982 -20.820 -53.736 1.00 53.10 ? 11 GLY A CA 1 ATOM 64 C C . GLY A 1 9 ? -22.228 -20.572 -52.926 1.00 51.72 ? 11 GLY A C 1 ATOM 65 O O . GLY A 1 9 ? -22.140 -20.336 -51.710 1.00 48.93 ? 11 GLY A O 1 ATOM 66 N N . LYS A 1 10 ? -23.386 -20.613 -53.604 1.00 52.30 ? 12 LYS A N 1 ATOM 67 C CA . LYS A 1 10 ? -24.683 -20.348 -52.967 1.00 51.96 ? 12 LYS A CA 1 ATOM 68 C C . LYS A 1 10 ? -25.170 -21.490 -52.049 1.00 49.84 ? 12 LYS A C 1 ATOM 69 O O . LYS A 1 10 ? -24.937 -22.683 -52.320 1.00 49.49 ? 12 LYS A O 1 ATOM 70 C CB . LYS A 1 10 ? -25.740 -20.042 -54.035 1.00 54.24 ? 12 LYS A CB 1 ATOM 71 C CG . LYS A 1 10 ? -25.366 -18.850 -54.893 1.00 59.27 ? 12 LYS A CG 1 ATOM 72 C CD . LYS A 1 10 ? -26.512 -18.425 -55.811 1.00 63.69 ? 12 LYS A CD 1 ATOM 73 C CE . LYS A 1 10 ? -26.381 -16.964 -56.222 1.00 67.53 ? 12 LYS A CE 1 ATOM 74 N NZ . LYS A 1 10 ? -27.426 -16.629 -57.241 1.00 70.44 ? 12 LYS A NZ 1 ATOM 75 N N . VAL A 1 11 ? -25.837 -21.124 -50.963 1.00 48.18 ? 13 VAL A N 1 ATOM 76 C CA . VAL A 1 11 ? -26.491 -22.109 -50.114 1.00 47.59 ? 13 VAL A CA 1 ATOM 77 C C . VAL A 1 11 ? -27.936 -21.691 -49.811 1.00 47.96 ? 13 VAL A C 1 ATOM 78 O O . VAL A 1 11 ? -28.205 -20.555 -49.449 1.00 49.15 ? 13 VAL A O 1 ATOM 79 C CB . VAL A 1 11 ? -25.690 -22.461 -48.793 1.00 44.75 ? 13 VAL A CB 1 ATOM 80 C CG1 . VAL A 1 11 ? -24.248 -22.769 -49.090 1.00 47.12 ? 13 VAL A CG1 1 ATOM 81 C CG2 . VAL A 1 11 ? -25.724 -21.348 -47.833 1.00 45.34 ? 13 VAL A CG2 1 ATOM 82 N N . ARG A 1 12 ? -28.868 -22.614 -49.982 1.00 48.32 ? 14 ARG A N 1 ATOM 83 C CA . ARG A 1 12 ? -30.270 -22.398 -49.590 1.00 48.16 ? 14 ARG A CA 1 ATOM 84 C C . ARG A 1 12 ? -30.501 -22.965 -48.176 1.00 45.65 ? 14 ARG A C 1 ATOM 85 O O . ARG A 1 12 ? -30.070 -24.093 -47.865 1.00 44.46 ? 14 ARG A O 1 ATOM 86 C CB . ARG A 1 12 ? -31.170 -23.103 -50.599 1.00 49.19 ? 14 ARG A CB 1 ATOM 87 C CG . ARG A 1 12 ? -32.543 -23.459 -50.094 1.00 51.55 ? 14 ARG A CG 1 ATOM 88 C CD . ARG A 1 12 ? -33.440 -23.976 -51.234 1.00 56.83 ? 14 ARG A CD 1 ATOM 89 N NE . ARG A 1 12 ? -33.787 -22.929 -52.210 1.00 61.82 ? 14 ARG A NE 1 ATOM 90 C CZ . ARG A 1 12 ? -33.331 -22.883 -53.471 1.00 62.71 ? 14 ARG A CZ 1 ATOM 91 N NH1 . ARG A 1 12 ? -32.482 -23.833 -53.898 1.00 59.81 ? 14 ARG A NH1 1 ATOM 92 N NH2 . ARG A 1 12 ? -33.724 -21.890 -54.299 1.00 60.66 ? 14 ARG A NH2 1 ATOM 93 N N . GLY A 1 13 ? -31.154 -22.186 -47.325 1.00 45.08 ? 15 GLY A N 1 ATOM 94 C CA . GLY A 1 13 ? -31.488 -22.602 -45.971 1.00 44.66 ? 15 GLY A CA 1 ATOM 95 C C . GLY A 1 13 ? -32.953 -22.928 -45.883 1.00 47.75 ? 15 GLY A C 1 ATOM 96 O O . GLY A 1 13 ? -33.623 -23.007 -46.901 1.00 50.44 ? 15 GLY A O 1 ATOM 97 N N . MET A 1 14 ? -33.448 -23.137 -44.676 1.00 47.59 ? 16 MET A N 1 ATOM 98 C CA . MET A 1 14 ? -34.865 -23.336 -44.452 1.00 49.52 ? 16 MET A CA 1 ATOM 99 C C . MET A 1 14 ? -35.367 -22.495 -43.256 1.00 49.05 ? 16 MET A C 1 ATOM 100 O O . MET A 1 14 ? -34.626 -22.226 -42.351 1.00 47.90 ? 16 MET A O 1 ATOM 101 C CB . MET A 1 14 ? -35.141 -24.826 -44.231 1.00 49.81 ? 16 MET A CB 1 ATOM 102 C CG . MET A 1 14 ? -34.739 -25.385 -42.886 1.00 50.46 ? 16 MET A CG 1 ATOM 103 S SD . MET A 1 14 ? -35.012 -27.181 -42.856 1.00 61.59 ? 16 MET A SD 1 ATOM 104 C CE . MET A 1 14 ? -34.197 -27.566 -41.335 1.00 56.24 ? 16 MET A CE 1 ATOM 105 N N . GLN A 1 15 ? -36.623 -22.073 -43.270 1.00 51.46 ? 17 GLN A N 1 ATOM 106 C CA . GLN A 1 15 ? -37.176 -21.287 -42.167 1.00 51.72 ? 17 GLN A CA 1 ATOM 107 C C . GLN A 1 15 ? -37.729 -22.177 -41.077 1.00 49.45 ? 17 GLN A C 1 ATOM 108 O O . GLN A 1 15 ? -38.311 -23.198 -41.358 1.00 49.68 ? 17 GLN A O 1 ATOM 109 C CB . GLN A 1 15 ? -38.309 -20.391 -42.658 1.00 54.64 ? 17 GLN A CB 1 ATOM 110 C CG . GLN A 1 15 ? -37.950 -19.456 -43.800 1.00 61.44 ? 17 GLN A CG 1 ATOM 111 C CD . GLN A 1 15 ? -37.052 -18.297 -43.383 1.00 64.97 ? 17 GLN A CD 1 ATOM 112 O OE1 . GLN A 1 15 ? -37.296 -17.155 -43.760 1.00 70.24 ? 17 GLN A OE1 1 ATOM 113 N NE2 . GLN A 1 15 ? -35.999 -18.588 -42.645 1.00 64.79 ? 17 GLN A NE2 1 ATOM 114 N N . LEU A 1 16 ? -37.560 -21.769 -39.829 1.00 47.42 ? 18 LEU A N 1 ATOM 115 C CA . LEU A 1 16 ? -38.164 -22.484 -38.725 1.00 46.72 ? 18 LEU A CA 1 ATOM 116 C C . LEU A 1 16 ? -38.965 -21.553 -37.843 1.00 47.59 ? 18 LEU A C 1 ATOM 117 O O . LEU A 1 16 ? -38.531 -20.472 -37.502 1.00 48.74 ? 18 LEU A O 1 ATOM 118 C CB . LEU A 1 16 ? -37.099 -23.162 -37.867 1.00 43.10 ? 18 LEU A CB 1 ATOM 119 C CG . LEU A 1 16 ? -36.088 -24.107 -38.520 1.00 41.98 ? 18 LEU A CG 1 ATOM 120 C CD1 . LEU A 1 16 ? -34.988 -24.507 -37.510 1.00 33.90 ? 18 LEU A CD1 1 ATOM 121 C CD2 . LEU A 1 16 ? -36.753 -25.389 -39.242 1.00 41.07 ? 18 LEU A CD2 1 ATOM 122 N N . THR A 1 17 ? -40.122 -22.013 -37.420 1.00 48.22 ? 19 THR A N 1 ATOM 123 C CA . THR A 1 17 ? -40.860 -21.369 -36.372 1.00 48.04 ? 19 THR A CA 1 ATOM 124 C C . THR A 1 17 ? -40.320 -21.782 -35.020 1.00 45.91 ? 19 THR A C 1 ATOM 125 O O . THR A 1 17 ? -40.231 -22.958 -34.709 1.00 43.73 ? 19 THR A O 1 ATOM 126 C CB . THR A 1 17 ? -42.295 -21.771 -36.503 1.00 50.61 ? 19 THR A CB 1 ATOM 127 O OG1 . THR A 1 17 ? -42.645 -21.487 -37.855 1.00 53.57 ? 19 THR A OG1 1 ATOM 128 C CG2 . THR A 1 17 ? -43.220 -20.943 -35.541 1.00 51.05 ? 19 THR A CG2 1 ATOM 129 N N . VAL A 1 18 ? -39.929 -20.789 -34.229 1.00 45.19 ? 20 VAL A N 1 ATOM 130 C CA . VAL A 1 18 ? -39.475 -21.031 -32.888 1.00 44.01 ? 20 VAL A CA 1 ATOM 131 C C . VAL A 1 18 ? -40.044 -19.910 -32.061 1.00 45.55 ? 20 VAL A C 1 ATOM 132 O O . VAL A 1 18 ? -39.736 -18.731 -32.318 1.00 46.88 ? 20 VAL A O 1 ATOM 133 C CB . VAL A 1 18 ? -37.945 -21.007 -32.770 1.00 42.38 ? 20 VAL A CB 1 ATOM 134 C CG1 . VAL A 1 18 ? -37.517 -21.709 -31.509 1.00 40.92 ? 20 VAL A CG1 1 ATOM 135 C CG2 . VAL A 1 18 ? -37.292 -21.668 -33.957 1.00 41.58 ? 20 VAL A CG2 1 ATOM 136 N N . PHE A 1 19 ? -40.886 -20.277 -31.092 1.00 46.13 ? 21 PHE A N 1 ATOM 137 C CA . PHE A 1 19 ? -41.466 -19.357 -30.089 1.00 47.42 ? 21 PHE A CA 1 ATOM 138 C C . PHE A 1 19 ? -42.123 -18.168 -30.709 1.00 49.31 ? 21 PHE A C 1 ATOM 139 O O . PHE A 1 19 ? -41.912 -17.044 -30.266 1.00 50.34 ? 21 PHE A O 1 ATOM 140 C CB . PHE A 1 19 ? -40.440 -18.845 -29.058 1.00 45.51 ? 21 PHE A CB 1 ATOM 141 C CG . PHE A 1 19 ? -39.623 -19.931 -28.350 1.00 44.14 ? 21 PHE A CG 1 ATOM 142 C CD1 . PHE A 1 19 ? -38.321 -19.665 -27.964 1.00 41.75 ? 21 PHE A CD1 1 ATOM 143 C CD2 . PHE A 1 19 ? -40.160 -21.176 -28.045 1.00 45.09 ? 21 PHE A CD2 1 ATOM 144 C CE1 . PHE A 1 19 ? -37.543 -20.621 -27.263 1.00 38.91 ? 21 PHE A CE1 1 ATOM 145 C CE2 . PHE A 1 19 ? -39.417 -22.142 -27.372 1.00 42.98 ? 21 PHE A CE2 1 ATOM 146 C CZ . PHE A 1 19 ? -38.093 -21.859 -26.978 1.00 42.13 ? 21 PHE A CZ 1 ATOM 147 N N . GLY A 1 20 ? -42.929 -18.408 -31.727 1.00 51.01 ? 22 GLY A N 1 ATOM 148 C CA . GLY A 1 20 ? -43.708 -17.344 -32.369 1.00 53.31 ? 22 GLY A CA 1 ATOM 149 C C . GLY A 1 20 ? -42.841 -16.425 -33.222 1.00 53.29 ? 22 GLY A C 1 ATOM 150 O O . GLY A 1 20 ? -43.283 -15.346 -33.604 1.00 56.34 ? 22 GLY A O 1 ATOM 151 N N . GLY A 1 21 ? -41.606 -16.827 -33.508 1.00 50.60 ? 23 GLY A N 1 ATOM 152 C CA . GLY A 1 21 ? -40.746 -16.092 -34.431 1.00 49.63 ? 23 GLY A CA 1 ATOM 153 C C . GLY A 1 21 ? -40.172 -17.112 -35.398 1.00 49.00 ? 23 GLY A C 1 ATOM 154 O O . GLY A 1 21 ? -40.638 -18.268 -35.453 1.00 50.19 ? 23 GLY A O 1 ATOM 155 N N . THR A 1 22 ? -39.134 -16.714 -36.130 1.00 47.68 ? 24 THR A N 1 ATOM 156 C CA . THR A 1 22 ? -38.514 -17.540 -37.164 1.00 45.45 ? 24 THR A CA 1 ATOM 157 C C . THR A 1 22 ? -37.013 -17.567 -36.963 1.00 43.28 ? 24 THR A C 1 ATOM 158 O O . THR A 1 22 ? -36.395 -16.549 -36.624 1.00 43.23 ? 24 THR A O 1 ATOM 159 C CB . THR A 1 22 ? -38.834 -16.953 -38.555 1.00 46.81 ? 24 THR A CB 1 ATOM 160 O OG1 . THR A 1 22 ? -40.264 -16.863 -38.696 1.00 50.32 ? 24 THR A OG1 1 ATOM 161 C CG2 . THR A 1 22 ? -38.305 -17.818 -39.665 1.00 45.76 ? 24 THR A CG2 1 ATOM 162 N N . VAL A 1 23 ? -36.423 -18.742 -37.179 1.00 41.54 ? 25 VAL A N 1 ATOM 163 C CA . VAL A 1 23 ? -35.002 -18.912 -37.291 1.00 37.97 ? 25 VAL A CA 1 ATOM 164 C C . VAL A 1 23 ? -34.698 -19.500 -38.704 1.00 39.72 ? 25 VAL A C 1 ATOM 165 O O . VAL A 1 23 ? -35.448 -20.333 -39.200 1.00 39.75 ? 25 VAL A O 1 ATOM 166 C CB . VAL A 1 23 ? -34.519 -19.821 -36.153 1.00 37.06 ? 25 VAL A CB 1 ATOM 167 C CG1 . VAL A 1 23 ? -32.981 -20.180 -36.305 1.00 31.28 ? 25 VAL A CG1 1 ATOM 168 C CG2 . VAL A 1 23 ? -34.818 -19.151 -34.799 1.00 35.85 ? 25 VAL A CG2 1 ATOM 169 N N . THR A 1 24 ? -33.637 -19.029 -39.379 1.00 39.56 ? 26 THR A N 1 ATOM 170 C CA . THR A 1 24 ? -33.214 -19.673 -40.636 1.00 38.80 ? 26 THR A CA 1 ATOM 171 C C . THR A 1 24 ? -32.066 -20.656 -40.360 1.00 37.72 ? 26 THR A C 1 ATOM 172 O O . THR A 1 24 ? -31.086 -20.277 -39.706 1.00 36.41 ? 26 THR A O 1 ATOM 173 C CB . THR A 1 24 ? -32.694 -18.661 -41.608 1.00 39.34 ? 26 THR A CB 1 ATOM 174 O OG1 . THR A 1 24 ? -33.626 -17.606 -41.682 1.00 38.26 ? 26 THR A OG1 1 ATOM 175 C CG2 . THR A 1 24 ? -32.512 -19.290 -42.974 1.00 39.10 ? 26 THR A CG2 1 ATOM 176 N N . ALA A 1 25 ? -32.192 -21.901 -40.843 1.00 36.35 ? 27 ALA A N 1 ATOM 177 C CA . ALA A 1 25 ? -31.232 -22.911 -40.496 1.00 34.70 ? 27 ALA A CA 1 ATOM 178 C C . ALA A 1 25 ? -30.614 -23.330 -41.808 1.00 35.04 ? 27 ALA A C 1 ATOM 179 O O . ALA A 1 25 ? -31.332 -23.521 -42.791 1.00 35.68 ? 27 ALA A O 1 ATOM 180 C CB . ALA A 1 25 ? -31.899 -24.088 -39.796 1.00 32.62 ? 27 ALA A CB 1 ATOM 181 N N . PHE A 1 26 ? -29.289 -23.406 -41.823 1.00 32.75 ? 28 PHE A N 1 ATOM 182 C CA . PHE A 1 26 ? -28.552 -23.974 -42.943 1.00 33.34 ? 28 PHE A CA 1 ATOM 183 C C . PHE A 1 26 ? -27.862 -25.216 -42.386 1.00 32.27 ? 28 PHE A C 1 ATOM 184 O O . PHE A 1 26 ? -26.857 -25.129 -41.646 1.00 30.88 ? 28 PHE A O 1 ATOM 185 C CB . PHE A 1 26 ? -27.507 -22.968 -43.462 1.00 33.79 ? 28 PHE A CB 1 ATOM 186 C CG . PHE A 1 26 ? -28.102 -21.661 -43.948 1.00 35.53 ? 28 PHE A CG 1 ATOM 187 C CD1 . PHE A 1 26 ? -28.432 -20.654 -43.048 1.00 38.85 ? 28 PHE A CD1 1 ATOM 188 C CD2 . PHE A 1 26 ? -28.339 -21.455 -45.281 1.00 39.03 ? 28 PHE A CD2 1 ATOM 189 C CE1 . PHE A 1 26 ? -29.018 -19.457 -43.474 1.00 40.80 ? 28 PHE A CE1 1 ATOM 190 C CE2 . PHE A 1 26 ? -28.905 -20.250 -45.735 1.00 42.84 ? 28 PHE A CE2 1 ATOM 191 C CZ . PHE A 1 26 ? -29.236 -19.246 -44.816 1.00 42.30 ? 28 PHE A CZ 1 ATOM 192 N N . LEU A 1 27 ? -28.447 -26.368 -42.659 1.00 32.74 ? 29 LEU A N 1 ATOM 193 C CA . LEU A 1 27 ? -27.915 -27.623 -42.107 1.00 31.27 ? 29 LEU A CA 1 ATOM 194 C C . LEU A 1 27 ? -27.135 -28.356 -43.197 1.00 32.03 ? 29 LEU A C 1 ATOM 195 O O . LEU A 1 27 ? -27.638 -28.534 -44.337 1.00 32.77 ? 29 LEU A O 1 ATOM 196 C CB . LEU A 1 27 ? -29.084 -28.510 -41.609 1.00 30.34 ? 29 LEU A CB 1 ATOM 197 C CG . LEU A 1 27 ? -30.127 -27.881 -40.660 1.00 30.11 ? 29 LEU A CG 1 ATOM 198 C CD1 . LEU A 1 27 ? -31.189 -28.879 -40.288 1.00 27.39 ? 29 LEU A CD1 1 ATOM 199 C CD2 . LEU A 1 27 ? -29.486 -27.304 -39.346 1.00 27.17 ? 29 LEU A CD2 1 ATOM 200 N N . GLY A 1 28 ? -25.952 -28.866 -42.841 1.00 31.18 ? 30 GLY A N 1 ATOM 201 C CA . GLY A 1 28 ? -25.141 -29.625 -43.785 1.00 31.13 ? 30 GLY A CA 1 ATOM 202 C C . GLY A 1 28 ? -24.423 -28.851 -44.880 1.00 33.83 ? 30 GLY A C 1 ATOM 203 O O . GLY A 1 28 ? -24.500 -29.244 -46.055 1.00 36.19 ? 30 GLY A O 1 ATOM 204 N N . ILE A 1 29 ? -23.728 -27.750 -44.541 1.00 34.17 ? 31 ILE A N 1 ATOM 205 C CA . ILE A 1 29 ? -22.931 -27.024 -45.555 1.00 34.59 ? 31 ILE A CA 1 ATOM 206 C C . ILE A 1 29 ? -21.553 -27.721 -45.531 1.00 34.38 ? 31 ILE A C 1 ATOM 207 O O . ILE A 1 29 ? -21.004 -27.918 -44.438 1.00 32.24 ? 31 ILE A O 1 ATOM 208 C CB . ILE A 1 29 ? -22.695 -25.544 -45.170 1.00 34.86 ? 31 ILE A CB 1 ATOM 209 C CG1 . ILE A 1 29 ? -24.024 -24.763 -44.949 1.00 37.47 ? 31 ILE A CG1 1 ATOM 210 C CG2 . ILE A 1 29 ? -21.849 -24.811 -46.248 1.00 36.26 ? 31 ILE A CG2 1 ATOM 211 C CD1 . ILE A 1 29 ? -23.794 -23.276 -44.558 1.00 34.12 ? 31 ILE A CD1 1 ATOM 212 N N . PRO A 1 30 ? -20.981 -28.068 -46.711 1.00 34.56 ? 32 PRO A N 1 ATOM 213 C CA . PRO A 1 30 ? -19.645 -28.701 -46.634 1.00 34.34 ? 32 PRO A CA 1 ATOM 214 C C . PRO A 1 30 ? -18.559 -27.659 -46.363 1.00 34.55 ? 32 PRO A C 1 ATOM 215 O O . PRO A 1 30 ? -18.685 -26.516 -46.769 1.00 34.21 ? 32 PRO A O 1 ATOM 216 C CB . PRO A 1 30 ? -19.449 -29.343 -48.015 1.00 36.74 ? 32 PRO A CB 1 ATOM 217 C CG . PRO A 1 30 ? -20.403 -28.524 -48.965 1.00 37.81 ? 32 PRO A CG 1 ATOM 218 C CD . PRO A 1 30 ? -21.493 -27.911 -48.096 1.00 36.36 ? 32 PRO A CD 1 ATOM 219 N N . TYR A 1 31 ? -17.519 -28.036 -45.636 1.00 33.88 ? 33 TYR A N 1 ATOM 220 C CA . TYR A 1 31 ? -16.456 -27.073 -45.394 1.00 34.59 ? 33 TYR A CA 1 ATOM 221 C C . TYR A 1 31 ? -15.098 -27.671 -45.744 1.00 35.40 ? 33 TYR A C 1 ATOM 222 O O . TYR A 1 31 ? -14.088 -27.030 -45.545 1.00 35.86 ? 33 TYR A O 1 ATOM 223 C CB . TYR A 1 31 ? -16.460 -26.575 -43.936 1.00 32.91 ? 33 TYR A CB 1 ATOM 224 C CG . TYR A 1 31 ? -16.077 -27.622 -42.906 1.00 30.39 ? 33 TYR A CG 1 ATOM 225 C CD1 . TYR A 1 31 ? -17.056 -28.454 -42.296 1.00 27.20 ? 33 TYR A CD1 1 ATOM 226 C CD2 . TYR A 1 31 ? -14.772 -27.783 -42.534 1.00 27.36 ? 33 TYR A CD2 1 ATOM 227 C CE1 . TYR A 1 31 ? -16.689 -29.417 -41.337 1.00 24.55 ? 33 TYR A CE1 1 ATOM 228 C CE2 . TYR A 1 31 ? -14.378 -28.770 -41.549 1.00 25.67 ? 33 TYR A CE2 1 ATOM 229 C CZ . TYR A 1 31 ? -15.352 -29.543 -40.935 1.00 24.60 ? 33 TYR A CZ 1 ATOM 230 O OH . TYR A 1 31 ? -14.967 -30.477 -39.992 1.00 24.67 ? 33 TYR A OH 1 ATOM 231 N N . ALA A 1 32 ? -15.074 -28.889 -46.292 1.00 36.37 ? 34 ALA A N 1 ATOM 232 C CA . ALA A 1 32 ? -13.792 -29.484 -46.730 1.00 36.90 ? 34 ALA A CA 1 ATOM 233 C C . ALA A 1 32 ? -14.015 -30.517 -47.847 1.00 37.86 ? 34 ALA A C 1 ATOM 234 O O . ALA A 1 32 ? -15.125 -30.983 -48.050 1.00 37.98 ? 34 ALA A O 1 ATOM 235 C CB . ALA A 1 32 ? -13.086 -30.112 -45.509 1.00 34.37 ? 34 ALA A CB 1 ATOM 236 N N . GLN A 1 33 ? -12.965 -30.920 -48.545 1.00 39.37 ? 35 GLN A N 1 ATOM 237 C CA . GLN A 1 33 ? -13.072 -32.079 -49.426 1.00 40.40 ? 35 GLN A CA 1 ATOM 238 C C . GLN A 1 33 ? -13.441 -33.309 -48.619 1.00 38.23 ? 35 GLN A C 1 ATOM 239 O O . GLN A 1 33 ? -12.837 -33.520 -47.583 1.00 38.10 ? 35 GLN A O 1 ATOM 240 C CB . GLN A 1 33 ? -11.748 -32.319 -50.142 1.00 42.63 ? 35 GLN A CB 1 ATOM 241 C CG . GLN A 1 33 ? -11.554 -31.428 -51.375 1.00 50.05 ? 35 GLN A CG 1 ATOM 242 C CD . GLN A 1 33 ? -10.205 -31.675 -52.047 1.00 60.06 ? 35 GLN A CD 1 ATOM 243 O OE1 . GLN A 1 33 ? -9.811 -32.837 -52.254 1.00 62.71 ? 35 GLN A OE1 1 ATOM 244 N NE2 . GLN A 1 33 ? -9.471 -30.578 -52.378 1.00 61.91 ? 35 GLN A NE2 1 ATOM 245 N N . PRO A 1 34 ? -14.409 -34.141 -49.083 1.00 37.52 ? 36 PRO A N 1 ATOM 246 C CA . PRO A 1 34 ? -14.638 -35.429 -48.400 1.00 36.46 ? 36 PRO A CA 1 ATOM 247 C C . PRO A 1 34 ? -13.281 -36.194 -48.205 1.00 35.93 ? 36 PRO A C 1 ATOM 248 O O . PRO A 1 34 ? -12.502 -36.301 -49.162 1.00 37.32 ? 36 PRO A O 1 ATOM 249 C CB . PRO A 1 34 ? -15.588 -36.199 -49.374 1.00 36.78 ? 36 PRO A CB 1 ATOM 250 C CG . PRO A 1 34 ? -16.292 -35.142 -50.080 1.00 38.62 ? 36 PRO A CG 1 ATOM 251 C CD . PRO A 1 34 ? -15.272 -34.011 -50.269 1.00 38.96 ? 36 PRO A CD 1 ATOM 252 N N . PRO A 1 35 ? -12.989 -36.673 -46.975 1.00 34.12 ? 37 PRO A N 1 ATOM 253 C CA . PRO A 1 35 ? -11.630 -37.201 -46.747 1.00 34.12 ? 37 PRO A CA 1 ATOM 254 C C . PRO A 1 35 ? -11.561 -38.677 -47.005 1.00 35.61 ? 37 PRO A C 1 ATOM 255 O O . PRO A 1 35 ? -11.355 -39.463 -46.075 1.00 35.15 ? 37 PRO A O 1 ATOM 256 C CB . PRO A 1 35 ? -11.384 -36.889 -45.270 1.00 31.88 ? 37 PRO A CB 1 ATOM 257 C CG . PRO A 1 35 ? -12.835 -36.950 -44.654 1.00 31.66 ? 37 PRO A CG 1 ATOM 258 C CD . PRO A 1 35 ? -13.710 -36.373 -45.712 1.00 31.05 ? 37 PRO A CD 1 ATOM 259 N N . LEU A 1 36 ? -11.705 -39.041 -48.276 1.00 38.08 ? 38 LEU A N 1 ATOM 260 C CA . LEU A 1 36 ? -11.876 -40.462 -48.741 1.00 39.13 ? 38 LEU A CA 1 ATOM 261 C C . LEU A 1 36 ? -10.743 -40.879 -49.600 1.00 40.16 ? 38 LEU A C 1 ATOM 262 O O . LEU A 1 36 ? -10.064 -40.025 -50.162 1.00 40.28 ? 38 LEU A O 1 ATOM 263 C CB . LEU A 1 36 ? -13.091 -40.590 -49.633 1.00 40.17 ? 38 LEU A CB 1 ATOM 264 C CG . LEU A 1 36 ? -14.416 -39.888 -49.328 1.00 41.49 ? 38 LEU A CG 1 ATOM 265 C CD1 . LEU A 1 36 ? -15.352 -40.186 -50.488 1.00 43.73 ? 38 LEU A CD1 1 ATOM 266 C CD2 . LEU A 1 36 ? -15.040 -40.392 -48.049 1.00 39.93 ? 38 LEU A CD2 1 ATOM 267 N N . GLY A 1 37 ? -10.545 -42.193 -49.720 1.00 42.39 ? 39 GLY A N 1 ATOM 268 C CA . GLY A 1 37 ? -9.559 -42.753 -50.633 1.00 44.13 ? 39 GLY A CA 1 ATOM 269 C C . GLY A 1 37 ? -8.182 -42.337 -50.144 1.00 45.60 ? 39 GLY A C 1 ATOM 270 O O . GLY A 1 37 ? -7.840 -42.550 -48.976 1.00 44.19 ? 39 GLY A O 1 ATOM 271 N N . ARG A 1 38 ? -7.408 -41.699 -51.023 1.00 47.66 ? 40 ARG A N 1 ATOM 272 C CA . ARG A 1 38 ? -6.094 -41.159 -50.678 1.00 48.80 ? 40 ARG A CA 1 ATOM 273 C C . ARG A 1 38 ? -6.101 -40.087 -49.551 1.00 46.70 ? 40 ARG A C 1 ATOM 274 O O . ARG A 1 38 ? -5.088 -39.918 -48.888 1.00 47.94 ? 40 ARG A O 1 ATOM 275 C CB . ARG A 1 38 ? -5.356 -40.698 -51.963 1.00 51.89 ? 40 ARG A CB 1 ATOM 276 C CG . ARG A 1 38 ? -5.862 -39.372 -52.584 1.00 55.94 ? 40 ARG A CG 1 ATOM 277 C CD . ARG A 1 38 ? -5.735 -39.318 -54.113 0.50 61.64 ? 40 ARG A CD 1 ATOM 278 N NE . ARG A 1 38 ? -6.427 -40.419 -54.798 0.50 65.33 ? 40 ARG A NE 1 ATOM 279 C CZ . ARG A 1 38 ? -6.922 -40.349 -56.036 0.50 67.65 ? 40 ARG A CZ 1 ATOM 280 N NH1 . ARG A 1 38 ? -6.842 -39.215 -56.725 0.50 68.67 ? 40 ARG A NH1 1 ATOM 281 N NH2 . ARG A 1 38 ? -7.521 -41.406 -56.578 0.50 67.19 ? 40 ARG A NH2 1 ATOM 282 N N . LEU A 1 39 ? -7.245 -39.426 -49.289 1.00 43.95 ? 41 LEU A N 1 ATOM 283 C CA . LEU A 1 39 ? -7.366 -38.393 -48.254 1.00 39.50 ? 41 LEU A CA 1 ATOM 284 C C . LEU A 1 39 ? -7.636 -38.926 -46.850 1.00 38.00 ? 41 LEU A C 1 ATOM 285 O O . LEU A 1 39 ? -7.501 -38.188 -45.861 1.00 34.70 ? 41 LEU A O 1 ATOM 286 C CB . LEU A 1 39 ? -8.385 -37.292 -48.653 1.00 37.85 ? 41 LEU A CB 1 ATOM 287 C CG . LEU A 1 39 ? -8.113 -36.557 -49.981 1.00 39.43 ? 41 LEU A CG 1 ATOM 288 C CD1 . LEU A 1 39 ? -9.168 -35.545 -50.385 1.00 37.24 ? 41 LEU A CD1 1 ATOM 289 C CD2 . LEU A 1 39 ? -6.697 -35.883 -49.966 1.00 41.60 ? 41 LEU A CD2 1 ATOM 290 N N . ARG A 1 40 ? -8.005 -40.200 -46.744 1.00 37.87 ? 42 ARG A N 1 ATOM 291 C CA . ARG A 1 40 ? -8.261 -40.794 -45.414 1.00 36.79 ? 42 ARG A CA 1 ATOM 292 C C . ARG A 1 40 ? -7.007 -40.674 -44.556 1.00 36.56 ? 42 ARG A C 1 ATOM 293 O O . ARG A 1 40 ? -5.891 -41.001 -45.040 1.00 37.37 ? 42 ARG A O 1 ATOM 294 C CB . ARG A 1 40 ? -8.638 -42.289 -45.520 1.00 37.04 ? 42 ARG A CB 1 ATOM 295 C CG . ARG A 1 40 ? -8.812 -42.933 -44.184 1.00 35.53 ? 42 ARG A CG 1 ATOM 296 C CD . ARG A 1 40 ? -8.928 -44.461 -44.293 1.00 38.92 ? 42 ARG A CD 1 ATOM 297 N NE . ARG A 1 40 ? -10.261 -44.875 -44.733 1.00 34.19 ? 42 ARG A NE 1 ATOM 298 C CZ . ARG A 1 40 ? -10.622 -46.122 -44.966 1.00 35.54 ? 42 ARG A CZ 1 ATOM 299 N NH1 . ARG A 1 40 ? -9.757 -47.146 -44.842 1.00 38.25 ? 42 ARG A NH1 1 ATOM 300 N NH2 . ARG A 1 40 ? -11.851 -46.346 -45.355 1.00 36.31 ? 42 ARG A NH2 1 ATOM 301 N N . PHE A 1 41 ? -7.195 -40.252 -43.293 1.00 35.11 ? 43 PHE A N 1 ATOM 302 C CA . PHE A 1 41 ? -6.079 -40.046 -42.277 1.00 34.64 ? 43 PHE A CA 1 ATOM 303 C C . PHE A 1 41 ? -5.256 -38.762 -42.527 1.00 34.73 ? 43 PHE A C 1 ATOM 304 O O . PHE A 1 41 ? -4.321 -38.457 -41.781 1.00 35.00 ? 43 PHE A O 1 ATOM 305 C CB . PHE A 1 41 ? -5.070 -41.216 -42.188 1.00 35.62 ? 43 PHE A CB 1 ATOM 306 C CG . PHE A 1 41 ? -5.675 -42.569 -41.861 1.00 34.97 ? 43 PHE A CG 1 ATOM 307 C CD1 . PHE A 1 41 ? -6.403 -42.764 -40.726 1.00 32.05 ? 43 PHE A CD1 1 ATOM 308 C CD2 . PHE A 1 41 ? -5.409 -43.670 -42.667 1.00 36.18 ? 43 PHE A CD2 1 ATOM 309 C CE1 . PHE A 1 41 ? -6.931 -44.005 -40.440 1.00 30.55 ? 43 PHE A CE1 1 ATOM 310 C CE2 . PHE A 1 41 ? -5.905 -44.916 -42.371 1.00 34.44 ? 43 PHE A CE2 1 ATOM 311 C CZ . PHE A 1 41 ? -6.677 -45.090 -41.266 1.00 32.29 ? 43 PHE A CZ 1 ATOM 312 N N . LYS A 1 42 ? -5.569 -38.027 -43.583 1.00 34.89 ? 44 LYS A N 1 ATOM 313 C CA . LYS A 1 42 ? -4.849 -36.779 -43.815 1.00 36.12 ? 44 LYS A CA 1 ATOM 314 C C . LYS A 1 42 ? -5.668 -35.572 -43.309 1.00 35.66 ? 44 LYS A C 1 ATOM 315 O O . LYS A 1 42 ? -6.895 -35.676 -43.021 1.00 33.98 ? 44 LYS A O 1 ATOM 316 C CB . LYS A 1 42 ? -4.455 -36.623 -45.286 1.00 38.10 ? 44 LYS A CB 1 ATOM 317 C CG . LYS A 1 42 ? -3.490 -37.746 -45.797 1.00 41.34 ? 44 LYS A CG 1 ATOM 318 C CD . LYS A 1 42 ? -3.101 -37.593 -47.282 1.00 48.08 ? 44 LYS A CD 1 ATOM 319 C CE . LYS A 1 42 ? -2.420 -36.257 -47.567 1.00 54.64 ? 44 LYS A CE 1 ATOM 320 N NZ . LYS A 1 42 ? -1.255 -36.428 -48.535 1.00 61.03 ? 44 LYS A NZ 1 ATOM 321 N N . LYS A 1 43 ? -4.953 -34.449 -43.184 1.00 35.82 ? 45 LYS A N 1 ATOM 322 C CA . LYS A 1 43 ? -5.484 -33.186 -42.808 1.00 35.50 ? 45 LYS A CA 1 ATOM 323 C C . LYS A 1 43 ? -6.605 -32.852 -43.822 1.00 36.06 ? 45 LYS A C 1 ATOM 324 O O . LYS A 1 43 ? -6.523 -33.273 -45.001 1.00 37.12 ? 45 LYS A O 1 ATOM 325 C CB . LYS A 1 43 ? -4.339 -32.133 -42.765 1.00 36.63 ? 45 LYS A CB 1 ATOM 326 C CG . LYS A 1 43 ? -3.571 -32.171 -41.418 1.00 36.02 ? 45 LYS A CG 1 ATOM 327 C CD . LYS A 1 43 ? -2.266 -31.377 -41.426 1.00 37.06 ? 45 LYS A CD 1 ATOM 328 C CE . LYS A 1 43 ? -2.402 -29.862 -41.404 1.00 41.76 ? 45 LYS A CE 1 ATOM 329 N NZ . LYS A 1 43 ? -1.053 -29.095 -41.282 1.00 40.32 ? 45 LYS A NZ 1 ATOM 330 N N . PRO A 1 44 ? -7.662 -32.134 -43.370 1.00 34.27 ? 46 PRO A N 1 ATOM 331 C CA . PRO A 1 44 ? -8.761 -31.817 -44.275 1.00 34.60 ? 46 PRO A CA 1 ATOM 332 C C . PRO A 1 44 ? -8.219 -30.911 -45.349 1.00 37.68 ? 46 PRO A C 1 ATOM 333 O O . PRO A 1 44 ? -7.403 -30.021 -45.057 1.00 37.98 ? 46 PRO A O 1 ATOM 334 C CB . PRO A 1 44 ? -9.750 -31.043 -43.383 1.00 34.32 ? 46 PRO A CB 1 ATOM 335 C CG . PRO A 1 44 ? -8.892 -30.525 -42.181 1.00 29.73 ? 46 PRO A CG 1 ATOM 336 C CD . PRO A 1 44 ? -7.744 -31.453 -42.066 1.00 31.60 ? 46 PRO A CD 1 ATOM 337 N N . GLN A 1 45 ? -8.616 -31.152 -46.589 1.00 40.57 ? 47 GLN A N 1 ATOM 338 C CA . GLN A 1 45 ? -8.154 -30.338 -47.713 1.00 43.85 ? 47 GLN A CA 1 ATOM 339 C C . GLN A 1 45 ? -9.250 -29.361 -47.985 1.00 45.64 ? 47 GLN A C 1 ATOM 340 O O . GLN A 1 45 ? -10.448 -29.643 -47.753 1.00 43.16 ? 47 GLN A O 1 ATOM 341 C CB . GLN A 1 45 ? -7.964 -31.184 -48.975 1.00 45.27 ? 47 GLN A CB 1 ATOM 342 C CG . GLN A 1 45 ? -6.982 -32.324 -48.838 1.00 47.48 ? 47 GLN A CG 1 ATOM 343 C CD . GLN A 1 45 ? -5.602 -31.870 -48.418 1.00 53.78 ? 47 GLN A CD 1 ATOM 344 O OE1 . GLN A 1 45 ? -5.008 -31.031 -49.112 1.00 58.38 ? 47 GLN A OE1 1 ATOM 345 N NE2 . GLN A 1 45 ? -5.064 -32.416 -47.269 1.00 49.51 ? 47 GLN A NE2 1 ATOM 346 N N . SER A 1 46 ? -8.860 -28.218 -48.518 1.00 49.71 ? 48 SER A N 1 ATOM 347 C CA . SER A 1 46 ? -9.822 -27.145 -48.674 1.00 53.52 ? 48 SER A CA 1 ATOM 348 C C . SER A 1 46 ? -10.766 -27.432 -49.848 1.00 56.01 ? 48 SER A C 1 ATOM 349 O O . SER A 1 46 ? -10.431 -28.140 -50.802 1.00 57.46 ? 48 SER A O 1 ATOM 350 C CB . SER A 1 46 ? -9.140 -25.741 -48.740 1.00 54.93 ? 48 SER A CB 1 ATOM 351 O OG . SER A 1 46 ? -8.558 -25.523 -50.030 1.00 59.05 ? 48 SER A OG 1 ATOM 352 N N . LEU A 1 47 ? -11.950 -26.857 -49.730 1.00 58.42 ? 49 LEU A N 1 ATOM 353 C CA . LEU A 1 47 ? -13.063 -27.104 -50.615 1.00 62.28 ? 49 LEU A CA 1 ATOM 354 C C . LEU A 1 47 ? -12.904 -26.427 -51.975 1.00 66.33 ? 49 LEU A C 1 ATOM 355 O O . LEU A 1 47 ? -12.554 -25.242 -52.056 1.00 66.97 ? 49 LEU A O 1 ATOM 356 C CB . LEU A 1 47 ? -14.339 -26.630 -49.928 1.00 61.50 ? 49 LEU A CB 1 ATOM 357 C CG . LEU A 1 47 ? -15.585 -27.307 -50.441 1.00 62.89 ? 49 LEU A CG 1 ATOM 358 C CD1 . LEU A 1 47 ? -15.348 -28.773 -50.725 1.00 62.97 ? 49 LEU A CD1 1 ATOM 359 C CD2 . LEU A 1 47 ? -16.647 -27.069 -49.417 1.00 62.76 ? 49 LEU A CD2 1 ATOM 360 N N . THR A 1 48 ? -13.210 -27.215 -53.013 1.00 69.66 ? 50 THR A N 1 ATOM 361 C CA . THR A 1 48 ? -12.910 -26.944 -54.425 1.00 74.47 ? 50 THR A CA 1 ATOM 362 C C . THR A 1 48 ? -13.617 -25.726 -55.005 1.00 76.23 ? 50 THR A C 1 ATOM 363 O O . THR A 1 48 ? -13.002 -25.046 -55.844 1.00 78.67 ? 50 THR A O 1 ATOM 364 C CB . THR A 1 48 ? -13.225 -28.209 -55.354 1.00 76.52 ? 50 THR A CB 1 ATOM 365 O OG1 . THR A 1 48 ? -14.006 -29.181 -54.625 1.00 75.53 ? 50 THR A OG1 1 ATOM 366 C CG2 . THR A 1 48 ? -11.930 -28.901 -55.894 1.00 78.69 ? 50 THR A CG2 1 ATOM 367 N N . LYS A 1 49 ? -14.873 -25.475 -54.561 1.00 75.17 ? 51 LYS A N 1 ATOM 368 C CA . LYS A 1 49 ? -15.877 -24.529 -55.173 1.00 77.01 ? 51 LYS A CA 1 ATOM 369 C C . LYS A 1 49 ? -17.045 -25.199 -55.963 1.00 77.51 ? 51 LYS A C 1 ATOM 370 O O . LYS A 1 49 ? -16.844 -26.192 -56.679 1.00 79.16 ? 51 LYS A O 1 ATOM 371 C CB . LYS A 1 49 ? -15.221 -23.402 -56.002 1.00 79.76 ? 51 LYS A CB 1 ATOM 372 C CG . LYS A 1 49 ? -15.780 -23.152 -57.435 1.00 85.38 ? 51 LYS A CG 1 ATOM 373 C CD . LYS A 1 49 ? -15.317 -24.204 -58.539 1.00 91.37 ? 51 LYS A CD 1 ATOM 374 C CE . LYS A 1 49 ? -13.788 -24.207 -58.871 1.00 93.88 ? 51 LYS A CE 1 ATOM 375 N NZ . LYS A 1 49 ? -13.234 -22.862 -59.246 1.00 95.82 ? 51 LYS A NZ 1 ATOM 376 N N . TRP A 1 50 ? -18.264 -24.673 -55.822 1.00 76.06 ? 52 TRP A N 1 ATOM 377 C CA . TRP A 1 50 ? -19.409 -25.200 -56.596 1.00 75.52 ? 52 TRP A CA 1 ATOM 378 C C . TRP A 1 50 ? -20.185 -24.050 -57.238 1.00 77.07 ? 52 TRP A C 1 ATOM 379 O O . TRP A 1 50 ? -19.990 -22.869 -56.924 1.00 77.27 ? 52 TRP A O 1 ATOM 380 C CB . TRP A 1 50 ? -20.340 -26.112 -55.761 1.00 72.73 ? 52 TRP A CB 1 ATOM 381 C CG . TRP A 1 50 ? -21.146 -25.349 -54.748 1.00 67.69 ? 52 TRP A CG 1 ATOM 382 C CD1 . TRP A 1 50 ? -22.308 -24.647 -54.967 1.00 65.52 ? 52 TRP A CD1 1 ATOM 383 C CD2 . TRP A 1 50 ? -20.839 -25.182 -53.357 1.00 60.82 ? 52 TRP A CD2 1 ATOM 384 N NE1 . TRP A 1 50 ? -22.754 -24.076 -53.788 1.00 60.99 ? 52 TRP A NE1 1 ATOM 385 C CE2 . TRP A 1 50 ? -21.864 -24.374 -52.790 1.00 58.34 ? 52 TRP A CE2 1 ATOM 386 C CE3 . TRP A 1 50 ? -19.808 -25.641 -52.531 1.00 57.29 ? 52 TRP A CE3 1 ATOM 387 C CZ2 . TRP A 1 50 ? -21.869 -24.006 -51.435 1.00 54.06 ? 52 TRP A CZ2 1 ATOM 388 C CZ3 . TRP A 1 50 ? -19.828 -25.281 -51.163 1.00 51.39 ? 52 TRP A CZ3 1 ATOM 389 C CH2 . TRP A 1 50 ? -20.841 -24.475 -50.645 1.00 50.66 ? 52 TRP A CH2 1 ATOM 390 N N . SER A 1 51 ? -21.064 -24.412 -58.151 1.00 78.27 ? 53 SER A N 1 ATOM 391 C CA . SER A 1 51 ? -21.806 -23.441 -58.940 1.00 79.77 ? 53 SER A CA 1 ATOM 392 C C . SER A 1 51 ? -23.119 -24.133 -59.137 1.00 79.33 ? 53 SER A C 1 ATOM 393 O O . SER A 1 51 ? -23.142 -25.260 -59.628 1.00 80.74 ? 53 SER A O 1 ATOM 394 C CB . SER A 1 51 ? -21.114 -23.198 -60.276 1.00 82.19 ? 53 SER A CB 1 ATOM 395 O OG . SER A 1 51 ? -22.019 -22.620 -61.176 1.00 85.62 ? 53 SER A OG 1 ATOM 396 N N . ASP A 1 52 ? -24.196 -23.451 -58.763 1.00 77.77 ? 54 ASP A N 1 ATOM 397 C CA . ASP A 1 52 ? -25.491 -24.057 -58.409 1.00 75.64 ? 54 ASP A CA 1 ATOM 398 C C . ASP A 1 52 ? -25.765 -23.722 -56.939 1.00 70.35 ? 54 ASP A C 1 ATOM 399 O O . ASP A 1 52 ? -24.904 -23.179 -56.247 1.00 67.89 ? 54 ASP A O 1 ATOM 400 C CB . ASP A 1 52 ? -25.564 -25.582 -58.661 1.00 76.78 ? 54 ASP A CB 1 ATOM 401 C CG . ASP A 1 52 ? -24.608 -26.410 -57.742 1.00 77.30 ? 54 ASP A CG 1 ATOM 402 O OD1 . ASP A 1 52 ? -24.347 -26.012 -56.591 1.00 77.73 ? 54 ASP A OD1 1 ATOM 403 O OD2 . ASP A 1 52 ? -24.130 -27.492 -58.178 1.00 81.90 ? 54 ASP A OD2 1 ATOM 404 N N . ILE A 1 53 ? -26.974 -24.025 -56.485 1.00 67.43 ? 55 ILE A N 1 ATOM 405 C CA . ILE A 1 53 ? -27.355 -23.759 -55.126 1.00 62.93 ? 55 ILE A CA 1 ATOM 406 C C . ILE A 1 53 ? -27.298 -25.026 -54.310 1.00 60.85 ? 55 ILE A C 1 ATOM 407 O O . ILE A 1 53 ? -27.984 -26.003 -54.622 1.00 60.52 ? 55 ILE A O 1 ATOM 408 C CB . ILE A 1 53 ? -28.737 -23.134 -55.025 1.00 64.08 ? 55 ILE A CB 1 ATOM 409 C CG1 . ILE A 1 53 ? -28.788 -21.888 -55.949 1.00 63.43 ? 55 ILE A CG1 1 ATOM 410 C CG2 . ILE A 1 53 ? -29.072 -22.899 -53.503 1.00 59.58 ? 55 ILE A CG2 1 ATOM 411 C CD1 . ILE A 1 53 ? -30.017 -21.060 -55.879 1.00 61.02 ? 55 ILE A CD1 1 ATOM 412 N N . TRP A 1 54 ? -26.435 -25.009 -53.286 1.00 57.53 ? 56 TRP A N 1 ATOM 413 C CA . TRP A 1 54 ? -26.279 -26.138 -52.419 1.00 54.85 ? 56 TRP A CA 1 ATOM 414 C C . TRP A 1 54 ? -27.392 -26.085 -51.409 1.00 54.48 ? 56 TRP A C 1 ATOM 415 O O . TRP A 1 54 ? -27.518 -25.118 -50.675 1.00 54.20 ? 56 TRP A O 1 ATOM 416 C CB . TRP A 1 54 ? -24.952 -26.099 -51.696 1.00 52.09 ? 56 TRP A CB 1 ATOM 417 C CG . TRP A 1 54 ? -24.865 -27.208 -50.761 1.00 49.52 ? 56 TRP A CG 1 ATOM 418 C CD1 . TRP A 1 54 ? -25.502 -27.322 -49.546 1.00 45.57 ? 56 TRP A CD1 1 ATOM 419 C CD2 . TRP A 1 54 ? -24.142 -28.429 -50.959 1.00 49.02 ? 56 TRP A CD2 1 ATOM 420 N NE1 . TRP A 1 54 ? -25.192 -28.533 -48.971 1.00 46.46 ? 56 TRP A NE1 1 ATOM 421 C CE2 . TRP A 1 54 ? -24.350 -29.228 -49.802 1.00 47.68 ? 56 TRP A CE2 1 ATOM 422 C CE3 . TRP A 1 54 ? -23.269 -28.891 -51.961 1.00 53.46 ? 56 TRP A CE3 1 ATOM 423 C CZ2 . TRP A 1 54 ? -23.748 -30.497 -49.633 1.00 49.32 ? 56 TRP A CZ2 1 ATOM 424 C CZ3 . TRP A 1 54 ? -22.652 -30.166 -51.795 1.00 54.62 ? 56 TRP A CZ3 1 ATOM 425 C CH2 . TRP A 1 54 ? -22.911 -30.949 -50.639 1.00 51.44 ? 56 TRP A CH2 1 ATOM 426 N N . ASN A 1 55 ? -28.194 -27.132 -51.358 1.00 55.28 ? 57 ASN A N 1 ATOM 427 C CA . ASN A 1 55 ? -29.339 -27.149 -50.475 1.00 56.08 ? 57 ASN A CA 1 ATOM 428 C C . ASN A 1 55 ? -28.929 -27.600 -49.056 1.00 52.07 ? 57 ASN A C 1 ATOM 429 O O . ASN A 1 55 ? -28.592 -28.761 -48.848 1.00 52.36 ? 57 ASN A O 1 ATOM 430 C CB . ASN A 1 55 ? -30.410 -28.059 -51.078 1.00 59.71 ? 57 ASN A CB 1 ATOM 431 C CG . ASN A 1 55 ? -31.229 -27.374 -52.167 1.00 69.01 ? 57 ASN A CG 1 ATOM 432 O OD1 . ASN A 1 55 ? -31.107 -26.169 -52.399 1.00 69.54 ? 57 ASN A OD1 1 ATOM 433 N ND2 . ASN A 1 55 ? -32.087 -28.158 -52.841 1.00 84.03 ? 57 ASN A ND2 1 ATOM 434 N N . ALA A 1 56 ? -28.923 -26.672 -48.098 1.00 48.32 ? 58 ALA A N 1 ATOM 435 C CA . ALA A 1 56 ? -28.500 -26.948 -46.730 1.00 43.51 ? 58 ALA A CA 1 ATOM 436 C C . ALA A 1 56 ? -29.733 -27.112 -45.848 1.00 42.40 ? 58 ALA A C 1 ATOM 437 O O . ALA A 1 56 ? -29.986 -26.317 -44.900 1.00 42.30 ? 58 ALA A O 1 ATOM 438 C CB . ALA A 1 56 ? -27.616 -25.797 -46.222 1.00 41.55 ? 58 ALA A CB 1 ATOM 439 N N . THR A 1 57 ? -30.516 -28.129 -46.147 1.00 41.47 ? 59 THR A N 1 ATOM 440 C CA . THR A 1 57 ? -31.845 -28.206 -45.555 1.00 42.00 ? 59 THR A CA 1 ATOM 441 C C . THR A 1 57 ? -32.035 -29.505 -44.764 1.00 41.60 ? 59 THR A C 1 ATOM 442 O O . THR A 1 57 ? -33.125 -29.815 -44.328 1.00 42.04 ? 59 THR A O 1 ATOM 443 C CB . THR A 1 57 ? -32.947 -28.139 -46.638 1.00 44.81 ? 59 THR A CB 1 ATOM 444 O OG1 . THR A 1 57 ? -32.606 -29.073 -47.666 1.00 44.30 ? 59 THR A OG1 1 ATOM 445 C CG2 . THR A 1 57 ? -33.040 -26.756 -47.270 1.00 43.54 ? 59 THR A CG2 1 ATOM 446 N N . LYS A 1 58 ? -30.976 -30.275 -44.576 1.00 40.76 ? 60 LYS A N 1 ATOM 447 C CA . LYS A 1 58 ? -31.059 -31.416 -43.657 1.00 41.02 ? 60 LYS A CA 1 ATOM 448 C C . LYS A 1 58 ? -29.716 -31.652 -43.007 1.00 38.31 ? 60 LYS A C 1 ATOM 449 O O . LYS A 1 58 ? -28.688 -31.300 -43.588 1.00 37.71 ? 60 LYS A O 1 ATOM 450 C CB . LYS A 1 58 ? -31.670 -32.690 -44.309 1.00 42.20 ? 60 LYS A CB 1 ATOM 451 C CG . LYS A 1 58 ? -30.864 -33.345 -45.396 1.00 45.91 ? 60 LYS A CG 1 ATOM 452 C CD . LYS A 1 58 ? -31.708 -34.467 -46.081 1.00 53.85 ? 60 LYS A CD 1 ATOM 453 C CE . LYS A 1 58 ? -30.887 -35.408 -47.057 1.00 60.70 ? 60 LYS A CE 1 ATOM 454 N NZ . LYS A 1 58 ? -29.529 -34.873 -47.557 1.00 61.38 ? 60 LYS A NZ 1 ATOM 455 N N . TYR A 1 59 ? -29.720 -32.185 -41.791 1.00 35.86 ? 61 TYR A N 1 ATOM 456 C CA . TYR A 1 59 ? -28.428 -32.626 -41.238 1.00 34.91 ? 61 TYR A CA 1 ATOM 457 C C . TYR A 1 59 ? -27.629 -33.577 -42.176 1.00 34.41 ? 61 TYR A C 1 ATOM 458 O O . TYR A 1 59 ? -28.193 -34.377 -42.878 1.00 35.80 ? 61 TYR A O 1 ATOM 459 C CB . TYR A 1 59 ? -28.641 -33.272 -39.880 1.00 33.38 ? 61 TYR A CB 1 ATOM 460 C CG . TYR A 1 59 ? -29.095 -32.341 -38.756 1.00 30.81 ? 61 TYR A CG 1 ATOM 461 C CD1 . TYR A 1 59 ? -28.233 -31.393 -38.217 1.00 25.10 ? 61 TYR A CD1 1 ATOM 462 C CD2 . TYR A 1 59 ? -30.357 -32.473 -38.181 1.00 29.08 ? 61 TYR A CD2 1 ATOM 463 C CE1 . TYR A 1 59 ? -28.614 -30.587 -37.132 1.00 23.93 ? 61 TYR A CE1 1 ATOM 464 C CE2 . TYR A 1 59 ? -30.729 -31.691 -37.091 1.00 26.65 ? 61 TYR A CE2 1 ATOM 465 C CZ . TYR A 1 59 ? -29.830 -30.755 -36.585 1.00 27.49 ? 61 TYR A CZ 1 ATOM 466 O OH . TYR A 1 59 ? -30.153 -29.968 -35.529 1.00 34.22 ? 61 TYR A OH 1 ATOM 467 N N . ALA A 1 60 ? -26.313 -33.421 -42.222 1.00 32.38 ? 62 ALA A N 1 ATOM 468 C CA . ALA A 1 60 ? -25.463 -34.255 -43.087 1.00 32.64 ? 62 ALA A CA 1 ATOM 469 C C . ALA A 1 60 ? -25.081 -35.546 -42.343 1.00 32.49 ? 62 ALA A C 1 ATOM 470 O O . ALA A 1 60 ? -25.404 -35.704 -41.157 1.00 32.00 ? 62 ALA A O 1 ATOM 471 C CB . ALA A 1 60 ? -24.178 -33.450 -43.491 1.00 31.42 ? 62 ALA A CB 1 ATOM 472 N N . ASN A 1 61 ? -24.422 -36.458 -43.052 1.00 31.38 ? 63 ASN A N 1 ATOM 473 C CA . ASN A 1 61 ? -23.779 -37.604 -42.463 1.00 31.82 ? 63 ASN A CA 1 ATOM 474 C C . ASN A 1 61 ? -22.939 -37.285 -41.216 1.00 29.86 ? 63 ASN A C 1 ATOM 475 O O . ASN A 1 61 ? -22.103 -36.371 -41.229 1.00 27.50 ? 63 ASN A O 1 ATOM 476 C CB . ASN A 1 61 ? -22.797 -38.224 -43.478 1.00 32.85 ? 63 ASN A CB 1 ATOM 477 C CG . ASN A 1 61 ? -23.472 -38.721 -44.771 1.00 34.79 ? 63 ASN A CG 1 ATOM 478 O OD1 . ASN A 1 61 ? -24.640 -39.124 -44.783 1.00 34.79 ? 63 ASN A OD1 1 ATOM 479 N ND2 . ASN A 1 61 ? -22.688 -38.763 -45.857 1.00 36.48 ? 63 ASN A ND2 1 ATOM 480 N N . SER A 1 62 ? -23.128 -38.094 -40.165 1.00 29.36 ? 64 SER A N 1 ATOM 481 C CA . SER A 1 62 ? -22.198 -38.138 -39.043 1.00 28.28 ? 64 SER A CA 1 ATOM 482 C C . SER A 1 62 ? -20.929 -38.935 -39.481 1.00 29.69 ? 64 SER A C 1 ATOM 483 O O . SER A 1 62 ? -21.047 -39.823 -40.336 1.00 29.72 ? 64 SER A O 1 ATOM 484 C CB . SER A 1 62 ? -22.875 -38.784 -37.831 1.00 27.71 ? 64 SER A CB 1 ATOM 485 O OG . SER A 1 62 ? -24.032 -38.058 -37.390 1.00 23.68 ? 64 SER A OG 1 ATOM 486 N N . CYS A 1 63 ? -19.749 -38.617 -38.902 1.00 27.98 ? 65 CYS A N 1 ATOM 487 C CA . CYS A 1 63 ? -18.520 -39.389 -39.119 1.00 28.70 ? 65 CYS A CA 1 ATOM 488 C C . CYS A 1 63 ? -18.580 -40.876 -38.639 1.00 28.69 ? 65 CYS A C 1 ATOM 489 O O . CYS A 1 63 ? -19.278 -41.178 -37.666 1.00 27.88 ? 65 CYS A O 1 ATOM 490 C CB . CYS A 1 63 ? -17.292 -38.647 -38.497 1.00 27.63 ? 65 CYS A CB 1 ATOM 491 S SG . CYS A 1 63 ? -17.118 -36.940 -39.179 1.00 28.18 ? 65 CYS A SG 1 ATOM 492 N N . CYS A 1 64 ? -17.794 -41.762 -39.269 1.00 28.80 ? 66 CYS A N 1 ATOM 493 C CA . CYS A 1 64 ? -17.812 -43.181 -38.889 1.00 31.38 ? 66 CYS A CA 1 ATOM 494 C C . CYS A 1 64 ? -17.435 -43.256 -37.446 1.00 31.09 ? 66 CYS A C 1 ATOM 495 O O . CYS A 1 64 ? -16.546 -42.493 -36.977 1.00 30.38 ? 66 CYS A O 1 ATOM 496 C CB . CYS A 1 64 ? -16.780 -44.002 -39.689 1.00 32.54 ? 66 CYS A CB 1 ATOM 497 S SG . CYS A 1 64 ? -17.158 -43.988 -41.432 1.00 38.56 ? 66 CYS A SG 1 ATOM 498 N N . GLN A 1 65 ? -18.080 -44.155 -36.738 1.00 29.93 ? 67 GLN A N 1 ATOM 499 C CA . GLN A 1 65 ? -17.803 -44.291 -35.341 1.00 30.62 ? 67 GLN A CA 1 ATOM 500 C C . GLN A 1 65 ? -18.517 -45.568 -34.819 1.00 32.24 ? 67 GLN A C 1 ATOM 501 O O . GLN A 1 65 ? -19.567 -45.954 -35.354 1.00 31.83 ? 67 GLN A O 1 ATOM 502 C CB . GLN A 1 65 ? -18.284 -43.029 -34.591 1.00 28.96 ? 67 GLN A CB 1 ATOM 503 C CG . GLN A 1 65 ? -19.795 -42.812 -34.642 1.00 29.91 ? 67 GLN A CG 1 ATOM 504 C CD . GLN A 1 65 ? -20.225 -41.418 -34.115 1.00 31.69 ? 67 GLN A CD 1 ATOM 505 O OE1 . GLN A 1 65 ? -20.656 -41.298 -32.968 1.00 27.40 ? 67 GLN A OE1 1 ATOM 506 N NE2 . GLN A 1 65 ? -20.103 -40.369 -34.959 1.00 29.96 ? 67 GLN A NE2 1 ATOM 507 N N . ASN A 1 66 ? -17.928 -46.196 -33.804 1.00 31.95 ? 68 ASN A N 1 ATOM 508 C CA . ASN A 1 66 ? -18.634 -47.180 -32.998 1.00 33.79 ? 68 ASN A CA 1 ATOM 509 C C . ASN A 1 66 ? -19.773 -46.562 -32.189 1.00 33.64 ? 68 ASN A C 1 ATOM 510 O O . ASN A 1 66 ? -19.746 -45.414 -31.814 1.00 33.58 ? 68 ASN A O 1 ATOM 511 C CB . ASN A 1 66 ? -17.645 -47.924 -32.069 1.00 33.09 ? 68 ASN A CB 1 ATOM 512 C CG . ASN A 1 66 ? -16.682 -48.836 -32.873 1.00 37.77 ? 68 ASN A CG 1 ATOM 513 O OD1 . ASN A 1 66 ? -17.110 -49.568 -33.758 1.00 42.49 ? 68 ASN A OD1 1 ATOM 514 N ND2 . ASN A 1 66 ? -15.407 -48.737 -32.613 1.00 35.89 ? 68 ASN A ND2 1 ATOM 515 N N . ILE A 1 67 ? -20.744 -47.373 -31.870 1.00 35.00 ? 69 ILE A N 1 ATOM 516 C CA . ILE A 1 67 ? -21.951 -46.927 -31.271 1.00 37.18 ? 69 ILE A CA 1 ATOM 517 C C . ILE A 1 67 ? -22.130 -47.568 -29.896 1.00 37.01 ? 69 ILE A C 1 ATOM 518 O O . ILE A 1 67 ? -21.765 -48.699 -29.708 1.00 36.84 ? 69 ILE A O 1 ATOM 519 C CB . ILE A 1 67 ? -23.116 -47.313 -32.230 1.00 38.75 ? 69 ILE A CB 1 ATOM 520 C CG1 . ILE A 1 67 ? -23.560 -46.072 -32.993 1.00 40.17 ? 69 ILE A CG1 1 ATOM 521 C CG2 . ILE A 1 67 ? -24.264 -47.767 -31.497 1.00 41.36 ? 69 ILE A CG2 1 ATOM 522 C CD1 . ILE A 1 67 ? -23.047 -46.035 -34.343 1.00 40.59 ? 69 ILE A CD1 1 ATOM 523 N N . ASP A 1 68 ? -22.726 -46.832 -28.960 1.00 37.44 ? 70 ASP A N 1 ATOM 524 C CA . ASP A 1 68 ? -23.053 -47.343 -27.609 1.00 38.95 ? 70 ASP A CA 1 ATOM 525 C C . ASP A 1 68 ? -24.252 -48.352 -27.625 1.00 39.58 ? 70 ASP A C 1 ATOM 526 O O . ASP A 1 68 ? -25.380 -47.920 -27.752 1.00 40.06 ? 70 ASP A O 1 ATOM 527 C CB . ASP A 1 68 ? -23.353 -46.128 -26.663 1.00 38.47 ? 70 ASP A CB 1 ATOM 528 C CG . ASP A 1 68 ? -23.724 -46.560 -25.221 1.00 40.79 ? 70 ASP A CG 1 ATOM 529 O OD1 . ASP A 1 68 ? -24.078 -45.674 -24.427 1.00 41.30 ? 70 ASP A OD1 1 ATOM 530 O OD2 . ASP A 1 68 ? -23.660 -47.781 -24.873 1.00 43.59 ? 70 ASP A OD2 1 ATOM 531 N N . GLN A 1 69 ? -23.992 -49.651 -27.511 1.00 39.94 ? 71 GLN A N 1 ATOM 532 C CA . GLN A 1 69 ? -25.050 -50.698 -27.536 1.00 42.24 ? 71 GLN A CA 1 ATOM 533 C C . GLN A 1 69 ? -25.281 -51.313 -26.178 1.00 41.71 ? 71 GLN A C 1 ATOM 534 O O . GLN A 1 69 ? -25.934 -52.349 -26.089 1.00 41.30 ? 71 GLN A O 1 ATOM 535 C CB . GLN A 1 69 ? -24.671 -51.873 -28.454 1.00 42.67 ? 71 GLN A CB 1 ATOM 536 C CG . GLN A 1 69 ? -24.065 -51.430 -29.783 1.00 47.89 ? 71 GLN A CG 1 ATOM 537 C CD . GLN A 1 69 ? -23.327 -52.564 -30.517 1.00 50.33 ? 71 GLN A CD 1 ATOM 538 O OE1 . GLN A 1 69 ? -23.866 -53.663 -30.664 0.50 50.57 ? 71 GLN A OE1 1 ATOM 539 N NE2 . GLN A 1 69 ? -22.099 -52.286 -30.985 0.50 46.97 ? 71 GLN A NE2 1 ATOM 540 N N . SER A 1 70 ? -24.786 -50.669 -25.117 1.00 40.18 ? 72 SER A N 1 ATOM 541 C CA . SER A 1 70 ? -24.955 -51.247 -23.770 1.00 41.04 ? 72 SER A CA 1 ATOM 542 C C . SER A 1 70 ? -26.405 -51.222 -23.296 1.00 40.51 ? 72 SER A C 1 ATOM 543 O O . SER A 1 70 ? -26.775 -52.090 -22.550 1.00 41.95 ? 72 SER A O 1 ATOM 544 C CB . SER A 1 70 ? -24.036 -50.566 -22.709 1.00 40.79 ? 72 SER A CB 1 ATOM 545 O OG . SER A 1 70 ? -22.733 -50.329 -23.231 1.00 42.10 ? 72 SER A OG 1 ATOM 546 N N . PHE A 1 71 ? -27.222 -50.245 -23.710 1.00 37.85 ? 73 PHE A N 1 ATOM 547 C CA . PHE A 1 71 ? -28.629 -50.225 -23.252 1.00 37.92 ? 73 PHE A CA 1 ATOM 548 C C . PHE A 1 71 ? -29.611 -49.994 -24.397 1.00 37.10 ? 73 PHE A C 1 ATOM 549 O O . PHE A 1 71 ? -30.206 -48.921 -24.474 1.00 36.62 ? 73 PHE A O 1 ATOM 550 C CB . PHE A 1 71 ? -28.807 -49.112 -22.190 1.00 37.34 ? 73 PHE A CB 1 ATOM 551 C CG . PHE A 1 71 ? -27.826 -49.215 -21.054 1.00 34.99 ? 73 PHE A CG 1 ATOM 552 C CD1 . PHE A 1 71 ? -27.990 -50.227 -20.067 1.00 36.82 ? 73 PHE A CD1 1 ATOM 553 C CD2 . PHE A 1 71 ? -26.736 -48.378 -20.987 1.00 28.24 ? 73 PHE A CD2 1 ATOM 554 C CE1 . PHE A 1 71 ? -27.106 -50.373 -19.002 1.00 35.02 ? 73 PHE A CE1 1 ATOM 555 C CE2 . PHE A 1 71 ? -25.812 -48.531 -19.921 1.00 30.54 ? 73 PHE A CE2 1 ATOM 556 C CZ . PHE A 1 71 ? -26.002 -49.519 -18.919 1.00 29.83 ? 73 PHE A CZ 1 ATOM 557 N N . PRO A 1 72 ? -29.741 -50.965 -25.321 1.00 36.47 ? 74 PRO A N 1 ATOM 558 C CA . PRO A 1 72 ? -30.596 -50.696 -26.496 1.00 35.90 ? 74 PRO A CA 1 ATOM 559 C C . PRO A 1 72 ? -32.028 -50.388 -26.045 1.00 36.09 ? 74 PRO A C 1 ATOM 560 O O . PRO A 1 72 ? -32.515 -50.999 -25.102 1.00 36.01 ? 74 PRO A O 1 ATOM 561 C CB . PRO A 1 72 ? -30.590 -52.011 -27.281 1.00 36.29 ? 74 PRO A CB 1 ATOM 562 C CG . PRO A 1 72 ? -29.628 -52.911 -26.588 1.00 37.56 ? 74 PRO A CG 1 ATOM 563 C CD . PRO A 1 72 ? -29.214 -52.337 -25.266 1.00 36.20 ? 74 PRO A CD 1 ATOM 564 N N . GLY A 1 73 ? -32.668 -49.427 -26.705 1.00 35.86 ? 75 GLY A N 1 ATOM 565 C CA . GLY A 1 73 ? -34.046 -48.998 -26.382 1.00 36.39 ? 75 GLY A CA 1 ATOM 566 C C . GLY A 1 73 ? -34.140 -47.978 -25.248 1.00 35.56 ? 75 GLY A C 1 ATOM 567 O O . GLY A 1 73 ? -35.228 -47.571 -24.889 1.00 36.04 ? 75 GLY A O 1 ATOM 568 N N . PHE A 1 74 ? -33.006 -47.606 -24.658 1.00 33.43 ? 76 PHE A N 1 ATOM 569 C CA . PHE A 1 74 ? -33.009 -46.774 -23.456 1.00 33.26 ? 76 PHE A CA 1 ATOM 570 C C . PHE A 1 74 ? -32.560 -45.396 -23.859 1.00 32.42 ? 76 PHE A C 1 ATOM 571 O O . PHE A 1 74 ? -31.505 -45.242 -24.400 1.00 31.40 ? 76 PHE A O 1 ATOM 572 C CB . PHE A 1 74 ? -32.062 -47.321 -22.366 1.00 31.95 ? 76 PHE A CB 1 ATOM 573 C CG . PHE A 1 74 ? -31.956 -46.437 -21.155 1.00 28.71 ? 76 PHE A CG 1 ATOM 574 C CD1 . PHE A 1 74 ? -33.095 -46.069 -20.417 1.00 28.91 ? 76 PHE A CD1 1 ATOM 575 C CD2 . PHE A 1 74 ? -30.738 -45.969 -20.750 1.00 26.04 ? 76 PHE A CD2 1 ATOM 576 C CE1 . PHE A 1 74 ? -32.982 -45.218 -19.317 1.00 27.83 ? 76 PHE A CE1 1 ATOM 577 C CE2 . PHE A 1 74 ? -30.608 -45.172 -19.647 1.00 28.22 ? 76 PHE A CE2 1 ATOM 578 C CZ . PHE A 1 74 ? -31.738 -44.796 -18.928 1.00 27.52 ? 76 PHE A CZ 1 ATOM 579 N N . HIS A 1 75 ? -33.397 -44.405 -23.600 1.00 33.70 ? 77 HIS A N 1 ATOM 580 C CA . HIS A 1 75 ? -33.167 -43.022 -24.063 1.00 32.93 ? 77 HIS A CA 1 ATOM 581 C C . HIS A 1 75 ? -31.946 -42.383 -23.406 1.00 32.07 ? 77 HIS A C 1 ATOM 582 O O . HIS A 1 75 ? -31.289 -41.500 -23.992 1.00 30.96 ? 77 HIS A O 1 ATOM 583 C CB . HIS A 1 75 ? -34.463 -42.187 -23.816 1.00 32.39 ? 77 HIS A CB 1 ATOM 584 C CG . HIS A 1 75 ? -34.367 -40.800 -24.346 1.00 36.95 ? 77 HIS A CG 1 ATOM 585 N ND1 . HIS A 1 75 ? -34.109 -40.530 -25.677 1.00 38.00 ? 77 HIS A ND1 1 ATOM 586 C CD2 . HIS A 1 75 ? -34.391 -39.596 -23.717 1.00 39.81 ? 77 HIS A CD2 1 ATOM 587 C CE1 . HIS A 1 75 ? -34.015 -39.222 -25.850 1.00 40.38 ? 77 HIS A CE1 1 ATOM 588 N NE2 . HIS A 1 75 ? -34.165 -38.632 -24.672 1.00 40.50 ? 77 HIS A NE2 1 ATOM 589 N N . GLY A 1 76 ? -31.616 -42.826 -22.186 1.00 32.06 ? 78 GLY A N 1 ATOM 590 C CA . GLY A 1 76 ? -30.499 -42.252 -21.481 1.00 30.85 ? 78 GLY A CA 1 ATOM 591 C C . GLY A 1 76 ? -29.214 -42.458 -22.255 1.00 31.91 ? 78 GLY A C 1 ATOM 592 O O . GLY A 1 76 ? -28.348 -41.563 -22.262 1.00 29.03 ? 78 GLY A O 1 ATOM 593 N N . SER A 1 77 ? -29.046 -43.627 -22.917 1.00 32.08 ? 79 SER A N 1 ATOM 594 C CA . SER A 1 77 ? -27.798 -43.795 -23.669 1.00 31.63 ? 79 SER A CA 1 ATOM 595 C C . SER A 1 77 ? -28.008 -43.426 -25.105 1.00 31.03 ? 79 SER A C 1 ATOM 596 O O . SER A 1 77 ? -27.148 -42.828 -25.726 1.00 28.60 ? 79 SER A O 1 ATOM 597 C CB . SER A 1 77 ? -27.259 -45.225 -23.602 1.00 32.01 ? 79 SER A CB 1 ATOM 598 O OG . SER A 1 77 ? -28.280 -46.153 -23.817 1.00 35.01 ? 79 SER A OG 1 ATOM 599 N N . GLU A 1 78 ? -29.141 -43.856 -25.640 1.00 30.89 ? 80 GLU A N 1 ATOM 600 C CA . GLU A 1 78 ? -29.393 -43.688 -27.052 1.00 31.84 ? 80 GLU A CA 1 ATOM 601 C C . GLU A 1 78 ? -29.499 -42.238 -27.523 1.00 31.34 ? 80 GLU A C 1 ATOM 602 O O . GLU A 1 78 ? -29.198 -41.943 -28.687 1.00 32.07 ? 80 GLU A O 1 ATOM 603 C CB . GLU A 1 78 ? -30.615 -44.489 -27.480 1.00 32.56 ? 80 GLU A CB 1 ATOM 604 C CG . GLU A 1 78 ? -30.260 -45.994 -27.612 1.00 35.16 ? 80 GLU A CG 1 ATOM 605 C CD . GLU A 1 78 ? -31.408 -46.840 -28.196 1.00 40.55 ? 80 GLU A CD 1 ATOM 606 O OE1 . GLU A 1 78 ? -31.206 -48.026 -28.517 1.00 39.41 ? 80 GLU A OE1 1 ATOM 607 O OE2 . GLU A 1 78 ? -32.539 -46.320 -28.281 1.00 46.63 ? 80 GLU A OE2 1 ATOM 608 N N . MET A 1 79 ? -29.922 -41.328 -26.649 1.00 30.33 ? 81 MET A N 1 ATOM 609 C CA . MET A 1 79 ? -29.933 -39.912 -27.017 1.00 29.68 ? 81 MET A CA 1 ATOM 610 C C . MET A 1 79 ? -28.556 -39.398 -27.504 1.00 29.20 ? 81 MET A C 1 ATOM 611 O O . MET A 1 79 ? -28.510 -38.301 -28.106 1.00 29.99 ? 81 MET A O 1 ATOM 612 C CB . MET A 1 79 ? -30.415 -39.023 -25.835 1.00 29.94 ? 81 MET A CB 1 ATOM 613 C CG . MET A 1 79 ? -29.488 -39.069 -24.620 1.00 31.61 ? 81 MET A CG 1 ATOM 614 S SD . MET A 1 79 ? -30.181 -38.140 -23.224 1.00 33.11 ? 81 MET A SD 1 ATOM 615 C CE . MET A 1 79 ? -29.704 -36.463 -23.802 1.00 27.94 ? 81 MET A CE 1 ATOM 616 N N . TRP A 1 80 ? -27.463 -40.135 -27.225 1.00 27.43 ? 82 TRP A N 1 ATOM 617 C CA . TRP A 1 80 ? -26.075 -39.699 -27.572 1.00 27.66 ? 82 TRP A CA 1 ATOM 618 C C . TRP A 1 80 ? -25.525 -40.347 -28.854 1.00 28.35 ? 82 TRP A C 1 ATOM 619 O O . TRP A 1 80 ? -24.509 -39.880 -29.425 1.00 27.96 ? 82 TRP A O 1 ATOM 620 C CB . TRP A 1 80 ? -25.051 -39.923 -26.410 1.00 26.36 ? 82 TRP A CB 1 ATOM 621 C CG . TRP A 1 80 ? -25.483 -39.302 -25.084 1.00 26.58 ? 82 TRP A CG 1 ATOM 622 C CD1 . TRP A 1 80 ? -26.012 -39.946 -23.995 1.00 28.23 ? 82 TRP A CD1 1 ATOM 623 C CD2 . TRP A 1 80 ? -25.482 -37.903 -24.754 1.00 24.22 ? 82 TRP A CD2 1 ATOM 624 N NE1 . TRP A 1 80 ? -26.332 -39.026 -22.996 1.00 23.81 ? 82 TRP A NE1 1 ATOM 625 C CE2 . TRP A 1 80 ? -26.001 -37.772 -23.453 1.00 25.79 ? 82 TRP A CE2 1 ATOM 626 C CE3 . TRP A 1 80 ? -25.039 -36.757 -25.420 1.00 20.40 ? 82 TRP A CE3 1 ATOM 627 C CZ2 . TRP A 1 80 ? -26.058 -36.535 -22.806 1.00 29.62 ? 82 TRP A CZ2 1 ATOM 628 C CZ3 . TRP A 1 80 ? -25.101 -35.569 -24.806 1.00 21.08 ? 82 TRP A CZ3 1 ATOM 629 C CH2 . TRP A 1 80 ? -25.625 -35.433 -23.513 1.00 27.71 ? 82 TRP A CH2 1 ATOM 630 N N . ASN A 1 81 ? -26.184 -41.427 -29.284 1.00 28.33 ? 83 ASN A N 1 ATOM 631 C CA . ASN A 1 81 ? -25.875 -42.082 -30.522 1.00 28.77 ? 83 ASN A CA 1 ATOM 632 C C . ASN A 1 81 ? -26.236 -41.216 -31.728 1.00 29.26 ? 83 ASN A C 1 ATOM 633 O O . ASN A 1 81 ? -27.168 -40.404 -31.667 1.00 30.59 ? 83 ASN A O 1 ATOM 634 C CB . ASN A 1 81 ? -26.645 -43.399 -30.573 1.00 29.15 ? 83 ASN A CB 1 ATOM 635 C CG . ASN A 1 81 ? -26.047 -44.425 -29.642 1.00 32.08 ? 83 ASN A CG 1 ATOM 636 O OD1 . ASN A 1 81 ? -24.865 -44.277 -29.197 1.00 29.34 ? 83 ASN A OD1 1 ATOM 637 N ND2 . ASN A 1 81 ? -26.825 -45.473 -29.319 1.00 30.66 ? 83 ASN A ND2 1 ATOM 638 N N . PRO A 1 82 ? -25.553 -41.431 -32.838 1.00 28.49 ? 84 PRO A N 1 ATOM 639 C CA . PRO A 1 82 ? -25.711 -40.600 -34.004 1.00 28.00 ? 84 PRO A CA 1 ATOM 640 C C . PRO A 1 82 ? -27.088 -40.773 -34.609 1.00 29.06 ? 84 PRO A C 1 ATOM 641 O O . PRO A 1 82 ? -27.585 -41.868 -34.595 1.00 28.52 ? 84 PRO A O 1 ATOM 642 C CB . PRO A 1 82 ? -24.652 -41.116 -34.981 1.00 28.27 ? 84 PRO A CB 1 ATOM 643 C CG . PRO A 1 82 ? -23.826 -42.065 -34.249 1.00 30.52 ? 84 PRO A CG 1 ATOM 644 C CD . PRO A 1 82 ? -24.362 -42.307 -32.874 1.00 29.22 ? 84 PRO A CD 1 ATOM 645 N N . ASN A 1 83 ? -27.696 -39.695 -35.126 1.00 29.31 ? 85 ASN A N 1 ATOM 646 C CA . ASN A 1 83 ? -29.071 -39.714 -35.664 1.00 30.37 ? 85 ASN A CA 1 ATOM 647 C C . ASN A 1 83 ? -29.084 -39.372 -37.143 1.00 31.40 ? 85 ASN A C 1 ATOM 648 O O . ASN A 1 83 ? -30.141 -39.012 -37.702 1.00 32.87 ? 85 ASN A O 1 ATOM 649 C CB . ASN A 1 83 ? -29.984 -38.724 -34.881 1.00 29.91 ? 85 ASN A CB 1 ATOM 650 C CG . ASN A 1 83 ? -29.435 -37.276 -34.887 1.00 30.66 ? 85 ASN A CG 1 ATOM 651 O OD1 . ASN A 1 83 ? -28.238 -37.026 -35.177 1.00 32.72 ? 85 ASN A OD1 1 ATOM 652 N ND2 . ASN A 1 83 ? -30.291 -36.323 -34.519 1.00 30.35 ? 85 ASN A ND2 1 ATOM 653 N N . THR A 1 84 ? -27.916 -39.404 -37.782 1.00 31.53 ? 86 THR A N 1 ATOM 654 C CA . THR A 1 84 ? -27.849 -39.414 -39.255 1.00 32.21 ? 86 THR A CA 1 ATOM 655 C C . THR A 1 84 ? -26.896 -40.544 -39.689 1.00 33.88 ? 86 THR A C 1 ATOM 656 O O . THR A 1 84 ? -26.096 -41.016 -38.851 1.00 35.40 ? 86 THR A O 1 ATOM 657 C CB . THR A 1 84 ? -27.325 -38.096 -39.797 1.00 33.10 ? 86 THR A CB 1 ATOM 658 O OG1 . THR A 1 84 ? -25.920 -37.984 -39.488 1.00 27.86 ? 86 THR A OG1 1 ATOM 659 C CG2 . THR A 1 84 ? -28.154 -36.915 -39.252 1.00 30.10 ? 86 THR A CG2 1 ATOM 660 N N . ASP A 1 85 ? -26.957 -40.957 -40.950 1.00 32.93 ? 87 ASP A N 1 ATOM 661 C CA . ASP A 1 85 ? -26.030 -41.938 -41.503 1.00 34.60 ? 87 ASP A CA 1 ATOM 662 C C . ASP A 1 85 ? -24.613 -41.695 -41.202 1.00 33.60 ? 87 ASP A C 1 ATOM 663 O O . ASP A 1 85 ? -24.168 -40.557 -41.259 1.00 33.20 ? 87 ASP A O 1 ATOM 664 C CB . ASP A 1 85 ? -26.078 -41.988 -43.028 1.00 35.74 ? 87 ASP A CB 1 ATOM 665 C CG . ASP A 1 85 ? -27.445 -42.305 -43.549 1.00 39.08 ? 87 ASP A CG 1 ATOM 666 O OD1 . ASP A 1 85 ? -27.703 -43.441 -43.893 1.00 36.76 ? 87 ASP A OD1 1 ATOM 667 O OD2 . ASP A 1 85 ? -28.273 -41.381 -43.628 1.00 50.10 ? 87 ASP A OD2 1 ATOM 668 N N . LEU A 1 86 ? -23.891 -42.791 -40.956 1.00 34.45 ? 88 LEU A N 1 ATOM 669 C CA . LEU A 1 86 ? -22.453 -42.757 -40.733 1.00 34.06 ? 88 LEU A CA 1 ATOM 670 C C . LEU A 1 86 ? -21.773 -42.832 -42.105 1.00 35.53 ? 88 LEU A C 1 ATOM 671 O O . LEU A 1 86 ? -22.159 -43.615 -42.956 1.00 37.32 ? 88 LEU A O 1 ATOM 672 C CB . LEU A 1 86 ? -22.040 -43.964 -39.851 1.00 33.68 ? 88 LEU A CB 1 ATOM 673 C CG . LEU A 1 86 ? -22.665 -44.083 -38.438 1.00 30.67 ? 88 LEU A CG 1 ATOM 674 C CD1 . LEU A 1 86 ? -21.782 -45.018 -37.602 1.00 26.40 ? 88 LEU A CD1 1 ATOM 675 C CD2 . LEU A 1 86 ? -22.700 -42.684 -37.785 1.00 27.86 ? 88 LEU A CD2 1 ATOM 676 N N . SER A 1 87 ? -20.757 -42.025 -42.332 1.00 35.68 ? 89 SER A N 1 ATOM 677 C CA . SER A 1 87 ? -20.018 -42.123 -43.569 1.00 35.93 ? 89 SER A CA 1 ATOM 678 C C . SER A 1 87 ? -18.666 -41.421 -43.311 1.00 35.98 ? 89 SER A C 1 ATOM 679 O O . SER A 1 87 ? -18.620 -40.467 -42.539 1.00 34.42 ? 89 SER A O 1 ATOM 680 C CB . SER A 1 87 ? -20.784 -41.320 -44.619 1.00 35.88 ? 89 SER A CB 1 ATOM 681 O OG . SER A 1 87 ? -19.997 -41.209 -45.788 1.00 35.63 ? 89 SER A OG 1 ATOM 682 N N . GLU A 1 88 ? -17.596 -41.839 -43.980 1.00 35.72 ? 90 GLU A N 1 ATOM 683 C CA . GLU A 1 88 ? -16.366 -40.993 -44.033 1.00 34.65 ? 90 GLU A CA 1 ATOM 684 C C . GLU A 1 88 ? -16.653 -39.603 -44.638 1.00 34.76 ? 90 GLU A C 1 ATOM 685 O O . GLU A 1 88 ? -15.951 -38.619 -44.362 1.00 32.66 ? 90 GLU A O 1 ATOM 686 C CB . GLU A 1 88 ? -15.245 -41.686 -44.831 1.00 34.93 ? 90 GLU A CB 1 ATOM 687 C CG . GLU A 1 88 ? -14.822 -42.980 -44.243 1.00 32.29 ? 90 GLU A CG 1 ATOM 688 C CD . GLU A 1 88 ? -13.577 -43.521 -44.926 1.00 37.01 ? 90 GLU A CD 1 ATOM 689 O OE1 . GLU A 1 88 ? -13.694 -44.370 -45.857 1.00 34.74 ? 90 GLU A OE1 1 ATOM 690 O OE2 . GLU A 1 88 ? -12.482 -43.094 -44.537 1.00 33.41 ? 90 GLU A OE2 1 ATOM 691 N N . ASP A 1 89 ? -17.720 -39.520 -45.427 1.00 34.78 ? 91 ASP A N 1 ATOM 692 C CA . ASP A 1 89 ? -18.057 -38.278 -46.047 1.00 35.59 ? 91 ASP A CA 1 ATOM 693 C C . ASP A 1 89 ? -18.907 -37.474 -45.039 1.00 34.17 ? 91 ASP A C 1 ATOM 694 O O . ASP A 1 89 ? -20.135 -37.535 -45.081 1.00 34.84 ? 91 ASP A O 1 ATOM 695 C CB . ASP A 1 89 ? -18.783 -38.533 -47.377 1.00 35.71 ? 91 ASP A CB 1 ATOM 696 C CG . ASP A 1 89 ? -19.243 -37.216 -48.052 1.00 39.91 ? 91 ASP A CG 1 ATOM 697 O OD1 . ASP A 1 89 ? -18.889 -36.085 -47.590 1.00 34.78 ? 91 ASP A OD1 1 ATOM 698 O OD2 . ASP A 1 89 ? -20.002 -37.322 -49.034 1.00 43.62 ? 91 ASP A OD2 1 ATOM 699 N N . CYS A 1 90 ? -18.256 -36.750 -44.115 1.00 32.59 ? 92 CYS A N 1 ATOM 700 C CA . CYS A 1 90 ? -18.971 -36.210 -42.948 1.00 30.62 ? 92 CYS A CA 1 ATOM 701 C C . CYS A 1 90 ? -18.499 -34.803 -42.576 1.00 29.74 ? 92 CYS A C 1 ATOM 702 O O . CYS A 1 90 ? -18.860 -34.274 -41.502 1.00 27.93 ? 92 CYS A O 1 ATOM 703 C CB . CYS A 1 90 ? -18.800 -37.171 -41.725 1.00 29.32 ? 92 CYS A CB 1 ATOM 704 S SG . CYS A 1 90 ? -17.053 -37.321 -41.183 1.00 30.96 ? 92 CYS A SG 1 ATOM 705 N N . LEU A 1 91 ? -17.717 -34.161 -43.444 1.00 29.67 ? 93 LEU A N 1 ATOM 706 C CA . LEU A 1 91 ? -17.134 -32.854 -43.019 1.00 28.42 ? 93 LEU A CA 1 ATOM 707 C C . LEU A 1 91 ? -18.098 -31.741 -43.417 1.00 28.11 ? 93 LEU A C 1 ATOM 708 O O . LEU A 1 91 ? -17.961 -31.086 -44.478 1.00 29.76 ? 93 LEU A O 1 ATOM 709 C CB . LEU A 1 91 ? -15.700 -32.673 -43.568 1.00 28.17 ? 93 LEU A CB 1 ATOM 710 C CG . LEU A 1 91 ? -14.596 -33.652 -43.090 1.00 31.54 ? 93 LEU A CG 1 ATOM 711 C CD1 . LEU A 1 91 ? -13.167 -33.290 -43.630 1.00 26.94 ? 93 LEU A CD1 1 ATOM 712 C CD2 . LEU A 1 91 ? -14.560 -33.745 -41.551 1.00 28.23 ? 93 LEU A CD2 1 ATOM 713 N N . TYR A 1 92 ? -19.086 -31.516 -42.563 1.00 26.53 ? 94 TYR A N 1 ATOM 714 C CA . TYR A 1 92 ? -20.155 -30.541 -42.832 1.00 25.81 ? 94 TYR A CA 1 ATOM 715 C C . TYR A 1 92 ? -20.374 -29.809 -41.530 1.00 25.74 ? 94 TYR A C 1 ATOM 716 O O . TYR A 1 92 ? -19.925 -30.261 -40.405 1.00 23.28 ? 94 TYR A O 1 ATOM 717 C CB . TYR A 1 92 ? -21.494 -31.249 -43.301 1.00 27.37 ? 94 TYR A CB 1 ATOM 718 C CG . TYR A 1 92 ? -21.300 -32.104 -44.585 1.00 29.00 ? 94 TYR A CG 1 ATOM 719 C CD1 . TYR A 1 92 ? -20.842 -33.435 -44.508 1.00 28.61 ? 94 TYR A CD1 1 ATOM 720 C CD2 . TYR A 1 92 ? -21.570 -31.575 -45.864 1.00 27.93 ? 94 TYR A CD2 1 ATOM 721 C CE1 . TYR A 1 92 ? -20.649 -34.219 -45.662 1.00 30.84 ? 94 TYR A CE1 1 ATOM 722 C CE2 . TYR A 1 92 ? -21.353 -32.343 -47.026 1.00 27.16 ? 94 TYR A CE2 1 ATOM 723 C CZ . TYR A 1 92 ? -20.869 -33.635 -46.923 1.00 32.35 ? 94 TYR A CZ 1 ATOM 724 O OH . TYR A 1 92 ? -20.631 -34.370 -48.065 1.00 37.92 ? 94 TYR A OH 1 ATOM 725 N N . LEU A 1 93 ? -21.079 -28.680 -41.670 1.00 25.59 ? 95 LEU A N 1 ATOM 726 C CA . LEU A 1 93 ? -21.383 -27.814 -40.564 1.00 25.23 ? 95 LEU A CA 1 ATOM 727 C C . LEU A 1 93 ? -22.811 -27.188 -40.765 1.00 26.75 ? 95 LEU A C 1 ATOM 728 O O . LEU A 1 93 ? -23.378 -27.252 -41.898 1.00 27.69 ? 95 LEU A O 1 ATOM 729 C CB . LEU A 1 93 ? -20.267 -26.788 -40.327 1.00 23.18 ? 95 LEU A CB 1 ATOM 730 C CG . LEU A 1 93 ? -20.021 -25.754 -41.438 1.00 26.27 ? 95 LEU A CG 1 ATOM 731 C CD1 . LEU A 1 93 ? -21.192 -24.669 -41.605 1.00 24.17 ? 95 LEU A CD1 1 ATOM 732 C CD2 . LEU A 1 93 ? -18.664 -25.058 -41.162 1.00 24.13 ? 95 LEU A CD2 1 ATOM 733 N N . ASN A 1 94 ? -23.374 -26.677 -39.656 1.00 25.77 ? 96 ASN A N 1 ATOM 734 C CA . ASN A 1 94 ? -24.704 -26.119 -39.549 1.00 27.42 ? 96 ASN A CA 1 ATOM 735 C C . ASN A 1 94 ? -24.585 -24.685 -39.122 1.00 27.63 ? 96 ASN A C 1 ATOM 736 O O . ASN A 1 94 ? -23.680 -24.338 -38.330 1.00 27.00 ? 96 ASN A O 1 ATOM 737 C CB . ASN A 1 94 ? -25.505 -26.889 -38.486 1.00 26.75 ? 96 ASN A CB 1 ATOM 738 C CG . ASN A 1 94 ? -25.340 -28.399 -38.667 1.00 29.22 ? 96 ASN A CG 1 ATOM 739 O OD1 . ASN A 1 94 ? -25.669 -28.934 -39.734 1.00 30.20 ? 96 ASN A OD1 1 ATOM 740 N ND2 . ASN A 1 94 ? -24.741 -29.070 -37.665 1.00 24.95 ? 96 ASN A ND2 1 ATOM 741 N N . VAL A 1 95 ? -25.497 -23.852 -39.637 1.00 28.82 ? 97 VAL A N 1 ATOM 742 C CA . VAL A 1 95 ? -25.543 -22.456 -39.231 1.00 28.08 ? 97 VAL A CA 1 ATOM 743 C C . VAL A 1 95 ? -26.980 -22.099 -38.872 1.00 29.42 ? 97 VAL A C 1 ATOM 744 O O . VAL A 1 95 ? -27.937 -22.416 -39.643 1.00 30.83 ? 97 VAL A O 1 ATOM 745 C CB . VAL A 1 95 ? -25.001 -21.512 -40.302 1.00 29.37 ? 97 VAL A CB 1 ATOM 746 C CG1 . VAL A 1 95 ? -24.975 -20.098 -39.718 1.00 26.72 ? 97 VAL A CG1 1 ATOM 747 C CG2 . VAL A 1 95 ? -23.546 -21.908 -40.783 1.00 25.88 ? 97 VAL A CG2 1 ATOM 748 N N . TRP A 1 96 ? -27.179 -21.556 -37.670 1.00 27.80 ? 98 TRP A N 1 ATOM 749 C CA . TRP A 1 96 ? -28.539 -21.076 -37.332 1.00 29.46 ? 98 TRP A CA 1 ATOM 750 C C . TRP A 1 96 ? -28.458 -19.582 -37.213 1.00 29.98 ? 98 TRP A C 1 ATOM 751 O O . TRP A 1 96 ? -27.586 -19.092 -36.482 1.00 30.33 ? 98 TRP A O 1 ATOM 752 C CB . TRP A 1 96 ? -29.036 -21.627 -36.021 1.00 26.81 ? 98 TRP A CB 1 ATOM 753 C CG . TRP A 1 96 ? -29.442 -23.097 -36.071 1.00 30.07 ? 98 TRP A CG 1 ATOM 754 C CD1 . TRP A 1 96 ? -30.705 -23.572 -36.337 1.00 27.45 ? 98 TRP A CD1 1 ATOM 755 C CD2 . TRP A 1 96 ? -28.646 -24.249 -35.735 1.00 26.49 ? 98 TRP A CD2 1 ATOM 756 N NE1 . TRP A 1 96 ? -30.727 -24.930 -36.230 1.00 29.69 ? 98 TRP A NE1 1 ATOM 757 C CE2 . TRP A 1 96 ? -29.490 -25.383 -35.863 1.00 29.69 ? 98 TRP A CE2 1 ATOM 758 C CE3 . TRP A 1 96 ? -27.304 -24.443 -35.394 1.00 26.17 ? 98 TRP A CE3 1 ATOM 759 C CZ2 . TRP A 1 96 ? -29.037 -26.692 -35.672 1.00 24.47 ? 98 TRP A CZ2 1 ATOM 760 C CZ3 . TRP A 1 96 ? -26.845 -25.766 -35.151 1.00 26.66 ? 98 TRP A CZ3 1 ATOM 761 C CH2 . TRP A 1 96 ? -27.706 -26.859 -35.275 1.00 25.74 ? 98 TRP A CH2 1 ATOM 762 N N . ILE A 1 97 ? -29.303 -18.862 -37.944 1.00 31.35 ? 99 ILE A N 1 ATOM 763 C CA . ILE A 1 97 ? -29.288 -17.401 -37.836 1.00 33.57 ? 99 ILE A CA 1 ATOM 764 C C . ILE A 1 97 ? -30.668 -16.870 -37.430 1.00 34.68 ? 99 ILE A C 1 ATOM 765 O O . ILE A 1 97 ? -31.711 -17.478 -37.777 1.00 35.39 ? 99 ILE A O 1 ATOM 766 C CB . ILE A 1 97 ? -28.682 -16.687 -39.103 1.00 33.04 ? 99 ILE A CB 1 ATOM 767 C CG1 . ILE A 1 97 ? -29.677 -16.617 -40.247 1.00 36.74 ? 99 ILE A CG1 1 ATOM 768 C CG2 . ILE A 1 97 ? -27.361 -17.419 -39.507 1.00 33.39 ? 99 ILE A CG2 1 ATOM 769 C CD1 . ILE A 1 97 ? -29.311 -15.617 -41.439 1.00 40.72 ? 99 ILE A CD1 1 ATOM 770 N N . PRO A 1 98 ? -30.677 -15.774 -36.660 1.00 34.88 ? 100 PRO A N 1 ATOM 771 C CA . PRO A 1 98 ? -31.945 -15.129 -36.325 1.00 37.09 ? 100 PRO A CA 1 ATOM 772 C C . PRO A 1 98 ? -32.644 -14.618 -37.625 1.00 39.38 ? 100 PRO A C 1 ATOM 773 O O . PRO A 1 98 ? -31.989 -14.417 -38.651 1.00 39.24 ? 100 PRO A O 1 ATOM 774 C CB . PRO A 1 98 ? -31.516 -13.967 -35.399 1.00 36.72 ? 100 PRO A CB 1 ATOM 775 C CG . PRO A 1 98 ? -30.041 -14.373 -34.923 1.00 35.41 ? 100 PRO A CG 1 ATOM 776 C CD . PRO A 1 98 ? -29.496 -15.085 -36.079 1.00 34.60 ? 100 PRO A CD 1 ATOM 777 N N . ALA A 1 99 ? -33.956 -14.466 -37.587 1.00 41.07 ? 101 ALA A N 1 ATOM 778 C CA . ALA A 1 99 ? -34.708 -13.846 -38.669 1.00 44.78 ? 101 ALA A CA 1 ATOM 779 C C . ALA A 1 99 ? -35.479 -12.704 -38.028 1.00 46.50 ? 101 ALA A C 1 ATOM 780 O O . ALA A 1 99 ? -36.076 -12.883 -36.982 1.00 47.10 ? 101 ALA A O 1 ATOM 781 C CB . ALA A 1 99 ? -35.669 -14.828 -39.314 1.00 44.67 ? 101 ALA A CB 1 ATOM 782 N N . PRO A 1 100 ? -35.414 -11.503 -38.608 1.00 48.05 ? 102 PRO A N 1 ATOM 783 C CA . PRO A 1 100 ? -34.625 -11.188 -39.792 1.00 47.99 ? 102 PRO A CA 1 ATOM 784 C C . PRO A 1 100 ? -33.138 -11.286 -39.523 1.00 46.28 ? 102 PRO A C 1 ATOM 785 O O . PRO A 1 100 ? -32.712 -11.105 -38.381 1.00 45.89 ? 102 PRO A O 1 ATOM 786 C CB . PRO A 1 100 ? -35.038 -9.750 -40.135 1.00 49.55 ? 102 PRO A CB 1 ATOM 787 C CG . PRO A 1 100 ? -35.702 -9.231 -38.936 1.00 50.26 ? 102 PRO A CG 1 ATOM 788 C CD . PRO A 1 100 ? -36.227 -10.366 -38.139 1.00 49.70 ? 102 PRO A CD 1 ATOM 789 N N . LYS A 1 101 ? -32.399 -11.626 -40.584 1.00 45.60 ? 103 LYS A N 1 ATOM 790 C CA . LYS A 1 101 ? -30.948 -11.614 -40.684 1.00 44.47 ? 103 LYS A CA 1 ATOM 791 C C . LYS A 1 101 ? -30.311 -10.522 -39.802 1.00 43.79 ? 103 LYS A C 1 ATOM 792 O O . LYS A 1 101 ? -30.586 -9.377 -39.972 1.00 44.16 ? 103 LYS A O 1 ATOM 793 C CB . LYS A 1 101 ? -30.595 -11.369 -42.144 1.00 46.00 ? 103 LYS A CB 1 ATOM 794 C CG . LYS A 1 101 ? -29.230 -11.841 -42.597 1.00 47.08 ? 103 LYS A CG 1 ATOM 795 C CD . LYS A 1 101 ? -28.790 -10.933 -43.749 1.00 53.71 ? 103 LYS A CD 1 ATOM 796 C CE . LYS A 1 101 ? -27.469 -11.372 -44.357 1.00 56.01 ? 103 LYS A CE 1 ATOM 797 N NZ . LYS A 1 101 ? -26.625 -10.129 -44.568 1.00 60.18 ? 103 LYS A NZ 1 ATOM 798 N N . PRO A 1 102 ? -29.470 -10.902 -38.841 1.00 41.74 ? 104 PRO A N 1 ATOM 799 C CA . PRO A 1 102 ? -28.883 -9.942 -37.963 1.00 41.57 ? 104 PRO A CA 1 ATOM 800 C C . PRO A 1 102 ? -27.891 -9.080 -38.776 1.00 43.38 ? 104 PRO A C 1 ATOM 801 O O . PRO A 1 102 ? -27.630 -9.374 -39.962 1.00 42.79 ? 104 PRO A O 1 ATOM 802 C CB . PRO A 1 102 ? -28.209 -10.835 -36.894 1.00 39.41 ? 104 PRO A CB 1 ATOM 803 C CG . PRO A 1 102 ? -27.797 -11.987 -37.632 1.00 37.99 ? 104 PRO A CG 1 ATOM 804 C CD . PRO A 1 102 ? -28.899 -12.239 -38.629 1.00 40.85 ? 104 PRO A CD 1 ATOM 805 N N . LYS A 1 103 ? -27.434 -7.976 -38.188 1.00 44.61 ? 105 LYS A N 1 ATOM 806 C CA . LYS A 1 103 ? -26.466 -7.111 -38.837 1.00 46.66 ? 105 LYS A CA 1 ATOM 807 C C . LYS A 1 103 ? -25.032 -7.486 -38.439 1.00 46.99 ? 105 LYS A C 1 ATOM 808 O O . LYS A 1 103 ? -24.150 -7.631 -39.322 1.00 49.49 ? 105 LYS A O 1 ATOM 809 C CB . LYS A 1 103 ? -26.769 -5.637 -38.614 1.00 47.75 ? 105 LYS A CB 1 ATOM 810 C CG . LYS A 1 103 ? -27.901 -5.144 -39.521 1.00 50.37 ? 105 LYS A CG 1 ATOM 811 C CD . LYS A 1 103 ? -27.514 -3.906 -40.319 1.00 57.34 ? 105 LYS A CD 1 ATOM 812 C CE . LYS A 1 103 ? -28.519 -3.594 -41.493 1.00 59.07 ? 105 LYS A CE 1 ATOM 813 N NZ . LYS A 1 103 ? -29.891 -3.835 -40.988 1.00 58.65 ? 105 LYS A NZ 1 ATOM 814 N N . ASN A 1 104 ? -24.751 -7.662 -37.157 1.00 44.09 ? 106 ASN A N 1 ATOM 815 C CA . ASN A 1 104 ? -23.374 -8.027 -36.857 1.00 43.22 ? 106 ASN A CA 1 ATOM 816 C C . ASN A 1 104 ? -23.329 -8.924 -35.603 1.00 38.79 ? 106 ASN A C 1 ATOM 817 O O . ASN A 1 104 ? -22.824 -8.543 -34.561 1.00 37.44 ? 106 ASN A O 1 ATOM 818 C CB . ASN A 1 104 ? -22.612 -6.726 -36.638 1.00 45.18 ? 106 ASN A CB 1 ATOM 819 C CG . ASN A 1 104 ? -21.138 -6.799 -37.016 1.00 52.49 ? 106 ASN A CG 1 ATOM 820 O OD1 . ASN A 1 104 ? -20.646 -7.727 -37.678 1.00 52.38 ? 106 ASN A OD1 1 ATOM 821 N ND2 . ASN A 1 104 ? -20.414 -5.771 -36.565 1.00 64.06 ? 106 ASN A ND2 1 ATOM 822 N N . ALA A 1 105 ? -23.927 -10.089 -35.714 1.00 35.36 ? 107 ALA A N 1 ATOM 823 C CA . ALA A 1 105 ? -24.220 -10.893 -34.543 1.00 33.85 ? 107 ALA A CA 1 ATOM 824 C C . ALA A 1 105 ? -22.974 -11.647 -34.058 1.00 32.45 ? 107 ALA A C 1 ATOM 825 O O . ALA A 1 105 ? -22.164 -12.180 -34.875 1.00 30.92 ? 107 ALA A O 1 ATOM 826 C CB . ALA A 1 105 ? -25.309 -11.876 -34.871 1.00 32.39 ? 107 ALA A CB 1 ATOM 827 N N . THR A 1 106 ? -22.838 -11.715 -32.739 1.00 31.27 ? 108 THR A N 1 ATOM 828 C CA . THR A 1 106 ? -21.890 -12.650 -32.128 1.00 28.49 ? 108 THR A CA 1 ATOM 829 C C . THR A 1 106 ? -22.188 -14.098 -32.567 1.00 29.24 ? 108 THR A C 1 ATOM 830 O O . THR A 1 106 ? -23.382 -14.492 -32.731 1.00 30.21 ? 108 THR A O 1 ATOM 831 C CB . THR A 1 106 ? -21.985 -12.504 -30.624 1.00 27.42 ? 108 THR A CB 1 ATOM 832 O OG1 . THR A 1 106 ? -21.336 -11.303 -30.290 1.00 29.26 ? 108 THR A OG1 1 ATOM 833 C CG2 . THR A 1 106 ? -21.284 -13.630 -29.834 1.00 24.99 ? 108 THR A CG2 1 ATOM 834 N N . VAL A 1 107 ? -21.117 -14.882 -32.680 1.00 27.76 ? 109 VAL A N 1 ATOM 835 C CA . VAL A 1 107 ? -21.156 -16.228 -33.175 1.00 27.98 ? 109 VAL A CA 1 ATOM 836 C C . VAL A 1 107 ? -20.716 -17.224 -32.065 1.00 27.05 ? 109 VAL A C 1 ATOM 837 O O . VAL A 1 107 ? -19.688 -17.020 -31.446 1.00 26.77 ? 109 VAL A O 1 ATOM 838 C CB . VAL A 1 107 ? -20.258 -16.400 -34.426 1.00 29.08 ? 109 VAL A CB 1 ATOM 839 C CG1 . VAL A 1 107 ? -20.368 -17.879 -35.000 1.00 25.67 ? 109 VAL A CG1 1 ATOM 840 C CG2 . VAL A 1 107 ? -20.680 -15.403 -35.518 1.00 29.14 ? 109 VAL A CG2 1 ATOM 841 N N . LEU A 1 108 ? -21.522 -18.266 -31.840 1.00 26.26 ? 110 LEU A N 1 ATOM 842 C CA . LEU A 1 108 ? -21.239 -19.326 -30.872 1.00 26.56 ? 110 LEU A CA 1 ATOM 843 C C . LEU A 1 108 ? -20.951 -20.590 -31.664 1.00 26.30 ? 110 LEU A C 1 ATOM 844 O O . LEU A 1 108 ? -21.768 -21.003 -32.532 1.00 25.74 ? 110 LEU A O 1 ATOM 845 C CB . LEU A 1 108 ? -22.455 -19.487 -29.941 1.00 26.37 ? 110 LEU A CB 1 ATOM 846 C CG . LEU A 1 108 ? -22.436 -18.521 -28.752 1.00 31.96 ? 110 LEU A CG 1 ATOM 847 C CD1 . LEU A 1 108 ? -23.747 -18.586 -28.078 1.00 36.15 ? 110 LEU A CD1 1 ATOM 848 C CD2 . LEU A 1 108 ? -21.380 -19.095 -27.772 1.00 36.48 ? 110 LEU A CD2 1 ATOM 849 N N . ILE A 1 109 ? -19.775 -21.200 -31.454 1.00 25.43 ? 111 ILE A N 1 ATOM 850 C CA . ILE A 1 109 ? -19.436 -22.385 -32.279 1.00 23.01 ? 111 ILE A CA 1 ATOM 851 C C . ILE A 1 109 ? -19.310 -23.559 -31.377 1.00 22.23 ? 111 ILE A C 1 ATOM 852 O O . ILE A 1 109 ? -18.439 -23.538 -30.485 1.00 21.76 ? 111 ILE A O 1 ATOM 853 C CB . ILE A 1 109 ? -18.110 -22.199 -33.053 1.00 24.71 ? 111 ILE A CB 1 ATOM 854 C CG1 . ILE A 1 109 ? -18.189 -20.932 -33.945 1.00 23.95 ? 111 ILE A CG1 1 ATOM 855 C CG2 . ILE A 1 109 ? -17.744 -23.528 -33.795 1.00 20.52 ? 111 ILE A CG2 1 ATOM 856 C CD1 . ILE A 1 109 ? -16.944 -20.725 -34.847 1.00 25.66 ? 111 ILE A CD1 1 ATOM 857 N N . TRP A 1 110 ? -20.188 -24.553 -31.572 1.00 20.41 ? 112 TRP A N 1 ATOM 858 C CA . TRP A 1 110 ? -20.269 -25.688 -30.666 1.00 20.77 ? 112 TRP A CA 1 ATOM 859 C C . TRP A 1 110 ? -19.347 -26.825 -31.133 1.00 21.89 ? 112 TRP A C 1 ATOM 860 O O . TRP A 1 110 ? -19.360 -27.181 -32.316 1.00 23.59 ? 112 TRP A O 1 ATOM 861 C CB . TRP A 1 110 ? -21.702 -26.217 -30.656 1.00 21.16 ? 112 TRP A CB 1 ATOM 862 C CG . TRP A 1 110 ? -21.880 -27.500 -29.819 1.00 20.52 ? 112 TRP A CG 1 ATOM 863 C CD1 . TRP A 1 110 ? -22.092 -28.768 -30.291 1.00 20.85 ? 112 TRP A CD1 1 ATOM 864 C CD2 . TRP A 1 110 ? -21.776 -27.614 -28.373 1.00 19.01 ? 112 TRP A CD2 1 ATOM 865 N NE1 . TRP A 1 110 ? -22.190 -29.652 -29.226 1.00 22.77 ? 112 TRP A NE1 1 ATOM 866 C CE2 . TRP A 1 110 ? -22.001 -28.964 -28.045 1.00 22.97 ? 112 TRP A CE2 1 ATOM 867 C CE3 . TRP A 1 110 ? -21.579 -26.681 -27.331 1.00 19.92 ? 112 TRP A CE3 1 ATOM 868 C CZ2 . TRP A 1 110 ? -22.046 -29.410 -26.714 1.00 19.30 ? 112 TRP A CZ2 1 ATOM 869 C CZ3 . TRP A 1 110 ? -21.611 -27.097 -26.045 1.00 19.11 ? 112 TRP A CZ3 1 ATOM 870 C CH2 . TRP A 1 110 ? -21.808 -28.468 -25.731 1.00 21.78 ? 112 TRP A CH2 1 ATOM 871 N N . ILE A 1 111 ? -18.555 -27.398 -30.239 1.00 21.33 ? 113 ILE A N 1 ATOM 872 C CA . ILE A 1 111 ? -17.733 -28.559 -30.562 1.00 21.09 ? 113 ILE A CA 1 ATOM 873 C C . ILE A 1 111 ? -18.211 -29.687 -29.639 1.00 21.91 ? 113 ILE A C 1 ATOM 874 O O . ILE A 1 111 ? -17.982 -29.616 -28.408 1.00 21.29 ? 113 ILE A O 1 ATOM 875 C CB . ILE A 1 111 ? -16.194 -28.273 -30.374 1.00 20.34 ? 113 ILE A CB 1 ATOM 876 C CG1 . ILE A 1 111 ? -15.731 -27.062 -31.249 1.00 22.19 ? 113 ILE A CG1 1 ATOM 877 C CG2 . ILE A 1 111 ? -15.424 -29.524 -30.793 1.00 18.88 ? 113 ILE A CG2 1 ATOM 878 C CD1 . ILE A 1 111 ? -14.307 -26.614 -30.987 1.00 20.51 ? 113 ILE A CD1 1 ATOM 879 N N . TYR A 1 112 ? -18.863 -30.729 -30.202 1.00 22.72 ? 114 TYR A N 1 ATOM 880 C CA . TYR A 1 112 ? -19.412 -31.843 -29.374 1.00 21.48 ? 114 TYR A CA 1 ATOM 881 C C . TYR A 1 112 ? -18.300 -32.703 -28.739 1.00 22.23 ? 114 TYR A C 1 ATOM 882 O O . TYR A 1 112 ? -17.146 -32.778 -29.256 1.00 20.75 ? 114 TYR A O 1 ATOM 883 C CB . TYR A 1 112 ? -20.359 -32.723 -30.207 1.00 21.03 ? 114 TYR A CB 1 ATOM 884 C CG . TYR A 1 112 ? -19.718 -33.362 -31.442 1.00 20.92 ? 114 TYR A CG 1 ATOM 885 C CD1 . TYR A 1 112 ? -18.816 -34.470 -31.344 1.00 18.51 ? 114 TYR A CD1 1 ATOM 886 C CD2 . TYR A 1 112 ? -20.031 -32.893 -32.699 1.00 20.07 ? 114 TYR A CD2 1 ATOM 887 C CE1 . TYR A 1 112 ? -18.246 -35.037 -32.501 1.00 22.17 ? 114 TYR A CE1 1 ATOM 888 C CE2 . TYR A 1 112 ? -19.476 -33.452 -33.850 1.00 22.89 ? 114 TYR A CE2 1 ATOM 889 C CZ . TYR A 1 112 ? -18.623 -34.514 -33.765 1.00 23.66 ? 114 TYR A CZ 1 ATOM 890 O OH . TYR A 1 112 ? -18.103 -34.956 -34.967 1.00 27.33 ? 114 TYR A OH 1 ATOM 891 N N . GLY A 1 113 ? -18.650 -33.389 -27.642 1.00 22.95 ? 115 GLY A N 1 ATOM 892 C CA . GLY A 1 113 ? -17.762 -34.423 -27.080 1.00 23.95 ? 115 GLY A CA 1 ATOM 893 C C . GLY A 1 113 ? -18.183 -35.848 -27.544 1.00 25.31 ? 115 GLY A C 1 ATOM 894 O O . GLY A 1 113 ? -18.945 -36.012 -28.509 1.00 26.88 ? 115 GLY A O 1 ATOM 895 N N . GLY A 1 114 ? -17.679 -36.879 -26.866 1.00 25.33 ? 116 GLY A N 1 ATOM 896 C CA . GLY A 1 114 ? -17.874 -38.257 -27.300 1.00 25.47 ? 116 GLY A CA 1 ATOM 897 C C . GLY A 1 114 ? -16.497 -38.948 -27.146 1.00 26.85 ? 116 GLY A C 1 ATOM 898 O O . GLY A 1 114 ? -16.177 -39.913 -27.860 1.00 26.78 ? 116 GLY A O 1 ATOM 899 N N . GLY A 1 115 ? -15.616 -38.407 -26.286 1.00 26.14 ? 117 GLY A N 1 ATOM 900 C CA . GLY A 1 115 ? -14.349 -39.112 -26.029 1.00 24.20 ? 117 GLY A CA 1 ATOM 901 C C . GLY A 1 115 ? -13.368 -39.030 -27.204 1.00 23.57 ? 117 GLY A C 1 ATOM 902 O O . GLY A 1 115 ? -12.400 -39.778 -27.231 1.00 23.89 ? 117 GLY A O 1 ATOM 903 N N . PHE A 1 116 ? -13.637 -38.162 -28.199 1.00 22.17 ? 118 PHE A N 1 ATOM 904 C CA . PHE A 1 116 ? -12.863 -38.176 -29.461 1.00 23.53 ? 118 PHE A CA 1 ATOM 905 C C . PHE A 1 116 ? -13.083 -39.500 -30.243 1.00 24.52 ? 118 PHE A C 1 ATOM 906 O O . PHE A 1 116 ? -12.352 -39.739 -31.215 1.00 25.08 ? 118 PHE A O 1 ATOM 907 C CB . PHE A 1 116 ? -11.330 -37.980 -29.226 1.00 22.60 ? 118 PHE A CB 1 ATOM 908 C CG . PHE A 1 116 ? -10.962 -36.660 -28.589 1.00 23.65 ? 118 PHE A CG 1 ATOM 909 C CD1 . PHE A 1 116 ? -11.085 -35.463 -29.314 1.00 21.11 ? 118 PHE A CD1 1 ATOM 910 C CD2 . PHE A 1 116 ? -10.479 -36.615 -27.245 1.00 22.92 ? 118 PHE A CD2 1 ATOM 911 C CE1 . PHE A 1 116 ? -10.724 -34.182 -28.714 1.00 22.93 ? 118 PHE A CE1 1 ATOM 912 C CE2 . PHE A 1 116 ? -10.089 -35.379 -26.660 1.00 25.13 ? 118 PHE A CE2 1 ATOM 913 C CZ . PHE A 1 116 ? -10.234 -34.146 -27.403 1.00 22.66 ? 118 PHE A CZ 1 ATOM 914 N N . GLN A 1 117 ? -14.055 -40.343 -29.821 1.00 22.73 ? 119 GLN A N 1 ATOM 915 C CA . GLN A 1 117 ? -14.285 -41.607 -30.530 1.00 25.17 ? 119 GLN A CA 1 ATOM 916 C C . GLN A 1 117 ? -15.655 -41.543 -31.190 1.00 25.48 ? 119 GLN A C 1 ATOM 917 O O . GLN A 1 117 ? -15.909 -42.309 -32.130 1.00 27.17 ? 119 GLN A O 1 ATOM 918 C CB . GLN A 1 117 ? -14.214 -42.854 -29.618 1.00 24.40 ? 119 GLN A CB 1 ATOM 919 C CG . GLN A 1 117 ? -13.023 -42.939 -28.599 1.00 29.93 ? 119 GLN A CG 1 ATOM 920 C CD . GLN A 1 117 ? -11.664 -42.748 -29.279 1.00 32.58 ? 119 GLN A CD 1 ATOM 921 O OE1 . GLN A 1 117 ? -11.284 -43.543 -30.124 1.00 35.96 ? 119 GLN A OE1 1 ATOM 922 N NE2 . GLN A 1 117 ? -10.982 -41.635 -28.980 1.00 35.15 ? 119 GLN A NE2 1 ATOM 923 N N . THR A 1 118 ? -16.523 -40.653 -30.700 1.00 24.47 ? 120 THR A N 1 ATOM 924 C CA . THR A 1 118 ? -17.915 -40.617 -31.048 1.00 24.59 ? 120 THR A CA 1 ATOM 925 C C . THR A 1 118 ? -18.432 -39.154 -31.051 1.00 25.13 ? 120 THR A C 1 ATOM 926 O O . THR A 1 118 ? -17.700 -38.212 -30.613 1.00 24.34 ? 120 THR A O 1 ATOM 927 C CB . THR A 1 118 ? -18.845 -41.477 -30.070 1.00 26.83 ? 120 THR A CB 1 ATOM 928 O OG1 . THR A 1 118 ? -18.876 -40.875 -28.751 1.00 26.85 ? 120 THR A OG1 1 ATOM 929 C CG2 . THR A 1 118 ? -18.438 -42.990 -30.017 1.00 23.77 ? 120 THR A CG2 1 ATOM 930 N N . GLY A 1 119 ? -19.677 -38.976 -31.520 1.00 22.99 ? 121 GLY A N 1 ATOM 931 C CA . GLY A 1 119 ? -20.356 -37.719 -31.428 1.00 23.72 ? 121 GLY A CA 1 ATOM 932 C C . GLY A 1 119 ? -20.796 -37.231 -32.808 1.00 24.22 ? 121 GLY A C 1 ATOM 933 O O . GLY A 1 119 ? -20.314 -37.706 -33.867 1.00 23.73 ? 121 GLY A O 1 ATOM 934 N N . THR A 1 120 ? -21.753 -36.338 -32.796 1.00 22.32 ? 122 THR A N 1 ATOM 935 C CA . THR A 1 120 ? -22.161 -35.727 -34.026 1.00 25.21 ? 122 THR A CA 1 ATOM 936 C C . THR A 1 120 ? -22.846 -34.400 -33.684 1.00 25.32 ? 122 THR A C 1 ATOM 937 O O . THR A 1 120 ? -23.387 -34.243 -32.552 1.00 24.94 ? 122 THR A O 1 ATOM 938 C CB . THR A 1 120 ? -23.109 -36.668 -34.850 1.00 25.99 ? 122 THR A CB 1 ATOM 939 O OG1 . THR A 1 120 ? -23.476 -36.044 -36.094 1.00 27.42 ? 122 THR A OG1 1 ATOM 940 C CG2 . THR A 1 120 ? -24.379 -37.045 -34.040 1.00 22.48 ? 122 THR A CG2 1 ATOM 941 N N . SER A 1 121 ? -22.788 -33.435 -34.603 1.00 25.79 ? 123 SER A N 1 ATOM 942 C CA . SER A 1 121 ? -23.403 -32.134 -34.324 1.00 25.82 ? 123 SER A CA 1 ATOM 943 C C . SER A 1 121 ? -24.927 -32.087 -34.436 1.00 26.94 ? 123 SER A C 1 ATOM 944 O O . SER A 1 121 ? -25.533 -31.093 -34.060 1.00 27.01 ? 123 SER A O 1 ATOM 945 C CB . SER A 1 121 ? -22.774 -31.039 -35.183 1.00 26.40 ? 123 SER A CB 1 ATOM 946 O OG . SER A 1 121 ? -23.062 -31.288 -36.529 1.00 27.85 ? 123 SER A OG 1 ATOM 947 N N . SER A 1 122 ? -25.551 -33.144 -34.974 1.00 27.76 ? 124 SER A N 1 ATOM 948 C CA . SER A 1 122 ? -26.989 -33.148 -35.195 1.00 27.61 ? 124 SER A CA 1 ATOM 949 C C . SER A 1 122 ? -27.858 -33.673 -34.037 1.00 27.24 ? 124 SER A C 1 ATOM 950 O O . SER A 1 122 ? -29.053 -33.790 -34.191 1.00 28.32 ? 124 SER A O 1 ATOM 951 C CB . SER A 1 122 ? -27.325 -33.988 -36.457 1.00 29.44 ? 124 SER A CB 1 ATOM 952 O OG . SER A 1 122 ? -26.661 -35.242 -36.447 1.00 28.63 ? 124 SER A OG 1 ATOM 953 N N . LEU A 1 123 ? -27.301 -34.005 -32.899 1.00 25.62 ? 125 LEU A N 1 ATOM 954 C CA . LEU A 1 123 ? -28.149 -34.430 -31.802 1.00 26.14 ? 125 LEU A CA 1 ATOM 955 C C . LEU A 1 123 ? -29.104 -33.290 -31.430 1.00 27.97 ? 125 LEU A C 1 ATOM 956 O O . LEU A 1 123 ? -28.788 -32.098 -31.506 1.00 27.27 ? 125 LEU A O 1 ATOM 957 C CB . LEU A 1 123 ? -27.335 -34.860 -30.556 1.00 26.04 ? 125 LEU A CB 1 ATOM 958 C CG . LEU A 1 123 ? -26.225 -35.911 -30.733 1.00 25.50 ? 125 LEU A CG 1 ATOM 959 C CD1 . LEU A 1 123 ? -25.530 -36.124 -29.418 1.00 21.82 ? 125 LEU A CD1 1 ATOM 960 C CD2 . LEU A 1 123 ? -26.930 -37.250 -31.306 1.00 22.28 ? 125 LEU A CD2 1 ATOM 961 N N . HIS A 1 124 ? -30.277 -33.714 -31.019 1.00 28.21 ? 126 HIS A N 1 ATOM 962 C CA . HIS A 1 124 ? -31.324 -32.890 -30.504 1.00 29.85 ? 126 HIS A CA 1 ATOM 963 C C . HIS A 1 124 ? -30.831 -31.872 -29.414 1.00 28.64 ? 126 HIS A C 1 ATOM 964 O O . HIS A 1 124 ? -31.321 -30.732 -29.356 1.00 28.99 ? 126 HIS A O 1 ATOM 965 C CB . HIS A 1 124 ? -32.469 -33.865 -29.985 1.00 29.46 ? 126 HIS A CB 1 ATOM 966 C CG . HIS A 1 124 ? -33.618 -33.170 -29.346 1.00 38.40 ? 126 HIS A CG 1 ATOM 967 N ND1 . HIS A 1 124 ? -34.372 -32.216 -30.011 1.00 47.92 ? 126 HIS A ND1 1 ATOM 968 C CD2 . HIS A 1 124 ? -34.152 -33.273 -28.103 1.00 42.89 ? 126 HIS A CD2 1 ATOM 969 C CE1 . HIS A 1 124 ? -35.306 -31.750 -29.200 1.00 49.46 ? 126 HIS A CE1 1 ATOM 970 N NE2 . HIS A 1 124 ? -35.213 -32.396 -28.048 1.00 50.43 ? 126 HIS A NE2 1 ATOM 971 N N . VAL A 1 125 ? -29.954 -32.313 -28.517 1.00 27.02 ? 127 VAL A N 1 ATOM 972 C CA . VAL A 1 125 ? -29.534 -31.493 -27.390 1.00 26.13 ? 127 VAL A CA 1 ATOM 973 C C . VAL A 1 125 ? -28.563 -30.449 -27.840 1.00 26.88 ? 127 VAL A C 1 ATOM 974 O O . VAL A 1 125 ? -28.245 -29.543 -27.059 1.00 28.15 ? 127 VAL A O 1 ATOM 975 C CB . VAL A 1 125 ? -29.006 -32.319 -26.144 1.00 26.31 ? 127 VAL A CB 1 ATOM 976 C CG1 . VAL A 1 125 ? -30.200 -33.129 -25.528 1.00 25.59 ? 127 VAL A CG1 1 ATOM 977 C CG2 . VAL A 1 125 ? -27.767 -33.272 -26.474 1.00 20.97 ? 127 VAL A CG2 1 ATOM 978 N N . TYR A 1 126 ? -28.134 -30.510 -29.108 1.00 26.34 ? 128 TYR A N 1 ATOM 979 C CA . TYR A 1 126 ? -27.206 -29.484 -29.671 1.00 24.91 ? 128 TYR A CA 1 ATOM 980 C C . TYR A 1 126 ? -27.894 -28.558 -30.716 1.00 25.51 ? 128 TYR A C 1 ATOM 981 O O . TYR A 1 126 ? -27.218 -27.833 -31.494 1.00 24.13 ? 128 TYR A O 1 ATOM 982 C CB . TYR A 1 126 ? -25.974 -30.129 -30.346 1.00 23.24 ? 128 TYR A CB 1 ATOM 983 C CG . TYR A 1 126 ? -25.177 -31.159 -29.545 1.00 21.54 ? 128 TYR A CG 1 ATOM 984 C CD1 . TYR A 1 126 ? -25.095 -31.121 -28.138 1.00 21.39 ? 128 TYR A CD1 1 ATOM 985 C CD2 . TYR A 1 126 ? -24.454 -32.143 -30.209 1.00 17.36 ? 128 TYR A CD2 1 ATOM 986 C CE1 . TYR A 1 126 ? -24.329 -32.076 -27.434 1.00 20.30 ? 128 TYR A CE1 1 ATOM 987 C CE2 . TYR A 1 126 ? -23.672 -33.081 -29.527 1.00 17.68 ? 128 TYR A CE2 1 ATOM 988 C CZ . TYR A 1 126 ? -23.615 -33.058 -28.169 1.00 20.86 ? 128 TYR A CZ 1 ATOM 989 O OH . TYR A 1 126 ? -22.839 -34.016 -27.546 1.00 21.52 ? 128 TYR A OH 1 ATOM 990 N N . ASP A 1 127 ? -29.210 -28.614 -30.768 1.00 25.26 ? 129 ASP A N 1 ATOM 991 C CA . ASP A 1 127 ? -29.947 -27.855 -31.788 1.00 26.94 ? 129 ASP A CA 1 ATOM 992 C C . ASP A 1 127 ? -29.818 -26.357 -31.457 1.00 26.67 ? 129 ASP A C 1 ATOM 993 O O . ASP A 1 127 ? -30.352 -25.884 -30.437 1.00 25.22 ? 129 ASP A O 1 ATOM 994 C CB . ASP A 1 127 ? -31.407 -28.261 -31.730 1.00 27.30 ? 129 ASP A CB 1 ATOM 995 C CG . ASP A 1 127 ? -32.221 -27.778 -32.927 1.00 32.86 ? 129 ASP A CG 1 ATOM 996 O OD1 . ASP A 1 127 ? -31.897 -26.718 -33.519 1.00 32.51 ? 129 ASP A OD1 1 ATOM 997 O OD2 . ASP A 1 127 ? -33.241 -28.456 -33.237 1.00 34.44 ? 129 ASP A OD2 1 ATOM 998 N N . GLY A 1 128 ? -29.121 -25.604 -32.308 1.00 26.12 ? 130 GLY A N 1 ATOM 999 C CA . GLY A 1 128 ? -28.919 -24.208 -31.998 1.00 25.81 ? 130 GLY A CA 1 ATOM 1000 C C . GLY A 1 128 ? -30.056 -23.236 -32.291 1.00 29.43 ? 130 GLY A C 1 ATOM 1001 O O . GLY A 1 128 ? -29.885 -22.000 -32.117 1.00 29.73 ? 130 GLY A O 1 ATOM 1002 N N . LYS A 1 129 ? -31.227 -23.738 -32.687 1.00 28.87 ? 131 LYS A N 1 ATOM 1003 C CA . LYS A 1 129 ? -32.297 -22.819 -33.037 1.00 31.27 ? 131 LYS A CA 1 ATOM 1004 C C . LYS A 1 129 ? -32.856 -21.976 -31.853 1.00 31.18 ? 131 LYS A C 1 ATOM 1005 O O . LYS A 1 129 ? -33.405 -20.901 -32.059 1.00 32.00 ? 131 LYS A O 1 ATOM 1006 C CB . LYS A 1 129 ? -33.448 -23.564 -33.751 1.00 31.23 ? 131 LYS A CB 1 ATOM 1007 C CG . LYS A 1 129 ? -34.269 -24.456 -32.853 1.00 32.47 ? 131 LYS A CG 1 ATOM 1008 C CD . LYS A 1 129 ? -35.291 -25.272 -33.709 1.00 34.69 ? 131 LYS A CD 1 ATOM 1009 C CE . LYS A 1 129 ? -36.082 -26.238 -32.833 1.00 36.34 ? 131 LYS A CE 1 ATOM 1010 N NZ . LYS A 1 129 ? -37.140 -26.926 -33.675 1.00 40.80 ? 131 LYS A NZ 1 ATOM 1011 N N . PHE A 1 130 ? -32.749 -22.471 -30.630 1.00 31.85 ? 132 PHE A N 1 ATOM 1012 C CA . PHE A 1 130 ? -33.354 -21.775 -29.482 1.00 32.97 ? 132 PHE A CA 1 ATOM 1013 C C . PHE A 1 130 ? -32.469 -20.580 -29.122 1.00 32.40 ? 132 PHE A C 1 ATOM 1014 O O . PHE A 1 130 ? -32.975 -19.469 -28.927 1.00 34.01 ? 132 PHE A O 1 ATOM 1015 C CB . PHE A 1 130 ? -33.507 -22.720 -28.283 1.00 32.91 ? 132 PHE A CB 1 ATOM 1016 C CG . PHE A 1 130 ? -34.372 -23.898 -28.572 1.00 35.05 ? 132 PHE A CG 1 ATOM 1017 C CD1 . PHE A 1 130 ? -35.754 -23.726 -28.791 1.00 37.82 ? 132 PHE A CD1 1 ATOM 1018 C CD2 . PHE A 1 130 ? -33.818 -25.164 -28.680 1.00 33.37 ? 132 PHE A CD2 1 ATOM 1019 C CE1 . PHE A 1 130 ? -36.587 -24.818 -29.105 1.00 37.63 ? 132 PHE A CE1 1 ATOM 1020 C CE2 . PHE A 1 130 ? -34.612 -26.260 -28.973 1.00 35.77 ? 132 PHE A CE2 1 ATOM 1021 C CZ . PHE A 1 130 ? -36.040 -26.091 -29.190 1.00 37.31 ? 132 PHE A CZ 1 ATOM 1022 N N . LEU A 1 131 ? -31.159 -20.805 -29.089 1.00 30.57 ? 133 LEU A N 1 ATOM 1023 C CA . LEU A 1 131 ? -30.192 -19.713 -28.881 1.00 30.82 ? 133 LEU A CA 1 ATOM 1024 C C . LEU A 1 131 ? -30.304 -18.631 -29.973 1.00 31.20 ? 133 LEU A C 1 ATOM 1025 O O . LEU A 1 131 ? -30.197 -17.465 -29.659 1.00 32.50 ? 133 LEU A O 1 ATOM 1026 C CB . LEU A 1 131 ? -28.758 -20.226 -28.827 1.00 29.09 ? 133 LEU A CB 1 ATOM 1027 C CG . LEU A 1 131 ? -28.421 -21.076 -27.590 1.00 30.53 ? 133 LEU A CG 1 ATOM 1028 C CD1 . LEU A 1 131 ? -27.256 -22.003 -27.858 1.00 26.87 ? 133 LEU A CD1 1 ATOM 1029 C CD2 . LEU A 1 131 ? -28.081 -20.120 -26.504 1.00 32.81 ? 133 LEU A CD2 1 ATOM 1030 N N . ALA A 1 132 ? -30.548 -18.997 -31.229 1.00 30.43 ? 134 ALA A N 1 ATOM 1031 C CA . ALA A 1 132 ? -30.637 -17.974 -32.280 1.00 31.68 ? 134 ALA A CA 1 ATOM 1032 C C . ALA A 1 132 ? -31.930 -17.172 -32.080 1.00 32.74 ? 134 ALA A C 1 ATOM 1033 O O . ALA A 1 132 ? -31.903 -15.938 -32.007 1.00 36.35 ? 134 ALA A O 1 ATOM 1034 C CB . ALA A 1 132 ? -30.485 -18.614 -33.708 1.00 29.88 ? 134 ALA A CB 1 ATOM 1035 N N . ARG A 1 133 ? -33.033 -17.852 -31.831 1.00 32.48 ? 135 ARG A N 1 ATOM 1036 C CA . ARG A 1 133 ? -34.296 -17.177 -31.511 1.00 34.39 ? 135 ARG A CA 1 ATOM 1037 C C . ARG A 1 133 ? -34.235 -16.204 -30.303 1.00 34.58 ? 135 ARG A C 1 ATOM 1038 O O . ARG A 1 133 ? -34.655 -15.039 -30.409 1.00 34.46 ? 135 ARG A O 1 ATOM 1039 C CB . ARG A 1 133 ? -35.398 -18.234 -31.295 1.00 34.59 ? 135 ARG A CB 1 ATOM 1040 C CG . ARG A 1 133 ? -36.731 -17.696 -30.814 1.00 38.72 ? 135 ARG A CG 1 ATOM 1041 C CD . ARG A 1 133 ? -37.389 -16.841 -31.895 1.00 44.48 ? 135 ARG A CD 1 ATOM 1042 N NE . ARG A 1 133 ? -38.725 -16.390 -31.520 1.00 49.67 ? 135 ARG A NE 1 ATOM 1043 C CZ . ARG A 1 133 ? -38.982 -15.285 -30.816 1.00 54.60 ? 135 ARG A CZ 1 ATOM 1044 N NH1 . ARG A 1 133 ? -37.974 -14.530 -30.384 1.00 56.30 ? 135 ARG A NH1 1 ATOM 1045 N NH2 . ARG A 1 133 ? -40.247 -14.934 -30.523 1.00 53.46 ? 135 ARG A NH2 1 ATOM 1046 N N . VAL A 1 134 ? -33.711 -16.693 -29.171 1.00 33.11 ? 136 VAL A N 1 ATOM 1047 C CA . VAL A 1 134 ? -33.895 -16.046 -27.884 1.00 32.28 ? 136 VAL A CA 1 ATOM 1048 C C . VAL A 1 134 ? -32.809 -14.993 -27.676 1.00 32.13 ? 136 VAL A C 1 ATOM 1049 O O . VAL A 1 134 ? -33.089 -13.913 -27.208 1.00 32.38 ? 136 VAL A O 1 ATOM 1050 C CB . VAL A 1 134 ? -33.844 -17.102 -26.708 1.00 32.20 ? 136 VAL A CB 1 ATOM 1051 C CG1 . VAL A 1 134 ? -33.929 -16.384 -25.284 1.00 30.13 ? 136 VAL A CG1 1 ATOM 1052 C CG2 . VAL A 1 134 ? -35.000 -18.081 -26.850 1.00 30.15 ? 136 VAL A CG2 1 ATOM 1053 N N . GLU A 1 135 ? -31.572 -15.292 -28.061 1.00 30.68 ? 137 GLU A N 1 ATOM 1054 C CA . GLU A 1 135 ? -30.461 -14.385 -27.796 1.00 30.63 ? 137 GLU A CA 1 ATOM 1055 C C . GLU A 1 135 ? -29.992 -13.625 -29.047 1.00 30.73 ? 137 GLU A C 1 ATOM 1056 O O . GLU A 1 135 ? -29.116 -12.710 -28.966 1.00 30.06 ? 137 GLU A O 1 ATOM 1057 C CB . GLU A 1 135 ? -29.314 -15.159 -27.095 1.00 28.62 ? 137 GLU A CB 1 ATOM 1058 C CG . GLU A 1 135 ? -29.642 -15.531 -25.656 1.00 28.39 ? 137 GLU A CG 1 ATOM 1059 C CD . GLU A 1 135 ? -29.938 -14.331 -24.719 1.00 33.13 ? 137 GLU A CD 1 ATOM 1060 O OE1 . GLU A 1 135 ? -29.345 -13.222 -24.910 1.00 34.04 ? 137 GLU A OE1 1 ATOM 1061 O OE2 . GLU A 1 135 ? -30.777 -14.498 -23.768 1.00 30.55 ? 137 GLU A OE2 1 ATOM 1062 N N . ARG A 1 136 ? -30.585 -13.972 -30.191 1.00 31.11 ? 138 ARG A N 1 ATOM 1063 C CA . ARG A 1 136 ? -30.192 -13.327 -31.468 1.00 32.98 ? 138 ARG A CA 1 ATOM 1064 C C . ARG A 1 136 ? -28.691 -13.472 -31.747 1.00 31.84 ? 138 ARG A C 1 ATOM 1065 O O . ARG A 1 136 ? -28.088 -12.632 -32.369 1.00 34.29 ? 138 ARG A O 1 ATOM 1066 C CB . ARG A 1 136 ? -30.700 -11.846 -31.615 1.00 33.20 ? 138 ARG A CB 1 ATOM 1067 C CG . ARG A 1 136 ? -32.236 -11.742 -31.928 1.00 37.33 ? 138 ARG A CG 1 ATOM 1068 C CD . ARG A 1 136 ? -32.644 -10.297 -32.400 1.00 46.58 ? 138 ARG A CD 1 ATOM 1069 N NE . ARG A 1 136 ? -32.579 -10.082 -33.867 0.50 42.21 ? 138 ARG A NE 1 ATOM 1070 C CZ . ARG A 1 136 ? -33.324 -10.732 -34.773 0.50 41.25 ? 138 ARG A CZ 1 ATOM 1071 N NH1 . ARG A 1 136 ? -34.218 -11.676 -34.410 0.50 34.88 ? 138 ARG A NH1 1 ATOM 1072 N NH2 . ARG A 1 136 ? -33.157 -10.441 -36.056 0.50 38.60 ? 138 ARG A NH2 1 ATOM 1073 N N . VAL A 1 137 ? -28.103 -14.574 -31.317 1.00 30.42 ? 139 VAL A N 1 ATOM 1074 C CA . VAL A 1 137 ? -26.767 -14.951 -31.733 1.00 27.54 ? 139 VAL A CA 1 ATOM 1075 C C . VAL A 1 137 ? -26.826 -15.879 -32.940 1.00 28.90 ? 139 VAL A C 1 ATOM 1076 O O . VAL A 1 137 ? -27.883 -16.463 -33.220 1.00 29.17 ? 139 VAL A O 1 ATOM 1077 C CB . VAL A 1 137 ? -26.042 -15.652 -30.566 1.00 27.67 ? 139 VAL A CB 1 ATOM 1078 C CG1 . VAL A 1 137 ? -25.691 -14.625 -29.494 1.00 21.90 ? 139 VAL A CG1 1 ATOM 1079 C CG2 . VAL A 1 137 ? -26.914 -16.803 -29.999 1.00 23.55 ? 139 VAL A CG2 1 ATOM 1080 N N . ILE A 1 138 ? -25.717 -16.028 -33.674 1.00 27.75 ? 140 ILE A N 1 ATOM 1081 C CA . ILE A 1 138 ? -25.633 -17.070 -34.719 1.00 26.53 ? 140 ILE A CA 1 ATOM 1082 C C . ILE A 1 138 ? -24.926 -18.295 -34.076 1.00 27.55 ? 140 ILE A C 1 ATOM 1083 O O . ILE A 1 138 ? -23.900 -18.141 -33.324 1.00 28.70 ? 140 ILE A O 1 ATOM 1084 C CB . ILE A 1 138 ? -24.817 -16.491 -35.878 1.00 27.24 ? 140 ILE A CB 1 ATOM 1085 C CG1 . ILE A 1 138 ? -25.688 -15.506 -36.673 1.00 28.57 ? 140 ILE A CG1 1 ATOM 1086 C CG2 . ILE A 1 138 ? -24.175 -17.553 -36.766 1.00 24.28 ? 140 ILE A CG2 1 ATOM 1087 C CD1 . ILE A 1 138 ? -24.980 -14.954 -37.887 1.00 31.57 ? 140 ILE A CD1 1 ATOM 1088 N N . VAL A 1 139 ? -25.438 -19.489 -34.315 1.00 26.66 ? 141 VAL A N 1 ATOM 1089 C CA . VAL A 1 139 ? -24.838 -20.651 -33.721 1.00 25.14 ? 141 VAL A CA 1 ATOM 1090 C C . VAL A 1 139 ? -24.289 -21.524 -34.863 1.00 25.44 ? 141 VAL A C 1 ATOM 1091 O O . VAL A 1 139 ? -24.985 -21.762 -35.860 1.00 27.79 ? 141 VAL A O 1 ATOM 1092 C CB . VAL A 1 139 ? -25.901 -21.472 -32.916 1.00 26.15 ? 141 VAL A CB 1 ATOM 1093 C CG1 . VAL A 1 139 ? -25.305 -22.846 -32.388 1.00 19.49 ? 141 VAL A CG1 1 ATOM 1094 C CG2 . VAL A 1 139 ? -26.535 -20.597 -31.770 1.00 24.29 ? 141 VAL A CG2 1 ATOM 1095 N N . VAL A 1 140 ? -23.065 -21.993 -34.735 1.00 24.35 ? 142 VAL A N 1 ATOM 1096 C CA . VAL A 1 140 ? -22.447 -22.834 -35.736 1.00 24.27 ? 142 VAL A CA 1 ATOM 1097 C C . VAL A 1 140 ? -21.986 -24.133 -35.003 1.00 26.22 ? 142 VAL A C 1 ATOM 1098 O O . VAL A 1 140 ? -21.488 -24.045 -33.822 1.00 26.63 ? 142 VAL A O 1 ATOM 1099 C CB . VAL A 1 140 ? -21.205 -22.153 -36.402 1.00 24.64 ? 142 VAL A CB 1 ATOM 1100 C CG1 . VAL A 1 140 ? -20.432 -23.149 -37.333 1.00 18.81 ? 142 VAL A CG1 1 ATOM 1101 C CG2 . VAL A 1 140 ? -21.620 -20.837 -37.213 1.00 23.87 ? 142 VAL A CG2 1 ATOM 1102 N N . SER A 1 141 ? -22.127 -25.292 -35.692 1.00 25.18 ? 143 SER A N 1 ATOM 1103 C CA . SER A 1 141 ? -21.566 -26.554 -35.241 1.00 24.44 ? 143 SER A CA 1 ATOM 1104 C C . SER A 1 141 ? -21.052 -27.385 -36.418 1.00 25.44 ? 143 SER A C 1 ATOM 1105 O O . SER A 1 141 ? -21.620 -27.318 -37.471 1.00 25.96 ? 143 SER A O 1 ATOM 1106 C CB . SER A 1 141 ? -22.596 -27.333 -34.459 1.00 23.68 ? 143 SER A CB 1 ATOM 1107 O OG . SER A 1 141 ? -23.668 -27.716 -35.267 1.00 24.12 ? 143 SER A OG 1 ATOM 1108 N N . MET A 1 142 ? -19.947 -28.123 -36.236 1.00 24.84 ? 144 MET A N 1 ATOM 1109 C CA . MET A 1 142 ? -19.351 -28.925 -37.292 1.00 25.77 ? 144 MET A CA 1 ATOM 1110 C C . MET A 1 142 ? -19.205 -30.391 -36.865 1.00 26.58 ? 144 MET A C 1 ATOM 1111 O O . MET A 1 142 ? -19.031 -30.698 -35.639 1.00 27.60 ? 144 MET A O 1 ATOM 1112 C CB . MET A 1 142 ? -17.973 -28.360 -37.710 1.00 24.74 ? 144 MET A CB 1 ATOM 1113 C CG . MET A 1 142 ? -16.786 -28.820 -36.810 1.00 23.39 ? 144 MET A CG 1 ATOM 1114 S SD . MET A 1 142 ? -16.947 -28.344 -35.052 1.00 24.63 ? 144 MET A SD 1 ATOM 1115 C CE . MET A 1 142 ? -16.293 -26.657 -35.087 1.00 20.42 ? 144 MET A CE 1 ATOM 1116 N N . ASN A 1 143 ? -19.299 -31.290 -37.854 1.00 26.39 ? 145 ASN A N 1 ATOM 1117 C CA . ASN A 1 143 ? -18.830 -32.634 -37.652 1.00 26.96 ? 145 ASN A CA 1 ATOM 1118 C C . ASN A 1 143 ? -17.321 -32.687 -37.893 1.00 27.44 ? 145 ASN A C 1 ATOM 1119 O O . ASN A 1 143 ? -16.801 -32.030 -38.844 1.00 27.56 ? 145 ASN A O 1 ATOM 1120 C CB . ASN A 1 143 ? -19.574 -33.686 -38.537 1.00 27.50 ? 145 ASN A CB 1 ATOM 1121 C CG . ASN A 1 143 ? -21.028 -33.811 -38.168 1.00 27.24 ? 145 ASN A CG 1 ATOM 1122 O OD1 . ASN A 1 143 ? -21.428 -33.308 -37.125 1.00 27.42 ? 145 ASN A OD1 1 ATOM 1123 N ND2 . ASN A 1 143 ? -21.843 -34.416 -39.035 1.00 27.70 ? 145 ASN A ND2 1 ATOM 1124 N N . TYR A 1 144 ? -16.629 -33.475 -37.047 1.00 25.74 ? 146 TYR A N 1 ATOM 1125 C CA . TYR A 1 144 ? -15.183 -33.626 -37.184 1.00 25.32 ? 146 TYR A CA 1 ATOM 1126 C C . TYR A 1 144 ? -14.921 -35.091 -36.991 1.00 25.05 ? 146 TYR A C 1 ATOM 1127 O O . TYR A 1 144 ? -15.665 -35.720 -36.281 1.00 23.37 ? 146 TYR A O 1 ATOM 1128 C CB . TYR A 1 144 ? -14.404 -32.759 -36.167 1.00 23.42 ? 146 TYR A CB 1 ATOM 1129 C CG . TYR A 1 144 ? -14.635 -33.106 -34.709 1.00 23.32 ? 146 TYR A CG 1 ATOM 1130 C CD1 . TYR A 1 144 ? -13.852 -34.053 -34.063 1.00 21.10 ? 146 TYR A CD1 1 ATOM 1131 C CD2 . TYR A 1 144 ? -15.655 -32.474 -33.960 1.00 23.04 ? 146 TYR A CD2 1 ATOM 1132 C CE1 . TYR A 1 144 ? -14.077 -34.363 -32.705 1.00 17.66 ? 146 TYR A CE1 1 ATOM 1133 C CE2 . TYR A 1 144 ? -15.868 -32.766 -32.598 1.00 19.76 ? 146 TYR A CE2 1 ATOM 1134 C CZ . TYR A 1 144 ? -15.047 -33.703 -31.993 1.00 20.94 ? 146 TYR A CZ 1 ATOM 1135 O OH . TYR A 1 144 ? -15.268 -34.026 -30.663 1.00 23.28 ? 146 TYR A OH 1 ATOM 1136 N N . ARG A 1 145 ? -13.857 -35.618 -37.614 1.00 26.18 ? 147 ARG A N 1 ATOM 1137 C CA . ARG A 1 145 ? -13.582 -37.046 -37.612 1.00 26.62 ? 147 ARG A CA 1 ATOM 1138 C C . ARG A 1 145 ? -13.192 -37.504 -36.221 1.00 26.08 ? 147 ARG A C 1 ATOM 1139 O O . ARG A 1 145 ? -12.462 -36.780 -35.534 1.00 25.73 ? 147 ARG A O 1 ATOM 1140 C CB . ARG A 1 145 ? -12.454 -37.353 -38.578 1.00 27.47 ? 147 ARG A CB 1 ATOM 1141 C CG . ARG A 1 145 ? -12.924 -37.428 -40.055 1.00 29.11 ? 147 ARG A CG 1 ATOM 1142 C CD . ARG A 1 145 ? -11.693 -37.567 -40.950 1.00 25.97 ? 147 ARG A CD 1 ATOM 1143 N NE . ARG A 1 145 ? -11.025 -36.290 -41.065 1.00 24.10 ? 147 ARG A NE 1 ATOM 1144 C CZ . ARG A 1 145 ? -9.829 -36.097 -41.628 1.00 29.14 ? 147 ARG A CZ 1 ATOM 1145 N NH1 . ARG A 1 145 ? -9.122 -37.145 -42.146 1.00 26.49 ? 147 ARG A NH1 1 ATOM 1146 N NH2 . ARG A 1 145 ? -9.350 -34.845 -41.690 1.00 25.30 ? 147 ARG A NH2 1 ATOM 1147 N N . VAL A 1 146 ? -13.586 -38.732 -35.860 1.00 24.57 ? 148 VAL A N 1 ATOM 1148 C CA . VAL A 1 146 ? -13.356 -39.268 -34.523 1.00 24.19 ? 148 VAL A CA 1 ATOM 1149 C C . VAL A 1 146 ? -12.682 -40.674 -34.650 1.00 25.39 ? 148 VAL A C 1 ATOM 1150 O O . VAL A 1 146 ? -12.619 -41.243 -35.756 1.00 25.85 ? 148 VAL A O 1 ATOM 1151 C CB . VAL A 1 146 ? -14.693 -39.231 -33.731 1.00 25.06 ? 148 VAL A CB 1 ATOM 1152 C CG1 . VAL A 1 146 ? -15.112 -37.720 -33.486 1.00 19.88 ? 148 VAL A CG1 1 ATOM 1153 C CG2 . VAL A 1 146 ? -15.819 -40.013 -34.498 1.00 18.55 ? 148 VAL A CG2 1 ATOM 1154 N N . GLY A 1 147 ? -12.159 -41.226 -33.557 1.00 24.39 ? 149 GLY A N 1 ATOM 1155 C CA . GLY A 1 147 ? -11.533 -42.588 -33.593 1.00 23.63 ? 149 GLY A CA 1 ATOM 1156 C C . GLY A 1 147 ? -10.252 -42.536 -34.393 1.00 25.65 ? 149 GLY A C 1 ATOM 1157 O O . GLY A 1 147 ? -9.687 -41.434 -34.543 1.00 25.65 ? 149 GLY A O 1 ATOM 1158 N N . ALA A 1 148 ? -9.771 -43.694 -34.889 1.00 25.54 ? 150 ALA A N 1 ATOM 1159 C CA . ALA A 1 148 ? -8.554 -43.759 -35.643 1.00 27.24 ? 150 ALA A CA 1 ATOM 1160 C C . ALA A 1 148 ? -8.712 -42.925 -36.862 1.00 29.58 ? 150 ALA A C 1 ATOM 1161 O O . ALA A 1 148 ? -7.731 -42.373 -37.326 1.00 31.22 ? 150 ALA A O 1 ATOM 1162 C CB . ALA A 1 148 ? -8.240 -45.190 -36.083 1.00 29.28 ? 150 ALA A CB 1 ATOM 1163 N N . LEU A 1 149 ? -9.917 -42.843 -37.431 1.00 29.46 ? 151 LEU A N 1 ATOM 1164 C CA . LEU A 1 149 ? -10.063 -42.067 -38.674 1.00 31.11 ? 151 LEU A CA 1 ATOM 1165 C C . LEU A 1 149 ? -9.760 -40.569 -38.464 1.00 30.93 ? 151 LEU A C 1 ATOM 1166 O O . LEU A 1 149 ? -9.378 -39.838 -39.416 1.00 31.53 ? 151 LEU A O 1 ATOM 1167 C CB . LEU A 1 149 ? -11.449 -42.251 -39.346 1.00 30.12 ? 151 LEU A CB 1 ATOM 1168 C CG . LEU A 1 149 ? -11.738 -43.645 -39.970 1.00 29.97 ? 151 LEU A CG 1 ATOM 1169 C CD1 . LEU A 1 149 ? -13.241 -43.808 -40.141 1.00 25.47 ? 151 LEU A CD1 1 ATOM 1170 C CD2 . LEU A 1 149 ? -11.000 -44.003 -41.264 1.00 24.32 ? 151 LEU A CD2 1 ATOM 1171 N N . GLY A 1 150 ? -9.974 -40.124 -37.234 1.00 29.88 ? 152 GLY A N 1 ATOM 1172 C CA . GLY A 1 150 ? -9.727 -38.723 -36.818 1.00 29.56 ? 152 GLY A CA 1 ATOM 1173 C C . GLY A 1 150 ? -8.370 -38.497 -36.134 1.00 30.07 ? 152 GLY A C 1 ATOM 1174 O O . GLY A 1 150 ? -7.832 -37.379 -36.148 1.00 30.96 ? 152 GLY A O 1 ATOM 1175 N N . PHE A 1 151 ? -7.804 -39.524 -35.513 1.00 29.37 ? 153 PHE A N 1 ATOM 1176 C CA . PHE A 1 151 ? -6.668 -39.263 -34.637 1.00 28.96 ? 153 PHE A CA 1 ATOM 1177 C C . PHE A 1 151 ? -5.533 -40.263 -34.673 1.00 31.33 ? 153 PHE A C 1 ATOM 1178 O O . PHE A 1 151 ? -4.561 -40.127 -33.867 1.00 32.71 ? 153 PHE A O 1 ATOM 1179 C CB . PHE A 1 151 ? -7.163 -39.071 -33.225 1.00 27.21 ? 153 PHE A CB 1 ATOM 1180 C CG . PHE A 1 151 ? -7.988 -37.792 -33.032 1.00 24.39 ? 153 PHE A CG 1 ATOM 1181 C CD1 . PHE A 1 151 ? -7.354 -36.599 -32.755 1.00 20.16 ? 153 PHE A CD1 1 ATOM 1182 C CD2 . PHE A 1 151 ? -9.392 -37.818 -33.054 1.00 22.50 ? 153 PHE A CD2 1 ATOM 1183 C CE1 . PHE A 1 151 ? -8.084 -35.398 -32.519 1.00 20.49 ? 153 PHE A CE1 1 ATOM 1184 C CE2 . PHE A 1 151 ? -10.149 -36.653 -32.868 1.00 20.93 ? 153 PHE A CE2 1 ATOM 1185 C CZ . PHE A 1 151 ? -9.494 -35.427 -32.579 1.00 20.03 ? 153 PHE A CZ 1 ATOM 1186 N N . LEU A 1 152 ? -5.596 -41.237 -35.606 1.00 31.57 ? 154 LEU A N 1 ATOM 1187 C CA . LEU A 1 152 ? -4.430 -42.090 -35.843 1.00 33.77 ? 154 LEU A CA 1 ATOM 1188 C C . LEU A 1 152 ? -3.146 -41.218 -36.031 1.00 34.76 ? 154 LEU A C 1 ATOM 1189 O O . LEU A 1 152 ? -3.160 -40.210 -36.766 1.00 32.63 ? 154 LEU A O 1 ATOM 1190 C CB . LEU A 1 152 ? -4.604 -42.964 -37.069 1.00 34.52 ? 154 LEU A CB 1 ATOM 1191 C CG . LEU A 1 152 ? -3.582 -44.044 -37.456 1.00 37.20 ? 154 LEU A CG 1 ATOM 1192 C CD1 . LEU A 1 152 ? -4.144 -45.411 -37.168 1.00 36.60 ? 154 LEU A CD1 1 ATOM 1193 C CD2 . LEU A 1 152 ? -3.430 -44.044 -38.974 1.00 37.18 ? 154 LEU A CD2 1 ATOM 1194 N N . ALA A 1 153 ? -2.053 -41.648 -35.401 1.00 34.79 ? 155 ALA A N 1 ATOM 1195 C CA . ALA A 1 153 ? -0.841 -40.865 -35.425 1.00 38.10 ? 155 ALA A CA 1 ATOM 1196 C C . ALA A 1 153 ? 0.403 -41.726 -35.638 1.00 41.71 ? 155 ALA A C 1 ATOM 1197 O O . ALA A 1 153 ? 0.638 -42.722 -34.953 1.00 41.36 ? 155 ALA A O 1 ATOM 1198 C CB . ALA A 1 153 ? -0.729 -39.910 -34.150 1.00 35.10 ? 155 ALA A CB 1 ATOM 1199 N N . LEU A 1 154 ? 1.146 -41.357 -36.651 1.00 46.13 ? 156 LEU A N 1 ATOM 1200 C CA . LEU A 1 154 ? 2.498 -41.852 -36.806 1.00 52.90 ? 156 LEU A CA 1 ATOM 1201 C C . LEU A 1 154 ? 3.313 -40.531 -36.850 1.00 56.18 ? 156 LEU A C 1 ATOM 1202 O O . LEU A 1 154 ? 3.452 -39.893 -37.908 1.00 57.32 ? 156 LEU A O 1 ATOM 1203 C CB . LEU A 1 154 ? 2.527 -42.645 -38.101 1.00 54.20 ? 156 LEU A CB 1 ATOM 1204 C CG . LEU A 1 154 ? 3.192 -44.021 -38.096 1.00 57.72 ? 156 LEU A CG 1 ATOM 1205 C CD1 . LEU A 1 154 ? 3.177 -44.699 -36.708 1.00 55.28 ? 156 LEU A CD1 1 ATOM 1206 C CD2 . LEU A 1 154 ? 2.549 -44.876 -39.192 1.00 59.12 ? 156 LEU A CD2 1 ATOM 1207 N N . PRO A 1 155 ? 3.789 -40.049 -35.685 1.00 58.45 ? 157 PRO A N 1 ATOM 1208 C CA . PRO A 1 155 ? 3.904 -38.562 -35.736 1.00 59.23 ? 157 PRO A CA 1 ATOM 1209 C C . PRO A 1 155 ? 5.108 -38.070 -36.569 1.00 60.70 ? 157 PRO A C 1 ATOM 1210 O O . PRO A 1 155 ? 6.107 -38.805 -36.691 1.00 60.71 ? 157 PRO A O 1 ATOM 1211 C CB . PRO A 1 155 ? 3.930 -38.128 -34.239 1.00 59.50 ? 157 PRO A CB 1 ATOM 1212 C CG . PRO A 1 155 ? 3.789 -39.536 -33.404 1.00 60.40 ? 157 PRO A CG 1 ATOM 1213 C CD . PRO A 1 155 ? 4.231 -40.613 -34.396 1.00 58.89 ? 157 PRO A CD 1 ATOM 1214 N N . GLY A 1 156 ? 4.954 -36.889 -37.191 1.00 59.60 ? 158 GLY A N 1 ATOM 1215 C CA . GLY A 1 156 ? 5.875 -36.451 -38.252 1.00 61.00 ? 158 GLY A CA 1 ATOM 1216 C C . GLY A 1 156 ? 5.609 -36.863 -39.708 1.00 61.36 ? 158 GLY A C 1 ATOM 1217 O O . GLY A 1 156 ? 6.097 -36.198 -40.631 1.00 62.50 ? 158 GLY A O 1 ATOM 1218 N N . ASN A 1 157 ? 4.848 -37.952 -39.913 1.00 60.34 ? 159 ASN A N 1 ATOM 1219 C CA . ASN A 1 157 ? 4.443 -38.462 -41.231 1.00 58.86 ? 159 ASN A CA 1 ATOM 1220 C C . ASN A 1 157 ? 3.123 -37.879 -41.740 1.00 56.98 ? 159 ASN A C 1 ATOM 1221 O O . ASN A 1 157 ? 2.061 -38.155 -41.162 1.00 56.27 ? 159 ASN A O 1 ATOM 1222 C CB . ASN A 1 157 ? 4.270 -39.965 -41.129 1.00 59.66 ? 159 ASN A CB 1 ATOM 1223 C CG . ASN A 1 157 ? 4.021 -40.629 -42.488 1.00 61.29 ? 159 ASN A CG 1 ATOM 1224 O OD1 . ASN A 1 157 ? 3.395 -40.038 -43.386 1.00 61.69 ? 159 ASN A OD1 1 ATOM 1225 N ND2 . ASN A 1 157 ? 4.505 -41.860 -42.643 1.00 58.22 ? 159 ASN A ND2 1 ATOM 1226 N N . PRO A 1 158 ? 3.158 -37.097 -42.845 1.00 56.63 ? 160 PRO A N 1 ATOM 1227 C CA . PRO A 1 158 ? 1.903 -36.405 -43.267 1.00 53.90 ? 160 PRO A CA 1 ATOM 1228 C C . PRO A 1 158 ? 0.811 -37.328 -43.824 1.00 53.28 ? 160 PRO A C 1 ATOM 1229 O O . PRO A 1 158 ? -0.308 -36.877 -44.106 1.00 52.32 ? 160 PRO A O 1 ATOM 1230 C CB . PRO A 1 158 ? 2.368 -35.361 -44.304 1.00 55.03 ? 160 PRO A CB 1 ATOM 1231 C CG . PRO A 1 158 ? 3.825 -35.793 -44.713 1.00 56.47 ? 160 PRO A CG 1 ATOM 1232 C CD . PRO A 1 158 ? 4.337 -36.798 -43.711 1.00 57.50 ? 160 PRO A CD 1 ATOM 1233 N N . GLU A 1 159 ? 1.089 -38.626 -43.931 1.00 53.55 ? 161 GLU A N 1 ATOM 1234 C CA . GLU A 1 159 ? 0.047 -39.597 -44.360 1.00 51.99 ? 161 GLU A CA 1 ATOM 1235 C C . GLU A 1 159 ? -0.924 -39.890 -43.219 1.00 48.80 ? 161 GLU A C 1 ATOM 1236 O O . GLU A 1 159 ? -2.069 -40.373 -43.458 1.00 48.37 ? 161 GLU A O 1 ATOM 1237 C CB . GLU A 1 159 ? 0.637 -40.938 -44.910 1.00 53.75 ? 161 GLU A CB 1 ATOM 1238 C CG . GLU A 1 159 ? 1.685 -40.877 -46.050 1.00 58.03 ? 161 GLU A CG 1 ATOM 1239 C CD . GLU A 1 159 ? 1.348 -39.868 -47.139 1.00 64.56 ? 161 GLU A CD 1 ATOM 1240 O OE1 . GLU A 1 159 ? 0.250 -39.937 -47.748 1.00 66.49 ? 161 GLU A OE1 1 ATOM 1241 O OE2 . GLU A 1 159 ? 2.190 -38.977 -47.384 1.00 68.05 ? 161 GLU A OE2 1 ATOM 1242 N N . ALA A 1 160 ? -0.438 -39.665 -42.001 1.00 45.41 ? 162 ALA A N 1 ATOM 1243 C CA . ALA A 1 160 ? -1.189 -39.909 -40.733 1.00 42.99 ? 162 ALA A CA 1 ATOM 1244 C C . ALA A 1 160 ? -0.493 -39.129 -39.618 1.00 40.86 ? 162 ALA A C 1 ATOM 1245 O O . ALA A 1 160 ? 0.167 -39.748 -38.759 1.00 40.67 ? 162 ALA A O 1 ATOM 1246 C CB . ALA A 1 160 ? -1.208 -41.415 -40.351 1.00 41.90 ? 162 ALA A CB 1 ATOM 1247 N N . PRO A 1 161 ? -0.586 -37.789 -39.662 1.00 39.53 ? 163 PRO A N 1 ATOM 1248 C CA . PRO A 1 161 ? 0.216 -36.977 -38.747 1.00 38.32 ? 163 PRO A CA 1 ATOM 1249 C C . PRO A 1 161 ? -0.385 -36.890 -37.346 1.00 36.78 ? 163 PRO A C 1 ATOM 1250 O O . PRO A 1 161 ? 0.309 -36.442 -36.422 1.00 38.69 ? 163 PRO A O 1 ATOM 1251 C CB . PRO A 1 161 ? 0.197 -35.590 -39.406 1.00 36.81 ? 163 PRO A CB 1 ATOM 1252 C CG . PRO A 1 161 ? -1.114 -35.518 -40.101 1.00 36.58 ? 163 PRO A CG 1 ATOM 1253 C CD . PRO A 1 161 ? -1.437 -36.938 -40.540 1.00 39.32 ? 163 PRO A CD 1 ATOM 1254 N N . GLY A 1 162 ? -1.637 -37.303 -37.159 1.00 33.92 ? 164 GLY A N 1 ATOM 1255 C CA . GLY A 1 162 ? -2.316 -37.070 -35.889 1.00 30.84 ? 164 GLY A CA 1 ATOM 1256 C C . GLY A 1 162 ? -3.181 -35.817 -35.892 1.00 29.67 ? 164 GLY A C 1 ATOM 1257 O O . GLY A 1 162 ? -3.013 -34.958 -36.764 1.00 29.89 ? 164 GLY A O 1 ATOM 1258 N N . ASN A 1 163 ? -4.100 -35.707 -34.932 1.00 27.01 ? 165 ASN A N 1 ATOM 1259 C CA . ASN A 1 163 ? -4.932 -34.499 -34.740 1.00 26.25 ? 165 ASN A CA 1 ATOM 1260 C C . ASN A 1 163 ? -5.799 -34.067 -35.934 1.00 26.44 ? 165 ASN A C 1 ATOM 1261 O O . ASN A 1 163 ? -6.277 -32.891 -35.982 1.00 26.93 ? 165 ASN A O 1 ATOM 1262 C CB . ASN A 1 163 ? -4.078 -33.304 -34.257 1.00 26.74 ? 165 ASN A CB 1 ATOM 1263 C CG . ASN A 1 163 ? -3.417 -33.580 -32.944 1.00 27.45 ? 165 ASN A CG 1 ATOM 1264 O OD1 . ASN A 1 163 ? -3.817 -34.504 -32.226 1.00 25.48 ? 165 ASN A OD1 1 ATOM 1265 N ND2 . ASN A 1 163 ? -2.376 -32.806 -32.614 1.00 25.85 ? 165 ASN A ND2 1 ATOM 1266 N N . MET A 1 164 ? -6.001 -34.967 -36.900 1.00 25.72 ? 166 MET A N 1 ATOM 1267 C CA . MET A 1 164 ? -6.791 -34.619 -38.073 1.00 25.84 ? 166 MET A CA 1 ATOM 1268 C C . MET A 1 164 ? -8.151 -34.038 -37.680 1.00 24.77 ? 166 MET A C 1 ATOM 1269 O O . MET A 1 164 ? -8.639 -33.089 -38.307 1.00 25.32 ? 166 MET A O 1 ATOM 1270 C CB . MET A 1 164 ? -6.962 -35.867 -38.963 1.00 27.07 ? 166 MET A CB 1 ATOM 1271 C CG . MET A 1 164 ? -5.629 -36.391 -39.449 1.00 30.16 ? 166 MET A CG 1 ATOM 1272 S SD . MET A 1 164 ? -4.746 -37.567 -38.338 1.00 31.88 ? 166 MET A SD 1 ATOM 1273 C CE . MET A 1 164 ? -5.800 -39.043 -38.567 1.00 23.25 ? 166 MET A CE 1 ATOM 1274 N N . GLY A 1 165 ? -8.798 -34.591 -36.651 1.00 24.92 ? 167 GLY A N 1 ATOM 1275 C CA . GLY A 1 165 ? -10.146 -34.097 -36.272 1.00 24.08 ? 167 GLY A CA 1 ATOM 1276 C C . GLY A 1 165 ? -10.148 -32.708 -35.620 1.00 24.64 ? 167 GLY A C 1 ATOM 1277 O O . GLY A 1 165 ? -11.103 -31.951 -35.719 1.00 25.34 ? 167 GLY A O 1 ATOM 1278 N N . LEU A 1 166 ? -9.080 -32.393 -34.899 1.00 25.71 ? 168 LEU A N 1 ATOM 1279 C CA . LEU A 1 166 ? -8.798 -31.025 -34.435 1.00 24.46 ? 168 LEU A CA 1 ATOM 1280 C C . LEU A 1 166 ? -8.533 -30.101 -35.673 1.00 25.36 ? 168 LEU A C 1 ATOM 1281 O O . LEU A 1 166 ? -9.090 -29.004 -35.740 1.00 25.40 ? 168 LEU A O 1 ATOM 1282 C CB . LEU A 1 166 ? -7.582 -31.082 -33.516 1.00 23.93 ? 168 LEU A CB 1 ATOM 1283 C CG . LEU A 1 166 ? -7.941 -31.604 -32.124 1.00 22.13 ? 168 LEU A CG 1 ATOM 1284 C CD1 . LEU A 1 166 ? -6.635 -31.810 -31.412 1.00 22.94 ? 168 LEU A CD1 1 ATOM 1285 C CD2 . LEU A 1 166 ? -8.825 -30.615 -31.341 1.00 16.07 ? 168 LEU A CD2 1 ATOM 1286 N N . PHE A 1 167 ? -7.766 -30.565 -36.675 1.00 25.96 ? 169 PHE A N 1 ATOM 1287 C CA . PHE A 1 167 ? -7.673 -29.805 -37.933 1.00 27.45 ? 169 PHE A CA 1 ATOM 1288 C C . PHE A 1 167 ? -9.042 -29.644 -38.667 1.00 28.45 ? 169 PHE A C 1 ATOM 1289 O O . PHE A 1 167 ? -9.269 -28.627 -39.312 1.00 31.05 ? 169 PHE A O 1 ATOM 1290 C CB . PHE A 1 167 ? -6.585 -30.356 -38.858 1.00 27.11 ? 169 PHE A CB 1 ATOM 1291 C CG . PHE A 1 167 ? -5.202 -29.935 -38.434 1.00 30.26 ? 169 PHE A CG 1 ATOM 1292 C CD1 . PHE A 1 167 ? -4.289 -30.864 -37.948 1.00 29.74 ? 169 PHE A CD1 1 ATOM 1293 C CD2 . PHE A 1 167 ? -4.820 -28.582 -38.518 1.00 29.62 ? 169 PHE A CD2 1 ATOM 1294 C CE1 . PHE A 1 167 ? -3.022 -30.431 -37.548 1.00 32.28 ? 169 PHE A CE1 1 ATOM 1295 C CE2 . PHE A 1 167 ? -3.549 -28.151 -38.119 1.00 26.67 ? 169 PHE A CE2 1 ATOM 1296 C CZ . PHE A 1 167 ? -2.656 -29.087 -37.651 1.00 30.09 ? 169 PHE A CZ 1 ATOM 1297 N N . ASP A 1 168 ? -9.924 -30.645 -38.589 1.00 27.75 ? 170 ASP A N 1 ATOM 1298 C CA . ASP A 1 168 ? -11.263 -30.505 -39.127 1.00 27.11 ? 170 ASP A CA 1 ATOM 1299 C C . ASP A 1 168 ? -11.996 -29.342 -38.366 1.00 26.62 ? 170 ASP A C 1 ATOM 1300 O O . ASP A 1 168 ? -12.581 -28.474 -39.006 1.00 27.26 ? 170 ASP A O 1 ATOM 1301 C CB . ASP A 1 168 ? -12.073 -31.803 -38.939 1.00 25.68 ? 170 ASP A CB 1 ATOM 1302 C CG . ASP A 1 168 ? -11.563 -32.983 -39.777 1.00 29.17 ? 170 ASP A CG 1 ATOM 1303 O OD1 . ASP A 1 168 ? -10.786 -32.797 -40.735 1.00 26.54 ? 170 ASP A OD1 1 ATOM 1304 O OD2 . ASP A 1 168 ? -11.942 -34.146 -39.427 1.00 31.83 ? 170 ASP A OD2 1 ATOM 1305 N N . GLN A 1 169 ? -11.993 -29.370 -37.022 1.00 23.96 ? 171 GLN A N 1 ATOM 1306 C CA . GLN A 1 169 ? -12.510 -28.274 -36.244 1.00 24.74 ? 171 GLN A CA 1 ATOM 1307 C C . GLN A 1 169 ? -11.856 -26.936 -36.698 1.00 25.94 ? 171 GLN A C 1 ATOM 1308 O O . GLN A 1 169 ? -12.579 -25.974 -36.972 1.00 26.95 ? 171 GLN A O 1 ATOM 1309 C CB . GLN A 1 169 ? -12.333 -28.500 -34.752 1.00 23.18 ? 171 GLN A CB 1 ATOM 1310 C CG . GLN A 1 169 ? -13.067 -29.740 -34.198 1.00 22.66 ? 171 GLN A CG 1 ATOM 1311 C CD . GLN A 1 169 ? -12.544 -30.044 -32.815 1.00 25.05 ? 171 GLN A CD 1 ATOM 1312 O OE1 . GLN A 1 169 ? -11.915 -29.137 -32.187 1.00 23.70 ? 171 GLN A OE1 1 ATOM 1313 N NE2 . GLN A 1 169 ? -12.807 -31.279 -32.291 1.00 20.88 ? 171 GLN A NE2 1 ATOM 1314 N N . GLN A 1 170 ? -10.540 -26.907 -36.889 1.00 26.24 ? 172 GLN A N 1 ATOM 1315 C CA . GLN A 1 170 ? -9.896 -25.622 -37.190 1.00 27.88 ? 172 GLN A CA 1 ATOM 1316 C C . GLN A 1 170 ? -10.356 -25.101 -38.560 1.00 28.94 ? 172 GLN A C 1 ATOM 1317 O O . GLN A 1 170 ? -10.565 -23.904 -38.744 1.00 28.39 ? 172 GLN A O 1 ATOM 1318 C CB . GLN A 1 170 ? -8.375 -25.772 -37.208 1.00 27.38 ? 172 GLN A CB 1 ATOM 1319 C CG . GLN A 1 170 ? -7.660 -24.487 -37.184 1.00 27.27 ? 172 GLN A CG 1 ATOM 1320 C CD . GLN A 1 170 ? -6.159 -24.702 -37.048 1.00 29.80 ? 172 GLN A CD 1 ATOM 1321 O OE1 . GLN A 1 170 ? -5.585 -24.530 -35.961 1.00 33.21 ? 172 GLN A OE1 1 ATOM 1322 N NE2 . GLN A 1 170 ? -5.520 -25.097 -38.133 1.00 26.14 ? 172 GLN A NE2 1 ATOM 1323 N N . LEU A 1 171 ? -10.501 -26.022 -39.521 1.00 28.97 ? 173 LEU A N 1 ATOM 1324 C CA . LEU A 1 171 ? -10.836 -25.620 -40.852 1.00 28.60 ? 173 LEU A CA 1 ATOM 1325 C C . LEU A 1 171 ? -12.280 -25.089 -40.810 1.00 29.10 ? 173 LEU A C 1 ATOM 1326 O O . LEU A 1 171 ? -12.620 -24.203 -41.587 1.00 30.34 ? 173 LEU A O 1 ATOM 1327 C CB . LEU A 1 171 ? -10.673 -26.777 -41.851 1.00 29.16 ? 173 LEU A CB 1 ATOM 1328 C CG . LEU A 1 171 ? -10.939 -26.401 -43.316 1.00 31.30 ? 173 LEU A CG 1 ATOM 1329 C CD1 . LEU A 1 171 ? -9.983 -25.206 -43.840 1.00 29.99 ? 173 LEU A CD1 1 ATOM 1330 C CD2 . LEU A 1 171 ? -10.777 -27.551 -44.200 1.00 32.49 ? 173 LEU A CD2 1 ATOM 1331 N N . ALA A 1 172 ? -13.118 -25.596 -39.908 1.00 27.72 ? 174 ALA A N 1 ATOM 1332 C CA . ALA A 1 172 ? -14.483 -25.039 -39.782 1.00 28.14 ? 174 ALA A CA 1 ATOM 1333 C C . ALA A 1 172 ? -14.433 -23.656 -39.164 1.00 28.25 ? 174 ALA A C 1 ATOM 1334 O O . ALA A 1 172 ? -15.188 -22.745 -39.580 1.00 28.65 ? 174 ALA A O 1 ATOM 1335 C CB . ALA A 1 172 ? -15.372 -25.963 -38.954 1.00 26.51 ? 174 ALA A CB 1 ATOM 1336 N N . LEU A 1 173 ? -13.554 -23.477 -38.152 1.00 27.66 ? 175 LEU A N 1 ATOM 1337 C CA . LEU A 1 173 ? -13.324 -22.112 -37.641 1.00 28.34 ? 175 LEU A CA 1 ATOM 1338 C C . LEU A 1 173 ? -12.926 -21.102 -38.762 1.00 28.91 ? 175 LEU A C 1 ATOM 1339 O O . LEU A 1 173 ? -13.419 -19.950 -38.736 1.00 28.00 ? 175 LEU A O 1 ATOM 1340 C CB . LEU A 1 173 ? -12.336 -22.063 -36.452 1.00 28.11 ? 175 LEU A CB 1 ATOM 1341 C CG . LEU A 1 173 ? -12.454 -23.107 -35.339 1.00 28.19 ? 175 LEU A CG 1 ATOM 1342 C CD1 . LEU A 1 173 ? -11.562 -22.697 -34.185 1.00 25.80 ? 175 LEU A CD1 1 ATOM 1343 C CD2 . LEU A 1 173 ? -13.898 -23.342 -34.898 1.00 27.22 ? 175 LEU A CD2 1 ATOM 1344 N N . GLN A 1 174 ? -12.056 -21.535 -39.691 1.00 28.40 ? 176 GLN A N 1 ATOM 1345 C CA A GLN A 1 174 ? -11.624 -20.708 -40.811 0.50 30.91 ? 176 GLN A CA 1 ATOM 1346 C CA B GLN A 1 174 ? -11.642 -20.713 -40.808 0.50 30.91 ? 176 GLN A CA 1 ATOM 1347 C C . GLN A 1 174 ? -12.827 -20.383 -41.726 1.00 31.40 ? 176 GLN A C 1 ATOM 1348 O O . GLN A 1 174 ? -12.923 -19.277 -42.263 1.00 32.38 ? 176 GLN A O 1 ATOM 1349 C CB A GLN A 1 174 ? -10.488 -21.393 -41.628 0.50 31.54 ? 176 GLN A CB 1 ATOM 1350 C CB B GLN A 1 174 ? -10.570 -21.447 -41.616 0.50 31.60 ? 176 GLN A CB 1 ATOM 1351 C CG A GLN A 1 174 ? -9.063 -21.417 -40.974 0.50 35.81 ? 176 GLN A CG 1 ATOM 1352 C CG B GLN A 1 174 ? -10.124 -20.706 -42.856 0.50 36.74 ? 176 GLN A CG 1 ATOM 1353 C CD A GLN A 1 174 ? -7.932 -22.001 -41.889 0.50 39.61 ? 176 GLN A CD 1 ATOM 1354 C CD B GLN A 1 174 ? -9.249 -19.521 -42.513 0.50 42.53 ? 176 GLN A CD 1 ATOM 1355 O OE1 A GLN A 1 174 ? -8.070 -22.070 -43.126 0.50 41.82 ? 176 GLN A OE1 1 ATOM 1356 O OE1 B GLN A 1 174 ? -8.049 -19.676 -42.309 0.50 45.82 ? 176 GLN A OE1 1 ATOM 1357 N NE2 A GLN A 1 174 ? -6.807 -22.389 -41.271 0.50 37.81 ? 176 GLN A NE2 1 ATOM 1358 N NE2 B GLN A 1 174 ? -9.844 -18.328 -42.446 0.50 45.51 ? 176 GLN A NE2 1 ATOM 1359 N N . TRP A 1 175 ? -13.719 -21.358 -41.907 1.00 30.44 ? 177 TRP A N 1 ATOM 1360 C CA . TRP A 1 175 ? -14.869 -21.203 -42.802 1.00 31.28 ? 177 TRP A CA 1 ATOM 1361 C C . TRP A 1 175 ? -15.726 -20.049 -42.230 1.00 30.88 ? 177 TRP A C 1 ATOM 1362 O O . TRP A 1 175 ? -16.243 -19.201 -42.973 1.00 31.83 ? 177 TRP A O 1 ATOM 1363 C CB . TRP A 1 175 ? -15.674 -22.536 -42.893 1.00 29.01 ? 177 TRP A CB 1 ATOM 1364 C CG . TRP A 1 175 ? -16.919 -22.402 -43.779 1.00 34.27 ? 177 TRP A CG 1 ATOM 1365 C CD1 . TRP A 1 175 ? -17.016 -22.769 -45.096 1.00 33.21 ? 177 TRP A CD1 1 ATOM 1366 C CD2 . TRP A 1 175 ? -18.209 -21.823 -43.435 1.00 31.48 ? 177 TRP A CD2 1 ATOM 1367 N NE1 . TRP A 1 175 ? -18.257 -22.473 -45.571 1.00 34.84 ? 177 TRP A NE1 1 ATOM 1368 C CE2 . TRP A 1 175 ? -19.016 -21.905 -44.587 1.00 33.35 ? 177 TRP A CE2 1 ATOM 1369 C CE3 . TRP A 1 175 ? -18.760 -21.292 -42.265 1.00 29.70 ? 177 TRP A CE3 1 ATOM 1370 C CZ2 . TRP A 1 175 ? -20.349 -21.424 -44.628 1.00 33.23 ? 177 TRP A CZ2 1 ATOM 1371 C CZ3 . TRP A 1 175 ? -20.097 -20.834 -42.285 1.00 31.53 ? 177 TRP A CZ3 1 ATOM 1372 C CH2 . TRP A 1 175 ? -20.874 -20.892 -43.464 1.00 31.93 ? 177 TRP A CH2 1 ATOM 1373 N N . VAL A 1 176 ? -15.889 -20.045 -40.905 1.00 29.74 ? 178 VAL A N 1 ATOM 1374 C CA . VAL A 1 176 ? -16.643 -19.025 -40.222 1.00 30.11 ? 178 VAL A CA 1 ATOM 1375 C C . VAL A 1 176 ? -15.880 -17.689 -40.373 1.00 31.10 ? 178 VAL A C 1 ATOM 1376 O O . VAL A 1 176 ? -16.480 -16.694 -40.680 1.00 32.86 ? 178 VAL A O 1 ATOM 1377 C CB . VAL A 1 176 ? -16.919 -19.408 -38.720 1.00 29.24 ? 178 VAL A CB 1 ATOM 1378 C CG1 . VAL A 1 176 ? -17.379 -18.209 -37.907 1.00 27.19 ? 178 VAL A CG1 1 ATOM 1379 C CG2 . VAL A 1 176 ? -17.909 -20.574 -38.618 1.00 26.43 ? 178 VAL A CG2 1 ATOM 1380 N N . GLN A 1 177 ? -14.572 -17.638 -40.202 1.00 31.95 ? 179 GLN A N 1 ATOM 1381 C CA . GLN A 1 177 ? -13.877 -16.365 -40.473 1.00 33.23 ? 179 GLN A CA 1 ATOM 1382 C C . GLN A 1 177 ? -14.180 -15.829 -41.891 1.00 34.88 ? 179 GLN A C 1 ATOM 1383 O O . GLN A 1 177 ? -14.582 -14.675 -42.061 1.00 33.88 ? 179 GLN A O 1 ATOM 1384 C CB . GLN A 1 177 ? -12.376 -16.480 -40.211 1.00 33.99 ? 179 GLN A CB 1 ATOM 1385 C CG . GLN A 1 177 ? -12.010 -16.549 -38.736 1.00 32.13 ? 179 GLN A CG 1 ATOM 1386 C CD . GLN A 1 177 ? -12.532 -15.357 -37.961 1.00 33.15 ? 179 GLN A CD 1 ATOM 1387 O OE1 . GLN A 1 177 ? -12.028 -14.260 -38.111 1.00 35.54 ? 179 GLN A OE1 1 ATOM 1388 N NE2 . GLN A 1 177 ? -13.480 -15.580 -37.081 1.00 29.26 ? 179 GLN A NE2 1 ATOM 1389 N N . LYS A 1 178 ? -14.070 -16.695 -42.901 1.00 35.83 ? 180 LYS A N 1 ATOM 1390 C CA . LYS A 1 178 ? -14.278 -16.259 -44.308 1.00 38.55 ? 180 LYS A CA 1 ATOM 1391 C C . LYS A 1 178 ? -15.752 -16.006 -44.714 1.00 38.25 ? 180 LYS A C 1 ATOM 1392 O O . LYS A 1 178 ? -16.027 -15.184 -45.588 1.00 39.33 ? 180 LYS A O 1 ATOM 1393 C CB . LYS A 1 178 ? -13.682 -17.299 -45.265 1.00 38.72 ? 180 LYS A CB 1 ATOM 1394 C CG . LYS A 1 178 ? -12.163 -17.425 -45.131 1.00 45.31 ? 180 LYS A CG 1 ATOM 1395 C CD . LYS A 1 178 ? -11.667 -18.487 -46.165 1.00 54.15 ? 180 LYS A CD 1 ATOM 1396 C CE . LYS A 1 178 ? -10.156 -18.746 -46.110 1.00 59.44 ? 180 LYS A CE 1 ATOM 1397 N NZ . LYS A 1 178 ? -9.749 -19.672 -47.205 1.00 62.95 ? 180 LYS A NZ 1 ATOM 1398 N N . ASN A 1 179 ? -16.696 -16.701 -44.079 1.00 35.52 ? 181 ASN A N 1 ATOM 1399 C CA . ASN A 1 179 ? -18.030 -16.708 -44.627 1.00 35.15 ? 181 ASN A CA 1 ATOM 1400 C C . ASN A 1 179 ? -19.090 -16.107 -43.760 1.00 33.57 ? 181 ASN A C 1 ATOM 1401 O O . ASN A 1 179 ? -20.118 -15.699 -44.283 1.00 34.37 ? 181 ASN A O 1 ATOM 1402 C CB . ASN A 1 179 ? -18.440 -18.121 -45.000 1.00 33.76 ? 181 ASN A CB 1 ATOM 1403 C CG . ASN A 1 179 ? -17.611 -18.664 -46.122 1.00 36.63 ? 181 ASN A CG 1 ATOM 1404 O OD1 . ASN A 1 179 ? -17.827 -18.319 -47.278 1.00 40.41 ? 181 ASN A OD1 1 ATOM 1405 N ND2 . ASN A 1 179 ? -16.651 -19.515 -45.801 1.00 38.13 ? 181 ASN A ND2 1 ATOM 1406 N N . ILE A 1 180 ? -18.880 -16.092 -42.451 1.00 30.81 ? 182 ILE A N 1 ATOM 1407 C CA . ILE A 1 180 ? -19.997 -15.753 -41.580 1.00 31.08 ? 182 ILE A CA 1 ATOM 1408 C C . ILE A 1 180 ? -20.550 -14.327 -41.761 1.00 32.94 ? 182 ILE A C 1 ATOM 1409 O O . ILE A 1 180 ? -21.710 -14.121 -41.443 1.00 34.27 ? 182 ILE A O 1 ATOM 1410 C CB . ILE A 1 180 ? -19.730 -16.103 -40.082 1.00 30.76 ? 182 ILE A CB 1 ATOM 1411 C CG1 . ILE A 1 180 ? -21.015 -16.530 -39.347 1.00 27.27 ? 182 ILE A CG1 1 ATOM 1412 C CG2 . ILE A 1 180 ? -18.873 -15.029 -39.377 1.00 28.44 ? 182 ILE A CG2 1 ATOM 1413 C CD1 . ILE A 1 180 ? -21.427 -17.920 -39.746 1.00 27.68 ? 182 ILE A CD1 1 ATOM 1414 N N . ALA A 1 181 ? -19.780 -13.347 -42.275 1.00 33.62 ? 183 ALA A N 1 ATOM 1415 C CA . ALA A 1 181 ? -20.383 -11.992 -42.438 1.00 35.33 ? 183 ALA A CA 1 ATOM 1416 C C . ALA A 1 181 ? -21.511 -12.035 -43.456 1.00 36.58 ? 183 ALA A C 1 ATOM 1417 O O . ALA A 1 181 ? -22.402 -11.232 -43.389 1.00 39.20 ? 183 ALA A O 1 ATOM 1418 C CB . ALA A 1 181 ? -19.361 -10.916 -42.802 1.00 34.94 ? 183 ALA A CB 1 ATOM 1419 N N . ALA A 1 182 ? -21.478 -12.983 -44.379 1.00 37.16 ? 184 ALA A N 1 ATOM 1420 C CA . ALA A 1 182 ? -22.520 -13.120 -45.425 1.00 38.20 ? 184 ALA A CA 1 ATOM 1421 C C . ALA A 1 182 ? -23.881 -13.488 -44.817 1.00 38.38 ? 184 ALA A C 1 ATOM 1422 O O . ALA A 1 182 ? -24.958 -13.176 -45.369 1.00 40.40 ? 184 ALA A O 1 ATOM 1423 C CB . ALA A 1 182 ? -22.099 -14.170 -46.444 1.00 37.01 ? 184 ALA A CB 1 ATOM 1424 N N . PHE A 1 183 ? -23.809 -14.173 -43.686 1.00 37.01 ? 185 PHE A N 1 ATOM 1425 C CA . PHE A 1 183 ? -24.962 -14.611 -42.883 1.00 36.14 ? 185 PHE A CA 1 ATOM 1426 C C . PHE A 1 183 ? -25.378 -13.587 -41.813 1.00 35.67 ? 185 PHE A C 1 ATOM 1427 O O . PHE A 1 183 ? -26.277 -13.847 -41.052 1.00 36.00 ? 185 PHE A O 1 ATOM 1428 C CB . PHE A 1 183 ? -24.575 -15.905 -42.173 1.00 34.83 ? 185 PHE A CB 1 ATOM 1429 C CG . PHE A 1 183 ? -24.372 -17.066 -43.110 1.00 35.15 ? 185 PHE A CG 1 ATOM 1430 C CD1 . PHE A 1 183 ? -23.130 -17.266 -43.741 1.00 35.36 ? 185 PHE A CD1 1 ATOM 1431 C CD2 . PHE A 1 183 ? -25.426 -17.937 -43.384 1.00 32.95 ? 185 PHE A CD2 1 ATOM 1432 C CE1 . PHE A 1 183 ? -22.960 -18.308 -44.648 1.00 37.93 ? 185 PHE A CE1 1 ATOM 1433 C CE2 . PHE A 1 183 ? -25.263 -19.004 -44.293 1.00 36.01 ? 185 PHE A CE2 1 ATOM 1434 C CZ . PHE A 1 183 ? -24.032 -19.202 -44.903 1.00 36.66 ? 185 PHE A CZ 1 ATOM 1435 N N . GLY A 1 184 ? -24.685 -12.456 -41.738 1.00 35.86 ? 186 GLY A N 1 ATOM 1436 C CA . GLY A 1 184 ? -24.901 -11.463 -40.710 1.00 34.79 ? 186 GLY A CA 1 ATOM 1437 C C . GLY A 1 184 ? -24.109 -11.614 -39.430 1.00 34.02 ? 186 GLY A C 1 ATOM 1438 O O . GLY A 1 184 ? -24.459 -10.961 -38.438 1.00 34.24 ? 186 GLY A O 1 ATOM 1439 N N . GLY A 1 185 ? -23.059 -12.465 -39.418 1.00 32.94 ? 187 GLY A N 1 ATOM 1440 C CA . GLY A 1 185 ? -22.245 -12.693 -38.215 1.00 30.59 ? 187 GLY A CA 1 ATOM 1441 C C . GLY A 1 185 ? -21.049 -11.764 -38.193 1.00 32.51 ? 187 GLY A C 1 ATOM 1442 O O . GLY A 1 185 ? -20.648 -11.232 -39.211 1.00 33.21 ? 187 GLY A O 1 ATOM 1443 N N . ASN A 1 186 ? -20.543 -11.508 -36.997 1.00 31.77 ? 188 ASN A N 1 ATOM 1444 C CA . ASN A 1 186 ? -19.319 -10.844 -36.758 1.00 31.82 ? 188 ASN A CA 1 ATOM 1445 C C . ASN A 1 186 ? -18.156 -11.846 -36.533 1.00 31.76 ? 188 ASN A C 1 ATOM 1446 O O . ASN A 1 186 ? -17.989 -12.327 -35.425 1.00 30.13 ? 188 ASN A O 1 ATOM 1447 C CB . ASN A 1 186 ? -19.513 -10.069 -35.470 1.00 33.02 ? 188 ASN A CB 1 ATOM 1448 C CG . ASN A 1 186 ? -18.398 -9.097 -35.199 1.00 33.43 ? 188 ASN A CG 1 ATOM 1449 O OD1 . ASN A 1 186 ? -17.406 -9.068 -35.916 1.00 39.33 ? 188 ASN A OD1 1 ATOM 1450 N ND2 . ASN A 1 186 ? -18.549 -8.308 -34.161 1.00 30.50 ? 188 ASN A ND2 1 ATOM 1451 N N . PRO A 1 187 ? -17.309 -12.077 -37.559 1.00 32.85 ? 189 PRO A N 1 ATOM 1452 C CA . PRO A 1 187 ? -16.133 -12.933 -37.431 1.00 33.01 ? 189 PRO A CA 1 ATOM 1453 C C . PRO A 1 187 ? -15.188 -12.478 -36.300 1.00 34.13 ? 189 PRO A C 1 ATOM 1454 O O . PRO A 1 187 ? -14.344 -13.261 -35.863 1.00 33.77 ? 189 PRO A O 1 ATOM 1455 C CB . PRO A 1 187 ? -15.429 -12.762 -38.792 1.00 33.34 ? 189 PRO A CB 1 ATOM 1456 C CG . PRO A 1 187 ? -15.801 -11.393 -39.251 1.00 34.58 ? 189 PRO A CG 1 ATOM 1457 C CD . PRO A 1 187 ? -17.262 -11.258 -38.799 1.00 33.67 ? 189 PRO A CD 1 ATOM 1458 N N . LYS A 1 188 ? -15.334 -11.221 -35.845 1.00 34.88 ? 190 LYS A N 1 ATOM 1459 C CA . LYS A 1 188 ? -14.565 -10.695 -34.735 1.00 33.97 ? 190 LYS A CA 1 ATOM 1460 C C . LYS A 1 188 ? -15.221 -10.944 -33.392 1.00 32.98 ? 190 LYS A C 1 ATOM 1461 O O . LYS A 1 188 ? -14.674 -10.512 -32.373 1.00 31.52 ? 190 LYS A O 1 ATOM 1462 C CB . LYS A 1 188 ? -14.341 -9.192 -34.855 1.00 35.12 ? 190 LYS A CB 1 ATOM 1463 C CG . LYS A 1 188 ? -13.378 -8.798 -35.998 1.00 39.03 ? 190 LYS A CG 1 ATOM 1464 C CD . LYS A 1 188 ? -13.088 -7.312 -35.911 1.00 45.85 ? 190 LYS A CD 1 ATOM 1465 C CE . LYS A 1 188 ? -12.357 -6.784 -37.150 1.00 53.58 ? 190 LYS A CE 1 ATOM 1466 N NZ . LYS A 1 188 ? -11.925 -5.304 -36.970 1.00 61.33 ? 190 LYS A NZ 1 ATOM 1467 N N . SER A 1 189 ? -16.372 -11.622 -33.357 1.00 30.39 ? 191 SER A N 1 ATOM 1468 C CA . SER A 1 189 ? -16.927 -11.937 -32.065 1.00 28.69 ? 191 SER A CA 1 ATOM 1469 C C . SER A 1 189 ? -17.432 -13.371 -32.171 1.00 29.68 ? 191 SER A C 1 ATOM 1470 O O . SER A 1 189 ? -18.627 -13.578 -32.434 1.00 30.25 ? 191 SER A O 1 ATOM 1471 C CB . SER A 1 189 ? -18.034 -10.938 -31.713 1.00 29.06 ? 191 SER A CB 1 ATOM 1472 O OG . SER A 1 189 ? -18.712 -11.243 -30.500 1.00 28.97 ? 191 SER A OG 1 ATOM 1473 N N . VAL A 1 190 ? -16.521 -14.343 -31.935 1.00 27.75 ? 192 VAL A N 1 ATOM 1474 C CA . VAL A 1 190 ? -16.775 -15.749 -32.060 1.00 26.80 ? 192 VAL A CA 1 ATOM 1475 C C . VAL A 1 190 ? -16.392 -16.394 -30.729 1.00 26.58 ? 192 VAL A C 1 ATOM 1476 O O . VAL A 1 190 ? -15.279 -16.173 -30.245 1.00 29.36 ? 192 VAL A O 1 ATOM 1477 C CB . VAL A 1 190 ? -15.921 -16.322 -33.214 1.00 27.02 ? 192 VAL A CB 1 ATOM 1478 C CG1 . VAL A 1 190 ? -16.059 -17.852 -33.304 1.00 26.16 ? 192 VAL A CG1 1 ATOM 1479 C CG2 . VAL A 1 190 ? -16.290 -15.641 -34.528 1.00 26.58 ? 192 VAL A CG2 1 ATOM 1480 N N . THR A 1 191 ? -17.283 -17.153 -30.086 1.00 25.58 ? 193 THR A N 1 ATOM 1481 C CA . THR A 1 191 ? -16.898 -17.821 -28.843 1.00 23.58 ? 193 THR A CA 1 ATOM 1482 C C . THR A 1 191 ? -17.024 -19.311 -29.163 1.00 24.54 ? 193 THR A C 1 ATOM 1483 O O . THR A 1 191 ? -18.029 -19.730 -29.737 1.00 23.98 ? 193 THR A O 1 ATOM 1484 C CB . THR A 1 191 ? -17.870 -17.422 -27.742 1.00 24.67 ? 193 THR A CB 1 ATOM 1485 O OG1 . THR A 1 191 ? -17.736 -16.024 -27.510 1.00 27.85 ? 193 THR A OG1 1 ATOM 1486 C CG2 . THR A 1 191 ? -17.728 -18.182 -26.401 1.00 21.00 ? 193 THR A CG2 1 ATOM 1487 N N . LEU A 1 192 ? -15.978 -20.095 -28.872 1.00 24.11 ? 194 LEU A N 1 ATOM 1488 C CA . LEU A 1 192 ? -16.095 -21.550 -28.971 1.00 24.00 ? 194 LEU A CA 1 ATOM 1489 C C . LEU A 1 192 ? -16.715 -22.028 -27.682 1.00 23.68 ? 194 LEU A C 1 ATOM 1490 O O . LEU A 1 192 ? -16.322 -21.539 -26.612 1.00 22.00 ? 194 LEU A O 1 ATOM 1491 C CB . LEU A 1 192 ? -14.716 -22.273 -29.141 1.00 22.24 ? 194 LEU A CB 1 ATOM 1492 C CG . LEU A 1 192 ? -13.771 -21.626 -30.153 1.00 23.47 ? 194 LEU A CG 1 ATOM 1493 C CD1 . LEU A 1 192 ? -12.406 -22.305 -30.234 1.00 21.13 ? 194 LEU A CD1 1 ATOM 1494 C CD2 . LEU A 1 192 ? -14.420 -21.516 -31.573 1.00 19.25 ? 194 LEU A CD2 1 ATOM 1495 N N . PHE A 1 193 ? -17.625 -23.019 -27.799 1.00 23.64 ? 195 PHE A N 1 ATOM 1496 C CA . PHE A 1 193 ? -18.041 -23.771 -26.633 1.00 22.99 ? 195 PHE A CA 1 ATOM 1497 C C . PHE A 1 193 ? -18.153 -25.205 -26.951 1.00 22.85 ? 195 PHE A C 1 ATOM 1498 O O . PHE A 1 193 ? -18.412 -25.563 -28.096 1.00 23.98 ? 195 PHE A O 1 ATOM 1499 C CB . PHE A 1 193 ? -19.327 -23.180 -25.943 1.00 23.04 ? 195 PHE A CB 1 ATOM 1500 C CG . PHE A 1 193 ? -20.615 -23.250 -26.743 1.00 22.53 ? 195 PHE A CG 1 ATOM 1501 C CD1 . PHE A 1 193 ? -20.649 -23.005 -28.100 1.00 25.80 ? 195 PHE A CD1 1 ATOM 1502 C CD2 . PHE A 1 193 ? -21.853 -23.448 -26.069 1.00 21.60 ? 195 PHE A CD2 1 ATOM 1503 C CE1 . PHE A 1 193 ? -21.896 -23.006 -28.807 1.00 25.49 ? 195 PHE A CE1 1 ATOM 1504 C CE2 . PHE A 1 193 ? -23.048 -23.481 -26.754 1.00 23.06 ? 195 PHE A CE2 1 ATOM 1505 C CZ . PHE A 1 193 ? -23.078 -23.252 -28.144 1.00 22.26 ? 195 PHE A CZ 1 ATOM 1506 N N . GLY A 1 194 ? -18.007 -26.052 -25.936 1.00 22.99 ? 196 GLY A N 1 ATOM 1507 C CA . GLY A 1 194 ? -17.967 -27.500 -26.156 1.00 21.63 ? 196 GLY A CA 1 ATOM 1508 C C . GLY A 1 194 ? -18.059 -28.212 -24.818 1.00 22.02 ? 196 GLY A C 1 ATOM 1509 O O . GLY A 1 194 ? -17.821 -27.592 -23.781 1.00 21.08 ? 196 GLY A O 1 ATOM 1510 N N . GLU A 1 195 ? -18.466 -29.494 -24.830 1.00 22.03 ? 197 GLU A N 1 ATOM 1511 C CA . GLU A 1 195 ? -18.553 -30.280 -23.614 1.00 21.64 ? 197 GLU A CA 1 ATOM 1512 C C . GLU A 1 195 ? -17.696 -31.532 -23.674 1.00 22.79 ? 197 GLU A C 1 ATOM 1513 O O . GLU A 1 195 ? -17.560 -32.156 -24.742 1.00 22.75 ? 197 GLU A O 1 ATOM 1514 C CB . GLU A 1 195 ? -20.019 -30.653 -23.315 1.00 22.28 ? 197 GLU A CB 1 ATOM 1515 C CG . GLU A 1 195 ? -20.266 -31.346 -21.960 1.00 18.76 ? 197 GLU A CG 1 ATOM 1516 C CD . GLU A 1 195 ? -20.364 -32.826 -22.109 1.00 24.87 ? 197 GLU A CD 1 ATOM 1517 O OE1 . GLU A 1 195 ? -20.268 -33.249 -23.300 1.00 21.53 ? 197 GLU A OE1 1 ATOM 1518 O OE2 . GLU A 1 195 ? -20.602 -33.540 -21.071 1.00 23.40 ? 197 GLU A OE2 1 ATOM 1519 N N . SER A 1 196 ? -17.091 -31.896 -22.537 1.00 23.03 ? 198 SER A N 1 ATOM 1520 C CA . SER A 1 196 ? -16.306 -33.172 -22.444 1.00 23.54 ? 198 SER A CA 1 ATOM 1521 C C . SER A 1 196 ? -15.176 -33.097 -23.466 1.00 23.65 ? 198 SER A C 1 ATOM 1522 O O . SER A 1 196 ? -14.375 -32.120 -23.376 1.00 25.32 ? 198 SER A O 1 ATOM 1523 C CB . SER A 1 196 ? -17.210 -34.401 -22.571 1.00 24.50 ? 198 SER A CB 1 ATOM 1524 O OG . SER A 1 196 ? -16.632 -35.548 -21.969 1.00 26.74 ? 198 SER A OG 1 ATOM 1525 N N . ALA A 1 197 ? -15.034 -34.038 -24.407 1.00 21.67 ? 199 ALA A N 1 ATOM 1526 C CA . ALA A 1 197 ? -13.917 -33.895 -25.354 1.00 20.19 ? 199 ALA A CA 1 ATOM 1527 C C . ALA A 1 197 ? -14.048 -32.619 -26.214 1.00 21.34 ? 199 ALA A C 1 ATOM 1528 O O . ALA A 1 197 ? -13.044 -32.123 -26.771 1.00 22.74 ? 199 ALA A O 1 ATOM 1529 C CB . ALA A 1 197 ? -13.764 -35.137 -26.256 1.00 21.05 ? 199 ALA A CB 1 ATOM 1530 N N . GLY A 1 198 ? -15.283 -32.079 -26.343 1.00 21.02 ? 200 GLY A N 1 ATOM 1531 C CA . GLY A 1 198 ? -15.486 -30.859 -27.108 1.00 20.03 ? 200 GLY A CA 1 ATOM 1532 C C . GLY A 1 198 ? -14.872 -29.679 -26.314 1.00 20.62 ? 200 GLY A C 1 ATOM 1533 O O . GLY A 1 198 ? -14.279 -28.779 -26.908 1.00 19.23 ? 200 GLY A O 1 ATOM 1534 N N . ALA A 1 199 ? -14.950 -29.747 -24.987 1.00 20.65 ? 201 ALA A N 1 ATOM 1535 C CA . ALA A 1 199 ? -14.318 -28.768 -24.063 1.00 21.28 ? 201 ALA A CA 1 ATOM 1536 C C . ALA A 1 199 ? -12.811 -28.965 -24.069 1.00 22.25 ? 201 ALA A C 1 ATOM 1537 O O . ALA A 1 199 ? -12.069 -27.984 -24.120 1.00 22.90 ? 201 ALA A O 1 ATOM 1538 C CB . ALA A 1 199 ? -14.889 -28.900 -22.651 1.00 19.20 ? 201 ALA A CB 1 ATOM 1539 N N . ALA A 1 200 ? -12.339 -30.214 -24.081 1.00 21.88 ? 202 ALA A N 1 ATOM 1540 C CA . ALA A 1 200 ? -10.864 -30.403 -24.153 1.00 22.55 ? 202 ALA A CA 1 ATOM 1541 C C . ALA A 1 200 ? -10.325 -29.795 -25.473 1.00 22.82 ? 202 ALA A C 1 ATOM 1542 O O . ALA A 1 200 ? -9.292 -29.080 -25.467 1.00 25.33 ? 202 ALA A O 1 ATOM 1543 C CB . ALA A 1 200 ? -10.507 -31.889 -24.030 1.00 21.00 ? 202 ALA A CB 1 ATOM 1544 N N . SER A 1 201 ? -11.058 -30.029 -26.563 1.00 21.61 ? 203 SER A N 1 ATOM 1545 C CA . SER A 1 201 ? -10.791 -29.445 -27.884 1.00 23.34 ? 203 SER A CA 1 ATOM 1546 C C . SER A 1 201 ? -10.757 -27.927 -27.852 1.00 23.19 ? 203 SER A C 1 ATOM 1547 O O . SER A 1 201 ? -9.803 -27.316 -28.355 1.00 25.91 ? 203 SER A O 1 ATOM 1548 C CB . SER A 1 201 ? -11.898 -29.855 -28.859 1.00 22.31 ? 203 SER A CB 1 ATOM 1549 O OG . SER A 1 201 ? -11.853 -31.248 -29.169 1.00 26.88 ? 203 SER A OG 1 ATOM 1550 N N . VAL A 1 202 ? -11.765 -27.307 -27.210 1.00 22.55 ? 204 VAL A N 1 ATOM 1551 C CA . VAL A 1 202 ? -11.776 -25.863 -27.068 1.00 21.38 ? 204 VAL A CA 1 ATOM 1552 C C . VAL A 1 202 ? -10.493 -25.404 -26.327 1.00 21.87 ? 204 VAL A C 1 ATOM 1553 O O . VAL A 1 202 ? -9.764 -24.519 -26.796 1.00 21.32 ? 204 VAL A O 1 ATOM 1554 C CB . VAL A 1 202 ? -13.016 -25.367 -26.278 1.00 22.11 ? 204 VAL A CB 1 ATOM 1555 C CG1 . VAL A 1 202 ? -12.761 -23.890 -25.791 1.00 18.95 ? 204 VAL A CG1 1 ATOM 1556 C CG2 . VAL A 1 202 ? -14.294 -25.490 -27.121 1.00 20.37 ? 204 VAL A CG2 1 ATOM 1557 N N . SER A 1 203 ? -10.131 -26.118 -25.261 1.00 21.61 ? 205 SER A N 1 ATOM 1558 C CA . SER A 1 203 ? -8.921 -25.729 -24.540 1.00 21.98 ? 205 SER A CA 1 ATOM 1559 C C . SER A 1 203 ? -7.657 -25.867 -25.427 1.00 22.07 ? 205 SER A C 1 ATOM 1560 O O . SER A 1 203 ? -6.746 -25.053 -25.319 1.00 23.84 ? 205 SER A O 1 ATOM 1561 C CB . SER A 1 203 ? -8.853 -26.476 -23.185 1.00 20.91 ? 205 SER A CB 1 ATOM 1562 O OG . SER A 1 203 ? -8.455 -27.802 -23.361 1.00 22.05 ? 205 SER A OG 1 ATOM 1563 N N . LEU A 1 204 ? -7.641 -26.817 -26.360 1.00 21.76 ? 206 LEU A N 1 ATOM 1564 C CA . LEU A 1 204 ? -6.444 -27.018 -27.209 1.00 22.64 ? 206 LEU A CA 1 ATOM 1565 C C . LEU A 1 204 ? -6.363 -25.922 -28.295 1.00 23.21 ? 206 LEU A C 1 ATOM 1566 O O . LEU A 1 204 ? -5.286 -25.594 -28.708 1.00 23.47 ? 206 LEU A O 1 ATOM 1567 C CB . LEU A 1 204 ? -6.495 -28.428 -27.846 1.00 22.88 ? 206 LEU A CB 1 ATOM 1568 C CG . LEU A 1 204 ? -6.172 -29.589 -26.845 1.00 23.74 ? 206 LEU A CG 1 ATOM 1569 C CD1 . LEU A 1 204 ? -6.372 -30.907 -27.498 1.00 23.33 ? 206 LEU A CD1 1 ATOM 1570 C CD2 . LEU A 1 204 ? -4.685 -29.429 -26.231 1.00 19.16 ? 206 LEU A CD2 1 ATOM 1571 N N . HIS A 1 205 ? -7.521 -25.441 -28.791 1.00 21.88 ? 207 HIS A N 1 ATOM 1572 C CA . HIS A 1 205 ? -7.550 -24.260 -29.640 1.00 23.67 ? 207 HIS A CA 1 ATOM 1573 C C . HIS A 1 205 ? -6.985 -23.040 -28.908 1.00 24.76 ? 207 HIS A C 1 ATOM 1574 O O . HIS A 1 205 ? -6.347 -22.216 -29.541 1.00 27.61 ? 207 HIS A O 1 ATOM 1575 C CB . HIS A 1 205 ? -8.964 -23.944 -30.201 1.00 21.96 ? 207 HIS A CB 1 ATOM 1576 C CG . HIS A 1 205 ? -9.457 -24.968 -31.174 1.00 23.90 ? 207 HIS A CG 1 ATOM 1577 N ND1 . HIS A 1 205 ? -8.987 -25.043 -32.478 1.00 24.90 ? 207 HIS A ND1 1 ATOM 1578 C CD2 . HIS A 1 205 ? -10.377 -25.973 -31.043 1.00 21.03 ? 207 HIS A CD2 1 ATOM 1579 C CE1 . HIS A 1 205 ? -9.594 -26.042 -33.106 1.00 20.03 ? 207 HIS A CE1 1 ATOM 1580 N NE2 . HIS A 1 205 ? -10.421 -26.640 -32.252 1.00 18.75 ? 207 HIS A NE2 1 ATOM 1581 N N . LEU A 1 206 ? -7.174 -22.901 -27.595 1.00 25.20 ? 208 LEU A N 1 ATOM 1582 C CA . LEU A 1 206 ? -6.465 -21.824 -26.858 1.00 26.09 ? 208 LEU A CA 1 ATOM 1583 C C . LEU A 1 206 ? -4.946 -21.994 -26.932 1.00 27.15 ? 208 LEU A C 1 ATOM 1584 O O . LEU A 1 206 ? -4.187 -21.040 -26.812 1.00 29.00 ? 208 LEU A O 1 ATOM 1585 C CB . LEU A 1 206 ? -6.906 -21.800 -25.383 1.00 24.57 ? 208 LEU A CB 1 ATOM 1586 C CG . LEU A 1 206 ? -8.362 -21.310 -25.146 1.00 26.33 ? 208 LEU A CG 1 ATOM 1587 C CD1 . LEU A 1 206 ? -8.850 -21.667 -23.729 1.00 18.79 ? 208 LEU A CD1 1 ATOM 1588 C CD2 . LEU A 1 206 ? -8.471 -19.773 -25.350 1.00 18.40 ? 208 LEU A CD2 1 ATOM 1589 N N . LEU A 1 207 ? -4.487 -23.223 -27.116 1.00 28.73 ? 209 LEU A N 1 ATOM 1590 C CA . LEU A 1 207 ? -3.054 -23.466 -27.169 1.00 29.04 ? 209 LEU A CA 1 ATOM 1591 C C . LEU A 1 207 ? -2.525 -23.433 -28.580 1.00 29.85 ? 209 LEU A C 1 ATOM 1592 O O . LEU A 1 207 ? -1.357 -23.262 -28.752 1.00 31.25 ? 209 LEU A O 1 ATOM 1593 C CB . LEU A 1 207 ? -2.695 -24.807 -26.498 1.00 28.92 ? 209 LEU A CB 1 ATOM 1594 C CG . LEU A 1 207 ? -2.333 -24.787 -24.992 1.00 29.67 ? 209 LEU A CG 1 ATOM 1595 C CD1 . LEU A 1 207 ? -3.180 -23.932 -24.105 1.00 31.06 ? 209 LEU A CD1 1 ATOM 1596 C CD2 . LEU A 1 207 ? -2.452 -26.228 -24.540 1.00 28.57 ? 209 LEU A CD2 1 ATOM 1597 N N . SER A 1 208 ? -3.354 -23.637 -29.595 1.00 30.11 ? 210 SER A N 1 ATOM 1598 C CA . SER A 1 208 ? -2.782 -23.831 -30.932 1.00 32.68 ? 210 SER A CA 1 ATOM 1599 C C . SER A 1 208 ? -2.565 -22.527 -31.643 1.00 34.55 ? 210 SER A C 1 ATOM 1600 O O . SER A 1 208 ? -3.497 -21.727 -31.806 1.00 33.64 ? 210 SER A O 1 ATOM 1601 C CB . SER A 1 208 ? -3.721 -24.669 -31.801 1.00 33.41 ? 210 SER A CB 1 ATOM 1602 O OG . SER A 1 208 ? -3.036 -25.017 -32.980 1.00 34.31 ? 210 SER A OG 1 ATOM 1603 N N . PRO A 1 209 ? -1.351 -22.298 -32.129 1.00 37.24 ? 211 PRO A N 1 ATOM 1604 C CA . PRO A 1 209 ? -1.155 -20.979 -32.760 1.00 37.87 ? 211 PRO A CA 1 ATOM 1605 C C . PRO A 1 209 ? -1.972 -20.778 -34.060 1.00 36.99 ? 211 PRO A C 1 ATOM 1606 O O . PRO A 1 209 ? -2.491 -19.679 -34.271 1.00 39.09 ? 211 PRO A O 1 ATOM 1607 C CB . PRO A 1 209 ? 0.377 -20.878 -32.942 1.00 39.80 ? 211 PRO A CB 1 ATOM 1608 C CG . PRO A 1 209 ? 0.859 -22.278 -32.963 1.00 42.19 ? 211 PRO A CG 1 ATOM 1609 C CD . PRO A 1 209 ? -0.130 -23.120 -32.122 1.00 39.26 ? 211 PRO A CD 1 ATOM 1610 N N . GLY A 1 210 ? -2.208 -21.820 -34.855 1.00 35.59 ? 212 GLY A N 1 ATOM 1611 C CA . GLY A 1 210 ? -3.078 -21.686 -36.007 1.00 33.73 ? 212 GLY A CA 1 ATOM 1612 C C . GLY A 1 210 ? -4.550 -21.454 -35.652 1.00 33.49 ? 212 GLY A C 1 ATOM 1613 O O . GLY A 1 210 ? -5.317 -21.156 -36.532 1.00 33.77 ? 212 GLY A O 1 ATOM 1614 N N . SER A 1 211 ? -4.975 -21.614 -34.388 1.00 30.85 ? 213 SER A N 1 ATOM 1615 C CA . SER A 1 211 ? -6.333 -21.194 -34.019 1.00 29.79 ? 213 SER A CA 1 ATOM 1616 C C . SER A 1 211 ? -6.433 -19.804 -33.412 1.00 29.55 ? 213 SER A C 1 ATOM 1617 O O . SER A 1 211 ? -7.500 -19.293 -33.296 1.00 29.83 ? 213 SER A O 1 ATOM 1618 C CB . SER A 1 211 ? -6.994 -22.203 -33.069 1.00 28.11 ? 213 SER A CB 1 ATOM 1619 O OG . SER A 1 211 ? -7.066 -23.437 -33.730 1.00 29.05 ? 213 SER A OG 1 ATOM 1620 N N . HIS A 1 212 ? -5.329 -19.200 -32.997 1.00 30.74 ? 214 HIS A N 1 ATOM 1621 C CA . HIS A 1 212 ? -5.350 -17.932 -32.251 1.00 32.02 ? 214 HIS A CA 1 ATOM 1622 C C . HIS A 1 212 ? -6.220 -16.876 -32.932 1.00 31.27 ? 214 HIS A C 1 ATOM 1623 O O . HIS A 1 212 ? -6.991 -16.216 -32.280 1.00 31.34 ? 214 HIS A O 1 ATOM 1624 C CB . HIS A 1 212 ? -3.900 -17.482 -31.894 1.00 33.39 ? 214 HIS A CB 1 ATOM 1625 C CG . HIS A 1 212 ? -3.782 -16.135 -31.228 0.80 38.45 ? 214 HIS A CG 1 ATOM 1626 N ND1 . HIS A 1 212 ? -3.170 -15.966 -29.997 0.80 41.43 ? 214 HIS A ND1 1 ATOM 1627 C CD2 . HIS A 1 212 ? -4.082 -14.882 -31.660 0.80 42.23 ? 214 HIS A CD2 1 ATOM 1628 C CE1 . HIS A 1 212 ? -3.152 -14.686 -29.678 0.80 36.48 ? 214 HIS A CE1 1 ATOM 1629 N NE2 . HIS A 1 212 ? -3.705 -14.005 -30.665 0.80 39.26 ? 214 HIS A NE2 1 ATOM 1630 N N . SER A 1 213 ? -6.212 -16.769 -34.246 1.00 31.27 ? 215 SER A N 1 ATOM 1631 C CA . SER A 1 213 ? -6.957 -15.664 -34.828 1.00 31.46 ? 215 SER A CA 1 ATOM 1632 C C . SER A 1 213 ? -8.317 -16.068 -35.320 1.00 31.34 ? 215 SER A C 1 ATOM 1633 O O . SER A 1 213 ? -8.958 -15.241 -35.975 1.00 32.08 ? 215 SER A O 1 ATOM 1634 C CB . SER A 1 213 ? -6.181 -15.131 -36.034 1.00 34.34 ? 215 SER A CB 1 ATOM 1635 O OG . SER A 1 213 ? -6.234 -16.139 -37.077 1.00 40.31 ? 215 SER A OG 1 ATOM 1636 N N . LEU A 1 214 ? -8.764 -17.320 -35.025 1.00 29.05 ? 216 LEU A N 1 ATOM 1637 C CA . LEU A 1 214 ? -10.019 -17.842 -35.530 1.00 27.35 ? 216 LEU A CA 1 ATOM 1638 C C . LEU A 1 214 ? -11.134 -17.693 -34.521 1.00 26.88 ? 216 LEU A C 1 ATOM 1639 O O . LEU A 1 214 ? -12.237 -18.154 -34.770 1.00 26.31 ? 216 LEU A O 1 ATOM 1640 C CB . LEU A 1 214 ? -9.907 -19.286 -35.956 1.00 24.31 ? 216 LEU A CB 1 ATOM 1641 C CG . LEU A 1 214 ? -8.750 -19.585 -36.918 1.00 29.90 ? 216 LEU A CG 1 ATOM 1642 C CD1 . LEU A 1 214 ? -8.697 -21.112 -37.431 1.00 25.38 ? 216 LEU A CD1 1 ATOM 1643 C CD2 . LEU A 1 214 ? -8.770 -18.607 -38.071 1.00 26.49 ? 216 LEU A CD2 1 ATOM 1644 N N . PHE A 1 215 ? -10.866 -17.081 -33.367 1.00 25.78 ? 217 PHE A N 1 ATOM 1645 C CA . PHE A 1 215 ? -11.958 -16.938 -32.377 1.00 24.84 ? 217 PHE A CA 1 ATOM 1646 C C . PHE A 1 215 ? -11.583 -15.929 -31.326 1.00 24.72 ? 217 PHE A C 1 ATOM 1647 O O . PHE A 1 215 ? -10.409 -15.585 -31.219 1.00 26.58 ? 217 PHE A O 1 ATOM 1648 C CB . PHE A 1 215 ? -12.361 -18.293 -31.734 1.00 22.72 ? 217 PHE A CB 1 ATOM 1649 C CG . PHE A 1 215 ? -11.312 -18.866 -30.765 1.00 23.75 ? 217 PHE A CG 1 ATOM 1650 C CD1 . PHE A 1 215 ? -10.128 -19.452 -31.243 1.00 22.10 ? 217 PHE A CD1 1 ATOM 1651 C CD2 . PHE A 1 215 ? -11.540 -18.868 -29.382 1.00 22.06 ? 217 PHE A CD2 1 ATOM 1652 C CE1 . PHE A 1 215 ? -9.193 -19.999 -30.365 1.00 22.94 ? 217 PHE A CE1 1 ATOM 1653 C CE2 . PHE A 1 215 ? -10.596 -19.417 -28.495 1.00 22.88 ? 217 PHE A CE2 1 ATOM 1654 C CZ . PHE A 1 215 ? -9.424 -19.959 -28.993 1.00 22.48 ? 217 PHE A CZ 1 ATOM 1655 N N . THR A 1 216 ? -12.571 -15.449 -30.581 1.00 24.89 ? 218 THR A N 1 ATOM 1656 C CA . THR A 1 216 ? -12.371 -14.461 -29.569 1.00 26.13 ? 218 THR A CA 1 ATOM 1657 C C . THR A 1 216 ? -12.341 -15.049 -28.158 1.00 26.26 ? 218 THR A C 1 ATOM 1658 O O . THR A 1 216 ? -11.464 -14.732 -27.356 1.00 25.75 ? 218 THR A O 1 ATOM 1659 C CB . THR A 1 216 ? -13.573 -13.533 -29.593 1.00 28.71 ? 218 THR A CB 1 ATOM 1660 O OG1 . THR A 1 216 ? -13.892 -13.209 -30.964 1.00 31.17 ? 218 THR A OG1 1 ATOM 1661 C CG2 . THR A 1 216 ? -13.289 -12.241 -28.712 1.00 24.23 ? 218 THR A CG2 1 ATOM 1662 N N . ARG A 1 217 ? -13.337 -15.862 -27.790 1.00 25.47 ? 219 ARG A N 1 ATOM 1663 C CA . ARG A 1 217 ? -13.225 -16.429 -26.447 1.00 24.31 ? 219 ARG A CA 1 ATOM 1664 C C . ARG A 1 217 ? -13.750 -17.830 -26.314 1.00 24.43 ? 219 ARG A C 1 ATOM 1665 O O . ARG A 1 217 ? -14.111 -18.415 -27.357 1.00 24.26 ? 219 ARG A O 1 ATOM 1666 C CB . ARG A 1 217 ? -13.696 -15.453 -25.364 1.00 25.44 ? 219 ARG A CB 1 ATOM 1667 C CG . ARG A 1 217 ? -15.023 -14.915 -25.399 1.00 25.33 ? 219 ARG A CG 1 ATOM 1668 C CD . ARG A 1 217 ? -15.128 -13.621 -24.430 1.00 30.13 ? 219 ARG A CD 1 ATOM 1669 N NE . ARG A 1 217 ? -15.946 -12.799 -25.217 1.00 28.94 ? 219 ARG A NE 1 ATOM 1670 C CZ . ARG A 1 217 ? -15.683 -11.605 -25.654 1.00 31.32 ? 219 ARG A CZ 1 ATOM 1671 N NH1 . ARG A 1 217 ? -16.560 -11.112 -26.517 1.00 27.54 ? 219 ARG A NH1 1 ATOM 1672 N NH2 . ARG A 1 217 ? -14.621 -10.923 -25.234 1.00 27.89 ? 219 ARG A NH2 1 ATOM 1673 N N . ALA A 1 218 ? -13.750 -18.382 -25.080 1.00 23.39 ? 220 ALA A N 1 ATOM 1674 C CA . ALA A 1 218 ? -13.960 -19.822 -24.918 1.00 22.97 ? 220 ALA A CA 1 ATOM 1675 C C . ALA A 1 218 ? -14.731 -20.190 -23.663 1.00 22.20 ? 220 ALA A C 1 ATOM 1676 O O . ALA A 1 218 ? -14.576 -19.570 -22.579 1.00 20.98 ? 220 ALA A O 1 ATOM 1677 C CB . ALA A 1 218 ? -12.635 -20.527 -24.932 1.00 22.13 ? 220 ALA A CB 1 ATOM 1678 N N . ILE A 1 219 ? -15.572 -21.204 -23.856 1.00 21.52 ? 221 ILE A N 1 ATOM 1679 C CA . ILE A 1 219 ? -16.406 -21.819 -22.824 1.00 21.23 ? 221 ILE A CA 1 ATOM 1680 C C . ILE A 1 219 ? -16.060 -23.338 -22.736 1.00 21.97 ? 221 ILE A C 1 ATOM 1681 O O . ILE A 1 219 ? -16.127 -24.046 -23.743 1.00 22.66 ? 221 ILE A O 1 ATOM 1682 C CB . ILE A 1 219 ? -17.894 -21.654 -23.158 1.00 21.54 ? 221 ILE A CB 1 ATOM 1683 C CG1 . ILE A 1 219 ? -18.257 -20.134 -23.283 1.00 19.81 ? 221 ILE A CG1 1 ATOM 1684 C CG2 . ILE A 1 219 ? -18.859 -22.426 -22.064 1.00 18.07 ? 221 ILE A CG2 1 ATOM 1685 C CD1 . ILE A 1 219 ? -19.806 -19.862 -23.591 1.00 19.16 ? 221 ILE A CD1 1 ATOM 1686 N N . LEU A 1 220 ? -15.736 -23.832 -21.537 1.00 21.04 ? 222 LEU A N 1 ATOM 1687 C CA . LEU A 1 220 ? -15.362 -25.267 -21.365 1.00 22.16 ? 222 LEU A CA 1 ATOM 1688 C C . LEU A 1 220 ? -16.298 -25.975 -20.392 1.00 22.00 ? 222 LEU A C 1 ATOM 1689 O O . LEU A 1 220 ? -16.194 -25.741 -19.181 1.00 21.75 ? 222 LEU A O 1 ATOM 1690 C CB . LEU A 1 220 ? -13.948 -25.355 -20.777 1.00 20.55 ? 222 LEU A CB 1 ATOM 1691 C CG . LEU A 1 220 ? -12.808 -24.961 -21.703 1.00 22.79 ? 222 LEU A CG 1 ATOM 1692 C CD1 . LEU A 1 220 ? -12.853 -23.359 -21.980 1.00 25.75 ? 222 LEU A CD1 1 ATOM 1693 C CD2 . LEU A 1 220 ? -11.510 -25.329 -21.027 1.00 21.84 ? 222 LEU A CD2 1 ATOM 1694 N N . GLN A 1 221 ? -17.209 -26.801 -20.914 1.00 21.72 ? 223 GLN A N 1 ATOM 1695 C CA . GLN A 1 221 ? -18.163 -27.564 -20.099 1.00 20.46 ? 223 GLN A CA 1 ATOM 1696 C C . GLN A 1 221 ? -17.652 -28.974 -19.819 1.00 21.14 ? 223 GLN A C 1 ATOM 1697 O O . GLN A 1 221 ? -17.514 -29.836 -20.743 1.00 19.90 ? 223 GLN A O 1 ATOM 1698 C CB . GLN A 1 221 ? -19.531 -27.586 -20.771 1.00 20.88 ? 223 GLN A CB 1 ATOM 1699 C CG . GLN A 1 221 ? -20.105 -26.143 -20.987 1.00 20.54 ? 223 GLN A CG 1 ATOM 1700 C CD . GLN A 1 221 ? -21.355 -26.060 -21.887 1.00 21.13 ? 223 GLN A CD 1 ATOM 1701 O OE1 . GLN A 1 221 ? -21.601 -25.037 -22.484 1.00 27.30 ? 223 GLN A OE1 1 ATOM 1702 N NE2 . GLN A 1 221 ? -22.136 -27.099 -21.952 1.00 22.77 ? 223 GLN A NE2 1 ATOM 1703 N N . SER A 1 222 ? -17.283 -29.218 -18.553 1.00 21.31 ? 224 SER A N 1 ATOM 1704 C CA . SER A 1 222 ? -16.855 -30.609 -18.172 1.00 21.21 ? 224 SER A CA 1 ATOM 1705 C C . SER A 1 222 ? -15.720 -31.137 -19.079 1.00 22.88 ? 224 SER A C 1 ATOM 1706 O O . SER A 1 222 ? -15.851 -32.260 -19.661 1.00 21.65 ? 224 SER A O 1 ATOM 1707 C CB . SER A 1 222 ? -18.008 -31.598 -18.247 1.00 19.61 ? 224 SER A CB 1 ATOM 1708 O OG . SER A 1 222 ? -19.137 -31.209 -17.404 1.00 22.12 ? 224 SER A OG 1 ATOM 1709 N N . GLY A 1 223 ? -14.610 -30.381 -19.202 1.00 21.43 ? 225 GLY A N 1 ATOM 1710 C CA . GLY A 1 223 ? -13.468 -30.923 -19.983 1.00 21.26 ? 225 GLY A CA 1 ATOM 1711 C C . GLY A 1 223 ? -12.375 -29.865 -20.098 1.00 22.10 ? 225 GLY A C 1 ATOM 1712 O O . GLY A 1 223 ? -12.659 -28.613 -20.078 1.00 23.10 ? 225 GLY A O 1 ATOM 1713 N N . SER A 1 224 ? -11.144 -30.314 -20.220 1.00 20.79 ? 226 SER A N 1 ATOM 1714 C CA . SER A 1 224 ? -10.017 -29.422 -20.507 1.00 22.59 ? 226 SER A CA 1 ATOM 1715 C C . SER A 1 224 ? -8.896 -30.377 -20.865 1.00 23.46 ? 226 SER A C 1 ATOM 1716 O O . SER A 1 224 ? -8.969 -31.543 -20.445 1.00 23.18 ? 226 SER A O 1 ATOM 1717 C CB . SER A 1 224 ? -9.610 -28.663 -19.216 1.00 22.82 ? 226 SER A CB 1 ATOM 1718 O OG . SER A 1 224 ? -9.524 -29.572 -18.075 1.00 20.99 ? 226 SER A OG 1 ATOM 1719 N N . PHE A 1 225 ? -7.832 -29.912 -21.548 1.00 23.95 ? 227 PHE A N 1 ATOM 1720 C CA . PHE A 1 225 ? -6.907 -30.878 -22.154 1.00 24.86 ? 227 PHE A CA 1 ATOM 1721 C C . PHE A 1 225 ? -5.997 -31.482 -21.066 1.00 26.27 ? 227 PHE A C 1 ATOM 1722 O O . PHE A 1 225 ? -5.310 -32.414 -21.353 1.00 28.28 ? 227 PHE A O 1 ATOM 1723 C CB . PHE A 1 225 ? -6.008 -30.140 -23.149 1.00 26.81 ? 227 PHE A CB 1 ATOM 1724 C CG . PHE A 1 225 ? -4.991 -29.235 -22.440 1.00 29.92 ? 227 PHE A CG 1 ATOM 1725 C CD1 . PHE A 1 225 ? -3.963 -29.792 -21.713 1.00 37.25 ? 227 PHE A CD1 1 ATOM 1726 C CD2 . PHE A 1 225 ? -5.140 -27.873 -22.448 1.00 33.31 ? 227 PHE A CD2 1 ATOM 1727 C CE1 . PHE A 1 225 ? -3.084 -28.958 -20.987 1.00 40.79 ? 227 PHE A CE1 1 ATOM 1728 C CE2 . PHE A 1 225 ? -4.304 -27.047 -21.739 1.00 36.75 ? 227 PHE A CE2 1 ATOM 1729 C CZ . PHE A 1 225 ? -3.291 -27.580 -21.013 1.00 38.03 ? 227 PHE A CZ 1 ATOM 1730 N N . ASN A 1 226 ? -5.918 -30.902 -19.844 1.00 25.56 ? 228 ASN A N 1 ATOM 1731 C CA . ASN A 1 226 ? -5.066 -31.481 -18.798 1.00 25.14 ? 228 ASN A CA 1 ATOM 1732 C C . ASN A 1 226 ? -5.791 -32.629 -18.068 1.00 26.04 ? 228 ASN A C 1 ATOM 1733 O O . ASN A 1 226 ? -5.245 -33.166 -17.109 1.00 26.86 ? 228 ASN A O 1 ATOM 1734 C CB . ASN A 1 226 ? -4.616 -30.417 -17.800 1.00 24.33 ? 228 ASN A CB 1 ATOM 1735 C CG . ASN A 1 226 ? -5.835 -29.668 -17.141 1.00 28.35 ? 228 ASN A CG 1 ATOM 1736 O OD1 . ASN A 1 226 ? -6.865 -29.367 -17.786 1.00 27.59 ? 228 ASN A OD1 1 ATOM 1737 N ND2 . ASN A 1 226 ? -5.728 -29.432 -15.872 1.00 25.48 ? 228 ASN A ND2 1 ATOM 1738 N N . ALA A 1 227 ? -7.018 -32.992 -18.492 1.00 25.04 ? 229 ALA A N 1 ATOM 1739 C CA . ALA A 1 227 ? -7.733 -34.149 -17.903 1.00 24.58 ? 229 ALA A CA 1 ATOM 1740 C C . ALA A 1 227 ? -6.954 -35.420 -18.277 1.00 24.64 ? 229 ALA A C 1 ATOM 1741 O O . ALA A 1 227 ? -6.411 -35.484 -19.351 1.00 23.57 ? 229 ALA A O 1 ATOM 1742 C CB . ALA A 1 227 ? -9.164 -34.200 -18.471 1.00 21.94 ? 229 ALA A CB 1 ATOM 1743 N N . PRO A 1 228 ? -6.909 -36.441 -17.408 1.00 25.94 ? 230 PRO A N 1 ATOM 1744 C CA . PRO A 1 228 ? -5.991 -37.548 -17.767 1.00 26.21 ? 230 PRO A CA 1 ATOM 1745 C C . PRO A 1 228 ? -6.360 -38.357 -19.055 1.00 26.55 ? 230 PRO A C 1 ATOM 1746 O O . PRO A 1 228 ? -5.498 -39.084 -19.606 1.00 28.08 ? 230 PRO A O 1 ATOM 1747 C CB . PRO A 1 228 ? -5.975 -38.427 -16.516 1.00 27.03 ? 230 PRO A CB 1 ATOM 1748 C CG . PRO A 1 228 ? -7.301 -38.101 -15.783 1.00 27.16 ? 230 PRO A CG 1 ATOM 1749 C CD . PRO A 1 228 ? -7.749 -36.735 -16.219 1.00 25.39 ? 230 PRO A CD 1 ATOM 1750 N N . TRP A 1 229 ? -7.561 -38.181 -19.586 1.00 25.06 ? 231 TRP A N 1 ATOM 1751 C CA . TRP A 1 229 ? -7.924 -38.897 -20.799 1.00 25.05 ? 231 TRP A CA 1 ATOM 1752 C C . TRP A 1 229 ? -7.700 -38.054 -22.042 1.00 24.45 ? 231 TRP A C 1 ATOM 1753 O O . TRP A 1 229 ? -7.979 -38.477 -23.107 1.00 25.59 ? 231 TRP A O 1 ATOM 1754 C CB . TRP A 1 229 ? -9.424 -39.296 -20.739 1.00 23.29 ? 231 TRP A CB 1 ATOM 1755 C CG . TRP A 1 229 ? -10.301 -38.118 -20.245 1.00 24.97 ? 231 TRP A CG 1 ATOM 1756 C CD1 . TRP A 1 229 ? -10.664 -37.872 -18.943 1.00 27.25 ? 231 TRP A CD1 1 ATOM 1757 C CD2 . TRP A 1 229 ? -10.850 -37.022 -21.015 1.00 22.62 ? 231 TRP A CD2 1 ATOM 1758 N NE1 . TRP A 1 229 ? -11.444 -36.740 -18.859 1.00 27.09 ? 231 TRP A NE1 1 ATOM 1759 C CE2 . TRP A 1 229 ? -11.575 -36.190 -20.105 1.00 24.16 ? 231 TRP A CE2 1 ATOM 1760 C CE3 . TRP A 1 229 ? -10.878 -36.704 -22.380 1.00 22.80 ? 231 TRP A CE3 1 ATOM 1761 C CZ2 . TRP A 1 229 ? -12.300 -35.025 -20.515 1.00 23.87 ? 231 TRP A CZ2 1 ATOM 1762 C CZ3 . TRP A 1 229 ? -11.600 -35.475 -22.786 1.00 19.04 ? 231 TRP A CZ3 1 ATOM 1763 C CH2 . TRP A 1 229 ? -12.268 -34.683 -21.854 1.00 19.01 ? 231 TRP A CH2 1 ATOM 1764 N N . ALA A 1 230 ? -7.220 -36.836 -21.945 1.00 25.91 ? 232 ALA A N 1 ATOM 1765 C CA . ALA A 1 230 ? -7.450 -35.956 -23.107 1.00 25.56 ? 232 ALA A CA 1 ATOM 1766 C C . ALA A 1 230 ? -6.338 -35.952 -24.100 1.00 26.94 ? 232 ALA A C 1 ATOM 1767 O O . ALA A 1 230 ? -6.594 -35.671 -25.263 1.00 26.51 ? 232 ALA A O 1 ATOM 1768 C CB . ALA A 1 230 ? -7.803 -34.539 -22.686 1.00 24.14 ? 232 ALA A CB 1 ATOM 1769 N N . VAL A 1 231 ? -5.118 -36.292 -23.681 1.00 26.80 ? 233 VAL A N 1 ATOM 1770 C CA . VAL A 1 231 ? -4.045 -36.229 -24.617 1.00 30.89 ? 233 VAL A CA 1 ATOM 1771 C C . VAL A 1 231 ? -3.237 -37.538 -24.608 1.00 35.47 ? 233 VAL A C 1 ATOM 1772 O O . VAL A 1 231 ? -2.825 -38.006 -23.545 1.00 36.02 ? 233 VAL A O 1 ATOM 1773 C CB . VAL A 1 231 ? -3.107 -35.008 -24.308 1.00 31.40 ? 233 VAL A CB 1 ATOM 1774 C CG1 . VAL A 1 231 ? -1.956 -34.961 -25.309 1.00 29.61 ? 233 VAL A CG1 1 ATOM 1775 C CG2 . VAL A 1 231 ? -3.910 -33.677 -24.296 1.00 28.54 ? 233 VAL A CG2 1 ATOM 1776 N N . THR A 1 232 ? -3.024 -38.126 -25.778 1.00 38.80 ? 234 THR A N 1 ATOM 1777 C CA . THR A 1 232 ? -2.219 -39.369 -25.896 1.00 43.01 ? 234 THR A CA 1 ATOM 1778 C C . THR A 1 232 ? -0.721 -39.075 -26.018 1.00 44.97 ? 234 THR A C 1 ATOM 1779 O O . THR A 1 232 ? -0.305 -38.157 -26.741 1.00 45.61 ? 234 THR A O 1 ATOM 1780 C CB . THR A 1 232 ? -2.655 -40.168 -27.108 1.00 44.11 ? 234 THR A CB 1 ATOM 1781 O OG1 . THR A 1 232 ? -4.105 -40.211 -27.180 1.00 45.70 ? 234 THR A OG1 1 ATOM 1782 C CG2 . THR A 1 232 ? -2.081 -41.570 -27.057 1.00 46.49 ? 234 THR A CG2 1 ATOM 1783 N N . SER A 1 233 ? 0.110 -39.806 -25.270 1.00 47.49 ? 235 SER A N 1 ATOM 1784 C CA . SER A 1 233 ? 1.578 -39.662 -25.409 1.00 49.16 ? 235 SER A CA 1 ATOM 1785 C C . SER A 1 233 ? 2.073 -40.154 -26.794 1.00 48.53 ? 235 SER A C 1 ATOM 1786 O O . SER A 1 233 ? 1.439 -40.993 -27.414 1.00 48.21 ? 235 SER A O 1 ATOM 1787 C CB . SER A 1 233 ? 2.289 -40.438 -24.312 1.00 50.33 ? 235 SER A CB 1 ATOM 1788 O OG . SER A 1 233 ? 2.331 -41.808 -24.664 1.00 54.07 ? 235 SER A OG 1 ATOM 1789 N N . LEU A 1 234 ? 3.180 -39.614 -27.278 1.00 49.68 ? 236 LEU A N 1 ATOM 1790 C CA . LEU A 1 234 ? 3.813 -40.118 -28.508 1.00 51.38 ? 236 LEU A CA 1 ATOM 1791 C C . LEU A 1 234 ? 4.033 -41.622 -28.465 1.00 51.71 ? 236 LEU A C 1 ATOM 1792 O O . LEU A 1 234 ? 3.661 -42.364 -29.395 1.00 51.34 ? 236 LEU A O 1 ATOM 1793 C CB . LEU A 1 234 ? 5.157 -39.412 -28.749 1.00 53.00 ? 236 LEU A CB 1 ATOM 1794 C CG . LEU A 1 234 ? 5.006 -38.339 -29.840 1.00 55.85 ? 236 LEU A CG 1 ATOM 1795 C CD1 . LEU A 1 234 ? 3.497 -37.881 -30.049 1.00 47.81 ? 236 LEU A CD1 1 ATOM 1796 C CD2 . LEU A 1 234 ? 6.001 -37.149 -29.658 1.00 57.83 ? 236 LEU A CD2 1 ATOM 1797 N N . TYR A 1 235 ? 4.620 -42.063 -27.357 1.00 51.95 ? 237 TYR A N 1 ATOM 1798 C CA . TYR A 1 235 ? 4.770 -43.482 -27.080 1.00 52.85 ? 237 TYR A CA 1 ATOM 1799 C C . TYR A 1 235 ? 3.457 -44.280 -27.249 1.00 51.40 ? 237 TYR A C 1 ATOM 1800 O O . TYR A 1 235 ? 3.403 -45.267 -28.014 1.00 51.55 ? 237 TYR A O 1 ATOM 1801 C CB . TYR A 1 235 ? 5.425 -43.744 -25.694 1.00 53.75 ? 237 TYR A CB 1 ATOM 1802 C CG . TYR A 1 235 ? 5.607 -45.226 -25.402 0.50 58.16 ? 237 TYR A CG 1 ATOM 1803 C CD1 . TYR A 1 235 ? 6.293 -46.046 -26.297 0.50 61.48 ? 237 TYR A CD1 1 ATOM 1804 C CD2 . TYR A 1 235 ? 5.079 -45.812 -24.249 0.50 60.18 ? 237 TYR A CD2 1 ATOM 1805 C CE1 . TYR A 1 235 ? 6.450 -47.380 -26.064 0.50 65.26 ? 237 TYR A CE1 1 ATOM 1806 C CE2 . TYR A 1 235 ? 5.244 -47.178 -24.009 0.50 62.89 ? 237 TYR A CE2 1 ATOM 1807 C CZ . TYR A 1 235 ? 5.929 -47.947 -24.924 0.50 65.56 ? 237 TYR A CZ 1 ATOM 1808 O OH . TYR A 1 235 ? 6.125 -49.299 -24.722 0.50 69.48 ? 237 TYR A OH 1 ATOM 1809 N N A GLU A 1 236 ? 2.404 -43.892 -26.550 0.50 49.63 ? 238 GLU A N 1 ATOM 1810 N N B GLU A 1 236 ? 2.416 -43.853 -26.534 0.50 49.02 ? 238 GLU A N 1 ATOM 1811 C CA A GLU A 1 236 ? 1.203 -44.698 -26.667 0.50 49.24 ? 238 GLU A CA 1 ATOM 1812 C CA B GLU A 1 236 ? 1.120 -44.530 -26.582 0.50 47.96 ? 238 GLU A CA 1 ATOM 1813 C C A GLU A 1 236 ? 0.532 -44.591 -28.046 0.50 47.62 ? 238 GLU A C 1 ATOM 1814 C C B GLU A 1 236 ? 0.568 -44.568 -28.013 0.50 46.99 ? 238 GLU A C 1 ATOM 1815 O O A GLU A 1 236 ? -0.005 -45.577 -28.533 0.50 47.41 ? 238 GLU A O 1 ATOM 1816 O O B GLU A 1 236 ? 0.131 -45.610 -28.489 0.50 46.91 ? 238 GLU A O 1 ATOM 1817 C CB A GLU A 1 236 ? 0.244 -44.485 -25.493 0.50 48.77 ? 238 GLU A CB 1 ATOM 1818 C CB B GLU A 1 236 ? 0.099 -43.862 -25.640 0.50 46.57 ? 238 GLU A CB 1 ATOM 1819 C CG A GLU A 1 236 ? 0.385 -45.568 -24.420 0.50 52.29 ? 238 GLU A CG 1 ATOM 1820 C CG B GLU A 1 236 ? 0.398 -43.969 -24.140 0.50 46.67 ? 238 GLU A CG 1 ATOM 1821 C CD A GLU A 1 236 ? -0.579 -46.740 -24.625 0.50 57.18 ? 238 GLU A CD 1 ATOM 1822 C CD B GLU A 1 236 ? -0.610 -43.188 -23.284 0.50 45.87 ? 238 GLU A CD 1 ATOM 1823 O OE1 A GLU A 1 236 ? -0.716 -47.233 -25.773 0.50 58.59 ? 238 GLU A OE1 1 ATOM 1824 O OE1 B GLU A 1 236 ? -1.067 -42.103 -23.699 0.50 44.92 ? 238 GLU A OE1 1 ATOM 1825 O OE2 A GLU A 1 236 ? -1.205 -47.172 -23.622 0.50 59.63 ? 238 GLU A OE2 1 ATOM 1826 O OE2 B GLU A 1 236 ? -0.952 -43.663 -22.191 0.50 45.81 ? 238 GLU A OE2 1 ATOM 1827 N N . ALA A 1 237 ? 0.592 -43.417 -28.678 1.00 46.43 ? 239 ALA A N 1 ATOM 1828 C CA . ALA A 1 237 ? 0.100 -43.273 -30.067 1.00 45.89 ? 239 ALA A CA 1 ATOM 1829 C C . ALA A 1 237 ? 0.823 -44.229 -31.060 1.00 47.54 ? 239 ALA A C 1 ATOM 1830 O O . ALA A 1 237 ? 0.157 -45.048 -31.743 1.00 46.84 ? 239 ALA A O 1 ATOM 1831 C CB . ALA A 1 237 ? 0.211 -41.789 -30.536 1.00 44.31 ? 239 ALA A CB 1 ATOM 1832 N N . ARG A 1 238 ? 2.162 -44.158 -31.164 1.00 49.18 ? 240 ARG A N 1 ATOM 1833 C CA . ARG A 1 238 ? 2.864 -45.157 -32.050 1.00 51.79 ? 240 ARG A CA 1 ATOM 1834 C C . ARG A 1 238 ? 2.439 -46.571 -31.733 1.00 50.83 ? 240 ARG A C 1 ATOM 1835 O O . ARG A 1 238 ? 2.114 -47.295 -32.626 1.00 51.29 ? 240 ARG A O 1 ATOM 1836 C CB . ARG A 1 238 ? 4.418 -45.051 -32.078 1.00 54.31 ? 240 ARG A CB 1 ATOM 1837 C CG . ARG A 1 238 ? 4.962 -43.654 -32.607 1.00 59.38 ? 240 ARG A CG 1 ATOM 1838 C CD . ARG A 1 238 ? 6.202 -43.687 -33.574 1.00 63.72 ? 240 ARG A CD 1 ATOM 1839 N NE . ARG A 1 238 ? 6.994 -44.896 -33.356 1.00 70.31 ? 240 ARG A NE 1 ATOM 1840 C CZ . ARG A 1 238 ? 7.325 -45.776 -34.303 1.00 72.39 ? 240 ARG A CZ 1 ATOM 1841 N NH1 . ARG A 1 238 ? 6.942 -45.566 -35.564 1.00 73.18 ? 240 ARG A NH1 1 ATOM 1842 N NH2 . ARG A 1 238 ? 8.033 -46.861 -33.985 1.00 68.29 ? 240 ARG A NH2 1 ATOM 1843 N N . ASN A 1 239 ? 2.399 -46.945 -30.454 1.00 50.88 ? 241 ASN A N 1 ATOM 1844 C CA . ASN A 1 239 ? 2.075 -48.317 -30.076 1.00 52.27 ? 241 ASN A CA 1 ATOM 1845 C C . ASN A 1 239 ? 0.691 -48.708 -30.570 1.00 50.45 ? 241 ASN A C 1 ATOM 1846 O O . ASN A 1 239 ? 0.483 -49.877 -31.007 1.00 50.43 ? 241 ASN A O 1 ATOM 1847 C CB . ASN A 1 239 ? 2.152 -48.538 -28.545 1.00 53.90 ? 241 ASN A CB 1 ATOM 1848 C CG . ASN A 1 239 ? 2.410 -50.032 -28.145 1.00 61.19 ? 241 ASN A CG 1 ATOM 1849 O OD1 . ASN A 1 239 ? 3.352 -50.669 -28.624 1.00 59.79 ? 241 ASN A OD1 1 ATOM 1850 N ND2 . ASN A 1 239 ? 1.556 -50.560 -27.259 1.00 74.84 ? 241 ASN A ND2 1 ATOM 1851 N N . ARG A 1 240 ? -0.249 -47.748 -30.486 1.00 46.30 ? 242 ARG A N 1 ATOM 1852 C CA . ARG A 1 240 ? -1.626 -48.000 -30.859 1.00 43.75 ? 242 ARG A CA 1 ATOM 1853 C C . ARG A 1 240 ? -1.824 -48.076 -32.387 1.00 43.49 ? 242 ARG A C 1 ATOM 1854 O O . ARG A 1 240 ? -2.535 -48.985 -32.888 1.00 42.61 ? 242 ARG A O 1 ATOM 1855 C CB . ARG A 1 240 ? -2.580 -47.016 -30.158 1.00 42.33 ? 242 ARG A CB 1 ATOM 1856 C CG . ARG A 1 240 ? -2.576 -47.189 -28.649 1.00 43.91 ? 242 ARG A CG 1 ATOM 1857 C CD . ARG A 1 240 ? -3.339 -46.063 -27.994 1.00 44.59 ? 242 ARG A CD 1 ATOM 1858 N NE . ARG A 1 240 ? -3.152 -45.970 -26.538 1.00 45.62 ? 242 ARG A NE 1 ATOM 1859 C CZ . ARG A 1 240 ? -3.812 -45.106 -25.733 1.00 44.21 ? 242 ARG A CZ 1 ATOM 1860 N NH1 . ARG A 1 240 ? -4.730 -44.239 -26.193 1.00 37.43 ? 242 ARG A NH1 1 ATOM 1861 N NH2 . ARG A 1 240 ? -3.551 -45.109 -24.438 1.00 42.99 ? 242 ARG A NH2 1 ATOM 1862 N N . THR A 1 241 ? -1.179 -47.161 -33.124 1.00 43.21 ? 243 THR A N 1 ATOM 1863 C CA . THR A 1 241 ? -1.143 -47.228 -34.586 1.00 44.71 ? 243 THR A CA 1 ATOM 1864 C C . THR A 1 241 ? -0.588 -48.610 -35.044 1.00 47.44 ? 243 THR A C 1 ATOM 1865 O O . THR A 1 241 ? -1.232 -49.278 -35.840 1.00 47.73 ? 243 THR A O 1 ATOM 1866 C CB . THR A 1 241 ? -0.270 -46.125 -35.148 1.00 45.15 ? 243 THR A CB 1 ATOM 1867 O OG1 . THR A 1 241 ? -0.853 -44.870 -34.832 1.00 43.32 ? 243 THR A OG1 1 ATOM 1868 C CG2 . THR A 1 241 ? -0.028 -46.253 -36.673 1.00 46.51 ? 243 THR A CG2 1 ATOM 1869 N N . LEU A 1 242 ? 0.551 -49.065 -34.512 1.00 49.04 ? 244 LEU A N 1 ATOM 1870 C CA . LEU A 1 242 ? 1.093 -50.393 -34.919 1.00 51.95 ? 244 LEU A CA 1 ATOM 1871 C C . LEU A 1 242 ? 0.298 -51.581 -34.395 1.00 52.14 ? 244 LEU A C 1 ATOM 1872 O O . LEU A 1 242 ? 0.220 -52.626 -35.058 1.00 52.86 ? 244 LEU A O 1 ATOM 1873 C CB . LEU A 1 242 ? 2.558 -50.595 -34.504 1.00 53.91 ? 244 LEU A CB 1 ATOM 1874 C CG . LEU A 1 242 ? 3.502 -49.428 -34.654 1.00 56.50 ? 244 LEU A CG 1 ATOM 1875 C CD1 . LEU A 1 242 ? 4.831 -49.719 -33.890 1.00 59.20 ? 244 LEU A CD1 1 ATOM 1876 C CD2 . LEU A 1 242 ? 3.678 -49.179 -36.163 1.00 58.68 ? 244 LEU A CD2 1 ATOM 1877 N N . ASN A 1 243 ? -0.272 -51.441 -33.203 1.00 51.18 ? 245 ASN A N 1 ATOM 1878 C CA . ASN A 1 243 ? -1.287 -52.394 -32.776 1.00 51.26 ? 245 ASN A CA 1 ATOM 1879 C C . ASN A 1 243 ? -2.483 -52.469 -33.751 1.00 50.71 ? 245 ASN A C 1 ATOM 1880 O O . ASN A 1 243 ? -2.848 -53.564 -34.165 1.00 53.06 ? 245 ASN A O 1 ATOM 1881 C CB . ASN A 1 243 ? -1.715 -52.116 -31.342 1.00 49.98 ? 245 ASN A CB 1 ATOM 1882 C CG . ASN A 1 243 ? -0.720 -52.660 -30.352 1.00 53.97 ? 245 ASN A CG 1 ATOM 1883 O OD1 . ASN A 1 243 ? 0.156 -53.471 -30.704 1.00 56.34 ? 245 ASN A OD1 1 ATOM 1884 N ND2 . ASN A 1 243 ? -0.816 -52.213 -29.125 1.00 54.12 ? 245 ASN A ND2 1 ATOM 1885 N N . LEU A 1 244 ? -3.045 -51.323 -34.148 1.00 48.44 ? 246 LEU A N 1 ATOM 1886 C CA . LEU A 1 244 ? -4.064 -51.304 -35.203 1.00 47.76 ? 246 LEU A CA 1 ATOM 1887 C C . LEU A 1 244 ? -3.619 -52.065 -36.492 1.00 49.23 ? 246 LEU A C 1 ATOM 1888 O O . LEU A 1 244 ? -4.401 -52.870 -37.018 1.00 49.34 ? 246 LEU A O 1 ATOM 1889 C CB . LEU A 1 244 ? -4.510 -49.880 -35.552 1.00 43.88 ? 246 LEU A CB 1 ATOM 1890 C CG . LEU A 1 244 ? -5.783 -49.889 -36.391 1.00 44.37 ? 246 LEU A CG 1 ATOM 1891 C CD1 . LEU A 1 244 ? -6.969 -50.646 -35.724 1.00 37.22 ? 246 LEU A CD1 1 ATOM 1892 C CD2 . LEU A 1 244 ? -6.171 -48.422 -36.713 1.00 39.15 ? 246 LEU A CD2 1 ATOM 1893 N N . ALA A 1 245 ? -2.382 -51.815 -36.968 1.00 49.36 ? 247 ALA A N 1 ATOM 1894 C CA . ALA A 1 245 ? -1.840 -52.480 -38.165 1.00 51.27 ? 247 ALA A CA 1 ATOM 1895 C C . ALA A 1 245 ? -1.809 -53.992 -37.996 1.00 53.16 ? 247 ALA A C 1 ATOM 1896 O O . ALA A 1 245 ? -2.317 -54.716 -38.848 1.00 55.15 ? 247 ALA A O 1 ATOM 1897 C CB . ALA A 1 245 ? -0.447 -51.956 -38.515 1.00 50.87 ? 247 ALA A CB 1 ATOM 1898 N N . LYS A 1 246 ? -1.186 -54.452 -36.916 1.00 54.61 ? 248 LYS A N 1 ATOM 1899 C CA . LYS A 1 246 ? -1.129 -55.860 -36.546 1.00 57.07 ? 248 LYS A CA 1 ATOM 1900 C C . LYS A 1 246 ? -2.542 -56.432 -36.672 1.00 56.41 ? 248 LYS A C 1 ATOM 1901 O O . LYS A 1 246 ? -2.764 -57.340 -37.452 1.00 57.11 ? 248 LYS A O 1 ATOM 1902 C CB . LYS A 1 246 ? -0.583 -55.960 -35.119 1.00 58.08 ? 248 LYS A CB 1 ATOM 1903 C CG . LYS A 1 246 ? -0.071 -57.333 -34.590 1.00 63.30 ? 248 LYS A CG 1 ATOM 1904 C CD . LYS A 1 246 ? 0.808 -57.030 -33.278 1.00 70.35 ? 248 LYS A CD 1 ATOM 1905 C CE . LYS A 1 246 ? 1.240 -58.291 -32.450 1.00 72.48 ? 248 LYS A CE 1 ATOM 1906 N NZ . LYS A 1 246 ? 2.027 -59.294 -33.283 1.00 76.18 ? 248 LYS A NZ 1 ATOM 1907 N N . LEU A 1 247 ? -3.522 -55.838 -35.988 1.00 54.44 ? 249 LEU A N 1 ATOM 1908 C CA . LEU A 1 247 ? -4.915 -56.375 -36.000 1.00 53.22 ? 249 LEU A CA 1 ATOM 1909 C C . LEU A 1 247 ? -5.613 -56.428 -37.367 1.00 53.06 ? 249 LEU A C 1 ATOM 1910 O O . LEU A 1 247 ? -6.478 -57.282 -37.603 1.00 53.76 ? 249 LEU A O 1 ATOM 1911 C CB . LEU A 1 247 ? -5.805 -55.612 -35.024 1.00 51.40 ? 249 LEU A CB 1 ATOM 1912 C CG . LEU A 1 247 ? -5.427 -55.753 -33.548 1.00 52.53 ? 249 LEU A CG 1 ATOM 1913 C CD1 . LEU A 1 247 ? -5.839 -54.548 -32.693 1.00 49.05 ? 249 LEU A CD1 1 ATOM 1914 C CD2 . LEU A 1 247 ? -6.010 -57.067 -32.993 1.00 55.73 ? 249 LEU A CD2 1 ATOM 1915 N N . THR A 1 248 ? -5.241 -55.532 -38.268 1.00 51.83 ? 250 THR A N 1 ATOM 1916 C CA . THR A 1 248 ? -5.891 -55.453 -39.569 1.00 51.39 ? 250 THR A CA 1 ATOM 1917 C C . THR A 1 248 ? -5.033 -56.125 -40.630 1.00 54.07 ? 250 THR A C 1 ATOM 1918 O O . THR A 1 248 ? -5.392 -56.124 -41.813 1.00 55.36 ? 250 THR A O 1 ATOM 1919 C CB . THR A 1 248 ? -6.113 -53.998 -40.001 1.00 49.63 ? 250 THR A CB 1 ATOM 1920 O OG1 . THR A 1 248 ? -4.845 -53.318 -39.964 1.00 47.99 ? 250 THR A OG1 1 ATOM 1921 C CG2 . THR A 1 248 ? -7.126 -53.312 -39.099 1.00 44.93 ? 250 THR A CG2 1 ATOM 1922 N N . GLY A 1 249 ? -3.916 -56.710 -40.230 1.00 55.07 ? 251 GLY A N 1 ATOM 1923 C CA . GLY A 1 249 ? -3.090 -57.441 -41.219 1.00 57.58 ? 251 GLY A CA 1 ATOM 1924 C C . GLY A 1 249 ? -2.277 -56.462 -42.040 1.00 57.70 ? 251 GLY A C 1 ATOM 1925 O O . GLY A 1 249 ? -1.904 -56.764 -43.165 1.00 58.64 ? 251 GLY A O 1 ATOM 1926 N N . CYS A 1 250 ? -2.028 -55.277 -41.469 1.00 56.40 ? 252 CYS A N 1 ATOM 1927 C CA . CYS A 1 250 ? -1.299 -54.196 -42.146 1.00 56.80 ? 252 CYS A CA 1 ATOM 1928 C C . CYS A 1 250 ? 0.106 -53.910 -41.602 1.00 59.56 ? 252 CYS A C 1 ATOM 1929 O O . CYS A 1 250 ? 0.740 -52.921 -42.010 1.00 59.65 ? 252 CYS A O 1 ATOM 1930 C CB . CYS A 1 250 ? -2.101 -52.896 -42.098 1.00 53.95 ? 252 CYS A CB 1 ATOM 1931 S SG . CYS A 1 250 ? -3.453 -52.761 -43.275 1.00 50.02 ? 252 CYS A SG 1 ATOM 1932 N N . SER A 1 251 ? 0.612 -54.741 -40.691 1.00 62.48 ? 253 SER A N 1 ATOM 1933 C CA . SER A 1 251 ? 2.040 -54.636 -40.322 1.00 65.45 ? 253 SER A CA 1 ATOM 1934 C C . SER A 1 251 ? 2.907 -54.672 -41.606 1.00 68.24 ? 253 SER A C 1 ATOM 1935 O O . SER A 1 251 ? 2.769 -55.571 -42.424 1.00 69.28 ? 253 SER A O 1 ATOM 1936 C CB . SER A 1 251 ? 2.457 -55.727 -39.318 1.00 66.27 ? 253 SER A CB 1 ATOM 1937 O OG . SER A 1 251 ? 1.751 -55.585 -38.095 1.00 64.12 ? 253 SER A OG 1 ATOM 1938 N N . ARG A 1 252 ? 3.715 -53.631 -41.797 1.00 70.15 ? 254 ARG A N 1 ATOM 1939 C CA . ARG A 1 252 ? 4.696 -53.497 -42.890 1.00 73.68 ? 254 ARG A CA 1 ATOM 1940 C C . ARG A 1 252 ? 5.942 -52.904 -42.260 1.00 75.68 ? 254 ARG A C 1 ATOM 1941 O O . ARG A 1 252 ? 5.928 -52.445 -41.122 1.00 74.95 ? 254 ARG A O 1 ATOM 1942 C CB . ARG A 1 252 ? 4.240 -52.526 -44.017 1.00 72.33 ? 254 ARG A CB 1 ATOM 1943 C CG . ARG A 1 252 ? 2.996 -52.903 -44.823 1.00 72.13 ? 254 ARG A CG 1 ATOM 1944 C CD . ARG A 1 252 ? 3.115 -54.229 -45.513 1.00 71.62 ? 254 ARG A CD 1 ATOM 1945 N NE . ARG A 1 252 ? 1.975 -54.446 -46.440 1.00 72.26 ? 254 ARG A NE 1 ATOM 1946 C CZ . ARG A 1 252 ? 0.835 -55.163 -46.155 1.00 71.19 ? 254 ARG A CZ 1 ATOM 1947 N NH1 . ARG A 1 252 ? -0.117 -55.279 -47.066 1.00 71.49 ? 254 ARG A NH1 1 ATOM 1948 N NH2 . ARG A 1 252 ? 0.664 -55.749 -44.955 1.00 70.58 ? 254 ARG A NH2 1 ATOM 1949 N N . GLU A 1 253 ? 7.012 -52.881 -43.029 1.00 79.45 ? 255 GLU A N 1 ATOM 1950 C CA . GLU A 1 253 ? 8.264 -52.319 -42.580 1.00 81.67 ? 255 GLU A CA 1 ATOM 1951 C C . GLU A 1 253 ? 8.402 -50.797 -42.897 1.00 80.65 ? 255 GLU A C 1 ATOM 1952 O O . GLU A 1 253 ? 8.847 -50.018 -42.050 1.00 79.46 ? 255 GLU A O 1 ATOM 1953 C CB . GLU A 1 253 ? 9.435 -53.194 -43.069 1.00 84.73 ? 255 GLU A CB 1 ATOM 1954 C CG . GLU A 1 253 ? 9.348 -53.911 -44.519 1.00 90.86 ? 255 GLU A CG 1 ATOM 1955 C CD . GLU A 1 253 ? 7.935 -54.428 -45.008 1.00 92.46 ? 255 GLU A CD 1 ATOM 1956 O OE1 . GLU A 1 253 ? 7.059 -53.561 -45.290 1.00 89.95 ? 255 GLU A OE1 1 ATOM 1957 O OE2 . GLU A 1 253 ? 7.743 -55.678 -45.182 1.00 91.96 ? 255 GLU A OE2 1 ATOM 1958 N N . ASN A 1 254 ? 8.010 -50.377 -44.100 1.00 81.22 ? 256 ASN A N 1 ATOM 1959 C CA . ASN A 1 254 ? 7.970 -48.959 -44.471 1.00 80.18 ? 256 ASN A CA 1 ATOM 1960 C C . ASN A 1 254 ? 6.684 -48.487 -43.822 1.00 76.75 ? 256 ASN A C 1 ATOM 1961 O O . ASN A 1 254 ? 5.628 -49.107 -44.030 1.00 76.98 ? 256 ASN A O 1 ATOM 1962 C CB . ASN A 1 254 ? 7.925 -48.847 -46.010 1.00 82.99 ? 256 ASN A CB 1 ATOM 1963 C CG . ASN A 1 254 ? 7.978 -47.408 -46.555 1.00 87.92 ? 256 ASN A CG 1 ATOM 1964 O OD1 . ASN A 1 254 ? 7.564 -46.453 -45.906 1.00 88.40 ? 256 ASN A OD1 1 ATOM 1965 N ND2 . ASN A 1 254 ? 8.477 -47.275 -47.797 1.00 100.87 ? 256 ASN A ND2 1 ATOM 1966 N N . GLU A 1 255 ? 6.768 -47.438 -42.996 1.00 72.53 ? 257 GLU A N 1 ATOM 1967 C CA . GLU A 1 255 ? 5.594 -46.914 -42.302 1.00 68.10 ? 257 GLU A CA 1 ATOM 1968 C C . GLU A 1 255 ? 4.589 -46.248 -43.227 1.00 64.93 ? 257 GLU A C 1 ATOM 1969 O O . GLU A 1 255 ? 3.412 -46.264 -42.915 1.00 62.47 ? 257 GLU A O 1 ATOM 1970 C CB . GLU A 1 255 ? 5.972 -45.931 -41.178 1.00 67.43 ? 257 GLU A CB 1 ATOM 1971 C CG . GLU A 1 255 ? 6.888 -46.530 -40.093 1.00 68.33 ? 257 GLU A CG 1 ATOM 1972 C CD . GLU A 1 255 ? 7.061 -45.613 -38.865 1.00 67.98 ? 257 GLU A CD 1 ATOM 1973 O OE1 . GLU A 1 255 ? 6.900 -44.353 -38.963 1.00 59.48 ? 257 GLU A OE1 1 ATOM 1974 O OE2 . GLU A 1 255 ? 7.384 -46.201 -37.800 1.00 70.00 ? 257 GLU A OE2 1 ATOM 1975 N N . THR A 1 256 ? 5.051 -45.673 -44.348 1.00 62.80 ? 258 THR A N 1 ATOM 1976 C CA . THR A 1 256 ? 4.157 -45.050 -45.337 1.00 59.37 ? 258 THR A CA 1 ATOM 1977 C C . THR A 1 256 ? 3.320 -46.129 -45.998 0.50 58.43 ? 258 THR A C 1 ATOM 1978 O O . THR A 1 256 ? 2.234 -45.883 -46.515 0.50 57.02 ? 258 THR A O 1 ATOM 1979 C CB . THR A 1 256 ? 4.917 -44.195 -46.380 0.50 59.94 ? 258 THR A CB 1 ATOM 1980 O OG1 . THR A 1 256 ? 5.603 -43.133 -45.713 0.50 58.52 ? 258 THR A OG1 1 ATOM 1981 C CG2 . THR A 1 256 ? 3.950 -43.573 -47.383 0.50 58.90 ? 258 THR A CG2 1 ATOM 1982 N N . GLU A 1 257 ? 3.841 -47.340 -45.922 1.00 58.50 ? 259 GLU A N 1 ATOM 1983 C CA . GLU A 1 257 ? 3.179 -48.527 -46.453 1.00 58.60 ? 259 GLU A CA 1 ATOM 1984 C C . GLU A 1 257 ? 2.115 -49.072 -45.490 1.00 54.88 ? 259 GLU A C 1 ATOM 1985 O O . GLU A 1 257 ? 1.077 -49.501 -45.909 1.00 54.05 ? 259 GLU A O 1 ATOM 1986 C CB . GLU A 1 257 ? 4.192 -49.627 -46.804 1.00 61.54 ? 259 GLU A CB 1 ATOM 1987 C CG . GLU A 1 257 ? 4.709 -49.612 -48.242 1.00 67.74 ? 259 GLU A CG 1 ATOM 1988 C CD . GLU A 1 257 ? 5.533 -50.858 -48.539 1.00 77.03 ? 259 GLU A CD 1 ATOM 1989 O OE1 . GLU A 1 257 ? 4.925 -51.966 -48.528 1.00 83.43 ? 259 GLU A OE1 1 ATOM 1990 O OE2 . GLU A 1 257 ? 6.770 -50.755 -48.776 1.00 78.36 ? 259 GLU A OE2 1 ATOM 1991 N N . ILE A 1 258 ? 2.391 -49.069 -44.204 1.00 53.25 ? 260 ILE A N 1 ATOM 1992 C CA . ILE A 1 258 ? 1.346 -49.331 -43.204 1.00 52.40 ? 260 ILE A CA 1 ATOM 1993 C C . ILE A 1 258 ? 0.089 -48.495 -43.447 1.00 49.26 ? 260 ILE A C 1 ATOM 1994 O O . ILE A 1 258 ? -1.018 -49.027 -43.499 1.00 48.58 ? 260 ILE A O 1 ATOM 1995 C CB . ILE A 1 258 ? 1.838 -49.136 -41.755 1.00 51.58 ? 260 ILE A CB 1 ATOM 1996 C CG1 . ILE A 1 258 ? 2.874 -50.207 -41.427 1.00 54.37 ? 260 ILE A CG1 1 ATOM 1997 C CG2 . ILE A 1 258 ? 0.677 -49.248 -40.756 1.00 50.51 ? 260 ILE A CG2 1 ATOM 1998 C CD1 . ILE A 1 258 ? 3.697 -49.781 -40.209 1.00 60.50 ? 260 ILE A CD1 1 ATOM 1999 N N . ILE A 1 259 ? 0.293 -47.217 -43.686 1.00 47.50 ? 261 ILE A N 1 ATOM 2000 C CA . ILE A 1 259 ? -0.809 -46.278 -43.856 1.00 46.51 ? 261 ILE A CA 1 ATOM 2001 C C . ILE A 1 259 ? -1.524 -46.535 -45.157 1.00 47.03 ? 261 ILE A C 1 ATOM 2002 O O . ILE A 1 259 ? -2.753 -46.445 -45.209 1.00 45.79 ? 261 ILE A O 1 ATOM 2003 C CB . ILE A 1 259 ? -0.363 -44.803 -43.808 1.00 44.77 ? 261 ILE A CB 1 ATOM 2004 C CG1 . ILE A 1 259 ? 0.367 -44.507 -42.496 1.00 45.00 ? 261 ILE A CG1 1 ATOM 2005 C CG2 . ILE A 1 259 ? -1.581 -43.877 -43.955 1.00 45.20 ? 261 ILE A CG2 1 ATOM 2006 C CD1 . ILE A 1 259 ? -0.516 -44.793 -41.252 1.00 49.08 ? 261 ILE A CD1 1 ATOM 2007 N N . LYS A 1 260 ? -0.755 -46.845 -46.194 1.00 48.17 ? 262 LYS A N 1 ATOM 2008 C CA . LYS A 1 260 ? -1.338 -47.132 -47.481 1.00 50.43 ? 262 LYS A CA 1 ATOM 2009 C C . LYS A 1 260 ? -2.217 -48.386 -47.351 1.00 50.51 ? 262 LYS A C 1 ATOM 2010 O O . LYS A 1 260 ? -3.363 -48.358 -47.809 1.00 50.74 ? 262 LYS A O 1 ATOM 2011 C CB . LYS A 1 260 ? -0.257 -47.214 -48.562 1.00 52.04 ? 262 LYS A CB 1 ATOM 2012 C CG . LYS A 1 260 ? -0.583 -48.016 -49.803 1.00 58.76 ? 262 LYS A CG 1 ATOM 2013 C CD . LYS A 1 260 ? -1.506 -47.281 -50.817 1.00 66.64 ? 262 LYS A CD 1 ATOM 2014 C CE . LYS A 1 260 ? -1.640 -48.048 -52.171 1.00 71.15 ? 262 LYS A CE 1 ATOM 2015 N NZ . LYS A 1 260 ? -0.326 -48.245 -52.841 1.00 74.98 ? 262 LYS A NZ 1 ATOM 2016 N N . CYS A 1 261 ? -1.710 -49.442 -46.687 1.00 50.39 ? 263 CYS A N 1 ATOM 2017 C CA . CYS A 1 261 ? -2.520 -50.649 -46.383 1.00 49.98 ? 263 CYS A CA 1 ATOM 2018 C C . CYS A 1 261 ? -3.800 -50.244 -45.608 1.00 48.62 ? 263 CYS A C 1 ATOM 2019 O O . CYS A 1 261 ? -4.893 -50.669 -45.961 1.00 47.93 ? 263 CYS A O 1 ATOM 2020 C CB . CYS A 1 261 ? -1.717 -51.677 -45.570 1.00 50.83 ? 263 CYS A CB 1 ATOM 2021 S SG . CYS A 1 261 ? -2.585 -53.203 -45.071 1.00 50.27 ? 263 CYS A SG 1 ATOM 2022 N N . LEU A 1 262 ? -3.644 -49.408 -44.574 1.00 47.03 ? 264 LEU A N 1 ATOM 2023 C CA . LEU A 1 262 ? -4.757 -48.987 -43.744 1.00 45.62 ? 264 LEU A CA 1 ATOM 2024 C C . LEU A 1 262 ? -5.797 -48.222 -44.546 1.00 45.37 ? 264 LEU A C 1 ATOM 2025 O O . LEU A 1 262 ? -6.958 -48.253 -44.198 1.00 44.56 ? 264 LEU A O 1 ATOM 2026 C CB . LEU A 1 262 ? -4.294 -48.208 -42.531 1.00 43.84 ? 264 LEU A CB 1 ATOM 2027 C CG . LEU A 1 262 ? -3.811 -49.059 -41.348 1.00 45.60 ? 264 LEU A CG 1 ATOM 2028 C CD1 . LEU A 1 262 ? -3.185 -48.166 -40.302 1.00 40.70 ? 264 LEU A CD1 1 ATOM 2029 C CD2 . LEU A 1 262 ? -4.947 -49.935 -40.717 1.00 46.29 ? 264 LEU A CD2 1 ATOM 2030 N N . ARG A 1 263 ? -5.381 -47.616 -45.657 1.00 46.38 ? 265 ARG A N 1 ATOM 2031 C CA . ARG A 1 263 ? -6.254 -46.896 -46.546 1.00 46.66 ? 265 ARG A CA 1 ATOM 2032 C C . ARG A 1 263 ? -7.068 -47.838 -47.434 1.00 50.03 ? 265 ARG A C 1 ATOM 2033 O O . ARG A 1 263 ? -8.085 -47.427 -47.990 1.00 50.63 ? 265 ARG A O 1 ATOM 2034 C CB . ARG A 1 263 ? -5.437 -45.913 -47.381 1.00 46.75 ? 265 ARG A CB 1 ATOM 2035 C CG . ARG A 1 263 ? -5.141 -44.545 -46.647 1.00 46.55 ? 265 ARG A CG 1 ATOM 2036 C CD . ARG A 1 263 ? -4.867 -43.429 -47.655 1.00 48.82 ? 265 ARG A CD 1 ATOM 2037 N NE . ARG A 1 263 ? -3.565 -42.864 -47.353 1.00 58.28 ? 265 ARG A NE 1 ATOM 2038 C CZ . ARG A 1 263 ? -2.411 -43.171 -47.957 1.00 58.92 ? 265 ARG A CZ 1 ATOM 2039 N NH1 . ARG A 1 263 ? -1.312 -42.589 -47.515 1.00 58.97 ? 265 ARG A NH1 1 ATOM 2040 N NH2 . ARG A 1 263 ? -2.350 -44.013 -48.997 1.00 62.80 ? 265 ARG A NH2 1 ATOM 2041 N N . ASN A 1 264 ? -6.633 -49.088 -47.588 1.00 52.38 ? 266 ASN A N 1 ATOM 2042 C CA . ASN A 1 264 ? -7.416 -50.058 -48.323 1.00 55.10 ? 266 ASN A CA 1 ATOM 2043 C C . ASN A 1 264 ? -8.409 -50.787 -47.462 1.00 55.24 ? 266 ASN A C 1 ATOM 2044 O O . ASN A 1 264 ? -9.222 -51.530 -47.980 1.00 57.01 ? 266 ASN A O 1 ATOM 2045 C CB . ASN A 1 264 ? -6.528 -51.071 -49.061 1.00 58.15 ? 266 ASN A CB 1 ATOM 2046 C CG . ASN A 1 264 ? -5.687 -50.430 -50.161 1.00 61.84 ? 266 ASN A CG 1 ATOM 2047 O OD1 . ASN A 1 264 ? -5.937 -49.292 -50.573 1.00 64.03 ? 266 ASN A OD1 1 ATOM 2048 N ND2 . ASN A 1 264 ? -4.670 -51.163 -50.641 1.00 67.88 ? 266 ASN A ND2 1 ATOM 2049 N N . LYS A 1 265 ? -8.364 -50.605 -46.146 1.00 54.39 ? 267 LYS A N 1 ATOM 2050 C CA . LYS A 1 265 ? -9.321 -51.303 -45.279 1.00 53.62 ? 267 LYS A CA 1 ATOM 2051 C C . LYS A 1 265 ? -10.711 -50.688 -45.308 1.00 52.82 ? 267 LYS A C 1 ATOM 2052 O O . LYS A 1 265 ? -10.841 -49.457 -45.394 1.00 52.91 ? 267 LYS A O 1 ATOM 2053 C CB . LYS A 1 265 ? -8.807 -51.376 -43.844 1.00 52.80 ? 267 LYS A CB 1 ATOM 2054 C CG . LYS A 1 265 ? -7.474 -52.105 -43.654 1.00 52.89 ? 267 LYS A CG 1 ATOM 2055 C CD . LYS A 1 265 ? -7.364 -53.439 -44.445 1.00 59.15 ? 267 LYS A CD 1 ATOM 2056 C CE . LYS A 1 265 ? -7.949 -54.644 -43.725 1.00 61.90 ? 267 LYS A CE 1 ATOM 2057 N NZ . LYS A 1 265 ? -7.584 -55.969 -44.395 1.00 64.76 ? 267 LYS A NZ 1 ATOM 2058 N N . ASP A 1 266 ? -11.742 -51.538 -45.246 1.00 53.09 ? 268 ASP A N 1 ATOM 2059 C CA . ASP A 1 266 ? -13.121 -51.099 -45.052 1.00 51.83 ? 268 ASP A CA 1 ATOM 2060 C C . ASP A 1 266 ? -13.219 -50.279 -43.738 1.00 50.14 ? 268 ASP A C 1 ATOM 2061 O O . ASP A 1 266 ? -12.665 -50.684 -42.702 1.00 49.28 ? 268 ASP A O 1 ATOM 2062 C CB . ASP A 1 266 ? -14.085 -52.292 -44.931 1.00 52.25 ? 268 ASP A CB 1 ATOM 2063 C CG . ASP A 1 266 ? -14.313 -53.034 -46.257 0.50 53.57 ? 268 ASP A CG 1 ATOM 2064 O OD1 . ASP A 1 266 ? -14.746 -54.210 -46.182 0.50 52.52 ? 268 ASP A OD1 1 ATOM 2065 O OD2 . ASP A 1 266 ? -14.090 -52.460 -47.351 0.50 49.00 ? 268 ASP A OD2 1 ATOM 2066 N N . PRO A 1 267 ? -13.995 -49.183 -43.749 1.00 48.57 ? 269 PRO A N 1 ATOM 2067 C CA . PRO A 1 267 ? -13.965 -48.471 -42.479 1.00 46.99 ? 269 PRO A CA 1 ATOM 2068 C C . PRO A 1 267 ? -14.414 -49.332 -41.293 1.00 46.49 ? 269 PRO A C 1 ATOM 2069 O O . PRO A 1 267 ? -13.951 -49.084 -40.167 1.00 45.28 ? 269 PRO A O 1 ATOM 2070 C CB . PRO A 1 267 ? -14.832 -47.230 -42.707 1.00 46.17 ? 269 PRO A CB 1 ATOM 2071 C CG . PRO A 1 267 ? -15.294 -47.297 -44.196 1.00 47.99 ? 269 PRO A CG 1 ATOM 2072 C CD . PRO A 1 267 ? -14.511 -48.381 -44.869 1.00 48.67 ? 269 PRO A CD 1 ATOM 2073 N N . GLN A 1 268 ? -15.218 -50.375 -41.546 1.00 46.47 ? 270 GLN A N 1 ATOM 2074 C CA . GLN A 1 268 ? -15.715 -51.253 -40.462 1.00 46.21 ? 270 GLN A CA 1 ATOM 2075 C C . GLN A 1 268 ? -14.603 -52.024 -39.779 1.00 46.57 ? 270 GLN A C 1 ATOM 2076 O O . GLN A 1 268 ? -14.668 -52.276 -38.561 1.00 47.24 ? 270 GLN A O 1 ATOM 2077 C CB . GLN A 1 268 ? -16.715 -52.313 -40.988 1.00 47.36 ? 270 GLN A CB 1 ATOM 2078 C CG . GLN A 1 268 ? -18.188 -52.078 -40.671 1.00 47.62 ? 270 GLN A CG 1 ATOM 2079 C CD . GLN A 1 268 ? -18.483 -51.407 -39.330 0.50 45.61 ? 270 GLN A CD 1 ATOM 2080 O OE1 . GLN A 1 268 ? -18.496 -52.050 -38.278 0.50 46.07 ? 270 GLN A OE1 1 ATOM 2081 N NE2 . GLN A 1 268 ? -18.765 -50.115 -39.380 0.50 40.85 ? 270 GLN A NE2 1 ATOM 2082 N N . GLU A 1 269 ? -13.594 -52.430 -40.550 1.00 46.19 ? 271 GLU A N 1 ATOM 2083 C CA . GLU A 1 269 ? -12.509 -53.217 -39.969 1.00 46.60 ? 271 GLU A CA 1 ATOM 2084 C C . GLU A 1 269 ? -11.623 -52.345 -39.050 1.00 45.75 ? 271 GLU A C 1 ATOM 2085 O O . GLU A 1 269 ? -11.132 -52.809 -37.998 1.00 45.86 ? 271 GLU A O 1 ATOM 2086 C CB . GLU A 1 269 ? -11.671 -53.903 -41.068 1.00 48.66 ? 271 GLU A CB 1 ATOM 2087 C CG . GLU A 1 269 ? -10.899 -55.129 -40.554 0.50 50.21 ? 271 GLU A CG 1 ATOM 2088 C CD . GLU A 1 269 ? -10.074 -55.811 -41.619 0.50 52.39 ? 271 GLU A CD 1 ATOM 2089 O OE1 . GLU A 1 269 ? -8.982 -56.330 -41.276 0.50 52.65 ? 271 GLU A OE1 1 ATOM 2090 O OE2 . GLU A 1 269 ? -10.515 -55.826 -42.796 0.50 53.85 ? 271 GLU A OE2 1 ATOM 2091 N N . ILE A 1 270 ? -11.435 -51.080 -39.433 1.00 43.62 ? 272 ILE A N 1 ATOM 2092 C CA . ILE A 1 270 ? -10.735 -50.155 -38.603 1.00 42.38 ? 272 ILE A CA 1 ATOM 2093 C C . ILE A 1 270 ? -11.551 -49.989 -37.315 1.00 41.79 ? 272 ILE A C 1 ATOM 2094 O O . ILE A 1 270 ? -10.991 -50.166 -36.200 1.00 41.89 ? 272 ILE A O 1 ATOM 2095 C CB . ILE A 1 270 ? -10.529 -48.846 -39.348 1.00 42.00 ? 272 ILE A CB 1 ATOM 2096 C CG1 . ILE A 1 270 ? -9.388 -49.054 -40.334 1.00 44.65 ? 272 ILE A CG1 1 ATOM 2097 C CG2 . ILE A 1 270 ? -10.196 -47.669 -38.388 1.00 41.98 ? 272 ILE A CG2 1 ATOM 2098 C CD1 . ILE A 1 270 ? -9.386 -48.153 -41.522 1.00 47.01 ? 272 ILE A CD1 1 ATOM 2099 N N . LEU A 1 271 ? -12.857 -49.698 -37.440 1.00 40.78 ? 273 LEU A N 1 ATOM 2100 C CA . LEU A 1 271 ? -13.699 -49.478 -36.232 1.00 38.83 ? 273 LEU A CA 1 ATOM 2101 C C . LEU A 1 271 ? -13.716 -50.693 -35.306 1.00 39.89 ? 273 LEU A C 1 ATOM 2102 O O . LEU A 1 271 ? -13.654 -50.535 -34.051 1.00 36.84 ? 273 LEU A O 1 ATOM 2103 C CB . LEU A 1 271 ? -15.137 -49.118 -36.582 1.00 36.67 ? 273 LEU A CB 1 ATOM 2104 C CG . LEU A 1 271 ? -15.317 -47.756 -37.266 1.00 37.45 ? 273 LEU A CG 1 ATOM 2105 C CD1 . LEU A 1 271 ? -16.739 -47.695 -37.852 1.00 38.06 ? 273 LEU A CD1 1 ATOM 2106 C CD2 . LEU A 1 271 ? -15.115 -46.617 -36.270 1.00 31.41 ? 273 LEU A CD2 1 ATOM 2107 N N . LEU A 1 272 ? -13.804 -51.902 -35.919 1.00 41.96 ? 274 LEU A N 1 ATOM 2108 C CA . LEU A 1 272 ? -13.955 -53.107 -35.107 1.00 43.88 ? 274 LEU A CA 1 ATOM 2109 C C . LEU A 1 272 ? -12.693 -53.343 -34.265 1.00 45.03 ? 274 LEU A C 1 ATOM 2110 O O . LEU A 1 272 ? -12.780 -53.861 -33.153 1.00 45.87 ? 274 LEU A O 1 ATOM 2111 C CB . LEU A 1 272 ? -14.436 -54.345 -35.916 1.00 46.30 ? 274 LEU A CB 1 ATOM 2112 C CG . LEU A 1 272 ? -15.971 -54.540 -36.098 0.50 45.19 ? 274 LEU A CG 1 ATOM 2113 C CD1 . LEU A 1 272 ? -16.802 -53.250 -35.929 0.50 43.87 ? 274 LEU A CD1 1 ATOM 2114 C CD2 . LEU A 1 272 ? -16.309 -55.178 -37.430 0.50 47.06 ? 274 LEU A CD2 1 ATOM 2115 N N . ASN A 1 273 ? -11.527 -52.877 -34.736 1.00 45.71 ? 275 ASN A N 1 ATOM 2116 C CA . ASN A 1 273 ? -10.264 -53.158 -34.017 1.00 45.90 ? 275 ASN A CA 1 ATOM 2117 C C . ASN A 1 273 ? -9.771 -52.060 -33.068 1.00 46.29 ? 275 ASN A C 1 ATOM 2118 O O . ASN A 1 273 ? -8.824 -52.280 -32.307 1.00 47.39 ? 275 ASN A O 1 ATOM 2119 C CB . ASN A 1 273 ? -9.173 -53.573 -34.997 1.00 45.44 ? 275 ASN A CB 1 ATOM 2120 C CG . ASN A 1 273 ? -9.428 -54.944 -35.578 1.00 48.27 ? 275 ASN A CG 1 ATOM 2121 O OD1 . ASN A 1 273 ? -9.785 -55.059 -36.735 1.00 50.69 ? 275 ASN A OD1 1 ATOM 2122 N ND2 . ASN A 1 273 ? -9.289 -55.986 -34.766 1.00 45.63 ? 275 ASN A ND2 1 ATOM 2123 N N . GLU A 1 274 ? -10.406 -50.895 -33.124 1.00 44.62 ? 276 GLU A N 1 ATOM 2124 C CA . GLU A 1 274 ? -10.028 -49.782 -32.298 1.00 45.43 ? 276 GLU A CA 1 ATOM 2125 C C . GLU A 1 274 ? -9.975 -50.137 -30.800 1.00 46.01 ? 276 GLU A C 1 ATOM 2126 O O . GLU A 1 274 ? -9.083 -49.647 -30.077 1.00 45.96 ? 276 GLU A O 1 ATOM 2127 C CB . GLU A 1 274 ? -10.996 -48.571 -32.543 1.00 44.13 ? 276 GLU A CB 1 ATOM 2128 C CG . GLU A 1 274 ? -10.738 -47.819 -33.859 1.00 44.31 ? 276 GLU A CG 1 ATOM 2129 C CD . GLU A 1 274 ? -11.638 -46.587 -34.077 1.00 44.90 ? 276 GLU A CD 1 ATOM 2130 O OE1 . GLU A 1 274 ? -12.582 -46.317 -33.275 1.00 43.17 ? 276 GLU A OE1 1 ATOM 2131 O OE2 . GLU A 1 274 ? -11.397 -45.882 -35.088 1.00 43.74 ? 276 GLU A OE2 1 ATOM 2132 N N . ALA A 1 275 ? -10.930 -50.943 -30.326 1.00 46.77 ? 277 ALA A N 1 ATOM 2133 C CA . ALA A 1 275 ? -11.064 -51.197 -28.890 1.00 48.24 ? 277 ALA A CA 1 ATOM 2134 C C . ALA A 1 275 ? -9.847 -51.978 -28.377 1.00 50.54 ? 277 ALA A C 1 ATOM 2135 O O . ALA A 1 275 ? -9.351 -51.779 -27.256 1.00 50.75 ? 277 ALA A O 1 ATOM 2136 C CB . ALA A 1 275 ? -12.381 -51.954 -28.593 1.00 48.76 ? 277 ALA A CB 1 ATOM 2137 N N . PHE A 1 276 ? -9.309 -52.803 -29.256 1.00 52.92 ? 278 PHE A N 1 ATOM 2138 C CA . PHE A 1 276 ? -8.242 -53.697 -28.897 1.00 55.00 ? 278 PHE A CA 1 ATOM 2139 C C . PHE A 1 276 ? -6.813 -53.173 -29.037 1.00 54.89 ? 278 PHE A C 1 ATOM 2140 O O . PHE A 1 276 ? -5.905 -53.923 -28.738 1.00 55.38 ? 278 PHE A O 1 ATOM 2141 C CB . PHE A 1 276 ? -8.436 -55.002 -29.650 1.00 57.63 ? 278 PHE A CB 1 ATOM 2142 C CG . PHE A 1 276 ? -9.819 -55.515 -29.545 1.00 60.89 ? 278 PHE A CG 1 ATOM 2143 C CD1 . PHE A 1 276 ? -10.284 -56.017 -28.332 1.00 65.74 ? 278 PHE A CD1 1 ATOM 2144 C CD2 . PHE A 1 276 ? -10.677 -55.424 -30.614 1.00 65.44 ? 278 PHE A CD2 1 ATOM 2145 C CE1 . PHE A 1 276 ? -11.588 -56.458 -28.199 1.00 70.53 ? 278 PHE A CE1 1 ATOM 2146 C CE2 . PHE A 1 276 ? -11.981 -55.859 -30.509 1.00 69.60 ? 278 PHE A CE2 1 ATOM 2147 C CZ . PHE A 1 276 ? -12.447 -56.380 -29.298 1.00 71.40 ? 278 PHE A CZ 1 ATOM 2148 N N . VAL A 1 277 ? -6.599 -51.915 -29.445 1.00 52.72 ? 279 VAL A N 1 ATOM 2149 C CA . VAL A 1 277 ? -5.218 -51.415 -29.636 1.00 53.11 ? 279 VAL A CA 1 ATOM 2150 C C . VAL A 1 277 ? -4.473 -51.207 -28.305 1.00 54.21 ? 279 VAL A C 1 ATOM 2151 O O . VAL A 1 277 ? -3.276 -50.919 -28.253 1.00 55.42 ? 279 VAL A O 1 ATOM 2152 C CB . VAL A 1 277 ? -5.170 -50.161 -30.554 1.00 52.47 ? 279 VAL A CB 1 ATOM 2153 C CG1 . VAL A 1 277 ? -5.895 -50.460 -31.864 1.00 51.85 ? 279 VAL A CG1 1 ATOM 2154 C CG2 . VAL A 1 277 ? -5.855 -48.889 -29.867 1.00 48.80 ? 279 VAL A CG2 1 ATOM 2155 N N . VAL A 1 278 ? -5.198 -51.395 -27.220 1.00 55.46 ? 280 VAL A N 1 ATOM 2156 C CA . VAL A 1 278 ? -4.756 -51.135 -25.850 1.00 56.23 ? 280 VAL A CA 1 ATOM 2157 C C . VAL A 1 278 ? -4.894 -52.510 -25.103 1.00 59.05 ? 280 VAL A C 1 ATOM 2158 O O . VAL A 1 278 ? -5.861 -53.263 -25.364 1.00 59.17 ? 280 VAL A O 1 ATOM 2159 C CB . VAL A 1 278 ? -5.703 -50.032 -25.261 1.00 54.99 ? 280 VAL A CB 1 ATOM 2160 C CG1 . VAL A 1 278 ? -6.287 -50.430 -23.941 1.00 55.14 ? 280 VAL A CG1 1 ATOM 2161 C CG2 . VAL A 1 278 ? -5.027 -48.638 -25.209 1.00 52.75 ? 280 VAL A CG2 1 ATOM 2162 N N . PRO A 1 279 ? -3.959 -52.843 -24.181 1.00 60.74 ? 281 PRO A N 1 ATOM 2163 C CA . PRO A 1 279 ? -4.104 -54.161 -23.487 1.00 63.53 ? 281 PRO A CA 1 ATOM 2164 C C . PRO A 1 279 ? -5.301 -54.250 -22.516 1.00 63.43 ? 281 PRO A C 1 ATOM 2165 O O . PRO A 1 279 ? -5.840 -55.336 -22.307 1.00 64.00 ? 281 PRO A O 1 ATOM 2166 C CB . PRO A 1 279 ? -2.767 -54.358 -22.746 1.00 64.02 ? 281 PRO A CB 1 ATOM 2167 C CG . PRO A 1 279 ? -2.133 -52.935 -22.659 1.00 63.78 ? 281 PRO A CG 1 ATOM 2168 C CD . PRO A 1 279 ? -2.881 -51.998 -23.617 1.00 61.16 ? 281 PRO A CD 1 ATOM 2169 N N . TYR A 1 280 ? -5.707 -53.120 -21.940 1.00 62.16 ? 282 TYR A N 1 ATOM 2170 C CA . TYR A 1 280 ? -6.892 -53.097 -21.079 1.00 62.56 ? 282 TYR A CA 1 ATOM 2171 C C . TYR A 1 280 ? -7.484 -51.696 -21.088 1.00 59.75 ? 282 TYR A C 1 ATOM 2172 O O . TYR A 1 280 ? -6.830 -50.728 -20.695 1.00 60.90 ? 282 TYR A O 1 ATOM 2173 C CB . TYR A 1 280 ? -6.545 -53.516 -19.630 1.00 63.90 ? 282 TYR A CB 1 ATOM 2174 C CG . TYR A 1 280 ? -5.202 -52.991 -19.182 1.00 68.39 ? 282 TYR A CG 1 ATOM 2175 C CD1 . TYR A 1 280 ? -4.124 -53.876 -18.879 1.00 73.90 ? 282 TYR A CD1 1 ATOM 2176 C CD2 . TYR A 1 280 ? -4.975 -51.602 -19.102 1.00 68.54 ? 282 TYR A CD2 1 ATOM 2177 C CE1 . TYR A 1 280 ? -2.866 -53.350 -18.462 1.00 75.61 ? 282 TYR A CE1 1 ATOM 2178 C CE2 . TYR A 1 280 ? -3.746 -51.068 -18.704 1.00 71.13 ? 282 TYR A CE2 1 ATOM 2179 C CZ . TYR A 1 280 ? -2.699 -51.926 -18.386 1.00 74.90 ? 282 TYR A CZ 1 ATOM 2180 O OH . TYR A 1 280 ? -1.513 -51.333 -18.017 1.00 75.68 ? 282 TYR A OH 1 ATOM 2181 N N . GLY A 1 281 ? -8.712 -51.534 -21.528 1.00 57.42 ? 283 GLY A N 1 ATOM 2182 C CA . GLY A 1 281 ? -9.237 -50.162 -21.444 1.00 53.49 ? 283 GLY A CA 1 ATOM 2183 C C . GLY A 1 281 ? -10.113 -50.031 -20.216 1.00 50.36 ? 283 GLY A C 1 ATOM 2184 O O . GLY A 1 281 ? -10.228 -50.953 -19.389 1.00 51.37 ? 283 GLY A O 1 ATOM 2185 N N . THR A 1 282 ? -10.759 -48.900 -20.123 1.00 45.03 ? 284 THR A N 1 ATOM 2186 C CA . THR A 1 282 ? -11.623 -48.647 -19.018 1.00 41.64 ? 284 THR A CA 1 ATOM 2187 C C . THR A 1 282 ? -12.845 -47.986 -19.678 1.00 39.36 ? 284 THR A C 1 ATOM 2188 O O . THR A 1 282 ? -12.835 -47.675 -20.875 1.00 38.31 ? 284 THR A O 1 ATOM 2189 C CB . THR A 1 282 ? -10.939 -47.673 -17.978 1.00 41.42 ? 284 THR A CB 1 ATOM 2190 O OG1 . THR A 1 282 ? -11.073 -46.356 -18.447 1.00 39.57 ? 284 THR A OG1 1 ATOM 2191 C CG2 . THR A 1 282 ? -9.444 -47.912 -17.768 1.00 37.02 ? 284 THR A CG2 1 ATOM 2192 N N . PRO A 1 283 ? -13.905 -47.742 -18.915 1.00 37.71 ? 285 PRO A N 1 ATOM 2193 C CA . PRO A 1 283 ? -14.999 -46.992 -19.575 1.00 35.91 ? 285 PRO A CA 1 ATOM 2194 C C . PRO A 1 283 ? -14.596 -45.597 -19.990 1.00 35.91 ? 285 PRO A C 1 ATOM 2195 O O . PRO A 1 283 ? -15.393 -44.881 -20.636 1.00 37.08 ? 285 PRO A O 1 ATOM 2196 C CB . PRO A 1 283 ? -16.036 -46.875 -18.478 1.00 35.19 ? 285 PRO A CB 1 ATOM 2197 C CG . PRO A 1 283 ? -15.775 -48.126 -17.597 1.00 36.55 ? 285 PRO A CG 1 ATOM 2198 C CD . PRO A 1 283 ? -14.275 -48.278 -17.591 1.00 36.70 ? 285 PRO A CD 1 ATOM 2199 N N . LEU A 1 284 ? -13.413 -45.151 -19.592 1.00 34.63 ? 286 LEU A N 1 ATOM 2200 C CA . LEU A 1 284 ? -13.030 -43.795 -19.897 1.00 34.31 ? 286 LEU A CA 1 ATOM 2201 C C . LEU A 1 284 ? -11.919 -43.749 -20.984 1.00 34.38 ? 286 LEU A C 1 ATOM 2202 O O . LEU A 1 284 ? -11.303 -42.704 -21.227 1.00 33.24 ? 286 LEU A O 1 ATOM 2203 C CB . LEU A 1 284 ? -12.598 -43.082 -18.598 1.00 35.35 ? 286 LEU A CB 1 ATOM 2204 C CG . LEU A 1 284 ? -13.839 -42.633 -17.805 1.00 34.84 ? 286 LEU A CG 1 ATOM 2205 C CD1 . LEU A 1 284 ? -14.056 -43.612 -16.701 1.00 33.61 ? 286 LEU A CD1 1 ATOM 2206 C CD2 . LEU A 1 284 ? -13.677 -41.233 -17.243 1.00 36.14 ? 286 LEU A CD2 1 ATOM 2207 N N . SER A 1 285 ? -11.707 -44.867 -21.671 1.00 33.80 ? 287 SER A N 1 ATOM 2208 C CA . SER A 1 285 ? -10.579 -44.967 -22.611 1.00 34.52 ? 287 SER A CA 1 ATOM 2209 C C . SER A 1 285 ? -10.711 -44.070 -23.811 1.00 33.29 ? 287 SER A C 1 ATOM 2210 O O . SER A 1 285 ? -11.757 -43.990 -24.420 1.00 34.07 ? 287 SER A O 1 ATOM 2211 C CB . SER A 1 285 ? -10.459 -46.412 -23.120 1.00 35.23 ? 287 SER A CB 1 ATOM 2212 O OG . SER A 1 285 ? -9.821 -47.184 -22.144 1.00 35.49 ? 287 SER A OG 1 ATOM 2213 N N . VAL A 1 286 ? -9.635 -43.390 -24.152 1.00 32.87 ? 288 VAL A N 1 ATOM 2214 C CA . VAL A 1 286 ? -9.620 -42.609 -25.346 1.00 30.80 ? 288 VAL A CA 1 ATOM 2215 C C . VAL A 1 286 ? -8.505 -43.237 -26.146 1.00 32.31 ? 288 VAL A C 1 ATOM 2216 O O . VAL A 1 286 ? -7.366 -42.854 -26.001 1.00 33.75 ? 288 VAL A O 1 ATOM 2217 C CB . VAL A 1 286 ? -9.398 -41.096 -25.043 1.00 30.29 ? 288 VAL A CB 1 ATOM 2218 C CG1 . VAL A 1 286 ? -9.070 -40.307 -26.309 1.00 24.83 ? 288 VAL A CG1 1 ATOM 2219 C CG2 . VAL A 1 286 ? -10.700 -40.496 -24.427 1.00 26.52 ? 288 VAL A CG2 1 ATOM 2220 N N . ASN A 1 287 ? -8.816 -44.203 -26.980 1.00 31.16 ? 289 ASN A N 1 ATOM 2221 C CA . ASN A 1 287 ? -7.727 -44.932 -27.643 1.00 33.19 ? 289 ASN A CA 1 ATOM 2222 C C . ASN A 1 287 ? -6.964 -44.071 -28.709 1.00 31.97 ? 289 ASN A C 1 ATOM 2223 O O . ASN A 1 287 ? -5.744 -44.200 -28.848 1.00 31.72 ? 289 ASN A O 1 ATOM 2224 C CB . ASN A 1 287 ? -8.261 -46.252 -28.231 1.00 33.43 ? 289 ASN A CB 1 ATOM 2225 C CG . ASN A 1 287 ? -8.436 -47.370 -27.156 1.00 39.19 ? 289 ASN A CG 1 ATOM 2226 O OD1 . ASN A 1 287 ? -9.096 -48.420 -27.399 1.00 44.63 ? 289 ASN A OD1 1 ATOM 2227 N ND2 . ASN A 1 287 ? -7.815 -47.185 -26.004 1.00 37.81 ? 289 ASN A ND2 1 ATOM 2228 N N . PHE A 1 288 ? -7.699 -43.206 -29.427 1.00 29.75 ? 290 PHE A N 1 ATOM 2229 C CA . PHE A 1 288 ? -7.172 -42.384 -30.520 1.00 29.51 ? 290 PHE A CA 1 ATOM 2230 C C . PHE A 1 288 ? -7.602 -40.984 -30.191 1.00 28.65 ? 290 PHE A C 1 ATOM 2231 O O . PHE A 1 288 ? -8.743 -40.668 -30.349 1.00 29.42 ? 290 PHE A O 1 ATOM 2232 C CB . PHE A 1 288 ? -7.734 -42.858 -31.898 1.00 28.35 ? 290 PHE A CB 1 ATOM 2233 C CG . PHE A 1 288 ? -7.137 -44.182 -32.345 1.00 32.37 ? 290 PHE A CG 1 ATOM 2234 C CD1 . PHE A 1 288 ? -5.831 -44.239 -32.840 1.00 31.43 ? 290 PHE A CD1 1 ATOM 2235 C CD2 . PHE A 1 288 ? -7.819 -45.381 -32.122 1.00 32.98 ? 290 PHE A CD2 1 ATOM 2236 C CE1 . PHE A 1 288 ? -5.241 -45.479 -33.189 1.00 35.54 ? 290 PHE A CE1 1 ATOM 2237 C CE2 . PHE A 1 288 ? -7.255 -46.625 -32.462 1.00 29.65 ? 290 PHE A CE2 1 ATOM 2238 C CZ . PHE A 1 288 ? -5.971 -46.684 -32.991 1.00 33.97 ? 290 PHE A CZ 1 ATOM 2239 N N . GLY A 1 289 ? -6.706 -40.162 -29.676 1.00 28.90 ? 291 GLY A N 1 ATOM 2240 C CA . GLY A 1 289 ? -7.060 -38.815 -29.265 1.00 27.23 ? 291 GLY A CA 1 ATOM 2241 C C . GLY A 1 289 ? -5.946 -37.859 -29.690 1.00 27.27 ? 291 GLY A C 1 ATOM 2242 O O . GLY A 1 289 ? -5.055 -38.228 -30.464 1.00 27.44 ? 291 GLY A O 1 ATOM 2243 N N . PRO A 1 290 ? -6.003 -36.614 -29.220 1.00 27.54 ? 292 PRO A N 1 ATOM 2244 C CA . PRO A 1 290 ? -4.985 -35.566 -29.547 1.00 27.47 ? 292 PRO A CA 1 ATOM 2245 C C . PRO A 1 290 ? -3.592 -36.050 -29.198 1.00 28.63 ? 292 PRO A C 1 ATOM 2246 O O . PRO A 1 290 ? -3.424 -36.802 -28.254 1.00 29.63 ? 292 PRO A O 1 ATOM 2247 C CB . PRO A 1 290 ? -5.402 -34.405 -28.641 1.00 26.07 ? 292 PRO A CB 1 ATOM 2248 C CG . PRO A 1 290 ? -6.956 -34.551 -28.556 1.00 26.55 ? 292 PRO A CG 1 ATOM 2249 C CD . PRO A 1 290 ? -7.171 -36.059 -28.491 1.00 26.29 ? 292 PRO A CD 1 ATOM 2250 N N . THR A 1 291 ? -2.600 -35.683 -29.976 1.00 29.29 ? 293 THR A N 1 ATOM 2251 C CA . THR A 1 291 ? -1.232 -36.005 -29.630 1.00 31.67 ? 293 THR A CA 1 ATOM 2252 C C . THR A 1 291 ? -0.449 -34.710 -29.796 1.00 31.23 ? 293 THR A C 1 ATOM 2253 O O . THR A 1 291 ? -0.988 -33.764 -30.393 1.00 33.55 ? 293 THR A O 1 ATOM 2254 C CB . THR A 1 291 ? -0.566 -37.022 -30.591 1.00 33.18 ? 293 THR A CB 1 ATOM 2255 O OG1 . THR A 1 291 ? -1.009 -36.776 -31.943 1.00 34.14 ? 293 THR A OG1 1 ATOM 2256 C CG2 . THR A 1 291 ? -0.902 -38.362 -30.176 1.00 35.85 ? 293 THR A CG2 1 ATOM 2257 N N . VAL A 1 292 ? 0.777 -34.664 -29.287 1.00 29.08 ? 294 VAL A N 1 ATOM 2258 C CA . VAL A 1 292 ? 1.690 -33.598 -29.625 1.00 29.54 ? 294 VAL A CA 1 ATOM 2259 C C . VAL A 1 292 ? 2.255 -33.857 -31.035 1.00 30.94 ? 294 VAL A C 1 ATOM 2260 O O . VAL A 1 292 ? 3.146 -34.666 -31.212 1.00 32.37 ? 294 VAL A O 1 ATOM 2261 C CB . VAL A 1 292 ? 2.863 -33.512 -28.581 1.00 29.92 ? 294 VAL A CB 1 ATOM 2262 C CG1 . VAL A 1 292 ? 3.826 -32.347 -28.905 1.00 31.54 ? 294 VAL A CG1 1 ATOM 2263 C CG2 . VAL A 1 292 ? 2.299 -33.360 -27.176 1.00 27.12 ? 294 VAL A CG2 1 ATOM 2264 N N . ASP A 1 293 ? 1.717 -33.210 -32.055 1.00 31.23 ? 295 ASP A N 1 ATOM 2265 C CA . ASP A 1 293 ? 2.142 -33.514 -33.427 1.00 33.25 ? 295 ASP A CA 1 ATOM 2266 C C . ASP A 1 293 ? 3.211 -32.536 -33.996 1.00 34.85 ? 295 ASP A C 1 ATOM 2267 O O . ASP A 1 293 ? 3.654 -32.683 -35.151 1.00 36.52 ? 295 ASP A O 1 ATOM 2268 C CB . ASP A 1 293 ? 0.917 -33.465 -34.325 1.00 32.45 ? 295 ASP A CB 1 ATOM 2269 C CG . ASP A 1 293 ? 0.231 -32.112 -34.261 1.00 30.62 ? 295 ASP A CG 1 ATOM 2270 O OD1 . ASP A 1 293 ? 0.606 -31.286 -33.393 1.00 31.08 ? 295 ASP A OD1 1 ATOM 2271 O OD2 . ASP A 1 293 ? -0.655 -31.842 -35.083 1.00 30.09 ? 295 ASP A OD2 1 ATOM 2272 N N . GLY A 1 294 ? 3.572 -31.508 -33.242 1.00 34.25 ? 296 GLY A N 1 ATOM 2273 C CA . GLY A 1 294 ? 4.512 -30.516 -33.769 1.00 35.22 ? 296 GLY A CA 1 ATOM 2274 C C . GLY A 1 294 ? 3.858 -29.562 -34.757 1.00 35.48 ? 296 GLY A C 1 ATOM 2275 O O . GLY A 1 294 ? 4.540 -28.809 -35.417 1.00 37.03 ? 296 GLY A O 1 ATOM 2276 N N . ASP A 1 295 ? 2.527 -29.574 -34.854 1.00 34.55 ? 297 ASP A N 1 ATOM 2277 C CA . ASP A 1 295 ? 1.831 -28.826 -35.906 1.00 33.23 ? 297 ASP A CA 1 ATOM 2278 C C . ASP A 1 295 ? 0.667 -28.142 -35.174 1.00 32.26 ? 297 ASP A C 1 ATOM 2279 O O . ASP A 1 295 ? 0.808 -26.975 -34.710 1.00 31.43 ? 297 ASP A O 1 ATOM 2280 C CB . ASP A 1 295 ? 1.434 -29.785 -37.063 1.00 33.18 ? 297 ASP A CB 1 ATOM 2281 C CG . ASP A 1 295 ? 0.832 -29.047 -38.287 1.00 35.77 ? 297 ASP A CG 1 ATOM 2282 O OD1 . ASP A 1 295 ? 0.690 -27.811 -38.241 1.00 38.13 ? 297 ASP A OD1 1 ATOM 2283 O OD2 . ASP A 1 295 ? 0.421 -29.696 -39.287 1.00 37.32 ? 297 ASP A OD2 1 ATOM 2284 N N . PHE A 1 296 ? -0.432 -28.872 -34.948 1.00 31.87 ? 298 PHE A N 1 ATOM 2285 C CA . PHE A 1 296 ? -1.513 -28.309 -34.154 1.00 30.20 ? 298 PHE A CA 1 ATOM 2286 C C . PHE A 1 296 ? -1.028 -27.984 -32.720 1.00 30.50 ? 298 PHE A C 1 ATOM 2287 O O . PHE A 1 296 ? -1.333 -26.925 -32.187 1.00 30.11 ? 298 PHE A O 1 ATOM 2288 C CB . PHE A 1 296 ? -2.720 -29.230 -34.112 1.00 29.87 ? 298 PHE A CB 1 ATOM 2289 C CG . PHE A 1 296 ? -3.935 -28.606 -33.464 1.00 26.68 ? 298 PHE A CG 1 ATOM 2290 C CD1 . PHE A 1 296 ? -4.129 -28.692 -32.086 1.00 24.74 ? 298 PHE A CD1 1 ATOM 2291 C CD2 . PHE A 1 296 ? -4.876 -27.954 -34.231 1.00 23.65 ? 298 PHE A CD2 1 ATOM 2292 C CE1 . PHE A 1 296 ? -5.259 -28.112 -31.483 1.00 22.84 ? 298 PHE A CE1 1 ATOM 2293 C CE2 . PHE A 1 296 ? -6.017 -27.391 -33.661 1.00 22.45 ? 298 PHE A CE2 1 ATOM 2294 C CZ . PHE A 1 296 ? -6.199 -27.460 -32.297 1.00 25.48 ? 298 PHE A CZ 1 ATOM 2295 N N . LEU A 1 297 ? -0.301 -28.907 -32.120 1.00 30.18 ? 299 LEU A N 1 ATOM 2296 C CA . LEU A 1 297 ? 0.206 -28.785 -30.795 1.00 31.06 ? 299 LEU A CA 1 ATOM 2297 C C . LEU A 1 297 ? 1.729 -28.804 -30.883 1.00 33.14 ? 299 LEU A C 1 ATOM 2298 O O . LEU A 1 297 ? 2.308 -29.857 -31.270 1.00 33.82 ? 299 LEU A O 1 ATOM 2299 C CB . LEU A 1 297 ? -0.206 -30.016 -30.022 1.00 30.02 ? 299 LEU A CB 1 ATOM 2300 C CG . LEU A 1 297 ? -1.182 -29.931 -28.896 1.00 34.11 ? 299 LEU A CG 1 ATOM 2301 C CD1 . LEU A 1 297 ? -1.342 -31.251 -28.074 1.00 34.06 ? 299 LEU A CD1 1 ATOM 2302 C CD2 . LEU A 1 297 ? -0.734 -28.772 -27.966 1.00 42.06 ? 299 LEU A CD2 1 ATOM 2303 N N . THR A 1 298 ? 2.388 -27.692 -30.516 1.00 33.45 ? 300 THR A N 1 ATOM 2304 C CA . THR A 1 298 ? 3.826 -27.566 -30.654 1.00 36.76 ? 300 THR A CA 1 ATOM 2305 C C . THR A 1 298 ? 4.663 -28.179 -29.518 1.00 36.31 ? 300 THR A C 1 ATOM 2306 O O . THR A 1 298 ? 5.869 -28.347 -29.699 1.00 36.97 ? 300 THR A O 1 ATOM 2307 C CB . THR A 1 298 ? 4.252 -26.084 -30.828 1.00 37.73 ? 300 THR A CB 1 ATOM 2308 O OG1 . THR A 1 298 ? 4.060 -25.374 -29.598 1.00 41.67 ? 300 THR A OG1 1 ATOM 2309 C CG2 . THR A 1 298 ? 3.342 -25.410 -31.823 1.00 40.37 ? 300 THR A CG2 1 ATOM 2310 N N . ASP A 1 299 ? 4.047 -28.521 -28.376 1.00 33.23 ? 301 ASP A N 1 ATOM 2311 C CA . ASP A 1 299 ? 4.820 -28.994 -27.212 1.00 33.06 ? 301 ASP A CA 1 ATOM 2312 C C . ASP A 1 299 ? 3.830 -29.694 -26.290 1.00 32.04 ? 301 ASP A C 1 ATOM 2313 O O . ASP A 1 299 ? 2.661 -29.632 -26.509 1.00 28.91 ? 301 ASP A O 1 ATOM 2314 C CB . ASP A 1 299 ? 5.475 -27.776 -26.497 1.00 32.08 ? 301 ASP A CB 1 ATOM 2315 C CG . ASP A 1 299 ? 6.647 -28.141 -25.555 1.00 34.38 ? 301 ASP A CG 1 ATOM 2316 O OD1 . ASP A 1 299 ? 7.398 -27.178 -25.139 1.00 34.83 ? 301 ASP A OD1 1 ATOM 2317 O OD2 . ASP A 1 299 ? 6.820 -29.341 -25.210 1.00 33.17 ? 301 ASP A OD2 1 ATOM 2318 N N . MET A 1 300 ? 4.295 -30.350 -25.248 1.00 33.01 ? 302 MET A N 1 ATOM 2319 C CA . MET A 1 300 ? 3.361 -30.956 -24.329 1.00 33.77 ? 302 MET A CA 1 ATOM 2320 C C . MET A 1 300 ? 2.439 -29.931 -23.708 1.00 32.62 ? 302 MET A C 1 ATOM 2321 O O . MET A 1 300 ? 2.875 -28.903 -23.222 1.00 34.82 ? 302 MET A O 1 ATOM 2322 C CB . MET A 1 300 ? 4.135 -31.765 -23.300 1.00 35.41 ? 302 MET A CB 1 ATOM 2323 C CG . MET A 1 300 ? 4.968 -32.867 -23.987 1.00 39.84 ? 302 MET A CG 1 ATOM 2324 S SD . MET A 1 300 ? 6.063 -33.728 -22.801 1.00 54.82 ? 302 MET A SD 1 ATOM 2325 C CE . MET A 1 300 ? 4.664 -34.359 -21.774 1.00 53.45 ? 302 MET A CE 1 ATOM 2326 N N . PRO A 1 301 ? 1.130 -30.163 -23.755 1.00 32.19 ? 303 PRO A N 1 ATOM 2327 C CA . PRO A 1 301 ? 0.319 -28.986 -23.416 1.00 30.25 ? 303 PRO A CA 1 ATOM 2328 C C . PRO A 1 301 ? 0.434 -28.557 -21.937 1.00 29.36 ? 303 PRO A C 1 ATOM 2329 O O . PRO A 1 301 ? 0.130 -27.429 -21.612 1.00 28.23 ? 303 PRO A O 1 ATOM 2330 C CB . PRO A 1 301 ? -1.144 -29.444 -23.757 1.00 30.37 ? 303 PRO A CB 1 ATOM 2331 C CG . PRO A 1 301 ? -1.070 -30.937 -23.796 1.00 31.50 ? 303 PRO A CG 1 ATOM 2332 C CD . PRO A 1 301 ? 0.336 -31.245 -24.360 1.00 30.65 ? 303 PRO A CD 1 ATOM 2333 N N . ASP A 1 302 ? 0.803 -29.453 -21.038 1.00 28.18 ? 304 ASP A N 1 ATOM 2334 C CA . ASP A 1 302 ? 0.988 -29.058 -19.649 1.00 28.39 ? 304 ASP A CA 1 ATOM 2335 C C . ASP A 1 302 ? 2.071 -27.946 -19.514 1.00 29.15 ? 304 ASP A C 1 ATOM 2336 O O . ASP A 1 302 ? 1.996 -27.036 -18.641 1.00 29.50 ? 304 ASP A O 1 ATOM 2337 C CB . ASP A 1 302 ? 1.367 -30.296 -18.778 1.00 29.28 ? 304 ASP A CB 1 ATOM 2338 C CG . ASP A 1 302 ? 2.423 -31.183 -19.424 0.50 30.54 ? 304 ASP A CG 1 ATOM 2339 O OD1 . ASP A 1 302 ? 2.178 -31.740 -20.528 0.50 32.62 ? 304 ASP A OD1 1 ATOM 2340 O OD2 . ASP A 1 302 ? 3.467 -31.383 -18.795 0.50 29.21 ? 304 ASP A OD2 1 ATOM 2341 N N . ILE A 1 303 ? 3.069 -28.038 -20.386 1.00 28.96 ? 305 ILE A N 1 ATOM 2342 C CA . ILE A 1 303 ? 4.201 -27.100 -20.407 1.00 29.94 ? 305 ILE A CA 1 ATOM 2343 C C . ILE A 1 303 ? 3.702 -25.725 -20.921 1.00 29.71 ? 305 ILE A C 1 ATOM 2344 O O . ILE A 1 303 ? 4.018 -24.728 -20.330 1.00 30.05 ? 305 ILE A O 1 ATOM 2345 C CB . ILE A 1 303 ? 5.399 -27.680 -21.216 1.00 29.87 ? 305 ILE A CB 1 ATOM 2346 C CG1 . ILE A 1 303 ? 5.779 -29.060 -20.645 1.00 30.67 ? 305 ILE A CG1 1 ATOM 2347 C CG2 . ILE A 1 303 ? 6.566 -26.733 -21.185 1.00 30.06 ? 305 ILE A CG2 1 ATOM 2348 C CD1 . ILE A 1 303 ? 7.016 -29.790 -21.373 1.00 32.35 ? 305 ILE A CD1 1 ATOM 2349 N N . LEU A 1 304 ? 2.860 -25.715 -21.968 1.00 27.96 ? 306 LEU A N 1 ATOM 2350 C CA . LEU A 1 304 ? 2.336 -24.473 -22.537 1.00 28.61 ? 306 LEU A CA 1 ATOM 2351 C C . LEU A 1 304 ? 1.477 -23.737 -21.499 1.00 29.10 ? 306 LEU A C 1 ATOM 2352 O O . LEU A 1 304 ? 1.645 -22.521 -21.271 1.00 29.55 ? 306 LEU A O 1 ATOM 2353 C CB . LEU A 1 304 ? 1.546 -24.786 -23.846 1.00 27.20 ? 306 LEU A CB 1 ATOM 2354 C CG . LEU A 1 304 ? 2.391 -25.537 -24.916 1.00 25.80 ? 306 LEU A CG 1 ATOM 2355 C CD1 . LEU A 1 304 ? 1.577 -25.979 -26.103 1.00 23.10 ? 306 LEU A CD1 1 ATOM 2356 C CD2 . LEU A 1 304 ? 3.499 -24.673 -25.444 1.00 27.08 ? 306 LEU A CD2 1 ATOM 2357 N N . LEU A 1 305 ? 0.550 -24.483 -20.863 1.00 28.69 ? 307 LEU A N 1 ATOM 2358 C CA . LEU A 1 305 ? -0.299 -23.960 -19.802 1.00 27.72 ? 307 LEU A CA 1 ATOM 2359 C C . LEU A 1 305 ? 0.566 -23.354 -18.671 1.00 28.37 ? 307 LEU A C 1 ATOM 2360 O O . LEU A 1 305 ? 0.427 -22.174 -18.313 1.00 29.15 ? 307 LEU A O 1 ATOM 2361 C CB . LEU A 1 305 ? -1.175 -25.072 -19.210 1.00 26.71 ? 307 LEU A CB 1 ATOM 2362 C CG . LEU A 1 305 ? -2.226 -24.641 -18.167 1.00 25.64 ? 307 LEU A CG 1 ATOM 2363 C CD1 . LEU A 1 305 ? -3.120 -23.421 -18.650 1.00 27.07 ? 307 LEU A CD1 1 ATOM 2364 C CD2 . LEU A 1 305 ? -3.162 -25.870 -17.787 1.00 22.63 ? 307 LEU A CD2 1 ATOM 2365 N N . GLU A 1 306 ? 1.492 -24.158 -18.157 1.00 28.38 ? 308 GLU A N 1 ATOM 2366 C CA . GLU A 1 306 ? 2.251 -23.746 -17.002 1.00 29.64 ? 308 GLU A CA 1 ATOM 2367 C C . GLU A 1 306 ? 3.041 -22.467 -17.336 1.00 30.10 ? 308 GLU A C 1 ATOM 2368 O O . GLU A 1 306 ? 3.194 -21.577 -16.481 1.00 31.59 ? 308 GLU A O 1 ATOM 2369 C CB . GLU A 1 306 ? 3.136 -24.928 -16.528 1.00 29.34 ? 308 GLU A CB 1 ATOM 2370 C CG . GLU A 1 306 ? 4.150 -24.540 -15.496 1.00 32.49 ? 308 GLU A CG 1 ATOM 2371 C CD . GLU A 1 306 ? 3.542 -24.221 -14.131 1.00 39.20 ? 308 GLU A CD 1 ATOM 2372 O OE1 . GLU A 1 306 ? 4.166 -23.509 -13.317 1.00 44.75 ? 308 GLU A OE1 1 ATOM 2373 O OE2 . GLU A 1 306 ? 2.437 -24.676 -13.842 1.00 40.57 ? 308 GLU A OE2 1 ATOM 2374 N N . LEU A 1 307 ? 3.505 -22.344 -18.596 1.00 29.91 ? 309 LEU A N 1 ATOM 2375 C CA . LEU A 1 307 ? 4.476 -21.275 -18.948 1.00 30.23 ? 309 LEU A CA 1 ATOM 2376 C C . LEU A 1 307 ? 3.800 -20.185 -19.717 1.00 30.87 ? 309 LEU A C 1 ATOM 2377 O O . LEU A 1 307 ? 4.444 -19.310 -20.257 1.00 31.37 ? 309 LEU A O 1 ATOM 2378 C CB . LEU A 1 307 ? 5.661 -21.868 -19.702 1.00 29.46 ? 309 LEU A CB 1 ATOM 2379 C CG . LEU A 1 307 ? 6.492 -22.834 -18.817 1.00 27.70 ? 309 LEU A CG 1 ATOM 2380 C CD1 . LEU A 1 307 ? 7.668 -23.291 -19.628 1.00 26.83 ? 309 LEU A CD1 1 ATOM 2381 C CD2 . LEU A 1 307 ? 7.007 -22.152 -17.491 1.00 25.29 ? 309 LEU A CD2 1 ATOM 2382 N N . GLY A 1 308 ? 2.476 -20.250 -19.752 1.00 31.05 ? 310 GLY A N 1 ATOM 2383 C CA . GLY A 1 308 ? 1.662 -19.099 -20.184 1.00 32.61 ? 310 GLY A CA 1 ATOM 2384 C C . GLY A 1 308 ? 1.611 -18.950 -21.686 1.00 32.71 ? 310 GLY A C 1 ATOM 2385 O O . GLY A 1 308 ? 1.429 -17.848 -22.158 1.00 31.62 ? 310 GLY A O 1 ATOM 2386 N N . GLN A 1 309 ? 1.814 -20.051 -22.427 1.00 31.38 ? 311 GLN A N 1 ATOM 2387 C CA . GLN A 1 309 ? 1.812 -19.974 -23.865 1.00 31.49 ? 311 GLN A CA 1 ATOM 2388 C C . GLN A 1 309 ? 0.450 -20.329 -24.424 1.00 30.91 ? 311 GLN A C 1 ATOM 2389 O O . GLN A 1 309 ? 0.269 -21.471 -24.917 1.00 31.48 ? 311 GLN A O 1 ATOM 2390 C CB . GLN A 1 309 ? 2.841 -20.925 -24.467 1.00 32.37 ? 311 GLN A CB 1 ATOM 2391 C CG . GLN A 1 309 ? 4.205 -20.699 -23.941 1.00 37.32 ? 311 GLN A CG 1 ATOM 2392 C CD . GLN A 1 309 ? 4.688 -19.255 -24.221 1.00 41.56 ? 311 GLN A CD 1 ATOM 2393 O OE1 . GLN A 1 309 ? 5.020 -18.499 -23.285 1.00 41.20 ? 311 GLN A OE1 1 ATOM 2394 N NE2 . GLN A 1 309 ? 4.685 -18.870 -25.503 1.00 38.88 ? 311 GLN A NE2 1 ATOM 2395 N N . PHE A 1 310 ? -0.506 -19.385 -24.380 1.00 28.21 ? 312 PHE A N 1 ATOM 2396 C CA . PHE A 1 310 ? -1.836 -19.652 -24.904 1.00 27.33 ? 312 PHE A CA 1 ATOM 2397 C C . PHE A 1 310 ? -2.541 -18.316 -25.236 1.00 28.64 ? 312 PHE A C 1 ATOM 2398 O O . PHE A 1 310 ? -2.036 -17.240 -24.848 1.00 29.19 ? 312 PHE A O 1 ATOM 2399 C CB . PHE A 1 310 ? -2.700 -20.468 -23.902 1.00 24.13 ? 312 PHE A CB 1 ATOM 2400 C CG . PHE A 1 310 ? -2.614 -19.993 -22.506 1.00 25.35 ? 312 PHE A CG 1 ATOM 2401 C CD1 . PHE A 1 310 ? -3.330 -18.888 -22.087 1.00 24.82 ? 312 PHE A CD1 1 ATOM 2402 C CD2 . PHE A 1 310 ? -1.757 -20.613 -21.589 1.00 27.74 ? 312 PHE A CD2 1 ATOM 2403 C CE1 . PHE A 1 310 ? -3.276 -18.421 -20.730 1.00 25.38 ? 312 PHE A CE1 1 ATOM 2404 C CE2 . PHE A 1 310 ? -1.676 -20.168 -20.243 1.00 25.51 ? 312 PHE A CE2 1 ATOM 2405 C CZ . PHE A 1 310 ? -2.451 -19.053 -19.811 1.00 23.97 ? 312 PHE A CZ 1 ATOM 2406 N N . LYS A 1 311 ? -3.701 -18.387 -25.919 1.00 27.15 ? 313 LYS A N 1 ATOM 2407 C CA . LYS A 1 311 ? -4.392 -17.155 -26.316 1.00 27.26 ? 313 LYS A CA 1 ATOM 2408 C C . LYS A 1 311 ? -4.850 -16.375 -25.056 1.00 26.86 ? 313 LYS A C 1 ATOM 2409 O O . LYS A 1 311 ? -5.487 -16.992 -24.173 1.00 28.77 ? 313 LYS A O 1 ATOM 2410 C CB . LYS A 1 311 ? -5.601 -17.518 -27.177 1.00 26.58 ? 313 LYS A CB 1 ATOM 2411 C CG . LYS A 1 311 ? -6.395 -16.299 -27.673 1.00 26.49 ? 313 LYS A CG 1 ATOM 2412 C CD . LYS A 1 311 ? -7.665 -16.876 -28.374 1.00 26.17 ? 313 LYS A CD 1 ATOM 2413 C CE . LYS A 1 311 ? -8.576 -15.767 -28.854 1.00 27.05 ? 313 LYS A CE 1 ATOM 2414 N NZ . LYS A 1 311 ? -7.892 -14.775 -29.842 1.00 27.33 ? 313 LYS A NZ 1 ATOM 2415 N N . LYS A 1 312 ? -4.514 -15.097 -24.930 1.00 24.96 ? 314 LYS A N 1 ATOM 2416 C CA . LYS A 1 312 ? -4.926 -14.321 -23.754 1.00 27.30 ? 314 LYS A CA 1 ATOM 2417 C C . LYS A 1 312 ? -6.337 -13.778 -23.999 1.00 28.00 ? 314 LYS A C 1 ATOM 2418 O O . LYS A 1 312 ? -6.513 -12.923 -24.885 1.00 29.62 ? 314 LYS A O 1 ATOM 2419 C CB . LYS A 1 312 ? -3.962 -13.142 -23.461 1.00 28.48 ? 314 LYS A CB 1 ATOM 2420 C CG . LYS A 1 312 ? -2.456 -13.576 -23.147 1.00 31.45 ? 314 LYS A CG 1 ATOM 2421 C CD . LYS A 1 312 ? -2.355 -14.798 -22.170 1.00 37.83 ? 314 LYS A CD 1 ATOM 2422 C CE . LYS A 1 312 ? -0.916 -15.154 -21.815 1.00 43.07 ? 314 LYS A CE 1 ATOM 2423 N NZ . LYS A 1 312 ? -0.343 -15.871 -22.949 1.00 47.36 ? 314 LYS A NZ 1 ATOM 2424 N N . THR A 1 313 ? -7.330 -14.299 -23.273 1.00 26.81 ? 315 THR A N 1 ATOM 2425 C CA . THR A 1 313 ? -8.726 -13.954 -23.477 1.00 26.26 ? 315 THR A CA 1 ATOM 2426 C C . THR A 1 313 ? -9.523 -14.434 -22.273 1.00 26.78 ? 315 THR A C 1 ATOM 2427 O O . THR A 1 313 ? -8.958 -15.007 -21.363 1.00 27.56 ? 315 THR A O 1 ATOM 2428 C CB . THR A 1 313 ? -9.254 -14.589 -24.765 1.00 27.65 ? 315 THR A CB 1 ATOM 2429 O OG1 . THR A 1 313 ? -10.546 -14.043 -25.032 1.00 28.03 ? 315 THR A OG1 1 ATOM 2430 C CG2 . THR A 1 313 ? -9.308 -16.144 -24.698 1.00 19.93 ? 315 THR A CG2 1 ATOM 2431 N N . GLN A 1 314 ? -10.824 -14.230 -22.235 1.00 26.93 ? 316 GLN A N 1 ATOM 2432 C CA . GLN A 1 314 ? -11.616 -14.618 -21.035 1.00 26.46 ? 316 GLN A CA 1 ATOM 2433 C C . GLN A 1 314 ? -12.071 -16.049 -21.226 1.00 25.89 ? 316 GLN A C 1 ATOM 2434 O O . GLN A 1 314 ? -12.275 -16.476 -22.347 1.00 24.53 ? 316 GLN A O 1 ATOM 2435 C CB . GLN A 1 314 ? -12.876 -13.725 -20.849 1.00 25.88 ? 316 GLN A CB 1 ATOM 2436 C CG . GLN A 1 314 ? -12.640 -12.210 -20.759 1.00 29.51 ? 316 GLN A CG 1 ATOM 2437 C CD . GLN A 1 314 ? -12.232 -11.556 -22.111 1.00 32.36 ? 316 GLN A CD 1 ATOM 2438 O OE1 . GLN A 1 314 ? -12.708 -11.922 -23.194 1.00 27.78 ? 316 GLN A OE1 1 ATOM 2439 N NE2 . GLN A 1 314 ? -11.304 -10.623 -22.027 1.00 32.45 ? 316 GLN A NE2 1 ATOM 2440 N N . ILE A 1 315 ? -12.265 -16.791 -20.137 1.00 25.30 ? 317 ILE A N 1 ATOM 2441 C CA . ILE A 1 315 ? -12.799 -18.129 -20.268 1.00 23.86 ? 317 ILE A CA 1 ATOM 2442 C C . ILE A 1 315 ? -13.932 -18.326 -19.289 1.00 24.70 ? 317 ILE A C 1 ATOM 2443 O O . ILE A 1 315 ? -13.976 -17.684 -18.233 1.00 24.56 ? 317 ILE A O 1 ATOM 2444 C CB . ILE A 1 315 ? -11.762 -19.237 -20.028 1.00 24.43 ? 317 ILE A CB 1 ATOM 2445 C CG1 . ILE A 1 315 ? -11.029 -19.080 -18.680 1.00 25.51 ? 317 ILE A CG1 1 ATOM 2446 C CG2 . ILE A 1 315 ? -10.765 -19.345 -21.201 1.00 22.98 ? 317 ILE A CG2 1 ATOM 2447 C CD1 . ILE A 1 315 ? -10.220 -20.392 -18.320 1.00 28.68 ? 317 ILE A CD1 1 ATOM 2448 N N . LEU A 1 316 ? -14.846 -19.228 -19.643 1.00 23.36 ? 318 LEU A N 1 ATOM 2449 C CA . LEU A 1 316 ? -15.893 -19.647 -18.747 1.00 22.75 ? 318 LEU A CA 1 ATOM 2450 C C . LEU A 1 316 ? -15.749 -21.188 -18.632 1.00 21.84 ? 318 LEU A C 1 ATOM 2451 O O . LEU A 1 316 ? -15.747 -21.904 -19.651 1.00 21.57 ? 318 LEU A O 1 ATOM 2452 C CB . LEU A 1 316 ? -17.243 -19.224 -19.318 1.00 22.84 ? 318 LEU A CB 1 ATOM 2453 C CG . LEU A 1 316 ? -18.491 -19.379 -18.453 1.00 26.88 ? 318 LEU A CG 1 ATOM 2454 C CD1 . LEU A 1 316 ? -19.698 -18.751 -19.197 1.00 30.45 ? 318 LEU A CD1 1 ATOM 2455 C CD2 . LEU A 1 316 ? -18.803 -20.836 -18.317 1.00 27.43 ? 318 LEU A CD2 1 ATOM 2456 N N . VAL A 1 317 ? -15.638 -21.689 -17.421 1.00 20.12 ? 319 VAL A N 1 ATOM 2457 C CA . VAL A 1 317 ? -15.298 -23.137 -17.223 1.00 20.52 ? 319 VAL A CA 1 ATOM 2458 C C . VAL A 1 317 ? -16.285 -23.655 -16.172 1.00 20.68 ? 319 VAL A C 1 ATOM 2459 O O . VAL A 1 317 ? -16.668 -22.879 -15.233 1.00 21.08 ? 319 VAL A O 1 ATOM 2460 C CB . VAL A 1 317 ? -13.869 -23.281 -16.709 1.00 20.28 ? 319 VAL A CB 1 ATOM 2461 C CG1 . VAL A 1 317 ? -13.474 -24.720 -16.631 1.00 19.09 ? 319 VAL A CG1 1 ATOM 2462 C CG2 . VAL A 1 317 ? -12.879 -22.491 -17.626 1.00 19.59 ? 319 VAL A CG2 1 ATOM 2463 N N . GLY A 1 318 ? -16.728 -24.915 -16.299 1.00 21.26 ? 320 GLY A N 1 ATOM 2464 C CA . GLY A 1 318 ? -17.583 -25.474 -15.224 1.00 20.85 ? 320 GLY A CA 1 ATOM 2465 C C . GLY A 1 318 ? -17.678 -26.974 -15.246 1.00 21.65 ? 320 GLY A C 1 ATOM 2466 O O . GLY A 1 318 ? -17.155 -27.619 -16.196 1.00 22.62 ? 320 GLY A O 1 ATOM 2467 N N . VAL A 1 319 ? -18.362 -27.543 -14.236 1.00 20.08 ? 321 VAL A N 1 ATOM 2468 C CA . VAL A 1 319 ? -18.484 -28.981 -14.114 1.00 20.02 ? 321 VAL A CA 1 ATOM 2469 C C . VAL A 1 319 ? -19.795 -29.237 -13.418 1.00 21.51 ? 321 VAL A C 1 ATOM 2470 O O . VAL A 1 319 ? -20.374 -28.308 -12.841 1.00 21.81 ? 321 VAL A O 1 ATOM 2471 C CB . VAL A 1 319 ? -17.329 -29.604 -13.217 1.00 19.54 ? 321 VAL A CB 1 ATOM 2472 C CG1 . VAL A 1 319 ? -15.978 -29.444 -13.950 1.00 17.95 ? 321 VAL A CG1 1 ATOM 2473 C CG2 . VAL A 1 319 ? -17.321 -28.842 -11.879 1.00 14.58 ? 321 VAL A CG2 1 ATOM 2474 N N . ASN A 1 320 ? -20.231 -30.497 -13.454 1.00 21.33 ? 322 ASN A N 1 ATOM 2475 C CA . ASN A 1 320 ? -21.493 -30.909 -12.900 1.00 22.61 ? 322 ASN A CA 1 ATOM 2476 C C . ASN A 1 320 ? -21.205 -31.623 -11.625 1.00 25.01 ? 322 ASN A C 1 ATOM 2477 O O . ASN A 1 320 ? -20.114 -32.217 -11.431 1.00 24.61 ? 322 ASN A O 1 ATOM 2478 C CB . ASN A 1 320 ? -22.191 -31.856 -13.860 1.00 22.49 ? 322 ASN A CB 1 ATOM 2479 C CG . ASN A 1 320 ? -22.568 -31.154 -15.168 1.00 24.21 ? 322 ASN A CG 1 ATOM 2480 O OD1 . ASN A 1 320 ? -22.344 -29.925 -15.313 1.00 23.03 ? 322 ASN A OD1 1 ATOM 2481 N ND2 . ASN A 1 320 ? -23.106 -31.906 -16.122 1.00 20.99 ? 322 ASN A ND2 1 ATOM 2482 N N . LYS A 1 321 ? -22.195 -31.599 -10.748 1.00 25.67 ? 323 LYS A N 1 ATOM 2483 C CA . LYS A 1 321 ? -21.999 -32.132 -9.415 1.00 25.05 ? 323 LYS A CA 1 ATOM 2484 C C . LYS A 1 321 ? -21.644 -33.615 -9.398 1.00 24.84 ? 323 LYS A C 1 ATOM 2485 O O . LYS A 1 321 ? -20.853 -34.044 -8.530 1.00 23.03 ? 323 LYS A O 1 ATOM 2486 C CB . LYS A 1 321 ? -23.268 -31.877 -8.603 1.00 26.63 ? 323 LYS A CB 1 ATOM 2487 C CG . LYS A 1 321 ? -23.338 -32.602 -7.275 1.00 28.61 ? 323 LYS A CG 1 ATOM 2488 C CD . LYS A 1 321 ? -24.678 -32.317 -6.552 1.00 34.12 ? 323 LYS A CD 1 ATOM 2489 C CE . LYS A 1 321 ? -24.658 -33.104 -5.216 1.00 41.71 ? 323 LYS A CE 1 ATOM 2490 N NZ . LYS A 1 321 ? -25.794 -32.805 -4.294 1.00 51.30 ? 323 LYS A NZ 1 ATOM 2491 N N . ASP A 1 322 ? -22.221 -34.411 -10.305 1.00 23.32 ? 324 ASP A N 1 ATOM 2492 C CA . ASP A 1 322 ? -21.845 -35.848 -10.291 1.00 25.80 ? 324 ASP A CA 1 ATOM 2493 C C . ASP A 1 322 ? -21.231 -36.328 -11.626 1.00 24.74 ? 324 ASP A C 1 ATOM 2494 O O . ASP A 1 322 ? -21.724 -37.284 -12.240 1.00 28.36 ? 324 ASP A O 1 ATOM 2495 C CB . ASP A 1 322 ? -23.054 -36.778 -9.889 1.00 25.51 ? 324 ASP A CB 1 ATOM 2496 C CG . ASP A 1 322 ? -23.696 -36.378 -8.550 1.00 27.91 ? 324 ASP A CG 1 ATOM 2497 O OD1 . ASP A 1 322 ? -23.185 -36.757 -7.495 1.00 26.25 ? 324 ASP A OD1 1 ATOM 2498 O OD2 . ASP A 1 322 ? -24.771 -35.730 -8.535 1.00 26.85 ? 324 ASP A OD2 1 ATOM 2499 N N . GLU A 1 323 ? -20.173 -35.704 -12.061 1.00 23.36 ? 325 GLU A N 1 ATOM 2500 C CA . GLU A 1 323 ? -19.513 -36.072 -13.288 1.00 24.59 ? 325 GLU A CA 1 ATOM 2501 C C . GLU A 1 323 ? -19.264 -37.596 -13.446 1.00 25.93 ? 325 GLU A C 1 ATOM 2502 O O . GLU A 1 323 ? -19.451 -38.107 -14.532 1.00 28.34 ? 325 GLU A O 1 ATOM 2503 C CB . GLU A 1 323 ? -18.136 -35.379 -13.323 1.00 23.79 ? 325 GLU A CB 1 ATOM 2504 C CG . GLU A 1 323 ? -18.206 -33.792 -13.509 1.00 25.20 ? 325 GLU A CG 1 ATOM 2505 C CD . GLU A 1 323 ? -18.712 -33.369 -14.894 1.00 27.06 ? 325 GLU A CD 1 ATOM 2506 O OE1 . GLU A 1 323 ? -18.956 -34.245 -15.775 1.00 27.46 ? 325 GLU A OE1 1 ATOM 2507 O OE2 . GLU A 1 323 ? -18.857 -32.148 -15.129 1.00 28.39 ? 325 GLU A OE2 1 ATOM 2508 N N . GLY A 1 324 ? -18.798 -38.300 -12.387 1.00 25.75 ? 326 GLY A N 1 ATOM 2509 C CA . GLY A 1 324 ? -18.298 -39.666 -12.547 1.00 24.52 ? 326 GLY A CA 1 ATOM 2510 C C . GLY A 1 324 ? -19.360 -40.778 -12.608 1.00 25.22 ? 326 GLY A C 1 ATOM 2511 O O . GLY A 1 324 ? -19.023 -41.899 -12.948 1.00 26.81 ? 326 GLY A O 1 ATOM 2512 N N . THR A 1 325 ? -20.610 -40.505 -12.235 1.00 23.70 ? 327 THR A N 1 ATOM 2513 C CA . THR A 1 325 ? -21.614 -41.570 -12.098 1.00 24.99 ? 327 THR A CA 1 ATOM 2514 C C . THR A 1 325 ? -21.939 -42.306 -13.421 1.00 26.03 ? 327 THR A C 1 ATOM 2515 O O . THR A 1 325 ? -22.083 -43.546 -13.442 1.00 27.35 ? 327 THR A O 1 ATOM 2516 C CB . THR A 1 325 ? -22.904 -41.101 -11.435 1.00 23.92 ? 327 THR A CB 1 ATOM 2517 O OG1 . THR A 1 325 ? -23.425 -40.012 -12.193 1.00 24.54 ? 327 THR A OG1 1 ATOM 2518 C CG2 . THR A 1 325 ? -22.661 -40.638 -9.988 1.00 21.02 ? 327 THR A CG2 1 ATOM 2519 N N . ALA A 1 326 ? -22.055 -41.562 -14.497 1.00 25.59 ? 328 ALA A N 1 ATOM 2520 C CA . ALA A 1 326 ? -22.417 -42.122 -15.805 1.00 27.40 ? 328 ALA A CA 1 ATOM 2521 C C . ALA A 1 326 ? -21.491 -43.327 -16.093 1.00 28.93 ? 328 ALA A C 1 ATOM 2522 O O . ALA A 1 326 ? -21.942 -44.318 -16.668 1.00 27.93 ? 328 ALA A O 1 ATOM 2523 C CB . ALA A 1 326 ? -22.210 -41.088 -16.874 1.00 25.12 ? 328 ALA A CB 1 ATOM 2524 N N . PHE A 1 327 ? -20.210 -43.241 -15.688 1.00 27.84 ? 329 PHE A N 1 ATOM 2525 C CA . PHE A 1 327 ? -19.217 -44.279 -16.134 1.00 28.44 ? 329 PHE A CA 1 ATOM 2526 C C . PHE A 1 327 ? -19.255 -45.543 -15.345 1.00 29.59 ? 329 PHE A C 1 ATOM 2527 O O . PHE A 1 327 ? -18.690 -46.567 -15.756 1.00 31.23 ? 329 PHE A O 1 ATOM 2528 C CB . PHE A 1 327 ? -17.793 -43.683 -16.211 1.00 26.54 ? 329 PHE A CB 1 ATOM 2529 C CG . PHE A 1 327 ? -17.760 -42.406 -17.052 1.00 26.71 ? 329 PHE A CG 1 ATOM 2530 C CD1 . PHE A 1 327 ? -17.935 -41.147 -16.449 1.00 25.24 ? 329 PHE A CD1 1 ATOM 2531 C CD2 . PHE A 1 327 ? -17.602 -42.478 -18.451 1.00 24.91 ? 329 PHE A CD2 1 ATOM 2532 C CE1 . PHE A 1 327 ? -17.942 -40.004 -17.189 1.00 24.92 ? 329 PHE A CE1 1 ATOM 2533 C CE2 . PHE A 1 327 ? -17.595 -41.342 -19.217 1.00 23.66 ? 329 PHE A CE2 1 ATOM 2534 C CZ . PHE A 1 327 ? -17.769 -40.089 -18.586 1.00 24.97 ? 329 PHE A CZ 1 ATOM 2535 N N . LEU A 1 328 ? -19.953 -45.509 -14.225 1.00 30.90 ? 330 LEU A N 1 ATOM 2536 C CA . LEU A 1 328 ? -19.901 -46.644 -13.292 1.00 33.02 ? 330 LEU A CA 1 ATOM 2537 C C . LEU A 1 328 ? -20.730 -47.817 -13.789 1.00 35.29 ? 330 LEU A C 1 ATOM 2538 O O . LEU A 1 328 ? -20.416 -48.985 -13.476 1.00 35.20 ? 330 LEU A O 1 ATOM 2539 C CB . LEU A 1 328 ? -20.368 -46.236 -11.880 1.00 33.35 ? 330 LEU A CB 1 ATOM 2540 C CG . LEU A 1 328 ? -19.667 -45.006 -11.226 1.00 32.10 ? 330 LEU A CG 1 ATOM 2541 C CD1 . LEU A 1 328 ? -20.324 -44.706 -9.886 1.00 28.25 ? 330 LEU A CD1 1 ATOM 2542 C CD2 . LEU A 1 328 ? -18.233 -45.320 -11.031 1.00 28.25 ? 330 LEU A CD2 1 ATOM 2543 N N . VAL A 1 329 ? -21.785 -47.518 -14.558 1.00 35.34 ? 331 VAL A N 1 ATOM 2544 C CA . VAL A 1 329 ? -22.666 -48.563 -15.064 1.00 35.98 ? 331 VAL A CA 1 ATOM 2545 C C . VAL A 1 329 ? -22.176 -49.187 -16.365 1.00 37.79 ? 331 VAL A C 1 ATOM 2546 O O . VAL A 1 329 ? -22.843 -50.083 -16.911 1.00 39.99 ? 331 VAL A O 1 ATOM 2547 C CB . VAL A 1 329 ? -24.125 -48.078 -15.238 1.00 37.01 ? 331 VAL A CB 1 ATOM 2548 C CG1 . VAL A 1 329 ? -24.721 -47.684 -13.875 1.00 36.31 ? 331 VAL A CG1 1 ATOM 2549 C CG2 . VAL A 1 329 ? -24.248 -46.926 -16.340 1.00 31.62 ? 331 VAL A CG2 1 ATOM 2550 N N . TYR A 1 330 ? -20.999 -48.763 -16.831 1.00 37.68 ? 332 TYR A N 1 ATOM 2551 C CA . TYR A 1 330 ? -20.285 -49.421 -17.948 1.00 38.04 ? 332 TYR A CA 1 ATOM 2552 C C . TYR A 1 330 ? -19.137 -50.283 -17.461 1.00 40.29 ? 332 TYR A C 1 ATOM 2553 O O . TYR A 1 330 ? -18.077 -50.382 -18.117 1.00 42.07 ? 332 TYR A O 1 ATOM 2554 C CB . TYR A 1 330 ? -19.737 -48.376 -18.925 1.00 36.38 ? 332 TYR A CB 1 ATOM 2555 C CG . TYR A 1 330 ? -20.849 -47.656 -19.629 1.00 36.43 ? 332 TYR A CG 1 ATOM 2556 C CD1 . TYR A 1 330 ? -21.471 -46.549 -19.035 1.00 32.90 ? 332 TYR A CD1 1 ATOM 2557 C CD2 . TYR A 1 330 ? -21.303 -48.094 -20.875 1.00 35.38 ? 332 TYR A CD2 1 ATOM 2558 C CE1 . TYR A 1 330 ? -22.513 -45.912 -19.644 1.00 31.54 ? 332 TYR A CE1 1 ATOM 2559 C CE2 . TYR A 1 330 ? -22.333 -47.421 -21.544 1.00 31.79 ? 332 TYR A CE2 1 ATOM 2560 C CZ . TYR A 1 330 ? -22.941 -46.357 -20.911 1.00 33.85 ? 332 TYR A CZ 1 ATOM 2561 O OH . TYR A 1 330 ? -23.967 -45.716 -21.533 1.00 28.57 ? 332 TYR A OH 1 ATOM 2562 N N . GLY A 1 331 ? -19.296 -50.921 -16.304 1.00 41.75 ? 333 GLY A N 1 ATOM 2563 C CA . GLY A 1 331 ? -18.379 -51.993 -16.002 1.00 41.64 ? 333 GLY A CA 1 ATOM 2564 C C . GLY A 1 331 ? -17.930 -52.124 -14.582 1.00 42.51 ? 333 GLY A C 1 ATOM 2565 O O . GLY A 1 331 ? -17.310 -53.119 -14.266 1.00 44.64 ? 333 GLY A O 1 ATOM 2566 N N . ALA A 1 332 ? -18.182 -51.126 -13.733 1.00 39.68 ? 334 ALA A N 1 ATOM 2567 C CA . ALA A 1 332 ? -17.837 -51.263 -12.329 1.00 38.67 ? 334 ALA A CA 1 ATOM 2568 C C . ALA A 1 332 ? -18.764 -52.324 -11.711 1.00 40.97 ? 334 ALA A C 1 ATOM 2569 O O . ALA A 1 332 ? -19.982 -52.321 -11.976 1.00 40.26 ? 334 ALA A O 1 ATOM 2570 C CB . ALA A 1 332 ? -17.886 -49.890 -11.599 1.00 35.96 ? 334 ALA A CB 1 ATOM 2571 N N . PRO A 1 333 ? -18.191 -53.293 -10.943 1.00 41.91 ? 335 PRO A N 1 ATOM 2572 C CA . PRO A 1 333 ? -19.032 -54.435 -10.464 1.00 44.37 ? 335 PRO A CA 1 ATOM 2573 C C . PRO A 1 333 ? -20.022 -54.015 -9.365 1.00 43.73 ? 335 PRO A C 1 ATOM 2574 O O . PRO A 1 333 ? -19.677 -53.184 -8.563 1.00 42.78 ? 335 PRO A O 1 ATOM 2575 C CB . PRO A 1 333 ? -18.022 -55.427 -9.920 1.00 45.28 ? 335 PRO A CB 1 ATOM 2576 C CG . PRO A 1 333 ? -16.729 -54.703 -9.805 1.00 44.73 ? 335 PRO A CG 1 ATOM 2577 C CD . PRO A 1 333 ? -16.796 -53.377 -10.501 1.00 41.90 ? 335 PRO A CD 1 ATOM 2578 N N . GLY A 1 334 ? -21.254 -54.509 -9.388 1.00 46.23 ? 336 GLY A N 1 ATOM 2579 C CA . GLY A 1 334 ? -22.297 -54.145 -8.415 1.00 46.79 ? 336 GLY A CA 1 ATOM 2580 C C . GLY A 1 334 ? -23.139 -52.914 -8.787 1.00 45.83 ? 336 GLY A C 1 ATOM 2581 O O . GLY A 1 334 ? -24.146 -52.609 -8.104 1.00 47.20 ? 336 GLY A O 1 ATOM 2582 N N . PHE A 1 335 ? -22.754 -52.227 -9.865 1.00 42.59 ? 337 PHE A N 1 ATOM 2583 C CA . PHE A 1 335 ? -23.496 -51.046 -10.373 1.00 41.37 ? 337 PHE A CA 1 ATOM 2584 C C . PHE A 1 335 ? -24.515 -51.408 -11.395 1.00 42.94 ? 337 PHE A C 1 ATOM 2585 O O . PHE A 1 335 ? -24.339 -52.415 -12.130 1.00 46.34 ? 337 PHE A O 1 ATOM 2586 C CB . PHE A 1 335 ? -22.543 -50.020 -10.959 1.00 37.91 ? 337 PHE A CB 1 ATOM 2587 C CG . PHE A 1 335 ? -21.801 -49.283 -9.896 1.00 37.62 ? 337 PHE A CG 1 ATOM 2588 C CD1 . PHE A 1 335 ? -20.601 -49.770 -9.411 1.00 32.29 ? 337 PHE A CD1 1 ATOM 2589 C CD2 . PHE A 1 335 ? -22.365 -48.139 -9.311 1.00 34.21 ? 337 PHE A CD2 1 ATOM 2590 C CE1 . PHE A 1 335 ? -19.948 -49.108 -8.379 1.00 35.23 ? 337 PHE A CE1 1 ATOM 2591 C CE2 . PHE A 1 335 ? -21.715 -47.486 -8.301 1.00 34.97 ? 337 PHE A CE2 1 ATOM 2592 C CZ . PHE A 1 335 ? -20.486 -47.954 -7.837 1.00 31.21 ? 337 PHE A CZ 1 ATOM 2593 N N . SER A 1 336 ? -25.600 -50.646 -11.415 1.00 41.07 ? 338 SER A N 1 ATOM 2594 C CA . SER A 1 336 ? -26.654 -50.928 -12.390 1.00 42.18 ? 338 SER A CA 1 ATOM 2595 C C . SER A 1 336 ? -27.552 -49.725 -12.541 1.00 40.39 ? 338 SER A C 1 ATOM 2596 O O . SER A 1 336 ? -27.896 -49.123 -11.570 1.00 41.89 ? 338 SER A O 1 ATOM 2597 C CB . SER A 1 336 ? -27.471 -52.174 -11.972 1.00 45.13 ? 338 SER A CB 1 ATOM 2598 O OG . SER A 1 336 ? -28.629 -52.399 -12.805 1.00 45.98 ? 338 SER A OG 1 ATOM 2599 N N . LYS A 1 337 ? -27.965 -49.359 -13.738 1.00 39.77 ? 339 LYS A N 1 ATOM 2600 C CA . LYS A 1 337 ? -28.926 -48.269 -13.821 1.00 38.25 ? 339 LYS A CA 1 ATOM 2601 C C . LYS A 1 337 ? -30.276 -48.701 -13.236 1.00 40.57 ? 339 LYS A C 1 ATOM 2602 O O . LYS A 1 337 ? -31.122 -47.846 -12.977 1.00 40.32 ? 339 LYS A O 1 ATOM 2603 C CB . LYS A 1 337 ? -29.112 -47.780 -15.252 1.00 38.28 ? 339 LYS A CB 1 ATOM 2604 C CG . LYS A 1 337 ? -29.903 -48.717 -16.163 1.00 36.00 ? 339 LYS A CG 1 ATOM 2605 C CD . LYS A 1 337 ? -30.242 -47.972 -17.480 1.00 37.27 ? 339 LYS A CD 1 ATOM 2606 C CE . LYS A 1 337 ? -31.297 -48.728 -18.369 1.00 34.56 ? 339 LYS A CE 1 ATOM 2607 N NZ . LYS A 1 337 ? -32.622 -48.761 -17.607 1.00 39.00 ? 339 LYS A NZ 1 ATOM 2608 N N . ASP A 1 338 ? -30.478 -50.018 -13.029 1.00 41.59 ? 340 ASP A N 1 ATOM 2609 C CA . ASP A 1 338 ? -31.827 -50.522 -12.717 1.00 43.35 ? 340 ASP A CA 1 ATOM 2610 C C . ASP A 1 338 ? -32.046 -50.921 -11.261 1.00 45.12 ? 340 ASP A C 1 ATOM 2611 O O . ASP A 1 338 ? -33.072 -51.566 -10.939 1.00 46.46 ? 340 ASP A O 1 ATOM 2612 C CB . ASP A 1 338 ? -32.215 -51.705 -13.615 1.00 45.05 ? 340 ASP A CB 1 ATOM 2613 C CG . ASP A 1 338 ? -32.291 -51.329 -15.049 1.00 44.26 ? 340 ASP A CG 1 ATOM 2614 O OD1 . ASP A 1 338 ? -31.569 -51.938 -15.850 1.00 46.53 ? 340 ASP A OD1 1 ATOM 2615 O OD2 . ASP A 1 338 ? -33.019 -50.380 -15.366 1.00 43.65 ? 340 ASP A OD2 1 ATOM 2616 N N . ASN A 1 339 ? -31.083 -50.552 -10.415 1.00 42.95 ? 341 ASN A N 1 ATOM 2617 C CA . ASN A 1 339 ? -31.192 -50.656 -8.958 1.00 45.37 ? 341 ASN A CA 1 ATOM 2618 C C . ASN A 1 339 ? -30.298 -49.581 -8.308 1.00 44.22 ? 341 ASN A C 1 ATOM 2619 O O . ASN A 1 339 ? -29.647 -48.760 -9.023 1.00 42.14 ? 341 ASN A O 1 ATOM 2620 C CB . ASN A 1 339 ? -30.896 -52.100 -8.438 1.00 47.31 ? 341 ASN A CB 1 ATOM 2621 C CG . ASN A 1 339 ? -29.456 -52.501 -8.610 1.00 47.21 ? 341 ASN A CG 1 ATOM 2622 O OD1 . ASN A 1 339 ? -28.576 -51.646 -8.547 1.00 44.98 ? 341 ASN A OD1 1 ATOM 2623 N ND2 . ASN A 1 339 ? -29.203 -53.793 -8.833 1.00 53.88 ? 341 ASN A ND2 1 ATOM 2624 N N . ASN A 1 340 ? -30.259 -49.580 -6.978 1.00 45.91 ? 342 ASN A N 1 ATOM 2625 C CA . ASN A 1 340 ? -29.626 -48.493 -6.230 1.00 45.82 ? 342 ASN A CA 1 ATOM 2626 C C . ASN A 1 340 ? -28.126 -48.635 -6.028 1.00 44.41 ? 342 ASN A C 1 ATOM 2627 O O . ASN A 1 340 ? -27.485 -47.740 -5.451 1.00 44.02 ? 342 ASN A O 1 ATOM 2628 C CB . ASN A 1 340 ? -30.374 -48.196 -4.901 1.00 48.98 ? 342 ASN A CB 1 ATOM 2629 C CG . ASN A 1 340 ? -30.330 -49.354 -3.904 1.00 54.53 ? 342 ASN A CG 1 ATOM 2630 O OD1 . ASN A 1 340 ? -29.616 -50.364 -4.085 1.00 57.44 ? 342 ASN A OD1 1 ATOM 2631 N ND2 . ASN A 1 340 ? -31.121 -49.219 -2.827 1.00 63.71 ? 342 ASN A ND2 1 ATOM 2632 N N . SER A 1 341 ? -27.578 -49.764 -6.480 1.00 44.06 ? 343 SER A N 1 ATOM 2633 C CA . SER A 1 341 ? -26.159 -49.943 -6.626 1.00 42.19 ? 343 SER A CA 1 ATOM 2634 C C . SER A 1 341 ? -25.426 -49.776 -5.300 1.00 43.52 ? 343 SER A C 1 ATOM 2635 O O . SER A 1 341 ? -24.310 -49.186 -5.256 1.00 41.38 ? 343 SER A O 1 ATOM 2636 C CB . SER A 1 341 ? -25.608 -48.955 -7.682 1.00 38.78 ? 343 SER A CB 1 ATOM 2637 O OG . SER A 1 341 ? -26.067 -49.278 -8.981 1.00 39.40 ? 343 SER A OG 1 ATOM 2638 N N . ILE A 1 342 ? -26.023 -50.281 -4.216 1.00 45.50 ? 344 ILE A N 1 ATOM 2639 C CA . ILE A 1 342 ? -25.373 -50.205 -2.920 1.00 46.47 ? 344 ILE A CA 1 ATOM 2640 C C . ILE A 1 342 ? -24.218 -51.196 -3.036 1.00 47.45 ? 344 ILE A C 1 ATOM 2641 O O . ILE A 1 342 ? -24.453 -52.396 -3.117 1.00 51.67 ? 344 ILE A O 1 ATOM 2642 C CB . ILE A 1 342 ? -26.389 -50.575 -1.751 1.00 51.34 ? 344 ILE A CB 1 ATOM 2643 C CG1 . ILE A 1 342 ? -27.453 -49.470 -1.576 1.00 48.98 ? 344 ILE A CG1 1 ATOM 2644 C CG2 . ILE A 1 342 ? -25.653 -50.904 -0.386 1.00 48.28 ? 344 ILE A CG2 1 ATOM 2645 C CD1 . ILE A 1 342 ? -26.829 -48.138 -1.198 1.00 44.41 ? 344 ILE A CD1 1 ATOM 2646 N N . ILE A 1 343 ? -22.982 -50.739 -3.089 1.00 45.12 ? 345 ILE A N 1 ATOM 2647 C CA . ILE A 1 343 ? -21.870 -51.689 -3.276 1.00 44.80 ? 345 ILE A CA 1 ATOM 2648 C C . ILE A 1 343 ? -21.044 -51.879 -2.013 1.00 46.76 ? 345 ILE A C 1 ATOM 2649 O O . ILE A 1 343 ? -21.048 -51.005 -1.130 1.00 47.66 ? 345 ILE A O 1 ATOM 2650 C CB . ILE A 1 343 ? -20.944 -51.239 -4.449 1.00 41.69 ? 345 ILE A CB 1 ATOM 2651 C CG1 . ILE A 1 343 ? -20.455 -49.800 -4.242 1.00 39.71 ? 345 ILE A CG1 1 ATOM 2652 C CG2 . ILE A 1 343 ? -21.693 -51.345 -5.756 1.00 39.52 ? 345 ILE A CG2 1 ATOM 2653 C CD1 . ILE A 1 343 ? -18.978 -49.571 -4.579 1.00 33.68 ? 345 ILE A CD1 1 ATOM 2654 N N . THR A 1 344 ? -20.304 -52.993 -1.913 1.00 48.75 ? 346 THR A N 1 ATOM 2655 C CA . THR A 1 344 ? -19.397 -53.205 -0.767 1.00 49.65 ? 346 THR A CA 1 ATOM 2656 C C . THR A 1 344 ? -17.967 -52.609 -0.951 1.00 47.08 ? 346 THR A C 1 ATOM 2657 O O . THR A 1 344 ? -17.570 -52.186 -2.021 1.00 44.61 ? 346 THR A O 1 ATOM 2658 C CB . THR A 1 344 ? -19.273 -54.699 -0.395 1.00 53.81 ? 346 THR A CB 1 ATOM 2659 O OG1 . THR A 1 344 ? -18.698 -55.402 -1.501 1.00 56.35 ? 346 THR A OG1 1 ATOM 2660 C CG2 . THR A 1 344 ? -20.646 -55.326 -0.057 1.00 54.06 ? 346 THR A CG2 1 ATOM 2661 N N . ARG A 1 345 ? -17.209 -52.578 0.133 1.00 47.96 ? 347 ARG A N 1 ATOM 2662 C CA . ARG A 1 345 ? -15.802 -52.286 0.132 1.00 46.01 ? 347 ARG A CA 1 ATOM 2663 C C . ARG A 1 345 ? -15.049 -53.131 -0.915 1.00 46.04 ? 347 ARG A C 1 ATOM 2664 O O . ARG A 1 345 ? -14.255 -52.617 -1.691 1.00 43.71 ? 347 ARG A O 1 ATOM 2665 C CB . ARG A 1 345 ? -15.259 -52.593 1.525 1.00 47.52 ? 347 ARG A CB 1 ATOM 2666 C CG . ARG A 1 345 ? -13.842 -52.177 1.670 1.00 48.81 ? 347 ARG A CG 1 ATOM 2667 C CD . ARG A 1 345 ? -13.421 -52.320 3.109 1.00 54.08 ? 347 ARG A CD 1 ATOM 2668 N NE . ARG A 1 345 ? -11.992 -52.078 3.338 1.00 52.13 ? 347 ARG A NE 1 ATOM 2669 C CZ . ARG A 1 345 ? -11.420 -50.872 3.441 1.00 51.92 ? 347 ARG A CZ 1 ATOM 2670 N NH1 . ARG A 1 345 ? -10.126 -50.794 3.685 1.00 53.18 ? 347 ARG A NH1 1 ATOM 2671 N NH2 . ARG A 1 345 ? -12.116 -49.751 3.299 1.00 48.92 ? 347 ARG A NH2 1 ATOM 2672 N N . LYS A 1 346 ? -15.295 -54.435 -0.928 1.00 49.26 ? 348 LYS A N 1 ATOM 2673 C CA . LYS A 1 346 ? -14.701 -55.305 -1.938 1.00 50.80 ? 348 LYS A CA 1 ATOM 2674 C C . LYS A 1 346 ? -15.033 -54.863 -3.370 1.00 48.17 ? 348 LYS A C 1 ATOM 2675 O O . LYS A 1 346 ? -14.162 -54.886 -4.249 1.00 47.46 ? 348 LYS A O 1 ATOM 2676 C CB . LYS A 1 346 ? -15.120 -56.773 -1.725 1.00 54.88 ? 348 LYS A CB 1 ATOM 2677 C CG . LYS A 1 346 ? -13.982 -57.629 -1.186 1.00 60.89 ? 348 LYS A CG 1 ATOM 2678 C CD . LYS A 1 346 ? -14.369 -59.160 -1.192 1.00 68.92 ? 348 LYS A CD 1 ATOM 2679 C CE . LYS A 1 346 ? -13.304 -60.047 -0.475 1.00 74.18 ? 348 LYS A CE 1 ATOM 2680 N NZ . LYS A 1 346 ? -13.621 -61.506 -0.566 1.00 80.22 ? 348 LYS A NZ 1 ATOM 2681 N N . GLU A 1 347 ? -16.293 -54.499 -3.603 1.00 46.80 ? 349 GLU A N 1 ATOM 2682 C CA . GLU A 1 347 ? -16.718 -54.008 -4.907 1.00 44.66 ? 349 GLU A CA 1 ATOM 2683 C C . GLU A 1 347 ? -16.026 -52.697 -5.257 1.00 41.88 ? 349 GLU A C 1 ATOM 2684 O O . GLU A 1 347 ? -15.532 -52.544 -6.389 1.00 41.48 ? 349 GLU A O 1 ATOM 2685 C CB . GLU A 1 347 ? -18.259 -53.957 -5.014 1.00 44.28 ? 349 GLU A CB 1 ATOM 2686 C CG . GLU A 1 347 ? -18.891 -55.427 -5.242 1.00 50.54 ? 349 GLU A CG 1 ATOM 2687 C CD . GLU A 1 347 ? -20.381 -55.522 -4.952 1.00 53.35 ? 349 GLU A CD 1 ATOM 2688 O OE1 . GLU A 1 347 ? -21.079 -56.354 -5.587 1.00 57.67 ? 349 GLU A OE1 1 ATOM 2689 O OE2 . GLU A 1 347 ? -20.860 -54.790 -4.069 1.00 52.67 ? 349 GLU A OE2 1 ATOM 2690 N N . PHE A 1 348 ? -15.963 -51.764 -4.293 1.00 40.55 ? 350 PHE A N 1 ATOM 2691 C CA . PHE A 1 348 ? -15.223 -50.472 -4.469 1.00 37.33 ? 350 PHE A CA 1 ATOM 2692 C C . PHE A 1 348 ? -13.782 -50.754 -4.918 1.00 37.17 ? 350 PHE A C 1 ATOM 2693 O O . PHE A 1 348 ? -13.317 -50.210 -5.936 1.00 35.04 ? 350 PHE A O 1 ATOM 2694 C CB . PHE A 1 348 ? -15.210 -49.711 -3.167 1.00 37.03 ? 350 PHE A CB 1 ATOM 2695 C CG . PHE A 1 348 ? -14.519 -48.400 -3.242 1.00 35.02 ? 350 PHE A CG 1 ATOM 2696 C CD1 . PHE A 1 348 ? -15.203 -47.270 -3.706 1.00 31.41 ? 350 PHE A CD1 1 ATOM 2697 C CD2 . PHE A 1 348 ? -13.189 -48.269 -2.785 1.00 34.30 ? 350 PHE A CD2 1 ATOM 2698 C CE1 . PHE A 1 348 ? -14.545 -46.001 -3.770 1.00 33.37 ? 350 PHE A CE1 1 ATOM 2699 C CE2 . PHE A 1 348 ? -12.520 -47.007 -2.838 1.00 34.12 ? 350 PHE A CE2 1 ATOM 2700 C CZ . PHE A 1 348 ? -13.166 -45.887 -3.313 1.00 28.66 ? 350 PHE A CZ 1 ATOM 2701 N N . GLN A 1 349 ? -13.106 -51.659 -4.182 1.00 38.70 ? 351 GLN A N 1 ATOM 2702 C CA . GLN A 1 349 ? -11.737 -52.065 -4.482 1.00 39.15 ? 351 GLN A CA 1 ATOM 2703 C C . GLN A 1 349 ? -11.621 -52.624 -5.930 1.00 39.43 ? 351 GLN A C 1 ATOM 2704 O O . GLN A 1 349 ? -10.724 -52.193 -6.712 1.00 36.24 ? 351 GLN A O 1 ATOM 2705 C CB . GLN A 1 349 ? -11.238 -53.088 -3.425 1.00 41.97 ? 351 GLN A CB 1 ATOM 2706 C CG . GLN A 1 349 ? -10.779 -52.388 -2.116 1.00 42.02 ? 351 GLN A CG 1 ATOM 2707 C CD . GLN A 1 349 ? -10.517 -53.378 -0.946 1.00 46.54 ? 351 GLN A CD 1 ATOM 2708 O OE1 . GLN A 1 349 ? -11.218 -54.396 -0.773 1.00 46.50 ? 351 GLN A OE1 1 ATOM 2709 N NE2 . GLN A 1 349 ? -9.536 -53.051 -0.132 1.00 39.97 ? 351 GLN A NE2 1 ATOM 2710 N N . GLU A 1 350 ? -12.529 -53.559 -6.281 1.00 39.98 ? 352 GLU A N 1 ATOM 2711 C CA . GLU A 1 350 ? -12.626 -54.052 -7.664 1.00 41.82 ? 352 GLU A CA 1 ATOM 2712 C C . GLU A 1 350 ? -12.862 -52.920 -8.676 1.00 39.00 ? 352 GLU A C 1 ATOM 2713 O O . GLU A 1 350 ? -12.269 -52.952 -9.764 1.00 39.10 ? 352 GLU A O 1 ATOM 2714 C CB . GLU A 1 350 ? -13.677 -55.194 -7.841 1.00 44.79 ? 352 GLU A CB 1 ATOM 2715 C CG . GLU A 1 350 ? -13.359 -56.439 -7.058 1.00 54.91 ? 352 GLU A CG 1 ATOM 2716 C CD . GLU A 1 350 ? -11.994 -57.072 -7.444 1.00 67.18 ? 352 GLU A CD 1 ATOM 2717 O OE1 . GLU A 1 350 ? -11.026 -57.026 -6.634 1.00 72.18 ? 352 GLU A OE1 1 ATOM 2718 O OE2 . GLU A 1 350 ? -11.879 -57.612 -8.569 1.00 72.80 ? 352 GLU A OE2 1 ATOM 2719 N N . GLY A 1 351 ? -13.694 -51.940 -8.312 1.00 35.96 ? 353 GLY A N 1 ATOM 2720 C CA . GLY A 1 351 ? -14.016 -50.828 -9.192 1.00 35.44 ? 353 GLY A CA 1 ATOM 2721 C C . GLY A 1 351 ? -12.782 -49.968 -9.514 1.00 35.66 ? 353 GLY A C 1 ATOM 2722 O O . GLY A 1 351 ? -12.605 -49.571 -10.676 1.00 36.22 ? 353 GLY A O 1 ATOM 2723 N N . LEU A 1 352 ? -11.916 -49.720 -8.503 1.00 34.82 ? 354 LEU A N 1 ATOM 2724 C CA . LEU A 1 352 ? -10.630 -49.011 -8.702 1.00 34.82 ? 354 LEU A CA 1 ATOM 2725 C C . LEU A 1 352 ? -9.750 -49.777 -9.650 1.00 36.85 ? 354 LEU A C 1 ATOM 2726 O O . LEU A 1 352 ? -9.001 -49.178 -10.442 1.00 36.82 ? 354 LEU A O 1 ATOM 2727 C CB . LEU A 1 352 ? -9.820 -48.810 -7.412 1.00 33.24 ? 354 LEU A CB 1 ATOM 2728 C CG . LEU A 1 352 ? -10.515 -47.914 -6.415 1.00 33.22 ? 354 LEU A CG 1 ATOM 2729 C CD1 . LEU A 1 352 ? -9.699 -47.738 -5.149 1.00 31.91 ? 354 LEU A CD1 1 ATOM 2730 C CD2 . LEU A 1 352 ? -10.882 -46.579 -7.094 1.00 27.49 ? 354 LEU A CD2 1 ATOM 2731 N N . LYS A 1 353 ? -9.832 -51.098 -9.585 1.00 38.43 ? 355 LYS A N 1 ATOM 2732 C CA . LYS A 1 353 ? -8.997 -51.890 -10.463 1.00 41.55 ? 355 LYS A CA 1 ATOM 2733 C C . LYS A 1 353 ? -9.542 -51.704 -11.911 1.00 41.62 ? 355 LYS A C 1 ATOM 2734 O O . LYS A 1 353 ? -8.769 -51.609 -12.866 1.00 43.26 ? 355 LYS A O 1 ATOM 2735 C CB . LYS A 1 353 ? -8.957 -53.303 -9.959 1.00 42.97 ? 355 LYS A CB 1 ATOM 2736 C CG . LYS A 1 353 ? -8.083 -54.251 -10.726 1.00 53.10 ? 355 LYS A CG 1 ATOM 2737 C CD . LYS A 1 353 ? -7.876 -55.575 -9.878 1.00 64.90 ? 355 LYS A CD 1 ATOM 2738 C CE . LYS A 1 353 ? -7.777 -55.214 -8.323 1.00 69.09 ? 355 LYS A CE 1 ATOM 2739 N NZ . LYS A 1 353 ? -8.113 -56.324 -7.334 1.00 73.96 ? 355 LYS A NZ 1 ATOM 2740 N N . ILE A 1 354 ? -10.859 -51.572 -12.050 1.00 40.61 ? 356 ILE A N 1 ATOM 2741 C CA . ILE A 1 354 ? -11.477 -51.322 -13.362 1.00 42.07 ? 356 ILE A CA 1 ATOM 2742 C C . ILE A 1 354 ? -11.100 -49.911 -13.894 1.00 39.68 ? 356 ILE A C 1 ATOM 2743 O O . ILE A 1 354 ? -10.767 -49.778 -15.053 1.00 40.17 ? 356 ILE A O 1 ATOM 2744 C CB . ILE A 1 354 ? -13.003 -51.466 -13.284 1.00 42.25 ? 356 ILE A CB 1 ATOM 2745 C CG1 . ILE A 1 354 ? -13.397 -52.938 -12.987 1.00 45.57 ? 356 ILE A CG1 1 ATOM 2746 C CG2 . ILE A 1 354 ? -13.708 -50.899 -14.525 1.00 44.14 ? 356 ILE A CG2 1 ATOM 2747 C CD1 . ILE A 1 354 ? -13.569 -53.793 -14.142 1.00 49.05 ? 356 ILE A CD1 1 ATOM 2748 N N . PHE A 1 355 ? -11.065 -48.897 -13.025 1.00 36.24 ? 357 PHE A N 1 ATOM 2749 C CA . PHE A 1 355 ? -10.804 -47.533 -13.495 1.00 34.57 ? 357 PHE A CA 1 ATOM 2750 C C . PHE A 1 355 ? -9.343 -47.111 -13.544 1.00 35.08 ? 357 PHE A C 1 ATOM 2751 O O . PHE A 1 355 ? -9.035 -46.113 -14.220 1.00 36.16 ? 357 PHE A O 1 ATOM 2752 C CB . PHE A 1 355 ? -11.654 -46.527 -12.692 1.00 31.52 ? 357 PHE A CB 1 ATOM 2753 C CG . PHE A 1 355 ? -13.095 -46.548 -13.107 1.00 34.01 ? 357 PHE A CG 1 ATOM 2754 C CD1 . PHE A 1 355 ? -13.517 -45.814 -14.220 1.00 31.88 ? 357 PHE A CD1 1 ATOM 2755 C CD2 . PHE A 1 355 ? -14.010 -47.357 -12.442 1.00 34.60 ? 357 PHE A CD2 1 ATOM 2756 C CE1 . PHE A 1 355 ? -14.852 -45.883 -14.684 1.00 34.14 ? 357 PHE A CE1 1 ATOM 2757 C CE2 . PHE A 1 355 ? -15.347 -47.418 -12.863 1.00 39.70 ? 357 PHE A CE2 1 ATOM 2758 C CZ . PHE A 1 355 ? -15.774 -46.660 -14.024 1.00 36.70 ? 357 PHE A CZ 1 ATOM 2759 N N . PHE A 1 356 ? -8.473 -47.832 -12.823 1.00 34.66 ? 358 PHE A N 1 ATOM 2760 C CA . PHE A 1 356 ? -7.045 -47.522 -12.673 1.00 35.81 ? 358 PHE A CA 1 ATOM 2761 C C . PHE A 1 356 ? -6.194 -48.795 -12.926 1.00 39.94 ? 358 PHE A C 1 ATOM 2762 O O . PHE A 1 356 ? -5.355 -49.197 -12.092 1.00 39.87 ? 358 PHE A O 1 ATOM 2763 C CB . PHE A 1 356 ? -6.729 -46.916 -11.309 1.00 31.59 ? 358 PHE A CB 1 ATOM 2764 C CG . PHE A 1 356 ? -7.451 -45.632 -11.053 1.00 32.35 ? 358 PHE A CG 1 ATOM 2765 C CD1 . PHE A 1 356 ? -6.861 -44.388 -11.367 1.00 29.19 ? 358 PHE A CD1 1 ATOM 2766 C CD2 . PHE A 1 356 ? -8.763 -45.641 -10.538 1.00 30.81 ? 358 PHE A CD2 1 ATOM 2767 C CE1 . PHE A 1 356 ? -7.589 -43.179 -11.146 1.00 26.61 ? 358 PHE A CE1 1 ATOM 2768 C CE2 . PHE A 1 356 ? -9.455 -44.463 -10.314 1.00 28.11 ? 358 PHE A CE2 1 ATOM 2769 C CZ . PHE A 1 356 ? -8.865 -43.240 -10.610 1.00 26.94 ? 358 PHE A CZ 1 ATOM 2770 N N . PRO A 1 357 ? -6.378 -49.397 -14.115 1.00 42.71 ? 359 PRO A N 1 ATOM 2771 C CA . PRO A 1 357 ? -5.687 -50.622 -14.518 1.00 46.69 ? 359 PRO A CA 1 ATOM 2772 C C . PRO A 1 357 ? -4.175 -50.551 -14.554 1.00 49.19 ? 359 PRO A C 1 ATOM 2773 O O . PRO A 1 357 ? -3.508 -51.515 -14.140 1.00 52.72 ? 359 PRO A O 1 ATOM 2774 C CB . PRO A 1 357 ? -6.286 -50.950 -15.918 1.00 49.75 ? 359 PRO A CB 1 ATOM 2775 C CG . PRO A 1 357 ? -6.943 -49.696 -16.403 1.00 45.77 ? 359 PRO A CG 1 ATOM 2776 C CD . PRO A 1 357 ? -7.324 -48.909 -15.138 1.00 42.29 ? 359 PRO A CD 1 ATOM 2777 N N . GLY A 1 358 ? -3.570 -49.458 -14.993 1.00 49.55 ? 360 GLY A N 1 ATOM 2778 C CA . GLY A 1 358 ? -2.072 -49.494 -14.987 1.00 50.02 ? 360 GLY A CA 1 ATOM 2779 C C . GLY A 1 358 ? -1.446 -49.061 -13.652 1.00 48.57 ? 360 GLY A C 1 ATOM 2780 O O . GLY A 1 358 ? -0.222 -48.908 -13.531 1.00 50.52 ? 360 GLY A O 1 ATOM 2781 N N . VAL A 1 359 ? -2.263 -48.876 -12.627 1.00 44.52 ? 361 VAL A N 1 ATOM 2782 C CA . VAL A 1 359 ? -1.807 -48.169 -11.427 1.00 41.16 ? 361 VAL A CA 1 ATOM 2783 C C . VAL A 1 359 ? -1.309 -49.175 -10.368 1.00 41.98 ? 361 VAL A C 1 ATOM 2784 O O . VAL A 1 359 ? -1.893 -50.264 -10.180 1.00 42.86 ? 361 VAL A O 1 ATOM 2785 C CB . VAL A 1 359 ? -2.933 -47.179 -10.872 1.00 38.66 ? 361 VAL A CB 1 ATOM 2786 C CG1 . VAL A 1 359 ? -2.528 -46.570 -9.541 1.00 36.69 ? 361 VAL A CG1 1 ATOM 2787 C CG2 . VAL A 1 359 ? -3.249 -46.017 -11.898 1.00 34.24 ? 361 VAL A CG2 1 ATOM 2788 N N . SER A 1 360 ? -0.251 -48.815 -9.654 1.00 41.30 ? 362 SER A N 1 ATOM 2789 C CA . SER A 1 360 ? 0.297 -49.707 -8.649 1.00 42.69 ? 362 SER A CA 1 ATOM 2790 C C . SER A 1 360 ? -0.715 -49.957 -7.515 1.00 41.01 ? 362 SER A C 1 ATOM 2791 O O . SER A 1 360 ? -1.600 -49.133 -7.269 1.00 39.52 ? 362 SER A O 1 ATOM 2792 C CB . SER A 1 360 ? 1.584 -49.093 -8.082 1.00 42.03 ? 362 SER A CB 1 ATOM 2793 O OG . SER A 1 360 ? 1.262 -47.923 -7.325 1.00 41.30 ? 362 SER A OG 1 ATOM 2794 N N . GLU A 1 361 ? -0.549 -51.062 -6.809 1.00 42.62 ? 363 GLU A N 1 ATOM 2795 C CA A GLU A 1 361 ? -1.320 -51.364 -5.612 0.50 42.36 ? 363 GLU A CA 1 ATOM 2796 C CA B GLU A 1 361 ? -1.362 -51.345 -5.625 0.50 42.62 ? 363 GLU A CA 1 ATOM 2797 C C . GLU A 1 361 ? -1.291 -50.196 -4.614 1.00 40.77 ? 363 GLU A C 1 ATOM 2798 O O . GLU A 1 361 ? -2.325 -49.812 -4.021 1.00 40.50 ? 363 GLU A O 1 ATOM 2799 C CB A GLU A 1 361 ? -0.768 -52.649 -4.961 0.50 45.10 ? 363 GLU A CB 1 ATOM 2800 C CB B GLU A 1 361 ? -0.950 -52.680 -4.968 0.50 45.69 ? 363 GLU A CB 1 ATOM 2801 C CG A GLU A 1 361 ? -1.089 -53.910 -5.748 0.50 47.01 ? 363 GLU A CG 1 ATOM 2802 C CG B GLU A 1 361 ? -1.458 -52.888 -3.515 0.50 46.81 ? 363 GLU A CG 1 ATOM 2803 C CD A GLU A 1 361 ? -2.465 -53.839 -6.392 0.50 46.44 ? 363 GLU A CD 1 ATOM 2804 C CD B GLU A 1 361 ? -2.996 -53.016 -3.374 0.50 49.00 ? 363 GLU A CD 1 ATOM 2805 O OE1 A GLU A 1 361 ? -2.519 -53.783 -7.646 0.50 47.47 ? 363 GLU A OE1 1 ATOM 2806 O OE1 B GLU A 1 361 ? -3.765 -52.291 -4.070 0.50 44.76 ? 363 GLU A OE1 1 ATOM 2807 O OE2 A GLU A 1 361 ? -3.483 -53.824 -5.652 0.50 41.84 ? 363 GLU A OE2 1 ATOM 2808 O OE2 B GLU A 1 361 ? -3.420 -53.844 -2.529 0.50 50.21 ? 363 GLU A OE2 1 ATOM 2809 N N . PHE A 1 362 ? -0.101 -49.640 -4.385 1.00 40.56 ? 364 PHE A N 1 ATOM 2810 C CA . PHE A 1 362 ? -0.022 -48.477 -3.481 1.00 38.56 ? 364 PHE A CA 1 ATOM 2811 C C . PHE A 1 362 ? -0.869 -47.300 -4.028 1.00 35.85 ? 364 PHE A C 1 ATOM 2812 O O . PHE A 1 362 ? -1.618 -46.662 -3.303 1.00 35.56 ? 364 PHE A O 1 ATOM 2813 C CB . PHE A 1 362 ? 1.437 -48.080 -3.262 1.00 39.22 ? 364 PHE A CB 1 ATOM 2814 C CG . PHE A 1 362 ? 1.615 -46.736 -2.612 1.00 38.17 ? 364 PHE A CG 1 ATOM 2815 C CD1 . PHE A 1 362 ? 1.911 -45.617 -3.381 1.00 35.63 ? 364 PHE A CD1 1 ATOM 2816 C CD2 . PHE A 1 362 ? 1.442 -46.579 -1.239 1.00 32.77 ? 364 PHE A CD2 1 ATOM 2817 C CE1 . PHE A 1 362 ? 2.084 -44.352 -2.755 1.00 38.06 ? 364 PHE A CE1 1 ATOM 2818 C CE2 . PHE A 1 362 ? 1.560 -45.324 -0.656 1.00 38.37 ? 364 PHE A CE2 1 ATOM 2819 C CZ . PHE A 1 362 ? 1.906 -44.205 -1.406 1.00 33.27 ? 364 PHE A CZ 1 ATOM 2820 N N . GLY A 1 363 ? -0.772 -47.014 -5.328 1.00 35.87 ? 365 GLY A N 1 ATOM 2821 C CA . GLY A 1 363 ? -1.581 -45.968 -5.928 1.00 32.14 ? 365 GLY A CA 1 ATOM 2822 C C . GLY A 1 363 ? -3.046 -46.203 -5.629 1.00 33.11 ? 365 GLY A C 1 ATOM 2823 O O . GLY A 1 363 ? -3.765 -45.264 -5.222 1.00 32.05 ? 365 GLY A O 1 ATOM 2824 N N . LYS A 1 364 ? -3.520 -47.454 -5.820 1.00 34.50 ? 366 LYS A N 1 ATOM 2825 C CA . LYS A 1 364 ? -4.960 -47.699 -5.639 1.00 34.64 ? 366 LYS A CA 1 ATOM 2826 C C . LYS A 1 364 ? -5.321 -47.586 -4.161 1.00 34.20 ? 366 LYS A C 1 ATOM 2827 O O . LYS A 1 364 ? -6.392 -47.041 -3.850 1.00 33.42 ? 366 LYS A O 1 ATOM 2828 C CB . LYS A 1 364 ? -5.454 -49.043 -6.201 1.00 35.40 ? 366 LYS A CB 1 ATOM 2829 C CG . LYS A 1 364 ? -5.329 -49.211 -7.724 1.00 40.48 ? 366 LYS A CG 1 ATOM 2830 C CD . LYS A 1 364 ? -5.954 -50.496 -8.137 1.00 43.58 ? 366 LYS A CD 1 ATOM 2831 C CE . LYS A 1 364 ? -4.840 -51.560 -8.326 1.00 53.65 ? 366 LYS A CE 1 ATOM 2832 N NZ . LYS A 1 364 ? -4.531 -51.731 -9.788 1.00 56.42 ? 366 LYS A NZ 1 ATOM 2833 N N . GLU A 1 365 ? -4.483 -48.117 -3.268 1.00 34.77 ? 367 GLU A N 1 ATOM 2834 C CA . GLU A 1 365 ? -4.766 -47.931 -1.841 1.00 37.74 ? 367 GLU A CA 1 ATOM 2835 C C . GLU A 1 365 ? -4.807 -46.447 -1.469 1.00 34.84 ? 367 GLU A C 1 ATOM 2836 O O . GLU A 1 365 ? -5.617 -46.057 -0.614 1.00 34.75 ? 367 GLU A O 1 ATOM 2837 C CB . GLU A 1 365 ? -3.760 -48.625 -0.918 1.00 38.73 ? 367 GLU A CB 1 ATOM 2838 C CG . GLU A 1 365 ? -4.223 -50.015 -0.542 1.00 53.60 ? 367 GLU A CG 1 ATOM 2839 C CD . GLU A 1 365 ? -4.511 -50.217 0.977 1.00 65.13 ? 367 GLU A CD 1 ATOM 2840 O OE1 . GLU A 1 365 ? -5.716 -50.179 1.380 1.00 66.58 ? 367 GLU A OE1 1 ATOM 2841 O OE2 . GLU A 1 365 ? -3.522 -50.447 1.743 1.00 68.11 ? 367 GLU A OE2 1 ATOM 2842 N N . SER A 1 366 ? -3.950 -45.628 -2.077 1.00 33.59 ? 368 SER A N 1 ATOM 2843 C CA . SER A 1 366 ? -3.947 -44.197 -1.660 1.00 34.33 ? 368 SER A CA 1 ATOM 2844 C C . SER A 1 366 ? -5.320 -43.534 -2.009 1.00 32.44 ? 368 SER A C 1 ATOM 2845 O O . SER A 1 366 ? -5.847 -42.669 -1.283 1.00 31.74 ? 368 SER A O 1 ATOM 2846 C CB . SER A 1 366 ? -2.745 -43.429 -2.220 1.00 33.30 ? 368 SER A CB 1 ATOM 2847 O OG . SER A 1 366 ? -3.021 -43.058 -3.559 1.00 34.43 ? 368 SER A OG 1 ATOM 2848 N N . ILE A 1 367 ? -5.918 -44.000 -3.099 1.00 32.16 ? 369 ILE A N 1 ATOM 2849 C CA . ILE A 1 367 ? -7.236 -43.505 -3.518 1.00 31.09 ? 369 ILE A CA 1 ATOM 2850 C C . ILE A 1 367 ? -8.266 -43.956 -2.472 1.00 32.23 ? 369 ILE A C 1 ATOM 2851 O O . ILE A 1 367 ? -9.053 -43.147 -1.973 1.00 32.33 ? 369 ILE A O 1 ATOM 2852 C CB . ILE A 1 367 ? -7.662 -44.026 -4.938 1.00 30.46 ? 369 ILE A CB 1 ATOM 2853 C CG1 . ILE A 1 367 ? -6.718 -43.521 -6.045 1.00 26.80 ? 369 ILE A CG1 1 ATOM 2854 C CG2 . ILE A 1 367 ? -9.074 -43.578 -5.257 1.00 27.93 ? 369 ILE A CG2 1 ATOM 2855 C CD1 . ILE A 1 367 ? -7.012 -44.234 -7.420 1.00 22.95 ? 369 ILE A CD1 1 ATOM 2856 N N . LEU A 1 368 ? -8.201 -45.229 -2.092 1.00 34.02 ? 370 LEU A N 1 ATOM 2857 C CA . LEU A 1 368 ? -9.140 -45.808 -1.144 1.00 35.26 ? 370 LEU A CA 1 ATOM 2858 C C . LEU A 1 368 ? -9.026 -45.033 0.161 1.00 35.05 ? 370 LEU A C 1 ATOM 2859 O O . LEU A 1 368 ? -10.007 -44.672 0.743 1.00 35.21 ? 370 LEU A O 1 ATOM 2860 C CB . LEU A 1 368 ? -8.794 -47.262 -0.931 1.00 37.27 ? 370 LEU A CB 1 ATOM 2861 C CG . LEU A 1 368 ? -9.275 -48.303 0.099 1.00 42.51 ? 370 LEU A CG 1 ATOM 2862 C CD1 . LEU A 1 368 ? -9.118 -47.902 1.554 1.00 45.52 ? 370 LEU A CD1 1 ATOM 2863 C CD2 . LEU A 1 368 ? -10.665 -48.827 -0.204 1.00 45.26 ? 370 LEU A CD2 1 ATOM 2864 N N . PHE A 1 369 ? -7.815 -44.793 0.604 1.00 34.64 ? 371 PHE A N 1 ATOM 2865 C CA . PHE A 1 369 ? -7.571 -44.056 1.840 1.00 36.39 ? 371 PHE A CA 1 ATOM 2866 C C . PHE A 1 369 ? -8.121 -42.647 1.845 1.00 35.37 ? 371 PHE A C 1 ATOM 2867 O O . PHE A 1 369 ? -8.704 -42.199 2.863 1.00 34.48 ? 371 PHE A O 1 ATOM 2868 C CB . PHE A 1 369 ? -6.069 -44.002 2.078 1.00 38.23 ? 371 PHE A CB 1 ATOM 2869 C CG . PHE A 1 369 ? -5.672 -43.223 3.277 1.00 43.07 ? 371 PHE A CG 1 ATOM 2870 C CD1 . PHE A 1 369 ? -5.351 -41.844 3.152 1.00 45.75 ? 371 PHE A CD1 1 ATOM 2871 C CD2 . PHE A 1 369 ? -5.553 -43.865 4.533 1.00 47.32 ? 371 PHE A CD2 1 ATOM 2872 C CE1 . PHE A 1 369 ? -4.940 -41.079 4.308 1.00 50.02 ? 371 PHE A CE1 1 ATOM 2873 C CE2 . PHE A 1 369 ? -5.165 -43.126 5.698 1.00 53.55 ? 371 PHE A CE2 1 ATOM 2874 C CZ . PHE A 1 369 ? -4.848 -41.740 5.602 1.00 52.18 ? 371 PHE A CZ 1 ATOM 2875 N N . HIS A 1 370 ? -7.918 -41.933 0.733 1.00 33.61 ? 372 HIS A N 1 ATOM 2876 C CA A HIS A 1 370 ? -8.410 -40.535 0.623 0.50 34.83 ? 372 HIS A CA 1 ATOM 2877 C CA B HIS A 1 370 ? -8.390 -40.557 0.693 0.50 35.08 ? 372 HIS A CA 1 ATOM 2878 C C . HIS A 1 370 ? -9.932 -40.463 0.565 1.00 35.80 ? 372 HIS A C 1 ATOM 2879 O O . HIS A 1 370 ? -10.533 -39.542 1.089 1.00 37.83 ? 372 HIS A O 1 ATOM 2880 C CB A HIS A 1 370 ? -7.823 -39.733 -0.557 0.50 32.20 ? 372 HIS A CB 1 ATOM 2881 C CB B HIS A 1 370 ? -7.555 -39.711 -0.290 0.50 33.10 ? 372 HIS A CB 1 ATOM 2882 C CG A HIS A 1 370 ? -8.050 -38.254 -0.419 0.50 33.01 ? 372 HIS A CG 1 ATOM 2883 C CG B HIS A 1 370 ? -6.189 -39.369 0.256 0.50 33.97 ? 372 HIS A CG 1 ATOM 2884 N ND1 A HIS A 1 370 ? -9.096 -37.592 -1.040 0.50 30.82 ? 372 HIS A ND1 1 ATOM 2885 N ND1 B HIS A 1 370 ? -5.102 -40.216 0.146 0.50 30.35 ? 372 HIS A ND1 1 ATOM 2886 C CD2 A HIS A 1 370 ? -7.389 -37.316 0.304 0.50 30.87 ? 372 HIS A CD2 1 ATOM 2887 C CD2 B HIS A 1 370 ? -5.764 -38.315 0.996 0.50 31.08 ? 372 HIS A CD2 1 ATOM 2888 C CE1 A HIS A 1 370 ? -9.067 -36.317 -0.700 0.50 28.69 ? 372 HIS A CE1 1 ATOM 2889 C CE1 B HIS A 1 370 ? -4.058 -39.672 0.738 0.50 32.06 ? 372 HIS A CE1 1 ATOM 2890 N NE2 A HIS A 1 370 ? -8.056 -36.126 0.126 0.50 28.91 ? 372 HIS A NE2 1 ATOM 2891 N NE2 B HIS A 1 370 ? -4.434 -38.527 1.271 0.50 30.44 ? 372 HIS A NE2 1 ATOM 2892 N N . TYR A 1 371 ? -10.573 -41.471 -0.030 1.00 35.77 ? 373 TYR A N 1 ATOM 2893 C CA . TYR A 1 371 ? -11.991 -41.399 -0.227 1.00 36.91 ? 373 TYR A CA 1 ATOM 2894 C C . TYR A 1 371 ? -12.874 -42.152 0.755 1.00 40.88 ? 373 TYR A C 1 ATOM 2895 O O . TYR A 1 371 ? -14.106 -42.038 0.659 1.00 42.77 ? 373 TYR A O 1 ATOM 2896 C CB . TYR A 1 371 ? -12.299 -41.818 -1.675 1.00 34.73 ? 373 TYR A CB 1 ATOM 2897 C CG . TYR A 1 371 ? -12.151 -40.648 -2.613 1.00 33.20 ? 373 TYR A CG 1 ATOM 2898 C CD1 . TYR A 1 371 ? -13.283 -39.811 -2.954 1.00 29.26 ? 373 TYR A CD1 1 ATOM 2899 C CD2 . TYR A 1 371 ? -10.893 -40.330 -3.138 1.00 25.96 ? 373 TYR A CD2 1 ATOM 2900 C CE1 . TYR A 1 371 ? -13.109 -38.694 -3.832 1.00 28.22 ? 373 TYR A CE1 1 ATOM 2901 C CE2 . TYR A 1 371 ? -10.714 -39.215 -3.964 1.00 28.61 ? 373 TYR A CE2 1 ATOM 2902 C CZ . TYR A 1 371 ? -11.821 -38.418 -4.330 1.00 29.17 ? 373 TYR A CZ 1 ATOM 2903 O OH . TYR A 1 371 ? -11.592 -37.336 -5.116 1.00 26.63 ? 373 TYR A OH 1 ATOM 2904 N N . THR A 1 372 ? -12.307 -42.934 1.671 1.00 43.64 ? 374 THR A N 1 ATOM 2905 C CA . THR A 1 372 ? -13.140 -43.800 2.518 1.00 48.67 ? 374 THR A CA 1 ATOM 2906 C C . THR A 1 372 ? -13.035 -43.474 3.978 1.00 53.36 ? 374 THR A C 1 ATOM 2907 O O . THR A 1 372 ? -13.299 -44.316 4.807 1.00 56.14 ? 374 THR A O 1 ATOM 2908 C CB . THR A 1 372 ? -12.791 -45.304 2.398 1.00 48.35 ? 374 THR A CB 1 ATOM 2909 O OG1 . THR A 1 372 ? -11.393 -45.464 2.647 1.00 51.05 ? 374 THR A OG1 1 ATOM 2910 C CG2 . THR A 1 372 ? -13.116 -45.839 1.045 1.00 47.35 ? 374 THR A CG2 1 ATOM 2911 N N . ASP A 1 373 ? -12.627 -42.267 4.312 1.00 57.58 ? 375 ASP A N 1 ATOM 2912 C CA . ASP A 1 373 ? -12.661 -41.821 5.707 1.00 64.13 ? 375 ASP A CA 1 ATOM 2913 C C . ASP A 1 373 ? -14.020 -41.127 5.994 1.00 67.25 ? 375 ASP A C 1 ATOM 2914 O O . ASP A 1 373 ? -14.233 -39.942 5.661 1.00 68.31 ? 375 ASP A O 1 ATOM 2915 C CB . ASP A 1 373 ? -11.494 -40.888 5.937 1.00 64.97 ? 375 ASP A CB 1 ATOM 2916 C CG . ASP A 1 373 ? -10.997 -40.953 7.317 1.00 71.86 ? 375 ASP A CG 1 ATOM 2917 O OD1 . ASP A 1 373 ? -11.854 -40.737 8.198 1.00 76.96 ? 375 ASP A OD1 1 ATOM 2918 O OD2 . ASP A 1 373 ? -9.771 -41.221 7.526 1.00 74.11 ? 375 ASP A OD2 1 ATOM 2919 N N . TRP A 1 374 ? -14.981 -41.860 6.540 1.00 69.69 ? 376 TRP A N 1 ATOM 2920 C CA . TRP A 1 374 ? -16.270 -41.243 6.783 1.00 72.14 ? 376 TRP A CA 1 ATOM 2921 C C . TRP A 1 374 ? -16.384 -40.867 8.276 1.00 78.48 ? 376 TRP A C 1 ATOM 2922 O O . TRP A 1 374 ? -15.802 -41.578 9.113 1.00 80.13 ? 376 TRP A O 1 ATOM 2923 C CB . TRP A 1 374 ? -17.385 -42.181 6.380 1.00 71.13 ? 376 TRP A CB 1 ATOM 2924 C CG . TRP A 1 374 ? -16.997 -43.484 5.712 1.00 65.82 ? 376 TRP A CG 1 ATOM 2925 C CD1 . TRP A 1 374 ? -16.735 -44.684 6.338 1.00 64.80 ? 376 TRP A CD1 1 ATOM 2926 C CD2 . TRP A 1 374 ? -16.919 -43.749 4.290 1.00 57.65 ? 376 TRP A CD2 1 ATOM 2927 N NE1 . TRP A 1 374 ? -16.453 -45.659 5.395 1.00 60.13 ? 376 TRP A NE1 1 ATOM 2928 C CE2 . TRP A 1 374 ? -16.583 -45.123 4.139 1.00 55.07 ? 376 TRP A CE2 1 ATOM 2929 C CE3 . TRP A 1 374 ? -17.076 -42.957 3.137 1.00 52.07 ? 376 TRP A CE3 1 ATOM 2930 C CZ2 . TRP A 1 374 ? -16.411 -45.715 2.885 1.00 50.14 ? 376 TRP A CZ2 1 ATOM 2931 C CZ3 . TRP A 1 374 ? -16.903 -43.548 1.884 1.00 44.61 ? 376 TRP A CZ3 1 ATOM 2932 C CH2 . TRP A 1 374 ? -16.569 -44.906 1.770 1.00 46.89 ? 376 TRP A CH2 1 ATOM 2933 N N . VAL A 1 375 ? -17.094 -39.797 8.685 1.00 82.92 ? 377 VAL A N 1 ATOM 2934 C CA . VAL A 1 375 ? -18.010 -38.842 7.957 1.00 84.28 ? 377 VAL A CA 1 ATOM 2935 C C . VAL A 1 375 ? -19.520 -39.183 7.849 1.00 85.99 ? 377 VAL A C 1 ATOM 2936 O O . VAL A 1 375 ? -20.170 -38.754 6.881 1.00 84.97 ? 377 VAL A O 1 ATOM 2937 C CB . VAL A 1 375 ? -17.426 -38.102 6.649 1.00 81.23 ? 377 VAL A CB 1 ATOM 2938 C CG1 . VAL A 1 375 ? -17.972 -38.701 5.294 1.00 78.61 ? 377 VAL A CG1 1 ATOM 2939 C CG2 . VAL A 1 375 ? -17.756 -36.603 6.720 1.00 83.24 ? 377 VAL A CG2 1 ATOM 2940 N N . ASP A 1 376 ? -20.091 -39.974 8.776 1.00 89.40 ? 378 ASP A N 1 ATOM 2941 C CA . ASP A 1 376 ? -19.439 -41.079 9.523 1.00 90.17 ? 378 ASP A CA 1 ATOM 2942 C C . ASP A 1 376 ? -20.430 -42.245 9.642 1.00 90.89 ? 378 ASP A C 1 ATOM 2943 O O . ASP A 1 376 ? -20.021 -43.408 9.466 1.00 89.46 ? 378 ASP A O 1 ATOM 2944 C CB . ASP A 1 376 ? -18.886 -40.676 10.905 1.00 94.50 ? 378 ASP A CB 1 ATOM 2945 C CG . ASP A 1 376 ? -17.842 -41.705 11.483 1.00 96.66 ? 378 ASP A CG 1 ATOM 2946 O OD1 . ASP A 1 376 ? -17.971 -42.929 11.213 1.00 96.00 ? 378 ASP A OD1 1 ATOM 2947 O OD2 . ASP A 1 376 ? -16.903 -41.285 12.240 1.00 98.35 ? 378 ASP A OD2 1 ATOM 2948 N N . ASP A 1 377 ? -21.713 -41.937 9.925 1.00 92.39 ? 379 ASP A N 1 ATOM 2949 C CA . ASP A 1 377 ? -22.774 -42.945 10.006 1.00 93.15 ? 379 ASP A CA 1 ATOM 2950 C C . ASP A 1 377 ? -22.430 -43.970 8.937 1.00 89.07 ? 379 ASP A C 1 ATOM 2951 O O . ASP A 1 377 ? -21.871 -43.585 7.861 1.00 85.96 ? 379 ASP A O 1 ATOM 2952 C CB . ASP A 1 377 ? -24.133 -42.316 9.634 1.00 94.75 ? 379 ASP A CB 1 ATOM 2953 C CG . ASP A 1 377 ? -25.070 -42.055 10.844 1.00 100.41 ? 379 ASP A CG 1 ATOM 2954 O OD1 . ASP A 1 377 ? -25.195 -42.913 11.751 1.00 106.32 ? 379 ASP A OD1 1 ATOM 2955 O OD2 . ASP A 1 377 ? -25.742 -40.997 10.851 1.00 100.11 ? 379 ASP A OD2 1 ATOM 2956 N N . GLN A 1 378 ? -22.732 -45.253 9.173 1.00 88.76 ? 380 GLN A N 1 ATOM 2957 C CA . GLN A 1 378 ? -22.666 -46.239 8.050 1.00 83.67 ? 380 GLN A CA 1 ATOM 2958 C C . GLN A 1 378 ? -24.085 -46.641 7.584 1.00 82.95 ? 380 GLN A C 1 ATOM 2959 O O . GLN A 1 378 ? -24.488 -47.767 7.846 1.00 85.71 ? 380 GLN A O 1 ATOM 2960 C CB . GLN A 1 378 ? -21.821 -47.468 8.471 1.00 84.68 ? 380 GLN A CB 1 ATOM 2961 C CG . GLN A 1 378 ? -20.367 -47.505 7.934 1.00 79.48 ? 380 GLN A CG 1 ATOM 2962 C CD . GLN A 1 378 ? -19.512 -46.333 8.402 1.00 78.73 ? 380 GLN A CD 1 ATOM 2963 O OE1 . GLN A 1 378 ? -18.517 -46.505 9.093 1.00 80.44 ? 380 GLN A OE1 1 ATOM 2964 N NE2 . GLN A 1 378 ? -19.887 -45.136 8.006 1.00 79.18 ? 380 GLN A NE2 1 ATOM 2965 N N . ARG A 1 379 ? -24.836 -45.836 6.814 1.00 78.94 ? 381 ARG A N 1 ATOM 2966 C CA . ARG A 1 379 ? -24.538 -45.232 5.476 1.00 71.49 ? 381 ARG A CA 1 ATOM 2967 C C . ARG A 1 379 ? -24.168 -46.298 4.413 1.00 65.37 ? 381 ARG A C 1 ATOM 2968 O O . ARG A 1 379 ? -23.043 -46.378 3.954 1.00 62.65 ? 381 ARG A O 1 ATOM 2969 C CB . ARG A 1 379 ? -23.695 -43.931 5.478 1.00 70.68 ? 381 ARG A CB 1 ATOM 2970 C CG . ARG A 1 379 ? -24.547 -42.635 5.791 1.00 75.23 ? 381 ARG A CG 1 ATOM 2971 C CD . ARG A 1 379 ? -23.999 -41.290 5.207 1.00 75.49 ? 381 ARG A CD 1 ATOM 2972 N NE . ARG A 1 379 ? -24.770 -40.777 4.055 1.00 76.33 ? 381 ARG A NE 1 ATOM 2973 C CZ . ARG A 1 379 ? -24.363 -40.793 2.772 1.00 73.66 ? 381 ARG A CZ 1 ATOM 2974 N NH1 . ARG A 1 379 ? -23.169 -41.303 2.412 1.00 70.88 ? 381 ARG A NH1 1 ATOM 2975 N NH2 . ARG A 1 379 ? -25.151 -40.286 1.831 1.00 69.81 ? 381 ARG A NH2 1 ATOM 2976 N N . PRO A 1 380 ? -25.140 -47.142 4.041 1.00 63.49 ? 382 PRO A N 1 ATOM 2977 C CA . PRO A 1 380 ? -24.888 -48.145 3.007 1.00 59.48 ? 382 PRO A CA 1 ATOM 2978 C C . PRO A 1 380 ? -24.392 -47.605 1.670 1.00 53.55 ? 382 PRO A C 1 ATOM 2979 O O . PRO A 1 380 ? -23.681 -48.324 0.991 1.00 50.85 ? 382 PRO A O 1 ATOM 2980 C CB . PRO A 1 380 ? -26.253 -48.854 2.834 1.00 61.91 ? 382 PRO A CB 1 ATOM 2981 C CG . PRO A 1 380 ? -27.264 -48.006 3.570 1.00 65.41 ? 382 PRO A CG 1 ATOM 2982 C CD . PRO A 1 380 ? -26.465 -47.319 4.656 1.00 67.09 ? 382 PRO A CD 1 ATOM 2983 N N . GLU A 1 381 ? -24.763 -46.371 1.298 1.00 50.78 ? 383 GLU A N 1 ATOM 2984 C CA . GLU A 1 381 ? -24.336 -45.748 0.015 1.00 47.05 ? 383 GLU A CA 1 ATOM 2985 C C . GLU A 1 381 ? -22.896 -45.199 -0.001 1.00 44.58 ? 383 GLU A C 1 ATOM 2986 O O . GLU A 1 381 ? -22.444 -44.648 -1.027 1.00 41.76 ? 383 GLU A O 1 ATOM 2987 C CB . GLU A 1 381 ? -25.333 -44.673 -0.453 1.00 46.98 ? 383 GLU A CB 1 ATOM 2988 C CG . GLU A 1 381 ? -25.738 -43.599 0.573 1.00 55.09 ? 383 GLU A CG 1 ATOM 2989 C CD . GLU A 1 381 ? -26.672 -44.113 1.679 1.00 65.73 ? 383 GLU A CD 1 ATOM 2990 O OE1 . GLU A 1 381 ? -26.258 -44.106 2.860 1.00 70.77 ? 383 GLU A OE1 1 ATOM 2991 O OE2 . GLU A 1 381 ? -27.816 -44.551 1.384 1.00 71.69 ? 383 GLU A OE2 1 ATOM 2992 N N . ASN A 1 382 ? -22.185 -45.335 1.130 1.00 44.79 ? 384 ASN A N 1 ATOM 2993 C CA . ASN A 1 382 ? -20.837 -44.764 1.307 1.00 42.74 ? 384 ASN A CA 1 ATOM 2994 C C . ASN A 1 382 ? -19.922 -45.111 0.157 1.00 39.03 ? 384 ASN A C 1 ATOM 2995 O O . ASN A 1 382 ? -19.358 -44.217 -0.489 1.00 36.75 ? 384 ASN A O 1 ATOM 2996 C CB . ASN A 1 382 ? -20.194 -45.162 2.677 1.00 44.32 ? 384 ASN A CB 1 ATOM 2997 C CG . ASN A 1 382 ? -20.613 -44.231 3.835 1.00 49.41 ? 384 ASN A CG 1 ATOM 2998 O OD1 . ASN A 1 382 ? -21.222 -43.142 3.633 1.00 51.47 ? 384 ASN A OD1 1 ATOM 2999 N ND2 . ASN A 1 382 ? -20.314 -44.667 5.065 1.00 54.89 ? 384 ASN A ND2 1 ATOM 3000 N N . TYR A 1 383 ? -19.824 -46.399 -0.153 1.00 38.97 ? 385 TYR A N 1 ATOM 3001 C CA . TYR A 1 383 ? -18.872 -46.814 -1.175 1.00 36.79 ? 385 TYR A CA 1 ATOM 3002 C C . TYR A 1 383 ? -19.386 -46.472 -2.590 1.00 34.93 ? 385 TYR A C 1 ATOM 3003 O O . TYR A 1 383 ? -18.604 -46.116 -3.490 1.00 32.68 ? 385 TYR A O 1 ATOM 3004 C CB . TYR A 1 383 ? -18.501 -48.308 -1.034 1.00 37.68 ? 385 TYR A CB 1 ATOM 3005 C CG . TYR A 1 383 ? -17.557 -48.609 0.142 1.00 38.27 ? 385 TYR A CG 1 ATOM 3006 C CD1 . TYR A 1 383 ? -16.190 -48.221 0.120 1.00 34.60 ? 385 TYR A CD1 1 ATOM 3007 C CD2 . TYR A 1 383 ? -18.022 -49.340 1.262 1.00 40.49 ? 385 TYR A CD2 1 ATOM 3008 C CE1 . TYR A 1 383 ? -15.347 -48.499 1.227 1.00 35.86 ? 385 TYR A CE1 1 ATOM 3009 C CE2 . TYR A 1 383 ? -17.197 -49.637 2.318 1.00 40.98 ? 385 TYR A CE2 1 ATOM 3010 C CZ . TYR A 1 383 ? -15.870 -49.209 2.309 1.00 40.17 ? 385 TYR A CZ 1 ATOM 3011 O OH . TYR A 1 383 ? -15.084 -49.543 3.398 1.00 47.72 ? 385 TYR A OH 1 ATOM 3012 N N . ARG A 1 384 ? -20.690 -46.569 -2.791 1.00 34.54 ? 386 ARG A N 1 ATOM 3013 C CA . ARG A 1 384 ? -21.245 -46.200 -4.106 1.00 33.75 ? 386 ARG A CA 1 ATOM 3014 C C . ARG A 1 384 ? -20.920 -44.724 -4.436 1.00 31.74 ? 386 ARG A C 1 ATOM 3015 O O . ARG A 1 384 ? -20.545 -44.395 -5.547 1.00 31.33 ? 386 ARG A O 1 ATOM 3016 C CB . ARG A 1 384 ? -22.774 -46.439 -4.121 1.00 33.70 ? 386 ARG A CB 1 ATOM 3017 C CG . ARG A 1 384 ? -23.505 -46.187 -5.456 1.00 32.28 ? 386 ARG A CG 1 ATOM 3018 C CD . ARG A 1 384 ? -25.027 -46.092 -5.170 1.00 36.39 ? 386 ARG A CD 1 ATOM 3019 N NE . ARG A 1 384 ? -25.433 -44.802 -4.603 1.00 34.00 ? 386 ARG A NE 1 ATOM 3020 C CZ . ARG A 1 384 ? -26.598 -44.547 -3.983 1.00 38.10 ? 386 ARG A CZ 1 ATOM 3021 N NH1 . ARG A 1 384 ? -27.528 -45.490 -3.825 1.00 40.60 ? 386 ARG A NH1 1 ATOM 3022 N NH2 . ARG A 1 384 ? -26.838 -43.320 -3.501 1.00 35.19 ? 386 ARG A NH2 1 ATOM 3023 N N . GLU A 1 385 ? -21.075 -43.841 -3.458 1.00 33.33 ? 387 GLU A N 1 ATOM 3024 C CA . GLU A 1 385 ? -20.929 -42.414 -3.716 1.00 34.13 ? 387 GLU A CA 1 ATOM 3025 C C . GLU A 1 385 ? -19.473 -42.090 -3.907 1.00 31.39 ? 387 GLU A C 1 ATOM 3026 O O . GLU A 1 385 ? -19.148 -41.259 -4.776 1.00 30.44 ? 387 GLU A O 1 ATOM 3027 C CB . GLU A 1 385 ? -21.511 -41.555 -2.577 1.00 36.63 ? 387 GLU A CB 1 ATOM 3028 C CG . GLU A 1 385 ? -22.923 -41.937 -2.293 1.00 45.46 ? 387 GLU A CG 1 ATOM 3029 C CD . GLU A 1 385 ? -23.817 -40.767 -1.958 1.00 56.55 ? 387 GLU A CD 1 ATOM 3030 O OE1 . GLU A 1 385 ? -24.971 -40.719 -2.485 1.00 60.19 ? 387 GLU A OE1 1 ATOM 3031 O OE2 . GLU A 1 385 ? -23.359 -39.908 -1.162 1.00 60.72 ? 387 GLU A OE2 1 ATOM 3032 N N . ALA A 1 386 ? -18.613 -42.754 -3.118 1.00 29.57 ? 388 ALA A N 1 ATOM 3033 C CA . ALA A 1 386 ? -17.154 -42.497 -3.167 1.00 27.37 ? 388 ALA A CA 1 ATOM 3034 C C . ALA A 1 386 ? -16.620 -42.869 -4.528 1.00 26.84 ? 388 ALA A C 1 ATOM 3035 O O . ALA A 1 386 ? -15.753 -42.163 -5.051 1.00 24.99 ? 388 ALA A O 1 ATOM 3036 C CB . ALA A 1 386 ? -16.363 -43.305 -2.067 1.00 26.56 ? 388 ALA A CB 1 ATOM 3037 N N . LEU A 1 387 ? -17.111 -43.972 -5.107 1.00 27.12 ? 389 LEU A N 1 ATOM 3038 C CA . LEU A 1 387 ? -16.557 -44.371 -6.402 1.00 27.71 ? 389 LEU A CA 1 ATOM 3039 C C . LEU A 1 387 ? -16.921 -43.372 -7.499 1.00 28.83 ? 389 LEU A C 1 ATOM 3040 O O . LEU A 1 387 ? -16.067 -43.085 -8.379 1.00 29.82 ? 389 LEU A O 1 ATOM 3041 C CB . LEU A 1 387 ? -16.948 -45.796 -6.842 1.00 26.75 ? 389 LEU A CB 1 ATOM 3042 C CG . LEU A 1 387 ? -16.126 -46.339 -8.051 1.00 26.00 ? 389 LEU A CG 1 ATOM 3043 C CD1 . LEU A 1 387 ? -14.617 -46.428 -7.750 1.00 26.30 ? 389 LEU A CD1 1 ATOM 3044 C CD2 . LEU A 1 387 ? -16.674 -47.726 -8.527 1.00 30.42 ? 389 LEU A CD2 1 ATOM 3045 N N . GLY A 1 388 ? -18.171 -42.873 -7.483 1.00 29.01 ? 390 GLY A N 1 ATOM 3046 C CA . GLY A 1 388 ? -18.562 -41.825 -8.436 1.00 27.19 ? 390 GLY A CA 1 ATOM 3047 C C . GLY A 1 388 ? -17.665 -40.604 -8.240 1.00 27.79 ? 390 GLY A C 1 ATOM 3048 O O . GLY A 1 388 ? -17.202 -40.030 -9.216 1.00 28.14 ? 390 GLY A O 1 ATOM 3049 N N . ASP A 1 389 ? -17.387 -40.209 -6.992 1.00 27.31 ? 391 ASP A N 1 ATOM 3050 C CA . ASP A 1 389 ? -16.540 -38.996 -6.738 1.00 27.63 ? 391 ASP A CA 1 ATOM 3051 C C . ASP A 1 389 ? -15.079 -39.189 -7.136 1.00 26.32 ? 391 ASP A C 1 ATOM 3052 O O . ASP A 1 389 ? -14.470 -38.288 -7.705 1.00 26.53 ? 391 ASP A O 1 ATOM 3053 C CB . ASP A 1 389 ? -16.632 -38.520 -5.284 1.00 28.59 ? 391 ASP A CB 1 ATOM 3054 C CG . ASP A 1 389 ? -18.018 -37.908 -4.961 1.00 34.17 ? 391 ASP A CG 1 ATOM 3055 O OD1 . ASP A 1 389 ? -18.581 -37.140 -5.767 1.00 33.96 ? 391 ASP A OD1 1 ATOM 3056 O OD2 . ASP A 1 389 ? -18.546 -38.189 -3.880 1.00 37.61 ? 391 ASP A OD2 1 ATOM 3057 N N . VAL A 1 390 ? -14.537 -40.377 -6.903 1.00 25.42 ? 392 VAL A N 1 ATOM 3058 C CA . VAL A 1 390 ? -13.200 -40.710 -7.402 1.00 25.65 ? 392 VAL A CA 1 ATOM 3059 C C . VAL A 1 390 ? -13.156 -40.446 -8.907 1.00 24.92 ? 392 VAL A C 1 ATOM 3060 O O . VAL A 1 390 ? -12.303 -39.705 -9.373 1.00 23.29 ? 392 VAL A O 1 ATOM 3061 C CB . VAL A 1 390 ? -12.843 -42.195 -7.148 1.00 25.68 ? 392 VAL A CB 1 ATOM 3062 C CG1 . VAL A 1 390 ? -11.634 -42.604 -7.954 1.00 27.10 ? 392 VAL A CG1 1 ATOM 3063 C CG2 . VAL A 1 390 ? -12.608 -42.420 -5.707 1.00 26.30 ? 392 VAL A CG2 1 ATOM 3064 N N . VAL A 1 391 ? -14.116 -41.026 -9.643 1.00 25.56 ? 393 VAL A N 1 ATOM 3065 C CA . VAL A 1 391 ? -14.053 -40.935 -11.091 1.00 25.33 ? 393 VAL A CA 1 ATOM 3066 C C . VAL A 1 391 ? -14.297 -39.483 -11.585 1.00 24.23 ? 393 VAL A C 1 ATOM 3067 O O . VAL A 1 391 ? -13.641 -38.998 -12.554 1.00 24.48 ? 393 VAL A O 1 ATOM 3068 C CB . VAL A 1 391 ? -15.089 -41.932 -11.747 1.00 24.87 ? 393 VAL A CB 1 ATOM 3069 C CG1 . VAL A 1 391 ? -15.176 -41.728 -13.249 1.00 24.31 ? 393 VAL A CG1 1 ATOM 3070 C CG2 . VAL A 1 391 ? -14.716 -43.367 -11.415 1.00 28.13 ? 393 VAL A CG2 1 ATOM 3071 N N . GLY A 1 392 ? -15.263 -38.810 -10.969 1.00 21.35 ? 394 GLY A N 1 ATOM 3072 C CA . GLY A 1 392 ? -15.594 -37.470 -11.400 1.00 20.77 ? 394 GLY A CA 1 ATOM 3073 C C . GLY A 1 392 ? -14.453 -36.499 -11.034 1.00 22.22 ? 394 GLY A C 1 ATOM 3074 O O . GLY A 1 392 ? -14.124 -35.578 -11.840 1.00 20.61 ? 394 GLY A O 1 ATOM 3075 N N . ASP A 1 393 ? -13.861 -36.659 -9.835 1.00 22.40 ? 395 ASP A N 1 ATOM 3076 C CA . ASP A 1 393 ? -12.827 -35.696 -9.392 1.00 24.51 ? 395 ASP A CA 1 ATOM 3077 C C . ASP A 1 393 ? -11.561 -35.853 -10.235 1.00 24.87 ? 395 ASP A C 1 ATOM 3078 O O . ASP A 1 393 ? -10.928 -34.863 -10.652 1.00 26.31 ? 395 ASP A O 1 ATOM 3079 C CB . ASP A 1 393 ? -12.472 -35.873 -7.875 1.00 25.40 ? 395 ASP A CB 1 ATOM 3080 C CG . ASP A 1 393 ? -13.650 -35.483 -6.915 1.00 27.81 ? 395 ASP A CG 1 ATOM 3081 O OD1 . ASP A 1 393 ? -13.592 -35.951 -5.737 1.00 24.65 ? 395 ASP A OD1 1 ATOM 3082 O OD2 . ASP A 1 393 ? -14.643 -34.804 -7.361 1.00 23.77 ? 395 ASP A OD2 1 ATOM 3083 N N . TYR A 1 394 ? -11.171 -37.093 -10.469 1.00 25.31 ? 396 TYR A N 1 ATOM 3084 C CA . TYR A 1 394 ? -9.918 -37.358 -11.167 1.00 25.57 ? 396 TYR A CA 1 ATOM 3085 C C . TYR A 1 394 ? -10.023 -36.942 -12.624 1.00 25.01 ? 396 TYR A C 1 ATOM 3086 O O . TYR A 1 394 ? -9.129 -36.331 -13.140 1.00 24.62 ? 396 TYR A O 1 ATOM 3087 C CB . TYR A 1 394 ? -9.569 -38.840 -11.071 1.00 24.91 ? 396 TYR A CB 1 ATOM 3088 C CG . TYR A 1 394 ? -8.419 -39.304 -11.941 1.00 25.04 ? 396 TYR A CG 1 ATOM 3089 C CD1 . TYR A 1 394 ? -7.147 -38.733 -11.835 1.00 26.40 ? 396 TYR A CD1 1 ATOM 3090 C CD2 . TYR A 1 394 ? -8.579 -40.389 -12.843 1.00 29.20 ? 396 TYR A CD2 1 ATOM 3091 C CE1 . TYR A 1 394 ? -6.013 -39.236 -12.579 1.00 24.62 ? 396 TYR A CE1 1 ATOM 3092 C CE2 . TYR A 1 394 ? -7.450 -40.907 -13.599 1.00 28.38 ? 396 TYR A CE2 1 ATOM 3093 C CZ . TYR A 1 394 ? -6.201 -40.292 -13.459 1.00 27.22 ? 396 TYR A CZ 1 ATOM 3094 O OH . TYR A 1 394 ? -5.156 -40.722 -14.214 1.00 32.98 ? 396 TYR A OH 1 ATOM 3095 N N . ASN A 1 395 ? -11.092 -37.351 -13.271 1.00 22.81 ? 397 ASN A N 1 ATOM 3096 C CA . ASN A 1 395 ? -11.236 -37.154 -14.687 1.00 23.39 ? 397 ASN A CA 1 ATOM 3097 C C . ASN A 1 395 ? -11.754 -35.783 -15.152 1.00 22.47 ? 397 ASN A C 1 ATOM 3098 O O . ASN A 1 395 ? -11.508 -35.411 -16.312 1.00 22.05 ? 397 ASN A O 1 ATOM 3099 C CB . ASN A 1 395 ? -12.173 -38.272 -15.281 1.00 21.33 ? 397 ASN A CB 1 ATOM 3100 C CG . ASN A 1 395 ? -11.480 -39.581 -15.272 1.00 24.84 ? 397 ASN A CG 1 ATOM 3101 O OD1 . ASN A 1 395 ? -10.542 -39.768 -16.062 1.00 21.96 ? 397 ASN A OD1 1 ATOM 3102 N ND2 . ASN A 1 395 ? -11.844 -40.486 -14.337 1.00 23.24 ? 397 ASN A ND2 1 ATOM 3103 N N . PHE A 1 396 ? -12.557 -35.109 -14.331 1.00 21.48 ? 398 PHE A N 1 ATOM 3104 C CA . PHE A 1 396 ? -13.213 -33.876 -14.801 1.00 22.49 ? 398 PHE A CA 1 ATOM 3105 C C . PHE A 1 396 ? -12.969 -32.650 -13.894 1.00 23.37 ? 398 PHE A C 1 ATOM 3106 O O . PHE A 1 396 ? -12.504 -31.565 -14.377 1.00 23.45 ? 398 PHE A O 1 ATOM 3107 C CB . PHE A 1 396 ? -14.715 -34.086 -14.994 1.00 20.88 ? 398 PHE A CB 1 ATOM 3108 C CG . PHE A 1 396 ? -15.031 -35.150 -16.077 1.00 23.57 ? 398 PHE A CG 1 ATOM 3109 C CD1 . PHE A 1 396 ? -15.222 -36.498 -15.729 1.00 23.94 ? 398 PHE A CD1 1 ATOM 3110 C CD2 . PHE A 1 396 ? -15.036 -34.808 -17.426 1.00 21.71 ? 398 PHE A CD2 1 ATOM 3111 C CE1 . PHE A 1 396 ? -15.461 -37.527 -16.710 1.00 21.58 ? 398 PHE A CE1 1 ATOM 3112 C CE2 . PHE A 1 396 ? -15.343 -35.797 -18.402 1.00 24.46 ? 398 PHE A CE2 1 ATOM 3113 C CZ . PHE A 1 396 ? -15.488 -37.159 -18.048 1.00 22.59 ? 398 PHE A CZ 1 ATOM 3114 N N . ILE A 1 397 ? -13.332 -32.795 -12.620 1.00 22.77 ? 399 ILE A N 1 ATOM 3115 C CA . ILE A 1 397 ? -13.455 -31.602 -11.759 1.00 23.80 ? 399 ILE A CA 1 ATOM 3116 C C . ILE A 1 397 ? -12.053 -31.051 -11.383 1.00 23.88 ? 399 ILE A C 1 ATOM 3117 O O . ILE A 1 397 ? -11.837 -29.872 -11.551 1.00 24.75 ? 399 ILE A O 1 ATOM 3118 C CB . ILE A 1 397 ? -14.328 -31.893 -10.511 1.00 24.04 ? 399 ILE A CB 1 ATOM 3119 C CG1 . ILE A 1 397 ? -15.741 -32.389 -10.918 1.00 24.54 ? 399 ILE A CG1 1 ATOM 3120 C CG2 . ILE A 1 397 ? -14.263 -30.767 -9.530 1.00 25.08 ? 399 ILE A CG2 1 ATOM 3121 C CD1 . ILE A 1 397 ? -16.713 -32.546 -9.776 1.00 27.07 ? 399 ILE A CD1 1 ATOM 3122 N N . CYS A 1 398 ? -11.111 -31.869 -10.877 1.00 23.72 ? 400 CYS A N 1 ATOM 3123 C CA . CYS A 1 398 ? -9.829 -31.305 -10.518 1.00 23.69 ? 400 CYS A CA 1 ATOM 3124 C C . CYS A 1 398 ? -9.048 -30.794 -11.755 1.00 23.62 ? 400 CYS A C 1 ATOM 3125 O O . CYS A 1 398 ? -8.378 -29.763 -11.662 1.00 24.23 ? 400 CYS A O 1 ATOM 3126 C CB . CYS A 1 398 ? -8.970 -32.294 -9.656 1.00 25.50 ? 400 CYS A CB 1 ATOM 3127 S SG . CYS A 1 398 ? -9.911 -32.833 -8.219 1.00 26.78 ? 400 CYS A SG 1 ATOM 3128 N N . PRO A 1 399 ? -9.075 -31.522 -12.892 1.00 24.02 ? 401 PRO A N 1 ATOM 3129 C CA . PRO A 1 399 ? -8.350 -30.912 -14.015 1.00 23.97 ? 401 PRO A CA 1 ATOM 3130 C C . PRO A 1 399 ? -8.988 -29.582 -14.454 1.00 23.81 ? 401 PRO A C 1 ATOM 3131 O O . PRO A 1 399 ? -8.229 -28.661 -14.819 1.00 23.70 ? 401 PRO A O 1 ATOM 3132 C CB . PRO A 1 399 ? -8.489 -31.948 -15.162 1.00 22.56 ? 401 PRO A CB 1 ATOM 3133 C CG . PRO A 1 399 ? -8.688 -33.291 -14.410 1.00 23.31 ? 401 PRO A CG 1 ATOM 3134 C CD . PRO A 1 399 ? -9.510 -32.912 -13.197 1.00 23.64 ? 401 PRO A CD 1 ATOM 3135 N N . ALA A 1 400 ? -10.328 -29.457 -14.407 1.00 22.47 ? 402 ALA A N 1 ATOM 3136 C CA . ALA A 1 400 ? -10.966 -28.178 -14.813 1.00 22.41 ? 402 ALA A CA 1 ATOM 3137 C C . ALA A 1 400 ? -10.534 -27.078 -13.856 1.00 23.64 ? 402 ALA A C 1 ATOM 3138 O O . ALA A 1 400 ? -10.295 -25.945 -14.294 1.00 23.34 ? 402 ALA A O 1 ATOM 3139 C CB . ALA A 1 400 ? -12.487 -28.255 -14.802 1.00 20.74 ? 402 ALA A CB 1 ATOM 3140 N N . LEU A 1 401 ? -10.470 -27.374 -12.551 1.00 22.76 ? 403 LEU A N 1 ATOM 3141 C CA . LEU A 1 401 ? -10.160 -26.285 -11.626 1.00 23.44 ? 403 LEU A CA 1 ATOM 3142 C C . LEU A 1 401 ? -8.679 -25.953 -11.807 1.00 24.11 ? 403 LEU A C 1 ATOM 3143 O O . LEU A 1 401 ? -8.303 -24.848 -11.732 1.00 23.70 ? 403 LEU A O 1 ATOM 3144 C CB . LEU A 1 401 ? -10.396 -26.722 -10.193 1.00 23.95 ? 403 LEU A CB 1 ATOM 3145 C CG . LEU A 1 401 ? -11.877 -26.761 -9.765 1.00 24.90 ? 403 LEU A CG 1 ATOM 3146 C CD1 . LEU A 1 401 ? -11.998 -27.762 -8.641 1.00 20.87 ? 403 LEU A CD1 1 ATOM 3147 C CD2 . LEU A 1 401 ? -12.388 -25.386 -9.359 1.00 19.08 ? 403 LEU A CD2 1 ATOM 3148 N N . GLU A 1 402 ? -7.835 -26.959 -12.048 1.00 25.93 ? 404 GLU A N 1 ATOM 3149 C CA . GLU A 1 402 ? -6.423 -26.710 -12.229 1.00 26.75 ? 404 GLU A CA 1 ATOM 3150 C C . GLU A 1 402 ? -6.158 -25.879 -13.508 1.00 25.65 ? 404 GLU A C 1 ATOM 3151 O O . GLU A 1 402 ? -5.388 -24.933 -13.482 1.00 26.78 ? 404 GLU A O 1 ATOM 3152 C CB . GLU A 1 402 ? -5.605 -27.994 -12.157 1.00 26.28 ? 404 GLU A CB 1 ATOM 3153 C CG . GLU A 1 402 ? -4.104 -27.740 -12.472 1.00 34.96 ? 404 GLU A CG 1 ATOM 3154 C CD . GLU A 1 402 ? -3.269 -27.225 -11.214 1.00 44.46 ? 404 GLU A CD 1 ATOM 3155 O OE1 . GLU A 1 402 ? -3.904 -26.724 -10.235 1.00 35.77 ? 404 GLU A OE1 1 ATOM 3156 O OE2 . GLU A 1 402 ? -1.980 -27.390 -11.212 1.00 49.67 ? 404 GLU A OE2 1 ATOM 3157 N N . PHE A 1 403 ? -6.810 -26.234 -14.603 1.00 24.57 ? 405 PHE A N 1 ATOM 3158 C CA . PHE A 1 403 ? -6.776 -25.446 -15.819 1.00 24.14 ? 405 PHE A CA 1 ATOM 3159 C C . PHE A 1 403 ? -7.193 -23.983 -15.536 1.00 23.28 ? 405 PHE A C 1 ATOM 3160 O O . PHE A 1 403 ? -6.532 -23.031 -15.982 1.00 23.39 ? 405 PHE A O 1 ATOM 3161 C CB . PHE A 1 403 ? -7.729 -26.040 -16.880 1.00 21.61 ? 405 PHE A CB 1 ATOM 3162 C CG . PHE A 1 403 ? -7.750 -25.221 -18.107 1.00 24.27 ? 405 PHE A CG 1 ATOM 3163 C CD1 . PHE A 1 403 ? -6.790 -25.442 -19.114 1.00 24.18 ? 405 PHE A CD1 1 ATOM 3164 C CD2 . PHE A 1 403 ? -8.678 -24.189 -18.262 1.00 22.25 ? 405 PHE A CD2 1 ATOM 3165 C CE1 . PHE A 1 403 ? -6.771 -24.686 -20.242 1.00 23.59 ? 405 PHE A CE1 1 ATOM 3166 C CE2 . PHE A 1 403 ? -8.650 -23.406 -19.410 1.00 23.31 ? 405 PHE A CE2 1 ATOM 3167 C CZ . PHE A 1 403 ? -7.675 -23.663 -20.406 1.00 21.99 ? 405 PHE A CZ 1 ATOM 3168 N N . THR A 1 404 ? -8.321 -23.803 -14.835 1.00 22.28 ? 406 THR A N 1 ATOM 3169 C CA . THR A 1 404 ? -8.825 -22.463 -14.553 1.00 21.69 ? 406 THR A CA 1 ATOM 3170 C C . THR A 1 404 ? -7.823 -21.679 -13.719 1.00 22.92 ? 406 THR A C 1 ATOM 3171 O O . THR A 1 404 ? -7.556 -20.507 -14.051 1.00 23.64 ? 406 THR A O 1 ATOM 3172 C CB . THR A 1 404 ? -10.225 -22.515 -13.908 1.00 22.12 ? 406 THR A CB 1 ATOM 3173 O OG1 . THR A 1 404 ? -11.085 -23.331 -14.727 1.00 22.21 ? 406 THR A OG1 1 ATOM 3174 C CG2 . THR A 1 404 ? -10.873 -21.061 -13.764 1.00 19.41 ? 406 THR A CG2 1 ATOM 3175 N N . LYS A 1 405 ? -7.209 -22.287 -12.687 1.00 23.75 ? 407 LYS A N 1 ATOM 3176 C CA . LYS A 1 405 ? -6.212 -21.540 -11.899 1.00 26.22 ? 407 LYS A CA 1 ATOM 3177 C C . LYS A 1 405 ? -5.067 -21.122 -12.765 1.00 26.27 ? 407 LYS A C 1 ATOM 3178 O O . LYS A 1 405 ? -4.685 -19.936 -12.746 1.00 25.17 ? 407 LYS A O 1 ATOM 3179 C CB . LYS A 1 405 ? -5.591 -22.292 -10.721 1.00 26.99 ? 407 LYS A CB 1 ATOM 3180 C CG . LYS A 1 405 ? -6.525 -23.054 -9.934 1.00 34.51 ? 407 LYS A CG 1 ATOM 3181 C CD . LYS A 1 405 ? -5.839 -23.538 -8.577 1.00 44.50 ? 407 LYS A CD 1 ATOM 3182 C CE . LYS A 1 405 ? -6.757 -24.590 -7.821 1.00 47.45 ? 407 LYS A CE 1 ATOM 3183 N NZ . LYS A 1 405 ? -6.245 -25.118 -6.439 1.00 52.26 ? 407 LYS A NZ 1 ATOM 3184 N N . LYS A 1 406 ? -4.489 -22.082 -13.503 1.00 26.22 ? 408 LYS A N 1 ATOM 3185 C CA . LYS A 1 406 ? -3.232 -21.768 -14.255 1.00 28.20 ? 408 LYS A CA 1 ATOM 3186 C C . LYS A 1 406 ? -3.532 -20.747 -15.353 1.00 27.73 ? 408 LYS A C 1 ATOM 3187 O O . LYS A 1 406 ? -2.723 -19.870 -15.651 1.00 28.28 ? 408 LYS A O 1 ATOM 3188 C CB . LYS A 1 406 ? -2.583 -23.038 -14.869 1.00 28.63 ? 408 LYS A CB 1 ATOM 3189 C CG . LYS A 1 406 ? -2.059 -24.016 -13.846 1.00 32.62 ? 408 LYS A CG 1 ATOM 3190 C CD . LYS A 1 406 ? -0.796 -23.496 -13.164 1.00 45.60 ? 408 LYS A CD 1 ATOM 3191 C CE . LYS A 1 406 ? -0.195 -24.500 -12.125 1.00 50.01 ? 408 LYS A CE 1 ATOM 3192 N NZ . LYS A 1 406 ? 0.924 -23.756 -11.474 1.00 57.38 ? 408 LYS A NZ 1 ATOM 3193 N N . PHE A 1 407 ? -4.704 -20.860 -15.974 1.00 26.82 ? 409 PHE A N 1 ATOM 3194 C CA . PHE A 1 407 ? -5.047 -19.868 -16.973 1.00 26.57 ? 409 PHE A CA 1 ATOM 3195 C C . PHE A 1 407 ? -5.223 -18.467 -16.388 1.00 27.48 ? 409 PHE A C 1 ATOM 3196 O O . PHE A 1 407 ? -4.760 -17.461 -16.952 1.00 28.00 ? 409 PHE A O 1 ATOM 3197 C CB . PHE A 1 407 ? -6.311 -20.329 -17.698 1.00 26.24 ? 409 PHE A CB 1 ATOM 3198 C CG . PHE A 1 407 ? -6.562 -19.594 -19.006 1.00 26.62 ? 409 PHE A CG 1 ATOM 3199 C CD1 . PHE A 1 407 ? -6.157 -20.156 -20.195 1.00 22.95 ? 409 PHE A CD1 1 ATOM 3200 C CD2 . PHE A 1 407 ? -7.204 -18.354 -19.015 1.00 22.62 ? 409 PHE A CD2 1 ATOM 3201 C CE1 . PHE A 1 407 ? -6.392 -19.483 -21.372 1.00 24.96 ? 409 PHE A CE1 1 ATOM 3202 C CE2 . PHE A 1 407 ? -7.448 -17.676 -20.224 1.00 24.30 ? 409 PHE A CE2 1 ATOM 3203 C CZ . PHE A 1 407 ? -7.011 -18.258 -21.407 1.00 19.46 ? 409 PHE A CZ 1 ATOM 3204 N N . SER A 1 408 ? -5.900 -18.369 -15.247 1.00 27.98 ? 410 SER A N 1 ATOM 3205 C CA . SER A 1 408 ? -6.181 -17.051 -14.692 1.00 27.92 ? 410 SER A CA 1 ATOM 3206 C C . SER A 1 408 ? -4.894 -16.424 -14.164 1.00 29.30 ? 410 SER A C 1 ATOM 3207 O O . SER A 1 408 ? -4.800 -15.221 -14.057 1.00 28.25 ? 410 SER A O 1 ATOM 3208 C CB . SER A 1 408 ? -7.242 -17.188 -13.578 1.00 28.26 ? 410 SER A CB 1 ATOM 3209 O OG . SER A 1 408 ? -6.621 -17.740 -12.413 1.00 29.83 ? 410 SER A OG 1 ATOM 3210 N N . GLU A 1 409 ? -3.862 -17.224 -13.841 1.00 31.47 ? 411 GLU A N 1 ATOM 3211 C CA . GLU A 1 409 ? -2.638 -16.638 -13.267 1.00 32.55 ? 411 GLU A CA 1 ATOM 3212 C C . GLU A 1 409 ? -1.917 -15.770 -14.290 1.00 33.66 ? 411 GLU A C 1 ATOM 3213 O O . GLU A 1 409 ? -1.020 -15.056 -13.944 1.00 34.86 ? 411 GLU A O 1 ATOM 3214 C CB . GLU A 1 409 ? -1.670 -17.694 -12.779 1.00 33.76 ? 411 GLU A CB 1 ATOM 3215 C CG . GLU A 1 409 ? -1.900 -18.017 -11.330 1.00 39.37 ? 411 GLU A CG 1 ATOM 3216 C CD . GLU A 1 409 ? -1.360 -19.373 -10.944 1.00 50.86 ? 411 GLU A CD 1 ATOM 3217 O OE1 . GLU A 1 409 ? -0.503 -19.949 -11.693 1.00 54.89 ? 411 GLU A OE1 1 ATOM 3218 O OE2 . GLU A 1 409 ? -1.782 -19.857 -9.856 1.00 55.84 ? 411 GLU A OE2 1 ATOM 3219 N N . TRP A 1 410 ? -2.311 -15.805 -15.543 1.00 32.59 ? 412 TRP A N 1 ATOM 3220 C CA . TRP A 1 410 ? -1.603 -15.024 -16.490 1.00 32.80 ? 412 TRP A CA 1 ATOM 3221 C C . TRP A 1 410 ? -2.378 -13.818 -16.800 1.00 33.62 ? 412 TRP A C 1 ATOM 3222 O O . TRP A 1 410 ? -2.070 -13.143 -17.762 1.00 35.32 ? 412 TRP A O 1 ATOM 3223 C CB . TRP A 1 410 ? -1.283 -15.857 -17.731 1.00 32.83 ? 412 TRP A CB 1 ATOM 3224 C CG . TRP A 1 410 ? -0.180 -16.781 -17.444 1.00 31.48 ? 412 TRP A CG 1 ATOM 3225 C CD1 . TRP A 1 410 ? -0.255 -18.075 -16.999 1.00 31.15 ? 412 TRP A CD1 1 ATOM 3226 C CD2 . TRP A 1 410 ? 1.221 -16.479 -17.585 1.00 35.40 ? 412 TRP A CD2 1 ATOM 3227 N NE1 . TRP A 1 410 ? 1.032 -18.609 -16.838 1.00 32.60 ? 412 TRP A NE1 1 ATOM 3228 C CE2 . TRP A 1 410 ? 1.950 -17.648 -17.205 1.00 34.00 ? 412 TRP A CE2 1 ATOM 3229 C CE3 . TRP A 1 410 ? 1.935 -15.330 -17.997 1.00 35.31 ? 412 TRP A CE3 1 ATOM 3230 C CZ2 . TRP A 1 410 ? 3.342 -17.684 -17.202 1.00 35.85 ? 412 TRP A CZ2 1 ATOM 3231 C CZ3 . TRP A 1 410 ? 3.364 -15.388 -18.019 1.00 36.23 ? 412 TRP A CZ3 1 ATOM 3232 C CH2 . TRP A 1 410 ? 4.038 -16.552 -17.604 1.00 33.48 ? 412 TRP A CH2 1 ATOM 3233 N N . GLY A 1 411 ? -3.386 -13.475 -15.985 1.00 34.46 ? 413 GLY A N 1 ATOM 3234 C CA . GLY A 1 411 ? -3.954 -12.096 -16.093 1.00 32.63 ? 413 GLY A CA 1 ATOM 3235 C C . GLY A 1 411 ? -5.365 -12.029 -16.690 1.00 33.01 ? 413 GLY A C 1 ATOM 3236 O O . GLY A 1 411 ? -6.039 -11.016 -16.619 1.00 35.26 ? 413 GLY A O 1 ATOM 3237 N N . ASN A 1 412 ? -5.871 -13.136 -17.210 1.00 30.91 ? 414 ASN A N 1 ATOM 3238 C CA A ASN A 1 412 ? -7.195 -13.009 -17.837 0.50 28.79 ? 414 ASN A CA 1 ATOM 3239 C CA B ASN A 1 412 ? -7.150 -13.264 -17.883 0.50 29.08 ? 414 ASN A CA 1 ATOM 3240 C C . ASN A 1 412 ? -8.330 -13.370 -16.904 1.00 28.47 ? 414 ASN A C 1 ATOM 3241 O O . ASN A 1 412 ? -8.205 -14.162 -15.955 1.00 27.04 ? 414 ASN A O 1 ATOM 3242 C CB A ASN A 1 412 ? -7.339 -13.742 -19.184 0.50 26.96 ? 414 ASN A CB 1 ATOM 3243 C CB B ASN A 1 412 ? -7.060 -14.593 -18.636 0.50 26.93 ? 414 ASN A CB 1 ATOM 3244 C CG A ASN A 1 412 ? -6.669 -12.996 -20.341 0.50 23.82 ? 414 ASN A CG 1 ATOM 3245 C CG B ASN A 1 412 ? -5.692 -14.814 -19.306 0.50 26.21 ? 414 ASN A CG 1 ATOM 3246 O OD1 A ASN A 1 412 ? -5.611 -13.425 -20.741 0.50 19.74 ? 414 ASN A OD1 1 ATOM 3247 O OD1 B ASN A 1 412 ? -5.550 -14.466 -20.464 0.50 26.24 ? 414 ASN A OD1 1 ATOM 3248 N ND2 A ASN A 1 412 ? -7.256 -11.858 -20.847 0.50 15.52 ? 414 ASN A ND2 1 ATOM 3249 N ND2 B ASN A 1 412 ? -4.685 -15.347 -18.574 0.50 17.18 ? 414 ASN A ND2 1 ATOM 3250 N N . ASN A 1 413 ? -9.445 -12.673 -17.130 1.00 28.22 ? 415 ASN A N 1 ATOM 3251 C CA . ASN A 1 413 ? -10.668 -12.997 -16.363 1.00 28.72 ? 415 ASN A CA 1 ATOM 3252 C C . ASN A 1 413 ? -11.218 -14.432 -16.671 1.00 28.41 ? 415 ASN A C 1 ATOM 3253 O O . ASN A 1 413 ? -11.271 -14.847 -17.834 1.00 29.31 ? 415 ASN A O 1 ATOM 3254 C CB . ASN A 1 413 ? -11.772 -12.002 -16.692 1.00 29.66 ? 415 ASN A CB 1 ATOM 3255 C CG . ASN A 1 413 ? -11.619 -10.725 -15.971 1.00 31.41 ? 415 ASN A CG 1 ATOM 3256 O OD1 . ASN A 1 413 ? -10.664 -10.539 -15.166 1.00 30.98 ? 415 ASN A OD1 1 ATOM 3257 N ND2 . ASN A 1 413 ? -12.538 -9.785 -16.265 1.00 25.90 ? 415 ASN A ND2 1 ATOM 3258 N N . ALA A 1 414 ? -11.612 -15.165 -15.629 1.00 27.04 ? 416 ALA A N 1 ATOM 3259 C CA . ALA A 1 414 ? -12.058 -16.552 -15.733 1.00 25.25 ? 416 ALA A CA 1 ATOM 3260 C C . ALA A 1 414 ? -13.266 -16.623 -14.833 1.00 24.76 ? 416 ALA A C 1 ATOM 3261 O O . ALA A 1 414 ? -13.294 -15.975 -13.757 1.00 25.60 ? 416 ALA A O 1 ATOM 3262 C CB . ALA A 1 414 ? -10.956 -17.504 -15.214 1.00 24.62 ? 416 ALA A CB 1 ATOM 3263 N N . PHE A 1 415 ? -14.255 -17.383 -15.243 1.00 22.26 ? 417 PHE A N 1 ATOM 3264 C CA . PHE A 1 415 ? -15.458 -17.491 -14.474 1.00 22.57 ? 417 PHE A CA 1 ATOM 3265 C C . PHE A 1 415 ? -15.698 -18.990 -14.321 1.00 23.02 ? 417 PHE A C 1 ATOM 3266 O O . PHE A 1 415 ? -15.620 -19.722 -15.292 1.00 23.72 ? 417 PHE A O 1 ATOM 3267 C CB . PHE A 1 415 ? -16.607 -16.829 -15.270 1.00 22.64 ? 417 PHE A CB 1 ATOM 3268 C CG . PHE A 1 415 ? -16.382 -15.368 -15.492 1.00 22.79 ? 417 PHE A CG 1 ATOM 3269 C CD1 . PHE A 1 415 ? -15.769 -14.920 -16.649 1.00 21.83 ? 417 PHE A CD1 1 ATOM 3270 C CD2 . PHE A 1 415 ? -16.719 -14.425 -14.483 1.00 21.90 ? 417 PHE A CD2 1 ATOM 3271 C CE1 . PHE A 1 415 ? -15.527 -13.513 -16.851 1.00 22.35 ? 417 PHE A CE1 1 ATOM 3272 C CE2 . PHE A 1 415 ? -16.449 -13.063 -14.653 1.00 22.74 ? 417 PHE A CE2 1 ATOM 3273 C CZ . PHE A 1 415 ? -15.871 -12.597 -15.840 1.00 21.42 ? 417 PHE A CZ 1 ATOM 3274 N N . PHE A 1 416 ? -15.978 -19.471 -13.123 1.00 22.84 ? 418 PHE A N 1 ATOM 3275 C CA . PHE A 1 416 ? -16.128 -20.921 -12.955 1.00 21.83 ? 418 PHE A CA 1 ATOM 3276 C C . PHE A 1 416 ? -17.526 -21.271 -12.371 1.00 22.80 ? 418 PHE A C 1 ATOM 3277 O O . PHE A 1 416 ? -17.995 -20.578 -11.439 1.00 24.02 ? 418 PHE A O 1 ATOM 3278 C CB . PHE A 1 416 ? -14.994 -21.450 -12.024 1.00 21.22 ? 418 PHE A CB 1 ATOM 3279 C CG . PHE A 1 416 ? -14.858 -22.933 -12.066 1.00 22.66 ? 418 PHE A CG 1 ATOM 3280 C CD1 . PHE A 1 416 ? -15.767 -23.728 -11.381 1.00 19.70 ? 418 PHE A CD1 1 ATOM 3281 C CD2 . PHE A 1 416 ? -13.873 -23.556 -12.872 1.00 17.56 ? 418 PHE A CD2 1 ATOM 3282 C CE1 . PHE A 1 416 ? -15.665 -25.161 -11.420 1.00 23.30 ? 418 PHE A CE1 1 ATOM 3283 C CE2 . PHE A 1 416 ? -13.789 -24.947 -12.919 1.00 20.30 ? 418 PHE A CE2 1 ATOM 3284 C CZ . PHE A 1 416 ? -14.663 -25.748 -12.203 1.00 19.31 ? 418 PHE A CZ 1 ATOM 3285 N N . TYR A 1 417 ? -18.214 -22.292 -12.906 1.00 21.41 ? 419 TYR A N 1 ATOM 3286 C CA . TYR A 1 417 ? -19.558 -22.647 -12.379 1.00 23.55 ? 419 TYR A CA 1 ATOM 3287 C C . TYR A 1 417 ? -19.593 -24.097 -11.877 1.00 22.79 ? 419 TYR A C 1 ATOM 3288 O O . TYR A 1 417 ? -18.866 -24.939 -12.357 1.00 21.92 ? 419 TYR A O 1 ATOM 3289 C CB . TYR A 1 417 ? -20.723 -22.459 -13.436 1.00 23.35 ? 419 TYR A CB 1 ATOM 3290 C CG . TYR A 1 417 ? -20.635 -23.447 -14.595 1.00 22.27 ? 419 TYR A CG 1 ATOM 3291 C CD1 . TYR A 1 417 ? -19.946 -23.115 -15.779 1.00 22.55 ? 419 TYR A CD1 1 ATOM 3292 C CD2 . TYR A 1 417 ? -21.177 -24.707 -14.488 1.00 22.74 ? 419 TYR A CD2 1 ATOM 3293 C CE1 . TYR A 1 417 ? -19.817 -24.056 -16.863 1.00 25.17 ? 419 TYR A CE1 1 ATOM 3294 C CE2 . TYR A 1 417 ? -21.064 -25.649 -15.523 1.00 23.23 ? 419 TYR A CE2 1 ATOM 3295 C CZ . TYR A 1 417 ? -20.393 -25.338 -16.706 1.00 27.33 ? 419 TYR A CZ 1 ATOM 3296 O OH . TYR A 1 417 ? -20.282 -26.312 -17.706 1.00 21.63 ? 419 TYR A OH 1 ATOM 3297 N N . TYR A 1 418 ? -20.515 -24.389 -10.969 1.00 23.30 ? 420 TYR A N 1 ATOM 3298 C CA . TYR A 1 418 ? -20.709 -25.753 -10.539 1.00 21.70 ? 420 TYR A CA 1 ATOM 3299 C C . TYR A 1 418 ? -22.209 -26.032 -10.735 1.00 23.70 ? 420 TYR A C 1 ATOM 3300 O O . TYR A 1 418 ? -23.049 -25.493 -9.980 1.00 22.86 ? 420 TYR A O 1 ATOM 3301 C CB . TYR A 1 418 ? -20.344 -25.814 -9.070 1.00 21.64 ? 420 TYR A CB 1 ATOM 3302 C CG . TYR A 1 418 ? -20.404 -27.167 -8.419 1.00 22.24 ? 420 TYR A CG 1 ATOM 3303 C CD1 . TYR A 1 418 ? -19.630 -28.223 -8.885 1.00 21.23 ? 420 TYR A CD1 1 ATOM 3304 C CD2 . TYR A 1 418 ? -21.239 -27.374 -7.313 1.00 23.54 ? 420 TYR A CD2 1 ATOM 3305 C CE1 . TYR A 1 418 ? -19.624 -29.459 -8.235 1.00 28.19 ? 420 TYR A CE1 1 ATOM 3306 C CE2 . TYR A 1 418 ? -21.288 -28.608 -6.657 1.00 24.52 ? 420 TYR A CE2 1 ATOM 3307 C CZ . TYR A 1 418 ? -20.481 -29.664 -7.129 1.00 31.37 ? 420 TYR A CZ 1 ATOM 3308 O OH . TYR A 1 418 ? -20.503 -30.905 -6.506 1.00 29.61 ? 420 TYR A OH 1 ATOM 3309 N N . PHE A 1 419 ? -22.535 -26.859 -11.742 1.00 22.93 ? 421 PHE A N 1 ATOM 3310 C CA . PHE A 1 419 ? -23.930 -27.141 -12.116 1.00 23.05 ? 421 PHE A CA 1 ATOM 3311 C C . PHE A 1 419 ? -24.523 -28.249 -11.243 1.00 24.90 ? 421 PHE A C 1 ATOM 3312 O O . PHE A 1 419 ? -24.006 -29.404 -11.205 1.00 24.61 ? 421 PHE A O 1 ATOM 3313 C CB . PHE A 1 419 ? -23.982 -27.483 -13.606 1.00 21.41 ? 421 PHE A CB 1 ATOM 3314 C CG . PHE A 1 419 ? -25.395 -27.727 -14.155 1.00 23.84 ? 421 PHE A CG 1 ATOM 3315 C CD1 . PHE A 1 419 ? -26.185 -26.673 -14.599 1.00 24.40 ? 421 PHE A CD1 1 ATOM 3316 C CD2 . PHE A 1 419 ? -25.879 -29.028 -14.286 1.00 22.37 ? 421 PHE A CD2 1 ATOM 3317 C CE1 . PHE A 1 419 ? -27.472 -26.871 -15.100 1.00 27.91 ? 421 PHE A CE1 1 ATOM 3318 C CE2 . PHE A 1 419 ? -27.161 -29.271 -14.854 1.00 22.85 ? 421 PHE A CE2 1 ATOM 3319 C CZ . PHE A 1 419 ? -27.979 -28.198 -15.229 1.00 22.93 ? 421 PHE A CZ 1 ATOM 3320 N N . GLU A 1 420 ? -25.583 -27.937 -10.499 1.00 26.55 ? 422 GLU A N 1 ATOM 3321 C CA . GLU A 1 420 ? -26.014 -28.925 -9.534 1.00 28.97 ? 422 GLU A CA 1 ATOM 3322 C C . GLU A 1 420 ? -27.507 -29.164 -9.632 1.00 30.63 ? 422 GLU A C 1 ATOM 3323 O O . GLU A 1 420 ? -28.147 -29.569 -8.666 1.00 33.21 ? 422 GLU A O 1 ATOM 3324 C CB . GLU A 1 420 ? -25.483 -28.583 -8.098 1.00 31.45 ? 422 GLU A CB 1 ATOM 3325 C CG . GLU A 1 420 ? -26.195 -27.480 -7.413 1.00 35.60 ? 422 GLU A CG 1 ATOM 3326 C CD . GLU A 1 420 ? -25.417 -26.816 -6.240 1.00 40.41 ? 422 GLU A CD 1 ATOM 3327 O OE1 . GLU A 1 420 ? -24.406 -27.341 -5.748 1.00 37.88 ? 422 GLU A OE1 1 ATOM 3328 O OE2 . GLU A 1 420 ? -25.886 -25.744 -5.797 1.00 42.51 ? 422 GLU A OE2 1 ATOM 3329 N N . HIS A 1 421 ? -28.066 -28.996 -10.833 1.00 29.49 ? 423 HIS A N 1 ATOM 3330 C CA . HIS A 1 421 ? -29.467 -29.304 -11.034 1.00 29.17 ? 423 HIS A CA 1 ATOM 3331 C C . HIS A 1 421 ? -29.685 -30.588 -11.809 1.00 28.78 ? 423 HIS A C 1 ATOM 3332 O O . HIS A 1 421 ? -29.213 -30.730 -12.957 1.00 27.24 ? 423 HIS A O 1 ATOM 3333 C CB . HIS A 1 421 ? -30.191 -28.187 -11.783 1.00 28.05 ? 423 HIS A CB 1 ATOM 3334 C CG . HIS A 1 421 ? -31.614 -28.537 -12.035 1.00 29.49 ? 423 HIS A CG 1 ATOM 3335 N ND1 . HIS A 1 421 ? -32.550 -28.601 -11.015 1.00 34.00 ? 423 HIS A ND1 1 ATOM 3336 C CD2 . HIS A 1 421 ? -32.251 -28.951 -13.156 1.00 29.58 ? 423 HIS A CD2 1 ATOM 3337 C CE1 . HIS A 1 421 ? -33.699 -29.049 -11.495 1.00 31.29 ? 423 HIS A CE1 1 ATOM 3338 N NE2 . HIS A 1 421 ? -33.555 -29.241 -12.795 1.00 30.73 ? 423 HIS A NE2 1 ATOM 3339 N N . ARG A 1 422 ? -30.414 -31.508 -11.204 1.00 30.13 ? 424 ARG A N 1 ATOM 3340 C CA . ARG A 1 422 ? -30.814 -32.754 -11.894 1.00 32.86 ? 424 ARG A CA 1 ATOM 3341 C C . ARG A 1 422 ? -32.085 -32.568 -12.732 1.00 33.25 ? 424 ARG A C 1 ATOM 3342 O O . ARG A 1 422 ? -33.119 -32.195 -12.184 1.00 34.26 ? 424 ARG A O 1 ATOM 3343 C CB . ARG A 1 422 ? -31.069 -33.878 -10.898 1.00 33.60 ? 424 ARG A CB 1 ATOM 3344 C CG . ARG A 1 422 ? -31.416 -35.167 -11.596 1.00 36.22 ? 424 ARG A CG 1 ATOM 3345 C CD . ARG A 1 422 ? -31.411 -36.307 -10.638 1.00 36.31 ? 424 ARG A CD 1 ATOM 3346 N NE . ARG A 1 422 ? -32.257 -37.379 -11.101 1.00 39.04 ? 424 ARG A NE 1 ATOM 3347 C CZ . ARG A 1 422 ? -31.838 -38.524 -11.635 1.00 44.96 ? 424 ARG A CZ 1 ATOM 3348 N NH1 . ARG A 1 422 ? -30.496 -38.788 -11.839 1.00 39.15 ? 424 ARG A NH1 1 ATOM 3349 N NH2 . ARG A 1 422 ? -32.788 -39.430 -11.963 1.00 40.42 ? 424 ARG A NH2 1 ATOM 3350 N N . SER A 1 423 ? -32.005 -32.834 -14.033 1.00 32.79 ? 425 SER A N 1 ATOM 3351 C CA . SER A 1 423 ? -33.129 -32.621 -14.940 1.00 35.00 ? 425 SER A CA 1 ATOM 3352 C C . SER A 1 423 ? -34.346 -33.468 -14.487 1.00 36.16 ? 425 SER A C 1 ATOM 3353 O O . SER A 1 423 ? -34.182 -34.630 -14.121 1.00 35.41 ? 425 SER A O 1 ATOM 3354 C CB . SER A 1 423 ? -32.690 -32.972 -16.358 1.00 34.46 ? 425 SER A CB 1 ATOM 3355 O OG . SER A 1 423 ? -33.812 -32.999 -17.252 1.00 38.09 ? 425 SER A OG 1 ATOM 3356 N N . SER A 1 424 ? -35.540 -32.868 -14.446 1.00 37.81 ? 426 SER A N 1 ATOM 3357 C CA . SER A 1 424 ? -36.742 -33.540 -13.985 1.00 39.46 ? 426 SER A CA 1 ATOM 3358 C C . SER A 1 424 ? -37.060 -34.657 -14.980 1.00 41.25 ? 426 SER A C 1 ATOM 3359 O O . SER A 1 424 ? -37.750 -35.606 -14.644 1.00 40.88 ? 426 SER A O 1 ATOM 3360 C CB . SER A 1 424 ? -37.952 -32.568 -13.891 1.00 41.16 ? 426 SER A CB 1 ATOM 3361 O OG . SER A 1 424 ? -38.259 -31.975 -15.162 1.00 39.94 ? 426 SER A OG 1 ATOM 3362 N N . LYS A 1 425 ? -36.571 -34.518 -16.210 1.00 41.67 ? 427 LYS A N 1 ATOM 3363 C CA . LYS A 1 425 ? -36.797 -35.553 -17.218 1.00 44.15 ? 427 LYS A CA 1 ATOM 3364 C C . LYS A 1 425 ? -35.684 -36.648 -17.266 1.00 43.12 ? 427 LYS A C 1 ATOM 3365 O O . LYS A 1 425 ? -35.780 -37.571 -18.087 1.00 44.84 ? 427 LYS A O 1 ATOM 3366 C CB . LYS A 1 425 ? -36.960 -34.897 -18.613 1.00 44.09 ? 427 LYS A CB 1 ATOM 3367 C CG . LYS A 1 425 ? -38.133 -33.888 -18.687 1.00 50.97 ? 427 LYS A CG 1 ATOM 3368 C CD . LYS A 1 425 ? -38.274 -33.235 -20.098 1.00 55.12 ? 427 LYS A CD 1 ATOM 3369 C CE . LYS A 1 425 ? -38.651 -34.267 -21.220 1.00 56.34 ? 427 LYS A CE 1 ATOM 3370 N NZ . LYS A 1 425 ? -38.616 -33.673 -22.611 1.00 56.09 ? 427 LYS A NZ 1 ATOM 3371 N N . LEU A 1 426 ? -34.655 -36.573 -16.425 1.00 40.45 ? 428 LEU A N 1 ATOM 3372 C CA . LEU A 1 426 ? -33.513 -37.522 -16.549 1.00 38.48 ? 428 LEU A CA 1 ATOM 3373 C C . LEU A 1 426 ? -33.929 -39.037 -16.540 1.00 37.66 ? 428 LEU A C 1 ATOM 3374 O O . LEU A 1 426 ? -34.627 -39.516 -15.622 1.00 39.12 ? 428 LEU A O 1 ATOM 3375 C CB . LEU A 1 426 ? -32.424 -37.192 -15.505 1.00 38.18 ? 428 LEU A CB 1 ATOM 3376 C CG . LEU A 1 426 ? -31.011 -37.729 -15.863 1.00 39.71 ? 428 LEU A CG 1 ATOM 3377 C CD1 . LEU A 1 426 ? -30.302 -36.859 -16.764 1.00 38.26 ? 428 LEU A CD1 1 ATOM 3378 C CD2 . LEU A 1 426 ? -30.183 -37.943 -14.633 1.00 43.86 ? 428 LEU A CD2 1 ATOM 3379 N N . PRO A 1 427 ? -33.594 -39.793 -17.606 1.00 35.60 ? 429 PRO A N 1 ATOM 3380 C CA . PRO A 1 427 ? -34.059 -41.210 -17.691 1.00 34.10 ? 429 PRO A CA 1 ATOM 3381 C C . PRO A 1 427 ? -33.175 -42.121 -16.828 1.00 33.02 ? 429 PRO A C 1 ATOM 3382 O O . PRO A 1 427 ? -33.583 -43.205 -16.411 1.00 32.50 ? 429 PRO A O 1 ATOM 3383 C CB . PRO A 1 427 ? -33.862 -41.550 -19.158 1.00 34.09 ? 429 PRO A CB 1 ATOM 3384 C CG . PRO A 1 427 ? -33.341 -40.335 -19.820 1.00 33.62 ? 429 PRO A CG 1 ATOM 3385 C CD . PRO A 1 427 ? -32.865 -39.377 -18.803 1.00 34.08 ? 429 PRO A CD 1 ATOM 3386 N N . TRP A 1 428 ? -31.971 -41.660 -16.528 1.00 30.62 ? 430 TRP A N 1 ATOM 3387 C CA . TRP A 1 428 ? -31.109 -42.394 -15.584 1.00 30.83 ? 430 TRP A CA 1 ATOM 3388 C C . TRP A 1 428 ? -31.650 -42.334 -14.159 1.00 30.84 ? 430 TRP A C 1 ATOM 3389 O O . TRP A 1 428 ? -32.376 -41.412 -13.799 1.00 30.55 ? 430 TRP A O 1 ATOM 3390 C CB . TRP A 1 428 ? -29.691 -41.833 -15.628 1.00 28.68 ? 430 TRP A CB 1 ATOM 3391 C CG . TRP A 1 428 ? -29.025 -41.898 -17.001 1.00 25.85 ? 430 TRP A CG 1 ATOM 3392 C CD1 . TRP A 1 428 ? -28.978 -40.889 -17.968 1.00 22.04 ? 430 TRP A CD1 1 ATOM 3393 C CD2 . TRP A 1 428 ? -28.357 -43.028 -17.569 1.00 25.65 ? 430 TRP A CD2 1 ATOM 3394 N NE1 . TRP A 1 428 ? -28.335 -41.341 -19.078 1.00 25.27 ? 430 TRP A NE1 1 ATOM 3395 C CE2 . TRP A 1 428 ? -27.893 -42.633 -18.855 1.00 24.89 ? 430 TRP A CE2 1 ATOM 3396 C CE3 . TRP A 1 428 ? -28.095 -44.345 -17.117 1.00 24.70 ? 430 TRP A CE3 1 ATOM 3397 C CZ2 . TRP A 1 428 ? -27.145 -43.493 -19.685 1.00 21.02 ? 430 TRP A CZ2 1 ATOM 3398 C CZ3 . TRP A 1 428 ? -27.339 -45.215 -17.964 1.00 24.23 ? 430 TRP A CZ3 1 ATOM 3399 C CH2 . TRP A 1 428 ? -26.890 -44.777 -19.224 1.00 25.34 ? 430 TRP A CH2 1 ATOM 3400 N N . PRO A 1 429 ? -31.316 -43.328 -13.340 1.00 31.15 ? 431 PRO A N 1 ATOM 3401 C CA . PRO A 1 429 ? -31.885 -43.396 -11.960 1.00 33.30 ? 431 PRO A CA 1 ATOM 3402 C C . PRO A 1 429 ? -31.322 -42.297 -11.024 1.00 34.45 ? 431 PRO A C 1 ATOM 3403 O O . PRO A 1 429 ? -30.220 -41.748 -11.295 1.00 34.90 ? 431 PRO A O 1 ATOM 3404 C CB . PRO A 1 429 ? -31.452 -44.789 -11.467 1.00 32.66 ? 431 PRO A CB 1 ATOM 3405 C CG . PRO A 1 429 ? -30.179 -45.031 -12.245 1.00 32.65 ? 431 PRO A CG 1 ATOM 3406 C CD . PRO A 1 429 ? -30.433 -44.454 -13.639 1.00 30.24 ? 431 PRO A CD 1 ATOM 3407 N N . GLU A 1 430 ? -32.031 -42.006 -9.931 1.00 36.01 ? 432 GLU A N 1 ATOM 3408 C CA . GLU A 1 430 ? -31.633 -40.931 -8.974 1.00 37.76 ? 432 GLU A CA 1 ATOM 3409 C C . GLU A 1 430 ? -30.233 -40.973 -8.382 1.00 35.39 ? 432 GLU A C 1 ATOM 3410 O O . GLU A 1 430 ? -29.651 -39.927 -8.112 1.00 33.12 ? 432 GLU A O 1 ATOM 3411 C CB . GLU A 1 430 ? -32.580 -40.868 -7.752 1.00 39.38 ? 432 GLU A CB 1 ATOM 3412 C CG . GLU A 1 430 ? -33.790 -39.987 -7.913 1.00 50.26 ? 432 GLU A CG 1 ATOM 3413 C CD . GLU A 1 430 ? -34.819 -40.329 -6.821 1.00 63.95 ? 432 GLU A CD 1 ATOM 3414 O OE1 . GLU A 1 430 ? -34.470 -40.179 -5.613 1.00 67.90 ? 432 GLU A OE1 1 ATOM 3415 O OE2 . GLU A 1 430 ? -35.940 -40.802 -7.161 1.00 69.69 ? 432 GLU A OE2 1 ATOM 3416 N N . TRP A 1 431 ? -29.750 -42.175 -8.087 1.00 35.36 ? 433 TRP A N 1 ATOM 3417 C CA . TRP A 1 431 ? -28.483 -42.309 -7.389 1.00 34.92 ? 433 TRP A CA 1 ATOM 3418 C C . TRP A 1 431 ? -27.387 -41.663 -8.268 1.00 33.93 ? 433 TRP A C 1 ATOM 3419 O O . TRP A 1 431 ? -26.391 -41.211 -7.744 1.00 34.45 ? 433 TRP A O 1 ATOM 3420 C CB . TRP A 1 431 ? -28.191 -43.771 -6.980 1.00 34.19 ? 433 TRP A CB 1 ATOM 3421 C CG . TRP A 1 431 ? -27.847 -44.731 -8.106 1.00 33.50 ? 433 TRP A CG 1 ATOM 3422 C CD1 . TRP A 1 431 ? -28.673 -45.716 -8.639 1.00 30.84 ? 433 TRP A CD1 1 ATOM 3423 C CD2 . TRP A 1 431 ? -26.566 -44.863 -8.802 1.00 28.42 ? 433 TRP A CD2 1 ATOM 3424 N NE1 . TRP A 1 431 ? -27.990 -46.409 -9.651 1.00 31.56 ? 433 TRP A NE1 1 ATOM 3425 C CE2 . TRP A 1 431 ? -26.708 -45.922 -9.754 1.00 26.82 ? 433 TRP A CE2 1 ATOM 3426 C CE3 . TRP A 1 431 ? -25.316 -44.193 -8.699 1.00 29.86 ? 433 TRP A CE3 1 ATOM 3427 C CZ2 . TRP A 1 431 ? -25.666 -46.317 -10.604 1.00 31.89 ? 433 TRP A CZ2 1 ATOM 3428 C CZ3 . TRP A 1 431 ? -24.251 -44.570 -9.580 1.00 27.01 ? 433 TRP A CZ3 1 ATOM 3429 C CH2 . TRP A 1 431 ? -24.435 -45.614 -10.519 1.00 31.47 ? 433 TRP A CH2 1 ATOM 3430 N N . MET A 1 432 ? -27.593 -41.608 -9.582 1.00 31.90 ? 434 MET A N 1 ATOM 3431 C CA . MET A 1 432 ? -26.577 -41.065 -10.494 1.00 30.22 ? 434 MET A CA 1 ATOM 3432 C C . MET A 1 432 ? -26.541 -39.570 -10.453 1.00 28.11 ? 434 MET A C 1 ATOM 3433 O O . MET A 1 432 ? -25.598 -38.978 -11.010 1.00 27.46 ? 434 MET A O 1 ATOM 3434 C CB . MET A 1 432 ? -26.795 -41.536 -11.959 1.00 29.90 ? 434 MET A CB 1 ATOM 3435 C CG . MET A 1 432 ? -26.728 -43.057 -12.023 1.00 33.31 ? 434 MET A CG 1 ATOM 3436 S SD . MET A 1 432 ? -26.718 -43.910 -13.581 1.00 32.38 ? 434 MET A SD 1 ATOM 3437 C CE . MET A 1 432 ? -25.449 -43.168 -14.541 1.00 30.52 ? 434 MET A CE 1 ATOM 3438 N N . GLY A 1 433 ? -27.547 -38.956 -9.835 1.00 26.40 ? 435 GLY A N 1 ATOM 3439 C CA . GLY A 1 433 ? -27.493 -37.513 -9.519 1.00 26.72 ? 435 GLY A CA 1 ATOM 3440 C C . GLY A 1 433 ? -27.359 -36.613 -10.752 1.00 28.07 ? 435 GLY A C 1 ATOM 3441 O O . GLY A 1 433 ? -28.030 -36.858 -11.773 1.00 28.35 ? 435 GLY A O 1 ATOM 3442 N N . VAL A 1 434 ? -26.536 -35.551 -10.654 1.00 26.55 ? 436 VAL A N 1 ATOM 3443 C CA . VAL A 1 434 ? -26.397 -34.520 -11.711 1.00 25.75 ? 436 VAL A CA 1 ATOM 3444 C C . VAL A 1 434 ? -25.278 -34.920 -12.699 1.00 25.97 ? 436 VAL A C 1 ATOM 3445 O O . VAL A 1 434 ? -24.082 -34.533 -12.548 1.00 26.05 ? 436 VAL A O 1 ATOM 3446 C CB . VAL A 1 434 ? -26.015 -33.122 -11.067 1.00 25.72 ? 436 VAL A CB 1 ATOM 3447 C CG1 . VAL A 1 434 ? -25.942 -32.025 -12.151 1.00 22.60 ? 436 VAL A CG1 1 ATOM 3448 C CG2 . VAL A 1 434 ? -27.051 -32.760 -9.923 1.00 23.69 ? 436 VAL A CG2 1 ATOM 3449 N N . MET A 1 435 ? -25.665 -35.710 -13.682 1.00 24.53 ? 437 MET A N 1 ATOM 3450 C CA . MET A 1 435 ? -24.702 -36.464 -14.420 1.00 24.21 ? 437 MET A CA 1 ATOM 3451 C C . MET A 1 435 ? -23.957 -35.587 -15.403 1.00 24.09 ? 437 MET A C 1 ATOM 3452 O O . MET A 1 435 ? -24.450 -34.559 -15.912 1.00 23.66 ? 437 MET A O 1 ATOM 3453 C CB . MET A 1 435 ? -25.425 -37.594 -15.203 1.00 24.72 ? 437 MET A CB 1 ATOM 3454 C CG . MET A 1 435 ? -25.975 -38.748 -14.343 1.00 24.30 ? 437 MET A CG 1 ATOM 3455 S SD . MET A 1 435 ? -26.997 -39.888 -15.322 1.00 32.16 ? 437 MET A SD 1 ATOM 3456 C CE . MET A 1 435 ? -25.855 -40.510 -16.576 1.00 24.99 ? 437 MET A CE 1 ATOM 3457 N N . HIS A 1 436 ? -22.820 -36.118 -15.785 1.00 25.11 ? 438 HIS A N 1 ATOM 3458 C CA . HIS A 1 436 ? -22.087 -35.698 -16.932 1.00 25.42 ? 438 HIS A CA 1 ATOM 3459 C C . HIS A 1 436 ? -22.955 -35.617 -18.165 1.00 26.21 ? 438 HIS A C 1 ATOM 3460 O O . HIS A 1 436 ? -23.667 -36.588 -18.456 1.00 26.58 ? 438 HIS A O 1 ATOM 3461 C CB . HIS A 1 436 ? -21.019 -36.731 -17.156 1.00 25.26 ? 438 HIS A CB 1 ATOM 3462 C CG . HIS A 1 436 ? -20.124 -36.411 -18.308 1.00 28.41 ? 438 HIS A CG 1 ATOM 3463 N ND1 . HIS A 1 436 ? -19.103 -35.489 -18.219 1.00 24.02 ? 438 HIS A ND1 1 ATOM 3464 C CD2 . HIS A 1 436 ? -20.059 -36.933 -19.563 1.00 31.76 ? 438 HIS A CD2 1 ATOM 3465 C CE1 . HIS A 1 436 ? -18.454 -35.443 -19.374 1.00 26.39 ? 438 HIS A CE1 1 ATOM 3466 N NE2 . HIS A 1 436 ? -19.004 -36.315 -20.204 1.00 31.22 ? 438 HIS A NE2 1 ATOM 3467 N N . GLY A 1 437 ? -22.902 -34.460 -18.862 1.00 25.03 ? 439 GLY A N 1 ATOM 3468 C CA . GLY A 1 437 ? -23.648 -34.204 -20.114 1.00 23.39 ? 439 GLY A CA 1 ATOM 3469 C C . GLY A 1 437 ? -25.016 -33.573 -19.985 1.00 24.48 ? 439 GLY A C 1 ATOM 3470 O O . GLY A 1 437 ? -25.604 -33.206 -20.988 1.00 24.23 ? 439 GLY A O 1 ATOM 3471 N N . TYR A 1 438 ? -25.540 -33.445 -18.756 1.00 25.37 ? 440 TYR A N 1 ATOM 3472 C CA . TYR A 1 438 ? -26.946 -33.097 -18.527 1.00 24.67 ? 440 TYR A CA 1 ATOM 3473 C C . TYR A 1 438 ? -27.140 -31.633 -18.139 1.00 25.91 ? 440 TYR A C 1 ATOM 3474 O O . TYR A 1 438 ? -28.212 -31.273 -17.612 1.00 27.07 ? 440 TYR A O 1 ATOM 3475 C CB . TYR A 1 438 ? -27.627 -34.122 -17.551 1.00 25.50 ? 440 TYR A CB 1 ATOM 3476 C CG . TYR A 1 438 ? -27.851 -35.443 -18.343 1.00 26.47 ? 440 TYR A CG 1 ATOM 3477 C CD1 . TYR A 1 438 ? -26.887 -36.469 -18.339 1.00 25.37 ? 440 TYR A CD1 1 ATOM 3478 C CD2 . TYR A 1 438 ? -28.971 -35.595 -19.180 1.00 28.29 ? 440 TYR A CD2 1 ATOM 3479 C CE1 . TYR A 1 438 ? -27.021 -37.655 -19.146 1.00 22.59 ? 440 TYR A CE1 1 ATOM 3480 C CE2 . TYR A 1 438 ? -29.146 -36.752 -19.975 1.00 26.19 ? 440 TYR A CE2 1 ATOM 3481 C CZ . TYR A 1 438 ? -28.183 -37.767 -19.958 1.00 28.51 ? 440 TYR A CZ 1 ATOM 3482 O OH . TYR A 1 438 ? -28.397 -38.863 -20.749 1.00 27.63 ? 440 TYR A OH 1 ATOM 3483 N N . GLU A 1 439 ? -26.098 -30.799 -18.366 1.00 24.90 ? 441 GLU A N 1 ATOM 3484 C CA . GLU A 1 439 ? -26.284 -29.333 -18.394 1.00 24.37 ? 441 GLU A CA 1 ATOM 3485 C C . GLU A 1 439 ? -26.546 -28.850 -19.822 1.00 24.50 ? 441 GLU A C 1 ATOM 3486 O O . GLU A 1 439 ? -27.018 -27.724 -20.041 1.00 25.04 ? 441 GLU A O 1 ATOM 3487 C CB . GLU A 1 439 ? -25.033 -28.604 -17.822 1.00 24.37 ? 441 GLU A CB 1 ATOM 3488 C CG . GLU A 1 439 ? -23.881 -28.255 -18.816 1.00 20.45 ? 441 GLU A CG 1 ATOM 3489 C CD . GLU A 1 439 ? -23.126 -29.519 -19.335 1.00 26.33 ? 441 GLU A CD 1 ATOM 3490 O OE1 . GLU A 1 439 ? -23.350 -30.658 -18.804 1.00 22.77 ? 441 GLU A OE1 1 ATOM 3491 O OE2 . GLU A 1 439 ? -22.311 -29.345 -20.299 1.00 22.14 ? 441 GLU A OE2 1 ATOM 3492 N N . ILE A 1 440 ? -26.143 -29.675 -20.783 1.00 23.30 ? 442 ILE A N 1 ATOM 3493 C CA . ILE A 1 440 ? -26.154 -29.292 -22.178 1.00 23.60 ? 442 ILE A CA 1 ATOM 3494 C C . ILE A 1 440 ? -27.517 -28.795 -22.649 1.00 24.79 ? 442 ILE A C 1 ATOM 3495 O O . ILE A 1 440 ? -27.594 -27.752 -23.289 1.00 26.40 ? 442 ILE A O 1 ATOM 3496 C CB . ILE A 1 440 ? -25.612 -30.449 -23.088 1.00 23.72 ? 442 ILE A CB 1 ATOM 3497 C CG1 . ILE A 1 440 ? -24.129 -30.745 -22.756 1.00 21.27 ? 442 ILE A CG1 1 ATOM 3498 C CG2 . ILE A 1 440 ? -25.813 -30.040 -24.571 1.00 23.67 ? 442 ILE A CG2 1 ATOM 3499 C CD1 . ILE A 1 440 ? -23.602 -32.023 -23.436 1.00 18.79 ? 442 ILE A CD1 1 ATOM 3500 N N . GLU A 1 441 ? -28.577 -29.568 -22.363 1.00 25.83 ? 443 GLU A N 1 ATOM 3501 C CA . GLU A 1 441 ? -29.932 -29.186 -22.708 1.00 27.64 ? 443 GLU A CA 1 ATOM 3502 C C . GLU A 1 441 ? -30.332 -27.841 -22.047 1.00 27.69 ? 443 GLU A C 1 ATOM 3503 O O . GLU A 1 441 ? -31.061 -27.057 -22.640 1.00 29.56 ? 443 GLU A O 1 ATOM 3504 C CB . GLU A 1 441 ? -30.910 -30.326 -22.388 1.00 28.39 ? 443 GLU A CB 1 ATOM 3505 C CG . GLU A 1 441 ? -30.988 -30.758 -20.913 1.00 31.97 ? 443 GLU A CG 1 ATOM 3506 C CD . GLU A 1 441 ? -31.491 -32.208 -20.756 1.00 36.11 ? 443 GLU A CD 1 ATOM 3507 O OE1 . GLU A 1 441 ? -30.670 -33.160 -20.897 1.00 34.78 ? 443 GLU A OE1 1 ATOM 3508 O OE2 . GLU A 1 441 ? -32.723 -32.382 -20.524 1.00 38.89 ? 443 GLU A OE2 1 ATOM 3509 N N . PHE A 1 442 ? -29.814 -27.538 -20.858 1.00 27.28 ? 444 PHE A N 1 ATOM 3510 C CA . PHE A 1 442 ? -30.043 -26.215 -20.234 1.00 26.52 ? 444 PHE A CA 1 ATOM 3511 C C . PHE A 1 442 ? -29.327 -25.121 -20.986 1.00 26.22 ? 444 PHE A C 1 ATOM 3512 O O . PHE A 1 442 ? -29.938 -24.071 -21.276 1.00 25.19 ? 444 PHE A O 1 ATOM 3513 C CB . PHE A 1 442 ? -29.674 -26.220 -18.746 1.00 26.35 ? 444 PHE A CB 1 ATOM 3514 C CG . PHE A 1 442 ? -30.674 -26.977 -17.947 1.00 26.81 ? 444 PHE A CG 1 ATOM 3515 C CD1 . PHE A 1 442 ? -30.650 -28.365 -17.956 1.00 22.34 ? 444 PHE A CD1 1 ATOM 3516 C CD2 . PHE A 1 442 ? -31.763 -26.311 -17.350 1.00 24.29 ? 444 PHE A CD2 1 ATOM 3517 C CE1 . PHE A 1 442 ? -31.678 -29.098 -17.309 1.00 23.27 ? 444 PHE A CE1 1 ATOM 3518 C CE2 . PHE A 1 442 ? -32.757 -27.024 -16.733 1.00 27.26 ? 444 PHE A CE2 1 ATOM 3519 C CZ . PHE A 1 442 ? -32.713 -28.417 -16.693 1.00 25.00 ? 444 PHE A CZ 1 ATOM 3520 N N . VAL A 1 443 ? -28.058 -25.359 -21.333 1.00 24.81 ? 445 VAL A N 1 ATOM 3521 C CA . VAL A 1 443 ? -27.287 -24.389 -22.169 1.00 23.74 ? 445 VAL A CA 1 ATOM 3522 C C . VAL A 1 443 ? -27.950 -24.080 -23.545 1.00 25.00 ? 445 VAL A C 1 ATOM 3523 O O . VAL A 1 443 ? -27.908 -22.915 -23.955 1.00 25.32 ? 445 VAL A O 1 ATOM 3524 C CB . VAL A 1 443 ? -25.793 -24.877 -22.371 1.00 24.71 ? 445 VAL A CB 1 ATOM 3525 C CG1 . VAL A 1 443 ? -25.094 -24.041 -23.447 1.00 19.96 ? 445 VAL A CG1 1 ATOM 3526 C CG2 . VAL A 1 443 ? -25.021 -24.837 -21.013 1.00 22.16 ? 445 VAL A CG2 1 ATOM 3527 N N . PHE A 1 444 ? -28.556 -25.100 -24.237 1.00 24.54 ? 446 PHE A N 1 ATOM 3528 C CA . PHE A 1 444 ? -29.133 -24.908 -25.584 1.00 24.26 ? 446 PHE A CA 1 ATOM 3529 C C . PHE A 1 444 ? -30.587 -24.465 -25.516 1.00 26.38 ? 446 PHE A C 1 ATOM 3530 O O . PHE A 1 444 ? -31.260 -24.196 -26.557 1.00 27.16 ? 446 PHE A O 1 ATOM 3531 C CB . PHE A 1 444 ? -28.967 -26.124 -26.520 1.00 22.76 ? 446 PHE A CB 1 ATOM 3532 C CG . PHE A 1 444 ? -27.600 -26.226 -27.161 1.00 22.90 ? 446 PHE A CG 1 ATOM 3533 C CD1 . PHE A 1 444 ? -26.524 -26.836 -26.474 1.00 19.57 ? 446 PHE A CD1 1 ATOM 3534 C CD2 . PHE A 1 444 ? -27.404 -25.779 -28.440 1.00 20.50 ? 446 PHE A CD2 1 ATOM 3535 C CE1 . PHE A 1 444 ? -25.243 -26.940 -27.052 1.00 21.76 ? 446 PHE A CE1 1 ATOM 3536 C CE2 . PHE A 1 444 ? -26.154 -25.853 -29.037 1.00 24.47 ? 446 PHE A CE2 1 ATOM 3537 C CZ . PHE A 1 444 ? -25.034 -26.448 -28.336 1.00 21.16 ? 446 PHE A CZ 1 ATOM 3538 N N . GLY A 1 445 ? -31.081 -24.374 -24.280 1.00 27.80 ? 447 GLY A N 1 ATOM 3539 C CA . GLY A 1 445 ? -32.387 -23.757 -24.044 1.00 28.56 ? 447 GLY A CA 1 ATOM 3540 C C . GLY A 1 445 ? -33.565 -24.667 -24.357 1.00 30.40 ? 447 GLY A C 1 ATOM 3541 O O . GLY A 1 445 ? -34.672 -24.188 -24.677 1.00 31.04 ? 447 GLY A O 1 ATOM 3542 N N . LEU A 1 446 ? -33.360 -25.976 -24.238 1.00 29.63 ? 448 LEU A N 1 ATOM 3543 C CA . LEU A 1 446 ? -34.467 -26.842 -24.487 1.00 31.89 ? 448 LEU A CA 1 ATOM 3544 C C . LEU A 1 446 ? -35.598 -26.651 -23.481 1.00 32.64 ? 448 LEU A C 1 ATOM 3545 O O . LEU A 1 446 ? -36.760 -26.783 -23.871 1.00 33.94 ? 448 LEU A O 1 ATOM 3546 C CB . LEU A 1 446 ? -34.121 -28.343 -24.656 1.00 30.84 ? 448 LEU A CB 1 ATOM 3547 C CG . LEU A 1 446 ? -33.031 -28.962 -25.548 1.00 31.95 ? 448 LEU A CG 1 ATOM 3548 C CD1 . LEU A 1 446 ? -33.456 -30.357 -26.040 1.00 28.88 ? 448 LEU A CD1 1 ATOM 3549 C CD2 . LEU A 1 446 ? -32.398 -28.110 -26.656 1.00 28.57 ? 448 LEU A CD2 1 ATOM 3550 N N . PRO A 1 447 ? -35.283 -26.334 -22.206 1.00 32.58 ? 449 PRO A N 1 ATOM 3551 C CA . PRO A 1 447 ? -36.465 -26.153 -21.296 1.00 34.07 ? 449 PRO A CA 1 ATOM 3552 C C . PRO A 1 447 ? -37.267 -24.885 -21.567 1.00 34.74 ? 449 PRO A C 1 ATOM 3553 O O . PRO A 1 447 ? -38.313 -24.677 -20.934 1.00 35.07 ? 449 PRO A O 1 ATOM 3554 C CB . PRO A 1 447 ? -35.861 -26.123 -19.891 1.00 32.85 ? 449 PRO A CB 1 ATOM 3555 C CG . PRO A 1 447 ? -34.480 -26.873 -20.077 1.00 33.73 ? 449 PRO A CG 1 ATOM 3556 C CD . PRO A 1 447 ? -34.024 -26.483 -21.471 1.00 29.81 ? 449 PRO A CD 1 ATOM 3557 N N . LEU A 1 448 ? -36.807 -24.042 -22.490 1.00 35.44 ? 450 LEU A N 1 ATOM 3558 C CA . LEU A 1 448 ? -37.625 -22.851 -22.855 1.00 37.85 ? 450 LEU A CA 1 ATOM 3559 C C . LEU A 1 448 ? -38.884 -23.285 -23.617 1.00 41.42 ? 450 LEU A C 1 ATOM 3560 O O . LEU A 1 448 ? -39.900 -22.544 -23.671 1.00 44.11 ? 450 LEU A O 1 ATOM 3561 C CB . LEU A 1 448 ? -36.833 -21.796 -23.601 1.00 34.16 ? 450 LEU A CB 1 ATOM 3562 C CG . LEU A 1 448 ? -35.504 -21.399 -22.896 1.00 35.67 ? 450 LEU A CG 1 ATOM 3563 C CD1 . LEU A 1 448 ? -34.604 -20.460 -23.746 1.00 26.63 ? 450 LEU A CD1 1 ATOM 3564 C CD2 . LEU A 1 448 ? -35.772 -20.817 -21.485 1.00 34.86 ? 450 LEU A CD2 1 ATOM 3565 N N . GLU A 1 449 ? -38.837 -24.480 -24.198 1.00 43.76 ? 451 GLU A N 1 ATOM 3566 C CA . GLU A 1 449 ? -40.004 -24.998 -24.901 1.00 48.36 ? 451 GLU A CA 1 ATOM 3567 C C . GLU A 1 449 ? -40.993 -25.543 -23.863 1.00 51.11 ? 451 GLU A C 1 ATOM 3568 O O . GLU A 1 449 ? -40.823 -26.652 -23.352 1.00 50.80 ? 451 GLU A O 1 ATOM 3569 C CB . GLU A 1 449 ? -39.592 -26.076 -25.924 1.00 48.29 ? 451 GLU A CB 1 ATOM 3570 C CG . GLU A 1 449 ? -40.762 -26.752 -26.716 1.00 51.03 ? 451 GLU A CG 1 ATOM 3571 C CD . GLU A 1 449 ? -41.378 -25.851 -27.791 0.50 51.12 ? 451 GLU A CD 1 ATOM 3572 O OE1 . GLU A 1 449 ? -42.421 -25.209 -27.516 0.50 49.89 ? 451 GLU A OE1 1 ATOM 3573 O OE2 . GLU A 1 449 ? -40.799 -25.790 -28.903 0.50 51.81 ? 451 GLU A OE2 1 ATOM 3574 N N . ARG A 1 450 ? -42.001 -24.743 -23.543 1.00 55.44 ? 452 ARG A N 1 ATOM 3575 C CA . ARG A 1 450 ? -43.087 -25.149 -22.628 1.00 60.34 ? 452 ARG A CA 1 ATOM 3576 C C . ARG A 1 450 ? -43.800 -26.499 -23.017 1.00 61.53 ? 452 ARG A C 1 ATOM 3577 O O . ARG A 1 450 ? -44.190 -27.290 -22.131 1.00 62.19 ? 452 ARG A O 1 ATOM 3578 C CB . ARG A 1 450 ? -44.105 -24.002 -22.449 1.00 62.08 ? 452 ARG A CB 1 ATOM 3579 C CG . ARG A 1 450 ? -44.975 -24.116 -21.162 1.00 68.91 ? 452 ARG A CG 1 ATOM 3580 C CD . ARG A 1 450 ? -46.002 -22.934 -20.955 1.00 76.16 ? 452 ARG A CD 1 ATOM 3581 N NE . ARG A 1 450 ? -47.278 -23.115 -21.662 1.00 82.82 ? 452 ARG A NE 1 ATOM 3582 C CZ . ARG A 1 450 ? -47.778 -22.291 -22.601 1.00 86.98 ? 452 ARG A CZ 1 ATOM 3583 N NH1 . ARG A 1 450 ? -47.121 -21.189 -22.991 1.00 86.51 ? 452 ARG A NH1 1 ATOM 3584 N NH2 . ARG A 1 450 ? -48.963 -22.565 -23.148 1.00 88.92 ? 452 ARG A NH2 1 ATOM 3585 N N . ARG A 1 451 ? -43.894 -26.794 -24.317 1.00 61.91 ? 453 ARG A N 1 ATOM 3586 C CA . ARG A 1 451 ? -44.482 -28.069 -24.757 1.00 62.78 ? 453 ARG A CA 1 ATOM 3587 C C . ARG A 1 451 ? -43.754 -29.346 -24.275 1.00 61.97 ? 453 ARG A C 1 ATOM 3588 O O . ARG A 1 451 ? -44.346 -30.443 -24.314 1.00 62.51 ? 453 ARG A O 1 ATOM 3589 C CB . ARG A 1 451 ? -44.744 -28.056 -26.283 1.00 63.76 ? 453 ARG A CB 1 ATOM 3590 C CG . ARG A 1 451 ? -45.964 -27.192 -26.617 0.50 64.69 ? 453 ARG A CG 1 ATOM 3591 C CD . ARG A 1 451 ? -45.902 -26.490 -27.950 0.50 64.86 ? 453 ARG A CD 1 ATOM 3592 N NE . ARG A 1 451 ? -47.271 -26.250 -28.405 0.50 68.56 ? 453 ARG A NE 1 ATOM 3593 C CZ . ARG A 1 451 ? -48.319 -26.964 -27.981 0.50 70.25 ? 453 ARG A CZ 1 ATOM 3594 N NH1 . ARG A 1 451 ? -48.138 -27.954 -27.111 0.50 69.43 ? 453 ARG A NH1 1 ATOM 3595 N NH2 . ARG A 1 451 ? -49.542 -26.707 -28.426 0.50 70.55 ? 453 ARG A NH2 1 ATOM 3596 N N . ASP A 1 452 ? -42.514 -29.181 -23.777 1.00 59.78 ? 454 ASP A N 1 ATOM 3597 C CA . ASP A 1 452 ? -41.591 -30.289 -23.437 1.00 58.59 ? 454 ASP A CA 1 ATOM 3598 C C . ASP A 1 452 ? -41.652 -30.943 -22.011 1.00 57.78 ? 454 ASP A C 1 ATOM 3599 O O . ASP A 1 452 ? -40.873 -31.879 -21.734 1.00 58.58 ? 454 ASP A O 1 ATOM 3600 C CB . ASP A 1 452 ? -40.120 -29.911 -23.782 1.00 56.79 ? 454 ASP A CB 1 ATOM 3601 C CG . ASP A 1 452 ? -39.502 -30.795 -24.866 0.50 56.45 ? 454 ASP A CG 1 ATOM 3602 O OD1 . ASP A 1 452 ? -40.193 -31.165 -25.838 0.50 60.03 ? 454 ASP A OD1 1 ATOM 3603 O OD2 . ASP A 1 452 ? -38.297 -31.092 -24.768 0.50 55.86 ? 454 ASP A OD2 1 ATOM 3604 N N . GLN A 1 453 ? -42.541 -30.487 -21.124 1.00 57.70 ? 455 GLN A N 1 ATOM 3605 C CA A GLN A 1 453 ? -42.688 -31.116 -19.799 0.50 56.19 ? 455 GLN A CA 1 ATOM 3606 C CA B GLN A 1 453 ? -42.707 -31.092 -19.772 0.50 56.74 ? 455 GLN A CA 1 ATOM 3607 C C . GLN A 1 453 ? -41.491 -30.950 -18.819 1.00 54.11 ? 455 GLN A C 1 ATOM 3608 O O . GLN A 1 453 ? -41.388 -31.702 -17.837 1.00 55.04 ? 455 GLN A O 1 ATOM 3609 C CB A GLN A 1 453 ? -43.079 -32.580 -19.781 0.50 92.29 ? 455 GLN A CB 1 ATOM 3610 C CB B GLN A 1 453 ? -43.123 -32.581 -19.795 0.50 57.76 ? 455 GLN A CB 1 ATOM 3611 C CG A GLN A 1 453 ? -44.572 -32.813 -19.603 0.50 90.92 ? 455 GLN A CG 1 ATOM 3612 C CG B GLN A 1 453 ? -44.081 -33.056 -20.893 0.50 61.08 ? 455 GLN A CG 1 ATOM 3613 C CD A GLN A 1 453 ? -45.382 -32.428 -20.824 0.50 90.97 ? 455 GLN A CD 1 ATOM 3614 C CD B GLN A 1 453 ? -43.404 -34.079 -21.796 0.50 61.32 ? 455 GLN A CD 1 ATOM 3615 O OE1 A GLN A 1 453 ? -44.830 -32.110 -21.876 0.50 92.61 ? 455 GLN A OE1 1 ATOM 3616 O OE1 B GLN A 1 453 ? -43.130 -33.810 -22.969 0.50 61.74 ? 455 GLN A OE1 1 ATOM 3617 N NE2 A GLN A 1 453 ? -47.166 -32.016 -19.564 0.50 34.24 ? 455 GLN A NE2 1 ATOM 3618 N NE2 B GLN A 1 453 ? -43.095 -35.246 -21.234 0.50 59.42 ? 455 GLN A NE2 1 ATOM 3619 N N . TYR A 1 454 ? -40.571 -30.007 -19.081 1.00 48.63 ? 456 TYR A N 1 ATOM 3620 C CA . TYR A 1 454 ? -39.677 -29.544 -17.997 1.00 43.89 ? 456 TYR A CA 1 ATOM 3621 C C . TYR A 1 454 ? -40.508 -28.685 -17.006 1.00 43.65 ? 456 TYR A C 1 ATOM 3622 O O . TYR A 1 454 ? -41.546 -28.141 -17.386 1.00 43.23 ? 456 TYR A O 1 ATOM 3623 C CB . TYR A 1 454 ? -38.571 -28.670 -18.541 1.00 40.75 ? 456 TYR A CB 1 ATOM 3624 C CG . TYR A 1 454 ? -37.554 -29.369 -19.391 1.00 36.95 ? 456 TYR A CG 1 ATOM 3625 C CD1 . TYR A 1 454 ? -37.653 -29.375 -20.784 1.00 37.19 ? 456 TYR A CD1 1 ATOM 3626 C CD2 . TYR A 1 454 ? -36.471 -30.012 -18.809 1.00 32.66 ? 456 TYR A CD2 1 ATOM 3627 C CE1 . TYR A 1 454 ? -36.673 -30.009 -21.597 1.00 36.43 ? 456 TYR A CE1 1 ATOM 3628 C CE2 . TYR A 1 454 ? -35.468 -30.639 -19.612 1.00 36.41 ? 456 TYR A CE2 1 ATOM 3629 C CZ . TYR A 1 454 ? -35.567 -30.620 -20.997 1.00 36.66 ? 456 TYR A CZ 1 ATOM 3630 O OH . TYR A 1 454 ? -34.562 -31.231 -21.750 1.00 36.71 ? 456 TYR A OH 1 ATOM 3631 N N . THR A 1 455 ? -40.064 -28.553 -15.754 1.00 41.77 ? 457 THR A N 1 ATOM 3632 C CA . THR A 1 455 ? -40.819 -27.749 -14.763 1.00 40.59 ? 457 THR A CA 1 ATOM 3633 C C . THR A 1 455 ? -40.612 -26.267 -15.092 1.00 40.71 ? 457 THR A C 1 ATOM 3634 O O . THR A 1 455 ? -39.765 -25.898 -15.891 1.00 38.47 ? 457 THR A O 1 ATOM 3635 C CB . THR A 1 455 ? -40.324 -27.950 -13.300 1.00 39.87 ? 457 THR A CB 1 ATOM 3636 O OG1 . THR A 1 455 ? -38.956 -27.522 -13.193 1.00 36.59 ? 457 THR A OG1 1 ATOM 3637 C CG2 . THR A 1 455 ? -40.440 -29.410 -12.836 1.00 37.12 ? 457 THR A CG2 1 ATOM 3638 N N . LYS A 1 456 ? -41.391 -25.421 -14.457 1.00 41.07 ? 458 LYS A N 1 ATOM 3639 C CA . LYS A 1 456 ? -41.246 -23.974 -14.577 1.00 42.14 ? 458 LYS A CA 1 ATOM 3640 C C . LYS A 1 456 ? -39.885 -23.467 -13.980 1.00 39.47 ? 458 LYS A C 1 ATOM 3641 O O . LYS A 1 456 ? -39.190 -22.582 -14.543 1.00 39.97 ? 458 LYS A O 1 ATOM 3642 C CB . LYS A 1 456 ? -42.554 -23.312 -13.962 1.00 43.98 ? 458 LYS A CB 1 ATOM 3643 C CG . LYS A 1 456 ? -42.582 -21.814 -14.019 1.00 49.38 ? 458 LYS A CG 1 ATOM 3644 C CD . LYS A 1 456 ? -43.210 -21.280 -15.307 1.00 56.47 ? 458 LYS A CD 1 ATOM 3645 C CE . LYS A 1 456 ? -42.572 -19.892 -15.595 1.00 61.79 ? 458 LYS A CE 1 ATOM 3646 N NZ . LYS A 1 456 ? -43.004 -19.241 -16.892 1.00 63.96 ? 458 LYS A NZ 1 ATOM 3647 N N . ALA A 1 457 ? -39.433 -24.072 -12.887 1.00 37.93 ? 459 ALA A N 1 ATOM 3648 C CA . ALA A 1 457 ? -38.186 -23.645 -12.312 1.00 35.87 ? 459 ALA A CA 1 ATOM 3649 C C . ALA A 1 457 ? -37.061 -23.927 -13.311 1.00 35.02 ? 459 ALA A C 1 ATOM 3650 O O . ALA A 1 457 ? -36.100 -23.204 -13.332 1.00 34.83 ? 459 ALA A O 1 ATOM 3651 C CB . ALA A 1 457 ? -37.917 -24.305 -10.954 1.00 34.29 ? 459 ALA A CB 1 ATOM 3652 N N . GLU A 1 458 ? -37.208 -24.949 -14.141 1.00 34.14 ? 460 GLU A N 1 ATOM 3653 C CA . GLU A 1 458 ? -36.178 -25.334 -15.114 1.00 32.95 ? 460 GLU A CA 1 ATOM 3654 C C . GLU A 1 458 ? -36.180 -24.398 -16.317 1.00 32.93 ? 460 GLU A C 1 ATOM 3655 O O . GLU A 1 458 ? -35.151 -24.033 -16.829 1.00 31.31 ? 460 GLU A O 1 ATOM 3656 C CB . GLU A 1 458 ? -36.449 -26.793 -15.558 1.00 33.28 ? 460 GLU A CB 1 ATOM 3657 C CG . GLU A 1 458 ? -35.875 -27.800 -14.482 1.00 33.91 ? 460 GLU A CG 1 ATOM 3658 C CD . GLU A 1 458 ? -36.203 -29.277 -14.771 1.00 35.67 ? 460 GLU A CD 1 ATOM 3659 O OE1 . GLU A 1 458 ? -37.230 -29.518 -15.406 1.00 36.75 ? 460 GLU A OE1 1 ATOM 3660 O OE2 . GLU A 1 458 ? -35.442 -30.193 -14.337 1.00 37.25 ? 460 GLU A OE2 1 ATOM 3661 N N . GLU A 1 459 ? -37.362 -23.995 -16.759 1.00 34.63 ? 461 GLU A N 1 ATOM 3662 C CA . GLU A 1 459 ? -37.468 -23.012 -17.776 1.00 35.74 ? 461 GLU A CA 1 ATOM 3663 C C . GLU A 1 459 ? -36.697 -21.731 -17.356 1.00 35.10 ? 461 GLU A C 1 ATOM 3664 O O . GLU A 1 459 ? -35.944 -21.154 -18.135 1.00 36.32 ? 461 GLU A O 1 ATOM 3665 C CB . GLU A 1 459 ? -38.950 -22.725 -17.995 1.00 36.00 ? 461 GLU A CB 1 ATOM 3666 C CG . GLU A 1 459 ? -39.150 -21.598 -18.989 1.00 43.06 ? 461 GLU A CG 1 ATOM 3667 C CD . GLU A 1 459 ? -40.592 -21.010 -19.072 1.00 49.82 ? 461 GLU A CD 1 ATOM 3668 O OE1 . GLU A 1 459 ? -40.750 -20.004 -19.770 1.00 49.82 ? 461 GLU A OE1 1 ATOM 3669 O OE2 . GLU A 1 459 ? -41.543 -21.534 -18.461 1.00 54.51 ? 461 GLU A OE2 1 ATOM 3670 N N . ILE A 1 460 ? -36.872 -21.303 -16.116 1.00 36.28 ? 462 ILE A N 1 ATOM 3671 C CA . ILE A 1 460 ? -36.187 -20.122 -15.555 1.00 36.60 ? 462 ILE A CA 1 ATOM 3672 C C . ILE A 1 460 ? -34.649 -20.315 -15.422 1.00 34.58 ? 462 ILE A C 1 ATOM 3673 O O . ILE A 1 460 ? -33.892 -19.394 -15.728 1.00 33.74 ? 462 ILE A O 1 ATOM 3674 C CB . ILE A 1 460 ? -36.851 -19.689 -14.155 1.00 39.49 ? 462 ILE A CB 1 ATOM 3675 C CG1 . ILE A 1 460 ? -38.354 -19.308 -14.285 1.00 42.11 ? 462 ILE A CG1 1 ATOM 3676 C CG2 . ILE A 1 460 ? -36.181 -18.495 -13.502 1.00 39.68 ? 462 ILE A CG2 1 ATOM 3677 C CD1 . ILE A 1 460 ? -38.621 -18.068 -15.171 1.00 47.70 ? 462 ILE A CD1 1 ATOM 3678 N N . LEU A 1 461 ? -34.195 -21.506 -14.983 1.00 31.88 ? 463 LEU A N 1 ATOM 3679 C CA . LEU A 1 461 ? -32.802 -21.769 -14.842 1.00 30.30 ? 463 LEU A CA 1 ATOM 3680 C C . LEU A 1 461 ? -32.184 -21.721 -16.250 1.00 29.79 ? 463 LEU A C 1 ATOM 3681 O O . LEU A 1 461 ? -31.144 -21.085 -16.446 1.00 28.94 ? 463 LEU A O 1 ATOM 3682 C CB . LEU A 1 461 ? -32.566 -23.160 -14.214 1.00 30.13 ? 463 LEU A CB 1 ATOM 3683 C CG . LEU A 1 461 ? -31.093 -23.578 -14.171 1.00 27.49 ? 463 LEU A CG 1 ATOM 3684 C CD1 . LEU A 1 461 ? -30.161 -22.549 -13.424 1.00 27.46 ? 463 LEU A CD1 1 ATOM 3685 C CD2 . LEU A 1 461 ? -30.951 -25.029 -13.552 1.00 26.71 ? 463 LEU A CD2 1 ATOM 3686 N N . SER A 1 462 ? -32.881 -22.302 -17.234 1.00 28.35 ? 464 SER A N 1 ATOM 3687 C CA . SER A 1 462 ? -32.312 -22.361 -18.566 1.00 28.26 ? 464 SER A CA 1 ATOM 3688 C C . SER A 1 462 ? -32.212 -20.945 -19.195 1.00 28.68 ? 464 SER A C 1 ATOM 3689 O O . SER A 1 462 ? -31.210 -20.574 -19.829 1.00 27.77 ? 464 SER A O 1 ATOM 3690 C CB . SER A 1 462 ? -33.197 -23.267 -19.454 1.00 28.00 ? 464 SER A CB 1 ATOM 3691 O OG . SER A 1 462 ? -32.618 -23.371 -20.743 1.00 25.63 ? 464 SER A OG 1 ATOM 3692 N N . ARG A 1 463 ? -33.284 -20.185 -19.032 1.00 29.48 ? 465 ARG A N 1 ATOM 3693 C CA . ARG A 1 463 ? -33.328 -18.837 -19.564 1.00 31.62 ? 465 ARG A CA 1 ATOM 3694 C C . ARG A 1 463 ? -32.155 -18.010 -18.984 1.00 31.47 ? 465 ARG A C 1 ATOM 3695 O O . ARG A 1 463 ? -31.474 -17.232 -19.695 1.00 32.16 ? 465 ARG A O 1 ATOM 3696 C CB . ARG A 1 463 ? -34.698 -18.182 -19.202 1.00 32.07 ? 465 ARG A CB 1 ATOM 3697 C CG . ARG A 1 463 ? -34.790 -16.750 -19.653 1.00 34.30 ? 465 ARG A CG 1 ATOM 3698 C CD . ARG A 1 463 ? -35.011 -16.718 -21.138 1.00 37.47 ? 465 ARG A CD 1 ATOM 3699 N NE . ARG A 1 463 ? -34.728 -15.441 -21.823 1.00 37.51 ? 465 ARG A NE 1 ATOM 3700 C CZ . ARG A 1 463 ? -33.514 -15.072 -22.252 1.00 38.35 ? 465 ARG A CZ 1 ATOM 3701 N NH1 . ARG A 1 463 ? -32.405 -15.847 -22.018 1.00 24.92 ? 465 ARG A NH1 1 ATOM 3702 N NH2 . ARG A 1 463 ? -33.410 -13.927 -22.946 1.00 40.79 ? 465 ARG A NH2 1 ATOM 3703 N N . SER A 1 464 ? -31.903 -18.189 -17.698 1.00 30.35 ? 466 SER A N 1 ATOM 3704 C CA . SER A 1 464 ? -30.866 -17.420 -17.081 1.00 31.40 ? 466 SER A CA 1 ATOM 3705 C C . SER A 1 464 ? -29.443 -17.885 -17.597 1.00 29.55 ? 466 SER A C 1 ATOM 3706 O O . SER A 1 464 ? -28.565 -17.057 -17.907 1.00 30.60 ? 466 SER A O 1 ATOM 3707 C CB . SER A 1 464 ? -31.075 -17.524 -15.574 1.00 31.43 ? 466 SER A CB 1 ATOM 3708 O OG . SER A 1 464 ? -29.963 -17.062 -14.881 1.00 35.12 ? 466 SER A OG 1 ATOM 3709 N N . ILE A 1 465 ? -29.241 -19.191 -17.754 1.00 29.30 ? 467 ILE A N 1 ATOM 3710 C CA . ILE A 1 465 ? -27.945 -19.758 -18.242 1.00 27.88 ? 467 ILE A CA 1 ATOM 3711 C C . ILE A 1 465 ? -27.759 -19.324 -19.712 1.00 27.80 ? 467 ILE A C 1 ATOM 3712 O O . ILE A 1 465 ? -26.666 -18.912 -20.136 1.00 27.03 ? 467 ILE A O 1 ATOM 3713 C CB . ILE A 1 465 ? -27.951 -21.322 -18.125 1.00 28.58 ? 467 ILE A CB 1 ATOM 3714 C CG1 . ILE A 1 465 ? -27.821 -21.761 -16.640 1.00 29.73 ? 467 ILE A CG1 1 ATOM 3715 C CG2 . ILE A 1 465 ? -26.859 -22.016 -19.059 1.00 23.40 ? 467 ILE A CG2 1 ATOM 3716 C CD1 . ILE A 1 465 ? -28.067 -23.339 -16.391 1.00 23.20 ? 467 ILE A CD1 1 ATOM 3717 N N . VAL A 1 466 ? -28.840 -19.421 -20.482 1.00 26.72 ? 468 VAL A N 1 ATOM 3718 C CA . VAL A 1 466 ? -28.781 -18.941 -21.852 1.00 26.12 ? 468 VAL A CA 1 ATOM 3719 C C . VAL A 1 466 ? -28.334 -17.472 -21.927 1.00 26.31 ? 468 VAL A C 1 ATOM 3720 O O . VAL A 1 466 ? -27.450 -17.109 -22.725 1.00 24.95 ? 468 VAL A O 1 ATOM 3721 C CB . VAL A 1 466 ? -30.139 -19.151 -22.551 1.00 26.28 ? 468 VAL A CB 1 ATOM 3722 C CG1 . VAL A 1 466 ? -30.202 -18.334 -23.810 1.00 25.95 ? 468 VAL A CG1 1 ATOM 3723 C CG2 . VAL A 1 466 ? -30.317 -20.648 -22.834 1.00 23.05 ? 468 VAL A CG2 1 ATOM 3724 N N . LYS A 1 467 ? -28.907 -16.638 -21.070 1.00 25.78 ? 469 LYS A N 1 ATOM 3725 C CA . LYS A 1 467 ? -28.490 -15.239 -21.020 1.00 25.97 ? 469 LYS A CA 1 ATOM 3726 C C . LYS A 1 467 ? -27.034 -15.059 -20.545 1.00 25.92 ? 469 LYS A C 1 ATOM 3727 O O . LYS A 1 467 ? -26.243 -14.273 -21.132 1.00 27.23 ? 469 LYS A O 1 ATOM 3728 C CB . LYS A 1 467 ? -29.463 -14.436 -20.126 1.00 26.36 ? 469 LYS A CB 1 ATOM 3729 C CG . LYS A 1 467 ? -29.018 -12.978 -19.814 1.00 25.88 ? 469 LYS A CG 1 ATOM 3730 C CD . LYS A 1 467 ? -28.912 -12.185 -21.166 1.00 27.47 ? 469 LYS A CD 1 ATOM 3731 C CE . LYS A 1 467 ? -30.327 -11.875 -21.743 1.00 30.02 ? 469 LYS A CE 1 ATOM 3732 N NZ . LYS A 1 467 ? -30.173 -11.226 -23.076 1.00 29.07 ? 469 LYS A NZ 1 ATOM 3733 N N . ARG A 1 468 ? -26.636 -15.759 -19.491 1.00 26.46 ? 470 ARG A N 1 ATOM 3734 C CA . ARG A 1 468 ? -25.232 -15.648 -19.040 1.00 26.04 ? 470 ARG A CA 1 ATOM 3735 C C . ARG A 1 468 ? -24.229 -16.076 -20.159 1.00 26.77 ? 470 ARG A C 1 ATOM 3736 O O . ARG A 1 468 ? -23.181 -15.409 -20.370 1.00 26.24 ? 470 ARG A O 1 ATOM 3737 C CB . ARG A 1 468 ? -24.996 -16.471 -17.748 1.00 25.10 ? 470 ARG A CB 1 ATOM 3738 C CG . ARG A 1 468 ? -25.759 -15.976 -16.515 1.00 26.80 ? 470 ARG A CG 1 ATOM 3739 C CD . ARG A 1 468 ? -25.406 -16.801 -15.300 1.00 26.26 ? 470 ARG A CD 1 ATOM 3740 N NE . ARG A 1 468 ? -26.098 -16.387 -14.059 1.00 24.55 ? 470 ARG A NE 1 ATOM 3741 C CZ . ARG A 1 468 ? -25.719 -15.396 -13.254 1.00 27.45 ? 470 ARG A CZ 1 ATOM 3742 N NH1 . ARG A 1 468 ? -26.427 -15.137 -12.180 1.00 24.29 ? 470 ARG A NH1 1 ATOM 3743 N NH2 . ARG A 1 468 ? -24.650 -14.630 -13.511 1.00 27.09 ? 470 ARG A NH2 1 ATOM 3744 N N . TRP A 1 469 ? -24.521 -17.194 -20.849 1.00 26.33 ? 471 TRP A N 1 ATOM 3745 C CA . TRP A 1 469 ? -23.638 -17.705 -21.922 1.00 24.41 ? 471 TRP A CA 1 ATOM 3746 C C . TRP A 1 469 ? -23.532 -16.669 -23.043 1.00 25.17 ? 471 TRP A C 1 ATOM 3747 O O . TRP A 1 469 ? -22.426 -16.387 -23.566 1.00 25.15 ? 471 TRP A O 1 ATOM 3748 C CB . TRP A 1 469 ? -24.183 -19.054 -22.444 1.00 22.86 ? 471 TRP A CB 1 ATOM 3749 C CG . TRP A 1 469 ? -23.504 -20.356 -21.850 1.00 24.24 ? 471 TRP A CG 1 ATOM 3750 C CD1 . TRP A 1 469 ? -22.921 -21.401 -22.577 1.00 23.78 ? 471 TRP A CD1 1 ATOM 3751 C CD2 . TRP A 1 469 ? -23.294 -20.688 -20.451 1.00 22.95 ? 471 TRP A CD2 1 ATOM 3752 N NE1 . TRP A 1 469 ? -22.416 -22.354 -21.699 1.00 24.27 ? 471 TRP A NE1 1 ATOM 3753 C CE2 . TRP A 1 469 ? -22.617 -21.934 -20.406 1.00 20.34 ? 471 TRP A CE2 1 ATOM 3754 C CE3 . TRP A 1 469 ? -23.672 -20.069 -19.234 1.00 23.36 ? 471 TRP A CE3 1 ATOM 3755 C CZ2 . TRP A 1 469 ? -22.331 -22.580 -19.213 1.00 20.87 ? 471 TRP A CZ2 1 ATOM 3756 C CZ3 . TRP A 1 469 ? -23.402 -20.689 -18.064 1.00 22.46 ? 471 TRP A CZ3 1 ATOM 3757 C CH2 . TRP A 1 469 ? -22.691 -21.929 -18.037 1.00 23.82 ? 471 TRP A CH2 1 ATOM 3758 N N . ALA A 1 470 ? -24.683 -16.067 -23.400 1.00 24.99 ? 472 ALA A N 1 ATOM 3759 C CA . ALA A 1 470 ? -24.753 -15.113 -24.499 1.00 25.69 ? 472 ALA A CA 1 ATOM 3760 C C . ALA A 1 470 ? -24.043 -13.833 -24.078 1.00 25.27 ? 472 ALA A C 1 ATOM 3761 O O . ALA A 1 470 ? -23.263 -13.259 -24.842 1.00 25.88 ? 472 ALA A O 1 ATOM 3762 C CB . ALA A 1 470 ? -26.212 -14.791 -24.881 1.00 26.01 ? 472 ALA A CB 1 ATOM 3763 N N . ASN A 1 471 ? -24.304 -13.376 -22.874 1.00 24.45 ? 473 ASN A N 1 ATOM 3764 C CA . ASN A 1 471 ? -23.519 -12.224 -22.370 1.00 25.20 ? 473 ASN A CA 1 ATOM 3765 C C . ASN A 1 471 ? -22.016 -12.516 -22.327 1.00 25.43 ? 473 ASN A C 1 ATOM 3766 O O . ASN A 1 471 ? -21.207 -11.652 -22.715 1.00 26.35 ? 473 ASN A O 1 ATOM 3767 C CB . ASN A 1 471 ? -24.023 -11.716 -21.018 1.00 24.67 ? 473 ASN A CB 1 ATOM 3768 C CG . ASN A 1 471 ? -25.272 -10.820 -21.154 1.00 27.08 ? 473 ASN A CG 1 ATOM 3769 O OD1 . ASN A 1 471 ? -25.667 -10.411 -22.256 1.00 30.07 ? 473 ASN A OD1 1 ATOM 3770 N ND2 . ASN A 1 471 ? -25.914 -10.552 -20.036 1.00 25.81 ? 473 ASN A ND2 1 ATOM 3771 N N . PHE A 1 472 ? -21.628 -13.738 -21.944 1.00 23.75 ? 474 PHE A N 1 ATOM 3772 C CA . PHE A 1 472 ? -20.216 -14.093 -22.016 1.00 22.73 ? 474 PHE A CA 1 ATOM 3773 C C . PHE A 1 472 ? -19.712 -13.954 -23.454 1.00 23.50 ? 474 PHE A C 1 ATOM 3774 O O . PHE A 1 472 ? -18.735 -13.242 -23.710 1.00 23.95 ? 474 PHE A O 1 ATOM 3775 C CB . PHE A 1 472 ? -19.908 -15.513 -21.492 1.00 23.00 ? 474 PHE A CB 1 ATOM 3776 C CG . PHE A 1 472 ? -18.436 -15.809 -21.492 1.00 23.72 ? 474 PHE A CG 1 ATOM 3777 C CD1 . PHE A 1 472 ? -17.584 -15.144 -20.563 1.00 21.46 ? 474 PHE A CD1 1 ATOM 3778 C CD2 . PHE A 1 472 ? -17.895 -16.644 -22.440 1.00 20.29 ? 474 PHE A CD2 1 ATOM 3779 C CE1 . PHE A 1 472 ? -16.227 -15.403 -20.554 1.00 20.40 ? 474 PHE A CE1 1 ATOM 3780 C CE2 . PHE A 1 472 ? -16.519 -16.903 -22.447 1.00 20.99 ? 474 PHE A CE2 1 ATOM 3781 C CZ . PHE A 1 472 ? -15.694 -16.264 -21.526 1.00 22.95 ? 474 PHE A CZ 1 ATOM 3782 N N . ALA A 1 473 ? -20.412 -14.552 -24.418 1.00 22.64 ? 475 ALA A N 1 ATOM 3783 C CA . ALA A 1 473 ? -19.931 -14.507 -25.792 1.00 21.61 ? 475 ALA A CA 1 ATOM 3784 C C . ALA A 1 473 ? -19.855 -13.071 -26.337 1.00 23.05 ? 475 ALA A C 1 ATOM 3785 O O . ALA A 1 473 ? -18.817 -12.648 -26.949 1.00 22.54 ? 475 ALA A O 1 ATOM 3786 C CB . ALA A 1 473 ? -20.762 -15.380 -26.676 1.00 19.58 ? 475 ALA A CB 1 ATOM 3787 N N . LYS A 1 474 ? -20.923 -12.318 -26.142 1.00 24.20 ? 476 LYS A N 1 ATOM 3788 C CA . LYS A 1 474 ? -20.953 -10.925 -26.638 1.00 27.01 ? 476 LYS A CA 1 ATOM 3789 C C . LYS A 1 474 ? -19.985 -9.960 -25.888 1.00 27.68 ? 476 LYS A C 1 ATOM 3790 O O . LYS A 1 474 ? -19.348 -9.101 -26.507 1.00 28.96 ? 476 LYS A O 1 ATOM 3791 C CB . LYS A 1 474 ? -22.386 -10.363 -26.544 1.00 28.40 ? 476 LYS A CB 1 ATOM 3792 C CG . LYS A 1 474 ? -23.482 -11.150 -27.280 1.00 29.58 ? 476 LYS A CG 1 ATOM 3793 C CD . LYS A 1 474 ? -24.846 -10.456 -27.086 1.00 35.75 ? 476 LYS A CD 1 ATOM 3794 C CE . LYS A 1 474 ? -26.018 -11.231 -27.801 1.00 42.08 ? 476 LYS A CE 1 ATOM 3795 N NZ . LYS A 1 474 ? -27.376 -11.194 -27.059 1.00 41.87 ? 476 LYS A NZ 1 ATOM 3796 N N . TYR A 1 475 ? -19.878 -10.105 -24.568 1.00 26.82 ? 477 TYR A N 1 ATOM 3797 C CA . TYR A 1 475 ? -19.312 -9.021 -23.713 1.00 28.55 ? 477 TYR A CA 1 ATOM 3798 C C . TYR A 1 475 ? -18.194 -9.449 -22.783 1.00 28.12 ? 477 TYR A C 1 ATOM 3799 O O . TYR A 1 475 ? -17.659 -8.606 -22.062 1.00 28.67 ? 477 TYR A O 1 ATOM 3800 C CB . TYR A 1 475 ? -20.403 -8.375 -22.843 1.00 28.63 ? 477 TYR A CB 1 ATOM 3801 C CG . TYR A 1 475 ? -21.612 -7.978 -23.630 1.00 28.76 ? 477 TYR A CG 1 ATOM 3802 C CD1 . TYR A 1 475 ? -22.902 -8.401 -23.241 1.00 27.71 ? 477 TYR A CD1 1 ATOM 3803 C CD2 . TYR A 1 475 ? -21.480 -7.164 -24.748 1.00 28.48 ? 477 TYR A CD2 1 ATOM 3804 C CE1 . TYR A 1 475 ? -24.013 -8.086 -24.006 1.00 24.92 ? 477 TYR A CE1 1 ATOM 3805 C CE2 . TYR A 1 475 ? -22.601 -6.796 -25.487 1.00 30.24 ? 477 TYR A CE2 1 ATOM 3806 C CZ . TYR A 1 475 ? -23.846 -7.275 -25.129 1.00 28.42 ? 477 TYR A CZ 1 ATOM 3807 O OH . TYR A 1 475 ? -24.924 -6.917 -25.901 1.00 29.72 ? 477 TYR A OH 1 ATOM 3808 N N . GLY A 1 476 ? -17.885 -10.751 -22.811 1.00 27.50 ? 478 GLY A N 1 ATOM 3809 C CA . GLY A 1 476 ? -16.878 -11.387 -21.995 1.00 27.21 ? 478 GLY A CA 1 ATOM 3810 C C . GLY A 1 476 ? -17.210 -11.422 -20.517 1.00 27.35 ? 478 GLY A C 1 ATOM 3811 O O . GLY A 1 476 ? -16.286 -11.544 -19.706 1.00 28.78 ? 478 GLY A O 1 ATOM 3812 N N . ASN A 1 477 ? -18.493 -11.368 -20.159 1.00 25.37 ? 479 ASN A N 1 ATOM 3813 C CA . ASN A 1 477 ? -18.906 -11.252 -18.755 1.00 26.70 ? 479 ASN A CA 1 ATOM 3814 C C . ASN A 1 477 ? -20.241 -11.963 -18.527 1.00 25.66 ? 479 ASN A C 1 ATOM 3815 O O . ASN A 1 477 ? -21.252 -11.457 -18.944 1.00 29.23 ? 479 ASN A O 1 ATOM 3816 C CB . ASN A 1 477 ? -19.018 -9.756 -18.396 1.00 28.16 ? 479 ASN A CB 1 ATOM 3817 C CG . ASN A 1 477 ? -18.791 -9.457 -16.913 1.00 29.75 ? 479 ASN A CG 1 ATOM 3818 O OD1 . ASN A 1 477 ? -18.899 -10.329 -16.062 1.00 31.67 ? 479 ASN A OD1 1 ATOM 3819 N ND2 . ASN A 1 477 ? -18.480 -8.206 -16.612 1.00 32.32 ? 479 ASN A ND2 1 ATOM 3820 N N . PRO A 1 478 ? -20.260 -13.137 -17.861 1.00 24.28 ? 480 PRO A N 1 ATOM 3821 C CA . PRO A 1 478 ? -21.476 -14.005 -17.928 1.00 23.01 ? 480 PRO A CA 1 ATOM 3822 C C . PRO A 1 478 ? -22.459 -13.566 -16.841 1.00 24.93 ? 480 PRO A C 1 ATOM 3823 O O . PRO A 1 478 ? -22.848 -14.396 -15.994 1.00 23.41 ? 480 PRO A O 1 ATOM 3824 C CB . PRO A 1 478 ? -20.906 -15.419 -17.591 1.00 20.01 ? 480 PRO A CB 1 ATOM 3825 C CG . PRO A 1 478 ? -19.799 -15.098 -16.609 1.00 22.15 ? 480 PRO A CG 1 ATOM 3826 C CD . PRO A 1 478 ? -19.151 -13.804 -17.112 1.00 22.11 ? 480 PRO A CD 1 ATOM 3827 N N . GLN A 1 479 ? -22.822 -12.271 -16.829 1.00 26.59 ? 481 GLN A N 1 ATOM 3828 C CA . GLN A 1 479 ? -23.823 -11.732 -15.859 1.00 28.15 ? 481 GLN A CA 1 ATOM 3829 C C . GLN A 1 479 ? -25.227 -11.867 -16.422 1.00 29.40 ? 481 GLN A C 1 ATOM 3830 O O . GLN A 1 479 ? -25.385 -11.974 -17.654 1.00 30.04 ? 481 GLN A O 1 ATOM 3831 C CB . GLN A 1 479 ? -23.557 -10.248 -15.504 1.00 26.67 ? 481 GLN A CB 1 ATOM 3832 C CG . GLN A 1 479 ? -22.083 -9.954 -15.052 1.00 27.44 ? 481 GLN A CG 1 ATOM 3833 C CD . GLN A 1 479 ? -21.597 -10.850 -13.888 1.00 28.10 ? 481 GLN A CD 1 ATOM 3834 O OE1 . GLN A 1 479 ? -22.400 -11.278 -13.045 1.00 31.18 ? 481 GLN A OE1 1 ATOM 3835 N NE2 . GLN A 1 479 ? -20.304 -11.151 -13.854 1.00 21.26 ? 481 GLN A NE2 1 ATOM 3836 N N . GLU A 1 480 ? -26.232 -11.865 -15.534 1.00 30.01 ? 482 GLU A N 1 ATOM 3837 C CA . GLU A 1 480 ? -27.644 -11.759 -15.916 1.00 33.52 ? 482 GLU A CA 1 ATOM 3838 C C . GLU A 1 480 ? -27.998 -10.472 -15.200 1.00 35.42 ? 482 GLU A C 1 ATOM 3839 O O . GLU A 1 480 ? -28.111 -10.455 -13.946 1.00 36.77 ? 482 GLU A O 1 ATOM 3840 C CB . GLU A 1 480 ? -28.508 -12.979 -15.474 1.00 33.27 ? 482 GLU A CB 1 ATOM 3841 C CG . GLU A 1 480 ? -29.998 -12.931 -15.964 1.00 36.51 ? 482 GLU A CG 1 ATOM 3842 C CD . GLU A 1 480 ? -30.709 -11.661 -15.480 1.00 42.52 ? 482 GLU A CD 1 ATOM 3843 O OE1 . GLU A 1 480 ? -31.231 -10.810 -16.263 1.00 42.88 ? 482 GLU A OE1 1 ATOM 3844 O OE2 . GLU A 1 480 ? -30.725 -11.477 -14.259 1.00 48.13 ? 482 GLU A OE2 1 ATOM 3845 N N . THR A 1 481 ? -28.016 -9.362 -15.949 1.00 35.47 ? 483 THR A N 1 ATOM 3846 C CA . THR A 1 481 ? -28.051 -8.030 -15.298 1.00 36.34 ? 483 THR A CA 1 ATOM 3847 C C . THR A 1 481 ? -29.454 -7.469 -14.907 1.00 38.22 ? 483 THR A C 1 ATOM 3848 O O . THR A 1 481 ? -29.537 -6.491 -14.173 1.00 37.09 ? 483 THR A O 1 ATOM 3849 C CB . THR A 1 481 ? -27.355 -6.956 -16.176 1.00 36.46 ? 483 THR A CB 1 ATOM 3850 O OG1 . THR A 1 481 ? -28.104 -6.825 -17.371 1.00 36.78 ? 483 THR A OG1 1 ATOM 3851 C CG2 . THR A 1 481 ? -25.899 -7.350 -16.548 1.00 33.18 ? 483 THR A CG2 1 ATOM 3852 N N . GLN A 1 482 ? -30.543 -8.063 -15.396 1.00 39.85 ? 484 GLN A N 1 ATOM 3853 C CA . GLN A 1 482 ? -31.875 -7.397 -15.273 1.00 43.92 ? 484 GLN A CA 1 ATOM 3854 C C . GLN A 1 482 ? -32.746 -7.928 -14.148 1.00 45.17 ? 484 GLN A C 1 ATOM 3855 O O . GLN A 1 482 ? -33.667 -7.276 -13.736 1.00 45.53 ? 484 GLN A O 1 ATOM 3856 C CB . GLN A 1 482 ? -32.663 -7.519 -16.587 1.00 44.27 ? 484 GLN A CB 1 ATOM 3857 C CG . GLN A 1 482 ? -31.892 -7.058 -17.795 1.00 47.11 ? 484 GLN A CG 1 ATOM 3858 C CD . GLN A 1 482 ? -32.611 -7.291 -19.110 1.00 51.10 ? 484 GLN A CD 1 ATOM 3859 O OE1 . GLN A 1 482 ? -33.008 -8.429 -19.471 1.00 50.26 ? 484 GLN A OE1 1 ATOM 3860 N NE2 . GLN A 1 482 ? -32.769 -6.196 -19.861 1.00 54.21 ? 484 GLN A NE2 1 ATOM 3861 N N . ASN A 1 483 ? -32.457 -9.123 -13.652 1.00 46.79 ? 485 ASN A N 1 ATOM 3862 C CA . ASN A 1 483 ? -33.401 -9.762 -12.727 1.00 50.27 ? 485 ASN A CA 1 ATOM 3863 C C . ASN A 1 483 ? -32.939 -9.928 -11.257 1.00 51.03 ? 485 ASN A C 1 ATOM 3864 O O . ASN A 1 483 ? -33.301 -10.918 -10.584 1.00 52.44 ? 485 ASN A O 1 ATOM 3865 C CB . ASN A 1 483 ? -33.899 -11.096 -13.328 1.00 49.69 ? 485 ASN A CB 1 ATOM 3866 C CG . ASN A 1 483 ? -34.862 -10.883 -14.504 1.00 55.06 ? 485 ASN A CG 1 ATOM 3867 O OD1 . ASN A 1 483 ? -35.154 -9.761 -14.870 1.00 50.28 ? 485 ASN A OD1 1 ATOM 3868 N ND2 . ASN A 1 483 ? -35.336 -11.978 -15.112 1.00 67.87 ? 485 ASN A ND2 1 ATOM 3869 N N . GLN A 1 484 ? -32.149 -8.982 -10.758 1.00 62.70 ? 486 GLN A N 1 ATOM 3870 C CA . GLN A 1 484 ? -31.583 -9.083 -9.410 1.00 62.39 ? 486 GLN A CA 1 ATOM 3871 C C . GLN A 1 484 ? -30.827 -10.408 -9.205 1.00 59.39 ? 486 GLN A C 1 ATOM 3872 O O . GLN A 1 484 ? -30.974 -11.078 -8.177 1.00 60.66 ? 486 GLN A O 1 ATOM 3873 C CB . GLN A 1 484 ? -32.683 -8.902 -8.346 1.00 65.50 ? 486 GLN A CB 1 ATOM 3874 C CG . GLN A 1 484 ? -33.901 -7.958 -8.780 1.00 73.43 ? 486 GLN A CG 1 ATOM 3875 C CD . GLN A 1 484 ? -33.484 -6.482 -8.953 1.00 79.47 ? 486 GLN A CD 1 ATOM 3876 O OE1 . GLN A 1 484 ? -32.498 -6.032 -8.337 1.00 80.88 ? 486 GLN A OE1 1 ATOM 3877 N NE2 . GLN A 1 484 ? -34.238 -5.723 -9.778 1.00 82.84 ? 486 GLN A NE2 1 ATOM 3878 N N . SER A 1 485 ? -30.045 -10.826 -10.189 1.00 55.89 ? 487 SER A N 1 ATOM 3879 C CA . SER A 1 485 ? -29.336 -12.079 -10.052 1.00 52.14 ? 487 SER A CA 1 ATOM 3880 C C . SER A 1 485 ? -28.066 -11.872 -9.275 1.00 49.73 ? 487 SER A C 1 ATOM 3881 O O . SER A 1 485 ? -27.538 -10.746 -9.218 1.00 49.85 ? 487 SER A O 1 ATOM 3882 C CB . SER A 1 485 ? -28.979 -12.672 -11.407 1.00 50.19 ? 487 SER A CB 1 ATOM 3883 O OG . SER A 1 485 ? -30.160 -12.789 -12.152 1.00 55.39 ? 487 SER A OG 1 ATOM 3884 N N . THR A 1 486 ? -27.592 -12.980 -8.694 1.00 46.36 ? 488 THR A N 1 ATOM 3885 C CA . THR A 1 486 ? -26.281 -13.093 -8.093 1.00 43.09 ? 488 THR A CA 1 ATOM 3886 C C . THR A 1 486 ? -25.275 -12.755 -9.174 1.00 40.56 ? 488 THR A C 1 ATOM 3887 O O . THR A 1 486 ? -25.336 -13.277 -10.306 1.00 38.95 ? 488 THR A O 1 ATOM 3888 C CB . THR A 1 486 ? -25.997 -14.541 -7.708 1.00 41.88 ? 488 THR A CB 1 ATOM 3889 O OG1 . THR A 1 486 ? -27.055 -14.999 -6.873 1.00 45.57 ? 488 THR A OG1 1 ATOM 3890 C CG2 . THR A 1 486 ? -24.712 -14.649 -6.959 1.00 40.33 ? 488 THR A CG2 1 ATOM 3891 N N . SER A 1 487 ? -24.385 -11.863 -8.800 1.00 38.38 ? 489 SER A N 1 ATOM 3892 C CA . SER A 1 487 ? -23.265 -11.457 -9.596 1.00 38.15 ? 489 SER A CA 1 ATOM 3893 C C . SER A 1 487 ? -22.225 -12.584 -9.648 1.00 34.38 ? 489 SER A C 1 ATOM 3894 O O . SER A 1 487 ? -21.957 -13.227 -8.635 1.00 33.93 ? 489 SER A O 1 ATOM 3895 C CB . SER A 1 487 ? -22.653 -10.271 -8.884 1.00 39.73 ? 489 SER A CB 1 ATOM 3896 O OG . SER A 1 487 ? -22.218 -9.359 -9.832 1.00 46.82 ? 489 SER A OG 1 ATOM 3897 N N . TRP A 1 488 ? -21.716 -12.884 -10.835 1.00 31.00 ? 490 TRP A N 1 ATOM 3898 C CA . TRP A 1 488 ? -20.754 -13.970 -11.020 1.00 27.07 ? 490 TRP A CA 1 ATOM 3899 C C . TRP A 1 488 ? -19.319 -13.326 -10.904 1.00 25.92 ? 490 TRP A C 1 ATOM 3900 O O . TRP A 1 488 ? -18.905 -12.552 -11.765 1.00 24.88 ? 490 TRP A O 1 ATOM 3901 C CB . TRP A 1 488 ? -20.993 -14.607 -12.389 1.00 25.36 ? 490 TRP A CB 1 ATOM 3902 C CG . TRP A 1 488 ? -20.294 -15.951 -12.605 1.00 26.85 ? 490 TRP A CG 1 ATOM 3903 C CD1 . TRP A 1 488 ? -19.178 -16.461 -11.922 1.00 23.19 ? 490 TRP A CD1 1 ATOM 3904 C CD2 . TRP A 1 488 ? -20.649 -16.961 -13.568 1.00 24.55 ? 490 TRP A CD2 1 ATOM 3905 N NE1 . TRP A 1 488 ? -18.846 -17.702 -12.413 1.00 24.19 ? 490 TRP A NE1 1 ATOM 3906 C CE2 . TRP A 1 488 ? -19.724 -18.039 -13.411 1.00 22.55 ? 490 TRP A CE2 1 ATOM 3907 C CE3 . TRP A 1 488 ? -21.634 -17.050 -14.545 1.00 23.33 ? 490 TRP A CE3 1 ATOM 3908 C CZ2 . TRP A 1 488 ? -19.751 -19.167 -14.224 1.00 20.70 ? 490 TRP A CZ2 1 ATOM 3909 C CZ3 . TRP A 1 488 ? -21.685 -18.178 -15.355 1.00 23.78 ? 490 TRP A CZ3 1 ATOM 3910 C CH2 . TRP A 1 488 ? -20.747 -19.223 -15.191 1.00 26.30 ? 490 TRP A CH2 1 ATOM 3911 N N . PRO A 1 489 ? -18.601 -13.590 -9.809 1.00 25.84 ? 491 PRO A N 1 ATOM 3912 C CA . PRO A 1 489 ? -17.248 -13.036 -9.576 1.00 26.96 ? 491 PRO A CA 1 ATOM 3913 C C . PRO A 1 489 ? -16.205 -13.779 -10.436 1.00 26.96 ? 491 PRO A C 1 ATOM 3914 O O . PRO A 1 489 ? -16.477 -14.931 -10.801 1.00 26.02 ? 491 PRO A O 1 ATOM 3915 C CB . PRO A 1 489 ? -17.022 -13.316 -8.082 1.00 27.44 ? 491 PRO A CB 1 ATOM 3916 C CG . PRO A 1 489 ? -17.736 -14.664 -7.882 1.00 28.75 ? 491 PRO A CG 1 ATOM 3917 C CD . PRO A 1 489 ? -18.950 -14.658 -8.838 1.00 25.96 ? 491 PRO A CD 1 ATOM 3918 N N . VAL A 1 490 ? -15.116 -13.096 -10.865 1.00 27.67 ? 492 VAL A N 1 ATOM 3919 C CA . VAL A 1 490 ? -14.041 -13.744 -11.556 1.00 28.32 ? 492 VAL A CA 1 ATOM 3920 C C . VAL A 1 490 ? -13.372 -14.730 -10.594 1.00 29.61 ? 492 VAL A C 1 ATOM 3921 O O . VAL A 1 490 ? -13.323 -14.508 -9.358 1.00 29.90 ? 492 VAL A O 1 ATOM 3922 C CB . VAL A 1 490 ? -13.040 -12.764 -12.270 1.00 30.48 ? 492 VAL A CB 1 ATOM 3923 C CG1 . VAL A 1 490 ? -13.777 -11.558 -12.973 1.00 29.65 ? 492 VAL A CG1 1 ATOM 3924 C CG2 . VAL A 1 490 ? -11.994 -12.243 -11.357 1.00 33.97 ? 492 VAL A CG2 1 ATOM 3925 N N . PHE A 1 491 ? -12.939 -15.850 -11.154 1.00 29.35 ? 493 PHE A N 1 ATOM 3926 C CA . PHE A 1 491 ? -12.169 -16.872 -10.446 1.00 31.28 ? 493 PHE A CA 1 ATOM 3927 C C . PHE A 1 491 ? -10.713 -16.435 -10.442 1.00 34.92 ? 493 PHE A C 1 ATOM 3928 O O . PHE A 1 491 ? -10.092 -16.278 -11.502 1.00 36.05 ? 493 PHE A O 1 ATOM 3929 C CB . PHE A 1 491 ? -12.280 -18.204 -11.169 1.00 28.11 ? 493 PHE A CB 1 ATOM 3930 C CG . PHE A 1 491 ? -11.540 -19.365 -10.516 1.00 28.00 ? 493 PHE A CG 1 ATOM 3931 C CD1 . PHE A 1 491 ? -10.174 -19.533 -10.702 1.00 33.81 ? 493 PHE A CD1 1 ATOM 3932 C CD2 . PHE A 1 491 ? -12.234 -20.358 -9.832 1.00 27.39 ? 493 PHE A CD2 1 ATOM 3933 C CE1 . PHE A 1 491 ? -9.490 -20.659 -10.153 1.00 31.22 ? 493 PHE A CE1 1 ATOM 3934 C CE2 . PHE A 1 491 ? -11.590 -21.509 -9.316 1.00 28.21 ? 493 PHE A CE2 1 ATOM 3935 C CZ . PHE A 1 491 ? -10.215 -21.649 -9.483 1.00 30.52 ? 493 PHE A CZ 1 ATOM 3936 N N . LYS A 1 492 ? -10.185 -16.204 -9.252 1.00 37.30 ? 494 LYS A N 1 ATOM 3937 C CA . LYS A 1 492 ? -8.824 -15.794 -9.124 1.00 42.12 ? 494 LYS A CA 1 ATOM 3938 C C . LYS A 1 492 ? -8.097 -16.894 -8.347 1.00 43.24 ? 494 LYS A C 1 ATOM 3939 O O . LYS A 1 492 ? -8.720 -17.665 -7.600 1.00 42.08 ? 494 LYS A O 1 ATOM 3940 C CB . LYS A 1 492 ? -8.789 -14.433 -8.429 1.00 44.33 ? 494 LYS A CB 1 ATOM 3941 C CG . LYS A 1 492 ? -8.678 -13.284 -9.412 1.00 50.18 ? 494 LYS A CG 1 ATOM 3942 C CD . LYS A 1 492 ? -9.009 -11.906 -8.849 1.00 60.35 ? 494 LYS A CD 1 ATOM 3943 C CE . LYS A 1 492 ? -8.479 -10.836 -9.864 1.00 67.29 ? 494 LYS A CE 1 ATOM 3944 N NZ . LYS A 1 492 ? -9.287 -9.576 -10.010 1.00 68.29 ? 494 LYS A NZ 1 ATOM 3945 N N . SER A 1 493 ? -6.815 -17.060 -8.615 1.00 46.29 ? 495 SER A N 1 ATOM 3946 C CA . SER A 1 493 ? -5.909 -17.719 -7.670 1.00 49.70 ? 495 SER A CA 1 ATOM 3947 C C . SER A 1 493 ? -6.075 -17.022 -6.324 1.00 50.11 ? 495 SER A C 1 ATOM 3948 O O . SER A 1 493 ? -6.218 -15.765 -6.239 1.00 53.23 ? 495 SER A O 1 ATOM 3949 C CB . SER A 1 493 ? -4.402 -17.471 -8.054 1.00 53.28 ? 495 SER A CB 1 ATOM 3950 O OG . SER A 1 493 ? -3.832 -18.664 -8.592 1.00 57.72 ? 495 SER A OG 1 ATOM 3951 N N . THR A 1 494 ? -5.961 -17.804 -5.277 1.00 47.87 ? 496 THR A N 1 ATOM 3952 C CA . THR A 1 494 ? -6.125 -17.312 -3.914 1.00 49.05 ? 496 THR A CA 1 ATOM 3953 C C . THR A 1 494 ? -7.581 -17.506 -3.541 1.00 44.75 ? 496 THR A C 1 ATOM 3954 O O . THR A 1 494 ? -7.899 -18.542 -2.940 1.00 44.39 ? 496 THR A O 1 ATOM 3955 C CB . THR A 1 494 ? -5.390 -15.902 -3.505 1.00 52.05 ? 496 THR A CB 1 ATOM 3956 O OG1 . THR A 1 494 ? -6.212 -14.766 -3.787 1.00 56.66 ? 496 THR A OG1 1 ATOM 3957 C CG2 . THR A 1 494 ? -4.023 -15.717 -4.227 1.00 54.65 ? 496 THR A CG2 1 ATOM 3958 N N . GLU A 1 495 ? -8.493 -16.665 -3.983 1.00 41.61 ? 497 GLU A N 1 ATOM 3959 C CA . GLU A 1 495 ? -9.870 -16.887 -3.507 1.00 39.17 ? 497 GLU A CA 1 ATOM 3960 C C . GLU A 1 495 ? -10.684 -18.005 -4.163 1.00 35.18 ? 497 GLU A C 1 ATOM 3961 O O . GLU A 1 495 ? -11.437 -18.722 -3.494 1.00 33.51 ? 497 GLU A O 1 ATOM 3962 C CB . GLU A 1 495 ? -10.632 -15.596 -3.514 1.00 40.80 ? 497 GLU A CB 1 ATOM 3963 C CG . GLU A 1 495 ? -10.059 -14.591 -2.564 1.00 49.17 ? 497 GLU A CG 1 ATOM 3964 C CD . GLU A 1 495 ? -10.884 -13.340 -2.563 1.00 61.73 ? 497 GLU A CD 1 ATOM 3965 O OE1 . GLU A 1 495 ? -11.600 -13.069 -1.554 1.00 65.09 ? 497 GLU A OE1 1 ATOM 3966 O OE2 . GLU A 1 495 ? -10.848 -12.645 -3.609 1.00 67.89 ? 497 GLU A OE2 1 ATOM 3967 N N . GLN A 1 496 ? -10.516 -18.174 -5.451 1.00 32.27 ? 498 GLN A N 1 ATOM 3968 C CA . GLN A 1 496 ? -11.158 -19.277 -6.165 1.00 29.97 ? 498 GLN A CA 1 ATOM 3969 C C . GLN A 1 496 ? -12.688 -19.265 -6.018 1.00 28.39 ? 498 GLN A C 1 ATOM 3970 O O . GLN A 1 496 ? -13.318 -20.273 -5.706 1.00 27.24 ? 498 GLN A O 1 ATOM 3971 C CB . GLN A 1 496 ? -10.521 -20.601 -5.718 1.00 31.29 ? 498 GLN A CB 1 ATOM 3972 C CG . GLN A 1 496 ? -9.031 -20.779 -6.043 1.00 34.40 ? 498 GLN A CG 1 ATOM 3973 C CD . GLN A 1 496 ? -8.294 -21.838 -5.141 1.00 40.09 ? 498 GLN A CD 1 ATOM 3974 O OE1 . GLN A 1 496 ? -7.326 -21.512 -4.444 1.00 49.77 ? 498 GLN A OE1 1 ATOM 3975 N NE2 . GLN A 1 496 ? -8.750 -23.051 -5.148 1.00 32.85 ? 498 GLN A NE2 1 ATOM 3976 N N . LYS A 1 497 ? -13.308 -18.119 -6.244 1.00 28.48 ? 499 LYS A N 1 ATOM 3977 C CA . LYS A 1 497 ? -14.784 -18.060 -6.177 1.00 27.16 ? 499 LYS A CA 1 ATOM 3978 C C . LYS A 1 497 ? -15.428 -18.771 -7.359 1.00 25.84 ? 499 LYS A C 1 ATOM 3979 O O . LYS A 1 497 ? -14.910 -18.669 -8.490 1.00 26.45 ? 499 LYS A O 1 ATOM 3980 C CB . LYS A 1 497 ? -15.243 -16.615 -6.118 1.00 25.80 ? 499 LYS A CB 1 ATOM 3981 C CG . LYS A 1 497 ? -14.786 -15.997 -4.833 1.00 28.17 ? 499 LYS A CG 1 ATOM 3982 C CD . LYS A 1 497 ? -15.224 -14.500 -4.723 1.00 28.04 ? 499 LYS A CD 1 ATOM 3983 C CE . LYS A 1 497 ? -14.441 -13.731 -3.545 1.00 28.25 ? 499 LYS A CE 1 ATOM 3984 N NZ . LYS A 1 497 ? -15.064 -12.393 -3.590 1.00 32.49 ? 499 LYS A NZ 1 ATOM 3985 N N . TYR A 1 498 ? -16.522 -19.512 -7.110 1.00 23.93 ? 500 TYR A N 1 ATOM 3986 C CA . TYR A 1 498 ? -17.284 -20.045 -8.235 1.00 23.97 ? 500 TYR A CA 1 ATOM 3987 C C . TYR A 1 498 ? -18.772 -19.787 -8.015 1.00 24.65 ? 500 TYR A C 1 ATOM 3988 O O . TYR A 1 498 ? -19.188 -19.535 -6.894 1.00 25.39 ? 500 TYR A O 1 ATOM 3989 C CB . TYR A 1 498 ? -17.009 -21.534 -8.447 1.00 21.93 ? 500 TYR A CB 1 ATOM 3990 C CG . TYR A 1 498 ? -17.362 -22.438 -7.250 1.00 25.13 ? 500 TYR A CG 1 ATOM 3991 C CD1 . TYR A 1 498 ? -16.488 -22.546 -6.134 1.00 22.95 ? 500 TYR A CD1 1 ATOM 3992 C CD2 . TYR A 1 498 ? -18.526 -23.228 -7.258 1.00 18.16 ? 500 TYR A CD2 1 ATOM 3993 C CE1 . TYR A 1 498 ? -16.775 -23.424 -5.086 1.00 23.16 ? 500 TYR A CE1 1 ATOM 3994 C CE2 . TYR A 1 498 ? -18.828 -24.068 -6.185 1.00 18.27 ? 500 TYR A CE2 1 ATOM 3995 C CZ . TYR A 1 498 ? -17.971 -24.171 -5.122 1.00 22.97 ? 500 TYR A CZ 1 ATOM 3996 O OH . TYR A 1 498 ? -18.303 -25.017 -4.059 1.00 18.09 ? 500 TYR A OH 1 ATOM 3997 N N . LEU A 1 499 ? -19.569 -19.931 -9.068 1.00 23.64 ? 501 LEU A N 1 ATOM 3998 C CA . LEU A 1 499 ? -21.014 -19.727 -8.967 1.00 24.49 ? 501 LEU A CA 1 ATOM 3999 C C . LEU A 1 499 ? -21.741 -21.134 -9.057 1.00 24.29 ? 501 LEU A C 1 ATOM 4000 O O . LEU A 1 499 ? -21.412 -21.949 -9.946 1.00 24.32 ? 501 LEU A O 1 ATOM 4001 C CB . LEU A 1 499 ? -21.447 -18.805 -10.123 1.00 22.89 ? 501 LEU A CB 1 ATOM 4002 C CG . LEU A 1 499 ? -22.962 -18.442 -10.224 1.00 28.65 ? 501 LEU A CG 1 ATOM 4003 C CD1 . LEU A 1 499 ? -23.364 -17.551 -9.083 1.00 24.41 ? 501 LEU A CD1 1 ATOM 4004 C CD2 . LEU A 1 499 ? -23.334 -17.697 -11.466 1.00 25.24 ? 501 LEU A CD2 1 ATOM 4005 N N . THR A 1 500 ? -22.687 -21.422 -8.161 1.00 25.54 ? 502 THR A N 1 ATOM 4006 C CA . THR A 1 500 ? -23.505 -22.625 -8.279 1.00 26.02 ? 502 THR A CA 1 ATOM 4007 C C . THR A 1 500 ? -24.737 -22.341 -9.141 1.00 27.65 ? 502 THR A C 1 ATOM 4008 O O . THR A 1 500 ? -25.356 -21.265 -8.997 1.00 28.99 ? 502 THR A O 1 ATOM 4009 C CB . THR A 1 500 ? -23.901 -23.235 -6.912 1.00 27.61 ? 502 THR A CB 1 ATOM 4010 O OG1 . THR A 1 500 ? -24.811 -22.366 -6.232 1.00 26.10 ? 502 THR A OG1 1 ATOM 4011 C CG2 . THR A 1 500 ? -22.604 -23.493 -6.038 1.00 24.29 ? 502 THR A CG2 1 ATOM 4012 N N . LEU A 1 501 ? -25.087 -23.295 -10.020 1.00 25.54 ? 503 LEU A N 1 ATOM 4013 C CA . LEU A 1 501 ? -26.227 -23.153 -10.954 1.00 25.82 ? 503 LEU A CA 1 ATOM 4014 C C . LEU A 1 501 ? -27.247 -24.173 -10.499 1.00 28.58 ? 503 LEU A C 1 ATOM 4015 O O . LEU A 1 501 ? -27.007 -25.398 -10.536 1.00 26.28 ? 503 LEU A O 1 ATOM 4016 C CB . LEU A 1 501 ? -25.778 -23.429 -12.416 1.00 25.20 ? 503 LEU A CB 1 ATOM 4017 C CG . LEU A 1 501 ? -24.697 -22.440 -12.987 1.00 24.90 ? 503 LEU A CG 1 ATOM 4018 C CD1 . LEU A 1 501 ? -24.248 -22.863 -14.396 1.00 16.16 ? 503 LEU A CD1 1 ATOM 4019 C CD2 . LEU A 1 501 ? -25.381 -21.032 -12.981 1.00 24.86 ? 503 LEU A CD2 1 ATOM 4020 N N . ASN A 1 502 ? -28.396 -23.673 -10.055 1.00 31.02 ? 504 ASN A N 1 ATOM 4021 C CA . ASN A 1 502 ? -29.411 -24.533 -9.522 1.00 34.64 ? 504 ASN A CA 1 ATOM 4022 C C . ASN A 1 502 ? -30.719 -23.812 -9.622 1.00 37.95 ? 504 ASN A C 1 ATOM 4023 O O . ASN A 1 502 ? -30.788 -22.646 -9.978 1.00 38.09 ? 504 ASN A O 1 ATOM 4024 C CB . ASN A 1 502 ? -29.113 -25.041 -8.090 1.00 33.00 ? 504 ASN A CB 1 ATOM 4025 C CG . ASN A 1 502 ? -29.049 -23.924 -7.073 1.00 38.83 ? 504 ASN A CG 1 ATOM 4026 O OD1 . ASN A 1 502 ? -30.085 -23.376 -6.690 1.00 42.66 ? 504 ASN A OD1 1 ATOM 4027 N ND2 . ASN A 1 502 ? -27.815 -23.603 -6.570 1.00 37.89 ? 504 ASN A ND2 1 ATOM 4028 N N . THR A 1 503 ? -31.755 -24.532 -9.300 1.00 40.97 ? 505 THR A N 1 ATOM 4029 C CA . THR A 1 503 ? -33.045 -24.096 -9.588 1.00 46.60 ? 505 THR A CA 1 ATOM 4030 C C . THR A 1 503 ? -33.493 -23.196 -8.434 1.00 51.86 ? 505 THR A C 1 ATOM 4031 O O . THR A 1 503 ? -34.366 -22.317 -8.602 1.00 55.01 ? 505 THR A O 1 ATOM 4032 C CB . THR A 1 503 ? -33.858 -25.364 -9.774 1.00 47.21 ? 505 THR A CB 1 ATOM 4033 O OG1 . THR A 1 503 ? -34.484 -25.337 -11.053 1.00 48.49 ? 505 THR A OG1 1 ATOM 4034 C CG2 . THR A 1 503 ? -34.776 -25.639 -8.623 1.00 45.71 ? 505 THR A CG2 1 ATOM 4035 N N . GLU A 1 504 ? -32.875 -23.372 -7.264 1.00 52.92 ? 506 GLU A N 1 ATOM 4036 C CA A GLU A 1 504 ? -33.330 -22.698 -6.058 0.50 56.66 ? 506 GLU A CA 1 ATOM 4037 C CA B GLU A 1 504 ? -33.381 -22.658 -6.100 0.50 56.37 ? 506 GLU A CA 1 ATOM 4038 C C . GLU A 1 504 ? -32.678 -21.318 -5.890 1.00 56.90 ? 506 GLU A C 1 ATOM 4039 O O . GLU A 1 504 ? -33.346 -20.251 -6.006 1.00 59.71 ? 506 GLU A O 1 ATOM 4040 C CB A GLU A 1 504 ? -33.032 -23.564 -4.836 0.50 56.87 ? 506 GLU A CB 1 ATOM 4041 C CB B GLU A 1 504 ? -33.437 -23.524 -4.830 0.50 56.92 ? 506 GLU A CB 1 ATOM 4042 C CG A GLU A 1 504 ? -32.679 -25.010 -5.151 0.50 56.19 ? 506 GLU A CG 1 ATOM 4043 C CG B GLU A 1 504 ? -34.701 -24.395 -4.695 0.50 58.76 ? 506 GLU A CG 1 ATOM 4044 C CD A GLU A 1 504 ? -31.909 -25.635 -4.024 0.50 57.67 ? 506 GLU A CD 1 ATOM 4045 C CD B GLU A 1 504 ? -35.887 -23.854 -5.479 0.50 60.52 ? 506 GLU A CD 1 ATOM 4046 O OE1 A GLU A 1 504 ? -30.718 -25.229 -3.811 0.50 55.81 ? 506 GLU A OE1 1 ATOM 4047 O OE1 B GLU A 1 504 ? -36.809 -23.252 -4.874 0.50 61.95 ? 506 GLU A OE1 1 ATOM 4048 O OE2 A GLU A 1 504 ? -32.508 -26.512 -3.352 0.50 58.42 ? 506 GLU A OE2 1 ATOM 4049 O OE2 B GLU A 1 504 ? -35.891 -24.021 -6.712 0.50 57.89 ? 506 GLU A OE2 1 ATOM 4050 N N . SER A 1 505 ? -31.380 -21.332 -5.606 1.00 54.60 ? 507 SER A N 1 ATOM 4051 C CA . SER A 1 505 ? -30.663 -20.077 -5.357 1.00 55.32 ? 507 SER A CA 1 ATOM 4052 C C . SER A 1 505 ? -29.203 -20.292 -5.658 1.00 50.67 ? 507 SER A C 1 ATOM 4053 O O . SER A 1 505 ? -28.588 -21.195 -5.129 1.00 49.46 ? 507 SER A O 1 ATOM 4054 C CB . SER A 1 505 ? -30.819 -19.573 -3.898 1.00 58.50 ? 507 SER A CB 1 ATOM 4055 O OG . SER A 1 505 ? -30.162 -20.472 -2.971 1.00 62.36 ? 507 SER A OG 1 ATOM 4056 N N . THR A 1 506 ? -28.754 -19.501 -6.609 1.00 47.55 ? 508 THR A N 1 ATOM 4057 C CA . THR A 1 506 ? -27.411 -19.239 -6.974 1.00 45.69 ? 508 THR A CA 1 ATOM 4058 C C . THR A 1 506 ? -26.547 -18.775 -5.803 1.00 43.73 ? 508 THR A C 1 ATOM 4059 O O . THR A 1 506 ? -26.880 -17.813 -5.118 1.00 44.57 ? 508 THR A O 1 ATOM 4060 C CB . THR A 1 506 ? -27.531 -18.126 -7.968 1.00 46.63 ? 508 THR A CB 1 ATOM 4061 O OG1 . THR A 1 506 ? -28.329 -18.631 -9.018 1.00 53.39 ? 508 THR A OG1 1 ATOM 4062 C CG2 . THR A 1 506 ? -26.288 -17.744 -8.567 1.00 45.49 ? 508 THR A CG2 1 ATOM 4063 N N . ARG A 1 507 ? -25.427 -19.459 -5.582 1.00 39.22 ? 509 ARG A N 1 ATOM 4064 C CA . ARG A 1 507 ? -24.546 -19.063 -4.524 1.00 37.22 ? 509 ARG A CA 1 ATOM 4065 C C . ARG A 1 507 ? -23.163 -18.870 -5.002 1.00 34.51 ? 509 ARG A C 1 ATOM 4066 O O . ARG A 1 507 ? -22.693 -19.562 -5.935 1.00 33.39 ? 509 ARG A O 1 ATOM 4067 C CB . ARG A 1 507 ? -24.529 -20.113 -3.455 1.00 37.71 ? 509 ARG A CB 1 ATOM 4068 C CG . ARG A 1 507 ? -25.748 -20.008 -2.604 1.00 42.36 ? 509 ARG A CG 1 ATOM 4069 C CD . ARG A 1 507 ? -26.027 -21.321 -1.942 1.00 52.14 ? 509 ARG A CD 1 ATOM 4070 N NE . ARG A 1 507 ? -27.293 -21.336 -1.158 1.00 65.16 ? 509 ARG A NE 1 ATOM 4071 C CZ . ARG A 1 507 ? -27.873 -20.304 -0.517 1.00 68.81 ? 509 ARG A CZ 1 ATOM 4072 N NH1 . ARG A 1 507 ? -27.346 -19.073 -0.502 1.00 67.52 ? 509 ARG A NH1 1 ATOM 4073 N NH2 . ARG A 1 507 ? -29.013 -20.527 0.124 1.00 73.75 ? 509 ARG A NH2 1 ATOM 4074 N N . ILE A 1 508 ? -22.492 -17.905 -4.386 1.00 32.82 ? 510 ILE A N 1 ATOM 4075 C CA A ILE A 1 508 ? -21.058 -17.796 -4.565 0.50 30.14 ? 510 ILE A CA 1 ATOM 4076 C CA B ILE A 1 508 ? -21.061 -17.790 -4.570 0.50 30.03 ? 510 ILE A CA 1 ATOM 4077 C C . ILE A 1 508 ? -20.378 -18.641 -3.482 1.00 29.81 ? 510 ILE A C 1 ATOM 4078 O O . ILE A 1 508 ? -20.593 -18.429 -2.272 1.00 30.08 ? 510 ILE A O 1 ATOM 4079 C CB A ILE A 1 508 ? -20.569 -16.333 -4.522 0.50 30.68 ? 510 ILE A CB 1 ATOM 4080 C CB B ILE A 1 508 ? -20.574 -16.318 -4.512 0.50 30.48 ? 510 ILE A CB 1 ATOM 4081 C CG1 A ILE A 1 508 ? -21.232 -15.518 -5.643 0.50 29.46 ? 510 ILE A CG1 1 ATOM 4082 C CG1 B ILE A 1 508 ? -21.280 -15.440 -5.572 0.50 28.86 ? 510 ILE A CG1 1 ATOM 4083 C CG2 A ILE A 1 508 ? -19.054 -16.275 -4.678 0.50 29.25 ? 510 ILE A CG2 1 ATOM 4084 C CG2 B ILE A 1 508 ? -19.063 -16.255 -4.707 0.50 29.05 ? 510 ILE A CG2 1 ATOM 4085 C CD1 A ILE A 1 508 ? -21.275 -16.268 -6.923 0.50 28.19 ? 510 ILE A CD1 1 ATOM 4086 C CD1 B ILE A 1 508 ? -21.282 -13.940 -5.227 0.50 28.66 ? 510 ILE A CD1 1 ATOM 4087 N N . MET A 1 509 ? -19.525 -19.564 -3.926 1.00 28.19 ? 511 MET A N 1 ATOM 4088 C CA A MET A 1 509 ? -18.764 -20.443 -3.061 0.50 27.94 ? 511 MET A CA 1 ATOM 4089 C CA B MET A 1 509 ? -18.742 -20.348 -2.998 0.50 28.24 ? 511 MET A CA 1 ATOM 4090 C C . MET A 1 509 ? -17.257 -20.331 -3.356 1.00 27.29 ? 511 MET A C 1 ATOM 4091 O O . MET A 1 509 ? -16.848 -19.675 -4.328 1.00 27.94 ? 511 MET A O 1 ATOM 4092 C CB A MET A 1 509 ? -19.244 -21.888 -3.269 0.50 27.84 ? 511 MET A CB 1 ATOM 4093 C CB B MET A 1 509 ? -19.303 -21.767 -2.924 0.50 28.81 ? 511 MET A CB 1 ATOM 4094 C CG A MET A 1 509 ? -20.736 -22.102 -2.997 0.50 27.29 ? 511 MET A CG 1 ATOM 4095 C CG B MET A 1 509 ? -20.748 -21.771 -2.480 0.50 29.14 ? 511 MET A CG 1 ATOM 4096 S SD A MET A 1 509 ? -21.214 -21.689 -1.303 0.50 31.58 ? 511 MET A SD 1 ATOM 4097 S SD B MET A 1 509 ? -21.441 -23.401 -2.321 0.50 33.06 ? 511 MET A SD 1 ATOM 4098 C CE A MET A 1 509 ? -20.981 -23.280 -0.485 0.50 29.58 ? 511 MET A CE 1 ATOM 4099 C CE B MET A 1 509 ? -20.395 -24.014 -1.017 0.50 28.50 ? 511 MET A CE 1 ATOM 4100 N N . THR A 1 510 ? -16.444 -20.980 -2.535 1.00 26.09 ? 512 THR A N 1 ATOM 4101 C CA . THR A 1 510 ? -14.980 -20.951 -2.683 1.00 25.56 ? 512 THR A CA 1 ATOM 4102 C C . THR A 1 510 ? -14.312 -22.325 -2.599 1.00 23.74 ? 512 THR A C 1 ATOM 4103 O O . THR A 1 510 ? -14.729 -23.204 -1.799 1.00 23.10 ? 512 THR A O 1 ATOM 4104 C CB . THR A 1 510 ? -14.306 -19.951 -1.641 1.00 27.50 ? 512 THR A CB 1 ATOM 4105 O OG1 . THR A 1 510 ? -14.798 -20.241 -0.332 1.00 29.30 ? 512 THR A OG1 1 ATOM 4106 C CG2 . THR A 1 510 ? -14.696 -18.453 -1.976 1.00 26.75 ? 512 THR A CG2 1 ATOM 4107 N N . LYS A 1 511 ? -13.323 -22.528 -3.460 1.00 22.23 ? 513 LYS A N 1 ATOM 4108 C CA . LYS A 1 511 ? -12.406 -23.675 -3.318 1.00 23.74 ? 513 LYS A CA 1 ATOM 4109 C C . LYS A 1 511 ? -13.120 -24.959 -3.415 1.00 24.33 ? 513 LYS A C 1 ATOM 4110 O O . LYS A 1 511 ? -13.075 -25.802 -2.450 1.00 26.07 ? 513 LYS A O 1 ATOM 4111 C CB . LYS A 1 511 ? -11.634 -23.596 -1.982 1.00 25.28 ? 513 LYS A CB 1 ATOM 4112 C CG . LYS A 1 511 ? -10.625 -22.401 -1.959 1.00 30.30 ? 513 LYS A CG 1 ATOM 4113 C CD . LYS A 1 511 ? -10.005 -22.078 -0.586 1.00 34.26 ? 513 LYS A CD 1 ATOM 4114 C CE . LYS A 1 511 ? -9.088 -20.853 -0.742 1.00 38.85 ? 513 LYS A CE 1 ATOM 4115 N NZ . LYS A 1 511 ? -8.053 -20.695 0.393 1.00 47.27 ? 513 LYS A NZ 1 ATOM 4116 N N . LEU A 1 512 ? -13.876 -25.096 -4.514 1.00 23.81 ? 514 LEU A N 1 ATOM 4117 C CA . LEU A 1 512 ? -14.526 -26.372 -4.858 1.00 23.95 ? 514 LEU A CA 1 ATOM 4118 C C . LEU A 1 512 ? -13.553 -27.594 -4.679 1.00 24.22 ? 514 LEU A C 1 ATOM 4119 O O . LEU A 1 512 ? -12.413 -27.563 -5.179 1.00 23.77 ? 514 LEU A O 1 ATOM 4120 C CB . LEU A 1 512 ? -14.986 -26.322 -6.316 1.00 21.67 ? 514 LEU A CB 1 ATOM 4121 C CG . LEU A 1 512 ? -15.696 -27.559 -6.877 1.00 22.31 ? 514 LEU A CG 1 ATOM 4122 C CD1 . LEU A 1 512 ? -16.961 -27.799 -6.017 1.00 19.42 ? 514 LEU A CD1 1 ATOM 4123 C CD2 . LEU A 1 512 ? -16.127 -27.329 -8.311 1.00 20.62 ? 514 LEU A CD2 1 ATOM 4124 N N . ARG A 1 513 ? -13.982 -28.614 -3.937 1.00 25.22 ? 515 ARG A N 1 ATOM 4125 C CA . ARG A 1 513 ? -13.217 -29.857 -3.795 1.00 27.14 ? 515 ARG A CA 1 ATOM 4126 C C . ARG A 1 513 ? -11.792 -29.638 -3.342 1.00 28.51 ? 515 ARG A C 1 ATOM 4127 O O . ARG A 1 513 ? -10.896 -30.325 -3.821 1.00 29.77 ? 515 ARG A O 1 ATOM 4128 C CB . ARG A 1 513 ? -13.209 -30.678 -5.111 1.00 25.97 ? 515 ARG A CB 1 ATOM 4129 C CG . ARG A 1 513 ? -14.594 -31.145 -5.616 1.00 27.39 ? 515 ARG A CG 1 ATOM 4130 C CD . ARG A 1 513 ? -15.222 -32.455 -4.955 1.00 30.92 ? 515 ARG A CD 1 ATOM 4131 N NE . ARG A 1 513 ? -16.251 -33.033 -5.833 1.00 27.44 ? 515 ARG A NE 1 ATOM 4132 C CZ . ARG A 1 513 ? -17.468 -32.474 -5.993 1.00 36.48 ? 515 ARG A CZ 1 ATOM 4133 N NH1 . ARG A 1 513 ? -18.412 -32.975 -6.862 1.00 25.87 ? 515 ARG A NH1 1 ATOM 4134 N NH2 . ARG A 1 513 ? -17.768 -31.399 -5.224 1.00 36.32 ? 515 ARG A NH2 1 ATOM 4135 N N . ALA A 1 514 ? -11.555 -28.693 -2.431 1.00 29.20 ? 516 ALA A N 1 ATOM 4136 C CA . ALA A 1 514 ? -10.183 -28.301 -2.132 1.00 30.45 ? 516 ALA A CA 1 ATOM 4137 C C . ALA A 1 514 ? -9.375 -29.535 -1.728 1.00 31.80 ? 516 ALA A C 1 ATOM 4138 O O . ALA A 1 514 ? -8.286 -29.758 -2.278 1.00 30.23 ? 516 ALA A O 1 ATOM 4139 C CB . ALA A 1 514 ? -10.126 -27.221 -1.009 1.00 31.80 ? 516 ALA A CB 1 ATOM 4140 N N . GLN A 1 515 ? -9.917 -30.331 -0.785 1.00 32.36 ? 517 GLN A N 1 ATOM 4141 C CA . GLN A 1 515 ? -9.155 -31.463 -0.176 1.00 35.04 ? 517 GLN A CA 1 ATOM 4142 C C . GLN A 1 515 ? -8.947 -32.592 -1.194 1.00 32.86 ? 517 GLN A C 1 ATOM 4143 O O . GLN A 1 515 ? -7.867 -33.137 -1.314 1.00 33.75 ? 517 GLN A O 1 ATOM 4144 C CB . GLN A 1 515 ? -9.911 -32.050 1.022 1.00 37.30 ? 517 GLN A CB 1 ATOM 4145 C CG . GLN A 1 515 ? -9.616 -31.503 2.428 1.00 43.70 ? 517 GLN A CG 1 ATOM 4146 C CD . GLN A 1 515 ? -9.639 -32.661 3.443 0.50 47.54 ? 517 GLN A CD 1 ATOM 4147 O OE1 . GLN A 1 515 ? -8.938 -32.634 4.451 0.50 50.27 ? 517 GLN A OE1 1 ATOM 4148 N NE2 . GLN A 1 515 ? -10.424 -33.701 3.141 0.50 46.31 ? 517 GLN A NE2 1 ATOM 4149 N N . GLN A 1 516 ? -9.985 -32.895 -1.965 1.00 30.05 ? 518 GLN A N 1 ATOM 4150 C CA . GLN A 1 516 ? -9.894 -33.900 -3.001 1.00 28.99 ? 518 GLN A CA 1 ATOM 4151 C C . GLN A 1 516 ? -8.906 -33.559 -4.086 1.00 28.63 ? 518 GLN A C 1 ATOM 4152 O O . GLN A 1 516 ? -8.095 -34.387 -4.468 1.00 30.72 ? 518 GLN A O 1 ATOM 4153 C CB . GLN A 1 516 ? -11.285 -34.198 -3.614 1.00 28.86 ? 518 GLN A CB 1 ATOM 4154 C CG . GLN A 1 516 ? -12.304 -34.736 -2.578 1.00 29.18 ? 518 GLN A CG 1 ATOM 4155 C CD . GLN A 1 516 ? -13.162 -33.620 -1.865 1.00 34.70 ? 518 GLN A CD 1 ATOM 4156 O OE1 . GLN A 1 516 ? -14.283 -33.896 -1.464 1.00 40.11 ? 518 GLN A OE1 1 ATOM 4157 N NE2 . GLN A 1 516 ? -12.624 -32.404 -1.682 1.00 31.54 ? 518 GLN A NE2 1 ATOM 4158 N N . CYS A 1 517 ? -8.924 -32.328 -4.565 1.00 27.97 ? 519 CYS A N 1 ATOM 4159 C CA . CYS A 1 517 ? -8.090 -31.911 -5.699 1.00 27.10 ? 519 CYS A CA 1 ATOM 4160 C C . CYS A 1 517 ? -6.639 -31.771 -5.283 1.00 28.88 ? 519 CYS A C 1 ATOM 4161 O O . CYS A 1 517 ? -5.753 -32.090 -6.086 1.00 31.57 ? 519 CYS A O 1 ATOM 4162 C CB . CYS A 1 517 ? -8.667 -30.665 -6.391 1.00 24.35 ? 519 CYS A CB 1 ATOM 4163 S SG . CYS A 1 517 ? -10.200 -31.069 -7.218 1.00 30.17 ? 519 CYS A SG 1 ATOM 4164 N N . ARG A 1 518 ? -6.353 -31.430 -4.019 1.00 29.12 ? 520 ARG A N 1 ATOM 4165 C CA . ARG A 1 518 ? -4.962 -31.523 -3.536 1.00 31.20 ? 520 ARG A CA 1 ATOM 4166 C C . ARG A 1 518 ? -4.389 -32.896 -3.710 1.00 31.75 ? 520 ARG A C 1 ATOM 4167 O O . ARG A 1 518 ? -3.253 -33.014 -4.079 1.00 32.40 ? 520 ARG A O 1 ATOM 4168 C CB . ARG A 1 518 ? -4.830 -31.170 -2.074 1.00 33.95 ? 520 ARG A CB 1 ATOM 4169 C CG . ARG A 1 518 ? -5.009 -29.653 -1.840 1.00 42.01 ? 520 ARG A CG 1 ATOM 4170 C CD . ARG A 1 518 ? -4.673 -29.156 -0.392 1.00 52.01 ? 520 ARG A CD 1 ATOM 4171 N NE . ARG A 1 518 ? -5.782 -28.307 0.108 1.00 58.21 ? 520 ARG A NE 1 ATOM 4172 C CZ . ARG A 1 518 ? -6.577 -28.640 1.130 1.00 59.43 ? 520 ARG A CZ 1 ATOM 4173 N NH1 . ARG A 1 518 ? -7.563 -27.829 1.493 1.00 58.26 ? 520 ARG A NH1 1 ATOM 4174 N NH2 . ARG A 1 518 ? -6.370 -29.784 1.809 1.00 62.59 ? 520 ARG A NH2 1 ATOM 4175 N N . PHE A 1 519 ? -5.204 -33.930 -3.433 1.00 30.89 ? 521 PHE A N 1 ATOM 4176 C CA . PHE A 1 519 ? -4.848 -35.337 -3.626 1.00 31.85 ? 521 PHE A CA 1 ATOM 4177 C C . PHE A 1 519 ? -4.523 -35.653 -5.114 1.00 31.91 ? 521 PHE A C 1 ATOM 4178 O O . PHE A 1 519 ? -3.452 -36.172 -5.434 1.00 32.93 ? 521 PHE A O 1 ATOM 4179 C CB . PHE A 1 519 ? -5.975 -36.329 -3.059 1.00 29.72 ? 521 PHE A CB 1 ATOM 4180 C CG . PHE A 1 519 ? -5.745 -37.776 -3.463 1.00 30.04 ? 521 PHE A CG 1 ATOM 4181 C CD1 . PHE A 1 519 ? -4.753 -38.570 -2.798 1.00 26.35 ? 521 PHE A CD1 1 ATOM 4182 C CD2 . PHE A 1 519 ? -6.476 -38.342 -4.495 1.00 26.40 ? 521 PHE A CD2 1 ATOM 4183 C CE1 . PHE A 1 519 ? -4.528 -39.872 -3.194 1.00 30.78 ? 521 PHE A CE1 1 ATOM 4184 C CE2 . PHE A 1 519 ? -6.240 -39.683 -4.893 1.00 28.58 ? 521 PHE A CE2 1 ATOM 4185 C CZ . PHE A 1 519 ? -5.241 -40.439 -4.243 1.00 26.16 ? 521 PHE A CZ 1 ATOM 4186 N N . TRP A 1 520 ? -5.455 -35.344 -6.015 1.00 31.29 ? 522 TRP A N 1 ATOM 4187 C CA . TRP A 1 520 ? -5.309 -35.738 -7.414 1.00 31.48 ? 522 TRP A CA 1 ATOM 4188 C C . TRP A 1 520 ? -4.229 -34.937 -8.129 1.00 35.76 ? 522 TRP A C 1 ATOM 4189 O O . TRP A 1 520 ? -3.459 -35.460 -8.949 1.00 36.77 ? 522 TRP A O 1 ATOM 4190 C CB . TRP A 1 520 ? -6.651 -35.532 -8.110 1.00 28.47 ? 522 TRP A CB 1 ATOM 4191 C CG . TRP A 1 520 ? -7.645 -36.590 -7.741 1.00 26.45 ? 522 TRP A CG 1 ATOM 4192 C CD1 . TRP A 1 520 ? -8.817 -36.406 -7.063 1.00 26.47 ? 522 TRP A CD1 1 ATOM 4193 C CD2 . TRP A 1 520 ? -7.552 -37.994 -8.006 1.00 25.49 ? 522 TRP A CD2 1 ATOM 4194 N NE1 . TRP A 1 520 ? -9.461 -37.604 -6.879 1.00 25.45 ? 522 TRP A NE1 1 ATOM 4195 C CE2 . TRP A 1 520 ? -8.710 -38.601 -7.456 1.00 27.57 ? 522 TRP A CE2 1 ATOM 4196 C CE3 . TRP A 1 520 ? -6.582 -38.818 -8.623 1.00 29.38 ? 522 TRP A CE3 1 ATOM 4197 C CZ2 . TRP A 1 520 ? -8.941 -39.989 -7.515 1.00 24.68 ? 522 TRP A CZ2 1 ATOM 4198 C CZ3 . TRP A 1 520 ? -6.808 -40.230 -8.656 1.00 27.19 ? 522 TRP A CZ3 1 ATOM 4199 C CH2 . TRP A 1 520 ? -7.981 -40.784 -8.111 1.00 27.87 ? 522 TRP A CH2 1 ATOM 4200 N N . THR A 1 521 ? -4.175 -33.653 -7.783 1.00 38.57 ? 523 THR A N 1 ATOM 4201 C CA . THR A 1 521 ? -3.304 -32.685 -8.433 1.00 42.08 ? 523 THR A CA 1 ATOM 4202 C C . THR A 1 521 ? -1.875 -32.731 -7.946 1.00 45.13 ? 523 THR A C 1 ATOM 4203 O O . THR A 1 521 ? -0.982 -32.575 -8.761 1.00 47.41 ? 523 THR A O 1 ATOM 4204 C CB . THR A 1 521 ? -3.926 -31.227 -8.408 1.00 41.53 ? 523 THR A CB 1 ATOM 4205 O OG1 . THR A 1 521 ? -5.253 -31.274 -8.963 1.00 39.58 ? 523 THR A OG1 1 ATOM 4206 C CG2 . THR A 1 521 ? -3.129 -30.273 -9.260 1.00 44.91 ? 523 THR A CG2 1 ATOM 4207 N N . SER A 1 522 ? -1.613 -32.993 -6.663 1.00 47.24 ? 524 SER A N 1 ATOM 4208 C CA . SER A 1 522 ? -0.227 -32.866 -6.199 1.00 51.10 ? 524 SER A CA 1 ATOM 4209 C C . SER A 1 522 ? 0.322 -34.155 -5.801 1.00 53.19 ? 524 SER A C 1 ATOM 4210 O O . SER A 1 522 ? 1.535 -34.372 -5.909 1.00 58.19 ? 524 SER A O 1 ATOM 4211 C CB . SER A 1 522 ? -0.062 -31.867 -5.024 1.00 52.68 ? 524 SER A CB 1 ATOM 4212 O OG . SER A 1 522 ? -1.000 -30.754 -5.162 1.00 54.32 ? 524 SER A OG 1 ATOM 4213 N N . PHE A 1 523 ? -0.515 -35.028 -5.276 1.00 51.34 ? 525 PHE A N 1 ATOM 4214 C CA . PHE A 1 523 ? 0.014 -36.326 -4.943 1.00 51.56 ? 525 PHE A CA 1 ATOM 4215 C C . PHE A 1 523 ? -0.158 -37.415 -6.043 1.00 50.45 ? 525 PHE A C 1 ATOM 4216 O O . PHE A 1 523 ? 0.809 -38.066 -6.444 1.00 51.92 ? 525 PHE A O 1 ATOM 4217 C CB . PHE A 1 523 ? -0.507 -36.863 -3.629 1.00 51.29 ? 525 PHE A CB 1 ATOM 4218 C CG . PHE A 1 523 ? -0.073 -38.256 -3.417 1.00 56.36 ? 525 PHE A CG 1 ATOM 4219 C CD1 . PHE A 1 523 ? 1.297 -38.530 -3.168 1.00 62.85 ? 525 PHE A CD1 1 ATOM 4220 C CD2 . PHE A 1 523 ? -0.946 -39.298 -3.623 1.00 55.95 ? 525 PHE A CD2 1 ATOM 4221 C CE1 . PHE A 1 523 ? 1.753 -39.815 -3.037 1.00 64.39 ? 525 PHE A CE1 1 ATOM 4222 C CE2 . PHE A 1 523 ? -0.516 -40.612 -3.485 1.00 58.78 ? 525 PHE A CE2 1 ATOM 4223 C CZ . PHE A 1 523 ? 0.812 -40.882 -3.209 1.00 63.60 ? 525 PHE A CZ 1 ATOM 4224 N N . PHE A 1 524 ? -1.377 -37.641 -6.520 1.00 46.80 ? 526 PHE A N 1 ATOM 4225 C CA . PHE A 1 524 ? -1.575 -38.780 -7.449 1.00 44.58 ? 526 PHE A CA 1 ATOM 4226 C C . PHE A 1 524 ? -0.615 -38.870 -8.665 1.00 45.55 ? 526 PHE A C 1 ATOM 4227 O O . PHE A 1 524 ? -0.176 -39.979 -8.998 1.00 46.52 ? 526 PHE A O 1 ATOM 4228 C CB . PHE A 1 524 ? -3.017 -38.881 -7.913 1.00 40.60 ? 526 PHE A CB 1 ATOM 4229 C CG . PHE A 1 524 ? -3.352 -40.222 -8.523 1.00 40.06 ? 526 PHE A CG 1 ATOM 4230 C CD1 . PHE A 1 524 ? -3.381 -41.358 -7.725 1.00 36.34 ? 526 PHE A CD1 1 ATOM 4231 C CD2 . PHE A 1 524 ? -3.614 -40.344 -9.881 1.00 34.78 ? 526 PHE A CD2 1 ATOM 4232 C CE1 . PHE A 1 524 ? -3.656 -42.560 -8.241 1.00 34.36 ? 526 PHE A CE1 1 ATOM 4233 C CE2 . PHE A 1 524 ? -3.925 -41.571 -10.419 1.00 36.57 ? 526 PHE A CE2 1 ATOM 4234 C CZ . PHE A 1 524 ? -3.946 -42.685 -9.584 1.00 37.69 ? 526 PHE A CZ 1 ATOM 4235 N N . PRO A 1 525 ? -0.279 -37.724 -9.324 1.00 45.67 ? 527 PRO A N 1 ATOM 4236 C CA . PRO A 1 525 ? 0.633 -37.799 -10.454 1.00 47.55 ? 527 PRO A CA 1 ATOM 4237 C C . PRO A 1 525 ? 1.984 -38.443 -10.106 1.00 51.63 ? 527 PRO A C 1 ATOM 4238 O O . PRO A 1 525 ? 2.664 -38.876 -11.025 1.00 53.24 ? 527 PRO A O 1 ATOM 4239 C CB . PRO A 1 525 ? 0.854 -36.338 -10.844 1.00 47.18 ? 527 PRO A CB 1 ATOM 4240 C CG . PRO A 1 525 ? -0.409 -35.631 -10.437 1.00 46.32 ? 527 PRO A CG 1 ATOM 4241 C CD . PRO A 1 525 ? -0.789 -36.344 -9.136 1.00 45.19 ? 527 PRO A CD 1 ATOM 4242 N N . LYS A 1 526 ? 2.377 -38.495 -8.824 1.00 52.80 ? 528 LYS A N 1 ATOM 4243 C CA . LYS A 1 526 ? 3.649 -39.112 -8.450 1.00 56.64 ? 528 LYS A CA 1 ATOM 4244 C C . LYS A 1 526 ? 3.589 -40.646 -8.438 1.00 57.92 ? 528 LYS A C 1 ATOM 4245 O O . LYS A 1 526 ? 4.583 -41.337 -8.698 1.00 60.61 ? 528 LYS A O 1 ATOM 4246 C CB . LYS A 1 526 ? 4.143 -38.594 -7.099 1.00 57.79 ? 528 LYS A CB 1 ATOM 4247 C CG . LYS A 1 526 ? 4.408 -37.054 -7.007 1.00 59.32 ? 528 LYS A CG 1 ATOM 4248 C CD . LYS A 1 526 ? 4.230 -36.581 -5.548 1.00 59.25 ? 528 LYS A CD 1 ATOM 4249 C CE . LYS A 1 526 ? 4.931 -35.304 -5.217 1.00 58.84 ? 528 LYS A CE 1 ATOM 4250 N NZ . LYS A 1 526 ? 4.011 -34.173 -5.216 1.00 61.18 ? 528 LYS A NZ 1 ATOM 4251 N N . VAL A 1 527 ? 2.414 -41.173 -8.114 1.00 55.91 ? 529 VAL A N 1 ATOM 4252 C CA . VAL A 1 527 ? 2.184 -42.606 -7.911 1.00 55.98 ? 529 VAL A CA 1 ATOM 4253 C C . VAL A 1 527 ? 2.557 -43.458 -9.147 1.00 57.66 ? 529 VAL A C 1 ATOM 4254 O O . VAL A 1 527 ? 2.591 -42.898 -10.254 1.00 57.41 ? 529 VAL A O 1 ATOM 4255 C CB . VAL A 1 527 ? 0.717 -42.753 -7.529 1.00 53.56 ? 529 VAL A CB 1 ATOM 4256 C CG1 . VAL A 1 527 ? -0.036 -43.790 -8.408 1.00 50.57 ? 529 VAL A CG1 1 ATOM 4257 C CG2 . VAL A 1 527 ? 0.572 -42.947 -6.047 1.00 53.12 ? 529 VAL A CG2 1 ATOM 4258 O OXT . VAL A 1 527 ? 2.850 -44.676 -9.100 1.00 59.01 ? 529 VAL A OXT 1 HETATM 4259 X UNK . UNX B 2 . ? -3.334 -42.042 -21.746 1.00 56.97 ? 1501 UNX A UNK 1 HETATM 4260 X UNK . UNX C 2 . ? -2.976 -50.027 -21.371 1.00 47.51 ? 1502 UNX A UNK 1 HETATM 4261 X UNK . UNX D 2 . ? -1.692 -48.604 -23.061 1.00 47.74 ? 1503 UNX A UNK 1 HETATM 4262 X UNK . UNX E 2 . ? -32.845 -50.884 -5.703 1.00 26.10 ? 1504 UNX A UNK 1 HETATM 4263 X UNK . UNX F 2 . ? -32.204 -52.578 -4.343 1.00 37.47 ? 1505 UNX A UNK 1 HETATM 4264 X UNK . UNX G 2 . ? -31.279 -55.948 -8.918 1.00 23.00 ? 1506 UNX A UNK 1 HETATM 4265 X UNK . UNX H 2 . ? -20.558 -42.393 -21.309 1.00 55.00 ? 1507 UNX A UNK 1 HETATM 4266 X UNK . UNX I 2 . ? -25.479 -32.069 -47.002 1.00 20.30 ? 1508 UNX A UNK 1 HETATM 4267 X UNK . UNX J 2 . ? -27.270 -31.929 -45.743 1.00 29.06 ? 1509 UNX A UNK 1 HETATM 4268 X UNK . UNX K 2 . ? -27.258 -30.086 -46.779 1.00 32.40 ? 1510 UNX A UNK 1 HETATM 4269 X UNK . UNX L 2 . ? -24.296 -35.905 -46.158 1.00 26.92 ? 1511 UNX A UNK 1 HETATM 4270 X UNK . UNX M 2 . ? -24.797 -34.376 -47.933 1.00 33.41 ? 1512 UNX A UNK 1 HETATM 4271 X UNK . UNX N 2 . ? -27.011 -31.016 -51.673 1.00 24.56 ? 1513 UNX A UNK 1 HETATM 4272 X UNK . UNX O 2 . ? -27.309 -32.215 -52.755 1.00 36.23 ? 1514 UNX A UNK 1 HETATM 4273 X UNK . UNX P 2 . ? -28.079 -29.805 -52.777 1.00 34.89 ? 1515 UNX A UNK 1 HETATM 4274 X UNK . UNX Q 2 . ? 2.443 -17.336 -13.088 1.00 34.95 ? 1516 UNX A UNK 1 HETATM 4275 X UNK . UNX R 2 . ? 2.976 -15.544 -13.680 1.00 40.73 ? 1517 UNX A UNK 1 HETATM 4276 X UNK . UNX S 2 . ? 3.150 -13.718 -14.601 1.00 48.69 ? 1518 UNX A UNK 1 HETATM 4277 X UNK . UNX T 2 . ? -32.772 -37.597 -31.519 1.00 51.72 ? 1519 UNX A UNK 1 HETATM 4278 X UNK . UNX U 2 . ? -33.916 -36.099 -32.889 1.00 45.28 ? 1520 UNX A UNK 1 HETATM 4279 X UNK . UNX V 2 . ? -32.903 -37.368 -33.826 1.00 37.03 ? 1521 UNX A UNK 1 HETATM 4280 X UNK . UNX W 2 . ? -16.610 -29.864 -2.199 1.00 23.84 ? 1522 UNX A UNK 1 HETATM 4281 X UNK . UNX X 2 . ? -16.020 -27.873 -1.466 1.00 43.86 ? 1523 UNX A UNK 1 HETATM 4282 C C4 . VR Y 3 . ? -13.639 -39.426 -20.349 1.00 38.06 ? 1530 VR A C4 1 HETATM 4283 C C3 . VR Y 3 . ? -14.308 -39.691 -21.701 1.00 36.70 ? 1530 VR A C3 1 HETATM 4284 C C5 . VR Y 3 . ? -13.489 -40.608 -22.510 1.00 35.50 ? 1530 VR A C5 1 HETATM 4285 C C2 . VR Y 3 . ? -14.327 -38.394 -22.487 1.00 34.13 ? 1530 VR A C2 1 HETATM 4286 O O2 . VR Y 3 . ? -15.379 -37.706 -21.934 1.00 26.44 ? 1530 VR A O2 1 HETATM 4287 P P1 . VR Y 3 . ? -16.364 -36.933 -22.869 1.00 20.72 ? 1530 VR A P1 1 HETATM 4288 C C1 . VR Y 3 . ? -17.963 -37.813 -22.658 1.00 16.42 ? 1530 VR A C1 1 HETATM 4289 O O1 . VR Y 3 . ? -16.189 -36.701 -24.319 1.00 18.50 ? 1530 VR A O1 1 HETATM 4290 N N . GLY Z 4 . ? -32.862 -26.652 -35.766 1.00 39.77 ? 1548 GLY A N 1 HETATM 4291 C CA . GLY Z 4 . ? -32.871 -27.961 -36.424 1.00 41.17 ? 1548 GLY A CA 1 HETATM 4292 C C . GLY Z 4 . ? -34.248 -28.626 -36.466 1.00 42.74 ? 1548 GLY A C 1 HETATM 4293 O O . GLY Z 4 . ? -34.986 -28.565 -35.438 1.00 41.18 ? 1548 GLY A O 1 HETATM 4294 O OXT . GLY Z 4 . ? -34.579 -29.258 -37.525 1.00 42.88 ? 1548 GLY A OXT 1 HETATM 4295 S S . SO4 AA 5 . ? -9.479 -9.573 -19.087 0.50 32.91 ? 1549 SO4 A S 1 HETATM 4296 O O1 . SO4 AA 5 . ? -9.324 -10.968 -19.547 0.50 24.70 ? 1549 SO4 A O1 1 HETATM 4297 O O2 . SO4 AA 5 . ? -10.214 -8.812 -20.057 0.50 27.63 ? 1549 SO4 A O2 1 HETATM 4298 O O3 . SO4 AA 5 . ? -10.206 -9.530 -17.806 0.50 26.92 ? 1549 SO4 A O3 1 HETATM 4299 O O4 . SO4 AA 5 . ? -8.188 -8.934 -18.837 0.50 27.16 ? 1549 SO4 A O4 1 HETATM 4300 S S . SO4 BA 5 . ? -2.880 -34.991 0.549 0.75 65.93 ? 1550 SO4 A S 1 HETATM 4301 O O1 . SO4 BA 5 . ? -1.621 -34.852 -0.216 0.75 61.97 ? 1550 SO4 A O1 1 HETATM 4302 O O2 . SO4 BA 5 . ? -3.963 -34.651 -0.363 0.75 61.44 ? 1550 SO4 A O2 1 HETATM 4303 O O3 . SO4 BA 5 . ? -3.087 -36.350 1.123 0.75 61.32 ? 1550 SO4 A O3 1 HETATM 4304 O O4 . SO4 BA 5 . ? -2.867 -34.036 1.681 0.75 65.74 ? 1550 SO4 A O4 1 HETATM 4305 CA CA . CA CA 6 . ? -22.050 -37.843 -23.046 1.00 73.40 ? 1551 CA A CA 1 HETATM 4306 CA CA . CA DA 6 . ? -30.120 -15.700 -8.977 1.00 61.30 ? 1552 CA A CA 1 HETATM 4307 CA CA . CA EA 6 . ? -21.437 -31.734 -3.590 1.00 66.23 ? 1553 CA A CA 1 HETATM 4308 BR BR . BR FA 7 . ? -8.748 -54.118 3.054 1.00 105.57 ? 1554 BR A BR 1 HETATM 4309 NA NA . NA GA 8 . ? 0.050 -40.327 0.017 0.50 60.33 ? 1555 NA A NA 1 HETATM 4310 C C1 . NAG HA 9 . ? -27.905 -54.399 -8.999 1.00 35.78 ? 1556 NAG A C1 1 HETATM 4311 C C2 . NAG HA 9 . ? -27.686 -55.379 -7.862 1.00 43.67 ? 1556 NAG A C2 1 HETATM 4312 C C3 . NAG HA 9 . ? -26.343 -56.073 -8.035 1.00 46.15 ? 1556 NAG A C3 1 HETATM 4313 C C4 . NAG HA 9 . ? -26.176 -56.820 -9.352 1.00 50.90 ? 1556 NAG A C4 1 HETATM 4314 C C5 . NAG HA 9 . ? -26.445 -55.698 -10.360 1.00 49.76 ? 1556 NAG A C5 1 HETATM 4315 C C6 . NAG HA 9 . ? -26.125 -55.841 -11.852 1.00 56.38 ? 1556 NAG A C6 1 HETATM 4316 C C7 . NAG HA 9 . ? -28.763 -54.530 -5.805 1.00 49.34 ? 1556 NAG A C7 1 HETATM 4317 C C8 . NAG HA 9 . ? -30.023 -55.301 -6.059 1.00 51.27 ? 1556 NAG A C8 1 HETATM 4318 N N2 . NAG HA 9 . ? -27.726 -54.623 -6.641 1.00 44.04 ? 1556 NAG A N2 1 HETATM 4319 O O3 . NAG HA 9 . ? -26.122 -56.939 -6.970 1.00 47.96 ? 1556 NAG A O3 1 HETATM 4320 O O4 . NAG HA 9 . ? -24.847 -57.334 -9.386 1.00 55.24 ? 1556 NAG A O4 1 HETATM 4321 O O5 . NAG HA 9 . ? -27.742 -55.137 -10.191 1.00 44.14 ? 1556 NAG A O5 1 HETATM 4322 O O6 . NAG HA 9 . ? -26.362 -57.063 -12.533 1.00 65.46 ? 1556 NAG A O6 1 HETATM 4323 O O7 . NAG HA 9 . ? -28.706 -53.831 -4.782 1.00 53.13 ? 1556 NAG A O7 1 HETATM 4324 C C1 . NAG IA 9 . ? -24.756 -58.623 -10.034 1.00 66.65 ? 1557 NAG A C1 1 HETATM 4325 C C2 . NAG IA 9 . ? -23.351 -58.776 -10.623 1.00 68.46 ? 1557 NAG A C2 1 HETATM 4326 C C3 . NAG IA 9 . ? -22.971 -60.241 -10.847 1.00 71.44 ? 1557 NAG A C3 1 HETATM 4327 C C4 . NAG IA 9 . ? -23.100 -61.002 -9.533 1.00 75.22 ? 1557 NAG A C4 1 HETATM 4328 C C5 . NAG IA 9 . ? -24.617 -61.061 -9.264 1.00 75.71 ? 1557 NAG A C5 1 HETATM 4329 C C6 . NAG IA 9 . ? -24.871 -61.918 -8.012 1.00 74.83 ? 1557 NAG A C6 1 HETATM 4330 C C7 . NAG IA 9 . ? -22.307 -57.043 -11.998 1.00 71.27 ? 1557 NAG A C7 1 HETATM 4331 C C8 . NAG IA 9 . ? -22.154 -56.348 -13.329 1.00 68.74 ? 1557 NAG A C8 1 HETATM 4332 N N2 . NAG IA 9 . ? -23.185 -58.070 -11.889 1.00 70.69 ? 1557 NAG A N2 1 HETATM 4333 O O3 . NAG IA 9 . ? -21.694 -60.383 -11.427 1.00 69.42 ? 1557 NAG A O3 1 HETATM 4334 O O4 . NAG IA 9 . ? -22.491 -62.298 -9.573 1.00 79.73 ? 1557 NAG A O4 1 HETATM 4335 O O5 . NAG IA 9 . ? -25.184 -59.718 -9.165 1.00 74.17 ? 1557 NAG A O5 1 HETATM 4336 O O6 . NAG IA 9 . ? -26.213 -61.816 -7.572 1.00 72.76 ? 1557 NAG A O6 1 HETATM 4337 O O7 . NAG IA 9 . ? -21.633 -56.642 -11.040 1.00 70.37 ? 1557 NAG A O7 1 HETATM 4338 C C1 . FUL JA 10 . ? -27.777 -57.397 -12.528 1.00 71.97 ? 1558 FUL A C1 1 HETATM 4339 C C2 . FUL JA 10 . ? -28.178 -58.769 -13.104 1.00 75.84 ? 1558 FUL A C2 1 HETATM 4340 O O2 . FUL JA 10 . ? -27.106 -59.708 -13.189 1.00 73.10 ? 1558 FUL A O2 1 HETATM 4341 C C3 . FUL JA 10 . ? -29.312 -59.134 -12.119 1.00 76.64 ? 1558 FUL A C3 1 HETATM 4342 O O3 . FUL JA 10 . ? -29.787 -60.434 -12.330 1.00 79.04 ? 1558 FUL A O3 1 HETATM 4343 C C4 . FUL JA 10 . ? -30.446 -58.086 -12.210 1.00 76.46 ? 1558 FUL A C4 1 HETATM 4344 O O4 . FUL JA 10 . ? -31.066 -58.192 -13.478 1.00 76.97 ? 1558 FUL A O4 1 HETATM 4345 C C5 . FUL JA 10 . ? -29.867 -56.654 -12.047 1.00 75.35 ? 1558 FUL A C5 1 HETATM 4346 C C6 . FUL JA 10 . ? -30.892 -55.498 -12.074 1.00 73.18 ? 1558 FUL A C6 1 HETATM 4347 O O5 . FUL JA 10 . ? -28.773 -56.476 -12.961 1.00 72.21 ? 1558 FUL A O5 1 HETATM 4348 C C1 . NAG KA 9 . ? -19.010 -5.530 -36.754 1.00 54.55 ? 1559 NAG A C1 1 HETATM 4349 C C2 . NAG KA 9 . ? -18.756 -4.503 -37.901 1.00 61.59 ? 1559 NAG A C2 1 HETATM 4350 C C3 . NAG KA 9 . ? -17.221 -4.330 -38.044 1.00 62.55 ? 1559 NAG A C3 1 HETATM 4351 C C4 . NAG KA 9 . ? -16.579 -3.900 -36.702 1.00 62.78 ? 1559 NAG A C4 1 HETATM 4352 C C5 . NAG KA 9 . ? -16.963 -4.967 -35.627 1.00 61.77 ? 1559 NAG A C5 1 HETATM 4353 C C6 . NAG KA 9 . ? -16.358 -4.784 -34.222 1.00 61.68 ? 1559 NAG A C6 1 HETATM 4354 C C7 . NAG KA 9 . ? -20.685 -4.528 -39.597 1.00 64.18 ? 1559 NAG A C7 1 HETATM 4355 C C8 . NAG KA 9 . ? -21.663 -3.717 -38.780 1.00 62.13 ? 1559 NAG A C8 1 HETATM 4356 N N2 . NAG KA 9 . ? -19.432 -4.834 -39.176 1.00 61.77 ? 1559 NAG A N2 1 HETATM 4357 O O3 . NAG KA 9 . ? -16.868 -3.501 -39.131 1.00 63.47 ? 1559 NAG A O3 1 HETATM 4358 O O4 . NAG KA 9 . ? -15.171 -3.730 -36.849 1.00 64.11 ? 1559 NAG A O4 1 HETATM 4359 O O5 . NAG KA 9 . ? -18.400 -5.108 -35.518 1.00 59.66 ? 1559 NAG A O5 1 HETATM 4360 O O6 . NAG KA 9 . ? -16.565 -5.912 -33.376 1.00 58.20 ? 1559 NAG A O6 1 HETATM 4361 O O7 . NAG KA 9 . ? -21.074 -4.893 -40.715 1.00 67.90 ? 1559 NAG A O7 1 HETATM 4362 C C1 . NAG LA 9 . ? -32.965 -27.657 -53.891 1.00 63.67 ? 1560 NAG A C1 1 HETATM 4363 C C2 . NAG LA 9 . ? -33.010 -28.556 -55.115 1.00 71.48 ? 1560 NAG A C2 1 HETATM 4364 C C3 . NAG LA 9 . ? -33.799 -27.816 -56.194 1.00 73.64 ? 1560 NAG A C3 1 HETATM 4365 C C4 . NAG LA 9 . ? -35.230 -27.540 -55.702 1.00 75.71 ? 1560 NAG A C4 1 HETATM 4366 C C5 . NAG LA 9 . ? -35.357 -27.036 -54.237 1.00 74.53 ? 1560 NAG A C5 1 HETATM 4367 C C6 . NAG LA 9 . ? -36.699 -27.474 -53.598 1.00 74.38 ? 1560 NAG A C6 1 HETATM 4368 C C7 . NAG LA 9 . ? -31.319 -30.351 -55.536 1.00 68.71 ? 1560 NAG A C7 1 HETATM 4369 C C8 . NAG LA 9 . ? -32.310 -31.439 -55.186 1.00 68.34 ? 1560 NAG A C8 1 HETATM 4370 N N2 . NAG LA 9 . ? -31.677 -29.051 -55.499 1.00 69.79 ? 1560 NAG A N2 1 HETATM 4371 O O3 . NAG LA 9 . ? -33.878 -28.613 -57.357 1.00 75.36 ? 1560 NAG A O3 1 HETATM 4372 O O4 . NAG LA 9 . ? -35.886 -26.685 -56.634 1.00 78.36 ? 1560 NAG A O4 1 HETATM 4373 O O5 . NAG LA 9 . ? -34.311 -27.558 -53.404 1.00 71.21 ? 1560 NAG A O5 1 HETATM 4374 O O6 . NAG LA 9 . ? -37.518 -26.364 -53.272 1.00 76.82 ? 1560 NAG A O6 1 HETATM 4375 O O7 . NAG LA 9 . ? -30.177 -30.683 -55.848 1.00 67.76 ? 1560 NAG A O7 1 HETATM 4376 C C1 . NAG MA 9 . ? -36.284 -11.834 -16.205 1.00 59.60 ? 1561 NAG A C1 1 HETATM 4377 C C2 . NAG MA 9 . ? -36.147 -13.045 -17.147 1.00 62.60 ? 1561 NAG A C2 1 HETATM 4378 C C3 . NAG MA 9 . ? -37.437 -13.458 -17.895 1.00 67.28 ? 1561 NAG A C3 1 HETATM 4379 C C4 . NAG MA 9 . ? -38.718 -13.248 -17.037 1.00 70.40 ? 1561 NAG A C4 1 HETATM 4380 C C5 . NAG MA 9 . ? -38.727 -11.799 -16.488 1.00 71.08 ? 1561 NAG A C5 1 HETATM 4381 C C6 . NAG MA 9 . ? -40.054 -11.265 -15.846 1.00 73.99 ? 1561 NAG A C6 1 HETATM 4382 C C7 . NAG MA 9 . ? -33.872 -13.609 -17.872 1.00 51.74 ? 1561 NAG A C7 1 HETATM 4383 C C8 . NAG MA 9 . ? -32.784 -13.345 -18.862 1.00 47.37 ? 1561 NAG A C8 1 HETATM 4384 N N2 . NAG MA 9 . ? -35.008 -12.888 -18.038 1.00 57.10 ? 1561 NAG A N2 1 HETATM 4385 O O3 . NAG MA 9 . ? -37.327 -14.847 -18.185 1.00 69.02 ? 1561 NAG A O3 1 HETATM 4386 O O4 . NAG MA 9 . ? -39.899 -13.602 -17.760 1.00 72.76 ? 1561 NAG A O4 1 HETATM 4387 O O5 . NAG MA 9 . ? -37.599 -11.720 -15.611 1.00 66.41 ? 1561 NAG A O5 1 HETATM 4388 O O6 . NAG MA 9 . ? -40.085 -11.238 -14.413 1.00 74.59 ? 1561 NAG A O6 1 HETATM 4389 O O7 . NAG MA 9 . ? -33.670 -14.444 -16.974 1.00 49.17 ? 1561 NAG A O7 1 HETATM 4390 C C1 . NAG NA 9 . ? 8.605 -46.038 -48.555 1.00 76.02 ? 1562 NAG A C1 1 HETATM 4391 C C2 . NAG NA 9 . ? 9.790 -45.086 -48.875 1.00 84.05 ? 1562 NAG A C2 1 HETATM 4392 C C3 . NAG NA 9 . ? 9.296 -43.731 -49.468 1.00 84.87 ? 1562 NAG A C3 1 HETATM 4393 C C4 . NAG NA 9 . ? 8.232 -43.930 -50.572 1.00 85.36 ? 1562 NAG A C4 1 HETATM 4394 C C5 . NAG NA 9 . ? 7.101 -44.786 -49.978 1.00 83.38 ? 1562 NAG A C5 1 HETATM 4395 C C6 . NAG NA 9 . ? 5.831 -44.841 -50.854 1.00 83.75 ? 1562 NAG A C6 1 HETATM 4396 C C7 . NAG NA 9 . ? 11.394 -45.799 -47.055 1.00 90.54 ? 1562 NAG A C7 1 HETATM 4397 C C8 . NAG NA 9 . ? 12.213 -45.311 -45.877 1.00 90.76 ? 1562 NAG A C8 1 HETATM 4398 N N2 . NAG NA 9 . ? 10.667 -44.869 -47.715 1.00 86.64 ? 1562 NAG A N2 1 HETATM 4399 O O3 . NAG NA 9 . ? 10.353 -42.917 -49.967 1.00 85.56 ? 1562 NAG A O3 1 HETATM 4400 O O4 . NAG NA 9 . ? 7.770 -42.697 -51.134 1.00 86.59 ? 1562 NAG A O4 1 HETATM 4401 O O5 . NAG NA 9 . ? 7.668 -46.059 -49.653 1.00 80.02 ? 1562 NAG A O5 1 HETATM 4402 O O6 . NAG NA 9 . ? 5.816 -45.955 -51.724 1.00 84.94 ? 1562 NAG A O6 1 HETATM 4403 O O7 . NAG NA 9 . ? 11.419 -47.009 -47.348 1.00 92.07 ? 1562 NAG A O7 1 HETATM 4404 C C1 . NAG OA 9 . ? 1.498 -51.889 -26.640 1.00 66.75 ? 1563 NAG A C1 1 HETATM 4405 C C2 . NAG OA 9 . ? 1.481 -52.005 -25.115 1.00 76.17 ? 1563 NAG A C2 1 HETATM 4406 C C3 . NAG OA 9 . ? 1.816 -53.397 -24.578 1.00 77.50 ? 1563 NAG A C3 1 HETATM 4407 C C4 . NAG OA 9 . ? 1.234 -54.505 -25.463 1.00 79.80 ? 1563 NAG A C4 1 HETATM 4408 C C5 . NAG OA 9 . ? 1.743 -54.358 -26.902 1.00 76.18 ? 1563 NAG A C5 1 HETATM 4409 C C6 . NAG OA 9 . ? 0.824 -55.031 -27.918 1.00 76.39 ? 1563 NAG A C6 1 HETATM 4410 C C7 . NAG OA 9 . ? 1.850 -49.964 -23.729 1.00 86.55 ? 1563 NAG A C7 1 HETATM 4411 C C8 . NAG OA 9 . ? 0.460 -50.141 -23.143 1.00 86.97 ? 1563 NAG A C8 1 HETATM 4412 N N2 . NAG OA 9 . ? 2.289 -50.886 -24.621 1.00 81.94 ? 1563 NAG A N2 1 HETATM 4413 O O3 . NAG OA 9 . ? 1.264 -53.552 -23.284 1.00 74.49 ? 1563 NAG A O3 1 HETATM 4414 O O4 . NAG OA 9 . ? 1.596 -55.812 -24.988 1.00 86.81 ? 1563 NAG A O4 1 HETATM 4415 O O5 . NAG OA 9 . ? 2.009 -53.019 -27.332 1.00 73.20 ? 1563 NAG A O5 1 HETATM 4416 O O6 . NAG OA 9 . ? 0.042 -56.062 -27.327 1.00 77.20 ? 1563 NAG A O6 1 HETATM 4417 O O7 . NAG OA 9 . ? 2.546 -48.995 -23.361 1.00 88.60 ? 1563 NAG A O7 1 HETATM 4418 C C1 . NAG PA 9 . ? 0.594 -56.551 -24.228 1.00 93.40 ? 1564 NAG A C1 1 HETATM 4419 C C2 . NAG PA 9 . ? 0.204 -57.931 -24.875 1.00 97.14 ? 1564 NAG A C2 1 HETATM 4420 C C3 . NAG PA 9 . ? 1.334 -58.937 -24.630 1.00 98.10 ? 1564 NAG A C3 1 HETATM 4421 C C4 . NAG PA 9 . ? 1.447 -59.143 -23.098 1.00 99.48 ? 1564 NAG A C4 1 HETATM 4422 C C5 . NAG PA 9 . ? 0.816 -57.965 -22.297 1.00 98.84 ? 1564 NAG A C5 1 HETATM 4423 C C6 . NAG PA 9 . ? 1.155 -57.947 -20.806 1.00 99.24 ? 1564 NAG A C6 1 HETATM 4424 C C7 . NAG PA 9 . ? -1.857 -59.566 -24.692 1.00 101.28 ? 1564 NAG A C7 1 HETATM 4425 C C8 . NAG PA 9 . ? -3.115 -59.718 -23.875 1.00 101.02 ? 1564 NAG A C8 1 HETATM 4426 N N2 . NAG PA 9 . ? -1.101 -58.470 -24.372 1.00 100.49 ? 1564 NAG A N2 1 HETATM 4427 O O3 . NAG PA 9 . ? 2.540 -58.491 -25.250 1.00 95.45 ? 1564 NAG A O3 1 HETATM 4428 O O4 . NAG PA 9 . ? 0.765 -60.343 -22.745 1.00 100.63 ? 1564 NAG A O4 1 HETATM 4429 O O5 . NAG PA 9 . ? 1.049 -56.672 -22.881 1.00 95.24 ? 1564 NAG A O5 1 HETATM 4430 O O6 . NAG PA 9 . ? 0.588 -56.745 -20.318 1.00 99.80 ? 1564 NAG A O6 1 HETATM 4431 O O7 . NAG PA 9 . ? -1.624 -60.416 -25.569 1.00 100.47 ? 1564 NAG A O7 1 HETATM 4432 C C1 . FUL QA 10 . ? -1.267 -56.098 -27.941 1.00 77.51 ? 1565 FUL A C1 1 HETATM 4433 C C2 . FUL QA 10 . ? -2.429 -56.647 -27.105 1.00 78.28 ? 1565 FUL A C2 1 HETATM 4434 O O2 . FUL QA 10 . ? -2.356 -56.349 -25.730 1.00 80.49 ? 1565 FUL A O2 1 HETATM 4435 C C3 . FUL QA 10 . ? -3.649 -55.899 -27.625 1.00 78.80 ? 1565 FUL A C3 1 HETATM 4436 O O3 . FUL QA 10 . ? -4.819 -56.337 -26.931 1.00 78.80 ? 1565 FUL A O3 1 HETATM 4437 C C4 . FUL QA 10 . ? -3.722 -55.947 -29.173 1.00 78.29 ? 1565 FUL A C4 1 HETATM 4438 O O4 . FUL QA 10 . ? -4.495 -57.070 -29.556 1.00 80.67 ? 1565 FUL A O4 1 HETATM 4439 C C5 . FUL QA 10 . ? -2.332 -55.851 -29.890 1.00 77.42 ? 1565 FUL A C5 1 HETATM 4440 C C6 . FUL QA 10 . ? -2.294 -56.041 -31.410 1.00 75.56 ? 1565 FUL A C6 1 HETATM 4441 O O5 . FUL QA 10 . ? -1.360 -56.648 -29.247 1.00 75.89 ? 1565 FUL A O5 1 HETATM 4442 CL CL . CL RA 11 . ? -19.365 -12.503 -1.843 1.00 64.88 ? 1566 CL A CL 1 HETATM 4443 NA NA . NA SA 8 . ? -16.463 -49.615 6.295 1.00 63.12 ? 1567 NA A NA 1 HETATM 4444 O O . HOH TA 12 . ? -40.121 -18.143 -48.193 1.00 52.24 ? 2001 HOH A O 1 HETATM 4445 O O . HOH TA 12 . ? -32.988 -15.479 -50.415 1.00 21.82 ? 2002 HOH A O 1 HETATM 4446 O O . HOH TA 12 . ? -12.417 -22.310 -45.564 1.00 39.44 ? 2003 HOH A O 1 HETATM 4447 O O . HOH TA 12 . ? -14.222 -20.949 -47.596 1.00 19.94 ? 2004 HOH A O 1 HETATM 4448 O O . HOH TA 12 . ? -26.244 -14.113 -58.473 1.00 19.65 ? 2005 HOH A O 1 HETATM 4449 O O . HOH TA 12 . ? -33.748 -37.472 -29.003 1.00 36.68 ? 2006 HOH A O 1 HETATM 4450 O O . HOH TA 12 . ? -15.223 -36.342 -52.988 1.00 28.77 ? 2007 HOH A O 1 HETATM 4451 O O . HOH TA 12 . ? -18.894 -46.337 -27.846 1.00 29.64 ? 2008 HOH A O 1 HETATM 4452 O O . HOH TA 12 . ? -16.931 -45.119 -27.367 1.00 42.30 ? 2009 HOH A O 1 HETATM 4453 O O . HOH TA 12 . ? -38.144 -22.556 -45.876 1.00 17.36 ? 2010 HOH A O 1 HETATM 4454 O O . HOH TA 12 . ? -38.783 -25.235 -35.179 1.00 20.38 ? 2011 HOH A O 1 HETATM 4455 O O . HOH TA 12 . ? -2.033 -29.840 -45.282 1.00 43.76 ? 2012 HOH A O 1 HETATM 4456 O O . HOH TA 12 . ? -40.938 -25.757 -38.347 1.00 24.40 ? 2013 HOH A O 1 HETATM 4457 O O . HOH TA 12 . ? -41.267 -23.019 -30.844 1.00 13.27 ? 2014 HOH A O 1 HETATM 4458 O O . HOH TA 12 . ? -44.237 -21.281 -32.047 1.00 16.81 ? 2015 HOH A O 1 HETATM 4459 O O . HOH TA 12 . ? -22.437 -41.499 -23.932 1.00 38.76 ? 2016 HOH A O 1 HETATM 4460 O O . HOH TA 12 . ? -22.320 -42.536 -26.928 1.00 56.78 ? 2017 HOH A O 1 HETATM 4461 O O . HOH TA 12 . ? -32.292 -35.841 -26.968 1.00 31.52 ? 2018 HOH A O 1 HETATM 4462 O O . HOH TA 12 . ? -34.537 -35.918 -21.856 1.00 29.95 ? 2019 HOH A O 1 HETATM 4463 O O . HOH TA 12 . ? -17.411 -31.987 -47.174 1.00 7.24 ? 2020 HOH A O 1 HETATM 4464 O O . HOH TA 12 . ? 1.440 -16.919 -26.325 1.00 50.86 ? 2021 HOH A O 1 HETATM 4465 O O . HOH TA 12 . ? -12.845 -33.997 -52.941 1.00 34.07 ? 2022 HOH A O 1 HETATM 4466 O O . HOH TA 12 . ? -20.242 -44.188 -26.715 1.00 37.36 ? 2023 HOH A O 1 HETATM 4467 O O . HOH TA 12 . ? -12.573 -36.461 -51.728 1.00 16.42 ? 2024 HOH A O 1 HETATM 4468 O O . HOH TA 12 . ? 6.385 -34.838 -27.198 1.00 32.65 ? 2025 HOH A O 1 HETATM 4469 O O . HOH TA 12 . ? -10.692 -38.380 -52.332 1.00 15.31 ? 2026 HOH A O 1 HETATM 4470 O O . HOH TA 12 . ? -19.848 -46.498 -44.106 1.00 45.80 ? 2027 HOH A O 1 HETATM 4471 O O . HOH TA 12 . ? -18.936 -46.839 -41.803 1.00 44.00 ? 2028 HOH A O 1 HETATM 4472 O O . HOH TA 12 . ? -6.427 -45.008 -50.980 1.00 24.49 ? 2029 HOH A O 1 HETATM 4473 O O . HOH TA 12 . ? -8.371 -41.821 -53.960 1.00 9.48 ? 2030 HOH A O 1 HETATM 4474 O O . HOH TA 12 . ? -17.801 -31.178 -52.118 1.00 28.40 ? 2031 HOH A O 1 HETATM 4475 O O . HOH TA 12 . ? -8.253 -35.473 -45.650 1.00 10.39 ? 2032 HOH A O 1 HETATM 4476 O O . HOH TA 12 . ? -12.557 -48.186 -48.036 1.00 16.41 ? 2033 HOH A O 1 HETATM 4477 O O . HOH TA 12 . ? -2.758 -26.769 -41.323 1.00 28.66 ? 2034 HOH A O 1 HETATM 4478 O O . HOH TA 12 . ? 0.247 -29.442 -44.033 1.00 29.33 ? 2035 HOH A O 1 HETATM 4479 O O . HOH TA 12 . ? -5.838 -28.731 -42.842 1.00 16.71 ? 2036 HOH A O 1 HETATM 4480 O O . HOH TA 12 . ? -9.893 -33.546 -47.088 1.00 12.89 ? 2037 HOH A O 1 HETATM 4481 O O . HOH TA 12 . ? -6.140 -27.018 -47.619 1.00 23.36 ? 2038 HOH A O 1 HETATM 4482 O O . HOH TA 12 . ? -15.821 -46.185 -29.590 1.00 30.91 ? 2039 HOH A O 1 HETATM 4483 O O . HOH TA 12 . ? -21.175 -38.133 -25.021 1.00 31.76 ? 2040 HOH A O 1 HETATM 4484 O O . HOH TA 12 . ? -19.310 -40.986 -23.171 1.00 48.05 ? 2041 HOH A O 1 HETATM 4485 O O . HOH TA 12 . ? -16.918 -42.275 -23.889 1.00 51.28 ? 2042 HOH A O 1 HETATM 4486 O O . HOH TA 12 . ? -12.609 -25.381 -47.411 1.00 29.28 ? 2043 HOH A O 1 HETATM 4487 O O . HOH TA 12 . ? -11.551 -23.193 -56.667 1.00 30.74 ? 2044 HOH A O 1 HETATM 4488 O O . HOH TA 12 . ? -13.793 -31.566 -53.101 1.00 41.54 ? 2045 HOH A O 1 HETATM 4489 O O . HOH TA 12 . ? -16.191 -27.402 -54.255 1.00 32.03 ? 2046 HOH A O 1 HETATM 4490 O O . HOH TA 12 . ? -15.759 -20.745 -61.531 1.00 21.66 ? 2047 HOH A O 1 HETATM 4491 O O . HOH TA 12 . ? -37.296 -31.100 -32.761 1.00 44.36 ? 2048 HOH A O 1 HETATM 4492 O O . HOH TA 12 . ? -23.275 -21.367 -56.259 1.00 15.61 ? 2049 HOH A O 1 HETATM 4493 O O . HOH TA 12 . ? -31.845 -31.151 -52.142 1.00 25.17 ? 2050 HOH A O 1 HETATM 4494 O O . HOH TA 12 . ? -34.436 -31.465 -41.967 1.00 45.81 ? 2051 HOH A O 1 HETATM 4495 O O . HOH TA 12 . ? -32.333 -33.013 -40.934 1.00 16.72 ? 2052 HOH A O 1 HETATM 4496 O O . HOH TA 12 . ? -27.929 -36.669 -44.532 1.00 23.39 ? 2053 HOH A O 1 HETATM 4497 O O . HOH TA 12 . ? -40.175 -32.960 -10.798 1.00 46.25 ? 2054 HOH A O 1 HETATM 4498 O O . HOH TA 12 . ? -24.807 -34.703 -38.693 1.00 13.93 ? 2055 HOH A O 1 HETATM 4499 O O . HOH TA 12 . ? 0.662 -33.443 -42.144 1.00 31.61 ? 2056 HOH A O 1 HETATM 4500 O O . HOH TA 12 . ? -23.096 -39.724 -48.533 1.00 40.04 ? 2057 HOH A O 1 HETATM 4501 O O . HOH TA 12 . ? -26.019 -41.146 -47.002 1.00 19.48 ? 2058 HOH A O 1 HETATM 4502 O O . HOH TA 12 . ? -19.838 -36.823 -36.606 1.00 17.96 ? 2059 HOH A O 1 HETATM 4503 O O . HOH TA 12 . ? -15.110 -41.077 -40.415 1.00 15.86 ? 2060 HOH A O 1 HETATM 4504 O O . HOH TA 12 . ? -37.978 -15.500 -26.300 1.00 33.35 ? 2061 HOH A O 1 HETATM 4505 O O . HOH TA 12 . ? -20.604 -48.172 -36.666 1.00 23.65 ? 2062 HOH A O 1 HETATM 4506 O O . HOH TA 12 . ? -21.395 -43.392 -31.472 1.00 12.08 ? 2063 HOH A O 1 HETATM 4507 O O . HOH TA 12 . ? -12.227 -10.343 -39.434 1.00 47.37 ? 2064 HOH A O 1 HETATM 4508 O O . HOH TA 12 . ? -15.938 -10.802 -43.432 1.00 30.54 ? 2065 HOH A O 1 HETATM 4509 O O . HOH TA 12 . ? -20.286 -50.214 -32.759 1.00 45.20 ? 2066 HOH A O 1 HETATM 4510 O O . HOH TA 12 . ? -24.433 -43.328 -24.941 1.00 16.65 ? 2067 HOH A O 1 HETATM 4511 O O . HOH TA 12 . ? -26.446 -50.079 -30.452 1.00 34.78 ? 2068 HOH A O 1 HETATM 4512 O O . HOH TA 12 . ? -15.052 -15.106 -0.364 0.50 10.12 ? 2069 HOH A O 1 HETATM 4513 O O . HOH TA 12 . ? -20.840 -49.309 -24.928 1.00 34.86 ? 2070 HOH A O 1 HETATM 4514 O O . HOH TA 12 . ? -27.115 -48.149 -25.402 1.00 22.60 ? 2071 HOH A O 1 HETATM 4515 O O . HOH TA 12 . ? -31.720 -52.054 -22.834 1.00 22.50 ? 2072 HOH A O 1 HETATM 4516 O O . HOH TA 12 . ? -33.454 -35.416 -24.495 1.00 38.73 ? 2073 HOH A O 1 HETATM 4517 O O . HOH TA 12 . ? -33.446 -41.741 -27.811 1.00 31.90 ? 2074 HOH A O 1 HETATM 4518 O O . HOH TA 12 . ? -36.242 -45.189 -22.515 1.00 25.80 ? 2075 HOH A O 1 HETATM 4519 O O . HOH TA 12 . ? -32.688 -49.657 -30.184 1.00 31.74 ? 2076 HOH A O 1 HETATM 4520 O O . HOH TA 12 . ? -30.360 -43.858 -31.579 1.00 41.21 ? 2077 HOH A O 1 HETATM 4521 O O . HOH TA 12 . ? -34.085 -44.621 -27.044 1.00 33.47 ? 2078 HOH A O 1 HETATM 4522 O O . HOH TA 12 . ? -28.600 -48.621 -28.619 1.00 30.33 ? 2079 HOH A O 1 HETATM 4523 O O . HOH TA 12 . ? -0.363 -18.407 -29.064 1.00 51.66 ? 2080 HOH A O 1 HETATM 4524 O O . HOH TA 12 . ? -30.002 -35.667 -28.296 1.00 23.19 ? 2081 HOH A O 1 HETATM 4525 O O . HOH TA 12 . ? -22.614 -38.210 -28.704 1.00 9.03 ? 2082 HOH A O 1 HETATM 4526 O O . HOH TA 12 . ? -22.420 -43.200 -29.138 1.00 32.77 ? 2083 HOH A O 1 HETATM 4527 O O . HOH TA 12 . ? -29.609 -39.375 -30.842 1.00 27.67 ? 2084 HOH A O 1 HETATM 4528 O O . HOH TA 12 . ? -28.877 -45.988 -30.785 1.00 41.33 ? 2085 HOH A O 1 HETATM 4529 O O . HOH TA 12 . ? -32.284 -40.494 -38.439 1.00 26.06 ? 2086 HOH A O 1 HETATM 4530 O O . HOH TA 12 . ? -32.148 -36.412 -39.047 1.00 31.78 ? 2087 HOH A O 1 HETATM 4531 O O . HOH TA 12 . ? -1.646 -33.609 -17.749 1.00 37.28 ? 2088 HOH A O 1 HETATM 4532 O O . HOH TA 12 . ? -1.394 -29.445 -16.790 1.00 21.58 ? 2089 HOH A O 1 HETATM 4533 O O . HOH TA 12 . ? -2.646 -35.839 -17.234 1.00 41.77 ? 2090 HOH A O 1 HETATM 4534 O O . HOH TA 12 . ? -29.929 -40.024 -42.033 1.00 28.87 ? 2091 HOH A O 1 HETATM 4535 O O . HOH TA 12 . ? -26.500 -45.392 -42.991 1.00 17.15 ? 2092 HOH A O 1 HETATM 4536 O O . HOH TA 12 . ? -29.937 -41.540 -45.632 1.00 25.14 ? 2093 HOH A O 1 HETATM 4537 O O . HOH TA 12 . ? -27.422 -38.627 -43.619 1.00 15.73 ? 2094 HOH A O 1 HETATM 4538 O O . HOH TA 12 . ? 4.512 -36.398 -25.854 1.00 40.96 ? 2095 HOH A O 1 HETATM 4539 O O . HOH TA 12 . ? -18.882 -44.842 -41.483 1.00 7.78 ? 2096 HOH A O 1 HETATM 4540 O O . HOH TA 12 . ? -22.174 -42.566 -48.263 1.00 55.50 ? 2097 HOH A O 1 HETATM 4541 O O . HOH TA 12 . ? -18.018 -43.926 -46.106 1.00 17.52 ? 2098 HOH A O 1 HETATM 4542 O O . HOH TA 12 . ? -11.954 -43.833 -47.888 1.00 13.85 ? 2099 HOH A O 1 HETATM 4543 O O . HOH TA 12 . ? -11.933 -40.637 -43.727 1.00 7.37 ? 2100 HOH A O 1 HETATM 4544 O O . HOH TA 12 . ? -14.010 -39.434 -42.327 1.00 5.74 ? 2101 HOH A O 1 HETATM 4545 O O . HOH TA 12 . ? -15.970 -45.128 -47.079 1.00 22.26 ? 2102 HOH A O 1 HETATM 4546 O O . HOH TA 12 . ? -20.264 -35.411 -51.191 1.00 26.87 ? 2103 HOH A O 1 HETATM 4547 O O . HOH TA 12 . ? -17.069 -34.681 -46.278 1.00 8.75 ? 2104 HOH A O 1 HETATM 4548 O O . HOH TA 12 . ? -20.784 -39.931 -49.942 1.00 32.92 ? 2105 HOH A O 1 HETATM 4549 O O . HOH TA 12 . ? -18.771 -32.447 -49.677 1.00 18.39 ? 2106 HOH A O 1 HETATM 4550 O O . HOH TA 12 . ? -25.054 -31.453 -40.543 1.00 18.75 ? 2107 HOH A O 1 HETATM 4551 O O . HOH TA 12 . ? -32.682 -15.086 -41.135 1.00 22.89 ? 2108 HOH A O 1 HETATM 4552 O O . HOH TA 12 . ? -18.545 -49.427 -43.160 1.00 47.72 ? 2109 HOH A O 1 HETATM 4553 O O . HOH TA 12 . ? -38.090 -14.104 -35.658 1.00 35.29 ? 2110 HOH A O 1 HETATM 4554 O O . HOH TA 12 . ? -34.325 -13.554 -42.792 1.00 29.82 ? 2111 HOH A O 1 HETATM 4555 O O . HOH TA 12 . ? -33.980 -11.329 -43.754 1.00 36.11 ? 2112 HOH A O 1 HETATM 4556 O O . HOH TA 12 . ? -26.725 -8.532 -42.301 1.00 22.96 ? 2113 HOH A O 1 HETATM 4557 O O . HOH TA 12 . ? -9.466 -54.151 -24.152 1.00 39.31 ? 2114 HOH A O 1 HETATM 4558 O O . HOH TA 12 . ? -26.872 -7.738 -34.768 1.00 40.93 ? 2115 HOH A O 1 HETATM 4559 O O . HOH TA 12 . ? -23.738 -6.382 -32.681 1.00 22.75 ? 2116 HOH A O 1 HETATM 4560 O O . HOH TA 12 . ? -20.989 -8.738 -32.499 1.00 19.01 ? 2117 HOH A O 1 HETATM 4561 O O . HOH TA 12 . ? -18.752 -8.222 -40.239 1.00 37.57 ? 2118 HOH A O 1 HETATM 4562 O O . HOH TA 12 . ? -17.454 -48.375 -22.397 1.00 36.18 ? 2119 HOH A O 1 HETATM 4563 O O . HOH TA 12 . ? -20.555 -44.262 -23.211 1.00 49.61 ? 2120 HOH A O 1 HETATM 4564 O O . HOH TA 12 . ? -22.386 -8.061 -30.172 1.00 34.40 ? 2121 HOH A O 1 HETATM 4565 O O . HOH TA 12 . ? -25.261 -10.498 -31.180 1.00 32.46 ? 2122 HOH A O 1 HETATM 4566 O O . HOH TA 12 . ? -19.805 -29.726 -32.967 1.00 15.00 ? 2123 HOH A O 1 HETATM 4567 O O . HOH TA 12 . ? 2.795 -28.587 -15.221 1.00 36.91 ? 2124 HOH A O 1 HETATM 4568 O O . HOH TA 12 . ? 0.837 -36.355 -22.711 1.00 44.06 ? 2125 HOH A O 1 HETATM 4569 O O . HOH TA 12 . ? -9.424 -11.564 -28.029 1.00 35.30 ? 2126 HOH A O 1 HETATM 4570 O O . HOH TA 12 . ? -15.420 -44.791 -32.882 1.00 24.12 ? 2127 HOH A O 1 HETATM 4571 O O . HOH TA 12 . ? -21.098 -40.276 -27.401 1.00 26.51 ? 2128 HOH A O 1 HETATM 4572 O O . HOH TA 12 . ? -15.692 -36.656 -29.431 1.00 7.15 ? 2129 HOH A O 1 HETATM 4573 O O . HOH TA 12 . ? -18.165 -41.545 -25.712 1.00 38.00 ? 2130 HOH A O 1 HETATM 4574 O O . HOH TA 12 . ? -29.386 -35.138 -7.966 1.00 38.92 ? 2131 HOH A O 1 HETATM 4575 O O . HOH TA 12 . ? -26.920 -38.485 -5.234 1.00 26.66 ? 2132 HOH A O 1 HETATM 4576 O O . HOH TA 12 . ? -24.242 -32.318 -38.221 1.00 32.07 ? 2133 HOH A O 1 HETATM 4577 O O . HOH TA 12 . ? -24.545 -41.175 -19.975 1.00 20.32 ? 2134 HOH A O 1 HETATM 4578 O O . HOH TA 12 . ? -32.051 -32.777 -33.925 1.00 31.10 ? 2135 HOH A O 1 HETATM 4579 O O . HOH TA 12 . ? -25.518 -53.380 -18.608 1.00 44.64 ? 2136 HOH A O 1 HETATM 4580 O O . HOH TA 12 . ? -28.322 -30.339 -33.497 1.00 15.47 ? 2137 HOH A O 1 HETATM 4581 O O . HOH TA 12 . ? -30.604 -36.787 -30.748 1.00 22.91 ? 2138 HOH A O 1 HETATM 4582 O O . HOH TA 12 . ? -34.016 -33.785 -32.565 1.00 43.29 ? 2139 HOH A O 1 HETATM 4583 O O . HOH TA 12 . ? -37.248 -48.587 -14.943 1.00 33.35 ? 2140 HOH A O 1 HETATM 4584 O O . HOH TA 12 . ? -25.429 -28.406 -33.282 1.00 10.69 ? 2141 HOH A O 1 HETATM 4585 O O . HOH TA 12 . ? -21.638 -35.669 -29.034 1.00 10.84 ? 2142 HOH A O 1 HETATM 4586 O O . HOH TA 12 . ? -20.888 -32.785 -26.022 1.00 15.40 ? 2143 HOH A O 1 HETATM 4587 O O . HOH TA 12 . ? -33.416 -30.978 -32.894 1.00 35.45 ? 2144 HOH A O 1 HETATM 4588 O O . HOH TA 12 . ? -30.318 -23.569 -29.059 1.00 14.85 ? 2145 HOH A O 1 HETATM 4589 O O . HOH TA 12 . ? -37.776 -29.086 -31.714 1.00 39.55 ? 2146 HOH A O 1 HETATM 4590 O O . HOH TA 12 . ? -35.391 -14.010 -32.543 1.00 21.22 ? 2147 HOH A O 1 HETATM 4591 O O . HOH TA 12 . ? -34.942 -11.891 -29.013 1.00 39.98 ? 2148 HOH A O 1 HETATM 4592 O O . HOH TA 12 . ? 2.597 -52.686 -7.937 1.00 13.07 ? 2149 HOH A O 1 HETATM 4593 O O . HOH TA 12 . ? -31.067 -44.165 -4.581 1.00 38.78 ? 2150 HOH A O 1 HETATM 4594 O O . HOH TA 12 . ? -2.277 -37.720 -13.012 1.00 29.53 ? 2151 HOH A O 1 HETATM 4595 O O . HOH TA 12 . ? -14.481 -40.779 -37.605 1.00 10.56 ? 2152 HOH A O 1 HETATM 4596 O O . HOH TA 12 . ? -9.797 -39.948 -42.054 1.00 12.14 ? 2153 HOH A O 1 HETATM 4597 O O . HOH TA 12 . ? -3.847 -37.713 -32.894 1.00 7.96 ? 2154 HOH A O 1 HETATM 4598 O O . HOH TA 12 . ? -3.906 -41.037 -31.266 1.00 18.51 ? 2155 HOH A O 1 HETATM 4599 O O . HOH TA 12 . ? 6.625 -39.840 -38.835 1.00 36.03 ? 2156 HOH A O 1 HETATM 4600 O O . HOH TA 12 . ? -24.349 -24.128 -1.883 1.00 55.56 ? 2157 HOH A O 1 HETATM 4601 O O . HOH TA 12 . ? -37.234 -30.828 -10.968 1.00 38.37 ? 2158 HOH A O 1 HETATM 4602 O O . HOH TA 12 . ? -1.920 -34.386 -43.758 1.00 19.57 ? 2159 HOH A O 1 HETATM 4603 O O . HOH TA 12 . ? 2.722 -34.936 -36.886 1.00 16.93 ? 2160 HOH A O 1 HETATM 4604 O O . HOH TA 12 . ? 0.886 -37.006 -33.961 1.00 36.58 ? 2161 HOH A O 1 HETATM 4605 O O . HOH TA 12 . ? -7.234 -27.225 -41.009 1.00 24.51 ? 2162 HOH A O 1 HETATM 4606 O O . HOH TA 12 . ? -42.024 -19.539 -24.983 1.00 35.69 ? 2163 HOH A O 1 HETATM 4607 O O . HOH TA 12 . ? -3.003 -24.663 -39.034 1.00 39.83 ? 2164 HOH A O 1 HETATM 4608 O O . HOH TA 12 . ? -38.079 -17.292 -23.701 1.00 34.31 ? 2165 HOH A O 1 HETATM 4609 O O . HOH TA 12 . ? -6.985 -24.824 -40.461 1.00 35.80 ? 2166 HOH A O 1 HETATM 4610 O O . HOH TA 12 . ? -30.329 -8.879 -28.688 1.00 32.21 ? 2167 HOH A O 1 HETATM 4611 O O . HOH TA 12 . ? -11.714 -11.784 -37.175 1.00 22.06 ? 2168 HOH A O 1 HETATM 4612 O O . HOH TA 12 . ? -12.353 -12.526 -41.782 1.00 29.99 ? 2169 HOH A O 1 HETATM 4613 O O . HOH TA 12 . ? -16.811 -13.297 -42.438 1.00 16.67 ? 2170 HOH A O 1 HETATM 4614 O O . HOH TA 12 . ? -14.951 -7.134 -14.576 1.00 48.32 ? 2171 HOH A O 1 HETATM 4615 O O . HOH TA 12 . ? -18.593 -13.443 -45.672 1.00 20.20 ? 2172 HOH A O 1 HETATM 4616 O O . HOH TA 12 . ? -25.154 -12.663 -48.653 1.00 18.15 ? 2173 HOH A O 1 HETATM 4617 O O . HOH TA 12 . ? -12.811 -13.929 -33.774 1.00 32.68 ? 2174 HOH A O 1 HETATM 4618 O O . HOH TA 12 . ? -16.893 -15.501 -1.824 1.00 14.83 ? 2175 HOH A O 1 HETATM 4619 O O . HOH TA 12 . ? -17.435 -9.377 -28.894 1.00 26.25 ? 2176 HOH A O 1 HETATM 4620 O O . HOH TA 12 . ? -17.518 -13.812 -29.007 1.00 10.05 ? 2177 HOH A O 1 HETATM 4621 O O . HOH TA 12 . ? -21.176 -32.251 -18.993 1.00 8.38 ? 2178 HOH A O 1 HETATM 4622 O O . HOH TA 12 . ? -20.451 -36.065 -24.558 1.00 31.23 ? 2179 HOH A O 1 HETATM 4623 O O . HOH TA 12 . ? -4.456 -20.065 -30.021 1.00 18.93 ? 2180 HOH A O 1 HETATM 4624 O O . HOH TA 12 . ? -2.456 -24.906 -35.636 1.00 30.13 ? 2181 HOH A O 1 HETATM 4625 O O . HOH TA 12 . ? -4.785 -21.139 -39.458 1.00 37.78 ? 2182 HOH A O 1 HETATM 4626 O O . HOH TA 12 . ? -2.441 -18.958 -29.214 1.00 21.17 ? 2183 HOH A O 1 HETATM 4627 O O . HOH TA 12 . ? -5.744 -13.113 -29.322 1.00 39.37 ? 2184 HOH A O 1 HETATM 4628 O O . HOH TA 12 . ? -6.287 -11.737 -34.381 1.00 42.08 ? 2185 HOH A O 1 HETATM 4629 O O . HOH TA 12 . ? -4.312 -17.816 -35.961 1.00 23.89 ? 2186 HOH A O 1 HETATM 4630 O O . HOH TA 12 . ? -10.709 -13.577 -34.542 1.00 37.05 ? 2187 HOH A O 1 HETATM 4631 O O . HOH TA 12 . ? -14.210 -18.438 -36.576 1.00 11.90 ? 2188 HOH A O 1 HETATM 4632 O O . HOH TA 12 . ? -11.399 -12.439 -32.372 1.00 30.43 ? 2189 HOH A O 1 HETATM 4633 O O . HOH TA 12 . ? -13.620 -8.452 -27.500 1.00 38.16 ? 2190 HOH A O 1 HETATM 4634 O O . HOH TA 12 . ? -11.514 -31.330 -17.294 1.00 20.44 ? 2191 HOH A O 1 HETATM 4635 O O . HOH TA 12 . ? -2.581 -33.633 -20.796 1.00 35.78 ? 2192 HOH A O 1 HETATM 4636 O O . HOH TA 12 . ? -3.201 -29.754 -14.100 1.00 33.18 ? 2193 HOH A O 1 HETATM 4637 O O . HOH TA 12 . ? -4.873 -35.353 -14.821 1.00 31.79 ? 2194 HOH A O 1 HETATM 4638 O O . HOH TA 12 . ? -4.306 -31.557 -13.279 1.00 35.30 ? 2195 HOH A O 1 HETATM 4639 O O . HOH TA 12 . ? -3.969 -35.606 -20.886 1.00 26.45 ? 2196 HOH A O 1 HETATM 4640 O O . HOH TA 12 . ? -4.503 -41.949 -18.194 1.00 40.85 ? 2197 HOH A O 1 HETATM 4641 O O . HOH TA 12 . ? 1.634 -36.825 -27.584 1.00 28.35 ? 2198 HOH A O 1 HETATM 4642 O O . HOH TA 12 . ? -5.740 -38.450 -26.288 1.00 42.18 ? 2199 HOH A O 1 HETATM 4643 O O . HOH TA 12 . ? 3.241 -53.028 -29.745 1.00 25.36 ? 2200 HOH A O 1 HETATM 4644 O O . HOH TA 12 . ? -2.502 -43.381 -33.124 1.00 27.22 ? 2201 HOH A O 1 HETATM 4645 O O . HOH TA 12 . ? 2.452 -53.367 -36.689 1.00 24.15 ? 2202 HOH A O 1 HETATM 4646 O O . HOH TA 12 . ? 9.340 -45.782 -42.201 1.00 44.00 ? 2203 HOH A O 1 HETATM 4647 O O . HOH TA 12 . ? 5.854 -42.698 -40.521 1.00 37.41 ? 2204 HOH A O 1 HETATM 4648 O O . HOH TA 12 . ? 8.644 -43.208 -44.401 1.00 35.70 ? 2205 HOH A O 1 HETATM 4649 O O . HOH TA 12 . ? -9.287 -44.819 -47.855 1.00 10.44 ? 2206 HOH A O 1 HETATM 4650 O O . HOH TA 12 . ? -3.245 -41.063 -46.012 1.00 11.38 ? 2207 HOH A O 1 HETATM 4651 O O . HOH TA 12 . ? -4.074 -44.978 -51.629 1.00 19.09 ? 2208 HOH A O 1 HETATM 4652 O O . HOH TA 12 . ? -18.820 -50.131 -36.495 1.00 47.40 ? 2209 HOH A O 1 HETATM 4653 O O . HOH TA 12 . ? -21.149 -48.720 -39.216 1.00 33.78 ? 2210 HOH A O 1 HETATM 4654 O O . HOH TA 12 . ? -16.983 -50.896 -44.204 1.00 28.71 ? 2211 HOH A O 1 HETATM 4655 O O . HOH TA 12 . ? -13.613 -51.102 -31.342 1.00 26.66 ? 2212 HOH A O 1 HETATM 4656 O O . HOH TA 12 . ? -12.292 -44.136 -36.901 1.00 17.62 ? 2213 HOH A O 1 HETATM 4657 O O . HOH TA 12 . ? -10.157 -50.130 -25.279 1.00 32.37 ? 2214 HOH A O 1 HETATM 4658 O O . HOH TA 12 . ? -7.397 -55.124 -25.413 1.00 48.80 ? 2215 HOH A O 1 HETATM 4659 O O . HOH TA 12 . ? -10.956 -51.708 -17.144 1.00 26.48 ? 2216 HOH A O 1 HETATM 4660 O O . HOH TA 12 . ? -12.336 -51.647 -21.722 1.00 39.69 ? 2217 HOH A O 1 HETATM 4661 O O . HOH TA 12 . ? -8.796 -44.884 -18.768 1.00 38.73 ? 2218 HOH A O 1 HETATM 4662 O O . HOH TA 12 . ? -18.095 -45.921 -21.686 1.00 42.43 ? 2219 HOH A O 1 HETATM 4663 O O . HOH TA 12 . ? -8.819 -42.651 -20.118 1.00 20.45 ? 2220 HOH A O 1 HETATM 4664 O O . HOH TA 12 . ? -11.545 -45.389 -26.735 1.00 18.79 ? 2221 HOH A O 1 HETATM 4665 O O . HOH TA 12 . ? -14.824 -43.805 -23.691 1.00 36.31 ? 2222 HOH A O 1 HETATM 4666 O O . HOH TA 12 . ? -7.067 -46.699 -23.027 1.00 24.62 ? 2223 HOH A O 1 HETATM 4667 O O . HOH TA 12 . ? -5.880 -40.928 -24.647 1.00 25.70 ? 2224 HOH A O 1 HETATM 4668 O O . HOH TA 12 . ? -11.145 -47.349 -28.460 1.00 31.54 ? 2225 HOH A O 1 HETATM 4669 O O . HOH TA 12 . ? -3.450 -43.473 -30.660 1.00 28.49 ? 2226 HOH A O 1 HETATM 4670 O O . HOH TA 12 . ? 3.062 -33.049 -38.702 1.00 17.98 ? 2227 HOH A O 1 HETATM 4671 O O . HOH TA 12 . ? -0.836 -33.222 -37.430 1.00 15.74 ? 2228 HOH A O 1 HETATM 4672 O O . HOH TA 12 . ? 5.073 -31.677 -38.213 1.00 31.09 ? 2229 HOH A O 1 HETATM 4673 O O . HOH TA 12 . ? 7.331 -29.268 -35.885 1.00 23.19 ? 2230 HOH A O 1 HETATM 4674 O O . HOH TA 12 . ? 2.925 -25.447 -35.617 1.00 42.40 ? 2231 HOH A O 1 HETATM 4675 O O . HOH TA 12 . ? 0.850 -32.346 -39.159 1.00 2.88 ? 2232 HOH A O 1 HETATM 4676 O O . HOH TA 12 . ? 1.050 -26.708 -40.836 1.00 17.09 ? 2233 HOH A O 1 HETATM 4677 O O . HOH TA 12 . ? 6.244 -24.553 -28.407 1.00 36.60 ? 2234 HOH A O 1 HETATM 4678 O O . HOH TA 12 . ? 8.489 -27.564 -28.552 1.00 25.29 ? 2235 HOH A O 1 HETATM 4679 O O . HOH TA 12 . ? 3.048 -22.312 -28.890 1.00 33.35 ? 2236 HOH A O 1 HETATM 4680 O O . HOH TA 12 . ? 0.645 -25.512 -29.718 1.00 19.25 ? 2237 HOH A O 1 HETATM 4681 O O . HOH TA 12 . ? 0.555 -33.349 -21.836 1.00 59.14 ? 2238 HOH A O 1 HETATM 4682 O O . HOH TA 12 . ? 0.461 -27.543 -16.493 1.00 22.38 ? 2239 HOH A O 1 HETATM 4683 O O . HOH TA 12 . ? -1.130 -31.103 -18.437 1.00 39.45 ? 2240 HOH A O 1 HETATM 4684 O O . HOH TA 12 . ? 4.904 -20.538 -14.058 1.00 56.05 ? 2241 HOH A O 1 HETATM 4685 O O . HOH TA 12 . ? 6.833 -22.622 -13.745 1.00 36.45 ? 2242 HOH A O 1 HETATM 4686 O O . HOH TA 12 . ? -0.179 -26.244 -13.925 1.00 46.42 ? 2243 HOH A O 1 HETATM 4687 O O . HOH TA 12 . ? 6.748 -18.165 -19.599 1.00 17.83 ? 2244 HOH A O 1 HETATM 4688 O O . HOH TA 12 . ? 6.250 -16.050 -23.871 1.00 46.56 ? 2245 HOH A O 1 HETATM 4689 O O . HOH TA 12 . ? 4.631 -20.253 -27.486 1.00 38.70 ? 2246 HOH A O 1 HETATM 4690 O O . HOH TA 12 . ? 0.689 -22.320 -27.377 1.00 12.98 ? 2247 HOH A O 1 HETATM 4691 O O . HOH TA 12 . ? -9.589 -12.358 -30.432 1.00 19.51 ? 2248 HOH A O 1 HETATM 4692 O O . HOH TA 12 . ? -2.695 -13.756 -27.086 1.00 20.12 ? 2249 HOH A O 1 HETATM 4693 O O . HOH TA 12 . ? -10.627 -11.003 -25.703 1.00 34.18 ? 2250 HOH A O 1 HETATM 4694 O O . HOH TA 12 . ? -11.862 -8.303 -24.576 1.00 43.87 ? 2251 HOH A O 1 HETATM 4695 O O . HOH TA 12 . ? -14.647 -27.902 -17.634 1.00 13.94 ? 2252 HOH A O 1 HETATM 4696 O O . HOH TA 12 . ? -20.716 -28.883 -17.090 1.00 13.29 ? 2253 HOH A O 1 HETATM 4697 O O . HOH TA 12 . ? -27.757 -31.272 -5.934 1.00 44.05 ? 2254 HOH A O 1 HETATM 4698 O O . HOH TA 12 . ? -20.623 -38.007 -7.932 1.00 10.25 ? 2255 HOH A O 1 HETATM 4699 O O . HOH TA 12 . ? -23.347 -36.050 -4.904 1.00 46.51 ? 2256 HOH A O 1 HETATM 4700 O O . HOH TA 12 . ? -26.508 -35.596 -6.687 1.00 47.16 ? 2257 HOH A O 1 HETATM 4701 O O . HOH TA 12 . ? -22.054 -38.695 -14.615 1.00 9.24 ? 2258 HOH A O 1 HETATM 4702 O O . HOH TA 12 . ? -18.729 -37.192 -9.650 1.00 21.33 ? 2259 HOH A O 1 HETATM 4703 O O . HOH TA 12 . ? -24.481 -43.375 -18.189 1.00 27.83 ? 2260 HOH A O 1 HETATM 4704 O O . HOH TA 12 . ? -24.681 -51.895 -16.180 1.00 27.03 ? 2261 HOH A O 1 HETATM 4705 O O . HOH TA 12 . ? -24.340 -42.766 -22.050 1.00 29.63 ? 2262 HOH A O 1 HETATM 4706 O O . HOH TA 12 . ? -21.062 -52.102 -14.461 1.00 30.13 ? 2263 HOH A O 1 HETATM 4707 O O . HOH TA 12 . ? -17.501 -51.362 -8.246 1.00 20.25 ? 2264 HOH A O 1 HETATM 4708 O O . HOH TA 12 . ? -24.843 -53.483 -5.771 1.00 18.55 ? 2265 HOH A O 1 HETATM 4709 O O . HOH TA 12 . ? -33.139 -46.541 -15.914 1.00 38.76 ? 2266 HOH A O 1 HETATM 4710 O O . HOH TA 12 . ? -27.028 -51.160 -15.618 1.00 23.41 ? 2267 HOH A O 1 HETATM 4711 O O . HOH TA 12 . ? -34.833 -48.449 -14.595 1.00 31.47 ? 2268 HOH A O 1 HETATM 4712 O O . HOH TA 12 . ? -32.998 -47.911 -10.166 1.00 30.80 ? 2269 HOH A O 1 HETATM 4713 O O . HOH TA 12 . ? -22.039 -51.700 1.435 1.00 31.05 ? 2270 HOH A O 1 HETATM 4714 O O . HOH TA 12 . ? -18.363 -58.267 -1.991 1.00 24.78 ? 2271 HOH A O 1 HETATM 4715 O O . HOH TA 12 . ? -18.328 -53.592 3.173 1.00 22.19 ? 2272 HOH A O 1 HETATM 4716 O O . HOH TA 12 . ? -11.098 -47.585 4.695 1.00 29.50 ? 2273 HOH A O 1 HETATM 4717 O O . HOH TA 12 . ? -16.536 -56.030 1.418 1.00 10.20 ? 2274 HOH A O 1 HETATM 4718 O O . HOH TA 12 . ? -16.121 -57.534 -7.600 1.00 29.63 ? 2275 HOH A O 1 HETATM 4719 O O . HOH TA 12 . ? -23.810 -55.631 -5.142 1.00 28.73 ? 2276 HOH A O 1 HETATM 4720 O O . HOH TA 12 . ? -12.363 -55.997 1.310 1.00 36.08 ? 2277 HOH A O 1 HETATM 4721 O O . HOH TA 12 . ? -8.059 -51.969 -5.736 1.00 32.34 ? 2278 HOH A O 1 HETATM 4722 O O . HOH TA 12 . ? -12.075 -55.843 -10.742 1.00 32.34 ? 2279 HOH A O 1 HETATM 4723 O O . HOH TA 12 . ? -10.421 -44.518 -15.642 1.00 32.65 ? 2280 HOH A O 1 HETATM 4724 O O . HOH TA 12 . ? -6.828 -44.636 -15.698 1.00 32.91 ? 2281 HOH A O 1 HETATM 4725 O O . HOH TA 12 . ? -4.898 -46.436 -15.554 1.00 29.90 ? 2282 HOH A O 1 HETATM 4726 O O . HOH TA 12 . ? 2.620 -51.106 -4.963 1.00 23.85 ? 2283 HOH A O 1 HETATM 4727 O O . HOH TA 12 . ? -6.147 -47.310 3.199 1.00 36.44 ? 2284 HOH A O 1 HETATM 4728 O O . HOH TA 12 . ? -11.626 -36.954 -0.240 1.00 49.14 ? 2285 HOH A O 1 HETATM 4729 O O . HOH TA 12 . ? -15.873 -39.837 0.445 1.00 31.78 ? 2286 HOH A O 1 HETATM 4730 O O . HOH TA 12 . ? -9.899 -45.714 5.415 1.00 34.90 ? 2287 HOH A O 1 HETATM 4731 O O . HOH TA 12 . ? -12.714 -39.855 3.061 1.00 39.44 ? 2288 HOH A O 1 HETATM 4732 O O . HOH TA 12 . ? -14.747 -43.322 8.971 1.00 39.36 ? 2289 HOH A O 1 HETATM 4733 O O . HOH TA 12 . ? -14.190 -47.439 6.520 1.00 31.61 ? 2290 HOH A O 1 HETATM 4734 O O . HOH TA 12 . ? -20.711 -41.104 5.710 1.00 36.50 ? 2291 HOH A O 1 HETATM 4735 O O . HOH TA 12 . ? -27.566 -40.431 9.283 1.00 15.36 ? 2292 HOH A O 1 HETATM 4736 O O . HOH TA 12 . ? -19.024 -46.752 11.276 1.00 27.32 ? 2293 HOH A O 1 HETATM 4737 O O . HOH TA 12 . ? -27.430 -39.304 4.520 1.00 33.34 ? 2294 HOH A O 1 HETATM 4738 O O . HOH TA 12 . ? -22.236 -48.568 -1.147 1.00 13.06 ? 2295 HOH A O 1 HETATM 4739 O O . HOH TA 12 . ? -20.818 -48.421 2.457 1.00 33.20 ? 2296 HOH A O 1 HETATM 4740 O O . HOH TA 12 . ? -29.567 -42.959 -2.404 1.00 31.82 ? 2297 HOH A O 1 HETATM 4741 O O . HOH TA 12 . ? -24.357 -42.284 -5.805 1.00 18.15 ? 2298 HOH A O 1 HETATM 4742 O O . HOH TA 12 . ? -22.083 -42.734 -7.086 1.00 19.79 ? 2299 HOH A O 1 HETATM 4743 O O . HOH TA 12 . ? -30.149 -45.424 -2.337 1.00 25.50 ? 2300 HOH A O 1 HETATM 4744 O O . HOH TA 12 . ? -20.996 -40.241 -6.399 1.00 13.48 ? 2301 HOH A O 1 HETATM 4745 O O . HOH TA 12 . ? -21.682 -37.790 -3.739 1.00 30.73 ? 2302 HOH A O 1 HETATM 4746 O O . HOH TA 12 . ? -17.798 -39.346 -1.579 1.00 32.11 ? 2303 HOH A O 1 HETATM 4747 O O . HOH TA 12 . ? -20.854 -35.453 -5.891 1.00 32.45 ? 2304 HOH A O 1 HETATM 4748 O O . HOH TA 12 . ? -17.270 -35.478 -7.728 1.00 12.27 ? 2305 HOH A O 1 HETATM 4749 O O . HOH TA 12 . ? -15.586 -35.483 -3.868 1.00 18.42 ? 2306 HOH A O 1 HETATM 4750 O O . HOH TA 12 . ? -6.401 -42.350 -16.876 1.00 32.04 ? 2307 HOH A O 1 HETATM 4751 O O . HOH TA 12 . ? -6.625 -35.233 -12.192 1.00 14.28 ? 2308 HOH A O 1 HETATM 4752 O O . HOH TA 12 . ? -3.100 -39.653 -14.235 1.00 26.86 ? 2309 HOH A O 1 HETATM 4753 O O . HOH TA 12 . ? -10.694 -43.072 -13.558 1.00 21.85 ? 2310 HOH A O 1 HETATM 4754 O O . HOH TA 12 . ? -8.766 -41.620 -17.453 1.00 23.02 ? 2311 HOH A O 1 HETATM 4755 O O . HOH TA 12 . ? -7.214 -29.144 -9.149 1.00 14.47 ? 2312 HOH A O 1 HETATM 4756 O O . HOH TA 12 . ? -5.397 -27.295 -8.800 1.00 35.01 ? 2313 HOH A O 1 HETATM 4757 O O . HOH TA 12 . ? -4.875 -28.410 -6.064 1.00 45.28 ? 2314 HOH A O 1 HETATM 4758 O O . HOH TA 12 . ? -8.015 -27.305 -6.735 1.00 44.31 ? 2315 HOH A O 1 HETATM 4759 O O . HOH TA 12 . ? -0.031 -21.064 -15.586 1.00 30.25 ? 2316 HOH A O 1 HETATM 4760 O O . HOH TA 12 . ? -6.715 -13.320 -13.262 1.00 36.58 ? 2317 HOH A O 1 HETATM 4761 O O . HOH TA 12 . ? 1.717 -20.716 -13.585 1.00 40.40 ? 2318 HOH A O 1 HETATM 4762 O O . HOH TA 12 . ? -3.515 -11.776 -19.748 1.00 33.24 ? 2319 HOH A O 1 HETATM 4763 O O . HOH TA 12 . ? -15.913 -17.895 -10.908 1.00 17.00 ? 2320 HOH A O 1 HETATM 4764 O O . HOH TA 12 . ? -25.887 -23.890 -4.003 1.00 21.86 ? 2321 HOH A O 1 HETATM 4765 O O . HOH TA 12 . ? -24.181 -29.936 -4.097 1.00 33.09 ? 2322 HOH A O 1 HETATM 4766 O O . HOH TA 12 . ? -23.013 -26.341 -3.487 1.00 28.13 ? 2323 HOH A O 1 HETATM 4767 O O . HOH TA 12 . ? -29.403 -32.260 -15.113 1.00 17.70 ? 2324 HOH A O 1 HETATM 4768 O O . HOH TA 12 . ? -31.706 -27.468 -8.428 1.00 23.03 ? 2325 HOH A O 1 HETATM 4769 O O . HOH TA 12 . ? -35.272 -32.338 -10.556 1.00 33.23 ? 2326 HOH A O 1 HETATM 4770 O O . HOH TA 12 . ? -31.535 -31.174 -8.621 1.00 22.07 ? 2327 HOH A O 1 HETATM 4771 O O . HOH TA 12 . ? -34.883 -36.269 -12.270 1.00 25.12 ? 2328 HOH A O 1 HETATM 4772 O O . HOH TA 12 . ? -40.985 -32.802 -15.224 1.00 30.39 ? 2329 HOH A O 1 HETATM 4773 O O . HOH TA 12 . ? -35.545 -41.800 -14.042 1.00 33.43 ? 2330 HOH A O 1 HETATM 4774 O O . HOH TA 12 . ? -34.839 -45.761 -14.821 1.00 47.10 ? 2331 HOH A O 1 HETATM 4775 O O . HOH TA 12 . ? -34.692 -43.535 -9.510 1.00 31.92 ? 2332 HOH A O 1 HETATM 4776 O O . HOH TA 12 . ? -30.995 -37.073 -7.258 1.00 41.34 ? 2333 HOH A O 1 HETATM 4777 O O . HOH TA 12 . ? -31.687 -44.255 -7.387 1.00 29.49 ? 2334 HOH A O 1 HETATM 4778 O O . HOH TA 12 . ? -23.376 -38.869 -20.168 1.00 26.48 ? 2335 HOH A O 1 HETATM 4779 O O . HOH TA 12 . ? -28.344 -32.393 -21.759 1.00 16.90 ? 2336 HOH A O 1 HETATM 4780 O O . HOH TA 12 . ? -33.730 -35.084 -19.606 1.00 29.65 ? 2337 HOH A O 1 HETATM 4781 O O . HOH TA 12 . ? -32.244 -35.444 -21.313 1.00 17.50 ? 2338 HOH A O 1 HETATM 4782 O O . HOH TA 12 . ? -40.756 -27.293 -20.931 1.00 42.99 ? 2339 HOH A O 1 HETATM 4783 O O . HOH TA 12 . ? -39.706 -25.125 -31.894 1.00 25.85 ? 2340 HOH A O 1 HETATM 4784 O O . HOH TA 12 . ? -43.420 -23.236 -28.583 1.00 36.77 ? 2341 HOH A O 1 HETATM 4785 O O . HOH TA 12 . ? -45.029 -19.499 -22.832 1.00 40.35 ? 2342 HOH A O 1 HETATM 4786 O O . HOH TA 12 . ? -42.750 -22.340 -25.481 1.00 34.16 ? 2343 HOH A O 1 HETATM 4787 O O . HOH TA 12 . ? -37.398 -28.654 -25.933 1.00 22.86 ? 2344 HOH A O 1 HETATM 4788 O O . HOH TA 12 . ? -37.738 -28.331 -11.220 1.00 22.61 ? 2345 HOH A O 1 HETATM 4789 O O . HOH TA 12 . ? -42.668 -24.522 -18.486 1.00 40.63 ? 2346 HOH A O 1 HETATM 4790 O O . HOH TA 12 . ? -38.778 -17.882 -20.255 1.00 35.13 ? 2347 HOH A O 1 HETATM 4791 O O . HOH TA 12 . ? -39.963 -19.959 -22.470 1.00 29.59 ? 2348 HOH A O 1 HETATM 4792 O O . HOH TA 12 . ? -43.659 -19.422 -20.725 1.00 19.97 ? 2349 HOH A O 1 HETATM 4793 O O . HOH TA 12 . ? -32.197 -19.471 -12.200 1.00 27.64 ? 2350 HOH A O 1 HETATM 4794 O O . HOH TA 12 . ? -36.857 -12.509 -22.578 1.00 25.74 ? 2351 HOH A O 1 HETATM 4795 O O . HOH TA 12 . ? -28.164 -18.382 -13.359 1.00 25.30 ? 2352 HOH A O 1 HETATM 4796 O O . HOH TA 12 . ? -32.691 -11.086 -24.967 1.00 36.07 ? 2353 HOH A O 1 HETATM 4797 O O . HOH TA 12 . ? -32.866 -9.584 -22.874 1.00 44.83 ? 2354 HOH A O 1 HETATM 4798 O O . HOH TA 12 . ? -28.891 -16.434 -11.463 1.00 33.25 ? 2355 HOH A O 1 HETATM 4799 O O . HOH TA 12 . ? -27.818 -9.409 -23.436 1.00 12.16 ? 2356 HOH A O 1 HETATM 4800 O O . HOH TA 12 . ? -16.392 -7.575 -26.265 1.00 38.32 ? 2357 HOH A O 1 HETATM 4801 O O . HOH TA 12 . ? -20.343 -7.429 -29.241 1.00 28.69 ? 2358 HOH A O 1 HETATM 4802 O O . HOH TA 12 . ? -30.472 -9.812 -26.571 1.00 27.21 ? 2359 HOH A O 1 HETATM 4803 O O . HOH TA 12 . ? -14.569 -10.008 -18.408 1.00 15.66 ? 2360 HOH A O 1 HETATM 4804 O O . HOH TA 12 . ? -16.372 -9.006 -14.179 1.00 31.80 ? 2361 HOH A O 1 HETATM 4805 O O . HOH TA 12 . ? -19.716 -6.969 -13.436 1.00 42.88 ? 2362 HOH A O 1 HETATM 4806 O O . HOH TA 12 . ? -29.208 -8.770 -12.089 1.00 15.78 ? 2363 HOH A O 1 HETATM 4807 O O . HOH TA 12 . ? -30.839 -10.132 -18.853 1.00 13.09 ? 2364 HOH A O 1 HETATM 4808 O O . HOH TA 12 . ? -25.271 -11.661 -12.900 1.00 19.71 ? 2365 HOH A O 1 HETATM 4809 O O . HOH TA 12 . ? -29.447 -4.664 -17.214 1.00 33.80 ? 2366 HOH A O 1 HETATM 4810 O O . HOH TA 12 . ? -28.312 -9.306 -18.831 1.00 9.72 ? 2367 HOH A O 1 HETATM 4811 O O . HOH TA 12 . ? -31.050 -6.963 -11.682 1.00 31.71 ? 2368 HOH A O 1 HETATM 4812 O O . HOH TA 12 . ? -30.724 -15.109 -13.192 1.00 19.89 ? 2369 HOH A O 1 HETATM 4813 O O . HOH TA 12 . ? -24.411 -10.555 -6.059 1.00 22.12 ? 2370 HOH A O 1 HETATM 4814 O O . HOH TA 12 . ? -17.512 -10.213 -12.036 1.00 30.17 ? 2371 HOH A O 1 HETATM 4815 O O . HOH TA 12 . ? -15.024 -9.817 -9.514 1.00 29.05 ? 2372 HOH A O 1 HETATM 4816 O O . HOH TA 12 . ? -13.201 -12.208 -7.656 1.00 26.81 ? 2373 HOH A O 1 HETATM 4817 O O . HOH TA 12 . ? -12.138 -15.619 -7.132 1.00 15.78 ? 2374 HOH A O 1 HETATM 4818 O O . HOH TA 12 . ? -9.655 -14.504 -13.358 1.00 20.28 ? 2375 HOH A O 1 HETATM 4819 O O . HOH TA 12 . ? -11.529 -9.621 -8.753 1.00 50.65 ? 2376 HOH A O 1 HETATM 4820 O O . HOH TA 12 . ? -5.437 -13.852 -6.750 1.00 36.56 ? 2377 HOH A O 1 HETATM 4821 O O . HOH TA 12 . ? -5.444 -15.830 -10.721 1.00 42.95 ? 2378 HOH A O 1 HETATM 4822 O O . HOH TA 12 . ? -5.920 -19.500 -6.141 1.00 28.74 ? 2379 HOH A O 1 HETATM 4823 O O . HOH TA 12 . ? -13.181 -10.926 -1.673 1.00 29.58 ? 2380 HOH A O 1 HETATM 4824 O O . HOH TA 12 . ? -11.334 -18.102 -0.586 1.00 20.57 ? 2381 HOH A O 1 HETATM 4825 O O . HOH TA 12 . ? -11.467 -13.290 -5.746 1.00 16.25 ? 2382 HOH A O 1 HETATM 4826 O O . HOH TA 12 . ? -10.402 -24.116 -6.618 1.00 21.85 ? 2383 HOH A O 1 HETATM 4827 O O . HOH TA 12 . ? -8.295 -25.049 -3.579 1.00 32.20 ? 2384 HOH A O 1 HETATM 4828 O O . HOH TA 12 . ? -15.361 -10.304 -6.364 1.00 30.50 ? 2385 HOH A O 1 HETATM 4829 O O . HOH TA 12 . ? -16.758 -25.173 -1.939 1.00 19.67 ? 2386 HOH A O 1 HETATM 4830 O O . HOH TA 12 . ? -20.434 -26.956 -3.687 1.00 32.23 ? 2387 HOH A O 1 HETATM 4831 O O . HOH TA 12 . ? -35.143 -21.538 -11.179 1.00 30.94 ? 2388 HOH A O 1 HETATM 4832 O O . HOH TA 12 . ? -34.633 -15.796 -6.779 1.00 47.71 ? 2389 HOH A O 1 HETATM 4833 O O . HOH TA 12 . ? -28.555 -23.013 -3.246 1.00 34.24 ? 2390 HOH A O 1 HETATM 4834 O O . HOH TA 12 . ? -28.442 -20.950 -9.607 1.00 31.12 ? 2391 HOH A O 1 HETATM 4835 O O . HOH TA 12 . ? -25.338 -17.849 -0.223 1.00 34.72 ? 2392 HOH A O 1 HETATM 4836 O O . HOH TA 12 . ? -29.290 -19.483 3.225 1.00 29.86 ? 2393 HOH A O 1 HETATM 4837 O O . HOH TA 12 . ? -18.787 -17.060 -0.619 1.00 11.22 ? 2394 HOH A O 1 HETATM 4838 O O . HOH TA 12 . ? -21.996 -17.732 -0.071 1.00 23.15 ? 2395 HOH A O 1 HETATM 4839 O O . HOH TA 12 . ? -23.853 -16.393 -2.572 1.00 16.69 ? 2396 HOH A O 1 HETATM 4840 O O . HOH TA 12 . ? -14.390 -22.838 1.224 1.00 22.24 ? 2397 HOH A O 1 HETATM 4841 O O . HOH TA 12 . ? -13.588 -25.354 0.105 1.00 21.95 ? 2398 HOH A O 1 HETATM 4842 O O . HOH TA 12 . ? -6.240 -23.308 -0.954 1.00 42.53 ? 2399 HOH A O 1 HETATM 4843 O O . HOH TA 12 . ? -10.104 -26.478 -5.466 1.00 19.84 ? 2400 HOH A O 1 HETATM 4844 O O . HOH TA 12 . ? -13.018 -23.225 -6.500 1.00 13.53 ? 2401 HOH A O 1 HETATM 4845 O O . HOH TA 12 . ? -17.657 -34.089 -3.343 1.00 20.35 ? 2402 HOH A O 1 HETATM 4846 O O . HOH TA 12 . ? -7.056 -28.001 -4.185 1.00 33.49 ? 2403 HOH A O 1 HETATM 4847 O O . HOH TA 12 . ? -12.531 -29.817 0.342 1.00 43.69 ? 2404 HOH A O 1 HETATM 4848 O O . HOH TA 12 . ? -15.430 -36.996 -1.684 1.00 23.36 ? 2405 HOH A O 1 HETATM 4849 O O . HOH TA 12 . ? -9.372 -25.279 1.566 1.00 28.32 ? 2406 HOH A O 1 HETATM 4850 O O . HOH TA 12 . ? -5.579 -31.581 3.125 1.00 35.65 ? 2407 HOH A O 1 HETATM 4851 O O . HOH TA 12 . ? -4.262 -36.470 -11.127 1.00 27.82 ? 2408 HOH A O 1 HETATM 4852 O O . HOH TA 12 . ? -0.401 -32.034 -11.399 1.00 44.82 ? 2409 HOH A O 1 HETATM 4853 O O . HOH TA 12 . ? -6.081 -32.612 -11.765 1.00 10.22 ? 2410 HOH A O 1 HETATM 4854 O O . HOH TA 12 . ? 6.998 -44.715 -8.534 1.00 30.85 ? 2411 HOH A O 1 HETATM 4855 O O . HOH TA 12 . ? 1.195 -46.494 -10.650 1.00 20.78 ? 2412 HOH A O 1 HETATM 4856 O O . HOH TA 12 . ? -5.938 -33.559 0.742 1.00 32.48 ? 2413 HOH A O 1 HETATM 4857 O O . HOH TA 12 . ? -21.710 -63.654 -12.152 1.00 59.38 ? 2414 HOH A O 1 HETATM 4858 O O . HOH TA 12 . ? -24.020 -58.737 -7.010 1.00 52.62 ? 2415 HOH A O 1 HETATM 4859 O O . HOH TA 12 . ? -17.947 -6.835 -31.167 1.00 31.83 ? 2416 HOH A O 1 HETATM 4860 O O . HOH TA 12 . ? -15.441 -6.109 -31.474 1.00 46.04 ? 2417 HOH A O 1 HETATM 4861 O O . HOH TA 12 . ? -39.273 -26.956 -56.696 1.00 62.85 ? 2418 HOH A O 1 HETATM 4862 O O . HOH TA 12 . ? 6.837 -40.594 -52.757 1.00 63.40 ? 2419 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 . ASP A 1 ? 0.9996 0.9678 1.0298 0.1224 -0.3707 0.0393 3 ASP A N 2 C CA . ASP A 1 ? 0.9964 0.9430 0.9914 0.1033 -0.3581 0.0341 3 ASP A CA 3 C C . ASP A 1 ? 0.9890 0.8937 0.9625 0.1016 -0.3354 0.0432 3 ASP A C 4 O O . ASP A 1 ? 1.0316 0.9074 0.9754 0.1123 -0.3365 0.0594 3 ASP A O 5 C CB . ASP A 1 ? 1.0452 0.9891 0.9971 0.1032 -0.3758 0.0371 3 ASP A CB 6 C CG . ASP A 1 ? 1.0628 0.9910 0.9819 0.0844 -0.3638 0.0283 3 ASP A CG 7 O OD1 . ASP A 1 ? 1.0625 0.9898 0.9990 0.0701 -0.3450 0.0175 3 ASP A OD1 8 O OD2 . ASP A 1 ? 1.1156 1.0329 0.9901 0.0854 -0.3735 0.0323 3 ASP A OD2 9 N N . ILE A 2 ? 0.9261 0.8276 0.9151 0.0878 -0.3153 0.0333 4 ILE A N 10 C CA . ILE A 2 ? 0.9082 0.7755 0.8875 0.0858 -0.2946 0.0400 4 ILE A CA 11 C C . ILE A 2 ? 0.8767 0.7240 0.8252 0.0691 -0.2789 0.0379 4 ILE A C 12 O O . ILE A 2 ? 0.8344 0.6950 0.7955 0.0556 -0.2704 0.0243 4 ILE A O 13 C CB . ILE A 2 ? 0.8795 0.7558 0.9005 0.0865 -0.2828 0.0323 4 ILE A CB 14 C CG1 . ILE A 2 ? 0.8682 0.7871 0.9293 0.0890 -0.2932 0.0213 4 ILE A CG1 15 C CG2 . ILE A 2 ? 0.9077 0.7594 0.9311 0.1024 -0.2807 0.0439 4 ILE A CG2 16 C CD1 . ILE A 2 ? 0.8645 0.8101 0.9253 0.0774 -0.3042 0.0114 4 ILE A CD1 17 N N . ILE A 3 ? 0.8747 0.6905 0.7834 0.0712 -0.2749 0.0523 5 ILE A N 18 C CA . ILE A 3 ? 0.8499 0.6472 0.7255 0.0578 -0.2599 0.0529 5 ILE A CA 19 C C . ILE A 3 ? 0.8445 0.6101 0.7151 0.0539 -0.2395 0.0629 5 ILE A C 20 O O . ILE A 3 ? 0.8600 0.6027 0.7221 0.0639 -0.2410 0.0781 5 ILE A O 21 C CB . ILE A 3 ? 0.8891 0.6796 0.7181 0.0615 -0.2715 0.0611 5 ILE A CB 22 C CG1 . ILE A 3 ? 0.8928 0.7147 0.7259 0.0583 -0.2884 0.0456 5 ILE A CG1 23 C CG2 . ILE A 3 ? 0.8831 0.6490 0.6738 0.0513 -0.2531 0.0666 5 ILE A CG2 24 C CD1 . ILE A 3 ? 0.9384 0.7620 0.7342 0.0683 -0.3102 0.0529 5 ILE A CD1 25 N N . ILE A 4 ? 0.7974 0.5617 0.6746 0.0393 -0.2210 0.0542 6 ILE A N 26 C CA . ILE A 4 ? 0.7804 0.5193 0.6575 0.0329 -0.2019 0.0615 6 ILE A CA 27 C C . ILE A 4 ? 0.8051 0.5301 0.6488 0.0220 -0.1868 0.0664 6 ILE A C 28 O O . ILE A 4 ? 0.7974 0.5375 0.6356 0.0142 -0.1833 0.0551 6 ILE A O 29 C CB . ILE A 4 ? 0.7249 0.4752 0.6427 0.0267 -0.1923 0.0482 6 ILE A CB 30 C CG1 . ILE A 4 ? 0.6948 0.4568 0.6435 0.0391 -0.2045 0.0446 6 ILE A CG1 31 C CG2 . ILE A 4 ? 0.7183 0.4451 0.6384 0.0179 -0.1737 0.0534 6 ILE A CG2 32 C CD1 . ILE A 4 ? 0.7152 0.4523 0.6577 0.0526 -0.2107 0.0593 6 ILE A CD1 33 N N . ALA A 5 ? 0.8450 0.5406 0.6665 0.0218 -0.1773 0.0838 7 ALA A N 34 C CA . ALA A 5 ? 0.8703 0.5528 0.6631 0.0111 -0.1591 0.0904 7 ALA A CA 35 C C . ALA A 5 ? 0.8420 0.5264 0.6627 -0.0027 -0.1393 0.0826 7 ALA A C 36 O O . ALA A 5 ? 0.8444 0.5148 0.6864 -0.0043 -0.1343 0.0871 7 ALA A O 37 C CB . ALA A 5 ? 0.9185 0.5686 0.6782 0.0159 -0.1556 0.1144 7 ALA A CB 38 N N . THR A 6 ? 0.8276 0.5287 0.6488 -0.0119 -0.1291 0.0704 8 THR A N 39 C CA . THR A 6 ? 0.8060 0.5114 0.6529 -0.0242 -0.1105 0.0637 8 THR A CA 40 C C . THR A 6 ? 0.8413 0.5349 0.6632 -0.0327 -0.0905 0.0741 8 THR A C 41 O O . THR A 6 ? 0.8766 0.5588 0.6587 -0.0284 -0.0914 0.0853 8 THR A O 42 C CB . THR A 6 ? 0.7629 0.4960 0.6349 -0.0277 -0.1111 0.0432 8 THR A CB 43 O OG1 . THR A 6 ? 0.7852 0.5268 0.6332 -0.0304 -0.1059 0.0371 8 THR A OG1 44 C CG2 . THR A 6 ? 0.7543 0.5014 0.6454 -0.0189 -0.1303 0.0347 8 THR A CG2 45 N N . LYS A 7 ? 0.8246 0.5224 0.6690 -0.0442 -0.0727 0.0708 9 LYS A N 46 C CA . LYS A 7 ? 0.8571 0.5489 0.6824 -0.0528 -0.0511 0.0801 9 LYS A CA 47 C C . LYS A 7 ? 0.8722 0.5754 0.6662 -0.0502 -0.0476 0.0734 9 LYS A C 48 O O . LYS A 7 ? 0.9086 0.6023 0.6698 -0.0518 -0.0343 0.0846 9 LYS A O 49 C CB . LYS A 7 ? 0.8414 0.5419 0.7027 -0.0655 -0.0339 0.0757 9 LYS A CB 50 C CG . LYS A 7 ? 0.8621 0.5459 0.7502 -0.0713 -0.0334 0.0836 9 LYS A CG 51 C CD . LYS A 7 ? 0.9646 0.6184 0.8265 -0.0726 -0.0273 0.1063 9 LYS A CD 52 C CE . LYS A 7 ? 1.0402 0.6703 0.9106 -0.0664 -0.0424 0.1128 9 LYS A CE 53 N NZ . LYS A 7 ? 1.0500 0.6832 0.9653 -0.0741 -0.0423 0.1020 9 LYS A NZ 54 N N . ASN A 8 ? 0.8400 0.5621 0.6427 -0.0461 -0.0593 0.0554 10 ASN A N 55 C CA . ASN A 8 ? 0.8619 0.5927 0.6360 -0.0436 -0.0578 0.0458 10 ASN A CA 56 C C . ASN A 8 ? 0.8709 0.5979 0.6114 -0.0338 -0.0784 0.0452 10 ASN A C 57 O O . ASN A 8 ? 0.8899 0.6205 0.6011 -0.0317 -0.0787 0.0370 10 ASN A O 58 C CB . ASN A 8 ? 0.8372 0.5893 0.6407 -0.0468 -0.0554 0.0257 10 ASN A CB 59 C CG . ASN A 8 ? 0.8658 0.6256 0.7038 -0.0553 -0.0374 0.0254 10 ASN A CG 60 O OD1 . ASN A 8 ? 0.9415 0.7071 0.7748 -0.0593 -0.0191 0.0234 10 ASN A OD1 61 N ND2 . ASN A 8 ? 0.8542 0.6146 0.7269 -0.0577 -0.0427 0.0271 10 ASN A ND2 62 N N . GLY A 9 ? 0.8550 0.5751 0.5996 -0.0272 -0.0959 0.0530 11 GLY A N 63 C CA . GLY A 9 ? 0.8615 0.5803 0.5756 -0.0173 -0.1167 0.0540 11 GLY A CA 64 C C . GLY A 9 ? 0.8312 0.5595 0.5745 -0.0108 -0.1383 0.0499 11 GLY A C 65 O O . GLY A 9 ? 0.7802 0.5144 0.5644 -0.0138 -0.1360 0.0459 11 GLY A O 66 N N . LYS A 10 ? 0.8446 0.5758 0.5666 -0.0015 -0.1596 0.0507 12 LYS A N 67 C CA . LYS A 10 ? 0.8273 0.5707 0.5762 0.0065 -0.1811 0.0479 12 LYS A CA 68 C C . LYS A 10 ? 0.7794 0.5491 0.5652 0.0020 -0.1876 0.0270 12 LYS A C 69 O O . LYS A 10 ? 0.7745 0.5532 0.5528 -0.0044 -0.1848 0.0131 12 LYS A O 70 C CB . LYS A 10 ? 0.8679 0.6093 0.5836 0.0183 -0.2026 0.0559 12 LYS A CB 71 C CG . LYS A 10 ? 0.9532 0.6667 0.6321 0.0245 -0.1970 0.0794 12 LYS A CG 72 C CD . LYS A 10 ? 1.0193 0.7317 0.6688 0.0391 -0.2210 0.0892 12 LYS A CD 73 C CE . LYS A 10 ? 1.0847 0.7677 0.7133 0.0481 -0.2179 0.1154 12 LYS A CE 74 N NZ . LYS A 10 ? 1.1335 0.8158 0.7272 0.0638 -0.2415 0.1260 12 LYS A NZ 75 N N . VAL A 11 ? 0.7418 0.5222 0.5665 0.0056 -0.1952 0.0252 13 VAL A N 76 C CA . VAL A 11 ? 0.7144 0.5202 0.5735 0.0026 -0.2026 0.0086 13 VAL A CA 77 C C . VAL A 11 ? 0.7072 0.5283 0.5868 0.0131 -0.2235 0.0100 13 VAL A C 78 O O . VAL A 11 ? 0.7218 0.5350 0.6108 0.0219 -0.2259 0.0209 13 VAL A O 79 C CB . VAL A 11 ? 0.6649 0.4762 0.5592 -0.0055 -0.1856 0.0005 13 VAL A CB 80 C CG1 . VAL A 11 ? 0.7046 0.5034 0.5824 -0.0143 -0.1652 0.0005 13 VAL A CG1 81 C CG2 . VAL A 11 ? 0.6659 0.4722 0.5846 -0.0006 -0.1833 0.0079 13 VAL A CG2 82 N N . ARG A 12 ? 0.7017 0.5449 0.5893 0.0121 -0.2388 -0.0015 14 ARG A N 83 C CA . ARG A 12 ? 0.6829 0.5484 0.5985 0.0208 -0.2579 -0.0024 14 ARG A CA 84 C C . ARG A 12 ? 0.6287 0.5145 0.5915 0.0157 -0.2518 -0.0131 14 ARG A C 85 O O . ARG A 12 ? 0.6089 0.5007 0.5798 0.0043 -0.2431 -0.0250 14 ARG A O 86 C CB . ARG A 12 ? 0.6962 0.5767 0.5961 0.0210 -0.2788 -0.0091 14 ARG A CB 87 C CG . ARG A 12 ? 0.7022 0.6154 0.6410 0.0235 -0.2965 -0.0167 14 ARG A CG 88 C CD . ARG A 12 ? 0.7704 0.6979 0.6911 0.0243 -0.3206 -0.0223 14 ARG A CD 89 N NE . ARG A 12 ? 0.8475 0.7652 0.7360 0.0389 -0.3348 -0.0075 14 ARG A NE 90 C CZ . ARG A 12 ? 0.8826 0.7812 0.7189 0.0401 -0.3380 -0.0031 14 ARG A CZ 91 N NH1 . ARG A 12 ? 0.8578 0.7452 0.6694 0.0277 -0.3269 -0.0140 14 ARG A NH1 92 N NH2 . ARG A 12 ? 0.8689 0.7591 0.6767 0.0550 -0.3516 0.0127 14 ARG A NH2 93 N N . GLY A 13 ? 0.6086 0.5036 0.6005 0.0253 -0.2553 -0.0084 15 GLY A N 94 C CA . GLY A 13 ? 0.5823 0.4979 0.6167 0.0230 -0.2497 -0.0167 15 GLY A CA 95 C C . GLY A 13 ? 0.6018 0.5490 0.6634 0.0276 -0.2673 -0.0209 15 GLY A C 96 O O . GLY A 13 ? 0.6384 0.5924 0.6855 0.0305 -0.2848 -0.0199 15 GLY A O 97 N N . MET A 14 ? 0.5798 0.5479 0.6806 0.0283 -0.2628 -0.0257 16 MET A N 98 C CA . MET A 14 ? 0.5820 0.5839 0.7157 0.0333 -0.2772 -0.0284 16 MET A CA 99 C C . MET A 14 ? 0.5617 0.5750 0.7269 0.0462 -0.2719 -0.0246 16 MET A C 100 O O . MET A 14 ? 0.5504 0.5508 0.7186 0.0461 -0.2556 -0.0248 16 MET A O 101 C CB . MET A 14 ? 0.5720 0.5948 0.7258 0.0180 -0.2767 -0.0407 16 MET A CB 102 C CG . MET A 14 ? 0.5700 0.5980 0.7491 0.0115 -0.2579 -0.0454 16 MET A CG 103 S SD . MET A 14 ? 0.6995 0.7443 0.8965 -0.0075 -0.2580 -0.0579 16 MET A SD 104 C CE . MET A 14 ? 0.6277 0.6680 0.8411 -0.0113 -0.2334 -0.0587 16 MET A CE 105 N N . GLN A 15 ? 0.5764 0.6145 0.7646 0.0583 -0.2862 -0.0217 17 GLN A N 106 C CA . GLN A 15 ? 0.5656 0.6159 0.7835 0.0725 -0.2808 -0.0191 17 GLN A CA 107 C C . GLN A 15 ? 0.5127 0.5956 0.7707 0.0662 -0.2728 -0.0271 17 GLN A C 108 O O . GLN A 15 ? 0.5021 0.6092 0.7762 0.0554 -0.2801 -0.0325 17 GLN A O 109 C CB . GLN A 15 ? 0.5950 0.6593 0.8220 0.0910 -0.2990 -0.0115 17 GLN A CB 110 C CG . GLN A 15 ? 0.7046 0.7379 0.8920 0.0998 -0.3091 -0.0007 17 GLN A CG 111 C CD . GLN A 15 ? 0.7682 0.7633 0.9373 0.1079 -0.2956 0.0062 17 GLN A CD 112 O OE1 . GLN A 15 ? 0.8440 0.8228 1.0020 0.1241 -0.3030 0.0167 17 GLN A OE1 113 N NE2 . GLN A 15 ? 0.7723 0.7518 0.9378 0.0964 -0.2767 0.0006 17 GLN A NE2 114 N N . LEU A 16 ? 0.4818 0.5646 0.7553 0.0728 -0.2576 -0.0277 18 LEU A N 115 C CA . LEU A 16 ? 0.4499 0.5645 0.7607 0.0696 -0.2484 -0.0329 18 LEU A CA 116 C C . LEU A 16 ? 0.4468 0.5783 0.7831 0.0891 -0.2455 -0.0304 18 LEU A C 117 O O . LEU A 16 ? 0.4739 0.5820 0.7962 0.1018 -0.2404 -0.0280 18 LEU A O 118 C CB . LEU A 16 ? 0.4108 0.5118 0.7148 0.0576 -0.2291 -0.0377 18 LEU A CB 119 C CG . LEU A 16 ? 0.4119 0.4927 0.6906 0.0396 -0.2269 -0.0411 18 LEU A CG 120 C CD1 . LEU A 16 ? 0.3160 0.3828 0.5892 0.0331 -0.2075 -0.0443 18 LEU A CD1 121 C CD2 . LEU A 16 ? 0.3893 0.4910 0.6803 0.0251 -0.2376 -0.0458 18 LEU A CD2 122 N N . THR A 17 ? 0.4281 0.6006 0.8035 0.0909 -0.2473 -0.0318 19 THR A N 123 C CA . THR A 17 ? 0.4094 0.6030 0.8127 0.1081 -0.2395 -0.0311 19 THR A CA 124 C C . THR A 17 ? 0.3814 0.5739 0.7891 0.1036 -0.2174 -0.0353 19 THR A C 125 O O . THR A 17 ? 0.3459 0.5514 0.7643 0.0874 -0.2098 -0.0378 19 THR A O 126 C CB . THR A 17 ? 0.4119 0.6535 0.8575 0.1103 -0.2494 -0.0302 19 THR A CB 127 O OG1 . THR A 17 ? 0.4535 0.6934 0.8887 0.1128 -0.2722 -0.0267 19 THR A OG1 128 C CG2 . THR A 17 ? 0.3984 0.6661 0.8753 0.1329 -0.2424 -0.0286 19 THR A CG2 129 N N . VAL A 18 ? 0.3818 0.5561 0.7790 0.1184 -0.2076 -0.0363 20 VAL A N 130 C CA . VAL A 18 ? 0.3662 0.5407 0.7652 0.1178 -0.1880 -0.0407 20 VAL A CA 131 C C . VAL A 18 ? 0.3799 0.5607 0.7900 0.1413 -0.1827 -0.0421 20 VAL A C 132 O O . VAL A 18 ? 0.4127 0.5648 0.8038 0.1543 -0.1882 -0.0421 20 VAL A O 133 C CB . VAL A 18 ? 0.3709 0.5053 0.7339 0.1086 -0.1809 -0.0437 20 VAL A CB 134 C CG1 . VAL A 18 ? 0.3488 0.4905 0.7155 0.1030 -0.1631 -0.0475 20 VAL A CG1 135 C CG2 . VAL A 18 ? 0.3729 0.4905 0.7162 0.0909 -0.1899 -0.0419 20 VAL A CG2 136 N N . PHE A 19 ? 0.3649 0.5822 0.8056 0.1469 -0.1714 -0.0430 21 PHE A N 137 C CA . PHE A 19 ? 0.3736 0.6017 0.8264 0.1703 -0.1620 -0.0461 21 PHE A CA 138 C C . PHE A 19 ? 0.3971 0.6216 0.8549 0.1904 -0.1754 -0.0440 21 PHE A C 139 O O . PHE A 19 ? 0.4225 0.6237 0.8665 0.2083 -0.1722 -0.0481 21 PHE A O 140 C CB . PHE A 19 ? 0.3692 0.5664 0.7936 0.1755 -0.1484 -0.0534 21 PHE A CB 141 C CG . PHE A 19 ? 0.3557 0.5518 0.7697 0.1582 -0.1351 -0.0551 21 PHE A CG 142 C CD1 . PHE A 19 ? 0.3484 0.5086 0.7295 0.1544 -0.1307 -0.0607 21 PHE A CD1 143 C CD2 . PHE A 19 ? 0.3481 0.5787 0.7865 0.1464 -0.1271 -0.0507 21 PHE A CD2 144 C CE1 . PHE A 19 ? 0.3160 0.4755 0.6870 0.1411 -0.1191 -0.0618 21 PHE A CE1 145 C CE2 . PHE A 19 ? 0.3262 0.5531 0.7539 0.1327 -0.1146 -0.0508 21 PHE A CE2 146 C CZ . PHE A 19 ? 0.3387 0.5302 0.7317 0.1311 -0.1110 -0.0563 21 PHE A CZ 147 N N . GLY A 20 ? 0.4046 0.6514 0.8820 0.1883 -0.1912 -0.0380 22 GLY A N 148 C CA . GLY A 20 ? 0.4299 0.6793 0.9162 0.2093 -0.2059 -0.0341 22 GLY A CA 149 C C . GLY A 20 ? 0.4600 0.6581 0.9066 0.2124 -0.2173 -0.0316 22 GLY A C 150 O O . GLY A 20 ? 0.5020 0.6903 0.9482 0.2327 -0.2270 -0.0279 22 GLY A O 151 N N . GLY A 21 ? 0.4479 0.6129 0.8619 0.1932 -0.2153 -0.0327 23 GLY A N 152 C CA . GLY A 21 ? 0.4631 0.5818 0.8406 0.1922 -0.2250 -0.0285 23 GLY A CA 153 C C . GLY A 21 ? 0.4618 0.5765 0.8235 0.1683 -0.2320 -0.0258 23 GLY A C 154 O O . GLY A 21 ? 0.4589 0.6069 0.8411 0.1554 -0.2328 -0.0271 23 GLY A O 155 N N . THR A 22 ? 0.4711 0.5441 0.7965 0.1617 -0.2356 -0.0225 24 THR A N 156 C CA . THR A 22 ? 0.4528 0.5168 0.7573 0.1417 -0.2419 -0.0200 24 THR A CA 157 C C . THR A 22 ? 0.4473 0.4748 0.7223 0.1287 -0.2299 -0.0228 24 THR A C 158 O O . THR A 22 ? 0.4620 0.4583 0.7221 0.1364 -0.2245 -0.0226 24 THR A O 159 C CB . THR A 22 ? 0.4797 0.5318 0.7672 0.1487 -0.2610 -0.0102 24 THR A CB 160 O OG1 . THR A 22 ? 0.5012 0.5909 0.8199 0.1629 -0.2737 -0.0078 24 THR A OG1 161 C CG2 . THR A 22 ? 0.4762 0.5218 0.7405 0.1299 -0.2680 -0.0087 24 THR A CG2 162 N N . VAL A 23 ? 0.4263 0.4577 0.6945 0.1089 -0.2259 -0.0259 25 VAL A N 163 C CA . VAL A 23 ? 0.4005 0.4013 0.6410 0.0952 -0.2171 -0.0272 25 VAL A CA 164 C C . VAL A 23 ? 0.4326 0.4256 0.6509 0.0827 -0.2267 -0.0231 25 VAL A C 165 O O . VAL A 23 ? 0.4209 0.4389 0.6506 0.0778 -0.2358 -0.0241 25 VAL A O 166 C CB . VAL A 23 ? 0.3811 0.3938 0.6331 0.0853 -0.2019 -0.0353 25 VAL A CB 167 C CG1 . VAL A 23 ? 0.3256 0.3112 0.5518 0.0701 -0.1931 -0.0372 25 VAL A CG1 168 C CG2 . VAL A 23 ? 0.3583 0.3773 0.6264 0.0995 -0.1929 -0.0397 25 VAL A CG2 169 N N . THR A 24 ? 0.4527 0.4113 0.6391 0.0780 -0.2248 -0.0186 26 THR A N 170 C CA . THR A 24 ? 0.4541 0.4046 0.6156 0.0659 -0.2304 -0.0159 26 THR A CA 171 C C . THR A 24 ? 0.4448 0.3894 0.5989 0.0490 -0.2166 -0.0226 26 THR A C 172 O O . THR A 24 ? 0.4355 0.3627 0.5851 0.0468 -0.2041 -0.0239 26 THR A O 173 C CB . THR A 24 ? 0.4825 0.4001 0.6122 0.0702 -0.2344 -0.0055 26 THR A CB 174 O OG1 . THR A 24 ? 0.4664 0.3842 0.6033 0.0884 -0.2453 0.0014 26 THR A OG1 175 C CG2 . THR A 24 ? 0.4897 0.4036 0.5923 0.0613 -0.2421 -0.0025 26 THR A CG2 176 N N . ALA A 25 ? 0.4228 0.3818 0.5766 0.0375 -0.2194 -0.0274 27 ALA A N 177 C CA . ALA A 25 ? 0.4038 0.3596 0.5549 0.0238 -0.2065 -0.0339 27 ALA A CA 178 C C . ALA A 25 ? 0.4240 0.3637 0.5436 0.0151 -0.2093 -0.0329 27 ALA A C 179 O O . ALA A 25 ? 0.4330 0.3792 0.5437 0.0157 -0.2234 -0.0319 27 ALA A O 180 C CB . ALA A 25 ? 0.3585 0.3427 0.5381 0.0181 -0.2050 -0.0412 27 ALA A CB 181 N N . PHE A 26 ? 0.4073 0.3271 0.5099 0.0079 -0.1962 -0.0332 28 PHE A N 182 C CA . PHE A 26 ? 0.4291 0.3351 0.5025 -0.0008 -0.1943 -0.0339 28 PHE A CA 183 C C . PHE A 26 ? 0.4107 0.3220 0.4932 -0.0113 -0.1822 -0.0429 28 PHE A C 184 O O . PHE A 26 ? 0.3939 0.2983 0.4810 -0.0135 -0.1685 -0.0435 28 PHE A O 185 C CB . PHE A 26 ? 0.4525 0.3312 0.4999 0.0002 -0.1869 -0.0250 28 PHE A CB 186 C CG . PHE A 26 ? 0.4815 0.3495 0.5189 0.0115 -0.1974 -0.0139 28 PHE A CG 187 C CD1 . PHE A 26 ? 0.5177 0.3842 0.5742 0.0210 -0.1976 -0.0108 28 PHE A CD1 188 C CD2 . PHE A 26 ? 0.5390 0.3973 0.5465 0.0139 -0.2069 -0.0069 28 PHE A CD2 189 C CE1 . PHE A 26 ? 0.5491 0.4035 0.5975 0.0332 -0.2074 -0.0004 28 PHE A CE1 190 C CE2 . PHE A 26 ? 0.5945 0.4415 0.5917 0.0260 -0.2171 0.0051 28 PHE A CE2 191 C CZ . PHE A 26 ? 0.5813 0.4255 0.6004 0.0358 -0.2170 0.0085 28 PHE A CZ 192 N N . LEU A 27 ? 0.4105 0.3349 0.4987 -0.0172 -0.1881 -0.0503 29 LEU A N 193 C CA . LEU A 27 ? 0.3871 0.3152 0.4857 -0.0261 -0.1773 -0.0583 29 LEU A CA 194 C C . LEU A 27 ? 0.4116 0.3240 0.4814 -0.0334 -0.1740 -0.0630 29 LEU A C 195 O O . LEU A 27 ? 0.4282 0.3383 0.4786 -0.0346 -0.1858 -0.0652 29 LEU A O 196 C CB . LEU A 27 ? 0.3582 0.3092 0.4853 -0.0293 -0.1843 -0.0638 29 LEU A CB 197 C CG . LEU A 27 ? 0.3384 0.3103 0.4953 -0.0212 -0.1887 -0.0598 29 LEU A CG 198 C CD1 . LEU A 27 ? 0.2867 0.2820 0.4721 -0.0269 -0.1934 -0.0646 29 LEU A CD1 199 C CD2 . LEU A 27 ? 0.2982 0.2682 0.4661 -0.0153 -0.1750 -0.0567 29 LEU A CD2 200 N N . GLY A 28 ? 0.4045 0.3082 0.4719 -0.0374 -0.1586 -0.0656 30 GLY A N 201 C CA . GLY A 28 ? 0.4171 0.3067 0.4590 -0.0428 -0.1527 -0.0711 30 GLY A CA 202 C C . GLY A 28 ? 0.4680 0.3409 0.4763 -0.0408 -0.1498 -0.0652 30 GLY A C 203 O O . GLY A 28 ? 0.5098 0.3748 0.4906 -0.0426 -0.1546 -0.0690 30 GLY A O 204 N N . ILE A 29 ? 0.4743 0.3410 0.4830 -0.0374 -0.1419 -0.0559 31 ILE A N 205 C CA . ILE A 29 ? 0.4954 0.3453 0.4735 -0.0370 -0.1358 -0.0483 31 ILE A CA 206 C C . ILE A 29 ? 0.4953 0.3409 0.4702 -0.0419 -0.1177 -0.0527 31 ILE A C 207 O O . ILE A 29 ? 0.4571 0.3102 0.4574 -0.0430 -0.1093 -0.0549 31 ILE A O 208 C CB . ILE A 29 ? 0.4994 0.3423 0.4828 -0.0330 -0.1337 -0.0365 31 ILE A CB 209 C CG1 . ILE A 29 ? 0.5275 0.3757 0.5205 -0.0254 -0.1502 -0.0319 31 ILE A CG1 210 C CG2 . ILE A 29 ? 0.5338 0.3579 0.4861 -0.0341 -0.1255 -0.0265 31 ILE A CG2 211 C CD1 . ILE A 29 ? 0.4875 0.3238 0.4849 -0.0206 -0.1481 -0.0212 31 ILE A CD1 212 N N . PRO A 30 ? 0.5116 0.3464 0.4552 -0.0436 -0.1115 -0.0539 32 PRO A N 213 C CA . PRO A 30 ? 0.5089 0.3423 0.4534 -0.0465 -0.0930 -0.0579 32 PRO A CA 214 C C . PRO A 30 ? 0.5104 0.3411 0.4612 -0.0477 -0.0799 -0.0475 32 PRO A C 215 O O . PRO A 30 ? 0.5129 0.3349 0.4519 -0.0468 -0.0825 -0.0365 32 PRO A O 216 C CB . PRO A 30 ? 0.5553 0.3781 0.4625 -0.0467 -0.0902 -0.0631 32 PRO A CB 217 C CG . PRO A 30 ? 0.5804 0.3959 0.4601 -0.0437 -0.1053 -0.0557 32 PRO A CG 218 C CD . PRO A 30 ? 0.5500 0.3750 0.4566 -0.0416 -0.1205 -0.0519 32 PRO A CD 219 N N . TYR A 31 ? 0.4925 0.3309 0.4640 -0.0497 -0.0668 -0.0505 33 TYR A N 220 C CA . TYR A 31 ? 0.4985 0.3365 0.4792 -0.0526 -0.0551 -0.0418 33 TYR A CA 221 C C . TYR A 31 ? 0.5082 0.3501 0.4868 -0.0546 -0.0365 -0.0442 33 TYR A C 222 O O . TYR A 31 ? 0.5088 0.3544 0.4995 -0.0584 -0.0253 -0.0381 33 TYR A O 223 C CB . TYR A 31 ? 0.4623 0.3103 0.4777 -0.0527 -0.0590 -0.0417 33 TYR A CB 224 C CG . TYR A 31 ? 0.4173 0.2801 0.4572 -0.0515 -0.0554 -0.0509 33 TYR A CG 225 C CD1 . TYR A 31 ? 0.3718 0.2406 0.4210 -0.0481 -0.0653 -0.0578 33 TYR A CD1 226 C CD2 . TYR A 31 ? 0.3711 0.2426 0.4257 -0.0534 -0.0423 -0.0517 33 TYR A CD2 227 C CE1 . TYR A 31 ? 0.3277 0.2077 0.3974 -0.0463 -0.0611 -0.0641 33 TYR A CE1 228 C CE2 . TYR A 31 ? 0.3378 0.2231 0.4144 -0.0504 -0.0395 -0.0590 33 TYR A CE2 229 C CZ . TYR A 31 ? 0.3213 0.2092 0.4040 -0.0466 -0.0489 -0.0643 33 TYR A CZ 230 O OH . TYR A 31 ? 0.3124 0.2111 0.4139 -0.0431 -0.0456 -0.0691 33 TYR A OH 231 N N . ALA A 32 ? 0.5254 0.3666 0.4897 -0.0521 -0.0332 -0.0536 34 ALA A N 232 C CA . ALA A 32 ? 0.5323 0.3770 0.4926 -0.0518 -0.0142 -0.0563 34 ALA A CA 233 C C . ALA A 32 ? 0.5588 0.3934 0.4862 -0.0483 -0.0124 -0.0655 34 ALA A C 234 O O . ALA A 32 ? 0.5666 0.3943 0.4819 -0.0471 -0.0271 -0.0720 34 ALA A O 235 C CB . ALA A 32 ? 0.4829 0.3435 0.4794 -0.0504 -0.0088 -0.0619 34 ALA A CB 236 N N . GLN A 33 ? 0.5823 0.4171 0.4966 -0.0464 0.0055 -0.0673 35 GLN A N 237 C CA . GLN A 33 ? 0.6080 0.4330 0.4941 -0.0417 0.0082 -0.0797 35 GLN A CA 238 C C . GLN A 33 ? 0.5733 0.3996 0.4799 -0.0392 0.0013 -0.0927 35 GLN A C 239 O O . GLN A 33 ? 0.5563 0.3949 0.4963 -0.0381 0.0068 -0.0921 35 GLN A O 240 C CB . GLN A 33 ? 0.6392 0.4671 0.5134 -0.0384 0.0317 -0.0798 35 GLN A CB 241 C CG . GLN A 33 ? 0.7479 0.5681 0.5855 -0.0398 0.0398 -0.0690 35 GLN A CG 242 C CD . GLN A 33 ? 0.8758 0.7022 0.7041 -0.0363 0.0660 -0.0684 35 GLN A CD 243 O OE1 . GLN A 33 ? 0.9112 0.7372 0.7344 -0.0294 0.0744 -0.0820 35 GLN A OE1 244 N NE2 . GLN A 33 ? 0.8973 0.7295 0.7256 -0.0411 0.0800 -0.0523 35 GLN A NE2 245 N N . PRO A 34 ? 0.5749 0.3885 0.4621 -0.0385 -0.0110 -0.1042 36 PRO A N 246 C CA . PRO A 34 ? 0.5561 0.3674 0.4620 -0.0368 -0.0143 -0.1162 36 PRO A CA 247 C C . PRO A 34 ? 0.5442 0.3593 0.4616 -0.0302 0.0059 -0.1206 36 PRO A C 248 O O . PRO A 34 ? 0.5711 0.3821 0.4647 -0.0260 0.0204 -0.1232 36 PRO A O 249 C CB . PRO A 34 ? 0.5766 0.3704 0.4507 -0.0377 -0.0260 -0.1296 36 PRO A CB 250 C CG . PRO A 34 ? 0.6078 0.4008 0.4586 -0.0406 -0.0373 -0.1219 36 PRO A CG 251 C CD . PRO A 34 ? 0.6109 0.4112 0.4582 -0.0393 -0.0220 -0.1072 36 PRO A CD 252 N N . PRO A 35 ? 0.5063 0.3306 0.4594 -0.0280 0.0074 -0.1203 37 PRO A N 253 C CA . PRO A 35 ? 0.4989 0.3312 0.4663 -0.0204 0.0259 -0.1217 37 PRO A CA 254 C C . PRO A 35 ? 0.5259 0.3422 0.4851 -0.0136 0.0302 -0.1359 37 PRO A C 255 O O . PRO A 35 ? 0.5111 0.3288 0.4955 -0.0090 0.0312 -0.1378 37 PRO A O 256 C CB . PRO A 35 ? 0.4509 0.3015 0.4588 -0.0206 0.0230 -0.1132 37 PRO A CB 257 C CG . PRO A 35 ? 0.4486 0.2925 0.4617 -0.0261 0.0033 -0.1137 37 PRO A CG 258 C CD . PRO A 35 ? 0.4546 0.2879 0.4374 -0.0318 -0.0059 -0.1143 37 PRO A CD 259 N N . LEU A 36 ? 0.5752 0.3747 0.4972 -0.0123 0.0330 -0.1459 38 LEU A N 260 C CA . LEU A 36 ? 0.6014 0.3780 0.5073 -0.0072 0.0341 -0.1633 38 LEU A CA 261 C C . LEU A 36 ? 0.6220 0.3952 0.5087 0.0031 0.0546 -0.1702 38 LEU A C 262 O O . LEU A 36 ? 0.6229 0.4090 0.4986 0.0039 0.0663 -0.1624 38 LEU A O 263 C CB . LEU A 36 ? 0.6319 0.3899 0.5047 -0.0139 0.0181 -0.1730 38 LEU A CB 264 C CG . LEU A 36 ? 0.6453 0.4076 0.5234 -0.0247 -0.0037 -0.1666 38 LEU A CG 265 C CD1 . LEU A 36 ? 0.6923 0.4367 0.5324 -0.0286 -0.0169 -0.1795 38 LEU A CD1 266 C CD2 . LEU A 36 ? 0.6126 0.3772 0.5272 -0.0285 -0.0135 -0.1651 38 LEU A CD2 267 N N . GLY A 37 ? 0.6577 0.4126 0.5403 0.0110 0.0600 -0.1849 39 GLY A N 268 C CA . GLY A 37 ? 0.6896 0.4375 0.5497 0.0229 0.0799 -0.1950 39 GLY A CA 269 C C . GLY A 37 ? 0.6892 0.4649 0.5784 0.0307 0.0991 -0.1832 39 GLY A C 270 O O . GLY A 37 ? 0.6543 0.4421 0.5826 0.0336 0.0986 -0.1767 39 GLY A O 271 N N . ARG A 38 ? 0.7175 0.5051 0.5882 0.0336 0.1154 -0.1794 40 ARG A N 272 C CA . ARG A 38 ? 0.7121 0.5302 0.6119 0.0385 0.1340 -0.1674 40 ARG A CA 273 C C . ARG A 38 ? 0.6644 0.5073 0.6029 0.0285 0.1248 -0.1497 40 ARG A C 274 O O . ARG A 38 ? 0.6599 0.5279 0.6337 0.0328 0.1351 -0.1423 40 ARG A O 275 C CB . ARG A 38 ? 0.7594 0.5838 0.6283 0.0421 0.1547 -0.1666 40 ARG A CB 276 C CG . ARG A 38 ? 0.8179 0.6449 0.6625 0.0294 0.1492 -0.1544 40 ARG A CG 277 C CD . ARG A 38 ? 0.9116 0.7270 0.7032 0.0335 0.1625 -0.1597 40 ARG A CD 278 N NE . ARG A 38 ? 0.9817 0.7662 0.7345 0.0397 0.1549 -0.1808 40 ARG A NE 279 C CZ . ARG A 38 ? 1.0350 0.8017 0.7336 0.0399 0.1532 -0.1878 40 ARG A CZ 280 N NH1 . ARG A 38 ? 1.0527 0.8283 0.7281 0.0347 0.1590 -0.1733 40 ARG A NH1 281 N NH2 . ARG A 38 ? 1.0491 0.7879 0.7160 0.0449 0.1448 -0.2093 40 ARG A NH2 282 N N . LEU A 39 ? 0.6334 0.4696 0.5668 0.0163 0.1046 -0.1444 41 LEU A N 283 C CA . LEU A 39 ? 0.5599 0.4156 0.5253 0.0074 0.0948 -0.1298 41 LEU A CA 284 C C . LEU A 39 ? 0.5282 0.3874 0.5282 0.0090 0.0832 -0.1297 41 LEU A C 285 O O . LEU A 39 ? 0.4703 0.3484 0.4999 0.0045 0.0776 -0.1192 41 LEU A O 286 C CB . LEU A 39 ? 0.5483 0.3971 0.4925 -0.0046 0.0807 -0.1225 41 LEU A CB 287 C CG . LEU A 39 ? 0.5810 0.4272 0.4898 -0.0067 0.0918 -0.1181 41 LEU A CG 288 C CD1 . LEU A 39 ? 0.5639 0.4008 0.4501 -0.0162 0.0765 -0.1104 41 LEU A CD1 289 C CD2 . LEU A 39 ? 0.5930 0.4644 0.5231 -0.0061 0.1131 -0.1071 41 LEU A CD2 290 N N . ARG A 40 ? 0.5344 0.3744 0.5299 0.0155 0.0800 -0.1412 42 ARG A N 291 C CA . ARG A 40 ? 0.5102 0.3515 0.5362 0.0179 0.0707 -0.1394 42 ARG A CA 292 C C . ARG A 40 ? 0.4862 0.3548 0.5480 0.0259 0.0809 -0.1316 42 ARG A C 293 O O . ARG A 40 ? 0.4931 0.3701 0.5568 0.0357 0.0984 -0.1346 42 ARG A O 294 C CB . ARG A 40 ? 0.5256 0.3395 0.5421 0.0248 0.0698 -0.1526 42 ARG A CB 295 C CG . ARG A 40 ? 0.4966 0.3106 0.5429 0.0283 0.0629 -0.1484 42 ARG A CG 296 C CD . ARG A 40 ? 0.5511 0.3363 0.5912 0.0367 0.0659 -0.1603 42 ARG A CD 297 N NE . ARG A 40 ? 0.5074 0.2654 0.5264 0.0263 0.0526 -0.1694 42 ARG A NE 298 C CZ . ARG A 40 ? 0.5376 0.2653 0.5474 0.0290 0.0520 -0.1817 42 ARG A CZ 299 N NH1 . ARG A 40 ? 0.5734 0.2896 0.5902 0.0437 0.0649 -0.1866 42 ARG A NH1 300 N NH2 . ARG A 40 ? 0.5591 0.2671 0.5533 0.0170 0.0381 -0.1896 42 ARG A NH2 301 N N . PHE A 41 ? 0.4537 0.3369 0.5434 0.0227 0.0700 -0.1224 43 PHE A N 302 C CA . PHE A 41 ? 0.4255 0.3382 0.5522 0.0293 0.0749 -0.1146 43 PHE A CA 303 C C . PHE A 41 ? 0.4144 0.3534 0.5518 0.0230 0.0819 -0.1072 43 PHE A C 304 O O . PHE A 41 ? 0.3984 0.3644 0.5672 0.0262 0.0848 -0.1017 43 PHE A O 305 C CB . PHE A 41 ? 0.4329 0.3481 0.5723 0.0460 0.0879 -0.1194 43 PHE A CB 306 C CG . PHE A 41 ? 0.4357 0.3236 0.5693 0.0536 0.0833 -0.1256 43 PHE A CG 307 C CD1 . PHE A 41 ? 0.3960 0.2799 0.5419 0.0515 0.0694 -0.1201 43 PHE A CD1 308 C CD2 . PHE A 41 ? 0.4637 0.3302 0.5808 0.0639 0.0947 -0.1370 43 PHE A CD2 309 C CE1 . PHE A 41 ? 0.3871 0.2446 0.5290 0.0573 0.0667 -0.1242 43 PHE A CE1 310 C CE2 . PHE A 41 ? 0.4522 0.2907 0.5657 0.0703 0.0911 -0.1427 43 PHE A CE2 311 C CZ . PHE A 41 ? 0.4223 0.2559 0.5488 0.0663 0.0773 -0.1356 43 PHE A CZ 312 N N . LYS A 42 ? 0.4276 0.3587 0.5395 0.0140 0.0848 -0.1068 44 LYS A N 313 C CA . LYS A 42 ? 0.4325 0.3850 0.5548 0.0062 0.0919 -0.0981 44 LYS A CA 314 C C . LYS A 42 ? 0.4262 0.3780 0.5505 -0.0068 0.0758 -0.0904 44 LYS A C 315 O O . LYS A 42 ? 0.4150 0.3493 0.5268 -0.0097 0.0604 -0.0922 44 LYS A O 316 C CB . LYS A 42 ? 0.4688 0.4156 0.5631 0.0056 0.1087 -0.0996 44 LYS A CB 317 C CG . LYS A 42 ? 0.5087 0.4590 0.6029 0.0203 0.1276 -0.1079 44 LYS A CG 318 C CD . LYS A 42 ? 0.6064 0.5517 0.6689 0.0209 0.1462 -0.1097 44 LYS A CD 319 C CE . LYS A 42 ? 0.6784 0.6459 0.7519 0.0103 0.1562 -0.0966 44 LYS A CE 320 N NZ . LYS A 42 ? 0.7558 0.7378 0.8251 0.0174 0.1833 -0.0969 44 LYS A NZ 321 N N . LYS A 43 ? 0.4155 0.3872 0.5583 -0.0143 0.0802 -0.0822 45 LYS A N 322 C CA . LYS A 43 ? 0.4104 0.3817 0.5566 -0.0260 0.0684 -0.0750 45 LYS A CA 323 C C . LYS A 43 ? 0.4396 0.3843 0.5463 -0.0312 0.0636 -0.0742 45 LYS A C 324 O O . LYS A 43 ? 0.4659 0.3996 0.5448 -0.0284 0.0745 -0.0772 45 LYS A O 325 C CB . LYS A 43 ? 0.4085 0.4032 0.5801 -0.0338 0.0779 -0.0674 45 LYS A CB 326 C CG . LYS A 43 ? 0.3776 0.3996 0.5914 -0.0311 0.0727 -0.0682 45 LYS A CG 327 C CD . LYS A 43 ? 0.3713 0.4211 0.6159 -0.0383 0.0836 -0.0629 45 LYS A CD 328 C CE . LYS A 43 ? 0.4303 0.4771 0.6793 -0.0544 0.0785 -0.0556 45 LYS A CE 329 N NZ . LYS A 43 ? 0.3896 0.4660 0.6763 -0.0638 0.0883 -0.0510 45 LYS A NZ 330 N N . PRO A 44 ? 0.4214 0.3564 0.5245 -0.0374 0.0469 -0.0710 46 PRO A N 331 C CA . PRO A 44 ? 0.4446 0.3572 0.5129 -0.0411 0.0400 -0.0698 46 PRO A CA 332 C C . PRO A 44 ? 0.4897 0.4003 0.5417 -0.0470 0.0522 -0.0614 46 PRO A C 333 O O . PRO A 44 ? 0.4817 0.4060 0.5555 -0.0532 0.0587 -0.0538 46 PRO A O 334 C CB . PRO A 44 ? 0.4388 0.3485 0.5167 -0.0456 0.0217 -0.0663 46 PRO A CB 335 C CG . PRO A 44 ? 0.3611 0.2919 0.4766 -0.0474 0.0222 -0.0636 46 PRO A CG 336 C CD . PRO A 44 ? 0.3741 0.3209 0.5056 -0.0410 0.0351 -0.0678 46 PRO A CD 337 N N . GLN A 45 ? 0.5444 0.4385 0.5585 -0.0454 0.0560 -0.0627 47 GLN A N 338 C CA . GLN A 45 ? 0.5947 0.4847 0.5867 -0.0499 0.0691 -0.0531 47 GLN A CA 339 C C . GLN A 45 ? 0.6298 0.5027 0.6016 -0.0552 0.0544 -0.0453 47 GLN A C 340 O O . GLN A 45 ? 0.6049 0.4673 0.5678 -0.0530 0.0364 -0.0507 47 GLN A O 341 C CB . GLN A 45 ? 0.6278 0.5086 0.5837 -0.0431 0.0818 -0.0594 47 GLN A CB 342 C CG . GLN A 45 ? 0.6462 0.5403 0.6174 -0.0345 0.0965 -0.0691 47 GLN A CG 343 C CD . GLN A 45 ? 0.7052 0.6256 0.7127 -0.0371 0.1128 -0.0618 47 GLN A CD 344 O OE1 . GLN A 45 ? 0.7642 0.6891 0.7650 -0.0431 0.1269 -0.0511 47 GLN A OE1 345 N NE2 . GLN A 45 ? 0.6316 0.5705 0.6789 -0.0329 0.1110 -0.0669 47 GLN A NE2 346 N N . SER A 46 ? 0.6846 0.5546 0.6494 -0.0620 0.0626 -0.0319 48 SER A N 347 C CA . SER A 46 ? 0.7435 0.5969 0.6933 -0.0661 0.0488 -0.0225 48 SER A CA 348 C C . SER A 46 ? 0.7971 0.6318 0.6992 -0.0610 0.0421 -0.0235 48 SER A C 349 O O . SER A 46 ? 0.8256 0.6577 0.7001 -0.0565 0.0534 -0.0280 48 SER A O 350 C CB . SER A 46 ? 0.7578 0.6105 0.7187 -0.0759 0.0582 -0.0065 48 SER A CB 351 O OG . SER A 46 ? 0.8218 0.6687 0.7532 -0.0772 0.0765 0.0030 48 SER A OG 352 N N . LEU A 47 ? 0.8345 0.6572 0.7281 -0.0610 0.0229 -0.0201 49 LEU A N 353 C CA . LEU A 47 ? 0.9012 0.7093 0.7561 -0.0560 0.0099 -0.0224 49 LEU A CA 354 C C . LEU A 47 ? 0.9712 0.7653 0.7839 -0.0558 0.0185 -0.0095 49 LEU A C 355 O O . LEU A 47 ? 0.9803 0.7687 0.7955 -0.0607 0.0247 0.0065 49 LEU A O 356 C CB . LEU A 47 ? 0.8885 0.6931 0.7553 -0.0553 -0.0131 -0.0218 49 LEU A CB 357 C CG . LEU A 47 ? 0.9161 0.7147 0.7586 -0.0501 -0.0307 -0.0307 49 LEU A CG 358 C CD1 . LEU A 47 ? 0.9189 0.7207 0.7529 -0.0477 -0.0256 -0.0467 49 LEU A CD1 359 C CD2 . LEU A 47 ? 0.9039 0.7074 0.7732 -0.0496 -0.0496 -0.0325 49 LEU A CD2 360 N N . THR A 48 ? 1.0289 0.8160 0.8020 -0.0500 0.0178 -0.0172 50 THR A N 361 C CA . THR A 48 ? 1.1096 0.8853 0.8348 -0.0474 0.0295 -0.0085 50 THR A CA 362 C C . THR A 48 ? 1.1459 0.9057 0.8448 -0.0472 0.0193 0.0091 50 THR A C 363 O O . THR A 48 ? 1.1881 0.9397 0.8613 -0.0483 0.0353 0.0245 50 THR A O 364 C CB . THR A 48 ? 1.1504 0.9210 0.8360 -0.0399 0.0272 -0.0254 50 THR A CB 365 O OG1 . THR A 48 ? 1.1295 0.9044 0.8358 -0.0387 0.0094 -0.0433 50 THR A OG1 366 C CG2 . THR A 48 ? 1.1793 0.9559 0.8546 -0.0373 0.0544 -0.0307 50 THR A CG2 367 N N . LYS A 49 ? 1.1313 0.8874 0.8374 -0.0452 -0.0059 0.0075 51 LYS A N 368 C CA . LYS A 49 ? 1.1693 0.9102 0.8467 -0.0410 -0.0223 0.0210 51 LYS A CA 369 C C . LYS A 49 ? 1.1890 0.9264 0.8298 -0.0333 -0.0433 0.0105 51 LYS A C 370 O O . LYS A 49 ? 1.2189 0.9569 0.8320 -0.0307 -0.0387 -0.0021 51 LYS A O 371 C CB . LYS A 49 ? 1.2180 0.9442 0.8685 -0.0424 -0.0062 0.0438 51 LYS A CB 372 C CG . LYS A 49 ? 1.3148 1.0252 0.9042 -0.0344 -0.0123 0.0535 51 LYS A CG 373 C CD . LYS A 49 ? 1.4048 1.1167 0.9502 -0.0301 -0.0002 0.0428 51 LYS A CD 374 C CE . LYS A 49 ? 1.4362 1.1514 0.9793 -0.0349 0.0339 0.0496 51 LYS A CE 375 N NZ . LYS A 49 ? 1.4679 1.1707 1.0020 -0.0392 0.0494 0.0770 51 LYS A NZ 376 N N . TRP A 50 ? 1.1710 0.9057 0.8133 -0.0293 -0.0670 0.0146 52 TRP A N 377 C CA . TRP A 50 ? 1.1751 0.9092 0.7852 -0.0226 -0.0893 0.0056 52 TRP A CA 378 C C . TRP A 50 ? 1.2077 0.9299 0.7906 -0.0154 -0.1038 0.0241 52 TRP A C 379 O O . TRP A 50 ? 1.2093 0.9225 0.8041 -0.0156 -0.0986 0.0426 52 TRP A O 380 C CB . TRP A 50 ? 1.1234 0.8729 0.7672 -0.0241 -0.1084 -0.0137 52 TRP A CB 381 C CG . TRP A 50 ? 1.0445 0.8005 0.7270 -0.0234 -0.1227 -0.0071 52 TRP A CG 382 C CD1 . TRP A 50 ? 1.0194 0.7747 0.6952 -0.0166 -0.1444 0.0009 52 TRP A CD1 383 C CD2 . TRP A 50 ? 0.9379 0.7026 0.6705 -0.0282 -0.1161 -0.0078 52 TRP A CD2 384 N NE1 . TRP A 50 ? 0.9449 0.7078 0.6647 -0.0166 -0.1505 0.0043 52 TRP A NE1 385 C CE2 . TRP A 50 ? 0.8985 0.6665 0.6517 -0.0239 -0.1334 -0.0010 52 TRP A CE2 386 C CE3 . TRP A 50 ? 0.8814 0.6525 0.6429 -0.0346 -0.0979 -0.0140 52 TRP A CE3 387 C CZ2 . TRP A 50 ? 0.8266 0.6024 0.6251 -0.0260 -0.1319 -0.0009 52 TRP A CZ2 388 C CZ3 . TRP A 50 ? 0.7886 0.5685 0.5956 -0.0370 -0.0984 -0.0134 52 TRP A CZ3 389 C CH2 . TRP A 50 ? 0.7734 0.5547 0.5966 -0.0329 -0.1147 -0.0074 52 TRP A CH2 390 N N . SER A 51 ? 1.2356 0.9571 0.7814 -0.0086 -0.1226 0.0186 53 SER A N 391 C CA . SER A 51 ? 1.2693 0.9800 0.7815 0.0007 -0.1378 0.0359 53 SER A CA 392 C C . SER A 51 ? 1.2606 0.9845 0.7691 0.0051 -0.1674 0.0200 53 SER A C 393 O O . SER A 51 ? 1.2833 1.0121 0.7725 0.0033 -0.1705 0.0011 53 SER A O 394 C CB . SER A 51 ? 1.3255 1.0198 0.7776 0.0046 -0.1230 0.0482 53 SER A CB 395 O OG . SER A 51 ? 1.3850 1.0714 0.7967 0.0155 -0.1433 0.0597 53 SER A OG 396 N N . ASP A 52 ? 1.2325 0.9620 0.7606 0.0109 -0.1889 0.0273 54 ASP A N 397 C CA . ASP A 52 ? 1.1904 0.9405 0.7429 0.0120 -0.2162 0.0115 54 ASP A CA 398 C C . ASP A 52 ? 1.0989 0.8604 0.7134 0.0089 -0.2162 0.0119 54 ASP A C 399 O O . ASP A 52 ? 1.0638 0.8168 0.6988 0.0050 -0.1962 0.0208 54 ASP A O 400 C CB . ASP A 52 ? 1.2034 0.9638 0.7499 0.0054 -0.2207 -0.0148 54 ASP A CB 401 C CG . ASP A 52 ? 1.1979 0.9607 0.7785 -0.0056 -0.1982 -0.0275 54 ASP A CG 402 O OD1 . ASP A 52 ? 1.1872 0.9543 0.8120 -0.0090 -0.1888 -0.0220 54 ASP A OD1 403 O OD2 . ASP A 52 ? 1.2634 1.0234 0.8252 -0.0097 -0.1907 -0.0440 54 ASP A OD2 404 N N . ILE A 53 ? 1.0457 0.8273 0.6892 0.0106 -0.2389 0.0023 55 ILE A N 405 C CA . ILE A 53 ? 0.9658 0.7603 0.6648 0.0092 -0.2398 0.0018 55 ILE A CA 406 C C . ILE A 53 ? 0.9228 0.7331 0.6562 -0.0017 -0.2356 -0.0188 55 ILE A C 407 O O . ILE A 53 ? 0.9145 0.7379 0.6470 -0.0049 -0.2505 -0.0344 55 ILE A O 408 C CB . ILE A 53 ? 0.9705 0.7789 0.6854 0.0196 -0.2649 0.0076 55 ILE A CB 409 C CG1 . ILE A 53 ? 0.9819 0.7709 0.6571 0.0322 -0.2698 0.0298 55 ILE A CG1 410 C CG2 . ILE A 53 ? 0.8891 0.7116 0.6628 0.0185 -0.2622 0.0056 55 ILE A CG2 411 C CD1 . ILE A 53 ? 0.9436 0.7424 0.6324 0.0458 -0.2924 0.0395 55 ILE A CD1 412 N N . TRP A 54 ? 0.8720 0.6796 0.6343 -0.0076 -0.2152 -0.0186 56 TRP A N 413 C CA . TRP A 54 ? 0.8231 0.6430 0.6178 -0.0166 -0.2090 -0.0351 56 TRP A CA 414 C C . TRP A 54 ? 0.7966 0.6374 0.6359 -0.0151 -0.2228 -0.0379 56 TRP A C 415 O O . TRP A 54 ? 0.7855 0.6272 0.6464 -0.0099 -0.2211 -0.0273 56 TRP A O 416 C CB . TRP A 54 ? 0.7863 0.5980 0.5948 -0.0219 -0.1837 -0.0328 56 TRP A CB 417 C CG . TRP A 54 ? 0.7387 0.5627 0.5803 -0.0290 -0.1788 -0.0475 56 TRP A CG 418 C CD1 . TRP A 54 ? 0.6688 0.5091 0.5537 -0.0300 -0.1840 -0.0509 56 TRP A CD1 419 C CD2 . TRP A 54 ? 0.7362 0.5567 0.5696 -0.0354 -0.1675 -0.0609 56 TRP A CD2 420 N NE1 . TRP A 54 ? 0.6719 0.5181 0.5752 -0.0371 -0.1763 -0.0639 56 TRP A NE1 421 C CE2 . TRP A 54 ? 0.7016 0.5350 0.5752 -0.0403 -0.1664 -0.0705 56 TRP A CE2 422 C CE3 . TRP A 54 ? 0.8094 0.6164 0.6054 -0.0364 -0.1561 -0.0648 56 TRP A CE3 423 C CZ2 . TRP A 54 ? 0.7216 0.5528 0.5996 -0.0459 -0.1559 -0.0836 56 TRP A CZ2 424 C CZ3 . TRP A 54 ? 0.8228 0.6286 0.6238 -0.0414 -0.1451 -0.0797 56 TRP A CZ3 425 C CH2 . TRP A 54 ? 0.7651 0.5820 0.6073 -0.0460 -0.1458 -0.0886 56 TRP A CH2 426 N N . ASN A 55 ? 0.7964 0.6537 0.6503 -0.0200 -0.2357 -0.0526 57 ASN A N 427 C CA . ASN A 55 ? 0.7844 0.6651 0.6813 -0.0191 -0.2486 -0.0551 57 ASN A CA 428 C C . ASN A 55 ? 0.7180 0.6054 0.6550 -0.0251 -0.2328 -0.0596 57 ASN A C 429 O O . ASN A 55 ? 0.7192 0.6072 0.6630 -0.0342 -0.2259 -0.0717 57 ASN A O 430 C CB . ASN A 55 ? 0.8250 0.7217 0.7220 -0.0232 -0.2700 -0.0684 57 ASN A CB 431 C CG . ASN A 55 ? 0.9506 0.8506 0.8208 -0.0137 -0.2921 -0.0617 57 ASN A CG 432 O OD1 . ASN A 55 ? 0.9659 0.8560 0.8203 -0.0028 -0.2917 -0.0454 57 ASN A OD1 433 N ND2 . ASN A 55 ? 1.1379 1.0515 1.0033 -0.0179 -0.3127 -0.0746 57 ASN A ND2 434 N N . ALA A 56 ? 0.6616 0.5521 0.6224 -0.0192 -0.2271 -0.0498 58 ALA A N 435 C CA . ALA A 56 ? 0.5875 0.4840 0.5819 -0.0229 -0.2126 -0.0526 58 ALA A CA 436 C C . ALA A 56 ? 0.5516 0.4738 0.5857 -0.0212 -0.2227 -0.0555 58 ALA A C 437 O O . ALA A 56 ? 0.5402 0.4695 0.5976 -0.0141 -0.2200 -0.0493 58 ALA A O 438 C CB . ALA A 56 ? 0.5678 0.4500 0.5608 -0.0179 -0.1991 -0.0415 58 ALA A CB 439 N N . THR A 57 ? 0.5321 0.4686 0.5749 -0.0278 -0.2339 -0.0655 59 THR A N 440 C CA . THR A 57 ? 0.5172 0.4815 0.5971 -0.0262 -0.2459 -0.0668 59 THR A CA 441 C C . THR A 57 ? 0.4979 0.4750 0.6077 -0.0375 -0.2397 -0.0767 59 THR A C 442 O O . THR A 57 ? 0.4844 0.4861 0.6267 -0.0395 -0.2481 -0.0790 59 THR A O 443 C CB . THR A 57 ? 0.5515 0.5283 0.6229 -0.0238 -0.2698 -0.0685 59 THR A CB 444 O OG1 . THR A 57 ? 0.5586 0.5235 0.6010 -0.0331 -0.2740 -0.0788 59 THR A OG1 445 C CG2 . THR A 57 ? 0.5460 0.5141 0.5941 -0.0097 -0.2780 -0.0557 59 THR A CG2 446 N N . LYS A 58 ? 0.4961 0.4566 0.5961 -0.0448 -0.2244 -0.0817 60 LYS A N 447 C CA . LYS A 58 ? 0.4869 0.4558 0.6158 -0.0538 -0.2159 -0.0880 60 LYS A CA 448 C C . LYS A 58 ? 0.4604 0.4125 0.5828 -0.0542 -0.1953 -0.0868 60 LYS A C 449 O O . LYS A 58 ? 0.4691 0.4019 0.5619 -0.0518 -0.1889 -0.0854 60 LYS A O 450 C CB . LYS A 58 ? 0.4998 0.4720 0.6315 -0.0661 -0.2267 -0.1005 60 LYS A CB 451 C CG . LYS A 58 ? 0.5674 0.5150 0.6619 -0.0712 -0.2258 -0.1098 60 LYS A CG 452 C CD . LYS A 58 ? 0.6650 0.6172 0.7638 -0.0831 -0.2412 -0.1239 60 LYS A CD 453 C CE . LYS A 58 ? 0.7729 0.6977 0.8356 -0.0891 -0.2382 -0.1372 60 LYS A CE 454 N NZ . LYS A 58 ? 0.8025 0.7046 0.8250 -0.0806 -0.2245 -0.1328 60 LYS A NZ 455 N N . TYR A 59 ? 0.4171 0.3780 0.5675 -0.0566 -0.1849 -0.0863 61 TYR A N 456 C CA . TYR A 59 ? 0.4122 0.3580 0.5563 -0.0573 -0.1672 -0.0865 61 TYR A CA 457 C C . TYR A 59 ? 0.4213 0.3462 0.5401 -0.0638 -0.1636 -0.0953 61 TYR A C 458 O O . TYR A 59 ? 0.4407 0.3637 0.5560 -0.0711 -0.1728 -0.1039 61 TYR A O 459 C CB . TYR A 59 ? 0.3785 0.3363 0.5536 -0.0592 -0.1579 -0.0847 61 TYR A CB 460 C CG . TYR A 59 ? 0.3330 0.3086 0.5290 -0.0505 -0.1557 -0.0765 61 TYR A CG 461 C CD1 . TYR A 59 ? 0.2654 0.2350 0.4532 -0.0419 -0.1477 -0.0715 61 TYR A CD1 462 C CD2 . TYR A 59 ? 0.2935 0.2923 0.5190 -0.0512 -0.1606 -0.0747 61 TYR A CD2 463 C CE1 . TYR A 59 ? 0.2403 0.2238 0.4451 -0.0334 -0.1453 -0.0662 61 TYR A CE1 464 C CE2 . TYR A 59 ? 0.2516 0.2664 0.4947 -0.0419 -0.1563 -0.0682 61 TYR A CE2 465 C CZ . TYR A 59 ? 0.2696 0.2749 0.5001 -0.0326 -0.1489 -0.0647 61 TYR A CZ 466 O OH . TYR A 59 ? 0.3460 0.3641 0.5902 -0.0227 -0.1450 -0.0605 61 TYR A OH 467 N N . ALA A 60 ? 0.3848 0.3338 0.5116 -0.0540 -0.0909 -0.0628 62 ALA A N 468 C CA . ALA A 60 ? 0.3994 0.3324 0.5083 -0.0588 -0.0859 -0.0683 62 ALA A CA 469 C C . ALA A 60 ? 0.3949 0.3265 0.5130 -0.0613 -0.0799 -0.0726 62 ALA A C 470 O O . ALA A 60 ? 0.3789 0.3213 0.5157 -0.0597 -0.0792 -0.0707 62 ALA A O 471 C CB . ALA A 60 ? 0.3918 0.3140 0.4880 -0.0555 -0.0775 -0.0678 62 ALA A CB 472 N N . ASN A 61 ? 0.3905 0.3078 0.4940 -0.0650 -0.0756 -0.0785 63 ASN A N 473 C CA . ASN A 61 ? 0.3965 0.3078 0.5049 -0.0656 -0.0688 -0.0828 63 ASN A CA 474 C C . ASN A 61 ? 0.3644 0.2814 0.4886 -0.0590 -0.0609 -0.0805 63 ASN A C 475 O O . ASN A 61 ? 0.3348 0.2523 0.4578 -0.0544 -0.0555 -0.0789 63 ASN A O 476 C CB . ASN A 61 ? 0.4218 0.3158 0.5106 -0.0670 -0.0624 -0.0894 63 ASN A CB 477 C CG . ASN A 61 ? 0.4562 0.3405 0.5251 -0.0742 -0.0694 -0.0931 63 ASN A CG 478 O OD1 . ASN A 61 ? 0.4537 0.3426 0.5256 -0.0797 -0.0787 -0.0924 63 ASN A OD1 479 N ND2 . ASN A 61 ? 0.4890 0.3599 0.5373 -0.0748 -0.0643 -0.0976 63 ASN A ND2 480 N N . SER A 62 ? 0.3526 0.2728 0.4902 -0.0595 -0.0602 -0.0806 64 SER A N 481 C CA . SER A 62 ? 0.3343 0.2563 0.4838 -0.0541 -0.0528 -0.0798 64 SER A CA 482 C C . SER A 62 ? 0.3601 0.2680 0.5001 -0.0522 -0.0450 -0.0859 64 SER A C 483 O O . SER A 62 ? 0.3688 0.2647 0.4956 -0.0563 -0.0461 -0.0909 64 SER A O 484 C CB . SER A 62 ? 0.3202 0.2484 0.4843 -0.0559 -0.0551 -0.0777 64 SER A CB 485 O OG . SER A 62 ? 0.2605 0.2040 0.4352 -0.0569 -0.0612 -0.0728 64 SER A OG 486 N N . CYS A 63 ? 0.3355 0.2454 0.4824 -0.0460 -0.0374 -0.0857 65 CYS A N 487 C CA . CYS A 63 ? 0.3493 0.2495 0.4919 -0.0425 -0.0298 -0.0913 65 CYS A CA 488 C C . CYS A 63 ? 0.3520 0.2419 0.4963 -0.0429 -0.0303 -0.0946 65 CYS A C 489 O O . CYS A 63 ? 0.3372 0.2307 0.4913 -0.0446 -0.0346 -0.0909 65 CYS A O 490 C CB . CYS A 63 ? 0.3295 0.2379 0.4823 -0.0361 -0.0226 -0.0898 65 CYS A CB 491 S SG . CYS A 63 ? 0.3361 0.2517 0.4829 -0.0369 -0.0213 -0.0864 65 CYS A SG 492 N N . CYS A 64 ? 0.3610 0.2376 0.4955 -0.0408 -0.0253 -0.1013 66 CYS A N 493 C CA . CYS A 64 ? 0.3987 0.2616 0.5320 -0.0406 -0.0260 -0.1046 66 CYS A CA 494 C C . CYS A 64 ? 0.3875 0.2566 0.5374 -0.0355 -0.0252 -0.1003 66 CYS A C 495 O O . CYS A 64 ? 0.3714 0.2516 0.5315 -0.0294 -0.0206 -0.0984 66 CYS A O 496 C CB . CYS A 64 ? 0.4220 0.2703 0.5439 -0.0361 -0.0192 -0.1129 66 CYS A CB 497 S SG . CYS A 64 ? 0.5094 0.3479 0.6079 -0.0425 -0.0197 -0.1187 66 CYS A SG 498 N N . GLN A 65 ? 0.3746 0.2363 0.5264 -0.0386 -0.0296 -0.0988 67 GLN A N 499 C CA . GLN A 65 ? 0.3775 0.2432 0.5426 -0.0346 -0.0294 -0.0943 67 GLN A CA 500 C C . GLN A 65 ? 0.4043 0.2553 0.5655 -0.0397 -0.0339 -0.0938 67 GLN A C 501 O O . GLN A 65 ? 0.4037 0.2492 0.5565 -0.0486 -0.0386 -0.0948 67 GLN A O 502 C CB . GLN A 65 ? 0.3457 0.2311 0.5234 -0.0357 -0.0314 -0.0874 67 GLN A CB 503 C CG . GLN A 65 ? 0.3560 0.2472 0.5332 -0.0446 -0.0379 -0.0841 67 GLN A CG 504 C CD . GLN A 65 ? 0.3685 0.2790 0.5567 -0.0440 -0.0392 -0.0784 67 GLN A CD 505 O OE1 . GLN A 65 ? 0.3082 0.2262 0.5066 -0.0445 -0.0406 -0.0739 67 GLN A OE1 506 N NE2 . GLN A 65 ? 0.3456 0.2625 0.5303 -0.0428 -0.0385 -0.0788 67 GLN A NE2 507 N N . ASN A 66 ? 0.4010 0.2455 0.5676 -0.0344 -0.0328 -0.0923 68 ASN A N 508 C CA . ASN A 66 ? 0.4288 0.2616 0.5933 -0.0399 -0.0371 -0.0894 68 ASN A CA 509 C C . ASN A 66 ? 0.4188 0.2670 0.5922 -0.0474 -0.0409 -0.0825 68 ASN A C 510 O O . ASN A 66 ? 0.4084 0.2752 0.5924 -0.0450 -0.0399 -0.0789 68 ASN A O 511 C CB . ASN A 66 ? 0.4228 0.2444 0.5900 -0.0313 -0.0354 -0.0886 68 ASN A CB 512 C CG . ASN A 66 ? 0.4918 0.2944 0.6489 -0.0239 -0.0321 -0.0964 68 ASN A CG 513 O OD1 . ASN A 66 ? 0.5614 0.3482 0.7047 -0.0289 -0.0331 -0.1014 68 ASN A OD1 514 N ND2 . ASN A 66 ? 0.4645 0.2703 0.6289 -0.0122 -0.0280 -0.0978 68 ASN A ND2 515 N N . ILE A 67 ? 0.4404 0.2800 0.6094 -0.0565 -0.0450 -0.0808 69 ILE A N 516 C CA . ILE A 67 ? 0.4604 0.3150 0.6372 -0.0649 -0.0482 -0.0754 69 ILE A CA 517 C C . ILE A 67 ? 0.4595 0.3081 0.6387 -0.0674 -0.0487 -0.0703 69 ILE A C 518 O O . ILE A 67 ? 0.4675 0.2947 0.6376 -0.0673 -0.0490 -0.0714 69 ILE A O 519 C CB . ILE A 67 ? 0.4836 0.3359 0.6526 -0.0763 -0.0528 -0.0782 69 ILE A CB 520 C CG1 . ILE A 67 ? 0.4932 0.3655 0.6674 -0.0763 -0.0542 -0.0784 69 ILE A CG1 521 C CG2 . ILE A 67 ? 0.5147 0.3698 0.6869 -0.0871 -0.0562 -0.0742 69 ILE A CG2 522 C CD1 . ILE A 67 ? 0.5050 0.3693 0.6679 -0.0736 -0.0535 -0.0844 69 ILE A CD1 523 N N . ASP A 68 ? 0.4551 0.3218 0.6455 -0.0698 -0.0488 -0.0646 70 ASP A N 524 C CA . ASP A 68 ? 0.4749 0.3381 0.6668 -0.0740 -0.0490 -0.0591 70 ASP A CA 525 C C . ASP A 68 ? 0.4881 0.3424 0.6732 -0.0882 -0.0522 -0.0584 70 ASP A C 526 O O . ASP A 68 ? 0.4863 0.3577 0.6781 -0.0963 -0.0538 -0.0574 70 ASP A O 527 C CB . ASP A 68 ? 0.4565 0.3434 0.6620 -0.0721 -0.0472 -0.0541 70 ASP A CB 528 C CG . ASP A 68 ? 0.4864 0.3712 0.6924 -0.0769 -0.0466 -0.0482 70 ASP A CG 529 O OD1 . ASP A 68 ? 0.4837 0.3863 0.6991 -0.0765 -0.0449 -0.0447 70 ASP A OD1 530 O OD2 . ASP A 68 ? 0.5323 0.3961 0.7278 -0.0811 -0.0478 -0.0471 70 ASP A OD2 531 N N . GLN A 69 ? 0.5057 0.3340 0.6779 -0.0909 -0.0533 -0.0592 71 GLN A N 532 C CA . GLN A 69 ? 0.5417 0.3580 0.7052 -0.1057 -0.0563 -0.0587 71 GLN A CA 533 C C . GLN A 69 ? 0.5388 0.3465 0.6995 -0.1111 -0.0557 -0.0523 71 GLN A C 534 O O . GLN A 69 ? 0.5424 0.3340 0.6929 -0.1231 -0.0577 -0.0515 71 GLN A O 535 C CB . GLN A 69 ? 0.5626 0.3496 0.7091 -0.1067 -0.0583 -0.0646 71 GLN A CB 536 C CG . GLN A 69 ? 0.6286 0.4174 0.7735 -0.0986 -0.0578 -0.0716 71 GLN A CG 537 C CD . GLN A 69 ? 0.6757 0.4332 0.8033 -0.0950 -0.0580 -0.0779 71 GLN A CD 538 O OE1 . GLN A 69 ? 0.6902 0.4266 0.8047 -0.1050 -0.0610 -0.0792 71 GLN A OE1 539 N NE2 . GLN A 69 ? 0.6341 0.3889 0.7617 -0.0810 -0.0546 -0.0820 71 GLN A NE2 540 N N . SER A 70 ? 0.5135 0.3312 0.6819 -0.1036 -0.0530 -0.0476 72 SER A N 541 C CA . SER A 70 ? 0.5293 0.3373 0.6926 -0.1087 -0.0524 -0.0410 72 SER A CA 542 C C . SER A 70 ? 0.5162 0.3391 0.6841 -0.1243 -0.0517 -0.0375 72 SER A C 543 O O . SER A 70 ? 0.5424 0.3506 0.7008 -0.1336 -0.0518 -0.0333 72 SER A O 544 C CB . SER A 70 ? 0.5221 0.3368 0.6911 -0.0969 -0.0501 -0.0369 72 SER A CB 545 O OG . SER A 70 ? 0.5401 0.3497 0.7100 -0.0823 -0.0502 -0.0408 72 SER A OG 546 N N . PHE A 71 ? 0.4680 0.3197 0.6502 -0.1271 -0.0510 -0.0390 73 PHE A N 547 C CA . PHE A 71 ? 0.4608 0.3301 0.6499 -0.1416 -0.0500 -0.0360 73 PHE A CA 548 C C . PHE A 71 ? 0.4423 0.3281 0.6391 -0.1490 -0.0531 -0.0405 73 PHE A C 549 O O . PHE A 71 ? 0.4215 0.3362 0.6338 -0.1472 -0.0523 -0.0406 73 PHE A O 550 C CB . PHE A 71 ? 0.4408 0.3348 0.6430 -0.1372 -0.0456 -0.0319 73 PHE A CB 551 C CG . PHE A 71 ? 0.4182 0.2982 0.6130 -0.1296 -0.0433 -0.0276 73 PHE A CG 552 C CD1 . PHE A 71 ? 0.4517 0.3133 0.6339 -0.1386 -0.0425 -0.0224 73 PHE A CD1 553 C CD2 . PHE A 71 ? 0.3303 0.2137 0.5291 -0.1145 -0.0427 -0.0284 73 PHE A CD2 554 C CE1 . PHE A 71 ? 0.4365 0.2840 0.6103 -0.1318 -0.0416 -0.0178 73 PHE A CE1 555 C CE2 . PHE A 71 ? 0.3660 0.2366 0.5578 -0.1078 -0.0418 -0.0243 73 PHE A CE2 556 C CZ . PHE A 71 ? 0.3672 0.2199 0.5463 -0.1160 -0.0416 -0.0189 73 PHE A CZ 557 N N . PRO A 72 ? 0.4446 0.3113 0.6298 -0.1562 -0.0572 -0.0444 74 PRO A N 558 C CA . PRO A 72 ? 0.4301 0.3124 0.6216 -0.1624 -0.0613 -0.0489 74 PRO A CA 559 C C . PRO A 72 ? 0.4180 0.3289 0.6242 -0.1749 -0.0608 -0.0462 74 PRO A C 560 O O . PRO A 72 ? 0.4187 0.3265 0.6229 -0.1855 -0.0583 -0.0420 74 PRO A O 561 C CB . PRO A 72 ? 0.4507 0.3039 0.6243 -0.1714 -0.0653 -0.0529 74 PRO A CB 562 C CG . PRO A 72 ? 0.4826 0.3037 0.6408 -0.1673 -0.0633 -0.0507 74 PRO A CG 563 C CD . PRO A 72 ? 0.4599 0.2902 0.6254 -0.1598 -0.0585 -0.0445 74 PRO A CD 564 N N . GLY A 73 ? 0.4010 0.3398 0.6219 -0.1730 -0.0632 -0.0484 75 GLY A N 565 C CA . GLY A 73 ? 0.3909 0.3621 0.6295 -0.1826 -0.0631 -0.0467 75 GLY A CA 566 C C . GLY A 73 ? 0.3681 0.3619 0.6211 -0.1751 -0.0569 -0.0426 75 GLY A C 567 O O . GLY A 73 ? 0.3597 0.3814 0.6283 -0.1813 -0.0556 -0.0414 75 GLY A O 568 N N . PHE A 74 ? 0.3470 0.3287 0.5945 -0.1623 -0.0531 -0.0407 76 PHE A N 569 C CA . PHE A 74 ? 0.3363 0.3341 0.5934 -0.1564 -0.0470 -0.0369 76 PHE A CA 570 C C . PHE A 74 ? 0.3180 0.3298 0.5841 -0.1409 -0.0474 -0.0388 76 PHE A C 571 O O . PHE A 74 ? 0.3128 0.3093 0.5709 -0.1312 -0.0490 -0.0406 76 PHE A O 572 C CB . PHE A 74 ? 0.3321 0.3061 0.5756 -0.1538 -0.0430 -0.0329 76 PHE A CB 573 C CG . PHE A 74 ? 0.2839 0.2722 0.5345 -0.1472 -0.0371 -0.0294 76 PHE A CG 574 C CD1 . PHE A 74 ? 0.2738 0.2876 0.5368 -0.1544 -0.0327 -0.0274 76 PHE A CD1 575 C CD2 . PHE A 74 ? 0.2556 0.2329 0.5009 -0.1340 -0.0358 -0.0284 76 PHE A CD2 576 C CE1 . PHE A 74 ? 0.2545 0.2803 0.5225 -0.1477 -0.0269 -0.0250 76 PHE A CE1 577 C CE2 . PHE A 74 ? 0.2781 0.2664 0.5279 -0.1284 -0.0309 -0.0256 76 PHE A CE2 578 C CZ . PHE A 74 ? 0.2579 0.2696 0.5182 -0.1351 -0.0263 -0.0240 76 PHE A CZ 579 N N . HIS A 75 ? 0.3188 0.3601 0.6016 -0.1389 -0.0458 -0.0384 77 HIS A N 580 C CA . HIS A 75 ? 0.3014 0.3569 0.5931 -0.1251 -0.0469 -0.0402 77 HIS A CA 581 C C . HIS A 75 ? 0.2959 0.3405 0.5820 -0.1125 -0.0429 -0.0387 77 HIS A C 582 O O . HIS A 75 ? 0.2821 0.3261 0.5682 -0.1013 -0.0445 -0.0405 77 HIS A O 583 C CB . HIS A 75 ? 0.2766 0.3661 0.5880 -0.1261 -0.0459 -0.0401 77 HIS A CB 584 C CG . HIS A 75 ? 0.3272 0.4298 0.6468 -0.1124 -0.0481 -0.0418 77 HIS A CG 585 N ND1 . HIS A 75 ? 0.3435 0.4410 0.6593 -0.1079 -0.0547 -0.0445 77 HIS A ND1 586 C CD2 . HIS A 75 ? 0.3558 0.4725 0.6842 -0.1020 -0.0443 -0.0411 77 HIS A CD2 587 C CE1 . HIS A 75 ? 0.3681 0.4761 0.6902 -0.0958 -0.0552 -0.0448 77 HIS A CE1 588 N NE2 . HIS A 75 ? 0.3632 0.4824 0.6932 -0.0916 -0.0490 -0.0430 77 HIS A NE2 589 N N . GLY A 76 ? 0.3007 0.3363 0.5811 -0.1149 -0.0380 -0.0353 78 GLY A N 590 C CA . GLY A 76 ? 0.2900 0.3167 0.5654 -0.1040 -0.0348 -0.0338 78 GLY A CA 591 C C . GLY A 76 ? 0.3140 0.3193 0.5790 -0.0968 -0.0380 -0.0358 78 GLY A C 592 O O . GLY A 76 ? 0.2775 0.2826 0.5430 -0.0857 -0.0372 -0.0364 78 GLY A O 593 N N . SER A 77 ? 0.3256 0.3125 0.5806 -0.1029 -0.0412 -0.0371 79 SER A N 594 C CA . SER A 77 ? 0.3292 0.2974 0.5751 -0.0949 -0.0432 -0.0398 79 SER A CA 595 C C . SER A 77 ? 0.3193 0.2927 0.5671 -0.0935 -0.0471 -0.0441 79 SER A C 596 O O . SER A 77 ? 0.2902 0.2604 0.5361 -0.0843 -0.0474 -0.0464 79 SER A O 597 C CB . SER A 77 ? 0.3478 0.2890 0.5795 -0.0992 -0.0443 -0.0395 79 SER A CB 598 O OG . SER A 77 ? 0.3876 0.3261 0.6164 -0.1126 -0.0463 -0.0396 79 SER A OG 599 N N . GLU A 78 ? 0.3142 0.2949 0.5645 -0.1036 -0.0502 -0.0453 80 GLU A N 600 C CA . GLU A 78 ? 0.3258 0.3089 0.5752 -0.1039 -0.0551 -0.0493 80 GLU A CA 601 C C . GLU A 78 ? 0.3102 0.3119 0.5688 -0.0950 -0.0561 -0.0500 80 GLU A C 602 O O . GLU A 78 ? 0.3224 0.3202 0.5760 -0.0915 -0.0593 -0.0530 80 GLU A O 603 C CB . GLU A 78 ? 0.3330 0.3207 0.5833 -0.1178 -0.0592 -0.0504 80 GLU A CB 604 C CG . GLU A 78 ? 0.3805 0.3404 0.6150 -0.1258 -0.0601 -0.0517 80 GLU A CG 605 C CD . GLU A 78 ? 0.4488 0.4102 0.6818 -0.1410 -0.0649 -0.0535 80 GLU A CD 606 O OE1 . GLU A 78 ? 0.4471 0.3845 0.6658 -0.1480 -0.0666 -0.0555 80 GLU A OE1 607 O OE2 . GLU A 78 ? 0.5126 0.4999 0.7594 -0.1461 -0.0671 -0.0530 80 GLU A OE2 608 N N . MET A 79 ? 0.2872 0.3074 0.5577 -0.0914 -0.0533 -0.0472 81 MET A N 609 C CA . MET A 79 ? 0.2721 0.3061 0.5495 -0.0818 -0.0541 -0.0475 81 MET A CA 610 C C . MET A 79 ? 0.2738 0.2934 0.5422 -0.0720 -0.0531 -0.0489 81 MET A C 611 O O . MET A 79 ? 0.2809 0.3075 0.5513 -0.0652 -0.0547 -0.0495 81 MET A O 612 C CB . MET A 79 ? 0.2652 0.3174 0.5548 -0.0779 -0.0500 -0.0448 81 MET A CB 613 C CG . MET A 79 ? 0.2913 0.3332 0.5765 -0.0744 -0.0442 -0.0425 81 MET A CG 614 S SD . MET A 79 ? 0.2995 0.3618 0.5966 -0.0715 -0.0389 -0.0400 81 MET A SD 615 C CE . MET A 79 ? 0.2317 0.2987 0.5312 -0.0578 -0.0403 -0.0415 81 MET A CE 616 N N . TRP A 80 ? 0.2608 0.2614 0.5199 -0.0711 -0.0503 -0.0492 82 TRP A N 617 C CA . TRP A 80 ? 0.2697 0.2590 0.5222 -0.0622 -0.0484 -0.0506 82 TRP A CA 618 C C . TRP A 80 ? 0.2873 0.2614 0.5285 -0.0630 -0.0504 -0.0548 82 TRP A C 619 O O . TRP A 80 ? 0.2860 0.2540 0.5222 -0.0563 -0.0487 -0.0567 82 TRP A O 620 C CB . TRP A 80 ? 0.2567 0.2372 0.5077 -0.0581 -0.0441 -0.0486 82 TRP A CB 621 C CG . TRP A 80 ? 0.2525 0.2457 0.5118 -0.0572 -0.0414 -0.0449 82 TRP A CG 622 C CD1 . TRP A 80 ? 0.2726 0.2667 0.5333 -0.0631 -0.0398 -0.0420 82 TRP A CD1 623 C CD2 . TRP A 80 ? 0.2162 0.2220 0.4820 -0.0507 -0.0399 -0.0440 82 TRP A CD2 624 N NE1 . TRP A 80 ? 0.2097 0.2174 0.4777 -0.0603 -0.0369 -0.0397 82 TRP A NE1 625 C CE2 . TRP A 80 ? 0.2315 0.2458 0.5027 -0.0523 -0.0371 -0.0411 82 TRP A CE2 626 C CE3 . TRP A 80 ? 0.1667 0.1755 0.4328 -0.0438 -0.0403 -0.0453 82 TRP A CE3 627 C CZ2 . TRP A 80 ? 0.2747 0.2997 0.5512 -0.0464 -0.0348 -0.0402 82 TRP A CZ2 628 C CZ3 . TRP A 80 ? 0.1706 0.1886 0.4417 -0.0386 -0.0385 -0.0440 82 TRP A CZ3 629 C CH2 . TRP A 80 ? 0.2500 0.2763 0.5265 -0.0395 -0.0358 -0.0418 82 TRP A CH2 630 N N . ASN A 81 ? 0.2908 0.2585 0.5272 -0.0717 -0.0535 -0.0564 83 ASN A N 631 C CA . ASN A 81 ? 0.3051 0.2584 0.5296 -0.0738 -0.0557 -0.0609 83 ASN A CA 632 C C . ASN A 81 ? 0.3090 0.2708 0.5321 -0.0725 -0.0593 -0.0627 83 ASN A C 633 O O . ASN A 81 ? 0.3168 0.2965 0.5491 -0.0730 -0.0622 -0.0605 83 ASN A O 634 C CB . ASN A 81 ? 0.3145 0.2591 0.5341 -0.0849 -0.0587 -0.0619 83 ASN A CB 635 C CG . ASN A 81 ? 0.3587 0.2866 0.5737 -0.0856 -0.0556 -0.0607 83 ASN A CG 636 O OD1 . ASN A 81 ? 0.3268 0.2474 0.5406 -0.0765 -0.0517 -0.0602 83 ASN A OD1 637 N ND2 . ASN A 81 ? 0.3437 0.2652 0.5558 -0.0963 -0.0575 -0.0598 83 ASN A ND2 638 N N . PRO A 82 ? 0.3077 0.2564 0.5186 -0.0708 -0.0594 -0.0669 84 PRO A N 639 C CA . PRO A 82 ? 0.3015 0.2549 0.5075 -0.0691 -0.0624 -0.0683 84 PRO A CA 640 C C . PRO A 82 ? 0.3118 0.2738 0.5185 -0.0774 -0.0700 -0.0686 84 PRO A C 641 O O . PRO A 82 ? 0.3078 0.2638 0.5119 -0.0857 -0.0722 -0.0702 84 PRO A O 642 C CB . PRO A 82 ? 0.3162 0.2510 0.5069 -0.0672 -0.0597 -0.0734 84 PRO A CB 643 C CG . PRO A 82 ? 0.3493 0.2712 0.5393 -0.0654 -0.0550 -0.0745 84 PRO A CG 644 C CD . PRO A 82 ? 0.3266 0.2555 0.5281 -0.0678 -0.0551 -0.0700 84 PRO A CD 645 N N . ASN A 83 ? 0.3092 0.2850 0.5194 -0.0751 -0.0743 -0.0669 85 ASN A N 646 C CA . ASN A 83 ? 0.3172 0.3058 0.5311 -0.0819 -0.0827 -0.0668 85 ASN A CA 647 C C . ASN A 83 ? 0.3366 0.3198 0.5367 -0.0819 -0.0881 -0.0691 85 ASN A C 648 O O . ASN A 83 ? 0.3500 0.3458 0.5531 -0.0848 -0.0962 -0.0683 85 ASN A O 649 C CB . ASN A 83 ? 0.2972 0.3098 0.5295 -0.0785 -0.0845 -0.0623 85 ASN A CB 650 C CG . ASN A 83 ? 0.3053 0.3211 0.5384 -0.0673 -0.0825 -0.0598 85 ASN A CG 651 O OD1 . ASN A 83 ? 0.3397 0.3412 0.5621 -0.0624 -0.0779 -0.0609 85 ASN A OD1 652 N ND2 . ASN A 83 ? 0.2909 0.3255 0.5370 -0.0632 -0.0855 -0.0568 85 ASN A ND2 653 N N . THR A 84 ? 0.3491 0.3148 0.5342 -0.0783 -0.0837 -0.0720 86 THR A N 654 C CA . THR A 84 ? 0.3671 0.3227 0.5342 -0.0806 -0.0878 -0.0753 86 THR A CA 655 C C . THR A 84 ? 0.4008 0.3341 0.5526 -0.0831 -0.0826 -0.0811 86 THR A C 656 O O . THR A 84 ? 0.4208 0.3474 0.5768 -0.0799 -0.0754 -0.0816 86 THR A O 657 C CB . THR A 84 ? 0.3801 0.3363 0.5413 -0.0729 -0.0869 -0.0732 86 THR A CB 658 O OG1 . THR A 84 ? 0.3183 0.2642 0.4761 -0.0670 -0.0771 -0.0743 86 THR A OG1 659 C CG2 . THR A 84 ? 0.3304 0.3064 0.5068 -0.0682 -0.0912 -0.0676 86 THR A CG2 660 N N . ASP A 85 ? 0.3987 0.3202 0.5324 -0.0878 -0.0862 -0.0856 87 ASP A N 661 C CA . ASP A 85 ? 0.4326 0.3321 0.5499 -0.0889 -0.0808 -0.0920 87 ASP A CA 662 C C . ASP A 85 ? 0.4224 0.3151 0.5392 -0.0800 -0.0705 -0.0929 87 ASP A C 663 O O . ASP A 85 ? 0.4141 0.3143 0.5332 -0.0739 -0.0679 -0.0899 87 ASP A O 664 C CB . ASP A 85 ? 0.4581 0.3466 0.5534 -0.0928 -0.0845 -0.0965 87 ASP A CB 665 C CG . ASP A 85 ? 0.4994 0.3934 0.5922 -0.1026 -0.0960 -0.0967 87 ASP A CG 666 O OD1 . ASP A 85 ? 0.4775 0.3588 0.5605 -0.1105 -0.0983 -0.1016 87 ASP A OD1 667 O OD2 . ASP A 85 ? 0.6306 0.5418 0.7313 -0.1022 -0.1032 -0.0919 87 ASP A OD2 668 N N . LEU A 86 ? 0.4395 0.3171 0.5524 -0.0794 -0.0650 -0.0973 88 LEU A N 669 C CA . LEU A 86 ? 0.4368 0.3077 0.5494 -0.0707 -0.0552 -0.0993 88 LEU A CA 670 C C . LEU A 86 ? 0.4666 0.3245 0.5590 -0.0702 -0.0516 -0.1056 88 LEU A C 671 O O . LEU A 86 ? 0.4987 0.3436 0.5757 -0.0762 -0.0548 -0.1106 88 LEU A O 672 C CB . LEU A 86 ? 0.4342 0.2940 0.5513 -0.0694 -0.0518 -0.1012 88 LEU A CB 673 C CG . LEU A 86 ? 0.3871 0.2567 0.5215 -0.0711 -0.0545 -0.0953 88 LEU A CG 674 C CD1 . LEU A 86 ? 0.3364 0.1935 0.4733 -0.0662 -0.0492 -0.0967 88 LEU A CD1 675 C CD2 . LEU A 86 ? 0.3396 0.2299 0.4889 -0.0662 -0.0539 -0.0890 88 LEU A CD2 676 N N . SER A 87 ? 0.4677 0.3288 0.5593 -0.0636 -0.0446 -0.1056 89 SER A N 677 C CA . SER A 87 ? 0.4812 0.3305 0.5536 -0.0632 -0.0393 -0.1118 89 SER A CA 678 C C . SER A 87 ? 0.4774 0.3330 0.5566 -0.0550 -0.0292 -0.1114 89 SER A C 679 O O . SER A 87 ? 0.4482 0.3179 0.5417 -0.0521 -0.0293 -0.1052 89 SER A O 680 C CB . SER A 87 ? 0.4841 0.3361 0.5433 -0.0687 -0.0458 -0.1099 89 SER A CB 681 O OG . SER A 87 ? 0.4908 0.3326 0.5305 -0.0683 -0.0397 -0.1150 89 SER A OG 682 N N . GLU A 88 ? 0.4808 0.3269 0.5496 -0.0517 -0.0205 -0.1182 90 GLU A N 683 C CA . GLU A 88 ? 0.4631 0.3175 0.5359 -0.0461 -0.0109 -0.1181 90 GLU A CA 684 C C . GLU A 88 ? 0.4645 0.3262 0.5299 -0.0498 -0.0130 -0.1131 90 GLU A C 685 O O . GLU A 88 ? 0.4322 0.3039 0.5049 -0.0470 -0.0079 -0.1098 90 GLU A O 686 C CB . GLU A 88 ? 0.4740 0.3180 0.5353 -0.0426 -0.0007 -0.1272 90 GLU A CB 687 C CG . GLU A 88 ? 0.4411 0.2766 0.5093 -0.0371 0.0017 -0.1321 90 GLU A CG 688 C CD . GLU A 88 ? 0.5057 0.3344 0.5663 -0.0312 0.0130 -0.1411 90 GLU A CD 689 O OE1 . GLU A 88 ? 0.4889 0.3005 0.5305 -0.0332 0.0142 -0.1486 90 GLU A OE1 690 O OE2 . GLU A 88 ? 0.4515 0.2926 0.5253 -0.0246 0.0209 -0.1411 90 GLU A OE2 691 N N . ASP A 89 ? 0.4715 0.3275 0.5223 -0.0564 -0.0212 -0.1122 91 ASP A N 692 C CA . ASP A 89 ? 0.4836 0.3435 0.5251 -0.0594 -0.0245 -0.1073 91 ASP A CA 693 C C . ASP A 89 ? 0.4552 0.3287 0.5144 -0.0584 -0.0325 -0.0988 91 ASP A C 694 O O . ASP A 89 ? 0.4632 0.3385 0.5222 -0.0621 -0.0428 -0.0962 91 ASP A O 695 C CB . ASP A 89 ? 0.4973 0.3451 0.5144 -0.0663 -0.0305 -0.1101 91 ASP A CB 696 C CG . ASP A 89 ? 0.5535 0.4038 0.5590 -0.0692 -0.0359 -0.1040 91 ASP A CG 697 O OD1 . ASP A 89 ? 0.4828 0.3418 0.4969 -0.0660 -0.0335 -0.0982 91 ASP A OD1 698 O OD2 . ASP A 89 ? 0.6094 0.4516 0.5963 -0.0748 -0.0434 -0.1049 91 ASP A OD2 699 N N . CYS A 90 ? 0.4265 0.3103 0.5014 -0.0534 -0.0276 -0.0950 92 CYS A N 700 C CA . CYS A 90 ? 0.3914 0.2873 0.4848 -0.0513 -0.0336 -0.0884 92 CYS A CA 701 C C . CYS A 90 ? 0.3759 0.2794 0.4746 -0.0484 -0.0309 -0.0830 92 CYS A C 702 O O . CYS A 90 ? 0.3445 0.2578 0.4589 -0.0455 -0.0338 -0.0782 92 CYS A O 703 C CB . CYS A 90 ? 0.3678 0.2672 0.4789 -0.0483 -0.0318 -0.0897 92 CYS A CB 704 S SG . CYS A 90 ? 0.3851 0.2861 0.5050 -0.0418 -0.0195 -0.0930 92 CYS A SG 705 N N . LEU A 91 ? 0.3815 0.2798 0.4662 -0.0496 -0.0252 -0.0839 93 LEU A N 706 C CA . LEU A 91 ? 0.3621 0.2661 0.4517 -0.0477 -0.0216 -0.0791 93 LEU A CA 707 C C . LEU A 91 ? 0.3618 0.2638 0.4424 -0.0492 -0.0303 -0.0728 93 LEU A C 708 O O . LEU A 91 ? 0.3921 0.2854 0.4532 -0.0525 -0.0299 -0.0717 93 LEU A O 709 C CB . LEU A 91 ? 0.3623 0.2638 0.4444 -0.0487 -0.0100 -0.0827 93 LEU A CB 710 C CG . LEU A 91 ? 0.3994 0.3053 0.4935 -0.0452 -0.0011 -0.0887 93 LEU A CG 711 C CD1 . LEU A 91 ? 0.3424 0.2500 0.4314 -0.0463 0.0109 -0.0921 93 LEU A CD1 712 C CD2 . LEU A 91 ? 0.3461 0.2627 0.4638 -0.0403 -0.0027 -0.0861 93 LEU A CD2 713 N N . TYR A 92 ? 0.3347 0.2445 0.4289 -0.0464 -0.0380 -0.0687 94 TYR A N 714 C CA . TYR A 92 ? 0.3274 0.2370 0.4162 -0.0459 -0.0476 -0.0630 94 TYR A CA 715 C C . TYR A 92 ? 0.3172 0.2366 0.4242 -0.0408 -0.0487 -0.0586 94 TYR A C 716 O O . TYR A 92 ? 0.2780 0.2049 0.4018 -0.0387 -0.0439 -0.0601 94 TYR A O 717 C CB . TYR A 92 ? 0.3476 0.2585 0.4339 -0.0481 -0.0580 -0.0637 94 TYR A CB 718 C CG . TYR A 92 ? 0.3786 0.2782 0.4450 -0.0537 -0.0572 -0.0691 94 TYR A CG 719 C CD1 . TYR A 92 ? 0.3736 0.2708 0.4425 -0.0556 -0.0518 -0.0756 94 TYR A CD1 720 C CD2 . TYR A 92 ? 0.3760 0.2657 0.4197 -0.0569 -0.0618 -0.0676 94 TYR A CD2 721 C CE1 . TYR A 92 ? 0.4123 0.2976 0.4619 -0.0603 -0.0504 -0.0813 94 TYR A CE1 722 C CE2 . TYR A 92 ? 0.3767 0.2550 0.4003 -0.0623 -0.0604 -0.0730 94 TYR A CE2 723 C CZ . TYR A 92 ? 0.4421 0.3184 0.4688 -0.0639 -0.0542 -0.0801 94 TYR A CZ 724 O OH . TYR A 92 ? 0.5238 0.3875 0.5294 -0.0687 -0.0521 -0.0862 94 TYR A OH 725 N N . LEU A 93 ? 0.3171 0.2353 0.4198 -0.0386 -0.0555 -0.0533 95 LEU A N 726 C CA . LEU A 93 ? 0.3057 0.2309 0.4223 -0.0332 -0.0571 -0.0492 95 LEU A CA 727 C C . LEU A 93 ? 0.3239 0.2521 0.4402 -0.0296 -0.0687 -0.0450 95 LEU A C 728 O O . LEU A 93 ? 0.3424 0.2652 0.4445 -0.0318 -0.0754 -0.0445 95 LEU A O 729 C CB . LEU A 93 ? 0.2832 0.2020 0.3954 -0.0329 -0.0500 -0.0474 95 LEU A CB 730 C CG . LEU A 93 ? 0.3346 0.2390 0.4244 -0.0353 -0.0509 -0.0442 95 LEU A CG 731 C CD1 . LEU A 93 ? 0.3113 0.2116 0.3956 -0.0304 -0.0616 -0.0383 95 LEU A CD1 732 C CD2 . LEU A 93 ? 0.3101 0.2097 0.3972 -0.0378 -0.0412 -0.0440 95 LEU A CD2 733 N N . ASN A 94 ? 0.3029 0.2407 0.4354 -0.0239 -0.0709 -0.0425 96 ASN A N 734 C CA . ASN A 94 ? 0.3194 0.2645 0.4579 -0.0185 -0.0806 -0.0391 96 ASN A CA 735 C C . ASN A 94 ? 0.3247 0.2639 0.4612 -0.0124 -0.0805 -0.0350 96 ASN A C 736 O O . ASN A 94 ? 0.3164 0.2528 0.4565 -0.0122 -0.0728 -0.0354 96 ASN A O 737 C CB . ASN A 94 ? 0.2975 0.2604 0.4583 -0.0171 -0.0817 -0.0408 96 ASN A CB 738 C CG . ASN A 94 ? 0.3273 0.2928 0.4900 -0.0241 -0.0793 -0.0454 96 ASN A CG 739 O OD1 . ASN A 94 ? 0.3446 0.3063 0.4965 -0.0284 -0.0841 -0.0468 96 ASN A OD1 740 N ND2 . ASN A 94 ? 0.2682 0.2375 0.4421 -0.0253 -0.0719 -0.0477 96 ASN A ND2 741 N N . VAL A 95 ? 0.3427 0.2793 0.4731 -0.0073 -0.0898 -0.0312 97 VAL A N 742 C CA . VAL A 95 ? 0.3367 0.2658 0.4646 -0.0003 -0.0911 -0.0272 97 VAL A CA 743 C C . VAL A 95 ? 0.3449 0.2867 0.4861 0.0086 -0.1003 -0.0254 97 VAL A C 744 O O . VAL A 95 ? 0.3610 0.3092 0.5014 0.0093 -0.1096 -0.0247 97 VAL A O 745 C CB . VAL A 95 ? 0.3688 0.2761 0.4711 -0.0018 -0.0924 -0.0235 97 VAL A CB 746 C CG1 . VAL A 95 ? 0.3394 0.2367 0.4393 0.0051 -0.0929 -0.0198 97 VAL A CG1 747 C CG2 . VAL A 95 ? 0.3324 0.2294 0.4215 -0.0115 -0.0823 -0.0259 97 VAL A CG2 748 N N . TRP A 96 ? 0.3177 0.2658 0.4729 0.0151 -0.0977 -0.0253 98 TRP A N 749 C CA . TRP A 96 ? 0.3301 0.2909 0.4983 0.0250 -0.1058 -0.0239 98 TRP A CA 750 C C . TRP A 96 ? 0.3453 0.2902 0.5036 0.0334 -0.1075 -0.0203 98 TRP A C 751 O O . TRP A 96 ? 0.3538 0.2891 0.5095 0.0327 -0.0996 -0.0208 98 TRP A O 752 C CB . TRP A 96 ? 0.2815 0.2631 0.4740 0.0269 -0.1017 -0.0270 98 TRP A CB 753 C CG . TRP A 96 ? 0.3132 0.3119 0.5175 0.0195 -0.1019 -0.0301 98 TRP A CG 754 C CD1 . TRP A 96 ? 0.2699 0.2868 0.4862 0.0207 -0.1099 -0.0304 98 TRP A CD1 755 C CD2 . TRP A 96 ? 0.2668 0.2665 0.4734 0.0104 -0.0940 -0.0333 98 TRP A CD2 756 N NE1 . TRP A 96 ? 0.2925 0.3194 0.5164 0.0116 -0.1073 -0.0336 98 TRP A NE1 757 C CE2 . TRP A 96 ? 0.2981 0.3140 0.5159 0.0058 -0.0978 -0.0353 98 TRP A CE2 758 C CE3 . TRP A 96 ? 0.2687 0.2571 0.4688 0.0056 -0.0849 -0.0347 98 TRP A CE3 759 C CZ2 . TRP A 96 ? 0.2304 0.2483 0.4509 -0.0030 -0.0926 -0.0385 98 TRP A CZ2 760 C CZ3 . TRP A 96 ? 0.2717 0.2645 0.4768 -0.0020 -0.0797 -0.0380 98 TRP A CZ3 761 C CH2 . TRP A 96 ? 0.2527 0.2586 0.4670 -0.0060 -0.0835 -0.0397 98 TRP A CH2 762 N N . ILE A 97 ? 0.3664 0.3071 0.5178 0.0409 -0.1180 -0.0168 99 ILE A N 763 C CA . ILE A 97 ? 0.4041 0.3268 0.5445 0.0500 -0.1204 -0.0132 99 ILE A CA 764 C C . ILE A 97 ? 0.4084 0.3449 0.5644 0.0638 -0.1286 -0.0126 99 ILE A C 765 O O . ILE A 97 ? 0.4064 0.3631 0.5753 0.0659 -0.1362 -0.0132 99 ILE A O 766 C CB . ILE A 97 ? 0.4168 0.3117 0.5269 0.0468 -0.1242 -0.0084 99 ILE A CB 767 C CG1 . ILE A 97 ? 0.4658 0.3615 0.5686 0.0512 -0.1377 -0.0049 99 ILE A CG1 768 C CG2 . ILE A 97 ? 0.4275 0.3149 0.5261 0.0325 -0.1149 -0.0102 99 ILE A CG2 769 C CD1 . ILE A 97 ? 0.5372 0.4023 0.6076 0.0511 -0.1436 0.0012 99 ILE A CD1 770 N N . PRO A 98 ? 0.4141 0.3411 0.5701 0.0731 -0.1267 -0.0120 100 PRO A N 771 C CA . PRO A 98 ? 0.4339 0.3719 0.6033 0.0882 -0.1342 -0.0117 100 PRO A CA 772 C C . PRO A 98 ? 0.4702 0.3997 0.6266 0.0947 -0.1483 -0.0066 100 PRO A C 773 O O . PRO A 98 ? 0.4841 0.3913 0.6157 0.0884 -0.1509 -0.0028 100 PRO A O 774 C CB . PRO A 98 ? 0.4371 0.3573 0.6009 0.0953 -0.1285 -0.0120 100 PRO A CB 775 C CG . PRO A 98 ? 0.4264 0.3366 0.5825 0.0813 -0.1161 -0.0140 100 PRO A CG 776 C CD . PRO A 98 ? 0.4218 0.3274 0.5653 0.0699 -0.1176 -0.0121 100 PRO A CD 777 N N . ALA A 99 ? 0.4796 0.4282 0.6528 0.1068 -0.1573 -0.0067 101 ALA A N 778 C CA . ALA A 99 ? 0.5324 0.4737 0.6952 0.1158 -0.1720 -0.0017 101 ALA A CA 779 C C . ALA A 99 ? 0.5515 0.4923 0.7230 0.1344 -0.1758 -0.0015 101 ALA A C 780 O O . ALA A 99 ? 0.5426 0.5073 0.7396 0.1404 -0.1712 -0.0061 101 ALA A O 781 C CB . ALA A 99 ? 0.5170 0.4858 0.6944 0.1135 -0.1811 -0.0024 101 ALA A CB 782 N N . PRO A 100 ? 0.5884 0.5001 0.7374 0.1433 -0.1833 0.0037 102 PRO A N 783 C CA . PRO A 100 ? 0.6093 0.4893 0.7248 0.1353 -0.1873 0.0096 102 PRO A CA 784 C C . PRO A 100 ? 0.5998 0.4598 0.6991 0.1205 -0.1737 0.0087 102 PRO A C 785 O O . PRO A 100 ? 0.5917 0.4521 0.6998 0.1207 -0.1632 0.0048 102 PRO A O 786 C CB . PRO A 100 ? 0.6432 0.4975 0.7420 0.1512 -0.1976 0.0149 102 PRO A CB 787 C CG . PRO A 100 ? 0.6405 0.5075 0.7616 0.1662 -0.1949 0.0108 102 PRO A CG 788 C CD . PRO A 100 ? 0.6082 0.5167 0.7635 0.1631 -0.1888 0.0042 102 PRO A CD 789 N N . LYS A 101 ? 0.6037 0.4486 0.6804 0.1076 -0.1742 0.0118 103 LYS A N 790 C CA . LYS A 101 ? 0.6035 0.4264 0.6599 0.0933 -0.1633 0.0122 103 LYS A CA 791 C C . LYS A 101 ? 0.6046 0.4057 0.6534 0.0968 -0.1561 0.0122 103 LYS A C 792 O O . LYS A 101 ? 0.6215 0.4005 0.6560 0.1067 -0.1627 0.0163 103 LYS A O 793 C CB . LYS A 101 ? 0.6413 0.4401 0.6662 0.0869 -0.1701 0.0183 103 LYS A CB 794 C CG . LYS A 101 ? 0.6650 0.4515 0.6723 0.0691 -0.1595 0.0178 103 LYS A CG 795 C CD . LYS A 101 ? 0.7730 0.5244 0.7433 0.0660 -0.1647 0.0251 103 LYS A CD 796 C CE . LYS A 101 ? 0.8123 0.5522 0.7635 0.0481 -0.1543 0.0248 103 LYS A CE 797 N NZ . LYS A 101 ? 0.8868 0.5907 0.8090 0.0445 -0.1512 0.0300 103 LYS A NZ 798 N N . PRO A 102 ? 0.5735 0.3807 0.6319 0.0886 -0.1431 0.0074 104 PRO A N 799 C CA . PRO A 102 ? 0.5797 0.3681 0.6318 0.0908 -0.1366 0.0067 104 PRO A CA 800 C C . PRO A 102 ? 0.6263 0.3777 0.6442 0.0828 -0.1361 0.0122 104 PRO A C 801 O O . PRO A 102 ? 0.6269 0.3709 0.6280 0.0748 -0.1394 0.0159 104 PRO A O 802 C CB . PRO A 102 ? 0.5394 0.3475 0.6105 0.0817 -0.1238 0.0004 104 PRO A CB 803 C CG . PRO A 102 ? 0.5175 0.3371 0.5887 0.0694 -0.1219 0.0000 104 PRO A CG 804 C CD . PRO A 102 ? 0.5507 0.3788 0.6224 0.0756 -0.1342 0.0029 104 PRO A CD 805 N N . LYS A 103 ? 0.6539 0.3811 0.6599 0.0852 -0.1328 0.0128 105 LYS A N 806 C CA . LYS A 103 ? 0.7025 0.3942 0.6763 0.0762 -0.1314 0.0179 105 LYS A CA 807 C C . LYS A 103 ? 0.7071 0.3989 0.6794 0.0589 -0.1178 0.0148 105 LYS A C 808 O O . LYS A 103 ? 0.7487 0.4293 0.7025 0.0453 -0.1144 0.0176 105 LYS A O 809 C CB . LYS A 103 ? 0.7322 0.3927 0.6892 0.0876 -0.1369 0.0212 105 LYS A CB 810 C CG . LYS A 103 ? 0.7721 0.4228 0.7191 0.1016 -0.1520 0.0269 105 LYS A CG 811 C CD . LYS A 103 ? 0.8878 0.4939 0.7971 0.1004 -0.1572 0.0346 105 LYS A CD 812 C CE . LYS A 103 ? 0.9176 0.5138 0.8131 0.1117 -0.1734 0.0416 105 LYS A CE 813 N NZ . LYS A 103 ? 0.8930 0.5174 0.8180 0.1308 -0.1812 0.0382 105 LYS A NZ 814 N N . ASN A 104 ? 0.6599 0.3648 0.6507 0.0588 -0.1099 0.0090 106 ASN A N 815 C CA . ASN A 104 ? 0.6488 0.3548 0.6384 0.0426 -0.0983 0.0065 106 ASN A CA 816 C C . ASN A 104 ? 0.5731 0.3089 0.5919 0.0427 -0.0912 -0.0005 106 ASN A C 817 O O . ASN A 104 ? 0.5559 0.2881 0.5784 0.0412 -0.0853 -0.0036 106 ASN A O 818 C CB . ASN A 104 ? 0.6923 0.3651 0.6592 0.0383 -0.0957 0.0088 106 ASN A CB 819 C CG . ASN A 104 ? 0.7922 0.4564 0.7456 0.0193 -0.0867 0.0094 106 ASN A CG 820 O OD1 . ASN A 104 ? 0.7852 0.4638 0.7413 0.0096 -0.0828 0.0090 106 ASN A OD1 821 N ND2 . ASN A 104 ? 0.9519 0.5919 0.8904 0.0138 -0.0831 0.0100 106 ASN A ND2 822 N N . ALA A 105 ? 0.5139 0.2775 0.5521 0.0448 -0.0926 -0.0027 107 ALA A N 823 C CA . ALA A 105 ? 0.4768 0.2675 0.5420 0.0478 -0.0882 -0.0084 107 ALA A CA 824 C C . ALA A 105 ? 0.4537 0.2539 0.5253 0.0344 -0.0777 -0.0119 107 ALA A C 825 O O . ALA A 105 ? 0.4370 0.2366 0.5010 0.0233 -0.0745 -0.0109 107 ALA A O 826 C CB . ALA A 105 ? 0.4441 0.2599 0.5266 0.0536 -0.0937 -0.0092 107 ALA A CB 827 N N . THR A 106 ? 0.4309 0.2405 0.5167 0.0360 -0.0726 -0.0161 108 THR A N 828 C CA . THR A 106 ? 0.3866 0.2117 0.4843 0.0260 -0.0642 -0.0198 108 THR A CA 829 C C . THR A 106 ? 0.3835 0.2321 0.4955 0.0236 -0.0644 -0.0211 108 THR A C 830 O O . THR A 106 ? 0.3881 0.2495 0.5101 0.0317 -0.0701 -0.0210 108 THR A O 831 C CB . THR A 106 ? 0.3664 0.1987 0.4768 0.0302 -0.0606 -0.0238 108 THR A CB 832 O OG1 . THR A 106 ? 0.4028 0.2116 0.4974 0.0281 -0.0589 -0.0232 108 THR A OG1 833 C CG2 . THR A 106 ? 0.3236 0.1759 0.4500 0.0228 -0.0537 -0.0276 108 THR A CG2 834 N N . VAL A 107 ? 0.3619 0.2169 0.4759 0.0129 -0.0580 -0.0228 109 VAL A N 835 C CA . VAL A 107 ? 0.3558 0.2280 0.4793 0.0091 -0.0573 -0.0243 109 VAL A CA 836 C C . VAL A 107 ? 0.3317 0.2223 0.4739 0.0062 -0.0512 -0.0285 109 VAL A C 837 O O . VAL A 107 ? 0.3291 0.2168 0.4711 0.0010 -0.0456 -0.0299 109 VAL A O 838 C CB . VAL A 107 ? 0.3779 0.2409 0.4860 -0.0005 -0.0549 -0.0228 109 VAL A CB 839 C CG1 . VAL A 107 ? 0.3262 0.2059 0.4431 -0.0038 -0.0543 -0.0251 109 VAL A CG1 840 C CG2 . VAL A 107 ? 0.3926 0.2351 0.4793 0.0017 -0.0613 -0.0179 109 VAL A CG2 841 N N . LEU A 108 ? 0.3105 0.2193 0.4679 0.0094 -0.0530 -0.0302 110 LEU A N 842 C CA . LEU A 108 ? 0.3035 0.2285 0.4772 0.0069 -0.0483 -0.0335 110 LEU A CA 843 C C . LEU A 108 ? 0.2970 0.2295 0.4727 0.0011 -0.0473 -0.0347 110 LEU A C 844 O O . LEU A 108 ? 0.2893 0.2250 0.4636 0.0025 -0.0523 -0.0339 110 LEU A O 845 C CB . LEU A 108 ? 0.2920 0.2301 0.4800 0.0146 -0.0508 -0.0345 110 LEU A CB 846 C CG . LEU A 108 ? 0.3643 0.2973 0.5529 0.0192 -0.0487 -0.0352 110 LEU A CG 847 C CD1 . LEU A 108 ? 0.4089 0.3547 0.6099 0.0274 -0.0510 -0.0361 110 LEU A CD1 848 C CD2 . LEU A 108 ? 0.4179 0.3558 0.6124 0.0129 -0.0424 -0.0376 110 LEU A CD2 849 N N . ILE A 109 ? 0.2844 0.2194 0.4625 -0.0053 -0.0412 -0.0368 111 ILE A N 850 C CA . ILE A 109 ? 0.2520 0.1919 0.4304 -0.0101 -0.0397 -0.0386 111 ILE A CA 851 C C . ILE A 109 ? 0.2328 0.1857 0.4262 -0.0106 -0.0371 -0.0412 111 ILE A C 852 O O . ILE A 109 ? 0.2245 0.1793 0.4231 -0.0121 -0.0328 -0.0424 111 ILE A O 853 C CB . ILE A 109 ? 0.2801 0.2114 0.4473 -0.0169 -0.0346 -0.0391 111 ILE A CB 854 C CG1 . ILE A 109 ? 0.2820 0.1970 0.4309 -0.0175 -0.0370 -0.0357 111 ILE A CG1 855 C CG2 . ILE A 109 ? 0.2247 0.1618 0.3933 -0.0207 -0.0321 -0.0421 111 ILE A CG2 856 C CD1 . ILE A 109 ? 0.3108 0.2174 0.4467 -0.0256 -0.0313 -0.0359 111 ILE A CD1 857 N N . TRP A 110 ? 0.2049 0.1660 0.4046 -0.0098 -0.0402 -0.0420 112 TRP A N 858 C CA . TRP A 110 ? 0.2016 0.1733 0.4144 -0.0102 -0.0386 -0.0439 112 TRP A CA 859 C C . TRP A 110 ? 0.2162 0.1874 0.4283 -0.0148 -0.0349 -0.0466 112 TRP A C 860 O O . TRP A 110 ? 0.2418 0.2088 0.4457 -0.0172 -0.0359 -0.0476 112 TRP A O 861 C CB . TRP A 110 ? 0.2012 0.1818 0.4208 -0.0083 -0.0436 -0.0435 112 TRP A CB 862 C CG . TRP A 110 ? 0.1863 0.1760 0.4173 -0.0103 -0.0420 -0.0450 112 TRP A CG 863 C CD1 . TRP A 110 ? 0.1894 0.1811 0.4216 -0.0142 -0.0430 -0.0466 112 TRP A CD1 864 C CD2 . TRP A 110 ? 0.1623 0.1575 0.4023 -0.0091 -0.0391 -0.0449 112 TRP A CD2 865 N NE1 . TRP A 110 ? 0.2087 0.2063 0.4501 -0.0154 -0.0412 -0.0471 112 TRP A NE1 866 C CE2 . TRP A 110 ? 0.2088 0.2090 0.4549 -0.0124 -0.0388 -0.0458 112 TRP A CE2 867 C CE3 . TRP A 110 ? 0.1734 0.1685 0.4151 -0.0058 -0.0371 -0.0440 112 TRP A CE3 868 C CZ2 . TRP A 110 ? 0.1581 0.1634 0.4117 -0.0126 -0.0365 -0.0454 112 TRP A CZ2 869 C CZ3 . TRP A 110 ? 0.1587 0.1595 0.4078 -0.0059 -0.0348 -0.0441 112 TRP A CZ3 870 C CH2 . TRP A 110 ? 0.1889 0.1948 0.4438 -0.0093 -0.0345 -0.0445 112 TRP A CH2 871 N N . ILE A 111 ? 0.2052 0.1802 0.4251 -0.0155 -0.0311 -0.0480 113 ILE A N 872 C CA . ILE A 111 ? 0.2018 0.1768 0.4229 -0.0179 -0.0279 -0.0509 113 ILE A CA 873 C C . ILE A 111 ? 0.2069 0.1877 0.4378 -0.0173 -0.0291 -0.0513 113 ILE A C 874 O O . ILE A 111 ? 0.1954 0.1800 0.4333 -0.0158 -0.0281 -0.0503 113 ILE A O 875 C CB . ILE A 111 ? 0.1923 0.1666 0.4138 -0.0191 -0.0225 -0.0523 113 ILE A CB 876 C CG1 . ILE A 111 ? 0.2217 0.1893 0.4321 -0.0214 -0.0208 -0.0515 113 ILE A CG1 877 C CG2 . ILE A 111 ? 0.1729 0.1479 0.3964 -0.0200 -0.0193 -0.0559 113 ILE A CG2 878 C CD1 . ILE A 111 ? 0.1993 0.1684 0.4115 -0.0238 -0.0156 -0.0526 113 ILE A CD1 879 N N . TYR A 112 ? 0.2177 0.1979 0.4476 -0.0191 -0.0313 -0.0525 114 TYR A N 880 C CA . TYR A 112 ? 0.1984 0.1821 0.4357 -0.0199 -0.0326 -0.0525 114 TYR A CA 881 C C . TYR A 112 ? 0.2074 0.1887 0.4484 -0.0192 -0.0292 -0.0539 114 TYR A C 882 O O . TYR A 112 ? 0.1908 0.1686 0.4291 -0.0184 -0.0259 -0.0563 114 TYR A O 883 C CB . TYR A 112 ? 0.1941 0.1765 0.4283 -0.0233 -0.0361 -0.0537 114 TYR A CB 884 C CG . TYR A 112 ? 0.1988 0.1724 0.4237 -0.0251 -0.0348 -0.0573 114 TYR A CG 885 C CD1 . TYR A 112 ? 0.1702 0.1379 0.3951 -0.0250 -0.0315 -0.0602 114 TYR A CD1 886 C CD2 . TYR A 112 ? 0.1923 0.1628 0.4075 -0.0265 -0.0369 -0.0579 114 TYR A CD2 887 C CE1 . TYR A 112 ? 0.2222 0.1819 0.4382 -0.0260 -0.0294 -0.0643 114 TYR A CE1 888 C CE2 . TYR A 112 ? 0.2343 0.1963 0.4390 -0.0285 -0.0351 -0.0616 114 TYR A CE2 889 C CZ . TYR A 112 ? 0.2455 0.2025 0.4508 -0.0283 -0.0311 -0.0651 114 TYR A CZ 890 O OH . TYR A 112 ? 0.2985 0.2472 0.4926 -0.0297 -0.0286 -0.0693 114 TYR A OH 891 N N . GLY A 113 ? 0.2139 0.1973 0.4608 -0.0194 -0.0301 -0.0525 115 GLY A N 892 C CA . GLY A 113 ? 0.2272 0.2064 0.4764 -0.0184 -0.0285 -0.0534 115 GLY A CA 893 C C . GLY A 113 ? 0.2480 0.2197 0.4939 -0.0211 -0.0300 -0.0552 115 GLY A C 894 O O . GLY A 113 ? 0.2700 0.2401 0.5112 -0.0242 -0.0318 -0.0565 115 GLY A O 895 N N . GLY A 114 ? 0.2497 0.2158 0.4970 -0.0200 -0.0297 -0.0552 116 GLY A N 896 C CA . GLY A 114 ? 0.2567 0.2120 0.4991 -0.0221 -0.0309 -0.0572 116 GLY A CA 897 C C . GLY A 114 ? 0.2763 0.2247 0.5193 -0.0166 -0.0288 -0.0594 116 GLY A C 898 O O . GLY A 114 ? 0.2806 0.2186 0.5184 -0.0157 -0.0283 -0.0630 116 GLY A O 899 N N . GLY A 115 ? 0.2631 0.2177 0.5125 -0.0123 -0.0278 -0.0577 117 GLY A N 900 C CA . GLY A 115 ? 0.2390 0.1893 0.4912 -0.0063 -0.0269 -0.0595 117 GLY A CA 901 C C . GLY A 115 ? 0.2307 0.1819 0.4828 -0.0029 -0.0229 -0.0647 117 GLY A C 902 O O . GLY A 115 ? 0.2352 0.1827 0.4897 0.0028 -0.0217 -0.0674 117 GLY A O 903 N N . PHE A 116 ? 0.2126 0.1684 0.4613 -0.0060 -0.0206 -0.0663 118 PHE A N 904 C CA . PHE A 116 ? 0.2311 0.1863 0.4766 -0.0043 -0.0160 -0.0716 118 PHE A CA 905 C C . PHE A 116 ? 0.2510 0.1924 0.4883 -0.0039 -0.0160 -0.0757 118 PHE A C 906 O O . PHE A 116 ? 0.2598 0.1991 0.4939 -0.0015 -0.0116 -0.0809 118 PHE A O 907 C CB . PHE A 116 ? 0.2135 0.1771 0.4682 0.0015 -0.0123 -0.0736 118 PHE A CB 908 C CG . PHE A 116 ? 0.2204 0.1964 0.4818 0.0002 -0.0120 -0.0705 118 PHE A CG 909 C CD1 . PHE A 116 ? 0.1882 0.1687 0.4453 -0.0042 -0.0095 -0.0704 118 PHE A CD1 910 C CD2 . PHE A 116 ? 0.2064 0.1879 0.4767 0.0031 -0.0147 -0.0676 118 PHE A CD2 911 C CE1 . PHE A 116 ? 0.2066 0.1963 0.4684 -0.0060 -0.0093 -0.0677 118 PHE A CE1 912 C CE2 . PHE A 116 ? 0.2292 0.2212 0.5045 0.0013 -0.0146 -0.0653 118 PHE A CE2 913 C CZ . PHE A 116 ? 0.1982 0.1936 0.4691 -0.0035 -0.0117 -0.0655 118 PHE A CZ 914 N N . GLN A 117 ? 0.2328 0.1647 0.4662 -0.0069 -0.0204 -0.0738 119 GLN A N 915 C CA . GLN A 117 ? 0.2721 0.1884 0.4961 -0.0075 -0.0208 -0.0778 119 GLN A CA 916 C C . GLN A 117 ? 0.2798 0.1930 0.4953 -0.0158 -0.0239 -0.0774 119 GLN A C 917 O O . GLN A 117 ? 0.3085 0.2101 0.5137 -0.0181 -0.0240 -0.0817 119 GLN A O 918 C CB . GLN A 117 ? 0.2662 0.1703 0.4904 -0.0048 -0.0237 -0.0766 119 GLN A CB 919 C CG . GLN A 117 ? 0.3316 0.2398 0.5658 0.0036 -0.0232 -0.0751 119 GLN A CG 920 C CD . GLN A 117 ? 0.3613 0.2759 0.6006 0.0110 -0.0179 -0.0805 119 GLN A CD 921 O OE1 . GLN A 117 ? 0.4094 0.3140 0.6430 0.0144 -0.0153 -0.0862 119 GLN A OE1 922 N NE2 . GLN A 117 ? 0.3849 0.3164 0.6340 0.0126 -0.0158 -0.0791 119 GLN A NE2 923 N N . THR A 118 ? 0.2621 0.1859 0.4818 -0.0200 -0.0266 -0.0725 120 THR A N 924 C CA . THR A 118 ? 0.2650 0.1892 0.4803 -0.0274 -0.0307 -0.0712 120 THR A CA 925 C C . THR A 118 ? 0.2655 0.2041 0.4851 -0.0285 -0.0315 -0.0679 120 THR A C 926 O O . THR A 118 ? 0.2509 0.1975 0.4764 -0.0243 -0.0289 -0.0663 120 THR A O 927 C CB . THR A 118 ? 0.2942 0.2140 0.5111 -0.0321 -0.0345 -0.0678 120 THR A CB 928 O OG1 . THR A 118 ? 0.2879 0.2178 0.5143 -0.0305 -0.0345 -0.0627 120 THR A OG1 929 C CG2 . THR A 118 ? 0.2638 0.1652 0.4742 -0.0314 -0.0346 -0.0704 120 THR A CG2 930 N N . GLY A 119 ? 0.2382 0.1800 0.4551 -0.0341 -0.0357 -0.0669 121 GLY A N 931 C CA . GLY A 119 ? 0.2419 0.1961 0.4632 -0.0344 -0.0376 -0.0636 121 GLY A CA 932 C C . GLY A 119 ? 0.2512 0.2051 0.4638 -0.0366 -0.0400 -0.0654 121 GLY A C 933 O O . GLY A 119 ? 0.2518 0.1960 0.4539 -0.0374 -0.0386 -0.0695 121 GLY A O 934 N N . THR A 120 ? 0.2228 0.1866 0.4387 -0.0374 -0.0437 -0.0623 122 THR A N 935 C CA . THR A 120 ? 0.2624 0.2259 0.4696 -0.0386 -0.0470 -0.0630 122 THR A CA 936 C C . THR A 120 ? 0.2579 0.2328 0.4714 -0.0357 -0.0499 -0.0588 122 THR A C 937 O O . THR A 120 ? 0.2461 0.2304 0.4711 -0.0346 -0.0502 -0.0561 122 THR A O 938 C CB . THR A 120 ? 0.2756 0.2356 0.4765 -0.0451 -0.0524 -0.0653 122 THR A CB 939 O OG1 . THR A 120 ? 0.2973 0.2565 0.4880 -0.0461 -0.0565 -0.0657 122 THR A OG1 940 C CG2 . THR A 120 ? 0.2237 0.1944 0.4359 -0.0491 -0.0568 -0.0629 122 THR A CG2 941 N N . SER A 121 ? 0.2674 0.2402 0.4723 -0.0341 -0.0514 -0.0582 123 SER A N 942 C CA . SER A 121 ? 0.2636 0.2444 0.4729 -0.0302 -0.0544 -0.0543 123 SER A CA 943 C C . SER A 121 ? 0.2724 0.2639 0.4875 -0.0312 -0.0621 -0.0527 123 SER A C 944 O O . SER A 121 ? 0.2685 0.2680 0.4896 -0.0266 -0.0646 -0.0498 123 SER A O 945 C CB . SER A 121 ? 0.2776 0.2506 0.4747 -0.0280 -0.0536 -0.0534 123 SER A CB 946 O OG . SER A 121 ? 0.3024 0.2692 0.4865 -0.0313 -0.0575 -0.0549 123 SER A OG 947 N N . SER A 122 ? 0.2832 0.2751 0.4966 -0.0370 -0.0659 -0.0549 124 SER A N 948 C CA . SER A 122 ? 0.2750 0.2792 0.4947 -0.0390 -0.0738 -0.0538 124 SER A CA 949 C C . SER A 122 ? 0.2600 0.2785 0.4964 -0.0413 -0.0738 -0.0529 124 SER A C 950 O O . SER A 122 ? 0.2670 0.2982 0.5107 -0.0439 -0.0798 -0.0524 124 SER A O 951 C CB . SER A 122 ? 0.3042 0.3021 0.5124 -0.0458 -0.0791 -0.0567 124 SER A CB 952 O OG . SER A 122 ? 0.2994 0.2861 0.5023 -0.0509 -0.0746 -0.0604 124 SER A OG 953 N N . LEU A 123 ? 0.2379 0.2553 0.4802 -0.0408 -0.0673 -0.0527 125 LEU A N 954 C CA . LEU A 123 ? 0.2355 0.2661 0.4918 -0.0435 -0.0668 -0.0515 125 LEU A CA 955 C C . LEU A 123 ? 0.2492 0.2968 0.5169 -0.0379 -0.0694 -0.0490 125 LEU A C 956 O O . LEU A 123 ? 0.2416 0.2875 0.5069 -0.0303 -0.0692 -0.0476 125 LEU A O 957 C CB . LEU A 123 ? 0.2350 0.2603 0.4940 -0.0431 -0.0596 -0.0509 125 LEU A CB 958 C CG . LEU A 123 ? 0.2373 0.2453 0.4864 -0.0460 -0.0563 -0.0533 125 LEU A CG 959 C CD1 . LEU A 123 ? 0.1902 0.1956 0.4433 -0.0440 -0.0507 -0.0518 125 LEU A CD1 960 C CD2 . LEU A 123 ? 0.1987 0.2033 0.4445 -0.0553 -0.0602 -0.0555 125 LEU A CD2 961 N N . HIS A 124 ? 0.2428 0.3064 0.5227 -0.0421 -0.0718 -0.0487 126 HIS A N 962 C CA . HIS A 124 ? 0.2522 0.3355 0.5463 -0.0373 -0.0734 -0.0472 126 HIS A CA 963 C C . HIS A 124 ? 0.2360 0.3191 0.5333 -0.0287 -0.0672 -0.0457 126 HIS A C 964 O O . HIS A 124 ? 0.2357 0.3273 0.5383 -0.0206 -0.0691 -0.0447 126 HIS A O 965 C CB . HIS A 124 ? 0.2372 0.3375 0.5445 -0.0462 -0.0741 -0.0476 126 HIS A CB 966 C CG . HIS A 124 ? 0.3366 0.4610 0.6614 -0.0419 -0.0745 -0.0467 126 HIS A CG 967 N ND1 . HIS A 124 ? 0.4511 0.5878 0.7819 -0.0348 -0.0813 -0.0463 126 HIS A ND1 968 C CD2 . HIS A 124 ? 0.3845 0.5232 0.7219 -0.0432 -0.0689 -0.0462 126 HIS A CD2 969 C CE1 . HIS A 124 ? 0.4577 0.6161 0.8055 -0.0309 -0.0795 -0.0461 126 HIS A CE1 970 N NE2 . HIS A 124 ? 0.4678 0.6284 0.8198 -0.0366 -0.0716 -0.0461 126 HIS A NE2 971 N N . VAL A 125 ? 0.2195 0.2933 0.5137 -0.0305 -0.0605 -0.0456 127 VAL A N 972 C CA . VAL A 125 ? 0.2074 0.2813 0.5041 -0.0242 -0.0549 -0.0445 127 VAL A CA 973 C C . VAL A 125 ? 0.2247 0.2854 0.5112 -0.0173 -0.0548 -0.0442 127 VAL A C 974 O O . VAL A 125 ? 0.2410 0.3006 0.5281 -0.0115 -0.0513 -0.0436 127 VAL A O 975 C CB . VAL A 125 ? 0.2109 0.2808 0.5080 -0.0287 -0.0484 -0.0441 127 VAL A CB 976 C CG1 . VAL A 125 ? 0.1929 0.2785 0.5010 -0.0357 -0.0478 -0.0438 127 VAL A CG1 977 C CG2 . VAL A 125 ? 0.1533 0.2045 0.4389 -0.0329 -0.0472 -0.0448 127 VAL A CG2 978 N N . TYR A 126 ? 0.2248 0.2752 0.5009 -0.0184 -0.0585 -0.0448 128 TYR A N 979 C CA . TYR A 126 ? 0.2148 0.2520 0.4797 -0.0133 -0.0582 -0.0443 128 TYR A CA 980 C C . TYR A 126 ? 0.2231 0.2618 0.4844 -0.0087 -0.0650 -0.0432 128 TYR A C 981 O O . TYR A 126 ? 0.2142 0.2399 0.4629 -0.0064 -0.0659 -0.0425 128 TYR A O 982 C CB . TYR A 126 ? 0.2026 0.2247 0.4556 -0.0175 -0.0560 -0.0458 128 TYR A CB 983 C CG . TYR A 126 ? 0.1819 0.1999 0.4366 -0.0214 -0.0506 -0.0470 128 TYR A CG 984 C CD1 . TYR A 126 ? 0.1760 0.1987 0.4382 -0.0200 -0.0466 -0.0459 128 TYR A CD1 985 C CD2 . TYR A 126 ? 0.1349 0.1428 0.3820 -0.0257 -0.0497 -0.0491 128 TYR A CD2 986 C CE1 . TYR A 126 ? 0.1640 0.1813 0.4261 -0.0231 -0.0428 -0.0464 128 TYR A CE1 987 C CE2 . TYR A 126 ? 0.1404 0.1429 0.3884 -0.0277 -0.0456 -0.0501 128 TYR A CE2 988 C CZ . TYR A 126 ? 0.1767 0.1838 0.4321 -0.0265 -0.0427 -0.0484 128 TYR A CZ 989 O OH . TYR A 126 ? 0.1874 0.1879 0.4423 -0.0281 -0.0397 -0.0489 128 TYR A OH 990 N N . ASP A 127 ? 0.2112 0.2656 0.4830 -0.0079 -0.0700 -0.0429 129 ASP A N 991 C CA . ASP A 127 ? 0.2326 0.2895 0.5017 -0.0032 -0.0781 -0.0417 129 ASP A CA 992 C C . ASP A 127 ? 0.2315 0.2835 0.4983 0.0069 -0.0775 -0.0398 129 ASP A C 993 O O . ASP A 127 ? 0.2058 0.2684 0.4842 0.0123 -0.0751 -0.0399 129 ASP A O 994 C CB . ASP A 127 ? 0.2246 0.3033 0.5093 -0.0042 -0.0833 -0.0420 129 ASP A CB 995 C CG . ASP A 127 ? 0.2944 0.3773 0.5767 -0.0009 -0.0937 -0.0409 129 ASP A CG 996 O OD1 . ASP A 127 ? 0.2979 0.3687 0.5687 0.0059 -0.0967 -0.0389 129 ASP A OD1 997 O OD2 . ASP A 127 ? 0.3058 0.4048 0.5978 -0.0054 -0.0992 -0.0417 129 ASP A OD2 998 N N . GLY A 128 ? 0.2356 0.2704 0.4864 0.0091 -0.0793 -0.0384 130 GLY A N 999 C CA . GLY A 128 ? 0.2360 0.2624 0.4821 0.0175 -0.0787 -0.0366 130 GLY A CA 1000 C C . GLY A 128 ? 0.2786 0.3112 0.5285 0.0272 -0.0863 -0.0348 130 GLY A C 1001 O O . GLY A 128 ? 0.2882 0.3098 0.5315 0.0350 -0.0864 -0.0333 130 GLY A O 1002 N N . LYS A 129 ? 0.2621 0.3121 0.5229 0.0273 -0.0930 -0.0351 131 LYS A N 1003 C CA . LYS A 129 ? 0.2885 0.3457 0.5538 0.0376 -0.1013 -0.0333 131 LYS A CA 1004 C C . LYS A 129 ? 0.2797 0.3464 0.5584 0.0481 -0.0980 -0.0341 131 LYS A C 1005 O O . LYS A 129 ? 0.2911 0.3559 0.5690 0.0591 -0.1035 -0.0326 131 LYS A O 1006 C CB . LYS A 129 ? 0.2781 0.3546 0.5538 0.0349 -0.1100 -0.0336 131 LYS A CB 1007 C CG . LYS A 129 ? 0.2777 0.3800 0.5759 0.0311 -0.1069 -0.0364 131 LYS A CG 1008 C CD . LYS A 129 ? 0.2973 0.4170 0.6036 0.0257 -0.1161 -0.0368 131 LYS A CD 1009 C CE . LYS A 129 ? 0.3027 0.4477 0.6305 0.0195 -0.1124 -0.0394 131 LYS A CE 1010 N NZ . LYS A 129 ? 0.3501 0.5134 0.6867 0.0139 -0.1223 -0.0399 131 LYS A NZ 1011 N N . PHE A 130 ? 0.2813 0.3577 0.5712 0.0451 -0.0894 -0.0366 132 PHE A N 1012 C CA . PHE A 130 ? 0.2877 0.3749 0.5902 0.0544 -0.0856 -0.0382 132 PHE A CA 1013 C C . PHE A 130 ? 0.2932 0.3570 0.5808 0.0605 -0.0820 -0.0375 132 PHE A C 1014 O O . PHE A 130 ? 0.3139 0.3758 0.6025 0.0723 -0.0841 -0.0375 132 PHE A O 1015 C CB . PHE A 130 ? 0.2767 0.3803 0.5933 0.0479 -0.0772 -0.0409 132 PHE A CB 1016 C CG . PHE A 130 ? 0.2919 0.4173 0.6224 0.0404 -0.0803 -0.0416 132 PHE A CG 1017 C CD1 . PHE A 130 ? 0.3137 0.4624 0.6609 0.0462 -0.0863 -0.0421 132 PHE A CD1 1018 C CD2 . PHE A 130 ? 0.2730 0.3952 0.5998 0.0276 -0.0778 -0.0418 132 PHE A CD2 1019 C CE1 . PHE A 130 ? 0.2998 0.4698 0.6602 0.0378 -0.0898 -0.0428 132 PHE A CE1 1020 C CE2 . PHE A 130 ? 0.2939 0.4336 0.6316 0.0194 -0.0809 -0.0425 132 PHE A CE2 1021 C CZ . PHE A 130 ? 0.2992 0.4640 0.6543 0.0238 -0.0871 -0.0430 132 PHE A CZ 1022 N N . LEU A 131 ? 0.2805 0.3265 0.5544 0.0526 -0.0770 -0.0372 133 LEU A N 1023 C CA . LEU A 131 ? 0.2969 0.3194 0.5549 0.0558 -0.0741 -0.0364 133 LEU A CA 1024 C C . LEU A 131 ? 0.3118 0.3180 0.5557 0.0627 -0.0819 -0.0332 133 LEU A C 1025 O O . LEU A 131 ? 0.3354 0.3277 0.5717 0.0704 -0.0816 -0.0328 133 LEU A O 1026 C CB . LEU A 131 ? 0.2829 0.2922 0.5302 0.0452 -0.0683 -0.0364 133 LEU A CB 1027 C CG . LEU A 131 ? 0.2946 0.3138 0.5516 0.0396 -0.0604 -0.0390 133 LEU A CG 1028 C CD1 . LEU A 131 ? 0.2526 0.2651 0.5033 0.0291 -0.0572 -0.0390 133 LEU A CD1 1029 C CD2 . LEU A 131 ? 0.3272 0.3382 0.5811 0.0446 -0.0556 -0.0402 133 LEU A CD2 1030 N N . ALA A 132 ? 0.3036 0.3099 0.5426 0.0599 -0.0892 -0.0310 134 ALA A N 1031 C CA . ALA A 132 ? 0.3307 0.3194 0.5536 0.0660 -0.0971 -0.0273 134 ALA A CA 1032 C C . ALA A 132 ? 0.3373 0.3359 0.5709 0.0805 -0.1035 -0.0271 134 ALA A C 1033 O O . ALA A 132 ? 0.3920 0.3736 0.6155 0.0898 -0.1053 -0.0257 134 ALA A O 1034 C CB . ALA A 132 ? 0.3127 0.2976 0.5248 0.0583 -0.1032 -0.0251 134 ALA A CB 1035 N N . ARG A 133 ? 0.3175 0.3440 0.5726 0.0826 -0.1057 -0.0291 135 ARG A N 1036 C CA . ARG A 133 ? 0.3318 0.3731 0.6016 0.0969 -0.1105 -0.0299 135 ARG A CA 1037 C C . ARG A 133 ? 0.3358 0.3706 0.6073 0.1065 -0.1037 -0.0323 135 ARG A C 1038 O O . ARG A 133 ? 0.3393 0.3639 0.6060 0.1199 -0.1085 -0.0313 135 ARG A O 1039 C CB . ARG A 133 ? 0.3144 0.3905 0.6095 0.0945 -0.1118 -0.0324 135 ARG A CB 1040 C CG . ARG A 133 ? 0.3524 0.4509 0.6680 0.1085 -0.1148 -0.0342 135 ARG A CG 1041 C CD . ARG A 133 ? 0.4288 0.5222 0.7392 0.1203 -0.1281 -0.0308 135 ARG A CD 1042 N NE . ARG A 133 ? 0.4787 0.5970 0.8115 0.1347 -0.1320 -0.0329 135 ARG A NE 1043 C CZ . ARG A 133 ? 0.5422 0.6552 0.8770 0.1496 -0.1295 -0.0345 135 ARG A CZ 1044 N NH1 . ARG A 133 ? 0.5807 0.6630 0.8955 0.1505 -0.1232 -0.0343 135 ARG A NH1 1045 N NH2 . ARG A 133 ? 0.5118 0.6505 0.8690 0.1635 -0.1330 -0.0369 135 ARG A NH2 1046 N N . VAL A 134 ? 0.3139 0.3533 0.5908 0.0999 -0.0930 -0.0355 136 VAL A N 1047 C CA . VAL A 134 ? 0.3008 0.3419 0.5839 0.1080 -0.0859 -0.0391 136 VAL A CA 1048 C C . VAL A 134 ? 0.3172 0.3257 0.5780 0.1093 -0.0830 -0.0383 136 VAL A C 1049 O O . VAL A 134 ? 0.3245 0.3236 0.5822 0.1208 -0.0827 -0.0397 136 VAL A O 1050 C CB . VAL A 134 ? 0.2885 0.3491 0.5859 0.0993 -0.0759 -0.0427 136 VAL A CB 1051 C CG1 . VAL A 134 ? 0.2615 0.3213 0.5619 0.1070 -0.0675 -0.0467 136 VAL A CG1 1052 C CG2 . VAL A 134 ? 0.2444 0.3373 0.5640 0.0975 -0.0785 -0.0436 136 VAL A CG2 1053 N N . GLU A 135 ? 0.3098 0.3011 0.5550 0.0973 -0.0809 -0.0363 137 GLU A N 1054 C CA . GLU A 135 ? 0.3252 0.2879 0.5507 0.0958 -0.0772 -0.0358 137 GLU A CA 1055 C C . GLU A 135 ? 0.3422 0.2792 0.5461 0.0959 -0.0842 -0.0312 137 GLU A C 1056 O O . GLU A 135 ? 0.3488 0.2593 0.5340 0.0946 -0.0822 -0.0302 137 GLU A O 1057 C CB . GLU A 135 ? 0.3002 0.2628 0.5245 0.0826 -0.0685 -0.0375 137 GLU A CB 1058 C CG . GLU A 135 ? 0.2869 0.2662 0.5257 0.0838 -0.0611 -0.0419 137 GLU A CG 1059 C CD . GLU A 135 ? 0.3512 0.3210 0.5867 0.0948 -0.0584 -0.0448 137 GLU A CD 1060 O OE1 . GLU A 135 ? 0.3775 0.3208 0.5949 0.0975 -0.0599 -0.0437 137 GLU A OE1 1061 O OE2 . GLU A 135 ? 0.3073 0.2957 0.5577 0.1006 -0.0543 -0.0484 137 GLU A OE2 1062 N N . ARG A 136 ? 0.3443 0.2883 0.5496 0.0968 -0.0924 -0.0282 138 ARG A N 1063 C CA . ARG A 136 ? 0.3835 0.3031 0.5665 0.0960 -0.0994 -0.0232 138 ARG A CA 1064 C C . ARG A 136 ? 0.3811 0.2821 0.5466 0.0819 -0.0937 -0.0220 138 ARG A C 1065 O O . ARG A 136 ? 0.4279 0.3030 0.5719 0.0805 -0.0957 -0.0186 138 ARG A O 1066 C CB . ARG A 136 ? 0.3968 0.2962 0.5683 0.1105 -0.1058 -0.0210 138 ARG A CB 1067 C CG . ARG A 136 ? 0.4378 0.3558 0.6246 0.1250 -0.1154 -0.0207 138 ARG A CG 1068 C CD . ARG A 136 ? 0.5686 0.4616 0.7394 0.1394 -0.1240 -0.0172 138 ARG A CD 1069 N NE . ARG A 136 ? 0.5252 0.4016 0.6768 0.1377 -0.1343 -0.0109 138 ARG A NE 1070 C CZ . ARG A 136 ? 0.5046 0.3988 0.6640 0.1382 -0.1432 -0.0088 138 ARG A CZ 1071 N NH1 . ARG A 136 ? 0.4025 0.3330 0.5899 0.1396 -0.1433 -0.0124 138 ARG A NH1 1072 N NH2 . ARG A 136 ? 0.4846 0.3595 0.6224 0.1361 -0.1520 -0.0030 138 ARG A NH2 1073 N N . VAL A 137 ? 0.3554 0.2702 0.5302 0.0713 -0.0866 -0.0246 139 VAL A N 1074 C CA . VAL A 137 ? 0.3269 0.2304 0.4892 0.0582 -0.0818 -0.0238 139 VAL A CA 1075 C C . VAL A 137 ? 0.3425 0.2526 0.5028 0.0517 -0.0857 -0.0222 139 VAL A C 1076 O O . VAL A 137 ? 0.3359 0.2638 0.5085 0.0557 -0.0913 -0.0224 139 VAL A O 1077 C CB . VAL A 137 ? 0.3213 0.2353 0.4946 0.0513 -0.0724 -0.0278 139 VAL A CB 1078 C CG1 . VAL A 137 ? 0.2540 0.1553 0.4228 0.0551 -0.0683 -0.0293 139 VAL A CG1 1079 C CG2 . VAL A 137 ? 0.2523 0.1944 0.4482 0.0525 -0.0717 -0.0305 139 VAL A CG2 1080 N N . ILE A 138 ? 0.3375 0.2343 0.4824 0.0415 -0.0828 -0.0208 140 ILE A N 1081 C CA . ILE A 138 ? 0.3205 0.2241 0.4634 0.0341 -0.0845 -0.0206 140 ILE A CA 1082 C C . ILE A 138 ? 0.3245 0.2423 0.4801 0.0257 -0.0762 -0.0247 140 ILE A C 1083 O O . ILE A 138 ? 0.3408 0.2536 0.4959 0.0214 -0.0686 -0.0262 140 ILE A O 1084 C CB . ILE A 138 ? 0.3456 0.2260 0.4634 0.0282 -0.0852 -0.0171 140 ILE A CB 1085 C CG1 . ILE A 138 ? 0.3713 0.2384 0.4759 0.0368 -0.0956 -0.0124 140 ILE A CG1 1086 C CG2 . ILE A 138 ? 0.3088 0.1924 0.4213 0.0176 -0.0823 -0.0182 140 ILE A CG2 1087 C CD1 . ILE A 138 ? 0.4265 0.2694 0.5037 0.0304 -0.0968 -0.0082 140 ILE A CD1 1088 N N . VAL A 139 ? 0.3040 0.2384 0.4704 0.0232 -0.0779 -0.0264 141 VAL A N 1089 C CA . VAL A 139 ? 0.2775 0.2231 0.4547 0.0163 -0.0710 -0.0299 141 VAL A CA 1090 C C . VAL A 139 ? 0.2855 0.2278 0.4533 0.0080 -0.0705 -0.0306 141 VAL A C 1091 O O . VAL A 139 ? 0.3167 0.2599 0.4793 0.0081 -0.0772 -0.0295 141 VAL A O 1092 C CB . VAL A 139 ? 0.2760 0.2435 0.4741 0.0192 -0.0722 -0.0320 141 VAL A CB 1093 C CG1 . VAL A 139 ? 0.1855 0.1623 0.3928 0.0115 -0.0659 -0.0352 141 VAL A CG1 1094 C CG2 . VAL A 139 ? 0.2477 0.2198 0.4553 0.0283 -0.0720 -0.0321 141 VAL A CG2 1095 N N . VAL A 140 ? 0.2736 0.2125 0.4391 0.0012 -0.0628 -0.0327 142 VAL A N 1096 C CA . VAL A 140 ? 0.2766 0.2124 0.4334 -0.0060 -0.0608 -0.0343 142 VAL A CA 1097 C C . VAL A 140 ? 0.2926 0.2401 0.4635 -0.0096 -0.0551 -0.0383 142 VAL A C 1098 O O . VAL A 140 ? 0.2933 0.2447 0.4739 -0.0087 -0.0503 -0.0391 142 VAL A O 1099 C CB . VAL A 140 ? 0.2924 0.2120 0.4317 -0.0111 -0.0558 -0.0333 142 VAL A CB 1100 C CG1 . VAL A 140 ? 0.2214 0.1399 0.3534 -0.0185 -0.0514 -0.0362 142 VAL A CG1 1101 C CG2 . VAL A 140 ? 0.2941 0.1976 0.4152 -0.0082 -0.0619 -0.0285 142 VAL A CG2 1102 N N . SER A 141 ? 0.2786 0.2295 0.4487 -0.0137 -0.0560 -0.0406 143 SER A N 1103 C CA . SER A 141 ? 0.2642 0.2213 0.4430 -0.0173 -0.0508 -0.0443 143 SER A CA 1104 C C . SER A 141 ? 0.2828 0.2336 0.4504 -0.0226 -0.0491 -0.0472 143 SER A C 1105 O O . SER A 141 ? 0.2945 0.2408 0.4511 -0.0239 -0.0542 -0.0465 143 SER A O 1106 C CB . SER A 141 ? 0.2452 0.2153 0.4392 -0.0159 -0.0540 -0.0449 143 SER A CB 1107 O OG . SER A 141 ? 0.2504 0.2238 0.4422 -0.0168 -0.0610 -0.0448 143 SER A OG 1108 N N . MET A 142 ? 0.2746 0.2248 0.4443 -0.0253 -0.0419 -0.0506 144 MET A N 1109 C CA . MET A 142 ? 0.2919 0.2360 0.4512 -0.0295 -0.0388 -0.0543 144 MET A CA 1110 C C . MET A 142 ? 0.2977 0.2460 0.4662 -0.0304 -0.0366 -0.0583 144 MET A C 1111 O O . MET A 142 ? 0.3036 0.2587 0.4863 -0.0281 -0.0347 -0.0581 144 MET A O 1112 C CB . MET A 142 ? 0.2839 0.2217 0.4345 -0.0317 -0.0311 -0.0552 144 MET A CB 1113 C CG . MET A 142 ? 0.2606 0.2044 0.4236 -0.0311 -0.0235 -0.0579 144 MET A CG 1114 S SD . MET A 142 ? 0.2676 0.2203 0.4481 -0.0269 -0.0249 -0.0549 144 MET A SD 1115 C CE . MET A 142 ? 0.2187 0.1657 0.3914 -0.0281 -0.0225 -0.0517 144 MET A CE 1116 N N . ASN A 143 ? 0.3002 0.2430 0.4593 -0.0337 -0.0372 -0.0618 145 ASN A N 1117 C CA . ASN A 143 ? 0.3063 0.2482 0.4698 -0.0344 -0.0335 -0.0664 145 ASN A CA 1118 C C . ASN A 143 ? 0.3145 0.2531 0.4750 -0.0338 -0.0244 -0.0697 145 ASN A C 1119 O O . ASN A 143 ? 0.3218 0.2555 0.4696 -0.0358 -0.0212 -0.0701 145 ASN A O 1120 C CB . ASN A 143 ? 0.3182 0.2542 0.4727 -0.0383 -0.0379 -0.0697 145 ASN A CB 1121 C CG . ASN A 143 ? 0.3103 0.2530 0.4717 -0.0396 -0.0465 -0.0669 145 ASN A CG 1122 O OD1 . ASN A 143 ? 0.3052 0.2572 0.4795 -0.0368 -0.0479 -0.0633 145 ASN A OD1 1123 N ND2 . ASN A 143 ? 0.3203 0.2593 0.4729 -0.0440 -0.0522 -0.0688 145 ASN A ND2 1124 N N . TYR A 144 ? 0.2880 0.2299 0.4601 -0.0312 -0.0204 -0.0720 146 TYR A N 1125 C CA . TYR A 144 ? 0.2822 0.2244 0.4553 -0.0296 -0.0120 -0.0757 146 TYR A CA 1126 C C . TYR A 144 ? 0.2785 0.2174 0.4557 -0.0274 -0.0105 -0.0802 146 TYR A C 1127 O O . TYR A 144 ? 0.2553 0.1939 0.4386 -0.0270 -0.0153 -0.0788 146 TYR A O 1128 C CB . TYR A 144 ? 0.2512 0.2023 0.4361 -0.0273 -0.0090 -0.0729 146 TYR A CB 1129 C CG . TYR A 144 ? 0.2430 0.2001 0.4429 -0.0240 -0.0120 -0.0706 146 TYR A CG 1130 C CD1 . TYR A 144 ? 0.2110 0.1702 0.4204 -0.0205 -0.0092 -0.0733 146 TYR A CD1 1131 C CD2 . TYR A 144 ? 0.2370 0.1973 0.4410 -0.0241 -0.0176 -0.0658 146 TYR A CD2 1132 C CE1 . TYR A 144 ? 0.1624 0.1256 0.3831 -0.0180 -0.0123 -0.0706 146 TYR A CE1 1133 C CE2 . TYR A 144 ? 0.1898 0.1552 0.4058 -0.0217 -0.0196 -0.0638 146 TYR A CE2 1134 C CZ . TYR A 144 ? 0.2020 0.1682 0.4254 -0.0191 -0.0170 -0.0660 146 TYR A CZ 1135 O OH . TYR A 144 ? 0.2273 0.1970 0.4601 -0.0173 -0.0193 -0.0636 146 TYR A OH 1136 N N . ARG A 145 ? 0.2951 0.2311 0.4685 -0.0259 -0.0035 -0.0857 147 ARG A N 1137 C CA . ARG A 145 ? 0.3025 0.2320 0.4769 -0.0229 -0.0019 -0.0909 147 ARG A CA 1138 C C . ARG A 145 ? 0.2884 0.2232 0.4794 -0.0178 -0.0026 -0.0893 147 ARG A C 1139 O O . ARG A 145 ? 0.2770 0.2222 0.4784 -0.0155 -0.0002 -0.0870 147 ARG A O 1140 C CB . ARG A 145 ? 0.3164 0.2434 0.4840 -0.0213 0.0067 -0.0974 147 ARG A CB 1141 C CG . ARG A 145 ? 0.3478 0.2640 0.4945 -0.0264 0.0070 -0.1007 147 ARG A CG 1142 C CD . ARG A 145 ? 0.3100 0.2260 0.4505 -0.0248 0.0175 -0.1073 147 ARG A CD 1143 N NE . ARG A 145 ? 0.2825 0.2087 0.4245 -0.0270 0.0224 -0.1045 147 ARG A NE 1144 C CZ . ARG A 145 ? 0.3448 0.2765 0.4857 -0.0265 0.0325 -0.1088 147 ARG A CZ 1145 N NH1 . ARG A 145 ? 0.3130 0.2416 0.4519 -0.0223 0.0395 -0.1169 147 ARG A NH1 1146 N NH2 . ARG A 145 ? 0.2934 0.2333 0.4346 -0.0305 0.0360 -0.1052 147 ARG A NH2 1147 N N . VAL A 146 ? 0.2718 0.1982 0.4634 -0.0164 -0.0057 -0.0908 148 VAL A N 1148 C CA . VAL A 146 ? 0.2621 0.1905 0.4665 -0.0120 -0.0076 -0.0886 148 VAL A CA 1149 C C . VAL A 146 ? 0.2813 0.1989 0.4844 -0.0066 -0.0050 -0.0942 148 VAL A C 1150 O O . VAL A 146 ? 0.2943 0.2022 0.4858 -0.0073 -0.0023 -0.0999 148 VAL A O 1151 C CB . VAL A 146 ? 0.2724 0.2007 0.4789 -0.0163 -0.0149 -0.0830 148 VAL A CB 1152 C CG1 . VAL A 146 ? 0.2017 0.1419 0.4117 -0.0188 -0.0164 -0.0779 148 VAL A CG1 1153 C CG2 . VAL A 146 ? 0.1978 0.1147 0.3923 -0.0220 -0.0191 -0.0849 148 VAL A CG2 1154 N N . GLY A 147 ? 0.2649 0.1831 0.4786 -0.0009 -0.0059 -0.0929 149 GLY A N 1155 C CA . GLY A 147 ? 0.2599 0.1659 0.4723 0.0057 -0.0044 -0.0979 149 GLY A CA 1156 C C . GLY A 147 ? 0.2831 0.1943 0.4972 0.0116 0.0036 -0.1043 149 GLY A C 1157 O O . GLY A 147 ? 0.2759 0.2026 0.4960 0.0108 0.0075 -0.1035 149 GLY A O 1158 N N . ALA A 148 ? 0.2876 0.1863 0.4965 0.0175 0.0064 -0.1109 150 ALA A N 1159 C CA . ALA A 148 ? 0.3064 0.2107 0.5177 0.0240 0.0149 -0.1180 150 ALA A CA 1160 C C . ALA A 148 ? 0.3382 0.2469 0.5390 0.0171 0.0199 -0.1203 150 ALA A C 1161 O O . ALA A 148 ? 0.3530 0.2745 0.5588 0.0193 0.0275 -0.1235 150 ALA A O 1162 C CB . ALA A 148 ? 0.3408 0.2270 0.5447 0.0312 0.0168 -0.1253 150 ALA A CB 1163 N N . LEU A 149 ? 0.3450 0.2433 0.5309 0.0084 0.0157 -0.1188 151 LEU A N 1164 C CA . LEU A 149 ? 0.3695 0.2698 0.5426 0.0020 0.0198 -0.1208 151 LEU A CA 1165 C C . LEU A 149 ? 0.3586 0.2771 0.5397 -0.0012 0.0216 -0.1157 151 LEU A C 1166 O O . LEU A 149 ? 0.3672 0.2903 0.5406 -0.0047 0.0276 -0.1177 151 LEU A O 1167 C CB . LEU A 149 ? 0.3676 0.2540 0.5230 -0.0066 0.0136 -0.1200 151 LEU A CB 1168 C CG . LEU A 149 ? 0.3774 0.2429 0.5186 -0.0060 0.0130 -0.1268 151 LEU A CG 1169 C CD1 . LEU A 149 ? 0.3273 0.1831 0.4575 -0.0153 0.0038 -0.1237 151 LEU A CD1 1170 C CD2 . LEU A 149 ? 0.3127 0.1711 0.4403 -0.0038 0.0217 -0.1360 151 LEU A CD2 1171 N N . GLY A 150 ? 0.3380 0.2648 0.5324 -0.0008 0.0164 -0.1090 152 GLY A N 1172 C CA . GLY A 150 ? 0.3263 0.2683 0.5287 -0.0037 0.0170 -0.1038 152 GLY A CA 1173 C C . GLY A 150 ? 0.3219 0.2790 0.5416 0.0022 0.0218 -0.1046 152 GLY A C 1174 O O . GLY A 150 ? 0.3277 0.2971 0.5517 -0.0008 0.0252 -0.1027 152 GLY A O 1175 N N . PHE A 151 ? 0.3101 0.2664 0.5396 0.0103 0.0215 -0.1071 153 PHE A N 1176 C CA . PHE A 151 ? 0.2934 0.2658 0.5413 0.0157 0.0233 -0.1064 153 PHE A CA 1177 C C . PHE A 151 ? 0.3194 0.2946 0.5764 0.0259 0.0278 -0.1128 153 PHE A C 1178 O O . PHE A 151 ? 0.3261 0.3163 0.6005 0.0314 0.0280 -0.1122 153 PHE A O 1179 C CB . PHE A 151 ? 0.2681 0.2419 0.5239 0.0156 0.0150 -0.0993 153 PHE A CB 1180 C CG . PHE A 151 ? 0.2328 0.2097 0.4843 0.0071 0.0119 -0.0933 153 PHE A CG 1181 C CD1 . PHE A 151 ? 0.1720 0.1631 0.4310 0.0045 0.0142 -0.0911 153 PHE A CD1 1182 C CD2 . PHE A 151 ? 0.2160 0.1817 0.4571 0.0022 0.0062 -0.0898 153 PHE A CD2 1183 C CE1 . PHE A 151 ? 0.1774 0.1693 0.4319 -0.0023 0.0111 -0.0857 153 PHE A CE1 1184 C CE2 . PHE A 151 ? 0.1962 0.1650 0.4342 -0.0038 0.0033 -0.0846 153 PHE A CE2 1185 C CZ . PHE A 151 ? 0.1787 0.1594 0.4229 -0.0056 0.0056 -0.0825 153 PHE A CZ 1186 N N . LEU A 152 ? 0.3305 0.2923 0.5766 0.0289 0.0313 -0.1193 154 LEU A N 1187 C CA . LEU A 152 ? 0.3545 0.3199 0.6088 0.0396 0.0374 -0.1268 154 LEU A CA 1188 C C . LEU A 152 ? 0.3538 0.3444 0.6226 0.0403 0.0457 -0.1291 154 LEU A C 1189 O O . LEU A 152 ? 0.3267 0.3241 0.5890 0.0316 0.0509 -0.1288 154 LEU A O 1190 C CB . LEU A 152 ? 0.3749 0.3238 0.6127 0.0410 0.0424 -0.1346 154 LEU A CB 1191 C CG . LEU A 152 ? 0.4080 0.3552 0.6504 0.0532 0.0489 -0.1437 154 LEU A CG 1192 C CD1 . LEU A 152 ? 0.4114 0.3339 0.6454 0.0589 0.0427 -0.1450 154 LEU A CD1 1193 C CD2 . LEU A 152 ? 0.4141 0.3574 0.6412 0.0502 0.0589 -0.1517 154 LEU A CD2 1194 N N . ALA A 153 ? 0.3435 0.3471 0.6312 0.0505 0.0467 -0.1315 155 ALA A N 1195 C CA . ALA A 153 ? 0.3712 0.4010 0.6755 0.0508 0.0535 -0.1334 155 ALA A CA 1196 C C . ALA A 153 ? 0.4085 0.4492 0.7272 0.0637 0.0599 -0.1417 155 ALA A C 1197 O O . ALA A 153 ? 0.4031 0.4385 0.7299 0.0752 0.0547 -0.1425 155 ALA A O 1198 C CB . ALA A 153 ? 0.3236 0.3681 0.6419 0.0468 0.0465 -0.1253 155 ALA A CB 1199 N N . LEU A 154 ? 0.4595 0.5138 0.7794 0.0617 0.0715 -0.1479 156 LEU A N 1200 C CA . LEU A 154 ? 0.5326 0.6061 0.8713 0.0730 0.0792 -0.1558 156 LEU A CA 1201 C C . LEU A 154 ? 0.5599 0.6625 0.9120 0.0640 0.0855 -0.1544 156 LEU A C 1202 O O . LEU A 154 ? 0.5759 0.6835 0.9186 0.0552 0.0956 -0.1574 156 LEU A O 1203 C CB . LEU A 154 ? 0.5581 0.6191 0.8822 0.0771 0.0888 -0.1653 156 LEU A CB 1204 C CG . LEU A 154 ? 0.6010 0.6584 0.9338 0.0946 0.0907 -0.1734 156 LEU A CG 1205 C CD1 . LEU A 154 ? 0.5674 0.6199 0.9132 0.1051 0.0780 -0.1684 156 LEU A CD1 1206 C CD2 . LEU A 154 ? 0.6365 0.6661 0.9439 0.0956 0.0950 -0.1800 156 LEU A CD2 1207 N N . PRO A 155 ? 0.5762 0.6965 0.9481 0.0646 0.0788 -0.1492 157 PRO A N 1208 C CA . PRO A 155 ? 0.5811 0.7159 0.9536 0.0498 0.0816 -0.1448 157 PRO A CA 1209 C C . PRO A 155 ? 0.5872 0.7484 0.9709 0.0466 0.0954 -0.1514 157 PRO A C 1210 O O . PRO A 155 ? 0.5760 0.7535 0.9771 0.0581 0.1010 -0.1588 157 PRO A O 1211 C CB . PRO A 155 ? 0.5771 0.7200 0.9637 0.0495 0.0699 -0.1371 157 PRO A CB 1212 C CG . PRO A 155 ? 0.5905 0.7214 0.9830 0.0653 0.0605 -0.1372 157 PRO A CG 1213 C CD . PRO A 155 ? 0.5729 0.7004 0.9643 0.0759 0.0693 -0.1469 157 PRO A CD 1214 N N . GLY A 156 ? 0.5765 0.7397 0.9484 0.0314 0.1011 -0.1489 158 GLY A N 1215 C CA . GLY A 156 ? 0.5871 0.7692 0.9616 0.0257 0.1161 -0.1553 158 GLY A CA 1216 C C . GLY A 156 ? 0.6036 0.7715 0.9564 0.0247 0.1269 -0.1618 158 GLY A C 1217 O O . GLY A 156 ? 0.6165 0.7947 0.9636 0.0151 0.1388 -0.1646 158 GLY A O 1218 N N . ASN A 157 ? 0.6033 0.7468 0.9426 0.0337 0.1228 -0.1641 159 ASN A N 1219 C CA . ASN A 157 ? 0.5986 0.7239 0.9141 0.0331 0.1309 -0.1702 159 ASN A CA 1220 C C . ASN A 157 ? 0.5933 0.6926 0.8789 0.0208 0.1261 -0.1640 159 ASN A C 1221 O O . ASN A 157 ? 0.5935 0.6731 0.8713 0.0221 0.1139 -0.1584 159 ASN A O 1222 C CB . ASN A 157 ? 0.6135 0.7240 0.9292 0.0489 0.1276 -0.1759 159 ASN A CB 1223 C CG . ASN A 157 ? 0.6477 0.7406 0.9403 0.0499 0.1368 -0.1843 159 ASN A CG 1224 O OD1 . ASN A 157 ? 0.6650 0.7454 0.9334 0.0377 0.1400 -0.1827 159 ASN A OD1 1225 N ND2 . ASN A 157 ? 0.6076 0.6982 0.9064 0.0648 0.1406 -0.1932 159 ASN A ND2 1226 N N . PRO A 158 ? 0.5949 0.6937 0.8631 0.0089 0.1355 -0.1649 160 PRO A N 1227 C CA . PRO A 158 ? 0.5773 0.6526 0.8181 -0.0027 0.1294 -0.1578 160 PRO A CA 1228 C C . PRO A 158 ? 0.5864 0.6333 0.8047 0.0009 0.1245 -0.1599 160 PRO A C 1229 O O . PRO A 158 ? 0.5874 0.6156 0.7849 -0.0072 0.1175 -0.1541 160 PRO A O 1230 C CB . PRO A 158 ? 0.5935 0.6760 0.8213 -0.0159 0.1411 -0.1582 160 PRO A CB 1231 C CG . PRO A 158 ? 0.5975 0.7054 0.8427 -0.0104 0.1562 -0.1683 160 PRO A CG 1232 C CD . PRO A 158 ? 0.5972 0.7173 0.8702 0.0055 0.1519 -0.1720 160 PRO A CD 1233 N N . GLU A 159 ? 0.5896 0.6329 0.8123 0.0131 0.1270 -0.1680 161 GLU A N 1234 C CA . GLU A 159 ? 0.5861 0.6012 0.7881 0.0163 0.1213 -0.1702 161 GLU A CA 1235 C C . GLU A 159 ? 0.5482 0.5512 0.7550 0.0191 0.1058 -0.1628 161 GLU A C 1236 O O . GLU A 159 ? 0.5567 0.5363 0.7451 0.0172 0.0983 -0.1615 161 GLU A O 1237 C CB . GLU A 159 ? 0.6098 0.6206 0.8117 0.0285 0.1293 -0.1821 161 GLU A CB 1238 C CG . GLU A 159 ? 0.6610 0.6847 0.8593 0.0281 0.1467 -0.1916 161 GLU A CG 1239 C CD . GLU A 159 ? 0.7535 0.7723 0.9270 0.0126 0.1523 -0.1893 161 GLU A CD 1240 O OE1 . GLU A 159 ? 0.7952 0.7892 0.9417 0.0064 0.1467 -0.1874 161 GLU A OE1 1241 O OE2 . GLU A 159 ? 0.7884 0.8283 0.9690 0.0061 0.1621 -0.1892 161 GLU A OE2 1242 N N . ALA A 160 ? 0.4915 0.5110 0.7229 0.0235 0.1013 -0.1586 162 ALA A N 1243 C CA . ALA A 160 ? 0.4608 0.4726 0.6999 0.0266 0.0875 -0.1514 162 ALA A CA 1244 C C . ALA A 160 ? 0.4183 0.4529 0.6811 0.0267 0.0852 -0.1462 162 ALA A C 1245 O O . ALA A 160 ? 0.4061 0.4505 0.6888 0.0371 0.0829 -0.1476 162 ALA A O 1246 C CB . ALA A 160 ? 0.4499 0.4493 0.6930 0.0396 0.0838 -0.1560 162 ALA A CB 1247 N N . PRO A 161 ? 0.3998 0.4423 0.6598 0.0152 0.0857 -0.1405 163 PRO A N 1248 C CA . PRO A 161 ? 0.3699 0.4349 0.6510 0.0138 0.0851 -0.1368 163 PRO A CA 1249 C C . PRO A 161 ? 0.3490 0.4103 0.6384 0.0155 0.0722 -0.1291 163 PRO A C 1250 O O . PRO A 161 ? 0.3610 0.4400 0.6691 0.0164 0.0702 -0.1267 163 PRO A O 1251 C CB . PRO A 161 ? 0.3536 0.4221 0.6231 -0.0002 0.0903 -0.1336 163 PRO A CB 1252 C CG . PRO A 161 ? 0.3676 0.4114 0.6108 -0.0059 0.0862 -0.1308 163 PRO A CG 1253 C CD . PRO A 161 ? 0.4094 0.4390 0.6456 0.0030 0.0862 -0.1370 163 PRO A CD 1254 N N . GLY A 162 ? 0.3243 0.3642 0.6003 0.0156 0.0637 -0.1255 164 GLY A N 1255 C CA . GLY A 162 ? 0.2848 0.3212 0.5659 0.0152 0.0526 -0.1179 164 GLY A CA 1256 C C . GLY A 162 ? 0.2756 0.3068 0.5451 0.0041 0.0489 -0.1110 164 GLY A C 1257 O O . GLY A 162 ? 0.2805 0.3142 0.5409 -0.0037 0.0551 -0.1114 164 GLY A O 1258 N N . ASN A 163 ? 0.2445 0.2680 0.5136 0.0036 0.0393 -0.1047 165 ASN A N 1259 C CA . ASN A 163 ? 0.2392 0.2585 0.4997 -0.0050 0.0349 -0.0981 165 ASN A CA 1260 C C . ASN A 163 ? 0.2530 0.2591 0.4925 -0.0119 0.0363 -0.0976 165 ASN A C 1261 O O . ASN A 163 ? 0.2625 0.2663 0.4943 -0.0188 0.0342 -0.0927 165 ASN A O 1262 C CB . ASN A 163 ? 0.2367 0.2718 0.5074 -0.0097 0.0372 -0.0958 165 ASN A CB 1263 C CG . ASN A 163 ? 0.2353 0.2825 0.5252 -0.0040 0.0332 -0.0949 165 ASN A CG 1264 O OD1 . ASN A 163 ? 0.2110 0.2523 0.5047 0.0028 0.0272 -0.0941 165 ASN A OD1 1265 N ND2 . ASN A 163 ? 0.2053 0.2697 0.5071 -0.0071 0.0362 -0.0950 165 ASN A ND2 1266 N N . MET A 164 ? 0.2505 0.2470 0.4796 -0.0099 0.0392 -0.1026 166 MET A N 1267 C CA . MET A 164 ? 0.2632 0.2472 0.4712 -0.0163 0.0397 -0.1023 166 MET A CA 1268 C C . MET A 164 ? 0.2551 0.2301 0.4560 -0.0201 0.0302 -0.0954 166 MET A C 1269 O O . MET A 164 ? 0.2682 0.2381 0.4558 -0.0265 0.0294 -0.0923 166 MET A O 1270 C CB . MET A 164 ? 0.2861 0.2588 0.4838 -0.0129 0.0422 -0.1089 166 MET A CB 1271 C CG . MET A 164 ? 0.3200 0.3018 0.5240 -0.0083 0.0527 -0.1165 166 MET A CG 1272 S SD . MET A 164 ? 0.3309 0.3218 0.5585 0.0043 0.0523 -0.1201 166 MET A SD 1273 C CE . MET A 164 ? 0.2339 0.2011 0.4484 0.0085 0.0464 -0.1229 166 MET A CE 1274 N N . GLY A 165 ? 0.2550 0.2278 0.4641 -0.0162 0.0228 -0.0928 167 GLY A N 1275 C CA . GLY A 165 ? 0.2482 0.2147 0.4521 -0.0193 0.0143 -0.0868 167 GLY A CA 1276 C C . GLY A 165 ? 0.2518 0.2247 0.4598 -0.0223 0.0125 -0.0812 167 GLY A C 1277 O O . GLY A 165 ? 0.2651 0.2328 0.4651 -0.0256 0.0078 -0.0770 167 GLY A O 1278 N N . LEU A 166 ? 0.2572 0.2415 0.4781 -0.0209 0.0159 -0.0814 168 LEU A N 1279 C CA . LEU A 166 ? 0.2389 0.2285 0.4619 -0.0249 0.0159 -0.0774 168 LEU A CA 1280 C C . LEU A 166 ? 0.2563 0.2422 0.4649 -0.0317 0.0212 -0.0776 168 LEU A C 1281 O O . LEU A 166 ? 0.2619 0.2417 0.4615 -0.0358 0.0182 -0.0731 168 LEU A O 1282 C CB . LEU A 166 ? 0.2219 0.2255 0.4620 -0.0224 0.0185 -0.0787 168 LEU A CB 1283 C CG . LEU A 166 ? 0.1947 0.2001 0.4460 -0.0172 0.0119 -0.0763 168 LEU A CG 1284 C CD1 . LEU A 166 ? 0.1950 0.2143 0.4622 -0.0141 0.0142 -0.0784 168 LEU A CD1 1285 C CD2 . LEU A 166 ? 0.1203 0.1218 0.3686 -0.0199 0.0061 -0.0707 168 LEU A CD2 1286 N N . PHE A 167 ? 0.2646 0.2525 0.4691 -0.0325 0.0288 -0.0828 169 PHE A N 1287 C CA . PHE A 167 ? 0.2915 0.2730 0.4784 -0.0396 0.0337 -0.0827 169 PHE A CA 1288 C C . PHE A 167 ? 0.3158 0.2812 0.4838 -0.0415 0.0274 -0.0797 169 PHE A C 1289 O O . PHE A 167 ? 0.3563 0.3140 0.5094 -0.0472 0.0273 -0.0764 169 PHE A O 1290 C CB . PHE A 167 ? 0.2855 0.2731 0.4713 -0.0402 0.0441 -0.0894 169 PHE A CB 1291 C CG . PHE A 167 ? 0.3148 0.3195 0.5155 -0.0419 0.0512 -0.0911 169 PHE A CG 1292 C CD1 . PHE A 167 ? 0.2972 0.3161 0.5168 -0.0352 0.0547 -0.0962 169 PHE A CD1 1293 C CD2 . PHE A 167 ? 0.3078 0.3140 0.5035 -0.0506 0.0537 -0.0874 169 PHE A CD2 1294 C CE1 . PHE A 167 ? 0.3180 0.3554 0.5530 -0.0371 0.0604 -0.0977 169 PHE A CE1 1295 C CE2 . PHE A 167 ? 0.2601 0.2834 0.4700 -0.0538 0.0599 -0.0889 169 PHE A CE2 1296 C CZ . PHE A 167 ? 0.2908 0.3311 0.5213 -0.0470 0.0632 -0.0942 169 PHE A CZ 1297 N N . ASP A 168 ? 0.3086 0.2689 0.4768 -0.0371 0.0218 -0.0808 170 ASP A N 1298 C CA . ASP A 168 ? 0.3092 0.2577 0.4632 -0.0387 0.0144 -0.0778 170 ASP A CA 1299 C C . ASP A 168 ? 0.3026 0.2503 0.4586 -0.0392 0.0076 -0.0709 170 ASP A C 1300 O O . ASP A 168 ? 0.3183 0.2574 0.4599 -0.0424 0.0044 -0.0674 170 ASP A O 1301 C CB . ASP A 168 ? 0.2910 0.2364 0.4484 -0.0347 0.0092 -0.0801 170 ASP A CB 1302 C CG . ASP A 168 ? 0.3383 0.2800 0.4901 -0.0337 0.0148 -0.0872 170 ASP A CG 1303 O OD1 . ASP A 168 ? 0.3085 0.2492 0.4505 -0.0365 0.0224 -0.0906 170 ASP A OD1 1304 O OD2 . ASP A 168 ? 0.3711 0.3102 0.5282 -0.0301 0.0118 -0.0897 170 ASP A OD2 1305 N N . GLN A 169 ? 0.2607 0.2163 0.4334 -0.0354 0.0050 -0.0693 171 GLN A N 1306 C CA . GLN A 169 ? 0.2701 0.2252 0.4449 -0.0354 0.0002 -0.0640 171 GLN A CA 1307 C C . GLN A 169 ? 0.2899 0.2410 0.4548 -0.0407 0.0041 -0.0618 171 GLN A C 1308 O O . GLN A 169 ? 0.3095 0.2514 0.4631 -0.0421 -0.0004 -0.0575 171 GLN A O 1309 C CB . GLN A 169 ? 0.2413 0.2055 0.4338 -0.0315 -0.0013 -0.0634 171 GLN A CB 1310 C CG . GLN A 169 ? 0.2315 0.1975 0.4321 -0.0272 -0.0055 -0.0644 171 GLN A CG 1311 C CD . GLN A 169 ? 0.2537 0.2281 0.4699 -0.0240 -0.0053 -0.0643 171 GLN A CD 1312 O OE1 . GLN A 169 ? 0.2337 0.2125 0.4542 -0.0250 -0.0039 -0.0627 171 GLN A OE1 1313 N NE2 . GLN A 169 ? 0.1982 0.1737 0.4215 -0.0206 -0.0074 -0.0657 171 GLN A NE2 1314 N N . GLN A 170 ? 0.2906 0.2480 0.4584 -0.0440 0.0122 -0.0647 172 GLN A N 1315 C CA . GLN A 170 ? 0.3155 0.2693 0.4746 -0.0506 0.0161 -0.0623 172 GLN A CA 1316 C C . GLN A 170 ? 0.3413 0.2809 0.4773 -0.0551 0.0159 -0.0604 172 GLN A C 1317 O O . GLN A 170 ? 0.3419 0.2710 0.4656 -0.0589 0.0140 -0.0558 172 GLN A O 1318 C CB . GLN A 170 ? 0.3020 0.2682 0.4700 -0.0541 0.0255 -0.0664 172 GLN A CB 1319 C CG . GLN A 170 ? 0.3026 0.2678 0.4659 -0.0617 0.0291 -0.0639 172 GLN A CG 1320 C CD . GLN A 170 ? 0.3244 0.3065 0.5012 -0.0650 0.0379 -0.0683 172 GLN A CD 1321 O OE1 . GLN A 170 ? 0.3587 0.3518 0.5514 -0.0645 0.0372 -0.0683 172 GLN A OE1 1322 N NE2 . GLN A 170 ? 0.2789 0.2643 0.4500 -0.0682 0.0463 -0.0722 172 GLN A NE2 1323 N N . LEU A 171 ? 0.3449 0.2825 0.4735 -0.0547 0.0178 -0.0639 173 LEU A N 1324 C CA . LEU A 171 ? 0.3523 0.2767 0.4577 -0.0594 0.0179 -0.0625 173 LEU A CA 1325 C C . LEU A 171 ? 0.3650 0.2784 0.4622 -0.0565 0.0066 -0.0570 173 LEU A C 1326 O O . LEU A 171 ? 0.3916 0.2918 0.4695 -0.0601 0.0041 -0.0529 173 LEU A O 1327 C CB . LEU A 171 ? 0.3617 0.2859 0.4603 -0.0596 0.0223 -0.0683 173 LEU A CB 1328 C CG . LEU A 171 ? 0.4026 0.3124 0.4742 -0.0654 0.0229 -0.0672 173 LEU A CG 1329 C CD1 . LEU A 171 ? 0.3918 0.2973 0.4503 -0.0742 0.0308 -0.0647 173 LEU A CD1 1330 C CD2 . LEU A 171 ? 0.4202 0.3295 0.4849 -0.0653 0.0273 -0.0736 173 LEU A CD2 1331 N N . ALA A 172 ? 0.3409 0.2600 0.4523 -0.0500 -0.0003 -0.0566 174 ALA A N 1332 C CA . ALA A 172 ? 0.3500 0.2622 0.4569 -0.0465 -0.0106 -0.0517 174 ALA A CA 1333 C C . ALA A 172 ? 0.3535 0.2606 0.4593 -0.0466 -0.0121 -0.0468 174 ALA A C 1334 O O . ALA A 172 ? 0.3669 0.2622 0.4593 -0.0459 -0.0183 -0.0422 174 ALA A O 1335 C CB . ALA A 172 ? 0.3210 0.2421 0.4440 -0.0405 -0.0163 -0.0529 174 ALA A CB 1336 N N . LEU A 173 ? 0.3388 0.2540 0.4583 -0.0471 -0.0072 -0.0480 175 LEU A N 1337 C CA . LEU A 173 ? 0.3510 0.2591 0.4667 -0.0490 -0.0076 -0.0441 175 LEU A CA 1338 C C . LEU A 173 ? 0.3709 0.2636 0.4637 -0.0562 -0.0050 -0.0411 175 LEU A C 1339 O O . LEU A 173 ? 0.3679 0.2468 0.4494 -0.0557 -0.0099 -0.0362 175 LEU A O 1340 C CB . LEU A 173 ? 0.3389 0.2581 0.4711 -0.0500 -0.0028 -0.0460 175 LEU A CB 1341 C CG . LEU A 173 ? 0.3281 0.2618 0.4812 -0.0442 -0.0040 -0.0489 175 LEU A CG 1342 C CD1 . LEU A 173 ? 0.2914 0.2324 0.4564 -0.0457 -0.0012 -0.0495 175 LEU A CD1 1343 C CD2 . LEU A 173 ? 0.3149 0.2478 0.4716 -0.0373 -0.0122 -0.0470 175 LEU A CD2 1344 N N . GLN A 174 ? 0.3663 0.2607 0.4520 -0.0624 0.0027 -0.0440 176 GLN A N 1345 C CA A GLN A 174 ? 0.4105 0.2907 0.4730 -0.0706 0.0064 -0.0414 176 GLN A CA 1346 C CA B GLN A 174 ? 0.4106 0.2907 0.4731 -0.0705 0.0063 -0.0414 176 GLN A CA 1347 C C . GLN A 174 ? 0.4290 0.2928 0.4712 -0.0682 -0.0023 -0.0371 176 GLN A C 1348 O O . GLN A 174 ? 0.4540 0.3003 0.4762 -0.0720 -0.0043 -0.0320 176 GLN A O 1349 C CB A GLN A 174 ? 0.4167 0.3047 0.4769 -0.0772 0.0175 -0.0465 176 GLN A CB 1350 C CB B GLN A 174 ? 0.4174 0.3054 0.4779 -0.0766 0.0169 -0.0465 176 GLN A CB 1351 C CG A GLN A 174 ? 0.4601 0.3637 0.5368 -0.0818 0.0272 -0.0501 176 GLN A CG 1352 C CG B GLN A 174 ? 0.4958 0.3696 0.5307 -0.0861 0.0219 -0.0441 176 GLN A CG 1353 C CD A GLN A 174 ? 0.5063 0.4185 0.5802 -0.0881 0.0391 -0.0554 176 GLN A CD 1354 C CD B GLN A 174 ? 0.5715 0.4413 0.6033 -0.0942 0.0268 -0.0413 176 GLN A CD 1355 O OE1 A GLN A 174 ? 0.5444 0.4466 0.5979 -0.0919 0.0415 -0.0555 176 GLN A OE1 1356 O OE1 B GLN A 174 ? 0.6049 0.4884 0.6476 -0.0998 0.0364 -0.0451 176 GLN A OE1 1357 N NE2 A GLN A 174 ? 0.4704 0.4016 0.5646 -0.0890 0.0464 -0.0600 176 GLN A NE2 1358 N NE2 B GLN A 174 ? 0.6203 0.4712 0.6375 -0.0948 0.0199 -0.0347 176 GLN A NE2 1359 N N . TRP A 175 ? 0.4135 0.2825 0.4605 -0.0622 -0.0079 -0.0390 177 TRP A N 1360 C CA . TRP A 175 ? 0.4340 0.2907 0.4638 -0.0599 -0.0170 -0.0355 177 TRP A CA 1361 C C . TRP A 175 ? 0.4325 0.2798 0.4608 -0.0544 -0.0260 -0.0295 177 TRP A C 1362 O O . TRP A 175 ? 0.4570 0.2874 0.4648 -0.0546 -0.0319 -0.0244 177 TRP A O 1363 C CB . TRP A 175 ? 0.3986 0.2656 0.4380 -0.0550 -0.0217 -0.0394 177 TRP A CB 1364 C CG . TRP A 175 ? 0.4738 0.3307 0.4975 -0.0526 -0.0325 -0.0360 177 TRP A CG 1365 C CD1 . TRP A 175 ? 0.4700 0.3185 0.4734 -0.0570 -0.0332 -0.0368 177 TRP A CD1 1366 C CD2 . TRP A 175 ? 0.4384 0.2931 0.4648 -0.0453 -0.0443 -0.0313 177 TRP A CD2 1367 N NE1 . TRP A 175 ? 0.4960 0.3377 0.4899 -0.0532 -0.0454 -0.0327 177 TRP A NE1 1368 C CE2 . TRP A 175 ? 0.4708 0.3170 0.4794 -0.0456 -0.0524 -0.0293 177 TRP A CE2 1369 C CE3 . TRP A 175 ? 0.4087 0.2688 0.4512 -0.0382 -0.0487 -0.0290 177 TRP A CE3 1370 C CZ2 . TRP A 175 ? 0.4704 0.3143 0.4780 -0.0386 -0.0653 -0.0248 177 TRP A CZ2 1371 C CZ3 . TRP A 175 ? 0.4327 0.2907 0.4746 -0.0309 -0.0604 -0.0251 177 TRP A CZ3 1372 C CH2 . TRP A 175 ? 0.4457 0.2964 0.4711 -0.0309 -0.0688 -0.0229 177 TRP A CH2 1373 N N . VAL A 176 ? 0.4076 0.2654 0.4569 -0.0489 -0.0272 -0.0304 178 VAL A N 1374 C CA . VAL A 176 ? 0.4144 0.2649 0.4646 -0.0427 -0.0343 -0.0260 178 VAL A CA 1375 C C . VAL A 176 ? 0.4384 0.2713 0.4720 -0.0487 -0.0308 -0.0223 178 VAL A C 1376 O O . VAL A 176 ? 0.4714 0.2873 0.4898 -0.0460 -0.0373 -0.0172 178 VAL A O 1377 C CB . VAL A 176 ? 0.3895 0.2559 0.4655 -0.0363 -0.0349 -0.0285 178 VAL A CB 1378 C CG1 . VAL A 176 ? 0.3664 0.2242 0.4424 -0.0310 -0.0393 -0.0251 178 VAL A CG1 1379 C CG2 . VAL A 176 ? 0.3448 0.2252 0.4342 -0.0307 -0.0399 -0.0309 178 VAL A CG2 1380 N N . GLN A 177 ? 0.4475 0.2836 0.4830 -0.0569 -0.0210 -0.0245 179 GLN A N 1381 C CA . GLN A 177 ? 0.4759 0.2938 0.4930 -0.0646 -0.0178 -0.0207 179 GLN A CA 1382 C C . GLN A 177 ? 0.5134 0.3107 0.5013 -0.0684 -0.0208 -0.0159 179 GLN A C 1383 O O . GLN A 177 ? 0.5135 0.2896 0.4840 -0.0674 -0.0264 -0.0102 179 GLN A O 1384 C CB . GLN A 177 ? 0.4798 0.3075 0.5040 -0.0745 -0.0062 -0.0243 179 GLN A CB 1385 C CG . GLN A 177 ? 0.4440 0.2855 0.4914 -0.0719 -0.0048 -0.0272 179 GLN A CG 1386 C CD . GLN A 177 ? 0.4634 0.2901 0.5062 -0.0682 -0.0110 -0.0233 179 GLN A CD 1387 O OE1 . GLN A 177 ? 0.5041 0.3144 0.5317 -0.0753 -0.0091 -0.0203 179 GLN A OE1 1388 N NE2 . GLN A 177 ? 0.4076 0.2403 0.4639 -0.0577 -0.0174 -0.0239 179 GLN A NE2 1389 N N . LYS A 178 ? 0.5260 0.3280 0.5074 -0.0716 -0.0180 -0.0181 180 LYS A N 1390 C CA . LYS A 178 ? 0.5771 0.3593 0.5283 -0.0763 -0.0204 -0.0137 180 LYS A CA 1391 C C . LYS A 178 ? 0.5804 0.3514 0.5215 -0.0670 -0.0345 -0.0090 180 LYS A C 1392 O O . LYS A 178 ? 0.6103 0.3593 0.5249 -0.0690 -0.0393 -0.0032 180 LYS A O 1393 C CB . LYS A 178 ? 0.5780 0.3688 0.5244 -0.0829 -0.0125 -0.0185 180 LYS A CB 1394 C CG . LYS A 178 ? 0.6560 0.4568 0.6086 -0.0928 0.0018 -0.0226 180 LYS A CG 1395 C CD . LYS A 178 ? 0.7675 0.5761 0.7140 -0.0977 0.0097 -0.0279 180 LYS A CD 1396 C CE . LYS A 178 ? 0.8269 0.6493 0.7820 -0.1065 0.0246 -0.0331 180 LYS A CE 1397 N NZ . LYS A 178 ? 0.8731 0.7001 0.8188 -0.1104 0.0324 -0.0383 180 LYS A NZ 1398 N N . ASN A 179 ? 0.5338 0.3200 0.4956 -0.0569 -0.0413 -0.0114 181 ASN A N 1399 C CA . ASN A 179 ? 0.5334 0.3145 0.4878 -0.0491 -0.0539 -0.0082 181 ASN A CA 1400 C C . ASN A 179 ? 0.5094 0.2908 0.4755 -0.0375 -0.0636 -0.0054 181 ASN A C 1401 O O . ASN A 179 ? 0.5260 0.2983 0.4816 -0.0310 -0.0747 -0.0011 181 ASN A O 1402 C CB . ASN A 179 ? 0.5069 0.3048 0.4710 -0.0482 -0.0551 -0.0132 181 ASN A CB 1403 C CG . ASN A 179 ? 0.5503 0.3441 0.4972 -0.0583 -0.0473 -0.0157 181 ASN A CG 1404 O OD1 . ASN A 179 ? 0.6122 0.3899 0.5331 -0.0616 -0.0512 -0.0121 181 ASN A OD1 1405 N ND2 . ASN A 179 ? 0.5601 0.3681 0.5206 -0.0628 -0.0361 -0.0220 181 ASN A ND2 1406 N N . ILE A 180 ? 0.4633 0.2561 0.4512 -0.0343 -0.0598 -0.0081 182 ILE A N 1407 C CA . ILE A 180 ? 0.4603 0.2580 0.4626 -0.0223 -0.0683 -0.0070 182 ILE A CA 1408 C C . ILE A 180 ? 0.4973 0.2720 0.4822 -0.0163 -0.0764 -0.0006 182 ILE A C 1409 O O . ILE A 180 ? 0.5102 0.2887 0.5034 -0.0049 -0.0856 0.0007 182 ILE A O 1410 C CB . ILE A 180 ? 0.4415 0.2567 0.4703 -0.0198 -0.0627 -0.0116 182 ILE A CB 1411 C CG1 . ILE A 180 ? 0.3849 0.2166 0.4345 -0.0087 -0.0699 -0.0129 182 ILE A CG1 1412 C CG2 . ILE A 180 ? 0.4180 0.2205 0.4421 -0.0230 -0.0572 -0.0104 182 ILE A CG2 1413 C CD1 . ILE A 180 ? 0.3809 0.2302 0.4407 -0.0099 -0.0711 -0.0163 182 ILE A CD1 1414 N N . ALA A 181 ? 0.5220 0.2727 0.4827 -0.0234 -0.0733 0.0034 183 ALA A N 1415 C CA . ALA A 181 ? 0.5581 0.2837 0.5006 -0.0166 -0.0821 0.0099 183 ALA A CA 1416 C C . ALA A 181 ? 0.5795 0.3001 0.5104 -0.0095 -0.0945 0.0139 183 ALA A C 1417 O O . ALA A 181 ? 0.6179 0.3274 0.5442 0.0013 -0.1044 0.0179 183 ALA A O 1418 C CB . ALA A 181 ? 0.5709 0.2691 0.4874 -0.0267 -0.0767 0.0139 183 ALA A CB 1419 N N . ALA A 182 ? 0.5854 0.3146 0.5119 -0.0153 -0.0942 0.0125 184 ALA A N 1420 C CA . ALA A 182 ? 0.6037 0.3294 0.5182 -0.0101 -0.1066 0.0161 184 ALA A CA 1421 C C . ALA A 182 ? 0.5908 0.3371 0.5303 0.0037 -0.1166 0.0144 184 ALA A C 1422 O O . ALA A 182 ? 0.6199 0.3620 0.5530 0.0124 -0.1297 0.0184 184 ALA A O 1423 C CB . ALA A 182 ? 0.5896 0.3214 0.4950 -0.0204 -0.1026 0.0135 184 ALA A CB 1424 N N . PHE A 183 ? 0.5562 0.3255 0.5244 0.0051 -0.1102 0.0085 185 PHE A N 1425 C CA . PHE A 183 ? 0.5283 0.3209 0.5241 0.0162 -0.1163 0.0058 185 PHE A CA 1426 C C . PHE A 183 ? 0.5205 0.3090 0.5257 0.0274 -0.1183 0.0070 185 PHE A C 1427 O O . PHE A 183 ? 0.5106 0.3185 0.5388 0.0366 -0.1218 0.0045 185 PHE A O 1428 C CB . PHE A 183 ? 0.4955 0.3129 0.5149 0.0107 -0.1073 -0.0012 185 PHE A CB 1429 C CG . PHE A 183 ? 0.4990 0.3233 0.5132 0.0020 -0.1061 -0.0037 185 PHE A CG 1430 C CD1 . PHE A 183 ? 0.5109 0.3243 0.5083 -0.0097 -0.0968 -0.0046 185 PHE A CD1 1431 C CD2 . PHE A 183 ? 0.4616 0.3033 0.4872 0.0052 -0.1141 -0.0054 185 PHE A CD2 1432 C CE1 . PHE A 183 ? 0.5442 0.3622 0.5348 -0.0170 -0.0955 -0.0075 185 PHE A CE1 1433 C CE2 . PHE A 183 ? 0.5015 0.3470 0.5198 -0.0032 -0.1136 -0.0081 185 PHE A CE2 1434 C CZ . PHE A 183 ? 0.5196 0.3528 0.5204 -0.0137 -0.1040 -0.0094 185 PHE A CZ 1435 N N . GLY A 184 ? 0.5373 0.3007 0.5243 0.0256 -0.1152 0.0102 186 GLY A N 1436 C CA . GLY A 184 ? 0.5245 0.2801 0.5172 0.0348 -0.1155 0.0106 186 GLY A CA 1437 C C . GLY A 184 ? 0.5066 0.2710 0.5151 0.0306 -0.1040 0.0055 186 GLY A C 1438 O O . GLY A 184 ? 0.5071 0.2697 0.5243 0.0394 -0.1045 0.0045 186 GLY A O 1439 N N . GLY A 185 ? 0.4885 0.2624 0.5008 0.0180 -0.0940 0.0021 187 GLY A N 1440 C CA . GLY A 185 ? 0.4503 0.2340 0.4780 0.0135 -0.0838 -0.0026 187 GLY A CA 1441 C C . GLY A 185 ? 0.4883 0.2493 0.4976 0.0045 -0.0774 -0.0009 187 GLY A C 1442 O O . GLY A 185 ? 0.5119 0.2526 0.4972 -0.0016 -0.0783 0.0034 187 GLY A O 1443 N N . ASN A 186 ? 0.4746 0.2383 0.4944 0.0038 -0.0715 -0.0040 188 ASN A N 1444 C CA . ASN A 186 ? 0.4839 0.2328 0.4924 -0.0065 -0.0642 -0.0039 188 ASN A CA 1445 C C . ASN A 186 ? 0.4726 0.2405 0.4937 -0.0181 -0.0541 -0.0083 188 ASN A C 1446 O O . ASN A 186 ? 0.4398 0.2244 0.4806 -0.0167 -0.0505 -0.0127 188 ASN A O 1447 C CB . ASN A 186 ? 0.4988 0.2422 0.5136 0.0001 -0.0644 -0.0056 188 ASN A CB 1448 C CG . ASN A 186 ? 0.5160 0.2386 0.5156 -0.0098 -0.0591 -0.0049 188 ASN A CG 1449 O OD1 . ASN A 186 ? 0.5973 0.3129 0.5842 -0.0225 -0.0541 -0.0033 188 ASN A OD1 1450 N ND2 . ASN A 186 ? 0.4817 0.1947 0.4823 -0.0045 -0.0597 -0.0064 188 ASN A ND2 1451 N N . PRO A 187 ? 0.4921 0.2559 0.5002 -0.0293 -0.0495 -0.0072 189 PRO A N 1452 C CA . PRO A 187 ? 0.4848 0.2655 0.5038 -0.0396 -0.0396 -0.0114 189 PRO A CA 1453 C C . PRO A 187 ? 0.4960 0.2779 0.5227 -0.0449 -0.0336 -0.0139 189 PRO A C 1454 O O . PRO A 187 ? 0.4801 0.2807 0.5223 -0.0503 -0.0268 -0.0182 189 PRO A O 1455 C CB . PRO A 187 ? 0.5007 0.2687 0.4974 -0.0504 -0.0359 -0.0087 189 PRO A CB 1456 C CG . PRO A 187 ? 0.5348 0.2728 0.5062 -0.0494 -0.0417 -0.0024 189 PRO A CG 1457 C CD . PRO A 187 ? 0.5206 0.2589 0.4997 -0.0336 -0.0524 -0.0013 189 PRO A CD 1458 N N . LYS A 188 ? 0.5164 0.2775 0.5315 -0.0431 -0.0366 -0.0114 190 LYS A N 1459 C CA . LYS A 188 ? 0.5035 0.2633 0.5239 -0.0479 -0.0324 -0.0138 190 LYS A CA 1460 C C . LYS A 188 ? 0.4803 0.2527 0.5201 -0.0374 -0.0351 -0.0173 190 LYS A C 1461 O O . LYS A 188 ? 0.4609 0.2319 0.5047 -0.0405 -0.0325 -0.0196 190 LYS A O 1462 C CB . LYS A 188 ? 0.5365 0.2650 0.5328 -0.0522 -0.0339 -0.0099 190 LYS A CB 1463 C CG . LYS A 188 ? 0.5975 0.3123 0.5730 -0.0667 -0.0289 -0.0065 190 LYS A CG 1464 C CD . LYS A 188 ? 0.7023 0.3851 0.6546 -0.0723 -0.0300 -0.0029 190 LYS A CD 1465 C CE . LYS A 188 ? 0.8150 0.4791 0.7417 -0.0863 -0.0262 0.0018 190 LYS A CE 1466 N NZ . LYS A 188 ? 0.9321 0.5631 0.8352 -0.0944 -0.0265 0.0052 190 LYS A NZ 1467 N N . SER A 189 ? 0.4396 0.2242 0.4908 -0.0260 -0.0401 -0.0178 191 SER A N 1468 C CA . SER A 189 ? 0.4073 0.2058 0.4771 -0.0177 -0.0411 -0.0214 191 SER A CA 1469 C C . SER A 189 ? 0.4053 0.2288 0.4935 -0.0139 -0.0414 -0.0235 191 SER A C 1470 O O . SER A 189 ? 0.4102 0.2374 0.5017 -0.0046 -0.0473 -0.0224 191 SER A O 1471 C CB . SER A 189 ? 0.4195 0.2023 0.4822 -0.0059 -0.0477 -0.0198 191 SER A CB 1472 O OG . SER A 189 ? 0.4079 0.2049 0.4881 0.0030 -0.0482 -0.0234 191 SER A OG 1473 N N . VAL A 190 ? 0.3711 0.2117 0.4716 -0.0211 -0.0354 -0.0266 192 VAL A N 1474 C CA . VAL A 190 ? 0.3470 0.2084 0.4628 -0.0196 -0.0348 -0.0288 192 VAL A CA 1475 C C . VAL A 190 ? 0.3327 0.2104 0.4669 -0.0195 -0.0314 -0.0326 192 VAL A C 1476 O O . VAL A 190 ? 0.3677 0.2453 0.5025 -0.0263 -0.0268 -0.0341 192 VAL A O 1477 C CB . VAL A 190 ? 0.3512 0.2144 0.4609 -0.0283 -0.0305 -0.0289 192 VAL A CB 1478 C CG1 . VAL A 190 ? 0.3286 0.2118 0.4536 -0.0272 -0.0293 -0.0319 192 VAL A CG1 1479 C CG2 . VAL A 190 ? 0.3588 0.2040 0.4473 -0.0291 -0.0341 -0.0246 192 VAL A CG2 1480 N N . THR A 191 ? 0.3107 0.2022 0.4591 -0.0124 -0.0337 -0.0341 193 THR A N 1481 C CA . THR A 191 ? 0.2757 0.1811 0.4392 -0.0129 -0.0306 -0.0371 193 THR A CA 1482 C C . THR A 191 ? 0.2786 0.2000 0.4537 -0.0132 -0.0299 -0.0386 193 THR A C 1483 O O . THR A 191 ? 0.2702 0.1947 0.4462 -0.0091 -0.0336 -0.0377 193 THR A O 1484 C CB . THR A 191 ? 0.2875 0.1938 0.4561 -0.0049 -0.0332 -0.0377 193 THR A CB 1485 O OG1 . THR A 191 ? 0.3379 0.2265 0.4938 -0.0043 -0.0339 -0.0368 193 THR A OG1 1486 C CG2 . THR A 191 ? 0.2314 0.1520 0.4144 -0.0045 -0.0308 -0.0404 193 THR A CG2 1487 N N . LEU A 192 ? 0.2675 0.1981 0.4504 -0.0183 -0.0256 -0.0408 194 LEU A N 1488 C CA . LEU A 192 ? 0.2582 0.2019 0.4519 -0.0177 -0.0250 -0.0425 194 LEU A CA 1489 C C . LEU A 192 ? 0.2472 0.2000 0.4526 -0.0133 -0.0264 -0.0432 194 LEU A C 1490 O O . LEU A 192 ? 0.2254 0.1778 0.4328 -0.0134 -0.0253 -0.0437 194 LEU A O 1491 C CB . LEU A 192 ? 0.2322 0.1824 0.4305 -0.0234 -0.0200 -0.0449 194 LEU A CB 1492 C CG . LEU A 192 ? 0.2539 0.1966 0.4412 -0.0298 -0.0164 -0.0447 194 LEU A CG 1493 C CD1 . LEU A 192 ? 0.2185 0.1710 0.4132 -0.0345 -0.0108 -0.0476 194 LEU A CD1 1494 C CD2 . LEU A 192 ? 0.2077 0.1416 0.3820 -0.0298 -0.0182 -0.0430 194 LEU A CD2 1495 N N . PHE A 193 ? 0.2418 0.2026 0.4539 -0.0105 -0.0286 -0.0434 195 PHE A N 1496 C CA . PHE A 193 ? 0.2266 0.1971 0.4499 -0.0083 -0.0286 -0.0441 195 PHE A CA 1497 C C . PHE A 193 ? 0.2204 0.1980 0.4498 -0.0098 -0.0286 -0.0451 195 PHE A C 1498 O O . PHE A 193 ? 0.2366 0.2126 0.4621 -0.0109 -0.0299 -0.0453 195 PHE A O 1499 C CB . PHE A 193 ? 0.2259 0.1982 0.4513 -0.0027 -0.0312 -0.0432 195 PHE A CB 1500 C CG . PHE A 193 ? 0.2185 0.1935 0.4442 0.0007 -0.0352 -0.0421 195 PHE A CG 1501 C CD1 . PHE A 193 ? 0.2650 0.2334 0.4820 -0.0001 -0.0377 -0.0411 195 PHE A CD1 1502 C CD2 . PHE A 193 ? 0.2004 0.1854 0.4348 0.0049 -0.0368 -0.0421 195 PHE A CD2 1503 C CE1 . PHE A 193 ? 0.2599 0.2315 0.4772 0.0034 -0.0429 -0.0400 195 PHE A CE1 1504 C CE2 . PHE A 193 ? 0.2164 0.2067 0.4532 0.0081 -0.0411 -0.0414 195 PHE A CE2 1505 C CZ . PHE A 193 ? 0.2114 0.1949 0.4396 0.0076 -0.0448 -0.0402 195 PHE A CZ 1506 N N . GLY A 194 ? 0.2172 0.2013 0.4549 -0.0099 -0.0276 -0.0458 196 GLY A N 1507 C CA . GLY A 194 ? 0.1971 0.1852 0.4395 -0.0116 -0.0274 -0.0468 196 GLY A CA 1508 C C . GLY A 194 ? 0.1980 0.1912 0.4476 -0.0112 -0.0272 -0.0463 196 GLY A C 1509 O O . GLY A 194 ? 0.1856 0.1793 0.4360 -0.0102 -0.0264 -0.0457 196 GLY A O 1510 N N . GLU A 195 ? 0.1962 0.1916 0.4494 -0.0124 -0.0280 -0.0465 197 GLU A N 1511 C CA . GLU A 195 ? 0.1889 0.1869 0.4466 -0.0129 -0.0278 -0.0455 197 GLU A CA 1512 C C . GLU A 195 ? 0.2042 0.1988 0.4631 -0.0138 -0.0274 -0.0465 197 GLU A C 1513 O O . GLU A 195 ? 0.2054 0.1966 0.4623 -0.0147 -0.0275 -0.0483 197 GLU A O 1514 C CB . GLU A 195 ? 0.1941 0.1974 0.4548 -0.0139 -0.0291 -0.0443 197 GLU A CB 1515 C CG . GLU A 195 ? 0.1479 0.1535 0.4114 -0.0153 -0.0283 -0.0426 197 GLU A CG 1516 C CD . GLU A 195 ? 0.2263 0.2286 0.4900 -0.0188 -0.0292 -0.0424 197 GLU A CD 1517 O OE1 . GLU A 195 ? 0.1858 0.1846 0.4478 -0.0197 -0.0304 -0.0441 197 GLU A OE1 1518 O OE2 . GLU A 195 ? 0.2078 0.2097 0.4718 -0.0210 -0.0288 -0.0405 197 GLU A OE2 1519 N N . SER A 196 ? 0.2064 0.2010 0.4675 -0.0132 -0.0273 -0.0454 198 SER A N 1520 C CA . SER A 196 ? 0.2138 0.2042 0.4763 -0.0126 -0.0278 -0.0459 198 SER A CA 1521 C C . SER A 196 ? 0.2154 0.2049 0.4784 -0.0111 -0.0262 -0.0489 198 SER A C 1522 O O . SER A 196 ? 0.2348 0.2280 0.4990 -0.0104 -0.0249 -0.0495 198 SER A O 1523 C CB . SER A 196 ? 0.2279 0.2140 0.4889 -0.0151 -0.0291 -0.0453 198 SER A CB 1524 O OG . SER A 196 ? 0.2585 0.2384 0.5193 -0.0142 -0.0302 -0.0445 198 SER A OG 1525 N N . ALA A 197 ? 0.1923 0.1772 0.4538 -0.0109 -0.0257 -0.0512 199 ALA A N 1526 C CA . ALA A 197 ? 0.1732 0.1588 0.4352 -0.0093 -0.0228 -0.0546 199 ALA A CA 1527 C C . ALA A 197 ? 0.1884 0.1763 0.4463 -0.0115 -0.0210 -0.0551 199 ALA A C 1528 O O . ALA A 197 ? 0.2051 0.1955 0.4634 -0.0115 -0.0179 -0.0571 199 ALA A O 1529 C CB . ALA A 197 ? 0.1871 0.1659 0.4466 -0.0083 -0.0220 -0.0577 199 ALA A CB 1530 N N . GLY A 198 ? 0.1858 0.1730 0.4398 -0.0134 -0.0229 -0.0532 200 GLY A N 1531 C CA . GLY A 198 ? 0.1752 0.1621 0.4237 -0.0147 -0.0223 -0.0530 200 GLY A CA 1532 C C . GLY A 198 ? 0.1812 0.1709 0.4314 -0.0144 -0.0213 -0.0518 200 GLY A C 1533 O O . GLY A 198 ? 0.1654 0.1537 0.4114 -0.0159 -0.0193 -0.0523 200 GLY A O 1534 N N . ALA A 199 ? 0.1791 0.1716 0.4340 -0.0132 -0.0227 -0.0502 201 ALA A N 1535 C CA . ALA A 199 ? 0.1860 0.1804 0.4420 -0.0133 -0.0223 -0.0494 201 ALA A CA 1536 C C . ALA A 199 ? 0.1956 0.1936 0.4561 -0.0138 -0.0205 -0.0512 201 ALA A C 1537 O O . ALA A 199 ? 0.2039 0.2030 0.4633 -0.0160 -0.0191 -0.0517 201 ALA A O 1538 C CB . ALA A 199 ? 0.1585 0.1545 0.4166 -0.0121 -0.0243 -0.0474 201 ALA A CB 1539 N N . ALA A 200 ? 0.1886 0.1885 0.4543 -0.0118 -0.0206 -0.0524 202 ALA A N 1540 C CA . ALA A 200 ? 0.1929 0.1988 0.4651 -0.0111 -0.0187 -0.0546 202 ALA A CA 1541 C C . ALA A 200 ? 0.1970 0.2039 0.4663 -0.0139 -0.0144 -0.0571 202 ALA A C 1542 O O . ALA A 200 ? 0.2258 0.2385 0.4981 -0.0164 -0.0122 -0.0581 202 ALA A O 1543 C CB . ALA A 200 ? 0.1715 0.1775 0.4491 -0.0070 -0.0197 -0.0558 202 ALA A CB 1544 N N . SER A 201 ? 0.1860 0.1868 0.4482 -0.0145 -0.0132 -0.0578 203 SER A N 1545 C CA . SER A 201 ? 0.2109 0.2097 0.4663 -0.0177 -0.0093 -0.0595 203 SER A CA 1546 C C . SER A 201 ? 0.2115 0.2084 0.4612 -0.0217 -0.0089 -0.0575 203 SER A C 1547 O O . SER A 201 ? 0.2454 0.2449 0.4940 -0.0255 -0.0050 -0.0588 203 SER A O 1548 C CB . SER A 201 ? 0.2033 0.1944 0.4500 -0.0178 -0.0104 -0.0595 203 SER A CB 1549 O OG . SER A 201 ? 0.2608 0.2508 0.5097 -0.0152 -0.0100 -0.0622 203 SER A OG 1550 N N . VAL A 202 ? 0.2061 0.1983 0.4522 -0.0211 -0.0127 -0.0546 204 VAL A N 1551 C CA . VAL A 202 ? 0.1952 0.1827 0.4347 -0.0240 -0.0128 -0.0528 204 VAL A CA 1552 C C . VAL A 202 ? 0.1973 0.1909 0.4427 -0.0269 -0.0112 -0.0537 204 VAL A C 1553 O O . VAL A 202 ? 0.1922 0.1846 0.4334 -0.0320 -0.0084 -0.0541 204 VAL A O 1554 C CB . VAL A 202 ? 0.2068 0.1897 0.4436 -0.0211 -0.0169 -0.0503 204 VAL A CB 1555 C CG1 . VAL A 202 ? 0.1707 0.1478 0.4015 -0.0235 -0.0170 -0.0492 204 VAL A CG1 1556 C CG2 . VAL A 202 ? 0.1883 0.1664 0.4192 -0.0191 -0.0190 -0.0492 204 VAL A CG2 1557 N N . SER A 203 ? 0.1882 0.1893 0.4435 -0.0243 -0.0131 -0.0542 205 SER A N 1558 C CA . SER A 203 ? 0.1882 0.1968 0.4500 -0.0271 -0.0128 -0.0551 205 SER A CA 1559 C C . SER A 203 ? 0.1847 0.2018 0.4518 -0.0302 -0.0080 -0.0579 205 SER A C 1560 O O . SER A 203 ? 0.2052 0.2268 0.4738 -0.0357 -0.0064 -0.0586 205 SER A O 1561 C CB . SER A 203 ? 0.1703 0.1841 0.4400 -0.0233 -0.0168 -0.0544 205 SER A CB 1562 O OG . SER A 203 ? 0.1800 0.1999 0.4580 -0.0192 -0.0166 -0.0558 205 SER A OG 1563 N N . LEU A 204 ? 0.1798 0.1985 0.4485 -0.0276 -0.0053 -0.0598 206 LEU A N 1564 C CA . LEU A 204 ? 0.1858 0.2141 0.4601 -0.0298 0.0004 -0.0633 206 LEU A CA 1565 C C . LEU A 204 ? 0.1990 0.2213 0.4616 -0.0371 0.0050 -0.0631 206 LEU A C 1566 O O . LEU A 204 ? 0.1982 0.2290 0.4646 -0.0419 0.0099 -0.0651 206 LEU A O 1567 C CB . LEU A 204 ? 0.1872 0.2169 0.4651 -0.0241 0.0021 -0.0660 206 LEU A CB 1568 C CG . LEU A 204 ? 0.1918 0.2281 0.4822 -0.0171 -0.0016 -0.0666 206 LEU A CG 1569 C CD1 . LEU A 204 ? 0.1877 0.2205 0.4782 -0.0116 -0.0003 -0.0692 206 LEU A CD1 1570 C CD2 . LEU A 204 ? 0.1234 0.1762 0.4283 -0.0175 -0.0010 -0.0684 206 LEU A CD2 1571 N N . HIS A 205 ? 0.1916 0.1997 0.4402 -0.0376 0.0033 -0.0605 207 HIS A N 1572 C CA . HIS A 205 ? 0.2219 0.2207 0.4567 -0.0442 0.0059 -0.0590 207 HIS A CA 1573 C C . HIS A 205 ? 0.2361 0.2344 0.4703 -0.0501 0.0054 -0.0577 207 HIS A C 1574 O O . HIS A 205 ? 0.2753 0.2713 0.5027 -0.0577 0.0095 -0.0576 207 HIS A O 1575 C CB . HIS A 205 ? 0.2101 0.1937 0.4305 -0.0422 0.0025 -0.0561 207 HIS A CB 1576 C CG . HIS A 205 ? 0.2360 0.2185 0.4536 -0.0391 0.0033 -0.0577 207 HIS A CG 1577 N ND1 . HIS A 205 ? 0.2519 0.2329 0.4614 -0.0430 0.0087 -0.0596 207 HIS A ND1 1578 C CD2 . HIS A 205 ? 0.1989 0.1809 0.4194 -0.0333 -0.0005 -0.0579 207 HIS A CD2 1579 C CE1 . HIS A 205 ? 0.1917 0.1705 0.3988 -0.0393 0.0078 -0.0611 207 HIS A CE1 1580 N NE2 . HIS A 205 ? 0.1728 0.1525 0.3871 -0.0337 0.0022 -0.0602 207 HIS A NE2 1581 N N . LEU A 206 ? 0.2395 0.2389 0.4793 -0.0476 0.0006 -0.0567 208 LEU A N 1582 C CA . LEU A 206 ? 0.2506 0.2504 0.4902 -0.0540 0.0000 -0.0563 208 LEU A CA 1583 C C . LEU A 206 ? 0.2544 0.2710 0.5062 -0.0594 0.0042 -0.0592 208 LEU A C 1584 O O . LEU A 206 ? 0.2782 0.2956 0.5282 -0.0678 0.0057 -0.0594 208 LEU A O 1585 C CB . LEU A 206 ? 0.2305 0.2295 0.4738 -0.0499 -0.0058 -0.0553 208 LEU A CB 1586 C CG . LEU A 206 ? 0.2617 0.2452 0.4934 -0.0456 -0.0094 -0.0527 208 LEU A CG 1587 C CD1 . LEU A 206 ? 0.1637 0.1496 0.4006 -0.0404 -0.0139 -0.0524 208 LEU A CD1 1588 C CD2 . LEU A 206 ? 0.1714 0.1393 0.3882 -0.0511 -0.0092 -0.0512 208 LEU A CD2 1589 N N . LEU A 207 ? 0.2655 0.2959 0.5302 -0.0545 0.0060 -0.0619 209 LEU A N 1590 C CA . LEU A 207 ? 0.2584 0.3077 0.5374 -0.0579 0.0099 -0.0652 209 LEU A CA 1591 C C . LEU A 207 ? 0.2685 0.3211 0.5444 -0.0627 0.0182 -0.0673 209 LEU A C 1592 O O . LEU A 207 ? 0.2783 0.3457 0.5635 -0.0682 0.0228 -0.0698 209 LEU A O 1593 C CB . LEU A 207 ? 0.2464 0.3098 0.5425 -0.0490 0.0071 -0.0672 209 LEU A CB 1594 C CG . LEU A 207 ? 0.2504 0.3210 0.5561 -0.0476 0.0004 -0.0664 209 LEU A CG 1595 C CD1 . LEU A 207 ? 0.2766 0.3328 0.5707 -0.0496 -0.0049 -0.0631 209 LEU A CD1 1596 C CD2 . LEU A 207 ? 0.2314 0.3073 0.5470 -0.0370 -0.0030 -0.0670 209 LEU A CD2 1597 N N . SER A 208 ? 0.2803 0.3204 0.5432 -0.0607 0.0203 -0.0666 210 SER A N 1598 C CA . SER A 208 ? 0.3124 0.3569 0.5724 -0.0644 0.0287 -0.0694 210 SER A CA 1599 C C . SER A 208 ? 0.3441 0.3796 0.5891 -0.0758 0.0329 -0.0674 210 SER A C 1600 O O . SER A 208 ? 0.3449 0.3608 0.5725 -0.0777 0.0295 -0.0634 210 SER A O 1601 C CB . SER A 208 ? 0.3281 0.3625 0.5789 -0.0581 0.0289 -0.0698 210 SER A CB 1602 O OG . SER A 208 ? 0.3378 0.3786 0.5872 -0.0608 0.0375 -0.0736 210 SER A OG 1603 N N . PRO A 209 ? 0.3716 0.4209 0.6224 -0.0836 0.0406 -0.0702 211 PRO A N 1604 C CA . PRO A 209 ? 0.3889 0.4270 0.6231 -0.0962 0.0446 -0.0675 211 PRO A CA 1605 C C . PRO A 209 ? 0.3921 0.4104 0.6030 -0.0975 0.0470 -0.0653 211 PRO A C 1606 O O . PRO A 209 ? 0.4316 0.4301 0.6236 -0.1033 0.0448 -0.0608 211 PRO A O 1607 C CB . PRO A 209 ? 0.4011 0.4620 0.6493 -0.1048 0.0528 -0.0714 211 PRO A CB 1608 C CG . PRO A 209 ? 0.4179 0.4994 0.6858 -0.0952 0.0555 -0.0766 211 PRO A CG 1609 C CD . PRO A 209 ? 0.3817 0.4564 0.6536 -0.0819 0.0460 -0.0755 211 PRO A CD 1610 N N . GLY A 210 ? 0.3736 0.3945 0.5842 -0.0913 0.0501 -0.0681 212 GLY A N 1611 C CA . GLY A 210 ? 0.3638 0.3657 0.5520 -0.0919 0.0506 -0.0658 212 GLY A CA 1612 C C . GLY A 210 ? 0.3709 0.3535 0.5482 -0.0854 0.0404 -0.0612 212 GLY A C 1613 O O . GLY A 210 ? 0.3864 0.3524 0.5444 -0.0863 0.0390 -0.0584 212 GLY A O 1614 N N . SER A 211 ? 0.3324 0.3179 0.5218 -0.0788 0.0331 -0.0603 213 SER A N 1615 C CA . SER A 211 ? 0.3280 0.2966 0.5075 -0.0738 0.0245 -0.0560 213 SER A CA 1616 C C . SER A 211 ? 0.3317 0.2882 0.5029 -0.0786 0.0211 -0.0522 213 SER A C 1617 O O . SER A 211 ? 0.3439 0.2851 0.5045 -0.0749 0.0151 -0.0487 213 SER A O 1618 C CB . SER A 211 ? 0.2996 0.2751 0.4933 -0.0633 0.0186 -0.0571 213 SER A CB 1619 O OG . SER A 211 ? 0.3083 0.2897 0.5056 -0.0589 0.0209 -0.0603 213 SER A OG 1620 N N . HIS A 212 ? 0.3426 0.3061 0.5191 -0.0868 0.0248 -0.0531 214 HIS A N 1621 C CA . HIS A 212 ? 0.3651 0.3167 0.5346 -0.0917 0.0213 -0.0502 214 HIS A CA 1622 C C . HIS A 212 ? 0.3727 0.2980 0.5175 -0.0935 0.0185 -0.0454 214 HIS A C 1623 O O . HIS A 212 ? 0.3801 0.2919 0.5188 -0.0896 0.0123 -0.0429 214 HIS A O 1624 C CB . HIS A 212 ? 0.3752 0.3398 0.5536 -0.1026 0.0264 -0.0523 214 HIS A CB 1625 C CG . HIS A 212 ? 0.4472 0.3978 0.6161 -0.1100 0.0234 -0.0499 214 HIS A CG 1626 N ND1 . HIS A 212 ? 0.4770 0.4381 0.6590 -0.1122 0.0209 -0.0518 214 HIS A ND1 1627 C CD2 . HIS A 212 ? 0.5105 0.4370 0.6570 -0.1167 0.0228 -0.0460 214 HIS A CD2 1628 C CE1 . HIS A 212 ? 0.4249 0.3684 0.5929 -0.1198 0.0190 -0.0496 214 HIS A CE1 1629 N NE2 . HIS A 212 ? 0.4746 0.3962 0.6209 -0.1224 0.0201 -0.0460 214 HIS A NE2 1630 N N . SER A 213 ? 0.3804 0.2976 0.5103 -0.0979 0.0226 -0.0440 215 SER A N 1631 C CA . SER A 213 ? 0.3997 0.2904 0.5051 -0.0998 0.0190 -0.0388 215 SER A CA 1632 C C . SER A 213 ? 0.4037 0.2853 0.5016 -0.0894 0.0128 -0.0368 215 SER A C 1633 O O . SER A 213 ? 0.4274 0.2873 0.5042 -0.0900 0.0094 -0.0323 215 SER A O 1634 C CB . SER A 213 ? 0.4444 0.3276 0.5329 -0.1122 0.0265 -0.0374 215 SER A CB 1635 O OG . SER A 213 ? 0.5173 0.4087 0.6054 -0.1100 0.0305 -0.0395 215 SER A OG 1636 N N . LEU A 214 ? 0.3642 0.2613 0.4784 -0.0803 0.0109 -0.0398 216 LEU A N 1637 C CA . LEU A 214 ? 0.3460 0.2378 0.4552 -0.0717 0.0053 -0.0385 216 LEU A CA 1638 C C . LEU A 214 ? 0.3390 0.2280 0.4545 -0.0621 -0.0029 -0.0371 216 LEU A C 1639 O O . LEU A 214 ? 0.3322 0.2202 0.4472 -0.0546 -0.0082 -0.0362 216 LEU A O 1640 C CB . LEU A 214 ? 0.2987 0.2064 0.4187 -0.0687 0.0082 -0.0426 216 LEU A CB 1641 C CG . LEU A 214 ? 0.3686 0.2825 0.4850 -0.0771 0.0177 -0.0454 216 LEU A CG 1642 C CD1 . LEU A 214 ? 0.3039 0.2312 0.4292 -0.0729 0.0207 -0.0503 216 LEU A CD1 1643 C CD2 . LEU A 214 ? 0.3403 0.2352 0.4311 -0.0847 0.0192 -0.0414 216 LEU A CD2 1644 N N . PHE A 215 ? 0.3230 0.2119 0.4447 -0.0624 -0.0037 -0.0372 217 PHE A N 1645 C CA . PHE A 215 ? 0.3099 0.1966 0.4372 -0.0529 -0.0105 -0.0364 217 PHE A CA 1646 C C . PHE A 215 ? 0.3110 0.1907 0.4373 -0.0554 -0.0109 -0.0362 217 PHE A C 1647 O O . PHE A 215 ? 0.3341 0.2156 0.4603 -0.0646 -0.0062 -0.0373 217 PHE A O 1648 C CB . PHE A 215 ? 0.2703 0.1759 0.4170 -0.0459 -0.0117 -0.0394 217 PHE A CB 1649 C CG . PHE A 215 ? 0.2725 0.1941 0.4358 -0.0486 -0.0079 -0.0428 217 PHE A CG 1650 C CD1 . PHE A 215 ? 0.2460 0.1787 0.4149 -0.0546 -0.0018 -0.0454 217 PHE A CD1 1651 C CD2 . PHE A 215 ? 0.2461 0.1725 0.4194 -0.0444 -0.0107 -0.0436 217 PHE A CD2 1652 C CE1 . PHE A 215 ? 0.2460 0.1944 0.4312 -0.0558 0.0006 -0.0484 217 PHE A CE1 1653 C CE2 . PHE A 215 ? 0.2470 0.1878 0.4346 -0.0465 -0.0085 -0.0463 217 PHE A CE2 1654 C CZ . PHE A 215 ? 0.2362 0.1880 0.4300 -0.0519 -0.0033 -0.0486 217 PHE A CZ 1655 N N . THR A 216 ? 0.3160 0.1881 0.4414 -0.0475 -0.0164 -0.0352 218 THR A N 1656 C CA . THR A 216 ? 0.3361 0.1987 0.4581 -0.0487 -0.0173 -0.0354 218 THR A CA 1657 C C . THR A 216 ? 0.3269 0.2047 0.4662 -0.0449 -0.0177 -0.0387 218 THR A C 1658 O O . THR A 216 ? 0.3187 0.1986 0.4610 -0.0507 -0.0159 -0.0405 218 THR A O 1659 C CB . THR A 216 ? 0.3794 0.2229 0.4886 -0.0406 -0.0230 -0.0327 218 THR A CB 1660 O OG1 . THR A 216 ? 0.4201 0.2505 0.5137 -0.0413 -0.0245 -0.0290 218 THR A OG1 1661 C CG2 . THR A 216 ? 0.3318 0.1579 0.4311 -0.0430 -0.0237 -0.0330 218 THR A CG2 1662 N N . ARG A 217 ? 0.3100 0.1979 0.4597 -0.0357 -0.0205 -0.0393 219 ARG A N 1663 C CA . ARG A 217 ? 0.2863 0.1873 0.4500 -0.0334 -0.0204 -0.0420 219 ARG A CA 1664 C C . ARG A 217 ? 0.2773 0.1953 0.4555 -0.0281 -0.0209 -0.0429 219 ARG A C 1665 O O . ARG A 217 ? 0.2745 0.1949 0.4523 -0.0269 -0.0211 -0.0420 219 ARG A O 1666 C CB . ARG A 217 ? 0.3062 0.1961 0.4644 -0.0297 -0.0227 -0.0425 219 ARG A CB 1667 C CG . ARG A 217 ? 0.3102 0.1900 0.4621 -0.0205 -0.0262 -0.0412 219 ARG A CG 1668 C CD . ARG A 217 ? 0.3801 0.2431 0.5215 -0.0190 -0.0273 -0.0424 219 ARG A CD 1669 N NE . ARG A 217 ? 0.3748 0.2211 0.5036 -0.0135 -0.0303 -0.0399 219 ARG A NE 1670 C CZ . ARG A 217 ? 0.4183 0.2421 0.5295 -0.0165 -0.0312 -0.0382 219 ARG A CZ 1671 N NH1 . ARG A 217 ? 0.3779 0.1892 0.4794 -0.0098 -0.0350 -0.0352 219 ARG A NH1 1672 N NH2 . ARG A 217 ? 0.3809 0.1946 0.4841 -0.0260 -0.0291 -0.0393 219 ARG A NH2 1673 N N . ALA A 218 ? 0.2570 0.1854 0.4462 -0.0257 -0.0212 -0.0447 220 ALA A N 1674 C CA . ALA A 218 ? 0.2423 0.1860 0.4446 -0.0229 -0.0211 -0.0456 220 ALA A CA 1675 C C . ALA A 218 ? 0.2284 0.1778 0.4375 -0.0175 -0.0228 -0.0461 220 ALA A C 1676 O O . ALA A 218 ? 0.2147 0.1608 0.4217 -0.0177 -0.0231 -0.0470 220 ALA A O 1677 C CB . ALA A 218 ? 0.2255 0.1795 0.4357 -0.0284 -0.0183 -0.0472 220 ALA A CB 1678 N N . ILE A 219 ? 0.2148 0.1723 0.4307 -0.0136 -0.0237 -0.0457 221 ILE A N 1679 C CA . ILE A 219 ? 0.2062 0.1712 0.4293 -0.0094 -0.0246 -0.0459 221 ILE A CA 1680 C C . ILE A 219 ? 0.2087 0.1844 0.4415 -0.0109 -0.0241 -0.0462 221 ILE A C 1681 O O . ILE A 219 ? 0.2162 0.1941 0.4506 -0.0115 -0.0241 -0.0461 221 ILE A O 1682 C CB . ILE A 219 ? 0.2103 0.1752 0.4329 -0.0036 -0.0266 -0.0450 221 ILE A CB 1683 C CG1 . ILE A 219 ? 0.1960 0.1482 0.4083 -0.0004 -0.0277 -0.0446 221 ILE A CG1 1684 C CG2 . ILE A 219 ? 0.1597 0.1354 0.3913 -0.0003 -0.0264 -0.0453 221 ILE A CG2 1685 C CD1 . ILE A 219 ? 0.1870 0.1406 0.4003 0.0072 -0.0304 -0.0439 221 ILE A CD1 1686 N N . LEU A 220 ? 0.1937 0.1744 0.4313 -0.0112 -0.0240 -0.0466 222 LEU A N 1687 C CA . LEU A 220 ? 0.2028 0.1910 0.4481 -0.0120 -0.0241 -0.0465 222 LEU A CA 1688 C C . LEU A 220 ? 0.1985 0.1907 0.4469 -0.0100 -0.0248 -0.0455 222 LEU A C 1689 O O . LEU A 220 ? 0.1956 0.1879 0.4427 -0.0099 -0.0248 -0.0453 222 LEU A O 1690 C CB . LEU A 220 ? 0.1808 0.1714 0.4288 -0.0147 -0.0240 -0.0473 222 LEU A CB 1691 C CG . LEU A 220 ? 0.2092 0.1996 0.4570 -0.0181 -0.0224 -0.0486 222 LEU A CG 1692 C CD1 . LEU A 220 ? 0.2531 0.2343 0.4912 -0.0204 -0.0217 -0.0486 222 LEU A CD1 1693 C CD2 . LEU A 220 ? 0.1927 0.1899 0.4471 -0.0199 -0.0230 -0.0495 222 LEU A CD2 1694 N N . GLN A 221 ? 0.1929 0.1881 0.4443 -0.0091 -0.0251 -0.0448 223 GLN A N 1695 C CA . GLN A 221 ? 0.1743 0.1741 0.4289 -0.0087 -0.0252 -0.0437 223 GLN A CA 1696 C C . GLN A 221 ? 0.1816 0.1821 0.4393 -0.0107 -0.0259 -0.0429 223 GLN A C 1697 O O . GLN A 221 ? 0.1656 0.1652 0.4251 -0.0115 -0.0264 -0.0434 223 GLN A O 1698 C CB . GLN A 221 ? 0.1778 0.1813 0.4343 -0.0075 -0.0257 -0.0435 223 GLN A CB 1699 C CG . GLN A 221 ? 0.1751 0.1769 0.4283 -0.0037 -0.0257 -0.0440 223 GLN A CG 1700 C CD . GLN A 221 ? 0.1803 0.1865 0.4360 -0.0015 -0.0276 -0.0438 223 GLN A CD 1701 O OE1 . GLN A 221 ? 0.2610 0.2633 0.5129 0.0017 -0.0289 -0.0440 223 GLN A OE1 1702 N NE2 . GLN A 221 ? 0.1966 0.2105 0.4582 -0.0034 -0.0282 -0.0433 223 GLN A NE2 1703 N N . SER A 222 ? 0.1842 0.1845 0.4409 -0.0111 -0.0261 -0.0418 224 SER A N 1704 C CA . SER A 222 ? 0.1828 0.1817 0.4412 -0.0122 -0.0275 -0.0404 224 SER A CA 1705 C C . SER A 222 ? 0.2036 0.2007 0.4650 -0.0114 -0.0285 -0.0418 224 SER A C 1706 O O . SER A 222 ? 0.1884 0.1829 0.4511 -0.0116 -0.0289 -0.0419 224 SER A O 1707 C CB . SER A 222 ? 0.1622 0.1616 0.4212 -0.0142 -0.0273 -0.0390 224 SER A CB 1708 O OG . SER A 222 ? 0.1930 0.1966 0.4507 -0.0152 -0.0254 -0.0379 224 SER A OG 1709 N N . GLY A 223 ? 0.1844 0.1829 0.4469 -0.0107 -0.0284 -0.0433 225 GLY A N 1710 C CA . GLY A 223 ? 0.1805 0.1799 0.4474 -0.0096 -0.0284 -0.0451 225 GLY A CA 1711 C C . GLY A 223 ? 0.1893 0.1925 0.4578 -0.0105 -0.0276 -0.0467 225 GLY A C 1712 O O . GLY A 223 ? 0.2038 0.2059 0.4679 -0.0124 -0.0266 -0.0469 225 GLY A O 1713 N N . SER A 224 ? 0.1693 0.1768 0.4439 -0.0093 -0.0280 -0.0481 226 SER A N 1714 C CA . SER A 224 ? 0.1890 0.2024 0.4669 -0.0114 -0.0266 -0.0501 226 SER A CA 1715 C C . SER A 224 ? 0.1948 0.2146 0.4818 -0.0085 -0.0265 -0.0520 226 SER A C 1716 O O . SER A 224 ? 0.1913 0.2090 0.4804 -0.0045 -0.0290 -0.0510 226 SER A O 1717 C CB . SER A 224 ? 0.1915 0.2070 0.4685 -0.0133 -0.0295 -0.0490 226 SER A CB 1718 O OG . SER A 224 ? 0.1678 0.1835 0.4463 -0.0105 -0.0336 -0.0470 226 SER A OG 1719 N N . PHE A 225 ? 0.1967 0.2242 0.4890 -0.0102 -0.0237 -0.0547 227 PHE A N 1720 C CA . PHE A 225 ? 0.2029 0.2372 0.5044 -0.0063 -0.0220 -0.0575 227 PHE A CA 1721 C C . PHE A 225 ? 0.2152 0.2570 0.5261 -0.0021 -0.0268 -0.0569 227 PHE A C 1722 O O . PHE A 225 ? 0.2364 0.2828 0.5553 0.0031 -0.0267 -0.0590 227 PHE A O 1723 C CB . PHE A 225 ? 0.2237 0.2663 0.5287 -0.0101 -0.0168 -0.0607 227 PHE A CB 1724 C CG . PHE A 225 ? 0.2573 0.3106 0.5688 -0.0141 -0.0182 -0.0608 227 PHE A CG 1725 C CD1 . PHE A 225 ? 0.3421 0.4071 0.6660 -0.0104 -0.0216 -0.0616 227 PHE A CD1 1726 C CD2 . PHE A 225 ? 0.3037 0.3539 0.6079 -0.0212 -0.0171 -0.0600 227 PHE A CD2 1727 C CE1 . PHE A 225 ? 0.3816 0.4570 0.7111 -0.0150 -0.0241 -0.0617 227 PHE A CE1 1728 C CE2 . PHE A 225 ? 0.3434 0.4012 0.6516 -0.0259 -0.0190 -0.0602 227 PHE A CE2 1729 C CZ . PHE A 225 ? 0.3509 0.4220 0.6720 -0.0233 -0.0225 -0.0611 227 PHE A CZ 1730 N N . ASN A 226 ? 0.2061 0.2493 0.5158 -0.0042 -0.0313 -0.0545 228 ASN A N 1731 C CA . ASN A 226 ? 0.1959 0.2458 0.5134 -0.0003 -0.0371 -0.0536 228 ASN A CA 1732 C C . ASN A 226 ? 0.2129 0.2518 0.5247 0.0046 -0.0413 -0.0502 228 ASN A C 1733 O O . ASN A 226 ? 0.2216 0.2625 0.5366 0.0082 -0.0471 -0.0484 228 ASN A O 1734 C CB . ASN A 226 ? 0.1841 0.2394 0.5011 -0.0052 -0.0406 -0.0526 228 ASN A CB 1735 C CG . ASN A 226 ? 0.2440 0.2869 0.5464 -0.0094 -0.0411 -0.0500 228 ASN A CG 1736 O OD1 . ASN A 226 ? 0.2396 0.2741 0.5344 -0.0109 -0.0370 -0.0499 228 ASN A OD1 1737 N ND2 . ASN A 226 ? 0.2090 0.2514 0.5078 -0.0105 -0.0462 -0.0481 228 ASN A ND2 1738 N N . ALA A 227 ? 0.2071 0.2342 0.5101 0.0040 -0.0388 -0.0492 229 ALA A N 1739 C CA . ALA A 227 ? 0.2070 0.2230 0.5041 0.0071 -0.0421 -0.0460 229 ALA A CA 1740 C C . ALA A 227 ? 0.2055 0.2212 0.5096 0.0143 -0.0435 -0.0475 229 ALA A C 1741 O O . ALA A 227 ? 0.1879 0.2091 0.4986 0.0162 -0.0395 -0.0515 229 ALA A O 1742 C CB . ALA A 227 ? 0.1797 0.1861 0.4679 0.0039 -0.0385 -0.0454 229 ALA A CB 1743 N N . PRO A 228 ? 0.2254 0.2335 0.5270 0.0186 -0.0489 -0.0444 230 PRO A N 1744 C CA . PRO A 228 ? 0.2261 0.2344 0.5356 0.0271 -0.0507 -0.0464 230 PRO A CA 1745 C C . PRO A 228 ? 0.2337 0.2337 0.5416 0.0293 -0.0458 -0.0498 230 PRO A C 1746 O O . PRO A 228 ? 0.2497 0.2518 0.5653 0.0367 -0.0453 -0.0533 230 PRO A O 1747 C CB . PRO A 228 ? 0.2415 0.2400 0.5455 0.0309 -0.0583 -0.0414 230 PRO A CB 1748 C CG . PRO A 228 ? 0.2512 0.2396 0.5410 0.0232 -0.0582 -0.0371 230 PRO A CG 1749 C CD . PRO A 228 ? 0.2257 0.2230 0.5161 0.0164 -0.0529 -0.0392 230 PRO A CD 1750 N N . TRP A 229 ? 0.2205 0.2124 0.5191 0.0233 -0.0421 -0.0496 231 TRP A N 1751 C CA . TRP A 229 ? 0.2241 0.2079 0.5198 0.0244 -0.0382 -0.0530 231 TRP A CA 1752 C C . TRP A 229 ? 0.2120 0.2056 0.5115 0.0218 -0.0318 -0.0576 231 TRP A C 1753 O O . TRP A 229 ? 0.2295 0.2174 0.5254 0.0218 -0.0282 -0.0609 231 TRP A O 1754 C CB . TRP A 229 ? 0.2107 0.1804 0.4940 0.0187 -0.0384 -0.0502 231 TRP A CB 1755 C CG . TRP A 229 ? 0.2313 0.2065 0.5111 0.0113 -0.0378 -0.0473 231 TRP A CG 1756 C CD1 . TRP A 229 ? 0.2616 0.2360 0.5378 0.0091 -0.0411 -0.0427 231 TRP A CD1 1757 C CD2 . TRP A 229 ? 0.1996 0.1811 0.4787 0.0064 -0.0337 -0.0490 231 TRP A CD2 1758 N NE1 . TRP A 229 ? 0.2586 0.2384 0.5323 0.0035 -0.0388 -0.0421 231 TRP A NE1 1759 C CE2 . TRP A 229 ? 0.2195 0.2034 0.4952 0.0021 -0.0347 -0.0456 231 TRP A CE2 1760 C CE3 . TRP A 229 ? 0.2011 0.1847 0.4804 0.0052 -0.0294 -0.0529 231 TRP A CE3 1761 C CZ2 . TRP A 229 ? 0.2150 0.2034 0.4886 -0.0022 -0.0320 -0.0460 231 TRP A CZ2 1762 C CZ3 . TRP A 229 ? 0.1531 0.1411 0.4293 0.0001 -0.0271 -0.0527 231 TRP A CZ3 1763 C CH2 . TRP A 229 ? 0.1527 0.1428 0.4267 -0.0029 -0.0287 -0.0493 231 TRP A CH2 1764 N N . ALA A 230 ? 0.2243 0.2311 0.5291 0.0187 -0.0303 -0.0580 232 ALA A N 1765 C CA . ALA A 230 ? 0.2193 0.2300 0.5218 0.0137 -0.0244 -0.0608 232 ALA A CA 1766 C C . ALA A 230 ? 0.2310 0.2512 0.5414 0.0163 -0.0194 -0.0660 232 ALA A C 1767 O O . ALA A 230 ? 0.2277 0.2464 0.5332 0.0133 -0.0143 -0.0687 232 ALA A O 1768 C CB . ALA A 230 ? 0.2004 0.2162 0.5005 0.0072 -0.0245 -0.0584 232 ALA A CB 1769 N N . VAL A 231 ? 0.2218 0.2522 0.5442 0.0222 -0.0208 -0.0675 233 VAL A N 1770 C CA . VAL A 231 ? 0.2666 0.3091 0.5981 0.0244 -0.0149 -0.0729 233 VAL A CA 1771 C C . VAL A 231 ? 0.3213 0.3646 0.6616 0.0352 -0.0160 -0.0760 233 VAL A C 1772 O O . VAL A 231 ? 0.3257 0.3706 0.6722 0.0407 -0.0225 -0.0735 233 VAL A O 1773 C CB . VAL A 231 ? 0.2635 0.3246 0.6050 0.0199 -0.0139 -0.0730 233 VAL A CB 1774 C CG1 . VAL A 231 ? 0.2323 0.3084 0.5844 0.0214 -0.0067 -0.0789 233 VAL A CG1 1775 C CG2 . VAL A 231 ? 0.2320 0.2891 0.5632 0.0100 -0.0132 -0.0700 233 VAL A CG2 1776 N N . THR A 232 ? 0.3645 0.4055 0.7040 0.0385 -0.0100 -0.0814 234 THR A N 1777 C CA . THR A 232 ? 0.4153 0.4561 0.7628 0.0501 -0.0100 -0.0855 234 THR A CA 1778 C C . THR A 232 ? 0.4256 0.4906 0.7922 0.0547 -0.0066 -0.0897 234 THR A C 1779 O O . THR A 232 ? 0.4279 0.5067 0.7982 0.0485 0.0004 -0.0925 234 THR A O 1780 C CB . THR A 232 ? 0.4374 0.4640 0.7746 0.0520 -0.0046 -0.0903 234 THR A CB 1781 O OG1 . THR A 232 ? 0.4695 0.4773 0.7896 0.0450 -0.0070 -0.0867 234 THR A OG1 1782 C CG2 . THR A 232 ? 0.4685 0.4880 0.8101 0.0646 -0.0062 -0.0937 234 THR A CG2 1783 N N . SER A 233 ? 0.4513 0.5225 0.8306 0.0651 -0.0118 -0.0899 235 SER A N 1784 C CA . SER A 233 ? 0.4569 0.5539 0.8572 0.0708 -0.0088 -0.0947 235 SER A CA 1785 C C . SER A 233 ? 0.4467 0.5474 0.8500 0.0758 0.0016 -0.1030 235 SER A C 1786 O O . SER A 233 ? 0.4535 0.5342 0.8439 0.0791 0.0037 -0.1052 235 SER A O 1787 C CB . SER A 233 ? 0.4661 0.5675 0.8787 0.0825 -0.0179 -0.0929 235 SER A CB 1788 O OG . SER A 233 ? 0.5190 0.6062 0.9293 0.0947 -0.0179 -0.0962 235 SER A OG 1789 N N . LEU A 234 ? 0.4473 0.5736 0.8667 0.0754 0.0084 -0.1079 236 LEU A N 1790 C CA . LEU A 234 ? 0.4649 0.5980 0.8893 0.0814 0.0190 -0.1165 236 LEU A CA 1791 C C . LEU A 234 ? 0.4720 0.5938 0.8988 0.0976 0.0164 -0.1201 236 LEU A C 1792 O O . LEU A 234 ? 0.4768 0.5820 0.8917 0.1012 0.0220 -0.1250 236 LEU A O 1793 C CB . LEU A 234 ? 0.4668 0.6339 0.9132 0.0800 0.0255 -0.1209 236 LEU A CB 1794 C CG . LEU A 234 ? 0.5042 0.6762 0.9417 0.0660 0.0364 -0.1229 236 LEU A CG 1795 C CD1 . LEU A 234 ? 0.4205 0.5650 0.8311 0.0551 0.0344 -0.1174 236 LEU A CD1 1796 C CD2 . LEU A 234 ? 0.5134 0.7158 0.9680 0.0571 0.0395 -0.1229 236 LEU A CD2 1797 N N . TYR A 235 ? 0.4680 0.5969 0.9088 0.1072 0.0071 -0.1175 237 TYR A N 1798 C CA . TYR A 235 ? 0.4841 0.5984 0.9256 0.1231 0.0020 -0.1191 237 TYR A CA 1799 C C . TYR A 235 ? 0.4867 0.5639 0.9024 0.1219 -0.0005 -0.1167 237 TYR A C 1800 O O . TYR A 235 ? 0.4960 0.5578 0.9047 0.1300 0.0038 -0.1225 237 TYR A O 1801 C CB . TYR A 235 ? 0.4873 0.6112 0.9438 0.1321 -0.0102 -0.1143 237 TYR A CB 1802 C CG . TYR A 235 ? 0.5492 0.6555 1.0051 0.1495 -0.0163 -0.1155 237 TYR A CG 1803 C CD1 . TYR A 235 ? 0.5876 0.6968 1.0515 0.1626 -0.0090 -0.1246 237 TYR A CD1 1804 C CD2 . TYR A 235 ? 0.5853 0.6702 1.0310 0.1528 -0.0288 -0.1077 237 TYR A CD2 1805 C CE1 . TYR A 235 ? 0.6425 0.7330 1.1043 0.1790 -0.0145 -0.1259 237 TYR A CE1 1806 C CE2 . TYR A 235 ? 0.6271 0.6926 1.0700 0.1686 -0.0345 -0.1084 237 TYR A CE2 1807 C CZ . TYR A 235 ? 0.6574 0.7253 1.1084 0.1819 -0.0275 -0.1176 237 TYR A CZ 1808 O OH . TYR A 235 ? 0.7152 0.7621 1.1628 0.1986 -0.0331 -0.1188 237 TYR A OH 1809 N N A GLU A 236 ? 0.4738 0.5365 0.8755 0.1119 -0.0071 -0.1087 238 GLU A N 1810 N N B GLU A 236 ? 0.4658 0.5291 0.8678 0.1117 -0.0071 -0.1086 238 GLU A N 1811 C CA A GLU A 236 ? 0.4871 0.5172 0.8666 0.1105 -0.0097 -0.1066 238 GLU A CA 1812 C CA B GLU A 236 ? 0.4707 0.5018 0.8498 0.1085 -0.0101 -0.1056 238 GLU A CA 1813 C C A GLU A 236 ? 0.4748 0.4949 0.8397 0.1030 -0.0001 -0.1116 238 GLU A C 1814 C C B GLU A 236 ? 0.4662 0.4873 0.8319 0.1031 -0.0002 -0.1115 238 GLU A C 1815 O O A GLU A 236 ? 0.4845 0.4812 0.8356 0.1065 0.0005 -0.1142 238 GLU A O 1816 O O B GLU A 236 ? 0.4770 0.4754 0.8301 0.1078 0.0004 -0.1144 238 GLU A O 1817 C CB A GLU A 236 ? 0.4891 0.5061 0.8579 0.1030 -0.0193 -0.0971 238 GLU A CB 1818 C CB B GLU A 236 ? 0.4591 0.4826 0.8278 0.0969 -0.0170 -0.0966 238 GLU A CB 1819 C CG A GLU A 236 ? 0.5388 0.5413 0.9069 0.1137 -0.0295 -0.0930 238 GLU A CG 1820 C CG B GLU A 236 ? 0.4573 0.4833 0.8325 0.1012 -0.0280 -0.0899 238 GLU A CG 1821 C CD A GLU A 236 ? 0.6187 0.5874 0.9665 0.1150 -0.0314 -0.0924 238 GLU A CD 1822 C CD B GLU A 236 ? 0.4527 0.4730 0.8170 0.0888 -0.0329 -0.0820 238 GLU A CD 1823 O OE1 A GLU A 236 ? 0.6420 0.6010 0.9832 0.1167 -0.0243 -0.0990 238 GLU A OE1 1824 O OE1 B GLU A 236 ? 0.4394 0.4670 0.8005 0.0776 -0.0280 -0.0819 238 GLU A OE1 1825 O OE2 A GLU A 236 ? 0.6590 0.6102 0.9964 0.1135 -0.0398 -0.0852 238 GLU A OE2 1826 O OE2 B GLU A 236 ? 0.4582 0.4659 0.8163 0.0907 -0.0416 -0.0760 238 GLU A OE2 1827 N N . ALA A 237 ? 0.4535 0.4902 0.8205 0.0928 0.0070 -0.1129 239 ALA A N 1828 C CA . ALA A 237 ? 0.4537 0.4830 0.8071 0.0863 0.0162 -0.1179 239 ALA A CA 1829 C C . ALA A 237 ? 0.4745 0.5020 0.8299 0.0973 0.0240 -0.1276 239 ALA A C 1830 O O . ALA A 237 ? 0.4791 0.4830 0.8175 0.0983 0.0256 -0.1309 239 ALA A O 1831 C CB . ALA A 237 ? 0.4266 0.4748 0.7823 0.0741 0.0223 -0.1172 239 ALA A CB 1832 N N . ARG A 238 ? 0.4803 0.5323 0.8561 0.1056 0.0291 -0.1328 240 ARG A N 1833 C CA . ARG A 238 ? 0.5130 0.5630 0.8915 0.1182 0.0368 -0.1428 240 ARG A CA 1834 C C . ARG A 238 ? 0.5141 0.5351 0.8823 0.1289 0.0300 -0.1431 240 ARG A C 1835 O O . ARG A 238 ? 0.5310 0.5331 0.8847 0.1313 0.0349 -0.1491 240 ARG A O 1836 C CB . ARG A 238 ? 0.5252 0.6077 0.9308 0.1282 0.0425 -0.1488 240 ARG A CB 1837 C CG . ARG A 238 ? 0.5763 0.6884 0.9914 0.1162 0.0517 -0.1499 240 ARG A CG 1838 C CD . ARG A 238 ? 0.6177 0.7549 1.0483 0.1223 0.0653 -0.1604 240 ARG A CD 1839 N NE . ARG A 238 ? 0.6957 0.8352 1.1406 0.1420 0.0641 -0.1662 240 ARG A NE 1840 C CZ . ARG A 238 ? 0.7252 0.8583 1.1668 0.1524 0.0731 -0.1761 240 ARG A CZ 1841 N NH1 . ARG A 238 ? 0.7441 0.8688 1.1676 0.1439 0.0844 -0.1812 240 ARG A NH1 1842 N NH2 . ARG A 238 ? 0.6685 0.8024 1.1237 0.1717 0.0706 -0.1808 240 ARG A NH2 1843 N N . ASN A 239 ? 0.5147 0.5302 0.8882 0.1344 0.0185 -0.1364 241 ASN A N 1844 C CA . ASN A 239 ? 0.5454 0.5319 0.9087 0.1448 0.0116 -0.1361 241 ASN A CA 1845 C C . ASN A 239 ? 0.5420 0.4968 0.8781 0.1351 0.0111 -0.1349 241 ASN A C 1846 O O . ASN A 239 ? 0.5545 0.4837 0.8778 0.1423 0.0115 -0.1395 241 ASN A O 1847 C CB . ASN A 239 ? 0.5644 0.5488 0.9346 0.1497 -0.0015 -0.1274 241 ASN A CB 1848 C CG . ASN A 239 ? 0.6657 0.6266 1.0325 0.1663 -0.0080 -0.1286 241 ASN A CG 1849 O OD1 . ASN A 239 ? 0.6427 0.6089 1.0201 0.1811 -0.0036 -0.1366 241 ASN A OD1 1850 N ND2 . ASN A 239 ? 0.8523 0.7871 1.2040 0.1635 -0.0181 -0.1206 241 ASN A ND2 1851 N N . ARG A 240 ? 0.4917 0.4481 0.8193 0.1191 0.0100 -0.1288 242 ARG A N 1852 C CA . ARG A 240 ? 0.4758 0.4064 0.7802 0.1086 0.0083 -0.1267 242 ARG A CA 1853 C C . ARG A 240 ? 0.4789 0.4032 0.7706 0.1050 0.0181 -0.1351 242 ARG A C 1854 O O . ARG A 240 ? 0.4828 0.3801 0.7561 0.1043 0.0174 -0.1379 242 ARG A O 1855 C CB . ARG A 240 ? 0.4576 0.3922 0.7584 0.0946 0.0029 -0.1174 242 ARG A CB 1856 C CG . ARG A 240 ? 0.4761 0.4091 0.7830 0.0977 -0.0073 -0.1094 242 ARG A CG 1857 C CD . ARG A 240 ? 0.4823 0.4239 0.7880 0.0849 -0.0108 -0.1015 242 ARG A CD 1858 N NE . ARG A 240 ? 0.4914 0.4373 0.8047 0.0872 -0.0194 -0.0942 242 ARG A NE 1859 C CZ . ARG A 240 ? 0.4725 0.4235 0.7840 0.0775 -0.0234 -0.0871 242 ARG A CZ 1860 N NH1 . ARG A 240 ? 0.3885 0.3413 0.6923 0.0654 -0.0202 -0.0859 242 ARG A NH1 1861 N NH2 . ARG A 240 ? 0.4543 0.4081 0.7712 0.0804 -0.0309 -0.0812 242 ARG A NH2 1862 N N . THR A 241 ? 0.4645 0.4125 0.7649 0.1023 0.0272 -0.1393 243 THR A N 1863 C CA . THR A 241 ? 0.4885 0.4329 0.7775 0.1002 0.0375 -0.1479 243 THR A CA 1864 C C . THR A 241 ? 0.5293 0.4580 0.8153 0.1148 0.0408 -0.1570 243 THR A C 1865 O O . THR A 241 ? 0.5477 0.4523 0.8134 0.1125 0.0426 -0.1614 243 THR A O 1866 C CB . THR A 241 ? 0.4799 0.4540 0.7815 0.0971 0.0471 -0.1509 243 THR A CB 1867 O OG1 . THR A 241 ? 0.4538 0.4376 0.7546 0.0835 0.0442 -0.1431 243 THR A OG1 1868 C CG2 . THR A 241 ? 0.5017 0.4736 0.7919 0.0964 0.0593 -0.1607 243 THR A CG2 1869 N N . LEU A 242 ? 0.5392 0.4796 0.8443 0.1298 0.0408 -0.1596 244 LEU A N 1870 C CA . LEU A 242 ? 0.5824 0.5067 0.8849 0.1455 0.0437 -0.1685 244 LEU A CA 1871 C C . LEU A 242 ? 0.6024 0.4902 0.8883 0.1488 0.0339 -0.1655 244 LEU A C 1872 O O . LEU A 242 ? 0.6245 0.4879 0.8961 0.1555 0.0366 -0.1730 244 LEU A O 1873 C CB . LEU A 242 ? 0.5904 0.5383 0.9195 0.1625 0.0458 -0.1724 244 LEU A CB 1874 C CG . LEU A 242 ? 0.6024 0.5906 0.9537 0.1597 0.0534 -0.1737 244 LEU A CG 1875 C CD1 . LEU A 242 ? 0.6193 0.6308 0.9994 0.1767 0.0511 -0.1753 244 LEU A CD1 1876 C CD2 . LEU A 242 ? 0.6313 0.6245 0.9737 0.1553 0.0681 -0.1833 244 LEU A CD2 1877 N N . ASN A 243 ? 0.5915 0.4748 0.8785 0.1440 0.0228 -0.1549 245 ASN A N 1878 C CA . ASN A 243 ? 0.6108 0.4587 0.8781 0.1415 0.0140 -0.1508 245 ASN A CA 1879 C C . ASN A 243 ? 0.6188 0.4463 0.8615 0.1276 0.0167 -0.1530 245 ASN A C 1880 O O . ASN A 243 ? 0.6644 0.4620 0.8897 0.1305 0.0159 -0.1576 245 ASN A O 1881 C CB . ASN A 243 ? 0.5926 0.4418 0.8647 0.1370 0.0029 -0.1389 245 ASN A CB 1882 C CG . ASN A 243 ? 0.6367 0.4897 0.9242 0.1532 -0.0031 -0.1371 245 ASN A CG 1883 O OD1 . ASN A 243 ? 0.6665 0.5151 0.9590 0.1690 -0.0002 -0.1447 245 ASN A OD1 1884 N ND2 . ASN A 243 ? 0.6331 0.4948 0.9284 0.1502 -0.0115 -0.1275 245 ASN A ND2 1885 N N . LEU A 244 ? 0.5854 0.4284 0.8265 0.1132 0.0196 -0.1503 246 LEU A N 1886 C CA . LEU A 244 ? 0.5891 0.4170 0.8086 0.1008 0.0223 -0.1532 246 LEU A CA 1887 C C . LEU A 244 ? 0.6160 0.4307 0.8238 0.1077 0.0312 -0.1656 246 LEU A C 1888 O O . LEU A 244 ? 0.6340 0.4202 0.8203 0.1035 0.0294 -0.1687 246 LEU A O 1889 C CB . LEU A 244 ? 0.5322 0.3815 0.7534 0.0870 0.0250 -0.1494 246 LEU A CB 1890 C CG . LEU A 244 ? 0.5517 0.3838 0.7503 0.0735 0.0240 -0.1498 246 LEU A CG 1891 C CD1 . LEU A 244 ? 0.4735 0.2807 0.6599 0.0673 0.0138 -0.1441 246 LEU A CD1 1892 C CD2 . LEU A 244 ? 0.4778 0.3310 0.6786 0.0614 0.0260 -0.1456 246 LEU A CD2 1893 N N . ALA A 245 ? 0.6060 0.4415 0.8278 0.1178 0.0407 -0.1726 247 ALA A N 1894 C CA . ALA A 245 ? 0.6365 0.4626 0.8489 0.1256 0.0508 -0.1851 247 ALA A CA 1895 C C . ALA A 245 ? 0.6745 0.4685 0.8768 0.1377 0.0469 -0.1897 247 ALA A C 1896 O O . ALA A 245 ? 0.7161 0.4835 0.8958 0.1353 0.0490 -0.1964 247 ALA A O 1897 C CB . ALA A 245 ? 0.6140 0.4718 0.8472 0.1352 0.0617 -0.1913 247 ALA A CB 1898 N N . LYS A 246 ? 0.6869 0.4828 0.9051 0.1507 0.0410 -0.1863 248 LYS A N 1899 C CA . LYS A 246 ? 0.7317 0.4957 0.9411 0.1631 0.0355 -0.1887 248 LYS A CA 1900 C C . LYS A 246 ? 0.7444 0.4729 0.9260 0.1495 0.0288 -0.1858 248 LYS A C 1901 O O . LYS A 246 ? 0.7693 0.4696 0.9309 0.1515 0.0314 -0.1939 248 LYS A O 1902 C CB . LYS A 246 ? 0.7350 0.5078 0.9641 0.1733 0.0265 -0.1807 248 LYS A CB 1903 C CG . LYS A 246 ? 0.8102 0.5571 1.0377 0.1920 0.0209 -0.1831 248 LYS A CG 1904 C CD . LYS A 246 ? 0.8825 0.6535 1.1370 0.2031 0.0139 -0.1756 248 LYS A CD 1905 C CE . LYS A 246 ? 0.9184 0.6638 1.1718 0.2211 0.0047 -0.1743 248 LYS A CE 1906 N NZ . LYS A 246 ? 0.9707 0.7020 1.2217 0.2398 0.0117 -0.1873 248 LYS A NZ 1907 N N . LEU A 247 ? 0.7190 0.4504 0.8989 0.1345 0.0209 -0.1748 249 LEU A N 1908 C CA . LEU A 247 ? 0.7218 0.4225 0.8777 0.1205 0.0139 -0.1712 249 LEU A CA 1909 C C . LEU A 247 ? 0.7313 0.4192 0.8655 0.1096 0.0191 -0.1786 249 LEU A C 1910 O O . LEU A 247 ? 0.7581 0.4143 0.8704 0.1027 0.0147 -0.1800 249 LEU A O 1911 C CB . LEU A 247 ? 0.6934 0.4051 0.8544 0.1068 0.0058 -0.1585 249 LEU A CB 1912 C CG . LEU A 247 ? 0.7019 0.4169 0.8769 0.1145 -0.0021 -0.1498 249 LEU A CG 1913 C CD1 . LEU A 247 ? 0.6449 0.3859 0.8330 0.1041 -0.0060 -0.1393 249 LEU A CD1 1914 C CD2 . LEU A 247 ? 0.7614 0.4375 0.9186 0.1148 -0.0103 -0.1471 249 LEU A CD2 1915 N N . THR A 248 ? 0.7063 0.4179 0.8453 0.1072 0.0282 -0.1834 250 THR A N 1916 C CA . THR A 248 ? 0.7109 0.4128 0.8288 0.0962 0.0328 -0.1897 250 THR A CA 1917 C C . THR A 248 ? 0.7511 0.4428 0.8606 0.1080 0.0431 -0.2034 250 THR A C 1918 O O . THR A 248 ? 0.7768 0.4596 0.8671 0.1006 0.0482 -0.2105 250 THR A O 1919 C CB . THR A 248 ? 0.6767 0.4083 0.8008 0.0846 0.0364 -0.1861 250 THR A CB 1920 O OG1 . THR A 248 ? 0.6388 0.4002 0.7844 0.0948 0.0447 -0.1882 250 THR A OG1 1921 C CG2 . THR A 248 ? 0.6127 0.3524 0.7419 0.0719 0.0267 -0.1737 250 THR A CG2 1922 N N . GLY A 249 ? 0.7590 0.4516 0.8818 0.1264 0.0460 -0.2076 251 GLY A N 1923 C CA . GLY A 249 ? 0.7971 0.4788 0.9120 0.1395 0.0564 -0.2217 251 GLY A CA 1924 C C . GLY A 249 ? 0.7838 0.4988 0.9099 0.1405 0.0692 -0.2272 251 GLY A C 1925 O O . GLY A 249 ? 0.8019 0.5105 0.9156 0.1443 0.0795 -0.2388 251 GLY A O 1926 N N . CYS A 250 ? 0.7484 0.4979 0.8965 0.1362 0.0687 -0.2188 252 CYS A N 1927 C CA . CYS A 250 ? 0.7386 0.5216 0.8981 0.1344 0.0803 -0.2221 252 CYS A CA 1928 C C . CYS A 250 ? 0.7525 0.5672 0.9432 0.1493 0.0857 -0.2233 252 CYS A C 1929 O O . CYS A 250 ? 0.7393 0.5849 0.9424 0.1463 0.0948 -0.2246 252 CYS A O 1930 C CB . CYS A 250 ? 0.6973 0.4965 0.8561 0.1157 0.0767 -0.2123 252 CYS A CB 1931 S SG . CYS A 250 ? 0.6661 0.4433 0.7911 0.0971 0.0757 -0.2137 252 CYS A SG 1932 N N . SER A 251 ? 0.7876 0.5955 0.9910 0.1647 0.0800 -0.2227 253 SER A N 1933 C CA . SER A 251 ? 0.8054 0.6431 1.0384 0.1813 0.0856 -0.2262 253 SER A CA 1934 C C . SER A 251 ? 0.8370 0.6864 1.0693 0.1879 0.1023 -0.2401 253 SER A C 1935 O O . SER A 251 ? 0.8660 0.6887 1.0778 0.1928 0.1070 -0.2498 253 SER A O 1936 C CB . SER A 251 ? 0.8176 0.6404 1.0601 0.1993 0.0768 -0.2252 253 SER A CB 1937 O OG . SER A 251 ? 0.7919 0.6081 1.0362 0.1924 0.0626 -0.2120 253 SER A OG 1938 N N . ARG A 252 ? 0.8414 0.7299 1.0940 0.1858 0.1112 -0.2406 254 ARG A N 1939 C CA . ARG A 252 ? 0.8780 0.7861 1.1354 0.1917 0.1283 -0.2529 254 ARG A CA 1940 C C . ARG A 252 ? 0.8767 0.8278 1.1711 0.2004 0.1317 -0.2517 254 ARG A C 1941 O O . ARG A 252 ? 0.8572 0.8216 1.1690 0.1986 0.1211 -0.2412 254 ARG A O 1942 C CB . ARG A 252 ? 0.8650 0.7792 1.1041 0.1726 0.1374 -0.2539 254 ARG A CB 1943 C CG . ARG A 252 ? 0.8873 0.7641 1.0891 0.1608 0.1349 -0.2553 254 ARG A CG 1944 C CD . ARG A 252 ? 0.8967 0.7440 1.0807 0.1731 0.1400 -0.2680 254 ARG A CD 1945 N NE . ARG A 252 ? 0.9277 0.7429 1.0750 0.1593 0.1388 -0.2702 254 ARG A NE 1946 C CZ . ARG A 252 ? 0.9330 0.7120 1.0599 0.1541 0.1261 -0.2663 254 ARG A CZ 1947 N NH1 . ARG A 252 ? 0.9555 0.7100 1.0510 0.1410 0.1256 -0.2689 254 ARG A NH1 1948 N NH2 . ARG A 252 ? 0.9252 0.6933 1.0630 0.1615 0.1138 -0.2596 254 ARG A NH2 1949 N N . GLU A 253 ? 0.9098 0.8682 1.2408 0.1790 0.1236 -0.3263 255 GLU A N 1950 C CA . GLU A 253 ? 0.9177 0.9120 1.2734 0.1900 0.1262 -0.3210 255 GLU A CA 1951 C C . GLU A 253 ? 0.8914 0.9260 1.2470 0.1745 0.1294 -0.3125 255 GLU A C 1952 O O . GLU A 253 ? 0.8643 0.9196 1.2352 0.1742 0.1247 -0.2985 255 GLU A O 1953 C CB . GLU A 253 ? 0.9494 0.9510 1.3190 0.2118 0.1359 -0.3385 255 GLU A CB 1954 C CG . GLU A 253 ? 1.0357 1.0280 1.3885 0.2132 0.1476 -0.3621 255 GLU A CG 1955 C CD . GLU A 253 ? 1.0789 1.0314 1.4026 0.1986 0.1441 -0.3674 255 GLU A CD 1956 O OE1 . GLU A 253 ? 1.0503 1.0094 1.3579 0.1774 0.1416 -0.3593 255 GLU A OE1 1957 O OE2 . GLU A 253 ? 1.0868 1.0035 1.4039 0.2082 0.1446 -0.3804 255 GLU A OE2 1958 N N . ASN A 254 ? 0.9013 0.9458 1.2389 0.1611 0.1369 -0.3205 256 ASN A N 1959 C CA . ASN A 254 ? 0.8787 0.9555 1.2123 0.1445 0.1392 -0.3116 256 ASN A CA 1960 C C . ASN A 254 ? 0.8465 0.9022 1.1675 0.1292 0.1277 -0.2960 256 ASN A C 1961 O O . ASN A 254 ? 0.8658 0.8903 1.1690 0.1234 0.1240 -0.2994 256 ASN A O 1962 C CB . ASN A 254 ? 0.9154 1.0059 1.2320 0.1364 0.1508 -0.3261 256 ASN A CB 1963 C CG . ASN A 254 ? 0.9680 1.0928 1.2796 0.1196 0.1545 -0.3177 256 ASN A CG 1964 O OD1 . ASN A 254 ? 0.9725 1.1013 1.2851 0.1087 0.1470 -0.3007 256 ASN A OD1 1965 N ND2 . ASN A 254 ? 1.1262 1.2751 1.4313 0.1173 0.1667 -0.3303 256 ASN A ND2 1966 N N . GLU A 255 ? 0.7845 0.8564 1.1150 0.1231 0.1219 -0.2793 257 GLU A N 1967 C CA . GLU A 255 ? 0.7374 0.7921 1.0578 0.1097 0.1113 -0.2641 257 GLU A CA 1968 C C . GLU A 255 ? 0.7045 0.7599 1.0025 0.0910 0.1128 -0.2632 257 GLU A C 1969 O O . GLU A 255 ? 0.6850 0.7181 0.9704 0.0817 0.1052 -0.2562 257 GLU A O 1970 C CB . GLU A 255 ? 0.7182 0.7900 1.0540 0.1082 0.1051 -0.2476 257 GLU A CB 1971 C CG . GLU A 255 ? 0.7221 0.7939 1.0803 0.1258 0.1013 -0.2455 257 GLU A CG 1972 C CD . GLU A 255 ? 0.7095 0.7935 1.0797 0.1224 0.0932 -0.2286 257 GLU A CD 1973 O OE1 . GLU A 255 ? 0.5971 0.6994 0.9635 0.1085 0.0934 -0.2204 257 GLU A OE1 1974 O OE2 . GLU A 255 ? 0.7341 0.8083 1.1172 0.1343 0.0866 -0.2240 257 GLU A OE2 1975 N N . THR A 256 ? 0.6703 0.7524 0.9636 0.0854 0.1225 -0.2699 258 THR A N 1976 C CA . THR A 256 ? 0.6331 0.7181 0.9045 0.0680 0.1243 -0.2691 258 THR A CA 1977 C C . THR A 256 ? 0.6364 0.6940 0.8895 0.0668 0.1245 -0.2815 258 THR A C 1978 O O . THR A 256 ? 0.6278 0.6770 0.8617 0.0528 0.1218 -0.2791 258 THR A O 1979 C CB . THR A 256 ? 0.6287 0.7498 0.8991 0.0622 0.1347 -0.2726 258 THR A CB 1980 O OG1 . THR A 256 ? 0.5975 0.7420 0.8840 0.0609 0.1334 -0.2599 258 THR A OG1 1981 C CG2 . THR A 256 ? 0.6227 0.7456 0.8695 0.0444 0.1355 -0.2704 258 THR A CG2 1982 N N . GLU A 257 ? 0.6399 0.6830 0.8998 0.0820 0.1273 -0.2945 259 GLU A N 1983 C CA . GLU A 257 ? 0.6564 0.6695 0.9006 0.0829 0.1276 -0.3081 259 GLU A CA 1984 C C . GLU A 257 ? 0.6225 0.6000 0.8627 0.0804 0.1157 -0.2995 259 GLU A C 1985 O O . GLU A 257 ? 0.6251 0.5816 0.8470 0.0708 0.1128 -0.3032 259 GLU A O 1986 C CB . GLU A 257 ? 0.6918 0.7017 0.9446 0.1010 0.1361 -0.3266 259 GLU A CB 1987 C CG . GLU A 257 ? 0.7662 0.7979 1.0095 0.0997 0.1491 -0.3433 259 GLU A CG 1988 C CD . GLU A 257 ? 0.8850 0.9068 1.1352 0.1187 0.1568 -0.3631 259 GLU A CD 1989 O OE1 . GLU A 257 ? 0.9816 0.9665 1.2217 0.1218 0.1535 -0.3720 259 GLU A OE1 1990 O OE2 . GLU A 257 ? 0.8872 0.9372 1.1530 0.1306 0.1660 -0.3698 259 GLU A OE2 1991 N N . ILE A 258 ? 0.5980 0.5699 0.8552 0.0888 0.1088 -0.2880 260 ILE A N 1992 C CA . ILE A 258 ? 0.5979 0.5418 0.8514 0.0839 0.0972 -0.2763 260 ILE A CA 1993 C C . ILE A 258 ? 0.5631 0.5087 0.8000 0.0642 0.0925 -0.2665 260 ILE A C 1994 O O . ILE A 258 ? 0.5674 0.4886 0.7900 0.0560 0.0874 -0.2669 260 ILE A O 1995 C CB . ILE A 258 ? 0.5803 0.5257 0.8540 0.0932 0.0904 -0.2624 260 ILE A CB 1996 C CG1 . ILE A 258 ? 0.6135 0.5497 0.9024 0.1135 0.0928 -0.2714 260 ILE A CG1 1997 C CG2 . ILE A 258 ? 0.5769 0.4974 0.8448 0.0855 0.0789 -0.2491 260 ILE A CG2 1998 C CD1 . ILE A 258 ? 0.6787 0.6299 0.9899 0.1232 0.0882 -0.2588 260 ILE A CD1 1999 N N . ILE A 259 ? 0.5304 0.5054 0.7691 0.0568 0.0949 -0.2587 261 ILE A N 2000 C CA . ILE A 259 ? 0.5207 0.5002 0.7462 0.0400 0.0903 -0.2476 261 ILE A CA 2001 C C . ILE A 259 ? 0.5356 0.5116 0.7397 0.0293 0.0939 -0.2579 261 ILE A C 2002 O O . ILE A 259 ? 0.5281 0.4928 0.7188 0.0173 0.0877 -0.2522 261 ILE A O 2003 C CB . ILE A 259 ? 0.4860 0.4963 0.7186 0.0349 0.0920 -0.2365 261 ILE A CB 2004 C CG1 . ILE A 259 ? 0.4803 0.4957 0.7338 0.0444 0.0881 -0.2266 261 ILE A CG1 2005 C CG2 . ILE A 259 ? 0.4955 0.5072 0.7146 0.0188 0.0867 -0.2247 261 ILE A CG2 2006 C CD1 . ILE A 259 ? 0.5397 0.5309 0.7943 0.0438 0.0772 -0.2157 261 ILE A CD1 2007 N N . LYS A 260 ? 0.5472 0.5349 0.7483 0.0336 0.1038 -0.2729 262 LYS A N 2008 C CA . LYS A 260 ? 0.5835 0.5694 0.7632 0.0238 0.1078 -0.2843 262 LYS A CA 2009 C C . LYS A 260 ? 0.6000 0.5500 0.7692 0.0229 0.1025 -0.2917 262 LYS A C 2010 O O . LYS A 260 ? 0.6112 0.5537 0.7629 0.0089 0.0983 -0.2903 262 LYS A O 2011 C CB . LYS A 260 ? 0.5970 0.6042 0.7761 0.0293 0.1203 -0.2994 262 LYS A CB 2012 C CG . LYS A 260 ? 0.6918 0.6904 0.8505 0.0249 0.1259 -0.3176 262 LYS A CG 2013 C CD . LYS A 260 ? 0.7946 0.8060 0.9314 0.0059 0.1253 -0.3142 262 LYS A CD 2014 C CE . LYS A 260 ? 0.8598 0.8680 0.9757 0.0016 0.1324 -0.3344 262 LYS A CE 2015 N NZ . LYS A 260 ? 0.9001 0.9276 1.0213 0.0123 0.1454 -0.3494 262 LYS A NZ 2016 N N . CYS A 261 ? 0.6021 0.5304 0.7823 0.0373 0.1019 -0.2981 263 CYS A N 2017 C CA . CYS A 261 ? 0.6122 0.5028 0.7840 0.0365 0.0959 -0.3031 263 CYS A CA 2018 C C . CYS A 261 ? 0.5997 0.4806 0.7672 0.0238 0.0846 -0.2859 263 CYS A C 2019 O O . CYS A 261 ? 0.6019 0.4663 0.7531 0.0120 0.0804 -0.2883 263 CYS A O 2020 C CB . CYS A 261 ? 0.6247 0.4944 0.8122 0.0550 0.0957 -0.3080 263 CYS A CB 2021 S SG . CYS A 261 ? 0.6372 0.4569 0.8160 0.0551 0.0880 -0.3127 263 CYS A SG 2022 N N . LEU A 262 ? 0.5708 0.4635 0.7529 0.0261 0.0800 -0.2692 264 LEU A N 2023 C CA . LEU A 262 ? 0.5558 0.4415 0.7360 0.0161 0.0701 -0.2530 264 LEU A CA 2024 C C . LEU A 262 ? 0.5537 0.4524 0.7177 -0.0009 0.0688 -0.2491 264 LEU A C 2025 O O . LEU A 262 ? 0.5495 0.4371 0.7064 -0.0109 0.0613 -0.2411 264 LEU A O 2026 C CB . LEU A 262 ? 0.5233 0.4207 0.7216 0.0225 0.0665 -0.2377 264 LEU A CB 2027 C CG . LEU A 262 ? 0.5478 0.4249 0.7601 0.0358 0.0625 -0.2356 264 LEU A CG 2028 C CD1 . LEU A 262 ? 0.4739 0.3688 0.7036 0.0418 0.0601 -0.2221 264 LEU A CD1 2029 C CD2 . LEU A 262 ? 0.5698 0.4149 0.7741 0.0300 0.0539 -0.2314 264 LEU A CD2 2030 N N . ARG A 263 ? 0.5609 0.4829 0.7186 -0.0041 0.0761 -0.2551 265 ARG A N 2031 C CA . ARG A 263 ? 0.5650 0.5011 0.7067 -0.0193 0.0753 -0.2518 265 ARG A CA 2032 C C . ARG A 263 ? 0.6198 0.5395 0.7418 -0.0284 0.0748 -0.2645 265 ARG A C 2033 O O . ARG A 263 ? 0.6297 0.5561 0.7378 -0.0423 0.0712 -0.2602 265 ARG A O 2034 C CB . ARG A 263 ? 0.5557 0.5228 0.6976 -0.0196 0.0834 -0.2527 265 ARG A CB 2035 C CG . ARG A 263 ? 0.5421 0.5290 0.6977 -0.0189 0.0813 -0.2352 265 ARG A CG 2036 C CD . ARG A 263 ? 0.5637 0.5791 0.7124 -0.0264 0.0869 -0.2327 265 ARG A CD 2037 N NE . ARG A 263 ? 0.6721 0.7053 0.8370 -0.0175 0.0926 -0.2309 265 ARG A NE 2038 C CZ . ARG A 263 ? 0.6747 0.7204 0.8434 -0.0103 0.1022 -0.2433 265 ARG A CZ 2039 N NH1 . ARG A 263 ? 0.6640 0.7271 0.8495 -0.0031 0.1059 -0.2392 265 ARG A NH1 2040 N NH2 . ARG A 263 ? 0.7292 0.7717 0.8851 -0.0105 0.1083 -0.2598 265 ARG A NH2 2041 N N . ASN A 264 ? 0.6571 0.5555 0.7776 -0.0206 0.0783 -0.2803 266 ASN A N 2042 C CA . ASN A 264 ? 0.7044 0.5831 0.8062 -0.0296 0.0772 -0.2930 266 ASN A CA 2043 C C . ASN A 264 ? 0.7160 0.5660 0.8168 -0.0343 0.0676 -0.2873 266 ASN A C 2044 O O . ASN A 264 ? 0.7493 0.5826 0.8343 -0.0445 0.0650 -0.2957 266 ASN A O 2045 C CB . ASN A 264 ? 0.7479 0.6159 0.8456 -0.0201 0.0862 -0.3149 266 ASN A CB 2046 C CG . ASN A 264 ? 0.7857 0.6842 0.8797 -0.0187 0.0966 -0.3229 266 ASN A CG 2047 O OD1 . ASN A 264 ? 0.8060 0.7312 0.8957 -0.0280 0.0965 -0.3129 266 ASN A OD1 2048 N ND2 . ASN A 264 ? 0.8629 0.7576 0.9586 -0.0067 0.1058 -0.3408 266 ASN A ND2 2049 N N . LYS A 265 ? 0.7019 0.5460 0.8186 -0.0280 0.0621 -0.2733 267 LYS A N 2050 C CA . LYS A 265 ? 0.7014 0.5190 0.8170 -0.0332 0.0531 -0.2668 267 LYS A CA 2051 C C . LYS A 265 ? 0.6911 0.5181 0.7975 -0.0501 0.0459 -0.2550 267 LYS A C 2052 O O . LYS A 265 ? 0.6824 0.5365 0.7915 -0.0536 0.0457 -0.2441 267 LYS A O 2053 C CB . LYS A 265 ? 0.6878 0.4960 0.8224 -0.0208 0.0497 -0.2559 267 LYS A CB 2054 C CG . LYS A 265 ? 0.6889 0.4857 0.8349 -0.0026 0.0554 -0.2662 267 LYS A CG 2055 C CD . LYS A 265 ? 0.7811 0.5513 0.9153 -0.0007 0.0593 -0.2863 267 LYS A CD 2056 C CE . LYS A 265 ? 0.8296 0.5610 0.9612 -0.0018 0.0523 -0.2860 267 LYS A CE 2057 N NZ . LYS A 265 ? 0.8786 0.5808 1.0014 0.0039 0.0569 -0.3065 267 LYS A NZ 2058 N N . ASP A 266 ? 0.7054 0.5103 0.8014 -0.0607 0.0400 -0.2570 268 ASP A N 2059 C CA . ASP A 266 ? 0.6889 0.5012 0.7791 -0.0759 0.0320 -0.2446 268 ASP A CA 2060 C C . ASP A 266 ? 0.6589 0.4807 0.7655 -0.0712 0.0274 -0.2252 268 ASP A C 2061 O O . ASP A 266 ? 0.6489 0.4556 0.7677 -0.0605 0.0266 -0.2217 268 ASP A O 2062 C CB . ASP A 266 ? 0.7072 0.4910 0.7871 -0.0866 0.0261 -0.2491 268 ASP A CB 2063 C CG . ASP A 266 ? 0.7333 0.5084 0.7936 -0.0959 0.0289 -0.2675 268 ASP A CG 2064 O OD1 . ASP A 266 ? 0.7326 0.4778 0.7850 -0.1016 0.0258 -0.2754 268 ASP A OD1 2065 O OD2 . ASP A 266 ? 0.6709 0.4680 0.7229 -0.0983 0.0339 -0.2740 268 ASP A OD2 2066 N N . PRO A 267 ? 0.6312 0.4768 0.7374 -0.0794 0.0240 -0.2126 269 PRO A N 2067 C CA . PRO A 267 ? 0.6040 0.4561 0.7254 -0.0734 0.0206 -0.1965 269 PRO A CA 2068 C C . PRO A 267 ? 0.6040 0.4321 0.7303 -0.0734 0.0147 -0.1911 269 PRO A C 2069 O O . PRO A 267 ? 0.5846 0.4115 0.7244 -0.0641 0.0135 -0.1820 269 PRO A O 2070 C CB . PRO A 267 ? 0.5854 0.4641 0.7047 -0.0822 0.0177 -0.1847 269 PRO A CB 2071 C CG . PRO A 267 ? 0.6113 0.4989 0.7133 -0.0933 0.0192 -0.1942 269 PRO A CG 2072 C CD . PRO A 267 ? 0.6281 0.4980 0.7231 -0.0895 0.0248 -0.2125 269 PRO A CD 2073 N N . GLN A 268 ? 0.6140 0.4224 0.7290 -0.0838 0.0112 -0.1971 270 GLN A N 2074 C CA . GLN A 268 ? 0.6179 0.4020 0.7358 -0.0860 0.0053 -0.1913 270 GLN A CA 2075 C C . GLN A 268 ? 0.6272 0.3881 0.7541 -0.0713 0.0074 -0.1953 270 GLN A C 2076 O O . GLN A 268 ? 0.6367 0.3862 0.7720 -0.0679 0.0031 -0.1850 270 GLN A O 2077 C CB . GLN A 268 ? 0.6439 0.4089 0.7467 -0.1012 0.0015 -0.1989 270 GLN A CB 2078 C CG . GLN A 268 ? 0.6450 0.4199 0.7444 -0.1169 -0.0056 -0.1873 270 GLN A CG 2079 C CD . GLN A 268 ? 0.6115 0.3970 0.7243 -0.1135 -0.0094 -0.1693 270 GLN A CD 2080 O OE1 . GLN A 268 ? 0.6221 0.3884 0.7400 -0.1115 -0.0124 -0.1637 270 GLN A OE1 2081 N NE2 . GLN A 268 ? 0.5395 0.3555 0.6571 -0.1134 -0.0092 -0.1602 270 GLN A NE2 2082 N N . GLU A 269 ? 0.6252 0.3795 0.7502 -0.0624 0.0139 -0.2100 271 GLU A N 2083 C CA . GLU A 269 ? 0.6346 0.3672 0.7689 -0.0471 0.0160 -0.2145 271 GLU A CA 2084 C C . GLU A 269 ? 0.6120 0.3622 0.7641 -0.0336 0.0170 -0.2035 271 GLU A C 2085 O O . GLU A 269 ? 0.6149 0.3502 0.7773 -0.0237 0.0145 -0.1980 271 GLU A O 2086 C CB . GLU A 269 ? 0.6662 0.3883 0.7942 -0.0403 0.0233 -0.2344 271 GLU A CB 2087 C CG . GLU A 269 ? 0.6950 0.3841 0.8285 -0.0272 0.0237 -0.2411 271 GLU A CG 2088 C CD . GLU A 269 ? 0.7280 0.4067 0.8559 -0.0192 0.0315 -0.2617 271 GLU A CD 2089 O OE1 . GLU A 269 ? 0.7317 0.3982 0.8705 -0.0020 0.0347 -0.2665 271 GLU A OE1 2090 O OE2 . GLU A 269 ? 0.7499 0.4336 0.8625 -0.0298 0.0345 -0.2732 271 GLU A OE2 2091 N N . ILE A 270 ? 0.5735 0.3550 0.7287 -0.0338 0.0202 -0.1998 272 ILE A N 2092 C CA . ILE A 270 ? 0.5468 0.3462 0.7173 -0.0241 0.0206 -0.1892 272 ILE A CA 2093 C C . ILE A 270 ? 0.5391 0.3349 0.7138 -0.0287 0.0129 -0.1733 272 ILE A C 2094 O O . ILE A 270 ? 0.5390 0.3276 0.7250 -0.0191 0.0106 -0.1665 272 ILE A O 2095 C CB . ILE A 270 ? 0.5316 0.3625 0.7019 -0.0262 0.0251 -0.1883 272 ILE A CB 2096 C CG1 . ILE A 270 ? 0.5636 0.3990 0.7339 -0.0178 0.0335 -0.2031 272 ILE A CG1 2097 C CG2 . ILE A 270 ? 0.5203 0.3707 0.7042 -0.0211 0.0236 -0.1742 272 ILE A CG2 2098 C CD1 . ILE A 270 ? 0.5878 0.4480 0.7504 -0.0241 0.0386 -0.2068 272 ILE A CD1 2099 N N . LEU A 271 ? 0.5274 0.3287 0.6933 -0.0431 0.0088 -0.1673 273 LEU A N 2100 C CA . LEU A 271 ? 0.5014 0.3027 0.6712 -0.0480 0.0022 -0.1521 273 LEU A CA 2101 C C . LEU A 271 ? 0.5240 0.2962 0.6952 -0.0458 -0.0021 -0.1500 273 LEU A C 2102 O O . LEU A 271 ? 0.4826 0.2545 0.6626 -0.0415 -0.0057 -0.1383 273 LEU A O 2103 C CB . LEU A 271 ? 0.4737 0.2856 0.6341 -0.0637 -0.0013 -0.1472 273 LEU A CB 2104 C CG . LEU A 271 ? 0.4737 0.3156 0.6335 -0.0663 0.0011 -0.1445 273 LEU A CG 2105 C CD1 . LEU A 271 ? 0.4826 0.3321 0.6315 -0.0819 -0.0026 -0.1425 273 LEU A CD1 2106 C CD2 . LEU A 271 ? 0.3876 0.2465 0.5595 -0.0600 0.0003 -0.1317 273 LEU A CD2 2107 N N . LEU A 272 ? 0.5617 0.3088 0.7235 -0.0490 -0.0017 -0.1614 274 LEU A N 2108 C CA . LEU A 272 ? 0.5967 0.3128 0.7578 -0.0489 -0.0064 -0.1587 274 LEU A CA 2109 C C . LEU A 272 ? 0.6098 0.3173 0.7840 -0.0313 -0.0057 -0.1565 274 LEU A C 2110 O O . LEU A 272 ? 0.6243 0.3162 0.8024 -0.0295 -0.0107 -0.1469 274 LEU A O 2111 C CB . LEU A 272 ? 0.6412 0.3296 0.7882 -0.0580 -0.0069 -0.1711 274 LEU A CB 2112 C CG . LEU A 272 ? 0.6316 0.3188 0.7666 -0.0783 -0.0118 -0.1674 274 LEU A CG 2113 C CD1 . LEU A 272 ? 0.6024 0.3241 0.7401 -0.0862 -0.0135 -0.1556 274 LEU A CD1 2114 C CD2 . LEU A 272 ? 0.6640 0.3402 0.7841 -0.0879 -0.0098 -0.1833 274 LEU A CD2 2115 N N . ASN A 273 ? 0.6113 0.3324 0.7932 -0.0186 0.0003 -0.1637 275 ASN A N 2116 C CA . ASN A 273 ? 0.6112 0.3260 0.8066 -0.0012 0.0010 -0.1626 275 ASN A CA 2117 C C . ASN A 273 ? 0.6034 0.3431 0.8121 0.0054 -0.0001 -0.1502 275 ASN A C 2118 O O . ASN A 273 ? 0.6148 0.3509 0.8350 0.0186 -0.0011 -0.1469 275 ASN A O 2119 C CB . ASN A 273 ? 0.6061 0.3171 0.8032 0.0102 0.0081 -0.1790 275 ASN A CB 2120 C CG . ASN A 273 ? 0.6570 0.3342 0.8430 0.0078 0.0082 -0.1910 275 ASN A CG 2121 O OD1 . ASN A 273 ? 0.6915 0.3686 0.8658 0.0000 0.0119 -0.2031 275 ASN A OD1 2122 N ND2 . ASN A 273 ? 0.6325 0.2800 0.8211 0.0137 0.0036 -0.1875 275 ASN A ND2 2123 N N . GLU A 274 ? 0.5746 0.3390 0.7817 -0.0035 -0.0001 -0.1437 276 GLU A N 2124 C CA . GLU A 274 ? 0.5737 0.3610 0.7915 0.0011 -0.0009 -0.1332 276 GLU A CA 2125 C C . GLU A 274 ? 0.5824 0.3592 0.8068 0.0055 -0.0072 -0.1210 276 GLU A C 2126 O O . GLU A 274 ? 0.5738 0.3626 0.8098 0.0154 -0.0074 -0.1160 276 GLU A O 2127 C CB . GLU A 274 ? 0.5513 0.3615 0.7641 -0.0107 -0.0010 -0.1273 276 GLU A CB 2128 C CG . GLU A 274 ? 0.5484 0.3772 0.7581 -0.0123 0.0053 -0.1361 276 GLU A CG 2129 C CD . GLU A 274 ? 0.5499 0.4007 0.7556 -0.0222 0.0047 -0.1290 276 GLU A CD 2130 O OE1 . GLU A 274 ? 0.5276 0.3801 0.7326 -0.0286 -0.0001 -0.1184 276 GLU A OE1 2131 O OE2 . GLU A 274 ? 0.5307 0.3975 0.7339 -0.0235 0.0094 -0.1342 276 GLU A OE2 2132 N N . ALA A 275 ? 0.6013 0.3579 0.8180 -0.0030 -0.0123 -0.1157 277 ALA A N 2133 C CA . ALA A 275 ? 0.6211 0.3702 0.8417 -0.0016 -0.0184 -0.1024 277 ALA A CA 2134 C C . ALA A 275 ? 0.6523 0.3860 0.8819 0.0138 -0.0195 -0.1032 277 ALA A C 2135 O O . ALA A 275 ? 0.6504 0.3895 0.8885 0.0208 -0.0231 -0.0934 277 ALA A O 2136 C CB . ALA A 275 ? 0.6375 0.3681 0.8470 -0.0155 -0.0232 -0.0967 277 ALA A CB 2137 N N . PHE A 276 ? 0.6884 0.4054 0.9168 0.0199 -0.0162 -0.1158 278 PHE A N 2138 C CA . PHE A 276 ? 0.7181 0.4172 0.9546 0.0350 -0.0173 -0.1178 278 PHE A CA 2139 C C . PHE A 276 ? 0.7051 0.4243 0.9562 0.0508 -0.0130 -0.1227 278 PHE A C 2140 O O . PHE A 276 ? 0.7129 0.4190 0.9722 0.0647 -0.0140 -0.1242 278 PHE A O 2141 C CB . PHE A 276 ? 0.7654 0.4316 0.9928 0.0341 -0.0164 -0.1287 278 PHE A CB 2142 C CG . PHE A 276 ? 0.8174 0.4653 1.0309 0.0171 -0.0207 -0.1241 278 PHE A CG 2143 C CD1 . PHE A 276 ? 0.8843 0.5168 1.0966 0.0136 -0.0279 -0.1099 278 PHE A CD1 2144 C CD2 . PHE A 276 ? 0.8784 0.5279 1.0800 0.0038 -0.0178 -0.1329 278 PHE A CD2 2145 C CE1 . PHE A 276 ? 0.9538 0.5722 1.1537 -0.0034 -0.0317 -0.1048 278 PHE A CE1 2146 C CE2 . PHE A 276 ? 0.9396 0.5756 1.1292 -0.0129 -0.0220 -0.1282 278 PHE A CE2 2147 C CZ . PHE A 276 ? 0.9678 0.5883 1.1568 -0.0169 -0.0288 -0.1142 278 PHE A CZ 2148 N N . VAL A 277 ? 0.6660 0.4164 0.9209 0.0490 -0.0086 -0.1244 279 VAL A N 2149 C CA . VAL A 277 ? 0.6593 0.4303 0.9282 0.0626 -0.0041 -0.1294 279 VAL A CA 2150 C C . VAL A 277 ? 0.6660 0.4457 0.9480 0.0722 -0.0092 -0.1178 279 VAL A C 2151 O O . VAL A 277 ? 0.6714 0.4675 0.9669 0.0842 -0.0070 -0.1202 279 VAL A O 2152 C CB . VAL A 277 ? 0.6417 0.4419 0.9099 0.0569 0.0024 -0.1349 279 VAL A CB 2153 C CG1 . VAL A 277 ? 0.6414 0.4329 0.8957 0.0475 0.0067 -0.1461 279 VAL A CG1 2154 C CG2 . VAL A 277 ? 0.5890 0.4093 0.8560 0.0466 -0.0007 -0.1225 279 VAL A CG2 2155 N N . VAL A 278 ? 0.6868 0.4559 0.9645 0.0664 -0.0163 -0.1051 280 VAL A N 2156 C CA . VAL A 278 ? 0.6907 0.4685 0.9772 0.0719 -0.0222 -0.0923 280 VAL A CA 2157 C C . VAL A 278 ? 0.7380 0.4838 1.0220 0.0762 -0.0288 -0.0857 280 VAL A C 2158 O O . VAL A 278 ? 0.7518 0.4730 1.0235 0.0672 -0.0300 -0.0865 280 VAL A O 2159 C CB . VAL A 278 ? 0.6714 0.4660 0.9519 0.0585 -0.0242 -0.0826 280 VAL A CB 2160 C CG1 . VAL A 278 ? 0.6785 0.4616 0.9550 0.0548 -0.0319 -0.0688 280 VAL A CG1 2161 C CG2 . VAL A 278 ? 0.6292 0.4565 0.9187 0.0605 -0.0213 -0.0826 280 VAL A CG2 2162 N N . PRO A 279 ? 0.7557 0.5014 1.0509 0.0891 -0.0334 -0.0787 281 PRO A N 2163 C CA . PRO A 279 ? 0.8029 0.5162 1.0949 0.0932 -0.0401 -0.0713 281 PRO A CA 2164 C C . PRO A 279 ? 0.8089 0.5121 1.0890 0.0792 -0.0463 -0.0573 281 PRO A C 2165 O O . PRO A 279 ? 0.8292 0.5016 1.1010 0.0760 -0.0502 -0.0533 281 PRO A O 2166 C CB . PRO A 279 ? 0.8013 0.5221 1.1091 0.1110 -0.0438 -0.0664 281 PRO A CB 2167 C CG . PRO A 279 ? 0.7814 0.5428 1.0992 0.1118 -0.0409 -0.0669 281 PRO A CG 2168 C CD . PRO A 279 ? 0.7465 0.5215 1.0560 0.0982 -0.0340 -0.0751 281 PRO A CD 2169 N N . TYR A 280 ? 0.7847 0.5133 1.0636 0.0707 -0.0470 -0.0501 282 TYR A N 2170 C CA . TYR A 280 ? 0.7952 0.5189 1.0630 0.0569 -0.0516 -0.0380 282 TYR A CA 2171 C C . TYR A 280 ? 0.7506 0.5034 1.0160 0.0466 -0.0485 -0.0375 282 TYR A C 2172 O O . TYR A 280 ? 0.7542 0.5320 1.0278 0.0514 -0.0480 -0.0361 282 TYR A O 2173 C CB . TYR A 280 ? 0.8129 0.5317 1.0833 0.0623 -0.0597 -0.0229 282 TYR A CB 2174 C CG . TYR A 280 ? 0.8576 0.5982 1.1427 0.0765 -0.0609 -0.0220 282 TYR A CG 2175 C CD1 . TYR A 280 ? 0.9283 0.6565 1.2231 0.0925 -0.0649 -0.0198 282 TYR A CD1 2176 C CD2 . TYR A 280 ? 0.8467 0.6206 1.1367 0.0742 -0.0580 -0.0237 282 TYR A CD2 2177 C CE1 . TYR A 280 ? 0.9368 0.6893 1.2465 0.1052 -0.0663 -0.0188 282 TYR A CE1 2178 C CE2 . TYR A 280 ? 0.8678 0.6636 1.1713 0.0855 -0.0591 -0.0231 282 TYR A CE2 2179 C CZ . TYR A 280 ? 0.9150 0.7020 1.2286 0.1006 -0.0633 -0.0207 282 TYR A CZ 2180 O OH . TYR A 280 ? 0.9118 0.7244 1.2394 0.1106 -0.0645 -0.0203 282 TYR A OH 2181 N N . GLY A 281 ? 0.7255 0.4760 0.9801 0.0326 -0.0464 -0.0388 283 GLY A N 2182 C CA . GLY A 281 ? 0.6668 0.4451 0.9203 0.0247 -0.0439 -0.0374 283 GLY A CA 2183 C C . GLY A 281 ? 0.6283 0.4096 0.8754 0.0159 -0.0486 -0.0241 283 GLY A C 2184 O O . GLY A 281 ? 0.6481 0.4117 0.8919 0.0157 -0.0540 -0.0149 283 GLY A O 2185 N N . THR A 282 ? 0.5544 0.3573 0.7993 0.0084 -0.0462 -0.0229 284 THR A N 2186 C CA . THR A 282 ? 0.5112 0.3208 0.7501 0.0001 -0.0494 -0.0117 284 THR A CA 2187 C C . THR A 282 ? 0.4808 0.3011 0.7136 -0.0115 -0.0453 -0.0150 284 THR A C 2188 O O . THR A 282 ? 0.4662 0.2896 0.7000 -0.0117 -0.0409 -0.0249 284 THR A O 2189 C CB . THR A 282 ? 0.4993 0.3306 0.7441 0.0060 -0.0510 -0.0066 284 THR A CB 2190 O OG1 . THR A 282 ? 0.4678 0.3207 0.7148 0.0041 -0.0461 -0.0125 284 THR A OG1 2191 C CG2 . THR A 282 ? 0.4403 0.2707 0.6955 0.0199 -0.0532 -0.0078 284 THR A CG2 2192 N N . PRO A 283 ? 0.4594 0.2873 0.6860 -0.0210 -0.0468 -0.0066 285 PRO A N 2193 C CA . PRO A 283 ? 0.4331 0.2751 0.6561 -0.0302 -0.0428 -0.0100 285 PRO A CA 2194 C C . PRO A 283 ? 0.4240 0.2877 0.6529 -0.0252 -0.0386 -0.0160 285 PRO A C 2195 O O . PRO A 283 ? 0.4354 0.3111 0.6623 -0.0309 -0.0353 -0.0191 285 PRO A O 2196 C CB . PRO A 283 ? 0.4231 0.2735 0.6406 -0.0388 -0.0449 0.0006 285 PRO A CB 2197 C CG . PRO A 283 ? 0.4483 0.2779 0.6624 -0.0387 -0.0504 0.0093 285 PRO A CG 2198 C CD . PRO A 283 ? 0.4500 0.2727 0.6717 -0.0249 -0.0517 0.0059 285 PRO A CD 2199 N N . LEU A 284 ? 0.4034 0.2731 0.6394 -0.0152 -0.0389 -0.0170 286 LEU A N 2200 C CA . LEU A 284 ? 0.3911 0.2804 0.6321 -0.0118 -0.0352 -0.0218 286 LEU A CA 2201 C C . LEU A 284 ? 0.3903 0.2780 0.6379 -0.0042 -0.0321 -0.0316 286 LEU A C 2202 O O . LEU A 284 ? 0.3692 0.2716 0.6221 -0.0004 -0.0293 -0.0356 286 LEU A O 2203 C CB . LEU A 284 ? 0.3992 0.3014 0.6427 -0.0082 -0.0374 -0.0160 286 LEU A CB 2204 C CG . LEU A 284 ? 0.3918 0.3035 0.6286 -0.0163 -0.0376 -0.0092 286 LEU A CG 2205 C CD1 . LEU A 284 ? 0.3809 0.2830 0.6130 -0.0187 -0.0425 0.0002 286 LEU A CD1 2206 C CD2 . LEU A 284 ? 0.4011 0.3319 0.6401 -0.0142 -0.0359 -0.0097 286 LEU A CD2 2207 N N . SER A 285 ? 0.3892 0.2590 0.6360 -0.0027 -0.0323 -0.0359 287 SER A N 2208 C CA . SER A 285 ? 0.3966 0.2649 0.6500 0.0056 -0.0292 -0.0454 287 SER A CA 2209 C C . SER A 285 ? 0.3770 0.2579 0.6299 0.0027 -0.0236 -0.0532 287 SER A C 2210 O O . SER A 285 ? 0.3894 0.2699 0.6351 -0.0058 -0.0223 -0.0542 287 SER A O 2211 C CB . SER A 285 ? 0.4144 0.2586 0.6654 0.0075 -0.0301 -0.0494 287 SER A CB 2212 O OG . SER A 285 ? 0.4201 0.2534 0.6751 0.0146 -0.0349 -0.0434 287 SER A OG 2213 N N . VAL A 286 ? 0.3650 0.2581 0.6257 0.0095 -0.0206 -0.0581 288 VAL A N 2214 C CA . VAL A 286 ? 0.3355 0.2393 0.5955 0.0071 -0.0153 -0.0652 288 VAL A CA 2215 C C . VAL A 286 ? 0.3544 0.2535 0.6198 0.0149 -0.0124 -0.0741 288 VAL A C 2216 O O . VAL A 286 ? 0.3661 0.2756 0.6408 0.0223 -0.0111 -0.0758 288 VAL A O 2217 C CB . VAL A 286 ? 0.3210 0.2450 0.5848 0.0067 -0.0138 -0.0627 288 VAL A CB 2218 C CG1 . VAL A 286 ? 0.2481 0.1828 0.5124 0.0057 -0.0083 -0.0696 288 VAL A CG1 2219 C CG2 . VAL A 286 ? 0.2741 0.2022 0.5314 -0.0009 -0.0158 -0.0554 288 VAL A CG2 2220 N N . ASN A 287 ? 0.3467 0.2308 0.6065 0.0133 -0.0111 -0.0801 289 ASN A N 2221 C CA . ASN A 287 ? 0.3727 0.2505 0.6379 0.0223 -0.0081 -0.0893 289 ASN A CA 2222 C C . ASN A 287 ? 0.3497 0.2461 0.6189 0.0243 -0.0015 -0.0974 289 ASN A C 2223 O O . ASN A 287 ? 0.3415 0.2436 0.6202 0.0337 0.0009 -0.1023 289 ASN A O 2224 C CB . ASN A 287 ? 0.3864 0.2405 0.6434 0.0199 -0.0085 -0.0948 289 ASN A CB 2225 C CG . ASN A 287 ? 0.4666 0.2991 0.7233 0.0223 -0.0147 -0.0878 289 ASN A CG 2226 O OD1 . ASN A 287 ? 0.5456 0.3560 0.7940 0.0177 -0.0164 -0.0897 289 ASN A OD1 2227 N ND2 . ASN A 287 ? 0.4444 0.2826 0.7095 0.0291 -0.0183 -0.0800 289 ASN A ND2 2228 N N . PHE A 288 ? 0.3206 0.2271 0.5826 0.0152 0.0011 -0.0978 290 PHE A N 2229 C CA . PHE A 288 ? 0.3118 0.2346 0.5747 0.0146 0.0072 -0.1041 290 PHE A CA 2230 C C . PHE A 288 ? 0.2960 0.2340 0.5584 0.0089 0.0065 -0.0966 290 PHE A C 2231 O O . PHE A 288 ? 0.3089 0.2460 0.5630 0.0009 0.0052 -0.0930 290 PHE A O 2232 C CB . PHE A 288 ? 0.3028 0.2193 0.5549 0.0088 0.0108 -0.1127 290 PHE A CB 2233 C CG . PHE A 288 ? 0.3586 0.2599 0.6114 0.0157 0.0127 -0.1226 290 PHE A CG 2234 C CD1 . PHE A 288 ? 0.3411 0.2509 0.6022 0.0248 0.0179 -0.1306 290 PHE A CD1 2235 C CD2 . PHE A 288 ? 0.3763 0.2541 0.6227 0.0139 0.0089 -0.1231 290 PHE A CD2 2236 C CE1 . PHE A 288 ? 0.3975 0.2926 0.6604 0.0331 0.0199 -0.1403 290 PHE A CE1 2237 C CE2 . PHE A 288 ? 0.3398 0.1999 0.5868 0.0211 0.0104 -0.1324 290 PHE A CE2 2238 C CZ . PHE A 288 ? 0.3890 0.2574 0.6444 0.0315 0.0160 -0.1412 290 PHE A CZ 2239 N N . GLY A 289 ? 0.2916 0.2432 0.5632 0.0130 0.0071 -0.0942 291 GLY A N 2240 C CA . GLY A 289 ? 0.2668 0.2302 0.5379 0.0081 0.0063 -0.0874 291 GLY A CA 2241 C C . GLY A 289 ? 0.2593 0.2395 0.5374 0.0098 0.0106 -0.0902 291 GLY A C 2242 O O . GLY A 289 ? 0.2586 0.2434 0.5407 0.0136 0.0148 -0.0975 291 GLY A O 2243 N N . PRO A 290 ? 0.2592 0.2488 0.5383 0.0064 0.0098 -0.0846 292 PRO A N 2244 C CA . PRO A 290 ? 0.2511 0.2564 0.5364 0.0059 0.0135 -0.0860 292 PRO A CA 2245 C C . PRO A 290 ? 0.2593 0.2717 0.5568 0.0136 0.0140 -0.0898 292 PRO A C 2246 O O . PRO A 290 ? 0.2725 0.2788 0.5747 0.0194 0.0097 -0.0881 292 PRO A O 2247 C CB . PRO A 290 ? 0.2328 0.2406 0.5171 0.0021 0.0104 -0.0788 292 PRO A CB 2248 C CG . PRO A 290 ? 0.2458 0.2429 0.5200 -0.0019 0.0078 -0.0746 292 PRO A CG 2249 C CD . PRO A 290 ? 0.2466 0.2323 0.5199 0.0017 0.0060 -0.0772 292 PRO A CD 2250 N N . THR A 291 ? 0.2612 0.2874 0.5642 0.0139 0.0191 -0.0946 293 THR A N 2251 C CA . THR A 291 ? 0.2832 0.3205 0.5996 0.0213 0.0197 -0.0978 293 THR A CA 2252 C C . THR A 291 ? 0.2698 0.3254 0.5914 0.0162 0.0225 -0.0967 293 THR A C 2253 O O . THR A 291 ? 0.3018 0.3581 0.6151 0.0079 0.0248 -0.0946 293 THR A O 2254 C CB . THR A 291 ? 0.3004 0.3397 0.6207 0.0279 0.0247 -0.1069 293 THR A CB 2255 O OG1 . THR A 291 ? 0.3156 0.3558 0.6260 0.0216 0.0304 -0.1111 293 THR A OG1 2256 C CG2 . THR A 291 ? 0.3402 0.3623 0.6599 0.0350 0.0212 -0.1082 293 THR A CG2 2257 N N . VAL A 292 ? 0.2335 0.3033 0.5682 0.0207 0.0221 -0.0978 294 VAL A N 2258 C CA . VAL A 292 ? 0.2308 0.3199 0.5716 0.0154 0.0258 -0.0982 294 VAL A CA 2259 C C . VAL A 292 ? 0.2446 0.3444 0.5867 0.0158 0.0338 -0.1056 294 VAL A C 2260 O O . VAL A 292 ? 0.2562 0.3653 0.6086 0.0241 0.0362 -0.1114 294 VAL A O 2261 C CB . VAL A 292 ? 0.2257 0.3297 0.5815 0.0197 0.0223 -0.0971 294 VAL A CB 2262 C CG1 . VAL A 292 ? 0.2371 0.3619 0.5993 0.0122 0.0259 -0.0973 294 VAL A CG1 2263 C CG2 . VAL A 292 ? 0.1946 0.2881 0.5476 0.0195 0.0144 -0.0905 294 VAL A CG2 2264 N N . ASP A 293 ? 0.2521 0.3510 0.5834 0.0075 0.0381 -0.1054 295 ASP A N 2265 C CA . ASP A 293 ? 0.2749 0.3836 0.6049 0.0073 0.0459 -0.1125 295 ASP A CA 2266 C C . ASP A 293 ? 0.2853 0.4172 0.6215 0.0009 0.0515 -0.1129 295 ASP A C 2267 O O . ASP A 293 ? 0.3030 0.4466 0.6381 -0.0002 0.0588 -0.1187 295 ASP A O 2268 C CB . ASP A 293 ? 0.2747 0.3703 0.5880 0.0013 0.0472 -0.1120 295 ASP A CB 2269 C CG . ASP A 293 ? 0.2553 0.3478 0.5602 -0.0089 0.0453 -0.1033 295 ASP A CG 2270 O OD1 . ASP A 293 ? 0.2578 0.3543 0.5689 -0.0112 0.0423 -0.0983 295 ASP A OD1 2271 O OD2 . ASP A 293 ? 0.2549 0.3412 0.5472 -0.0147 0.0466 -0.1017 295 ASP A OD2 2272 N N . GLY A 294 ? 0.2740 0.4123 0.6152 -0.0045 0.0485 -0.1069 296 GLY A N 2273 C CA . GLY A 294 ? 0.2778 0.4365 0.6238 -0.0127 0.0534 -0.1063 296 GLY A CA 2274 C C . GLY A 294 ? 0.2874 0.4417 0.6190 -0.0240 0.0568 -0.1022 296 GLY A C 2275 O O . GLY A 294 ? 0.3015 0.4712 0.6344 -0.0319 0.0618 -0.1015 296 GLY A O 2276 N N . ASP A 295 ? 0.2870 0.4209 0.6050 -0.0252 0.0538 -0.0989 297 ASP A N 2277 C CA . ASP A 295 ? 0.2763 0.4061 0.5802 -0.0343 0.0567 -0.0949 297 ASP A CA 2278 C C . ASP A 295 ? 0.2732 0.3834 0.5690 -0.0370 0.0501 -0.0869 297 ASP A C 2279 O O . ASP A 295 ? 0.2628 0.3722 0.5593 -0.0434 0.0482 -0.0810 297 ASP A O 2280 C CB . ASP A 295 ? 0.2787 0.4079 0.5743 -0.0315 0.0611 -0.1012 297 ASP A CB 2281 C CG . ASP A 295 ? 0.3165 0.4455 0.5971 -0.0413 0.0644 -0.0971 297 ASP A CG 2282 O OD1 . ASP A 295 ? 0.3481 0.4755 0.6250 -0.0495 0.0631 -0.0887 297 ASP A OD1 2283 O OD2 . ASP A 295 ? 0.3393 0.4680 0.6107 -0.0409 0.0677 -0.1018 297 ASP A OD2 2284 N N . PHE A 296 ? 0.2756 0.3705 0.5650 -0.0319 0.0463 -0.0871 298 PHE A N 2285 C CA . PHE A 296 ? 0.2616 0.3407 0.5453 -0.0331 0.0404 -0.0803 298 PHE A CA 2286 C C . PHE A 296 ? 0.2623 0.3408 0.5556 -0.0309 0.0359 -0.0786 298 PHE A C 2287 O O . PHE A 296 ? 0.2603 0.3326 0.5510 -0.0353 0.0333 -0.0732 298 PHE A O 2288 C CB . PHE A 296 ? 0.2643 0.3299 0.5409 -0.0285 0.0373 -0.0810 298 PHE A CB 2289 C CG . PHE A 296 ? 0.2305 0.2825 0.5006 -0.0300 0.0322 -0.0738 298 PHE A CG 2290 C CD1 . PHE A 296 ? 0.2067 0.2519 0.4816 -0.0259 0.0271 -0.0722 298 PHE A CD1 2291 C CD2 . PHE A 296 ? 0.1972 0.2447 0.4565 -0.0351 0.0324 -0.0688 298 PHE A CD2 2292 C CE1 . PHE A 296 ? 0.1882 0.2225 0.4573 -0.0267 0.0232 -0.0663 298 PHE A CE1 2293 C CE2 . PHE A 296 ? 0.1872 0.2239 0.4418 -0.0351 0.0280 -0.0625 298 PHE A CE2 2294 C CZ . PHE A 296 ? 0.2261 0.2564 0.4856 -0.0309 0.0238 -0.0617 298 PHE A CZ 2295 N N . LEU A 297 ? 0.2528 0.3374 0.5566 -0.0237 0.0350 -0.0835 299 LEU A N 2296 C CA . LEU A 297 ? 0.2604 0.3468 0.5731 -0.0211 0.0304 -0.0824 299 LEU A CA 2297 C C . LEU A 297 ? 0.2754 0.3823 0.6013 -0.0208 0.0334 -0.0864 299 LEU A C 2298 O O . LEU A 297 ? 0.2790 0.3944 0.6116 -0.0138 0.0361 -0.0922 299 LEU A O 2299 C CB . LEU A 297 ? 0.2494 0.3270 0.5641 -0.0120 0.0261 -0.0840 299 LEU A CB 2300 C CG . LEU A 297 ? 0.3077 0.3710 0.6173 -0.0110 0.0200 -0.0793 299 LEU A CG 2301 C CD1 . LEU A 297 ? 0.3080 0.3649 0.6211 -0.0023 0.0157 -0.0803 299 LEU A CD1 2302 C CD2 . LEU A 297 ? 0.4059 0.4734 0.7189 -0.0156 0.0173 -0.0761 299 LEU A CD2 2303 N N . THR A 298 ? 0.2752 0.3904 0.6052 -0.0280 0.0330 -0.0837 300 THR A N 2304 C CA . THR A 298 ? 0.3054 0.4430 0.6483 -0.0297 0.0361 -0.0868 300 THR A CA 2305 C C . THR A 298 ? 0.2916 0.4396 0.6485 -0.0224 0.0316 -0.0889 300 THR A C 2306 O O . THR A 298 ? 0.2884 0.4581 0.6581 -0.0213 0.0343 -0.0923 300 THR A O 2307 C CB . THR A 298 ? 0.3164 0.4595 0.6578 -0.0424 0.0377 -0.0829 300 THR A CB 2308 O OG1 . THR A 298 ? 0.3694 0.5036 0.7102 -0.0453 0.0314 -0.0795 300 THR A OG1 2309 C CG2 . THR A 298 ? 0.3588 0.4894 0.6856 -0.0491 0.0407 -0.0789 300 THR A CG2 2310 N N . ASP A 299 ? 0.2576 0.3924 0.6124 -0.0174 0.0249 -0.0867 301 ASP A N 2311 C CA . ASP A 299 ? 0.2482 0.3929 0.6150 -0.0114 0.0195 -0.0872 301 ASP A CA 2312 C C . ASP A 299 ? 0.2436 0.3697 0.6041 -0.0048 0.0136 -0.0846 301 ASP A C 2313 O O . ASP A 299 ? 0.2139 0.3225 0.5622 -0.0062 0.0137 -0.0826 301 ASP A O 2314 C CB . ASP A 299 ? 0.2313 0.3857 0.6020 -0.0208 0.0168 -0.0849 301 ASP A CB 2315 C CG . ASP A 299 ? 0.2486 0.4228 0.6348 -0.0166 0.0124 -0.0860 301 ASP A CG 2316 O OD1 . ASP A 299 ? 0.2485 0.4354 0.6396 -0.0255 0.0109 -0.0853 301 ASP A OD1 2317 O OD2 . ASP A 299 ? 0.2303 0.4068 0.6234 -0.0049 0.0099 -0.0872 301 ASP A OD2 2318 N N . MET A 300 ? 0.2515 0.3826 0.6203 0.0022 0.0081 -0.0840 302 MET A N 2319 C CA . MET A 300 ? 0.2690 0.3832 0.6309 0.0071 0.0024 -0.0806 302 MET A CA 2320 C C . MET A 300 ? 0.2625 0.3643 0.6126 -0.0007 -0.0002 -0.0767 302 MET A C 2321 O O . MET A 300 ? 0.2877 0.3964 0.6390 -0.0076 -0.0016 -0.0761 302 MET A O 2322 C CB . MET A 300 ? 0.2830 0.4064 0.6560 0.0155 -0.0034 -0.0796 302 MET A CB 2323 C CG . MET A 300 ? 0.3317 0.4653 0.7167 0.0254 -0.0004 -0.0839 302 MET A CG 2324 S SD . MET A 300 ? 0.5114 0.6595 0.9122 0.0363 -0.0078 -0.0818 302 MET A SD 2325 C CE . MET A 300 ? 0.5079 0.6287 0.8943 0.0387 -0.0145 -0.0754 302 MET A CE 2326 N N . PRO A 301 ? 0.2670 0.3505 0.6054 -0.0001 -0.0005 -0.0745 303 PRO A N 2327 C CA . PRO A 301 ? 0.2491 0.3231 0.5772 -0.0076 -0.0011 -0.0718 303 PRO A CA 2328 C C . PRO A 301 ? 0.2375 0.3127 0.5654 -0.0090 -0.0071 -0.0698 303 PRO A C 2329 O O . PRO A 301 ? 0.2266 0.2974 0.5485 -0.0155 -0.0073 -0.0692 303 PRO A O 2330 C CB . PRO A 301 ? 0.2600 0.3169 0.5770 -0.0057 -0.0004 -0.0698 303 PRO A CB 2331 C CG . PRO A 301 ? 0.2734 0.3289 0.5945 0.0025 -0.0016 -0.0708 303 PRO A CG 2332 C CD . PRO A 301 ? 0.2532 0.3247 0.5867 0.0054 0.0011 -0.0751 303 PRO A CD 2333 N N . ASP A 302 ? 0.2192 0.2990 0.5525 -0.0027 -0.0120 -0.0687 304 ASP A N 2334 C CA . ASP A 302 ? 0.2210 0.3043 0.5534 -0.0045 -0.0178 -0.0669 304 ASP A CA 2335 C C . ASP A 302 ? 0.2239 0.3215 0.5623 -0.0121 -0.0179 -0.0695 304 ASP A C 2336 O O . ASP A 302 ? 0.2306 0.3268 0.5637 -0.0181 -0.0207 -0.0696 304 ASP A O 2337 C CB . ASP A 302 ? 0.2287 0.3169 0.5670 0.0039 -0.0235 -0.0642 304 ASP A CB 2338 C CG . ASP A 302 ? 0.2360 0.3362 0.5880 0.0108 -0.0223 -0.0661 304 ASP A CG 2339 O OD1 . ASP A 302 ? 0.2642 0.3586 0.6165 0.0141 -0.0175 -0.0683 304 ASP A OD1 2340 O OD2 . ASP A 302 ? 0.2107 0.3265 0.5729 0.0136 -0.0265 -0.0656 304 ASP A OD2 2341 N N . ILE A 303 ? 0.2133 0.3247 0.5624 -0.0121 -0.0145 -0.0720 305 ILE A N 2342 C CA . ILE A 303 ? 0.2178 0.3455 0.5745 -0.0200 -0.0141 -0.0743 305 ILE A CA 2343 C C . ILE A 303 ? 0.2218 0.3384 0.5687 -0.0305 -0.0101 -0.0749 305 ILE A C 2344 O O . ILE A 303 ? 0.2261 0.3444 0.5712 -0.0386 -0.0122 -0.0758 305 ILE A O 2345 C CB . ILE A 303 ? 0.2049 0.3531 0.5768 -0.0164 -0.0110 -0.0767 305 ILE A CB 2346 C CG1 . ILE A 303 ? 0.2097 0.3650 0.5906 -0.0042 -0.0155 -0.0756 305 ILE A CG1 2347 C CG2 . ILE A 303 ? 0.1981 0.3656 0.5785 -0.0256 -0.0108 -0.0786 305 ILE A CG2 2348 C CD1 . ILE A 303 ? 0.2179 0.3950 0.6161 0.0025 -0.0125 -0.0786 305 ILE A CD1 2349 N N . LEU A 304 ? 0.2063 0.3102 0.5460 -0.0301 -0.0050 -0.0742 306 LEU A N 2350 C CA . LEU A 304 ? 0.2215 0.3137 0.5520 -0.0387 -0.0015 -0.0736 306 LEU A CA 2351 C C . LEU A 304 ? 0.2363 0.3131 0.5562 -0.0410 -0.0051 -0.0726 306 LEU A C 2352 O O . LEU A 304 ? 0.2447 0.3172 0.5609 -0.0495 -0.0052 -0.0735 306 LEU A O 2353 C CB . LEU A 304 ? 0.2084 0.2917 0.5334 -0.0363 0.0039 -0.0723 306 LEU A CB 2354 C CG . LEU A 304 ? 0.1824 0.2811 0.5167 -0.0338 0.0083 -0.0746 306 LEU A CG 2355 C CD1 . LEU A 304 ? 0.1533 0.2435 0.4809 -0.0312 0.0129 -0.0741 306 LEU A CD1 2356 C CD2 . LEU A 304 ? 0.1916 0.3048 0.5323 -0.0428 0.0116 -0.0757 306 LEU A CD2 2357 N N . LEU A 305 ? 0.2357 0.3039 0.5504 -0.0336 -0.0078 -0.0710 307 LEU A N 2358 C CA . LEU A 305 ? 0.2307 0.2869 0.5357 -0.0343 -0.0109 -0.0706 307 LEU A CA 2359 C C . LEU A 305 ? 0.2354 0.2999 0.5427 -0.0396 -0.0153 -0.0733 307 LEU A C 2360 O O . LEU A 305 ? 0.2502 0.3064 0.5509 -0.0464 -0.0154 -0.0753 307 LEU A O 2361 C CB . LEU A 305 ? 0.2205 0.2721 0.5221 -0.0260 -0.0135 -0.0682 307 LEU A CB 2362 C CG . LEU A 305 ? 0.2143 0.2547 0.5051 -0.0259 -0.0157 -0.0676 307 LEU A CG 2363 C CD1 . LEU A 305 ? 0.2403 0.2661 0.5223 -0.0295 -0.0118 -0.0681 307 LEU A CD1 2364 C CD2 . LEU A 305 ? 0.1785 0.2152 0.4661 -0.0185 -0.0174 -0.0641 307 LEU A CD2 2365 N N . GLU A 306 ? 0.2269 0.3078 0.5438 -0.0367 -0.0192 -0.0734 308 GLU A N 2366 C CA . GLU A 306 ? 0.2389 0.3298 0.5576 -0.0412 -0.0245 -0.0754 308 GLU A CA 2367 C C . GLU A 306 ? 0.2428 0.3373 0.5634 -0.0526 -0.0227 -0.0787 308 GLU A C 2368 O O . GLU A 306 ? 0.2643 0.3564 0.5797 -0.0597 -0.0257 -0.0816 308 GLU A O 2369 C CB . GLU A 306 ? 0.2250 0.3345 0.5551 -0.0347 -0.0291 -0.0738 308 GLU A CB 2370 C CG . GLU A 306 ? 0.2581 0.3835 0.5928 -0.0401 -0.0350 -0.0756 308 GLU A CG 2371 C CD . GLU A 306 ? 0.3496 0.4675 0.6723 -0.0418 -0.0398 -0.0760 308 GLU A CD 2372 O OE1 . GLU A 306 ? 0.4175 0.5436 0.7393 -0.0494 -0.0438 -0.0790 308 GLU A OE1 2373 O OE2 . GLU A 306 ? 0.3743 0.4790 0.6880 -0.0362 -0.0396 -0.0736 308 GLU A OE2 2374 N N . LEU A 307 ? 0.2367 0.3360 0.5637 -0.0551 -0.0176 -0.0784 309 LEU A N 2375 C CA . LEU A 307 ? 0.2368 0.3438 0.5681 -0.0669 -0.0162 -0.0806 309 LEU A CA 2376 C C . LEU A 307 ? 0.2547 0.3420 0.5760 -0.0732 -0.0114 -0.0800 309 LEU A C 2377 O O . LEU A 307 ? 0.2596 0.3494 0.5828 -0.0833 -0.0090 -0.0806 309 LEU A O 2378 C CB . LEU A 307 ? 0.2141 0.3447 0.5607 -0.0664 -0.0142 -0.0805 309 LEU A CB 2379 C CG . LEU A 307 ? 0.1809 0.3327 0.5390 -0.0601 -0.0200 -0.0808 309 LEU A CG 2380 C CD1 . LEU A 307 ? 0.1564 0.3323 0.5306 -0.0593 -0.0172 -0.0813 309 LEU A CD1 2381 C CD2 . LEU A 307 ? 0.1486 0.3068 0.5054 -0.0679 -0.0268 -0.0830 309 LEU A CD2 2382 N N . GLY A 308 ? 0.2671 0.3351 0.5777 -0.0672 -0.0102 -0.0783 310 GLY A N 2383 C CA . GLY A 308 ? 0.2977 0.3442 0.5973 -0.0719 -0.0071 -0.0775 310 GLY A CA 2384 C C . GLY A 308 ? 0.2993 0.3438 0.5996 -0.0738 -0.0014 -0.0740 310 GLY A C 2385 O O . GLY A 308 ? 0.2920 0.3233 0.5861 -0.0808 0.0009 -0.0727 310 GLY A O 2386 N N . GLN A 309 ? 0.2758 0.3332 0.5833 -0.0679 0.0008 -0.0726 311 GLN A N 2387 C CA . GLN A 309 ? 0.2770 0.3350 0.5845 -0.0701 0.0063 -0.0698 311 GLN A CA 2388 C C . GLN A 309 ? 0.2774 0.3210 0.5762 -0.0629 0.0081 -0.0667 311 GLN A C 2389 O O . GLN A 309 ? 0.2812 0.3317 0.5831 -0.0558 0.0094 -0.0666 311 GLN A O 2390 C CB . GLN A 309 ? 0.2764 0.3573 0.5961 -0.0681 0.0085 -0.0712 311 GLN A CB 2391 C CG . GLN A 309 ? 0.3292 0.4289 0.6597 -0.0743 0.0065 -0.0740 311 GLN A CG 2392 C CD . GLN A 309 ? 0.3852 0.4812 0.7128 -0.0885 0.0082 -0.0731 311 GLN A CD 2393 O OE1 . GLN A 309 ? 0.3819 0.4751 0.7083 -0.0953 0.0043 -0.0751 311 GLN A OE1 2394 N NE2 . GLN A 309 ? 0.3527 0.4472 0.6776 -0.0934 0.0138 -0.0701 311 GLN A NE2 2395 N N . PHE A 310 ? 0.2532 0.2772 0.5415 -0.0645 0.0081 -0.0644 312 PHE A N 2396 C CA . PHE A 310 ? 0.2484 0.2609 0.5293 -0.0580 0.0094 -0.0610 312 PHE A CA 2397 C C . PHE A 310 ? 0.2745 0.2680 0.5459 -0.0620 0.0106 -0.0574 312 PHE A C 2398 O O . PHE A 310 ? 0.2841 0.2709 0.5541 -0.0693 0.0099 -0.0586 312 PHE A O 2399 C CB . PHE A 310 ? 0.2094 0.2189 0.4886 -0.0490 0.0060 -0.0622 312 PHE A CB 2400 C CG . PHE A 310 ? 0.2267 0.2323 0.5043 -0.0498 0.0022 -0.0654 312 PHE A CG 2401 C CD1 . PHE A 310 ? 0.2282 0.2172 0.4974 -0.0512 0.0019 -0.0654 312 PHE A CD1 2402 C CD2 . PHE A 310 ? 0.2502 0.2690 0.5347 -0.0493 -0.0012 -0.0686 312 PHE A CD2 2403 C CE1 . PHE A 310 ? 0.2377 0.2226 0.5040 -0.0522 -0.0014 -0.0696 312 PHE A CE1 2404 C CE2 . PHE A 310 ? 0.2238 0.2400 0.5055 -0.0508 -0.0051 -0.0718 312 PHE A CE2 2405 C CZ . PHE A 310 ? 0.2133 0.2122 0.4852 -0.0526 -0.0049 -0.0728 312 PHE A CZ 2406 N N . LYS A 311 ? 0.2606 0.2454 0.5257 -0.0571 0.0119 -0.0532 313 LYS A N 2407 C CA . LYS A 311 ? 0.2706 0.2376 0.5274 -0.0594 0.0128 -0.0488 313 LYS A CA 2408 C C . LYS A 311 ? 0.2717 0.2242 0.5245 -0.0575 0.0101 -0.0517 313 LYS A C 2409 O O . LYS A 311 ? 0.2954 0.2494 0.5482 -0.0502 0.0080 -0.0543 313 LYS A O 2410 C CB . LYS A 311 ? 0.2648 0.2285 0.5168 -0.0532 0.0138 -0.0437 313 LYS A CB 2411 C CG . LYS A 311 ? 0.2721 0.2183 0.5162 -0.0538 0.0143 -0.0378 313 LYS A CG 2412 C CD . LYS A 311 ? 0.2687 0.2163 0.5094 -0.0466 0.0143 -0.0332 313 LYS A CD 2413 C CE . LYS A 311 ? 0.2874 0.2193 0.5211 -0.0449 0.0141 -0.0264 313 LYS A CE 2414 N NZ . LYS A 311 ? 0.2944 0.2196 0.5244 -0.0539 0.0160 -0.0209 313 LYS A NZ 2415 N N . LYS A 312 ? 0.2534 0.1925 0.5025 -0.0642 0.0101 -0.0517 314 LYS A N 2416 C CA . LYS A 312 ? 0.2896 0.2137 0.5339 -0.0624 0.0080 -0.0558 314 LYS A CA 2417 C C . LYS A 312 ? 0.3064 0.2138 0.5437 -0.0547 0.0087 -0.0518 314 LYS A C 2418 O O . LYS A 312 ? 0.3325 0.2274 0.5656 -0.0574 0.0102 -0.0462 314 LYS A O 2419 C CB . LYS A 312 ? 0.3084 0.2227 0.5511 -0.0735 0.0076 -0.0586 314 LYS A CB 2420 C CG . LYS A 312 ? 0.3366 0.2705 0.5877 -0.0822 0.0065 -0.0627 314 LYS A CG 2421 C CD . LYS A 312 ? 0.4099 0.3611 0.6666 -0.0758 0.0037 -0.0674 314 LYS A CD 2422 C CE . LYS A 312 ? 0.4667 0.4374 0.7324 -0.0831 0.0019 -0.0710 314 LYS A CE 2423 N NZ . LYS A 312 ? 0.5130 0.5002 0.7864 -0.0840 0.0048 -0.0674 314 LYS A NZ 2424 N N . THR A 313 ? 0.2912 0.1999 0.5274 -0.0452 0.0076 -0.0538 315 THR A N 2425 C CA . THR A 313 ? 0.2894 0.1874 0.5210 -0.0364 0.0083 -0.0500 315 THR A CA 2426 C C . THR A 313 ? 0.2949 0.1965 0.5260 -0.0283 0.0072 -0.0547 315 THR A C 2427 O O . THR A 313 ? 0.3010 0.2119 0.5343 -0.0301 0.0056 -0.0600 315 THR A O 2428 C CB . THR A 313 ? 0.3038 0.2101 0.5367 -0.0339 0.0094 -0.0426 315 THR A CB 2429 O OG1 . THR A 313 ? 0.3134 0.2092 0.5423 -0.0262 0.0096 -0.0380 315 THR A OG1 2430 C CG2 . THR A 313 ? 0.1978 0.1237 0.4357 -0.0310 0.0088 -0.0439 315 THR A CG2 2431 N N . GLN A 314 ? 0.2997 0.1956 0.5281 -0.0195 0.0078 -0.0525 316 GLN A N 2432 C CA . GLN A 314 ? 0.2925 0.1929 0.5199 -0.0122 0.0074 -0.0571 316 GLN A CA 2433 C C . GLN A 314 ? 0.2778 0.1965 0.5093 -0.0091 0.0067 -0.0541 316 GLN A C 2434 O O . GLN A 314 ? 0.2582 0.1819 0.4919 -0.0093 0.0071 -0.0483 316 GLN A O 2435 C CB . GLN A 314 ? 0.2907 0.1785 0.5143 -0.0031 0.0088 -0.0565 316 GLN A CB 2436 C CG . GLN A 314 ? 0.3460 0.2106 0.5646 -0.0045 0.0096 -0.0589 316 GLN A CG 2437 C CD . GLN A 314 ? 0.3858 0.2397 0.6040 -0.0096 0.0098 -0.0515 316 GLN A CD 2438 O OE1 . GLN A 314 ? 0.3250 0.1853 0.5453 -0.0075 0.0099 -0.0434 316 GLN A OE1 2439 N NE2 . GLN A 314 ? 0.3932 0.2317 0.6081 -0.0177 0.0097 -0.0542 316 GLN A NE2 2440 N N . ILE A 315 ? 0.2671 0.1952 0.4989 -0.0067 0.0057 -0.0580 317 ILE A N 2441 C CA . ILE A 315 ? 0.2430 0.1857 0.4779 -0.0041 0.0050 -0.0548 317 ILE A CA 2442 C C . ILE A 315 ? 0.2529 0.1999 0.4857 0.0025 0.0054 -0.0562 317 ILE A C 2443 O O . ILE A 315 ? 0.2541 0.1959 0.4831 0.0041 0.0059 -0.0616 317 ILE A O 2444 C CB . ILE A 315 ? 0.2452 0.1990 0.4839 -0.0089 0.0030 -0.0563 317 ILE A CB 2445 C CG1 . ILE A 315 ? 0.2592 0.2137 0.4963 -0.0113 0.0012 -0.0625 317 ILE A CG1 2446 C CG2 . ILE A 315 ? 0.2252 0.1802 0.4676 -0.0146 0.0033 -0.0543 317 ILE A CG2 2447 C CD1 . ILE A 315 ? 0.2934 0.2612 0.5349 -0.0136 -0.0016 -0.0626 317 ILE A CD1 2448 N N . LEU A 316 ? 0.2319 0.1890 0.4667 0.0057 0.0054 -0.0517 318 LEU A N 2449 C CA . LEU A 316 ? 0.2218 0.1872 0.4555 0.0106 0.0058 -0.0521 318 LEU A CA 2450 C C . LEU A 316 ? 0.2055 0.1831 0.4413 0.0074 0.0037 -0.0499 318 LEU A C 2451 O O . LEU A 316 ? 0.1999 0.1810 0.4387 0.0054 0.0030 -0.0458 318 LEU A O 2452 C CB . LEU A 316 ? 0.2224 0.1887 0.4569 0.0171 0.0076 -0.0479 318 LEU A CB 2453 C CG . LEU A 316 ? 0.2705 0.2464 0.5046 0.0232 0.0091 -0.0484 318 LEU A CG 2454 C CD1 . LEU A 316 ? 0.3145 0.2912 0.5512 0.0304 0.0106 -0.0440 318 LEU A CD1 2455 C CD2 . LEU A 316 ? 0.2720 0.2625 0.5078 0.0201 0.0076 -0.0453 318 LEU A CD2 2456 N N . VAL A 317 ? 0.1825 0.1657 0.4163 0.0069 0.0027 -0.0525 319 VAL A N 2457 C CA . VAL A 317 ? 0.1842 0.1758 0.4197 0.0036 0.0001 -0.0502 319 VAL A CA 2458 C C . VAL A 317 ? 0.1843 0.1848 0.4167 0.0057 0.0003 -0.0491 319 VAL A C 2459 O O . VAL A 317 ? 0.1906 0.1912 0.4190 0.0086 0.0020 -0.0529 319 VAL A O 2460 C CB . VAL A 317 ? 0.1814 0.1716 0.4174 -0.0003 -0.0024 -0.0535 319 VAL A CB 2461 C CG1 . VAL A 317 ? 0.1633 0.1601 0.4019 -0.0023 -0.0053 -0.0506 319 VAL A CG1 2462 C CG2 . VAL A 317 ? 0.1744 0.1569 0.4132 -0.0031 -0.0018 -0.0553 319 VAL A CG2 2463 N N . GLY A 318 ? 0.1887 0.1965 0.4225 0.0040 -0.0011 -0.0444 320 GLY A N 2464 C CA . GLY A 318 ? 0.1815 0.1988 0.4119 0.0044 -0.0010 -0.0426 320 GLY A CA 2465 C C . GLY A 318 ? 0.1899 0.2117 0.4211 0.0005 -0.0036 -0.0375 320 GLY A C 2466 O O . GLY A 318 ? 0.2026 0.2197 0.4372 -0.0017 -0.0053 -0.0359 320 GLY A O 2467 N N . VAL A 319 ? 0.1684 0.1987 0.3959 -0.0006 -0.0038 -0.0349 321 VAL A N 2468 C CA . VAL A 319 ? 0.1670 0.1996 0.3940 -0.0050 -0.0066 -0.0293 321 VAL A CA 2469 C C . VAL A 319 ? 0.1829 0.2274 0.4069 -0.0061 -0.0047 -0.0259 321 VAL A C 2470 O O . VAL A 319 ? 0.1852 0.2364 0.4073 -0.0025 -0.0014 -0.0288 321 VAL A O 2471 C CB . VAL A 319 ? 0.1628 0.1923 0.3874 -0.0069 -0.0105 -0.0290 321 VAL A CB 2472 C CG1 . VAL A 319 ? 0.1441 0.1646 0.3733 -0.0061 -0.0122 -0.0323 321 VAL A CG1 2473 C CG2 . VAL A 319 ? 0.1000 0.1354 0.3187 -0.0056 -0.0095 -0.0322 321 VAL A CG2 2474 N N . ASN A 320 ? 0.1800 0.2268 0.4036 -0.0111 -0.0067 -0.0199 322 ASN A N 2475 C CA . ASN A 320 ? 0.1927 0.2522 0.4140 -0.0140 -0.0051 -0.0154 322 ASN A CA 2476 C C . ASN A 320 ? 0.2246 0.2861 0.4396 -0.0176 -0.0073 -0.0120 322 ASN A C 2477 O O . ASN A 320 ? 0.2232 0.2749 0.4370 -0.0188 -0.0113 -0.0110 322 ASN A O 2478 C CB . ASN A 320 ? 0.1901 0.2499 0.4145 -0.0191 -0.0062 -0.0106 322 ASN A CB 2479 C CG . ASN A 320 ? 0.2100 0.2700 0.4399 -0.0159 -0.0044 -0.0131 322 ASN A CG 2480 O OD1 . ASN A 320 ? 0.1948 0.2538 0.4263 -0.0096 -0.0022 -0.0178 322 ASN A OD1 2481 N ND2 . ASN A 320 ? 0.1684 0.2287 0.4006 -0.0206 -0.0057 -0.0099 322 ASN A ND2 2482 N N . LYS A 321 ? 0.2295 0.3050 0.4407 -0.0193 -0.0046 -0.0096 323 LYS A N 2483 C CA . LYS A 321 ? 0.2228 0.3026 0.4264 -0.0228 -0.0062 -0.0060 323 LYS A CA 2484 C C . LYS A 321 ? 0.2235 0.2949 0.4253 -0.0294 -0.0113 0.0018 323 LYS A C 2485 O O . LYS A 321 ? 0.2036 0.2712 0.4002 -0.0306 -0.0149 0.0044 323 LYS A O 2486 C CB . LYS A 321 ? 0.2376 0.3364 0.4378 -0.0240 -0.0016 -0.0047 323 LYS A CB 2487 C CG . LYS A 321 ? 0.2631 0.3694 0.4543 -0.0297 -0.0029 0.0011 323 LYS A CG 2488 C CD . LYS A 321 ? 0.3266 0.4547 0.5150 -0.0310 0.0029 0.0019 323 LYS A CD 2489 C CE . LYS A 321 ? 0.4238 0.5591 0.6017 -0.0380 0.0013 0.0087 323 LYS A CE 2490 N NZ . LYS A 321 ? 0.5391 0.6977 0.7125 -0.0395 0.0073 0.0090 323 LYS A NZ 2491 N N . ASP A 322 ? 0.2042 0.2722 0.4097 -0.0338 -0.0121 0.0059 324 ASP A N 2492 C CA . ASP A 322 ? 0.2403 0.2965 0.4436 -0.0398 -0.0171 0.0129 324 ASP A CA 2493 C C . ASP A 322 ? 0.2304 0.2703 0.4394 -0.0389 -0.0195 0.0108 324 ASP A C 2494 O O . ASP A 322 ? 0.2779 0.3122 0.4875 -0.0447 -0.0209 0.0146 324 ASP A O 2495 C CB . ASP A 322 ? 0.2350 0.2997 0.4344 -0.0491 -0.0167 0.0213 324 ASP A CB 2496 C CG . ASP A 322 ? 0.2614 0.3446 0.4546 -0.0506 -0.0136 0.0236 324 ASP A CG 2497 O OD1 . ASP A 322 ? 0.2432 0.3250 0.4293 -0.0523 -0.0162 0.0277 324 ASP A OD1 2498 O OD2 . ASP A 322 ? 0.2415 0.3419 0.4366 -0.0501 -0.0086 0.0217 324 ASP A OD2 2499 N N . GLU A 323 ? 0.2140 0.2468 0.4267 -0.0325 -0.0200 0.0046 325 GLU A N 2500 C CA . GLU A 323 ? 0.2323 0.2518 0.4501 -0.0310 -0.0215 0.0018 325 GLU A CA 2501 C C . GLU A 323 ? 0.2544 0.2600 0.4709 -0.0355 -0.0257 0.0070 325 GLU A C 2502 O O . GLU A 323 ? 0.2867 0.2845 0.5055 -0.0377 -0.0258 0.0057 325 GLU A O 2503 C CB . GLU A 323 ? 0.2228 0.2375 0.4437 -0.0243 -0.0223 -0.0040 325 GLU A CB 2504 C CG . GLU A 323 ? 0.2373 0.2599 0.4602 -0.0197 -0.0182 -0.0107 325 GLU A CG 2505 C CD . GLU A 323 ? 0.2596 0.2816 0.4870 -0.0191 -0.0154 -0.0136 325 GLU A CD 2506 O OE1 . GLU A 323 ? 0.2661 0.2825 0.4949 -0.0225 -0.0165 -0.0118 325 GLU A OE1 2507 O OE2 . GLU A 323 ? 0.2744 0.3010 0.5034 -0.0153 -0.0124 -0.0178 325 GLU A OE2 2508 N N . GLY A 324 ? 0.2549 0.2563 0.4671 -0.0365 -0.0295 0.0127 326 GLY A N 2509 C CA . GLY A 324 ? 0.2452 0.2297 0.4569 -0.0384 -0.0340 0.0171 326 GLY A CA 2510 C C . GLY A 324 ? 0.2573 0.2366 0.4645 -0.0478 -0.0350 0.0239 326 GLY A C 2511 O O . GLY A 324 ? 0.2833 0.2454 0.4902 -0.0495 -0.0383 0.0264 326 GLY A O 2512 N N . THR A 325 ? 0.2341 0.2282 0.4382 -0.0539 -0.0322 0.0270 327 THR A N 2513 C CA . THR A 325 ? 0.2528 0.2443 0.4522 -0.0645 -0.0334 0.0347 327 THR A CA 2514 C C . THR A 325 ? 0.2696 0.2482 0.4713 -0.0692 -0.0340 0.0323 327 THR A C 2515 O O . THR A 325 ? 0.2927 0.2560 0.4905 -0.0762 -0.0373 0.0377 327 THR A O 2516 C CB . THR A 325 ? 0.2329 0.2465 0.4295 -0.0703 -0.0297 0.0383 327 THR A CB 2517 O OG1 . THR A 325 ? 0.2343 0.2614 0.4367 -0.0666 -0.0252 0.0311 327 THR A OG1 2518 C CG2 . THR A 325 ? 0.1942 0.2189 0.3855 -0.0678 -0.0294 0.0416 327 THR A CG2 2519 N N . ALA A 326 ? 0.2604 0.2443 0.4674 -0.0659 -0.0310 0.0245 328 ALA A N 2520 C CA . ALA A 326 ? 0.2859 0.2609 0.4943 -0.0706 -0.0313 0.0212 328 ALA A CA 2521 C C . ALA A 326 ? 0.3145 0.2635 0.5212 -0.0702 -0.0354 0.0210 328 ALA A C 2522 O O . ALA A 326 ? 0.3068 0.2435 0.5107 -0.0780 -0.0371 0.0219 328 ALA A O 2523 C CB . ALA A 326 ? 0.2531 0.2346 0.4670 -0.0643 -0.0283 0.0126 328 ALA A CB 2524 N N . PHE A 327 ? 0.3027 0.2436 0.5113 -0.0610 -0.0370 0.0197 329 PHE A N 2525 C CA . PHE A 327 ? 0.3181 0.2351 0.5273 -0.0577 -0.0402 0.0179 329 PHE A CA 2526 C C . PHE A 327 ? 0.3399 0.2409 0.5435 -0.0625 -0.0448 0.0269 329 PHE A C 2527 O O . PHE A 327 ? 0.3682 0.2468 0.5714 -0.0611 -0.0476 0.0260 329 PHE A O 2528 C CB . PHE A 327 ? 0.2921 0.2087 0.5076 -0.0455 -0.0400 0.0122 329 PHE A CB 2529 C CG . PHE A 327 ? 0.2879 0.2188 0.5082 -0.0417 -0.0355 0.0039 329 PHE A CG 2530 C CD1 . PHE A 327 ? 0.2627 0.2122 0.4840 -0.0393 -0.0331 0.0040 329 PHE A CD1 2531 C CD2 . PHE A 327 ? 0.2664 0.1911 0.4891 -0.0410 -0.0335 -0.0039 329 PHE A CD2 2532 C CE1 . PHE A 327 ? 0.2540 0.2139 0.4791 -0.0361 -0.0293 -0.0025 329 PHE A CE1 2533 C CE2 . PHE A 327 ? 0.2453 0.1823 0.4714 -0.0383 -0.0297 -0.0100 329 PHE A CE2 2534 C CZ . PHE A 327 ? 0.2558 0.2097 0.4833 -0.0357 -0.0278 -0.0089 329 PHE A CZ 2535 N N . LEU A 328 ? 0.3545 0.2662 0.5533 -0.0684 -0.0455 0.0357 330 LEU A N 2536 C CA . LEU A 328 ? 0.3883 0.2855 0.5808 -0.0729 -0.0502 0.0462 330 LEU A CA 2537 C C . LEU A 328 ? 0.4242 0.3050 0.6118 -0.0846 -0.0518 0.0494 330 LEU A C 2538 O O . LEU A 328 ? 0.4320 0.2899 0.6154 -0.0867 -0.0564 0.0557 330 LEU A O 2539 C CB . LEU A 328 ? 0.3880 0.3033 0.5756 -0.0763 -0.0502 0.0550 330 LEU A CB 2540 C CG . LEU A 328 ? 0.3654 0.2984 0.5560 -0.0665 -0.0486 0.0518 330 LEU A CG 2541 C CD1 . LEU A 328 ? 0.3130 0.2638 0.4968 -0.0718 -0.0480 0.0598 330 LEU A CD1 2542 C CD2 . LEU A 328 ? 0.3201 0.2396 0.5136 -0.0568 -0.0529 0.0516 330 LEU A CD2 2543 N N . VAL A 329 ? 0.4209 0.3127 0.6090 -0.0923 -0.0485 0.0454 331 VAL A N 2544 C CA . VAL A 329 ? 0.4349 0.3139 0.6182 -0.1054 -0.0500 0.0478 331 VAL A CA 2545 C C . VAL A 329 ? 0.4650 0.3214 0.6495 -0.1034 -0.0508 0.0387 331 VAL A C 2546 O O . VAL A 329 ? 0.4989 0.3418 0.6788 -0.1145 -0.0522 0.0388 331 VAL A O 2547 C CB . VAL A 329 ? 0.4400 0.3432 0.6231 -0.1163 -0.0467 0.0488 331 VAL A CB 2548 C CG1 . VAL A 329 ? 0.4250 0.3491 0.6054 -0.1199 -0.0456 0.0584 331 VAL A CG1 2549 C CG2 . VAL A 329 ? 0.3637 0.2841 0.5537 -0.1104 -0.0424 0.0379 331 VAL A CG2 2550 N N . TYR A 330 ? 0.4633 0.3152 0.6534 -0.0900 -0.0499 0.0306 332 TYR A N 2551 C CA . TYR A 330 ? 0.4750 0.3041 0.6662 -0.0857 -0.0505 0.0216 332 TYR A CA 2552 C C . TYR A 330 ? 0.5114 0.3164 0.7029 -0.0772 -0.0544 0.0244 332 TYR A C 2553 O O . TYR A 330 ? 0.5361 0.3301 0.7323 -0.0665 -0.0539 0.0162 332 TYR A O 2554 C CB . TYR A 330 ? 0.4475 0.2895 0.6454 -0.0766 -0.0463 0.0103 332 TYR A CB 2555 C CG . TYR A 330 ? 0.4416 0.3035 0.6392 -0.0844 -0.0431 0.0071 332 TYR A CG 2556 C CD1 . TYR A 330 ? 0.3871 0.2757 0.5870 -0.0849 -0.0408 0.0111 332 TYR A CD1 2557 C CD2 . TYR A 330 ? 0.4316 0.2861 0.6265 -0.0911 -0.0424 0.0000 332 TYR A CD2 2558 C CE1 . TYR A 330 ? 0.3635 0.2709 0.5641 -0.0909 -0.0383 0.0091 332 TYR A CE1 2559 C CE2 . TYR A 330 ? 0.3794 0.2542 0.5744 -0.0980 -0.0401 -0.0022 332 TYR A CE2 2560 C CZ . TYR A 330 ? 0.3956 0.2966 0.5940 -0.0976 -0.0382 0.0029 332 TYR A CZ 2561 O OH . TYR A 330 ? 0.3216 0.2429 0.5210 -0.1032 -0.0364 0.0016 332 TYR A OH 2562 N N . GLY A 331 ? 0.5342 0.3314 0.7208 -0.0813 -0.0585 0.0364 333 GLY A N 2563 C CA . GLY A 331 ? 0.5423 0.3115 0.7281 -0.0749 -0.0631 0.0398 333 GLY A CA 2564 C C . GLY A 331 ? 0.5535 0.3235 0.7380 -0.0710 -0.0673 0.0522 333 GLY A C 2565 O O . GLY A 331 ? 0.5892 0.3347 0.7722 -0.0668 -0.0720 0.0572 333 GLY A O 2566 N N . ALA A 332 ? 0.4593 0.3581 0.6902 -0.0642 -0.1596 -0.0562 334 ALA A N 2567 C CA . ALA A 332 ? 0.4561 0.3230 0.6902 -0.0642 -0.1611 -0.0341 334 ALA A CA 2568 C C . ALA A 332 ? 0.4878 0.3263 0.7426 -0.0803 -0.1776 -0.0173 334 ALA A C 2569 O O . ALA A 332 ? 0.4735 0.3259 0.7303 -0.0942 -0.1776 -0.0073 334 ALA A O 2570 C CB . ALA A 332 ? 0.4233 0.3075 0.6356 -0.0629 -0.1420 -0.0097 334 ALA A CB 2571 N N . PRO A 333 ? 0.5057 0.3060 0.7808 -0.0798 -0.1944 -0.0122 335 PRO A N 2572 C CA . PRO A 333 ? 0.5370 0.3087 0.8403 -0.0989 -0.2156 0.0076 335 PRO A CA 2573 C C . PRO A 333 ? 0.5267 0.3168 0.8182 -0.1164 -0.2054 0.0521 335 PRO A C 2574 O O . PRO A 333 ? 0.5167 0.3237 0.7850 -0.1101 -0.1895 0.0667 335 PRO A O 2575 C CB . PRO A 333 ? 0.5540 0.2826 0.8839 -0.0917 -0.2370 0.0057 335 PRO A CB 2576 C CG . PRO A 333 ? 0.5498 0.2897 0.8601 -0.0703 -0.2232 -0.0078 335 PRO A CG 2577 C CD . PRO A 333 ? 0.5102 0.2945 0.7875 -0.0637 -0.1971 -0.0203 335 PRO A CD 2578 N N . GLY A 334 ? 0.5515 0.3463 0.8590 -0.1374 -0.2137 0.0697 336 GLY A N 2579 C CA . GLY A 334 ? 0.5507 0.3774 0.8497 -0.1543 -0.2028 0.1101 336 GLY A CA 2580 C C . GLY A 334 ? 0.5302 0.4052 0.8059 -0.1509 -0.1787 0.1073 336 GLY A C 2581 O O . GLY A 334 ? 0.5366 0.4471 0.8095 -0.1630 -0.1692 0.1351 336 GLY A O 2582 N N . PHE A 335 ? 0.4913 0.3728 0.7541 -0.1348 -0.1702 0.0759 337 PHE A N 2583 C CA . PHE A 335 ? 0.4673 0.3902 0.7145 -0.1302 -0.1519 0.0741 337 PHE A CA 2584 C C . PHE A 335 ? 0.4774 0.4149 0.7391 -0.1424 -0.1602 0.0674 337 PHE A C 2585 O O . PHE A 335 ? 0.5228 0.4364 0.8016 -0.1479 -0.1793 0.0476 337 PHE A O 2586 C CB . PHE A 335 ? 0.4282 0.3565 0.6559 -0.1098 -0.1398 0.0528 337 PHE A CB 2587 C CG . PHE A 335 ? 0.4304 0.3564 0.6427 -0.0985 -0.1283 0.0614 337 PHE A CG 2588 C CD1 . PHE A 335 ? 0.3726 0.2697 0.5844 -0.0924 -0.1353 0.0560 337 PHE A CD1 2589 C CD2 . PHE A 335 ? 0.3810 0.3356 0.5831 -0.0936 -0.1127 0.0734 337 PHE A CD2 2590 C CE1 . PHE A 335 ? 0.4141 0.3129 0.6116 -0.0836 -0.1266 0.0636 337 PHE A CE1 2591 C CE2 . PHE A 335 ? 0.3951 0.3492 0.5845 -0.0834 -0.1046 0.0761 337 PHE A CE2 2592 C CZ . PHE A 335 ? 0.3579 0.2850 0.5430 -0.0793 -0.1113 0.0717 337 PHE A CZ 2593 N N . SER A 336 ? 0.4415 0.4188 0.7001 -0.1459 -0.1482 0.0814 338 SER A N 2594 C CA . SER A 336 ? 0.4439 0.4421 0.7167 -0.1584 -0.1566 0.0772 338 SER A CA 2595 C C . SER A 336 ? 0.4077 0.4526 0.6743 -0.1527 -0.1406 0.0882 338 SER A C 2596 O O . SER A 336 ? 0.4213 0.4851 0.6851 -0.1488 -0.1274 0.1064 338 SER A O 2597 C CB . SER A 336 ? 0.4748 0.4636 0.7762 -0.1840 -0.1744 0.0950 338 SER A CB 2598 O OG . SER A 336 ? 0.4713 0.4863 0.7893 -0.1988 -0.1830 0.0935 338 SER A OG 2599 N N . LYS A 337 ? 0.3922 0.4603 0.6587 -0.1514 -0.1427 0.0768 339 LYS A N 2600 C CA . LYS A 337 ? 0.3576 0.4690 0.6266 -0.1460 -0.1311 0.0914 339 LYS A CA 2601 C C . LYS A 337 ? 0.3703 0.5100 0.6612 -0.1629 -0.1327 0.1130 339 LYS A C 2602 O O . LYS A 337 ? 0.3516 0.5308 0.6495 -0.1564 -0.1216 0.1263 339 LYS A O 2603 C CB . LYS A 337 ? 0.3507 0.4872 0.6165 -0.1427 -0.1355 0.0808 339 LYS A CB 2604 C CG . LYS A 337 ? 0.3122 0.4642 0.5914 -0.1615 -0.1529 0.0724 339 LYS A CG 2605 C CD . LYS A 337 ? 0.3164 0.5099 0.5898 -0.1571 -0.1548 0.0691 339 LYS A CD 2606 C CE . LYS A 337 ? 0.2674 0.4902 0.5557 -0.1763 -0.1724 0.0625 339 LYS A CE 2607 N NZ . LYS A 337 ? 0.3081 0.5515 0.6221 -0.1874 -0.1705 0.0882 339 LYS A NZ 2608 N N . ASP A 338 ? 0.3842 0.5055 0.6904 -0.1847 -0.1481 0.1172 340 ASP A N 2609 C CA . ASP A 338 ? 0.3866 0.5416 0.7188 -0.2068 -0.1533 0.1401 340 ASP A CA 2610 C C . ASP A 338 ? 0.4038 0.5665 0.7440 -0.2183 -0.1480 0.1691 340 ASP A C 2611 O O . ASP A 338 ? 0.4030 0.5936 0.7685 -0.2425 -0.1551 0.1930 340 ASP A O 2612 C CB . ASP A 338 ? 0.4057 0.5463 0.7595 -0.2296 -0.1788 0.1296 340 ASP A CB 2613 C CG . ASP A 338 ? 0.3933 0.5488 0.7395 -0.2221 -0.1840 0.1044 340 ASP A CG 2614 O OD1 . ASP A 338 ? 0.4335 0.5591 0.7752 -0.2216 -0.1986 0.0751 340 ASP A OD1 2615 O OD2 . ASP A 338 ? 0.3708 0.5719 0.7156 -0.2147 -0.1735 0.1133 340 ASP A OD2 2616 N N . ASN A 339 ? 0.3896 0.5333 0.7090 -0.2031 -0.1368 0.1687 341 ASN A N 2617 C CA . ASN A 339 ? 0.4135 0.5786 0.7317 -0.2090 -0.1276 0.1955 341 ASN A CA 2618 C C . ASN A 339 ? 0.4091 0.5722 0.6990 -0.1812 -0.1093 0.1833 341 ASN A C 2619 O O . ASN A 339 ? 0.3941 0.5368 0.6702 -0.1599 -0.1050 0.1580 341 ASN A O 2620 C CB . ASN A 339 ? 0.4441 0.5750 0.7785 -0.2349 -0.1480 0.2164 341 ASN A CB 2621 C CG . ASN A 339 ? 0.4682 0.5337 0.7917 -0.2244 -0.1591 0.1965 341 ASN A CG 2622 O OD1 . ASN A 339 ? 0.4518 0.5082 0.7491 -0.1996 -0.1456 0.1778 341 ASN A OD1 2623 N ND2 . ASN A 339 ? 0.5597 0.5798 0.9077 -0.2425 -0.1853 0.1994 341 ASN A ND2 2624 N N . ASN A 340 ? 0.4247 0.6127 0.7072 -0.1831 -0.1001 0.2020 342 ASN A N 2625 C CA . ASN A 340 ? 0.4278 0.6266 0.6866 -0.1576 -0.0830 0.1885 342 ASN A CA 2626 C C . ASN A 340 ? 0.4344 0.5791 0.6740 -0.1488 -0.0886 0.1769 342 ASN A C 2627 O O . ASN A 340 ? 0.4345 0.5828 0.6555 -0.1286 -0.0773 0.1631 342 ASN A O 2628 C CB . ASN A 340 ? 0.4447 0.7147 0.7015 -0.1588 -0.0674 0.2066 342 ASN A CB 2629 C CG . ASN A 340 ? 0.5107 0.7927 0.7685 -0.1854 -0.0753 0.2422 342 ASN A CG 2630 O OD1 . ASN A 340 ? 0.5646 0.7913 0.8267 -0.2003 -0.0944 0.2526 342 ASN A OD1 2631 N ND2 . ASN A 340 ? 0.6010 0.9614 0.8583 -0.1915 -0.0618 0.2628 342 ASN A ND2 2632 N N . SER A 341 ? 0.4431 0.5395 0.6913 -0.1632 -0.1078 0.1804 343 SER A N 2633 C CA . SER A 341 ? 0.4408 0.4847 0.6777 -0.1526 -0.1155 0.1640 343 SER A CA 2634 C C . SER A 341 ? 0.4616 0.5114 0.6805 -0.1467 -0.1097 0.1741 343 SER A C 2635 O O . SER A 341 ? 0.4476 0.4746 0.6499 -0.1280 -0.1059 0.1542 343 SER A O 2636 C CB . SER A 341 ? 0.4059 0.4351 0.6324 -0.1310 -0.1089 0.1322 343 SER A CB 2637 O OG . SER A 341 ? 0.4113 0.4343 0.6512 -0.1375 -0.1180 0.1217 343 SER A OG 2638 N N . ILE A 342 ? 0.4735 0.5596 0.6956 -0.1638 -0.1097 0.2064 344 ILE A N 2639 C CA . ILE A 342 ? 0.4869 0.5889 0.6900 -0.1608 -0.1058 0.2190 344 ILE A CA 2640 C C . ILE A 342 ? 0.5174 0.5573 0.7282 -0.1656 -0.1274 0.2232 344 ILE A C 2641 O O . ILE A 342 ? 0.5696 0.5882 0.8055 -0.1874 -0.1472 0.2475 344 ILE A O 2642 C CB . ILE A 342 ? 0.5245 0.6965 0.7296 -0.1817 -0.1007 0.2586 344 ILE A CB 2643 C CG1 . ILE A 342 ? 0.4735 0.7152 0.6725 -0.1697 -0.0774 0.2460 344 ILE A CG1 2644 C CG2 . ILE A 342 ? 0.4858 0.6754 0.6731 -0.1868 -0.1042 0.2827 344 ILE A CG2 2645 C CD1 . ILE A 342 ? 0.4206 0.6720 0.5948 -0.1384 -0.0619 0.2105 344 ILE A CD1 2646 N N . ILE A 343 ? 0.5031 0.5124 0.6988 -0.1457 -0.1265 0.1993 345 ILE A N 2647 C CA . ILE A 343 ? 0.5135 0.4665 0.7220 -0.1467 -0.1477 0.1993 345 ILE A CA 2648 C C . ILE A 343 ? 0.5405 0.4995 0.7365 -0.1466 -0.1526 0.2192 345 ILE A C 2649 O O . ILE A 343 ? 0.5459 0.5495 0.7155 -0.1389 -0.1365 0.2191 345 ILE A O 2650 C CB . ILE A 343 ? 0.4874 0.4022 0.6945 -0.1257 -0.1468 0.1582 345 ILE A CB 2651 C CG1 . ILE A 343 ? 0.4643 0.3997 0.6449 -0.1052 -0.1273 0.1374 345 ILE A CG1 2652 C CG2 . ILE A 343 ? 0.4570 0.3657 0.6789 -0.1295 -0.1482 0.1426 345 ILE A CG2 2653 C CD1 . ILE A 343 ? 0.3999 0.3033 0.5764 -0.0885 -0.1310 0.1140 345 ILE A CD1 2654 N N . THR A 344 ? 0.5732 0.4892 0.7900 -0.1533 -0.1765 0.2337 346 THR A N 2655 C CA . THR A 344 ? 0.5864 0.5067 0.7934 -0.1523 -0.1846 0.2543 346 THR A CA 2656 C C . THR A 344 ? 0.5666 0.4617 0.7607 -0.1266 -0.1821 0.2204 346 THR A C 2657 O O . THR A 344 ? 0.5427 0.4128 0.7396 -0.1110 -0.1768 0.1838 346 THR A O 2658 C CB . THR A 344 ? 0.6379 0.5269 0.8796 -0.1726 -0.2156 0.2946 346 THR A CB 2659 O OG1 . THR A 344 ? 0.6812 0.5037 0.9560 -0.1640 -0.2347 0.2687 346 THR A OG1 2660 C CG2 . THR A 344 ? 0.6252 0.5456 0.8834 -0.2038 -0.2206 0.3379 346 THR A CG2 2661 N N . ARG A 345 ? 0.5774 0.4873 0.7574 -0.1243 -0.1864 0.2360 347 ARG A N 2662 C CA . ARG A 345 ? 0.5619 0.4491 0.7373 -0.1050 -0.1904 0.2138 347 ARG A CA 2663 C C . ARG A 345 ? 0.5705 0.3977 0.7811 -0.0966 -0.2091 0.1962 347 ARG A C 2664 O O . ARG A 345 ? 0.5464 0.3582 0.7562 -0.0780 -0.2029 0.1599 347 ARG A O 2665 C CB . ARG A 345 ? 0.5765 0.4880 0.7410 -0.1112 -0.2014 0.2466 347 ARG A CB 2666 C CG . ARG A 345 ? 0.5994 0.4981 0.7571 -0.0921 -0.2046 0.2248 347 ARG A CG 2667 C CD . ARG A 345 ? 0.6595 0.5953 0.8001 -0.0988 -0.2136 0.2566 347 ARG A CD 2668 N NE . ARG A 345 ? 0.6392 0.5633 0.7781 -0.0825 -0.2217 0.2407 347 ARG A NE 2669 C CZ . ARG A 345 ? 0.6382 0.5818 0.7529 -0.0679 -0.2069 0.2067 347 ARG A CZ 2670 N NH1 . ARG A 345 ? 0.6557 0.5908 0.7740 -0.0565 -0.2176 0.1978 347 ARG A NH1 2671 N NH2 . ARG A 345 ? 0.5988 0.5688 0.6911 -0.0646 -0.1841 0.1818 347 ARG A NH2 2672 N N . LYS A 346 ? 0.6100 0.4069 0.8548 -0.1104 -0.2335 0.2217 348 LYS A N 2673 C CA . LYS A 346 ? 0.6348 0.3765 0.9188 -0.1004 -0.2536 0.1984 348 LYS A CA 2674 C C . LYS A 346 ? 0.6037 0.3395 0.8871 -0.0908 -0.2397 0.1547 348 LYS A C 2675 O O . LYS A 346 ? 0.5975 0.3134 0.8926 -0.0716 -0.2422 0.1175 348 LYS A O 2676 C CB . LYS A 346 ? 0.6835 0.3898 1.0120 -0.1194 -0.2858 0.2332 348 LYS A CB 2677 C CG . LYS A 346 ? 0.7606 0.4331 1.1196 -0.1118 -0.3145 0.2483 348 LYS A CG 2678 C CD . LYS A 346 ? 0.8593 0.4820 1.2773 -0.1294 -0.3534 0.2788 348 LYS A CD 2679 C CE . LYS A 346 ? 0.9246 0.5145 1.3793 -0.1235 -0.3868 0.3051 348 LYS A CE 2680 N NZ . LYS A 346 ? 0.9980 0.5302 1.5197 -0.1386 -0.4292 0.3317 348 LYS A NZ 2681 N N . GLU A 347 ? 0.5823 0.3422 0.8537 -0.1044 -0.2261 0.1607 349 GLU A N 2682 C CA . GLU A 347 ? 0.5552 0.3185 0.8231 -0.0978 -0.2133 0.1256 349 GLU A CA 2683 C C . GLU A 347 ? 0.5223 0.3075 0.7616 -0.0785 -0.1909 0.0973 349 GLU A C 2684 O O . GLU A 347 ? 0.5177 0.2960 0.7622 -0.0656 -0.1886 0.0638 349 GLU A O 2685 C CB . GLU A 347 ? 0.5432 0.3301 0.8094 -0.1175 -0.2065 0.1428 349 GLU A CB 2686 C CG . GLU A 347 ? 0.6195 0.3724 0.9286 -0.1377 -0.2351 0.1595 349 GLU A CG 2687 C CD . GLU A 347 ? 0.6440 0.4273 0.9558 -0.1633 -0.2317 0.1912 349 GLU A CD 2688 O OE1 . GLU A 347 ? 0.6950 0.4576 1.0384 -0.1784 -0.2492 0.1913 349 GLU A OE1 2689 O OE2 . GLU A 347 ? 0.6283 0.4597 0.9131 -0.1686 -0.2128 0.2146 349 GLU A OE2 2690 N N . PHE A 348 ? 0.5046 0.3198 0.7161 -0.0771 -0.1762 0.1102 350 PHE A N 2691 C CA . PHE A 348 ? 0.4655 0.2970 0.6559 -0.0608 -0.1593 0.0868 350 PHE A CA 2692 C C . PHE A 348 ? 0.4664 0.2759 0.6700 -0.0459 -0.1685 0.0657 350 PHE A C 2693 O O . PHE A 348 ? 0.4377 0.2522 0.6414 -0.0356 -0.1604 0.0394 350 PHE A O 2694 C CB . PHE A 348 ? 0.4601 0.3207 0.6263 -0.0612 -0.1503 0.1013 350 PHE A CB 2695 C CG . PHE A 348 ? 0.4357 0.3082 0.5869 -0.0473 -0.1375 0.0788 350 PHE A CG 2696 C CD1 . PHE A 348 ? 0.3865 0.2771 0.5297 -0.0442 -0.1219 0.0665 350 PHE A CD1 2697 C CD2 . PHE A 348 ? 0.4292 0.2954 0.5787 -0.0381 -0.1437 0.0723 350 PHE A CD2 2698 C CE1 . PHE A 348 ? 0.4115 0.3082 0.5483 -0.0332 -0.1143 0.0481 350 PHE A CE1 2699 C CE2 . PHE A 348 ? 0.4265 0.3031 0.5669 -0.0281 -0.1345 0.0527 350 PHE A CE2 2700 C CZ . PHE A 348 ? 0.3547 0.2438 0.4903 -0.0263 -0.1210 0.0414 350 PHE A CZ 2701 N N . GLN A 349 ? 0.4874 0.2774 0.7055 -0.0455 -0.1868 0.0800 351 GLN A N 2702 C CA . GLN A 349 ? 0.4928 0.2648 0.7300 -0.0296 -0.1984 0.0613 351 GLN A CA 2703 C C . GLN A 349 ? 0.4933 0.2503 0.7547 -0.0208 -0.2035 0.0286 351 GLN A C 2704 O O . GLN A 349 ? 0.4479 0.2186 0.7106 -0.0059 -0.1962 -0.0004 351 GLN A O 2705 C CB . GLN A 349 ? 0.5292 0.2807 0.7849 -0.0321 -0.2219 0.0882 351 GLN A CB 2706 C CG . GLN A 349 ? 0.5296 0.3083 0.7585 -0.0334 -0.2166 0.1080 351 GLN A CG 2707 C CD . GLN A 349 ? 0.5855 0.3546 0.8281 -0.0411 -0.2405 0.1464 351 GLN A CD 2708 O OE1 . GLN A 349 ? 0.5843 0.3347 0.8479 -0.0554 -0.2571 0.1740 351 GLN A OE1 2709 N NE2 . GLN A 349 ? 0.5004 0.2853 0.7329 -0.0340 -0.2439 0.1515 351 GLN A NE2 2710 N N . GLU A 350 ? 0.5008 0.2364 0.7819 -0.0311 -0.2163 0.0329 352 GLU A N 2711 C CA . GLU A 350 ? 0.5200 0.2482 0.8209 -0.0241 -0.2213 -0.0026 352 GLU A CA 2712 C C . GLU A 350 ? 0.4801 0.2469 0.7550 -0.0214 -0.1971 -0.0233 352 GLU A C 2713 O O . GLU A 350 ? 0.4740 0.2553 0.7564 -0.0082 -0.1954 -0.0576 352 GLU A O 2714 C CB . GLU A 350 ? 0.5583 0.2564 0.8869 -0.0390 -0.2416 0.0055 352 GLU A CB 2715 C CG . GLU A 350 ? 0.6884 0.3432 1.0549 -0.0418 -0.2719 0.0258 352 GLU A CG 2716 C CD . GLU A 350 ? 0.8399 0.4735 1.2390 -0.0163 -0.2887 -0.0079 352 GLU A CD 2717 O OE1 . GLU A 350 ? 0.9033 0.5347 1.3044 -0.0070 -0.2931 0.0058 352 GLU A OE1 2718 O OE2 . GLU A 350 ? 0.9059 0.5307 1.3297 -0.0040 -0.2979 -0.0510 352 GLU A OE2 2719 N N . GLY A 351 ? 0.4436 0.2316 0.6912 -0.0328 -0.1799 -0.0023 353 GLY A N 2720 C CA . GLY A 351 ? 0.4324 0.2536 0.6605 -0.0320 -0.1607 -0.0138 353 GLY A CA 2721 C C . GLY A 351 ? 0.4306 0.2735 0.6508 -0.0188 -0.1503 -0.0286 353 GLY A C 2722 O O . GLY A 351 ? 0.4294 0.2994 0.6475 -0.0148 -0.1427 -0.0471 353 GLY A O 2723 N N . LEU A 352 ? 0.4232 0.2594 0.6405 -0.0138 -0.1514 -0.0188 354 LEU A N 2724 C CA . LEU A 352 ? 0.4169 0.2730 0.6331 -0.0032 -0.1450 -0.0308 354 LEU A CA 2725 C C . LEU A 352 ? 0.4328 0.2973 0.6701 0.0098 -0.1521 -0.0594 354 LEU A C 2726 O O . LEU A 352 ? 0.4207 0.3206 0.6575 0.0156 -0.1427 -0.0738 354 LEU A O 2727 C CB . LEU A 352 ? 0.4008 0.2481 0.6141 -0.0001 -0.1495 -0.0178 354 LEU A CB 2728 C CG . LEU A 352 ? 0.4068 0.2571 0.5982 -0.0092 -0.1416 0.0025 354 LEU A CG 2729 C CD1 . LEU A 352 ? 0.3924 0.2414 0.5786 -0.0063 -0.1475 0.0116 354 LEU A CD1 2730 C CD2 . LEU A 352 ? 0.3303 0.2019 0.5121 -0.0120 -0.1264 -0.0017 354 LEU A CD2 2731 N N . LYS A 353 ? 0.4549 0.2909 0.7144 0.0143 -0.1699 -0.0680 355 LYS A N 2732 C CA . LYS A 353 ? 0.4829 0.3278 0.7679 0.0311 -0.1788 -0.1033 355 LYS A CA 2733 C C . LYS A 353 ? 0.4745 0.3545 0.7522 0.0295 -0.1692 -0.1271 355 LYS A C 2734 O O . LYS A 353 ? 0.4796 0.4019 0.7622 0.0413 -0.1633 -0.1551 355 LYS A O 2735 C CB . LYS A 353 ? 0.5053 0.3044 0.8230 0.0370 -0.2046 -0.1060 355 LYS A CB 2736 C CG . LYS A 353 ? 0.6208 0.4225 0.9742 0.0592 -0.2188 -0.1480 355 LYS A CG 2737 C CD . LYS A 353 ? 0.7756 0.5203 1.1699 0.0654 -0.2502 -0.1401 355 LYS A CD 2738 C CE . LYS A 353 ? 0.8396 0.5663 1.2192 0.0533 -0.2516 -0.0899 355 LYS A CE 2739 N NZ . LYS A 353 ? 0.9090 0.5837 1.3173 0.0456 -0.2805 -0.0592 355 LYS A NZ 2740 N N . ILE A 354 ? 0.4687 0.3410 0.7333 0.0141 -0.1665 -0.1134 356 ILE A N 2741 C CA . ILE A 354 ? 0.4782 0.3875 0.7329 0.0101 -0.1584 -0.1304 356 ILE A CA 2742 C C . ILE A 354 ? 0.4383 0.3987 0.6707 0.0074 -0.1376 -0.1209 356 ILE A C 2743 O O . ILE A 354 ? 0.4289 0.4383 0.6592 0.0117 -0.1317 -0.1418 356 ILE A O 2744 C CB . ILE A 354 ? 0.4888 0.3790 0.7376 -0.0068 -0.1616 -0.1134 356 ILE A CB 2745 C CG1 . ILE A 354 ? 0.5366 0.3802 0.8148 -0.0079 -0.1860 -0.1226 356 ILE A CG1 2746 C CG2 . ILE A 354 ? 0.5030 0.4380 0.7361 -0.0134 -0.1513 -0.1213 356 ILE A CG2 2747 C CD1 . ILE A 354 ? 0.5718 0.4239 0.8680 -0.0022 -0.1984 -0.1627 356 ILE A CD1 2748 N N . PHE A 355 ? 0.4018 0.3535 0.6215 0.0005 -0.1289 -0.0905 357 PHE A N 2749 C CA . PHE A 355 ? 0.3718 0.3631 0.5786 -0.0050 -0.1141 -0.0770 357 PHE A CA 2750 C C . PHE A 355 ? 0.3667 0.3858 0.5805 0.0024 -0.1099 -0.0821 357 PHE A C 2751 O O . PHE A 355 ? 0.3677 0.4293 0.5769 -0.0042 -0.1001 -0.0718 357 PHE A O 2752 C CB . PHE A 355 ? 0.3440 0.3149 0.5388 -0.0159 -0.1087 -0.0463 357 PHE A CB 2753 C CG . PHE A 355 ? 0.3777 0.3487 0.5660 -0.0249 -0.1080 -0.0391 357 PHE A CG 2754 C CD1 . PHE A 355 ? 0.3395 0.3493 0.5224 -0.0311 -0.1013 -0.0334 357 PHE A CD1 2755 C CD2 . PHE A 355 ? 0.3953 0.3337 0.5857 -0.0285 -0.1155 -0.0356 357 PHE A CD2 2756 C CE1 . PHE A 355 ? 0.3676 0.3827 0.5466 -0.0390 -0.1023 -0.0276 357 PHE A CE1 2757 C CE2 . PHE A 355 ? 0.4589 0.4029 0.6468 -0.0379 -0.1155 -0.0292 357 PHE A CE2 2758 C CZ . PHE A 355 ? 0.4099 0.3928 0.5918 -0.0421 -0.1087 -0.0269 357 PHE A CZ 2759 N N . PHE A 356 ? 0.3639 0.3614 0.5917 0.0141 -0.1188 -0.0934 358 PHE A N 2760 C CA . PHE A 356 ? 0.3667 0.3886 0.6054 0.0217 -0.1168 -0.0976 358 PHE A CA 2761 C C . PHE A 356 ? 0.4089 0.4371 0.6714 0.0414 -0.1272 -0.1314 358 PHE A C 2762 O O . PHE A 356 ? 0.4093 0.4180 0.6877 0.0516 -0.1365 -0.1330 358 PHE A O 2763 C CB . PHE A 356 ? 0.3246 0.3154 0.5603 0.0177 -0.1193 -0.0749 358 PHE A CB 2764 C CG . PHE A 356 ? 0.3411 0.3270 0.5610 0.0029 -0.1115 -0.0499 358 PHE A CG 2765 C CD1 . PHE A 356 ? 0.2901 0.3060 0.5131 -0.0051 -0.1047 -0.0376 358 PHE A CD1 2766 C CD2 . PHE A 356 ? 0.3366 0.2904 0.5436 -0.0034 -0.1123 -0.0381 358 PHE A CD2 2767 C CE1 . PHE A 356 ? 0.2632 0.2680 0.4798 -0.0168 -0.1016 -0.0165 358 PHE A CE1 2768 C CE2 . PHE A 356 ? 0.3063 0.2574 0.5045 -0.0127 -0.1064 -0.0202 358 PHE A CE2 2769 C CZ . PHE A 356 ? 0.2822 0.2546 0.4868 -0.0182 -0.1023 -0.0110 358 PHE A CZ 2770 N N . PRO A 357 ? 0.4315 0.4922 0.6990 0.0484 -0.1268 -0.1608 359 PRO A N 2771 C CA . PRO A 357 ? 0.4696 0.5396 0.7648 0.0706 -0.1383 -0.2025 359 PRO A CA 2772 C C . PRO A 357 ? 0.4807 0.5937 0.7948 0.0857 -0.1353 -0.2167 359 PRO A C 2773 O O . PRO A 357 ? 0.5226 0.6140 0.8664 0.1055 -0.1505 -0.2383 359 PRO A O 2774 C CB . PRO A 357 ? 0.4959 0.6089 0.7855 0.0719 -0.1348 -0.2324 359 PRO A CB 2775 C CG . PRO A 357 ? 0.4446 0.5909 0.7034 0.0502 -0.1180 -0.2015 359 PRO A CG 2776 C CD . PRO A 357 ? 0.4222 0.5146 0.6703 0.0358 -0.1170 -0.1574 359 PRO A CD 2777 N N . GLY A 358 ? 0.4686 0.6420 0.7720 0.0769 -0.1186 -0.2028 360 GLY A N 2778 C CA . GLY A 358 ? 0.4513 0.6709 0.7783 0.0916 -0.1170 -0.2171 360 GLY A CA 2779 C C . GLY A 358 ? 0.4435 0.6252 0.7767 0.0876 -0.1229 -0.1889 360 GLY A C 2780 O O . GLY A 358 ? 0.4491 0.6688 0.8016 0.0956 -0.1217 -0.1931 360 GLY A O 2781 N N . VAL A 359 ? 0.4200 0.5336 0.7378 0.0757 -0.1296 -0.1615 361 VAL A N 2782 C CA . VAL A 359 ? 0.3864 0.4761 0.7014 0.0671 -0.1326 -0.1330 361 VAL A CA 2783 C C . VAL A 359 ? 0.4039 0.4517 0.7394 0.0829 -0.1519 -0.1383 361 VAL A C 2784 O O . VAL A 359 ? 0.4265 0.4318 0.7704 0.0915 -0.1654 -0.1474 361 VAL A O 2785 C CB . VAL A 359 ? 0.3766 0.4302 0.6621 0.0450 -0.1276 -0.1006 361 VAL A CB 2786 C CG1 . VAL A 359 ? 0.3614 0.3891 0.6438 0.0389 -0.1336 -0.0797 361 VAL A CG1 2787 C CG2 . VAL A 359 ? 0.3100 0.4075 0.5834 0.0288 -0.1120 -0.0885 361 VAL A CG2 2788 N N . SER A 360 ? 0.3879 0.4470 0.7344 0.0849 -0.1558 -0.1292 362 SER A N 2789 C CA . SER A 360 ? 0.4093 0.4358 0.7769 0.0994 -0.1758 -0.1293 362 SER A CA 2790 C C . SER A 360 ? 0.4155 0.3788 0.7638 0.0889 -0.1868 -0.1032 362 SER A C 2791 O O . SER A 360 ? 0.4108 0.3623 0.7284 0.0704 -0.1769 -0.0842 362 SER A O 2792 C CB . SER A 360 ? 0.3865 0.4442 0.7661 0.0998 -0.1772 -0.1212 362 SER A CB 2793 O OG . SER A 360 ? 0.3909 0.4355 0.7429 0.0778 -0.1724 -0.0934 362 SER A OG 2794 N N . GLU A 361 ? 0.4405 0.3690 0.8099 0.1007 -0.2081 -0.1006 363 GLU A N 2795 C CA A GLU A 361 ? 0.4577 0.3395 0.8123 0.0896 -0.2205 -0.0696 363 GLU A CA 2796 C CA B GLU A 361 ? 0.4614 0.3429 0.8149 0.0890 -0.2200 -0.0694 363 GLU A CA 2797 C C . GLU A 361 ? 0.4449 0.3362 0.7679 0.0733 -0.2132 -0.0452 363 GLU A C 2798 O O . GLU A 361 ? 0.4571 0.3311 0.7506 0.0576 -0.2087 -0.0254 363 GLU A O 2799 C CB A GLU A 361 ? 0.4898 0.3432 0.8806 0.1051 -0.2485 -0.0648 363 GLU A CB 2800 C CB B GLU A 361 ? 0.4995 0.3486 0.8879 0.1032 -0.2483 -0.0633 363 GLU A CB 2801 C CG A GLU A 361 ? 0.5112 0.3381 0.9369 0.1196 -0.2623 -0.0880 363 GLU A CG 2802 C CG B GLU A 361 ? 0.5293 0.3476 0.9019 0.0890 -0.2626 -0.0214 363 GLU A CG 2803 C CD A GLU A 361 ? 0.5161 0.3285 0.9197 0.1050 -0.2511 -0.0903 363 GLU A CD 2804 C CD B GLU A 361 ? 0.5740 0.3650 0.9230 0.0700 -0.2590 -0.0018 363 GLU A CD 2805 O OE1 A GLU A 361 ? 0.5194 0.3571 0.9271 0.1124 -0.2394 -0.1242 363 GLU A OE1 2806 O OE1 B GLU A 361 ? 0.5245 0.3270 0.8490 0.0607 -0.2378 -0.0123 363 GLU A OE1 2807 O OE2 A GLU A 361 ? 0.4747 0.2584 0.8567 0.0859 -0.2536 -0.0580 363 GLU A OE2 2808 O OE2 B GLU A 361 ? 0.5962 0.3581 0.9535 0.0633 -0.2787 0.0282 363 GLU A OE2 2809 N N . PHE A 362 ? 0.4290 0.3513 0.7609 0.0776 -0.2133 -0.0490 364 PHE A N 2810 C CA . PHE A 362 ? 0.4091 0.3410 0.7150 0.0626 -0.2089 -0.0329 364 PHE A CA 2811 C C . PHE A 362 ? 0.3812 0.3191 0.6619 0.0471 -0.1889 -0.0341 364 PHE A C 2812 O O . PHE A 362 ? 0.3904 0.3158 0.6449 0.0352 -0.1861 -0.0218 364 PHE A O 2813 C CB . PHE A 362 ? 0.3995 0.3657 0.7250 0.0683 -0.2142 -0.0386 364 PHE A CB 2814 C CG . PHE A 362 ? 0.3883 0.3683 0.6938 0.0524 -0.2099 -0.0309 364 PHE A CG 2815 C CD1 . PHE A 362 ? 0.3457 0.3530 0.6552 0.0428 -0.1963 -0.0389 364 PHE A CD1 2816 C CD2 . PHE A 362 ? 0.3308 0.2989 0.6153 0.0459 -0.2210 -0.0157 364 PHE A CD2 2817 C CE1 . PHE A 362 ? 0.3780 0.3911 0.6770 0.0277 -0.1972 -0.0341 364 PHE A CE1 2818 C CE2 . PHE A 362 ? 0.4031 0.3831 0.6717 0.0329 -0.2190 -0.0168 364 PHE A CE2 2819 C CZ . PHE A 362 ? 0.3291 0.3271 0.6081 0.0242 -0.2087 -0.0272 364 PHE A CZ 2820 N N . GLY A 363 ? 0.3701 0.3321 0.6606 0.0481 -0.1759 -0.0490 365 GLY A N 2821 C CA . GLY A 363 ? 0.3271 0.2945 0.5996 0.0338 -0.1603 -0.0455 365 GLY A CA 2822 C C . GLY A 363 ? 0.3584 0.2915 0.6081 0.0280 -0.1585 -0.0362 365 GLY A C 2823 O O . GLY A 363 ? 0.3540 0.2793 0.5845 0.0168 -0.1527 -0.0268 365 GLY A O 2824 N N . LYS A 364 ? 0.3806 0.2938 0.6366 0.0357 -0.1651 -0.0397 366 LYS A N 2825 C CA . LYS A 364 ? 0.3970 0.2840 0.6350 0.0273 -0.1632 -0.0285 366 LYS A CA 2826 C C . LYS A 364 ? 0.4025 0.2746 0.6223 0.0206 -0.1699 -0.0077 366 LYS A C 2827 O O . LYS A 364 ? 0.4007 0.2696 0.5994 0.0108 -0.1618 0.0013 366 LYS A O 2828 C CB . LYS A 364 ? 0.4082 0.2753 0.6616 0.0336 -0.1717 -0.0362 366 LYS A CB 2829 C CG . LYS A 364 ? 0.4604 0.3505 0.7271 0.0406 -0.1644 -0.0625 366 LYS A CG 2830 C CD . LYS A 364 ? 0.5028 0.3676 0.7854 0.0456 -0.1762 -0.0734 366 LYS A CD 2831 C CE . LYS A 364 ? 0.6186 0.4820 0.9379 0.0666 -0.1924 -0.0967 366 LYS A CE 2832 N NZ . LYS A 364 ? 0.6366 0.5379 0.9690 0.0786 -0.1853 -0.1343 366 LYS A NZ 2833 N N . GLU A 365 ? 0.4078 0.2769 0.6362 0.0263 -0.1848 -0.0004 367 GLU A N 2834 C CA . GLU A 365 ? 0.4527 0.3218 0.6595 0.0188 -0.1908 0.0196 367 GLU A CA 2835 C C . GLU A 365 ? 0.4164 0.3046 0.6027 0.0123 -0.1797 0.0127 367 GLU A C 2836 O O . GLU A 365 ? 0.4215 0.3149 0.5839 0.0053 -0.1768 0.0209 367 GLU A O 2837 C CB . GLU A 365 ? 0.4608 0.3311 0.6797 0.0251 -0.2105 0.0314 367 GLU A CB 2838 C CG . GLU A 365 ? 0.6530 0.4993 0.8840 0.0245 -0.2272 0.0541 367 GLU A CG 2839 C CD . GLU A 365 ? 0.8025 0.6595 1.0128 0.0139 -0.2386 0.0870 367 GLU A CD 2840 O OE1 . GLU A 365 ? 0.8268 0.6885 1.0147 0.0006 -0.2319 0.1037 367 GLU A OE1 2841 O OE2 . GLU A 365 ? 0.8342 0.7018 1.0520 0.0188 -0.2545 0.0971 367 GLU A OE2 2842 N N . SER A 366 ? 0.3920 0.2935 0.5906 0.0145 -0.1751 -0.0027 368 SER A N 2843 C CA . SER A 366 ? 0.4015 0.3139 0.5889 0.0076 -0.1702 -0.0096 368 SER A CA 2844 C C . SER A 366 ? 0.3846 0.2894 0.5587 0.0017 -0.1572 -0.0106 368 SER A C 2845 O O . SER A 366 ? 0.3793 0.2874 0.5394 -0.0012 -0.1556 -0.0154 368 SER A O 2846 C CB . SER A 366 ? 0.3756 0.3045 0.5851 0.0068 -0.1709 -0.0198 368 SER A CB 2847 O OG . SER A 366 ? 0.3849 0.3180 0.6054 0.0035 -0.1590 -0.0226 368 SER A OG 2848 N N . ILE A 367 ? 0.3814 0.2791 0.5614 0.0018 -0.1494 -0.0087 369 ILE A N 2849 C CA . ILE A 367 ? 0.3724 0.2655 0.5434 -0.0030 -0.1385 -0.0073 369 ILE A CA 2850 C C . ILE A 367 ? 0.3944 0.2851 0.5448 -0.0047 -0.1392 0.0024 369 ILE A C 2851 O O . ILE A 367 ? 0.3972 0.2953 0.5360 -0.0061 -0.1337 -0.0012 369 ILE A O 2852 C CB . ILE A 367 ? 0.3615 0.2537 0.5422 -0.0035 -0.1318 -0.0075 369 ILE A CB 2853 C CG1 . ILE A 367 ? 0.3028 0.2139 0.5016 -0.0037 -0.1287 -0.0144 369 ILE A CG1 2854 C CG2 . ILE A 367 ? 0.3331 0.2229 0.5050 -0.0085 -0.1227 -0.0032 369 ILE A CG2 2855 C CD1 . ILE A 367 ? 0.2481 0.1704 0.4536 -0.0021 -0.1233 -0.0195 369 ILE A CD1 2856 N N . LEU A 368 ? 0.4195 0.3040 0.5692 -0.0044 -0.1477 0.0150 370 LEU A N 2857 C CA . LEU A 368 ? 0.4389 0.3287 0.5722 -0.0101 -0.1497 0.0326 370 LEU A CA 2858 C C . LEU A 368 ? 0.4348 0.3492 0.5478 -0.0100 -0.1505 0.0298 370 LEU A C 2859 O O . LEU A 368 ? 0.4358 0.3698 0.5321 -0.0129 -0.1434 0.0313 370 LEU A O 2860 C CB . LEU A 368 ? 0.4651 0.3409 0.6099 -0.0109 -0.1648 0.0505 370 LEU A CB 2861 C CG . LEU A 368 ? 0.5323 0.4116 0.6715 -0.0197 -0.1766 0.0811 370 LEU A CG 2862 C CD1 . LEU A 368 ? 0.5674 0.4802 0.6819 -0.0229 -0.1794 0.0922 370 LEU A CD1 2863 C CD2 . LEU A 368 ? 0.5682 0.4436 0.7079 -0.0306 -0.1722 0.0956 370 LEU A CD2 2864 N N . PHE A 369 ? 0.4272 0.3457 0.5431 -0.0059 -0.1596 0.0229 371 PHE A N 2865 C CA . PHE A 369 ? 0.4468 0.3918 0.5441 -0.0053 -0.1633 0.0146 371 PHE A CA 2866 C C . PHE A 369 ? 0.4327 0.3855 0.5257 -0.0027 -0.1538 -0.0099 371 PHE A C 2867 O O . PHE A 369 ? 0.4186 0.4003 0.4911 -0.0014 -0.1519 -0.0184 371 PHE A O 2868 C CB . PHE A 369 ? 0.4662 0.4117 0.5745 -0.0018 -0.1764 0.0092 371 PHE A CB 2869 C CG . PHE A 369 ? 0.5238 0.4971 0.6153 -0.0014 -0.1832 -0.0040 371 PHE A CG 2870 C CD1 . PHE A 369 ? 0.5555 0.5274 0.6554 0.0004 -0.1821 -0.0325 371 PHE A CD1 2871 C CD2 . PHE A 369 ? 0.5749 0.5777 0.6453 -0.0039 -0.1939 0.0127 371 PHE A CD2 2872 C CE1 . PHE A 369 ? 0.6051 0.6033 0.6920 0.0014 -0.1918 -0.0524 371 PHE A CE1 2873 C CE2 . PHE A 369 ? 0.6484 0.6867 0.6996 -0.0032 -0.2013 -0.0041 371 PHE A CE2 2874 C CZ . PHE A 369 ? 0.6293 0.6645 0.6886 0.0004 -0.2006 -0.0404 371 PHE A CZ 2875 N N . HIS A 370 ? 0.4103 0.3418 0.5249 -0.0014 -0.1494 -0.0216 372 HIS A N 2876 C CA A HIS A 370 ? 0.4240 0.3542 0.5454 0.0014 -0.1449 -0.0428 372 HIS A CA 2877 C CA B HIS A 370 ? 0.4270 0.3584 0.5473 0.0014 -0.1453 -0.0429 372 HIS A CA 2878 C C . HIS A 370 ? 0.4364 0.3745 0.5492 0.0033 -0.1332 -0.0418 372 HIS A C 2879 O O . HIS A 370 ? 0.4586 0.4093 0.5695 0.0096 -0.1313 -0.0614 372 HIS A O 2880 C CB A HIS A 370 ? 0.3877 0.2971 0.5386 -0.0012 -0.1459 -0.0473 372 HIS A CB 2881 C CB B HIS A 370 ? 0.3986 0.3108 0.5482 -0.0010 -0.1489 -0.0497 372 HIS A CB 2882 C CG A HIS A 370 ? 0.3949 0.2981 0.5611 0.0011 -0.1497 -0.0678 372 HIS A CG 2883 C CG B HIS A 370 ? 0.4054 0.3224 0.5629 -0.0025 -0.1622 -0.0588 372 HIS A CG 2884 N ND1 A HIS A 370 ? 0.3663 0.2600 0.5449 0.0034 -0.1435 -0.0696 372 HIS A ND1 2885 N ND1 B HIS A 370 ? 0.3566 0.2781 0.5184 -0.0040 -0.1679 -0.0474 372 HIS A ND1 2886 C CD2 A HIS A 370 ? 0.3645 0.2682 0.5402 0.0023 -0.1622 -0.0889 372 HIS A CD2 2887 C CD2 B HIS A 370 ? 0.3656 0.2863 0.5292 -0.0019 -0.1729 -0.0805 372 HIS A CD2 2888 C CE1 A HIS A 370 ? 0.3357 0.2208 0.5337 0.0072 -0.1529 -0.0909 372 HIS A CE1 2889 C CE1 B HIS A 370 ? 0.3728 0.3027 0.5427 -0.0057 -0.1803 -0.0583 372 HIS A CE1 2890 N NE2 A HIS A 370 ? 0.3374 0.2277 0.5335 0.0062 -0.1645 -0.1048 372 HIS A NE2 2891 N NE2 B HIS A 370 ? 0.3526 0.2810 0.5229 -0.0054 -0.1841 -0.0789 372 HIS A NE2 2892 N N . TYR A 371 ? 0.4385 0.3720 0.5487 -0.0012 -0.1267 -0.0212 373 TYR A N 2893 C CA . TYR A 371 ? 0.4508 0.3939 0.5577 -0.0009 -0.1161 -0.0184 373 TYR A CA 2894 C C . TYR A 371 ? 0.4977 0.4730 0.5827 -0.0044 -0.1123 -0.0050 373 TYR A C 2895 O O . TYR A 371 ? 0.5164 0.5083 0.6005 -0.0042 -0.1027 -0.0034 373 TYR A O 2896 C CB . TYR A 371 ? 0.4251 0.3470 0.5475 -0.0056 -0.1117 -0.0066 373 TYR A CB 2897 C CG . TYR A 371 ? 0.4031 0.3117 0.5466 -0.0029 -0.1107 -0.0174 373 TYR A CG 2898 C CD1 . TYR A 371 ? 0.3487 0.2611 0.5020 0.0009 -0.1048 -0.0222 373 TYR A CD1 2899 C CD2 . TYR A 371 ? 0.3106 0.2072 0.4684 -0.0048 -0.1172 -0.0198 373 TYR A CD2 2900 C CE1 . TYR A 371 ? 0.3318 0.2301 0.5105 0.0016 -0.1081 -0.0254 373 TYR A CE1 2901 C CE2 . TYR A 371 ? 0.3392 0.2278 0.5200 -0.0064 -0.1187 -0.0223 373 TYR A CE2 2902 C CZ . TYR A 371 ? 0.3433 0.2301 0.5350 -0.0038 -0.1152 -0.0230 373 TYR A CZ 2903 O OH . TYR A 371 ? 0.3052 0.1826 0.5242 -0.0072 -0.1207 -0.0193 373 TYR A OH 2904 N N . THR A 372 ? 0.5329 0.5224 0.6026 -0.0089 -0.1203 0.0085 374 THR A N 2905 C CA . THR A 372 ? 0.5909 0.6156 0.6426 -0.0174 -0.1184 0.0324 374 THR A CA 2906 C C . THR A 372 ? 0.6420 0.7167 0.6686 -0.0152 -0.1202 0.0259 374 THR A C 2907 O O . THR A 372 ? 0.6713 0.7801 0.6816 -0.0252 -0.1233 0.0533 374 THR A O 2908 C CB . THR A 372 ? 0.5910 0.5971 0.6489 -0.0289 -0.1300 0.0665 374 THR A CB 2909 O OG1 . THR A 372 ? 0.6292 0.6205 0.6901 -0.0252 -0.1433 0.0646 374 THR A OG1 2910 C CG2 . THR A 372 ? 0.5836 0.5515 0.6641 -0.0320 -0.1288 0.0715 374 THR A CG2 2911 N N . ASP A 373 ? 0.6937 0.7757 0.7183 -0.0033 -0.1204 -0.0094 375 ASP A N 2912 C CA . ASP A 373 ? 0.7661 0.9053 0.7651 0.0014 -0.1213 -0.0258 375 ASP A CA 2913 C C . ASP A 373 ? 0.7929 0.9754 0.7871 0.0102 -0.1065 -0.0469 375 ASP A C 2914 O O . ASP A 373 ? 0.8051 0.9739 0.8166 0.0247 -0.1039 -0.0840 375 ASP A O 2915 C CB . ASP A 373 ? 0.7799 0.9042 0.7845 0.0101 -0.1326 -0.0582 375 ASP A CB 2916 C CG . ASP A 373 ? 0.8592 1.0353 0.8358 0.0096 -0.1412 -0.0633 375 ASP A CG 2917 O OD1 . ASP A 373 ? 0.9108 1.1481 0.8651 0.0135 -0.1332 -0.0746 375 ASP A OD1 2918 O OD2 . ASP A 373 ? 0.8920 1.0549 0.8688 0.0058 -0.1557 -0.0563 375 ASP A OD2 2919 N N . TRP A 374 ? 0.8121 1.0467 0.7889 0.0014 -0.0979 -0.0215 376 TRP A N 2920 C CA . TRP A 374 ? 0.8272 1.1111 0.8028 0.0111 -0.0829 -0.0420 376 TRP A CA 2921 C C . TRP A 374 ? 0.8891 1.2590 0.8340 0.0181 -0.0805 -0.0640 376 TRP A C 2922 O O . TRP A 374 ? 0.9075 1.3097 0.8272 0.0059 -0.0883 -0.0392 376 TRP A O 2923 C CB . TRP A 374 ? 0.8082 1.1065 0.7879 -0.0034 -0.0733 -0.0029 376 TRP A CB 2924 C CG . TRP A 374 ? 0.7543 1.0035 0.7430 -0.0233 -0.0828 0.0434 376 TRP A CG 2925 C CD1 . TRP A 374 ? 0.7394 1.0073 0.7154 -0.0420 -0.0922 0.0867 376 TRP A CD1 2926 C CD2 . TRP A 374 ? 0.6652 0.8439 0.6813 -0.0259 -0.0856 0.0502 376 TRP A CD2 2927 N NE1 . TRP A 374 ? 0.6937 0.8991 0.6919 -0.0535 -0.1025 0.1148 376 TRP A NE1 2928 C CE2 . TRP A 374 ? 0.6390 0.7943 0.6591 -0.0438 -0.0972 0.0911 376 TRP A CE2 2929 C CE3 . TRP A 374 ? 0.6009 0.7377 0.6398 -0.0150 -0.0813 0.0262 376 TRP A CE3 2930 C CZ2 . TRP A 374 ? 0.5887 0.6834 0.6331 -0.0485 -0.1032 0.1003 376 TRP A CZ2 2931 C CZ3 . TRP A 374 ? 0.5178 0.6010 0.5761 -0.0223 -0.0859 0.0412 376 TRP A CZ3 2932 C CH2 . TRP A 374 ? 0.5525 0.6164 0.6126 -0.0376 -0.0961 0.0738 376 TRP A CH2 2933 N N . VAL A 375 ? 0.9297 1.3443 0.8766 0.0382 -0.0715 -0.1107 377 VAL A N 2934 C CA . VAL A 375 ? 0.9420 1.3395 0.9206 0.0566 -0.0627 -0.1434 377 VAL A CA 2935 C C . VAL A 375 ? 0.9449 1.3950 0.9272 0.0550 -0.0448 -0.1271 377 VAL A C 2936 O O . VAL A 375 ? 0.9335 1.3478 0.9472 0.0631 -0.0407 -0.1341 377 VAL A O 2937 C CB . VAL A 375 ? 0.9236 1.2212 0.9416 0.0636 -0.0732 -0.1577 377 VAL A CB 2938 C CG1 . VAL A 375 ? 0.8992 1.1493 0.9381 0.0518 -0.0676 -0.1199 377 VAL A CG1 2939 C CG2 . VAL A 375 ? 0.9400 1.2374 0.9853 0.0904 -0.0760 -0.2159 377 VAL A CG2 2940 N N . ASP A 376 ? 0.9689 1.5057 0.9222 0.0422 -0.0353 -0.1002 378 ASP A N 2941 C CA . ASP A 376 ? 0.9804 1.5441 0.9015 0.0186 -0.0425 -0.0558 378 ASP A CA 2942 C C . ASP A 376 ? 0.9742 1.5899 0.8892 -0.0057 -0.0331 0.0011 378 ASP A C 2943 O O . ASP A 376 ? 0.9673 1.5514 0.8806 -0.0304 -0.0437 0.0546 378 ASP A O 2944 C CB . ASP A 376 ? 1.0222 1.6588 0.9095 0.0267 -0.0462 -0.0841 378 ASP A CB 2945 C CG . ASP A 376 ? 1.0579 1.6955 0.9191 0.0038 -0.0612 -0.0377 378 ASP A CG 2946 O OD1 . ASP A 376 ? 1.0537 1.6768 0.9172 -0.0210 -0.0644 0.0241 378 ASP A OD1 2947 O OD2 . ASP A 376 ? 1.0802 1.7349 0.9218 0.0111 -0.0722 -0.0638 378 ASP A OD2 2948 N N . ASP A 377 ? 0.9664 1.6606 0.8834 0.0014 -0.0153 -0.0107 379 ASP A N 2949 C CA . ASP A 377 ? 0.9570 1.7079 0.8743 -0.0232 -0.0059 0.0428 379 ASP A CA 2950 C C . ASP A 377 ? 0.9308 1.5842 0.8693 -0.0461 -0.0196 0.0911 379 ASP A C 2951 O O . ASP A 377 ? 0.9168 1.4724 0.8771 -0.0350 -0.0273 0.0698 379 ASP A O 2952 C CB . ASP A 377 ? 0.9558 1.7479 0.8964 -0.0076 0.0122 0.0171 379 ASP A CB 2953 C CG . ASP A 377 ? 0.9856 1.9236 0.9060 -0.0009 0.0308 0.0030 379 ASP A CG 2954 O OD1 . ASP A 377 ? 1.0418 2.0627 0.9350 -0.0258 0.0331 0.0486 379 ASP A OD1 2955 O OD2 . ASP A 377 ? 0.9644 1.9391 0.9003 0.0294 0.0427 -0.0524 379 ASP A OD2 2956 N N . GLN A 378 ? 0.9195 1.5975 0.8556 -0.0779 -0.0246 0.1546 380 GLN A N 2957 C CA . GLN A 378 ? 0.8751 1.4634 0.8406 -0.0977 -0.0380 0.1937 380 GLN A CA 2958 C C . GLN A 378 ? 0.8478 1.4678 0.8362 -0.1123 -0.0280 0.2182 380 GLN A C 2959 O O . GLN A 378 ? 0.8722 1.5179 0.8665 -0.1432 -0.0353 0.2752 380 GLN A O 2960 C CB . GLN A 378 ? 0.8972 1.4634 0.8569 -0.1230 -0.0594 0.2473 380 GLN A CB 2961 C CG . GLN A 378 ? 0.8623 1.3298 0.8278 -0.1133 -0.0773 0.2327 380 GLN A CG 2962 C CD . GLN A 378 ? 0.8579 1.3329 0.8008 -0.0869 -0.0737 0.1801 380 GLN A CD 2963 O OE1 . GLN A 378 ? 0.8839 1.3632 0.8095 -0.0883 -0.0860 0.1870 380 GLN A OE1 2964 N NE2 . GLN A 378 ? 0.8622 1.3361 0.8100 -0.0632 -0.0596 0.1279 380 GLN A NE2 2965 N N . ARG A 379 ? 0.7935 1.4051 0.8008 -0.0939 -0.0154 0.1823 381 ARG A N 2966 C CA . ARG A 379 ? 0.7230 1.2396 0.7536 -0.0758 -0.0192 0.1481 381 ARG A CA 2967 C C . ARG A 379 ? 0.6680 1.0967 0.7191 -0.0962 -0.0365 0.1810 381 ARG A C 2968 O O . ARG A 379 ? 0.6578 1.0131 0.7093 -0.0915 -0.0493 0.1725 381 ARG A O 2969 C CB . ARG A 379 ? 0.7254 1.2112 0.7488 -0.0439 -0.0184 0.0911 381 ARG A CB 2970 C CG . ARG A 379 ? 0.7606 1.3079 0.7898 -0.0157 -0.0019 0.0426 381 ARG A CG 2971 C CD . ARG A 379 ? 0.7784 1.2655 0.8243 0.0146 -0.0062 -0.0115 381 ARG A CD 2972 N NE . ARG A 379 ? 0.7881 1.2430 0.8689 0.0247 -0.0034 -0.0217 381 ARG A NE 2973 C CZ . ARG A 379 ? 0.7763 1.1463 0.8762 0.0210 -0.0133 -0.0140 381 ARG A CZ 2974 N NH1 . ARG A 379 ? 0.7657 1.0713 0.8562 0.0090 -0.0258 0.0007 381 ARG A NH1 2975 N NH2 . ARG A 379 ? 0.7222 1.0783 0.8520 0.0301 -0.0111 -0.0213 381 ARG A NH2 2976 N N . PRO A 380 ? 0.6331 1.0754 0.7041 -0.1192 -0.0378 0.2171 382 PRO A N 2977 C CA . PRO A 380 ? 0.6009 0.9632 0.6958 -0.1367 -0.0561 0.2405 382 PRO A CA 2978 C C . PRO A 380 ? 0.5481 0.8307 0.6557 -0.1183 -0.0592 0.2039 382 PRO A C 2979 O O . PRO A 380 ? 0.5327 0.7478 0.6515 -0.1255 -0.0756 0.2114 382 PRO A O 2980 C CB . PRO A 380 ? 0.6104 1.0141 0.7278 -0.1616 -0.0546 0.2758 382 PRO A CB 2981 C CG . PRO A 380 ? 0.6244 1.1294 0.7316 -0.1512 -0.0314 0.2632 382 PRO A CG 2982 C CD . PRO A 380 ? 0.6455 1.1845 0.7192 -0.1326 -0.0247 0.2405 382 PRO A CD 2983 N N . GLU A 381 ? 0.5087 0.8031 0.6176 -0.0948 -0.0453 0.1660 383 GLU A N 2984 C CA . GLU A 381 ? 0.4789 0.7080 0.6007 -0.0791 -0.0484 0.1368 383 GLU A CA 2985 C C . GLU A 381 ? 0.4676 0.6489 0.5775 -0.0633 -0.0543 0.1121 383 GLU A C 2986 O O . GLU A 381 ? 0.4440 0.5784 0.5644 -0.0524 -0.0570 0.0919 383 GLU A O 2987 C CB . GLU A 381 ? 0.4640 0.7208 0.6003 -0.0623 -0.0358 0.1132 383 GLU A CB 2988 C CG . GLU A 381 ? 0.5478 0.8693 0.6761 -0.0414 -0.0215 0.0874 383 GLU A CG 2989 C CD . GLU A 381 ? 0.6555 1.0664 0.7755 -0.0541 -0.0112 0.1099 383 GLU A CD 2990 O OE1 . GLU A 381 ? 0.7134 1.1662 0.8092 -0.0528 -0.0081 0.1087 383 GLU A OE1 2991 O OE2 . GLU A 381 ? 0.7134 1.1597 0.8506 -0.0674 -0.0068 0.1311 383 GLU A OE2 2992 N N . ASN A 382 ? 0.4710 0.6709 0.5600 -0.0637 -0.0567 0.1162 384 ASN A N 2993 C CA . ASN A 382 ? 0.4599 0.6261 0.5380 -0.0495 -0.0625 0.0927 384 ASN A CA 2994 C C . ASN A 382 ? 0.4323 0.5268 0.5238 -0.0508 -0.0741 0.0913 384 ASN A C 2995 O O . ASN A 382 ? 0.4113 0.4759 0.5093 -0.0367 -0.0736 0.0653 384 ASN A O 2996 C CB . ASN A 382 ? 0.4769 0.6763 0.5307 -0.0550 -0.0673 0.1059 384 ASN A CB 2997 C CG . ASN A 382 ? 0.5234 0.7960 0.5579 -0.0416 -0.0549 0.0828 384 ASN A CG 2998 O OD1 . ASN A 382 ? 0.5410 0.8300 0.5846 -0.0232 -0.0442 0.0493 384 ASN A OD1 2999 N ND2 . ASN A 382 ? 0.5844 0.9063 0.5947 -0.0499 -0.0577 0.0999 384 ASN A ND2 3000 N N . TYR A 383 ? 0.4368 0.5071 0.5367 -0.0680 -0.0855 0.1187 385 TYR A N 3001 C CA . TYR A 383 ? 0.4246 0.4356 0.5375 -0.0665 -0.0969 0.1120 385 TYR A CA 3002 C C . TYR A 383 ? 0.4021 0.3942 0.5309 -0.0633 -0.0927 0.0978 385 TYR A C 3003 O O . TYR A 383 ? 0.3819 0.3432 0.5166 -0.0546 -0.0950 0.0798 385 TYR A O 3004 C CB . TYR A 383 ? 0.4405 0.4273 0.5637 -0.0821 -0.1147 0.1400 385 TYR A CB 3005 C CG . TYR A 383 ? 0.4498 0.4440 0.5602 -0.0825 -0.1238 0.1534 385 TYR A CG 3006 C CD1 . TYR A 383 ? 0.4128 0.3824 0.5193 -0.0683 -0.1286 0.1333 385 TYR A CD1 3007 C CD2 . TYR A 383 ? 0.4677 0.4985 0.5720 -0.0994 -0.1295 0.1907 385 TYR A CD2 3008 C CE1 . TYR A 383 ? 0.4288 0.4099 0.5238 -0.0690 -0.1386 0.1469 385 TYR A CE1 3009 C CE2 . TYR A 383 ? 0.4738 0.5172 0.5660 -0.1012 -0.1397 0.2073 385 TYR A CE2 3010 C CZ . TYR A 383 ? 0.4738 0.4916 0.5608 -0.0851 -0.1444 0.1841 385 TYR A CZ 3011 O OH . TYR A 383 ? 0.5674 0.6027 0.6430 -0.0878 -0.1563 0.2032 385 TYR A OH 3012 N N . ARG A 384 ? 0.3861 0.4040 0.5224 -0.0713 -0.0868 0.1078 386 ARG A N 3013 C CA . ARG A 384 ? 0.3747 0.3824 0.5252 -0.0686 -0.0839 0.0964 386 ARG A CA 3014 C C . ARG A 384 ? 0.3499 0.3568 0.4992 -0.0496 -0.0758 0.0720 386 ARG A C 3015 O O . ARG A 384 ? 0.3495 0.3341 0.5069 -0.0457 -0.0783 0.0623 386 ARG A O 3016 C CB . ARG A 384 ? 0.3584 0.4032 0.5188 -0.0798 -0.0788 0.1120 386 ARG A CB 3017 C CG . ARG A 384 ? 0.3363 0.3779 0.5125 -0.0799 -0.0782 0.1049 386 ARG A CG 3018 C CD . ARG A 384 ? 0.3680 0.4604 0.5541 -0.0864 -0.0701 0.1180 386 ARG A CD 3019 N NE . ARG A 384 ? 0.3262 0.4555 0.5102 -0.0674 -0.0563 0.1040 386 ARG A NE 3020 C CZ . ARG A 384 ? 0.3567 0.5437 0.5474 -0.0665 -0.0460 0.1098 386 ARG A CZ 3021 N NH1 . ARG A 384 ? 0.3748 0.5936 0.5740 -0.0876 -0.0469 0.1355 386 ARG A NH1 3022 N NH2 . ARG A 384 ? 0.3092 0.5256 0.5023 -0.0439 -0.0357 0.0880 386 ARG A NH2 3023 N N . GLU A 385 ? 0.3633 0.3982 0.5050 -0.0385 -0.0679 0.0626 387 GLU A N 3024 C CA . GLU A 385 ? 0.3718 0.4031 0.5219 -0.0210 -0.0643 0.0400 387 GLU A CA 3025 C C . GLU A 385 ? 0.3499 0.3453 0.4974 -0.0164 -0.0715 0.0292 387 GLU A C 3026 O O . GLU A 385 ? 0.3394 0.3162 0.5011 -0.0105 -0.0738 0.0211 387 GLU A O 3027 C CB . GLU A 385 ? 0.3905 0.4633 0.5382 -0.0073 -0.0561 0.0245 387 GLU A CB 3028 C CG . GLU A 385 ? 0.4850 0.6062 0.6360 -0.0125 -0.0474 0.0367 387 GLU A CG 3029 C CD . GLU A 385 ? 0.6078 0.7672 0.7738 0.0073 -0.0392 0.0144 387 GLU A CD 3030 O OE1 . GLU A 385 ? 0.6401 0.8228 0.8241 0.0072 -0.0347 0.0213 387 GLU A OE1 3031 O OE2 . GLU A 385 ? 0.6591 0.8264 0.8217 0.0240 -0.0390 -0.0123 387 GLU A OE2 3032 N N . ALA A 386 ? 0.3338 0.3237 0.4659 -0.0206 -0.0762 0.0331 388 ALA A N 3033 C CA . ALA A 386 ? 0.3156 0.2779 0.4464 -0.0164 -0.0836 0.0231 388 ALA A CA 3034 C C . ALA A 386 ? 0.3141 0.2494 0.4563 -0.0211 -0.0880 0.0265 388 ALA A C 3035 O O . ALA A 386 ? 0.2924 0.2142 0.4428 -0.0166 -0.0905 0.0173 388 ALA A O 3036 C CB . ALA A 386 ? 0.3098 0.2753 0.4239 -0.0205 -0.0900 0.0307 388 ALA A CB 3037 N N . LEU A 387 ? 0.3180 0.2498 0.4625 -0.0308 -0.0900 0.0387 389 LEU A N 3038 C CA . LEU A 387 ? 0.3280 0.2429 0.4819 -0.0331 -0.0945 0.0349 389 LEU A CA 3039 C C . LEU A 387 ? 0.3362 0.2596 0.4997 -0.0306 -0.0896 0.0311 389 LEU A C 3040 O O . LEU A 387 ? 0.3478 0.2683 0.5170 -0.0295 -0.0915 0.0260 389 LEU A O 3041 C CB . LEU A 387 ? 0.3171 0.2234 0.4761 -0.0428 -0.1017 0.0419 389 LEU A CB 3042 C CG . LEU A 387 ? 0.3085 0.2026 0.4768 -0.0411 -0.1081 0.0284 389 LEU A CG 3043 C CD1 . LEU A 387 ? 0.3159 0.1984 0.4851 -0.0329 -0.1130 0.0195 389 LEU A CD1 3044 C CD2 . LEU A 387 ? 0.3644 0.2472 0.5441 -0.0497 -0.1188 0.0286 389 LEU A CD2 3045 N N . GLY A 388 ? 0.3315 0.2713 0.4993 -0.0304 -0.0843 0.0361 390 GLY A N 3046 C CA . GLY A 388 ? 0.3011 0.2492 0.4827 -0.0274 -0.0827 0.0372 390 GLY A CA 3047 C C . GLY A 388 ? 0.3094 0.2471 0.4995 -0.0195 -0.0850 0.0310 390 GLY A C 3048 O O . GLY A 388 ? 0.3101 0.2478 0.5114 -0.0219 -0.0882 0.0363 390 GLY A O 3049 N N . ASP A 389 ? 0.3062 0.2392 0.4924 -0.0120 -0.0850 0.0205 391 ASP A N 3050 C CA . ASP A 389 ? 0.3101 0.2299 0.5098 -0.0054 -0.0909 0.0112 391 ASP A CA 3051 C C . ASP A 389 ? 0.2976 0.2061 0.4962 -0.0115 -0.0958 0.0130 391 ASP A C 3052 O O . ASP A 389 ? 0.2959 0.1990 0.5130 -0.0137 -0.1014 0.0170 391 ASP A O 3053 C CB . ASP A 389 ? 0.3224 0.2460 0.5178 0.0054 -0.0911 -0.0071 391 ASP A CB 3054 C CG . ASP A 389 ? 0.3830 0.3255 0.5897 0.0162 -0.0869 -0.0147 391 ASP A CG 3055 O OD1 . ASP A 389 ? 0.3734 0.3119 0.6049 0.0197 -0.0899 -0.0099 391 ASP A OD1 3056 O OD2 . ASP A 389 ? 0.4232 0.3902 0.6157 0.0217 -0.0809 -0.0246 391 ASP A OD2 3057 N N . VAL A 390 ? 0.2921 0.2001 0.4738 -0.0150 -0.0950 0.0124 392 VAL A N 3058 C CA . VAL A 390 ? 0.2952 0.2004 0.4790 -0.0185 -0.0987 0.0121 392 VAL A CA 3059 C C . VAL A 390 ? 0.2773 0.1967 0.4728 -0.0247 -0.0974 0.0213 392 VAL A C 3060 O O . VAL A 390 ? 0.2501 0.1757 0.4591 -0.0283 -0.1006 0.0260 392 VAL A O 3061 C CB . VAL A 390 ? 0.3009 0.2028 0.4720 -0.0191 -0.1003 0.0103 392 VAL A CB 3062 C CG1 . VAL A 390 ? 0.3144 0.2221 0.4931 -0.0196 -0.1032 0.0060 392 VAL A CG1 3063 C CG2 . VAL A 390 ? 0.3144 0.2103 0.4744 -0.0157 -0.1039 0.0076 392 VAL A CG2 3064 N N . VAL A 391 ? 0.2742 0.2040 0.4928 -0.0208 -0.0809 0.0069 393 VAL A N 3065 C CA . VAL A 391 ? 0.2671 0.1993 0.4960 -0.0156 -0.0740 -0.0013 393 VAL A CA 3066 C C . VAL A 391 ? 0.2477 0.1957 0.4774 -0.0148 -0.0655 -0.0074 393 VAL A C 3067 O O . VAL A 391 ? 0.2458 0.1984 0.4861 -0.0089 -0.0610 -0.0140 393 VAL A O 3068 C CB . VAL A 391 ? 0.2667 0.1886 0.4895 -0.0201 -0.0723 -0.0013 393 VAL A CB 3069 C CG1 . VAL A 391 ? 0.2569 0.1811 0.4857 -0.0164 -0.0650 -0.0100 393 VAL A CG1 3070 C CG2 . VAL A 391 ? 0.3142 0.2175 0.5372 -0.0197 -0.0809 0.0039 393 VAL A CG2 3071 N N . GLY A 392 ? 0.2123 0.1679 0.4310 -0.0209 -0.0626 -0.0055 394 GLY A N 3072 C CA . GLY A 392 ? 0.2005 0.1688 0.4197 -0.0199 -0.0554 -0.0108 394 GLY A CA 3073 C C . GLY A 392 ? 0.2151 0.1892 0.4399 -0.0157 -0.0568 -0.0126 394 GLY A C 3074 O O . GLY A 392 ? 0.1902 0.1711 0.4216 -0.0120 -0.0518 -0.0183 394 GLY A O 3075 N N . ASP A 393 ? 0.2195 0.1907 0.4411 -0.0170 -0.0640 -0.0076 395 ASP A N 3076 C CA . ASP A 393 ? 0.2426 0.2199 0.4689 -0.0144 -0.0665 -0.0090 395 ASP A CA 3077 C C . ASP A 393 ? 0.2406 0.2188 0.4855 -0.0074 -0.0676 -0.0124 395 ASP A C 3078 O O . ASP A 393 ? 0.2535 0.2398 0.5063 -0.0048 -0.0643 -0.0169 395 ASP A O 3079 C CB . ASP A 393 ? 0.2585 0.2314 0.4751 -0.0184 -0.0756 -0.0023 395 ASP A CB 3080 C CG . ASP A 393 ? 0.2955 0.2693 0.4919 -0.0260 -0.0725 0.0000 395 ASP A CG 3081 O OD1 . ASP A 393 ? 0.2619 0.2289 0.4460 -0.0309 -0.0794 0.0065 395 ASP A OD1 3082 O OD2 . ASP A 393 ? 0.2431 0.2238 0.4362 -0.0270 -0.0632 -0.0045 395 ASP A OD2 3083 N N . TYR A 394 ? 0.2464 0.2162 0.4990 -0.0044 -0.0718 -0.0103 396 TYR A N 3084 C CA . TYR A 394 ? 0.2427 0.2139 0.5150 0.0030 -0.0725 -0.0138 396 TYR A CA 3085 C C . TYR A 394 ? 0.2323 0.2081 0.5100 0.0057 -0.0617 -0.0217 396 TYR A C 3086 O O . TYR A 394 ? 0.2206 0.2043 0.5106 0.0093 -0.0583 -0.0260 396 TYR A O 3087 C CB . TYR A 394 ? 0.2363 0.1952 0.5149 0.0064 -0.0794 -0.0101 396 TYR A CB 3088 C CG . TYR A 394 ? 0.2305 0.1901 0.5310 0.0152 -0.0780 -0.0151 396 TYR A CG 3089 C CD1 . TYR A 394 ? 0.2379 0.2087 0.5564 0.0198 -0.0800 -0.0166 396 TYR A CD1 3090 C CD2 . TYR A 394 ? 0.2856 0.2342 0.5895 0.0190 -0.0749 -0.0184 396 TYR A CD2 3091 C CE1 . TYR A 394 ? 0.2065 0.1799 0.5489 0.0286 -0.0782 -0.0213 396 TYR A CE1 3092 C CE2 . TYR A 394 ? 0.2681 0.2168 0.5935 0.0282 -0.0728 -0.0238 396 TYR A CE2 3093 C CZ . TYR A 394 ? 0.2424 0.2047 0.5873 0.0330 -0.0739 -0.0252 396 TYR A CZ 3094 O OH . TYR A 394 ? 0.3069 0.2721 0.6741 0.0418 -0.0700 -0.0311 396 TYR A OH 3095 N N . ASN A 395 ? 0.2096 0.1796 0.4776 0.0033 -0.0570 -0.0231 397 ASN A N 3096 C CA . ASN A 395 ? 0.2159 0.1869 0.4860 0.0052 -0.0482 -0.0300 397 ASN A CA 3097 C C . ASN A 395 ? 0.2034 0.1834 0.4670 0.0025 -0.0416 -0.0332 397 ASN A C 3098 O O . ASN A 395 ? 0.1964 0.1782 0.4630 0.0044 -0.0349 -0.0387 397 ASN A O 3099 C CB . ASN A 395 ? 0.1963 0.1556 0.4585 0.0032 -0.0474 -0.0303 397 ASN A CB 3100 C CG . ASN A 395 ? 0.2417 0.1897 0.5125 0.0077 -0.0519 -0.0297 397 ASN A CG 3101 O OD1 . ASN A 395 ? 0.2012 0.1489 0.4844 0.0140 -0.0481 -0.0354 397 ASN A OD1 3102 N ND2 . ASN A 395 ? 0.2263 0.1648 0.4917 0.0049 -0.0600 -0.0229 397 ASN A ND2 3103 N N . PHE A 396 ? 0.1929 0.1769 0.4462 -0.0019 -0.0431 -0.0299 398 PHE A N 3104 C CA . PHE A 396 ? 0.2057 0.1961 0.4528 -0.0037 -0.0374 -0.0328 398 PHE A CA 3105 C C . PHE A 396 ? 0.2153 0.2125 0.4603 -0.0048 -0.0386 -0.0320 398 PHE A C 3106 O O . PHE A 396 ? 0.2137 0.2154 0.4618 -0.0037 -0.0351 -0.0354 398 PHE A O 3107 C CB . PHE A 396 ? 0.1892 0.1781 0.4260 -0.0076 -0.0358 -0.0318 398 PHE A CB 3108 C CG . PHE A 396 ? 0.2259 0.2070 0.4627 -0.0076 -0.0346 -0.0337 398 PHE A CG 3109 C CD1 . PHE A 396 ? 0.2339 0.2062 0.4696 -0.0092 -0.0389 -0.0305 398 PHE A CD1 3110 C CD2 . PHE A 396 ? 0.2027 0.1831 0.4390 -0.0064 -0.0295 -0.0386 398 PHE A CD2 3111 C CE1 . PHE A 396 ? 0.2077 0.1701 0.4422 -0.0094 -0.0382 -0.0329 398 PHE A CE1 3112 C CE2 . PHE A 396 ? 0.2416 0.2129 0.4749 -0.0071 -0.0287 -0.0410 398 PHE A CE2 3113 C CZ . PHE A 396 ? 0.2210 0.1831 0.4542 -0.0083 -0.0329 -0.0386 398 PHE A CZ 3114 N N . ILE A 397 ? 0.2103 0.2069 0.4481 -0.0077 -0.0432 -0.0277 399 ILE A N 3115 C CA . ILE A 397 ? 0.2240 0.2252 0.4549 -0.0097 -0.0432 -0.0279 399 ILE A CA 3116 C C . ILE A 397 ? 0.2218 0.2252 0.4604 -0.0083 -0.0472 -0.0285 399 ILE A C 3117 O O . ILE A 397 ? 0.2317 0.2386 0.4702 -0.0083 -0.0445 -0.0317 399 ILE A O 3118 C CB . ILE A 397 ? 0.2318 0.2316 0.4501 -0.0143 -0.0455 -0.0237 399 ILE A CB 3119 C CG1 . ILE A 397 ? 0.2394 0.2397 0.4531 -0.0165 -0.0411 -0.0232 399 ILE A CG1 3120 C CG2 . ILE A 397 ? 0.2468 0.2492 0.4568 -0.0161 -0.0458 -0.0247 399 ILE A CG2 3121 C CD1 . ILE A 397 ? 0.2751 0.2765 0.4769 -0.0218 -0.0407 -0.0198 399 ILE A CD1 3122 N N . CYS A 398 ? 0.2180 0.2193 0.4640 -0.0073 -0.0542 -0.0251 400 CYS A N 3123 C CA . CYS A 398 ? 0.2131 0.2186 0.4685 -0.0065 -0.0588 -0.0255 400 CYS A CA 3124 C C . CYS A 398 ? 0.2054 0.2168 0.4754 -0.0033 -0.0530 -0.0305 400 CYS A C 3125 O O . CYS A 398 ? 0.2102 0.2265 0.4841 -0.0046 -0.0531 -0.0324 400 CYS A O 3126 C CB . CYS A 398 ? 0.2346 0.2374 0.4968 -0.0057 -0.0694 -0.0201 400 CYS A CB 3127 S SG . CYS A 398 ? 0.2608 0.2551 0.5015 -0.0114 -0.0754 -0.0135 400 CYS A SG 3128 N N . PRO A 399 ? 0.2085 0.2185 0.4857 0.0001 -0.0478 -0.0328 401 PRO A N 3129 C CA . PRO A 399 ? 0.2025 0.2180 0.4903 0.0017 -0.0411 -0.0376 401 PRO A CA 3130 C C . PRO A 399 ? 0.2040 0.2201 0.4808 -0.0013 -0.0354 -0.0402 401 PRO A C 3131 O O . PRO A 399 ? 0.1989 0.2197 0.4818 -0.0024 -0.0328 -0.0425 401 PRO A O 3132 C CB . PRO A 399 ? 0.1846 0.1960 0.4766 0.0052 -0.0357 -0.0403 401 PRO A CB 3133 C CG . PRO A 399 ? 0.1963 0.2009 0.4883 0.0068 -0.0430 -0.0360 401 PRO A CG 3134 C CD . PRO A 399 ? 0.2060 0.2090 0.4832 0.0022 -0.0483 -0.0314 401 PRO A CD 3135 N N . ALA A 400 ? 0.1933 0.2050 0.4555 -0.0028 -0.0339 -0.0396 402 ALA A N 3136 C CA . ALA A 400 ? 0.1956 0.2071 0.4488 -0.0046 -0.0295 -0.0419 402 ALA A CA 3137 C C . ALA A 400 ? 0.2113 0.2245 0.4623 -0.0068 -0.0329 -0.0417 402 ALA A C 3138 O O . ALA A 400 ? 0.2079 0.2210 0.4580 -0.0081 -0.0301 -0.0440 402 ALA A O 3139 C CB . ALA A 400 ? 0.1794 0.1880 0.4208 -0.0051 -0.0282 -0.0411 402 ALA A CB 3140 N N . LEU A 401 ? 0.2014 0.2144 0.4492 -0.0081 -0.0392 -0.0390 403 LEU A N 3141 C CA . LEU A 401 ? 0.2120 0.2246 0.4541 -0.0110 -0.0425 -0.0396 403 LEU A CA 3142 C C . LEU A 401 ? 0.2143 0.2315 0.4704 -0.0119 -0.0451 -0.0402 403 LEU A C 3143 O O . LEU A 401 ? 0.2097 0.2266 0.4644 -0.0145 -0.0451 -0.0422 403 LEU A O 3144 C CB . LEU A 401 ? 0.2224 0.2326 0.4551 -0.0132 -0.0489 -0.0365 403 LEU A CB 3145 C CG . LEU A 401 ? 0.2403 0.2476 0.4581 -0.0138 -0.0453 -0.0364 403 LEU A CG 3146 C CD1 . LEU A 401 ? 0.1923 0.1973 0.4033 -0.0163 -0.0510 -0.0317 403 LEU A CD1 3147 C CD2 . LEU A 401 ? 0.1710 0.1759 0.3779 -0.0149 -0.0424 -0.0404 403 LEU A CD2 3148 N N . GLU A 402 ? 0.2308 0.2525 0.5018 -0.0097 -0.0473 -0.0386 404 GLU A N 3149 C CA . GLU A 402 ? 0.2330 0.2622 0.5214 -0.0103 -0.0493 -0.0392 404 GLU A CA 3150 C C . GLU A 402 ? 0.2167 0.2483 0.5096 -0.0112 -0.0404 -0.0431 404 GLU A C 3151 O O . GLU A 402 ? 0.2281 0.2633 0.5263 -0.0149 -0.0409 -0.0441 404 GLU A O 3152 C CB . GLU A 402 ? 0.2197 0.2536 0.5252 -0.0065 -0.0537 -0.0369 404 GLU A CB 3153 C CG . GLU A 402 ? 0.3182 0.3634 0.6468 -0.0065 -0.0544 -0.0381 404 GLU A CG 3154 C CD . GLU A 402 ? 0.4357 0.4849 0.7687 -0.0107 -0.0660 -0.0352 404 GLU A CD 3155 O OE1 . GLU A 402 ? 0.3347 0.3762 0.6482 -0.0145 -0.0712 -0.0337 404 GLU A OE1 3156 O OE2 . GLU A 402 ? 0.4902 0.5506 0.8467 -0.0099 -0.0701 -0.0346 404 GLU A OE2 3157 N N . PHE A 403 ? 0.2052 0.2340 0.4945 -0.0089 -0.0328 -0.0448 405 PHE A N 3158 C CA . PHE A 403 ? 0.2005 0.2286 0.4882 -0.0106 -0.0246 -0.0476 405 PHE A CA 3159 C C . PHE A 403 ? 0.1956 0.2182 0.4706 -0.0145 -0.0253 -0.0480 405 PHE A C 3160 O O . PHE A 403 ? 0.1957 0.2193 0.4738 -0.0183 -0.0227 -0.0492 405 PHE A O 3161 C CB . PHE A 403 ? 0.1730 0.1957 0.4524 -0.0081 -0.0184 -0.0489 405 PHE A CB 3162 C CG . PHE A 403 ? 0.2094 0.2294 0.4835 -0.0106 -0.0111 -0.0510 405 PHE A CG 3163 C CD1 . PHE A 403 ? 0.2033 0.2279 0.4876 -0.0112 -0.0041 -0.0534 405 PHE A CD1 3164 C CD2 . PHE A 403 ? 0.1911 0.2039 0.4504 -0.0125 -0.0110 -0.0505 405 PHE A CD2 3165 C CE1 . PHE A 403 ? 0.1994 0.2205 0.4764 -0.0148 0.0028 -0.0547 405 PHE A CE1 3166 C CE2 . PHE A 403 ? 0.2080 0.2164 0.4611 -0.0154 -0.0054 -0.0514 405 PHE A CE2 3167 C CZ . PHE A 403 ? 0.1874 0.1997 0.4482 -0.0172 0.0016 -0.0533 405 PHE A CZ 3168 N N . THR A 404 ? 0.1898 0.2062 0.4507 -0.0137 -0.0281 -0.0473 406 THR A N 3169 C CA . THR A 404 ? 0.1886 0.1983 0.4374 -0.0159 -0.0284 -0.0485 406 THR A CA 3170 C C . THR A 404 ? 0.2026 0.2133 0.4549 -0.0203 -0.0336 -0.0488 406 THR A C 3171 O O . THR A 404 ? 0.2142 0.2204 0.4636 -0.0237 -0.0321 -0.0503 406 THR A O 3172 C CB . THR A 404 ? 0.2001 0.2049 0.4356 -0.0135 -0.0294 -0.0484 406 THR A CB 3173 O OG1 . THR A 404 ? 0.2013 0.2067 0.4360 -0.0104 -0.0256 -0.0477 406 THR A OG1 3174 C CG2 . THR A 404 ? 0.1723 0.1690 0.3962 -0.0140 -0.0285 -0.0508 406 THR A CG2 3175 N N . LYS A 405 ? 0.2095 0.2250 0.4677 -0.0209 -0.0404 -0.0472 407 LYS A N 3176 C CA . LYS A 405 ? 0.2393 0.2559 0.5009 -0.0260 -0.0468 -0.0474 407 LYS A CA 3177 C C . LYS A 405 ? 0.2326 0.2559 0.5098 -0.0293 -0.0439 -0.0479 407 LYS A C 3178 O O . LYS A 405 ? 0.2209 0.2403 0.4952 -0.0345 -0.0446 -0.0492 407 LYS A O 3179 C CB . LYS A 405 ? 0.2458 0.2671 0.5127 -0.0268 -0.0564 -0.0446 407 LYS A CB 3180 C CG . LYS A 405 ? 0.3466 0.3635 0.6010 -0.0243 -0.0588 -0.0429 407 LYS A CG 3181 C CD . LYS A 405 ? 0.4727 0.4909 0.7274 -0.0270 -0.0705 -0.0394 407 LYS A CD 3182 C CE . LYS A 405 ? 0.5157 0.5294 0.7577 -0.0250 -0.0727 -0.0363 407 LYS A CE 3183 N NZ . LYS A 405 ? 0.5789 0.5908 0.8159 -0.0283 -0.0850 -0.0318 407 LYS A NZ 3184 N N . LYS A 406 ? 0.2232 0.2561 0.5170 -0.0265 -0.0404 -0.0471 408 LYS A N 3185 C CA . LYS A 406 ? 0.2388 0.2815 0.5510 -0.0301 -0.0368 -0.0478 408 LYS A CA 3186 C C . LYS A 406 ? 0.2383 0.2742 0.5412 -0.0335 -0.0283 -0.0495 408 LYS A C 3187 O O . LYS A 406 ? 0.2424 0.2808 0.5514 -0.0397 -0.0268 -0.0499 408 LYS A O 3188 C CB . LYS A 406 ? 0.2338 0.2880 0.5661 -0.0254 -0.0330 -0.0478 408 LYS A CB 3189 C CG . LYS A 406 ? 0.2778 0.3386 0.6229 -0.0221 -0.0427 -0.0453 408 LYS A CG 3190 C CD . LYS A 406 ? 0.4334 0.5043 0.7950 -0.0272 -0.0505 -0.0440 408 LYS A CD 3191 C CE . LYS A 406 ? 0.4823 0.5599 0.8579 -0.0238 -0.0624 -0.0405 408 LYS A CE 3192 N NZ . LYS A 406 ? 0.5683 0.6547 0.9571 -0.0304 -0.0710 -0.0393 408 LYS A NZ 3193 N N . PHE A 407 ? 0.2346 0.2617 0.5227 -0.0299 -0.0234 -0.0501 409 PHE A N 3194 C CA . PHE A 407 ? 0.2379 0.2565 0.5152 -0.0331 -0.0173 -0.0507 409 PHE A CA 3195 C C . PHE A 407 ? 0.2566 0.2648 0.5225 -0.0376 -0.0217 -0.0509 409 PHE A C 3196 O O . PHE A 407 ? 0.2652 0.2691 0.5296 -0.0435 -0.0191 -0.0507 409 PHE A O 3197 C CB . PHE A 407 ? 0.2402 0.2518 0.5048 -0.0282 -0.0132 -0.0508 409 PHE A CB 3198 C CG . PHE A 407 ? 0.2510 0.2548 0.5058 -0.0312 -0.0067 -0.0506 409 PHE A CG 3199 C CD1 . PHE A 407 ? 0.2017 0.2095 0.4607 -0.0320 0.0011 -0.0513 409 PHE A CD1 3200 C CD2 . PHE A 407 ? 0.2092 0.2004 0.4498 -0.0331 -0.0087 -0.0499 409 PHE A CD2 3201 C CE1 . PHE A 407 ? 0.2342 0.2333 0.4810 -0.0358 0.0064 -0.0505 409 PHE A CE1 3202 C CE2 . PHE A 407 ? 0.2371 0.2191 0.4671 -0.0361 -0.0042 -0.0486 409 PHE A CE2 3203 C CZ . PHE A 407 ? 0.1736 0.1598 0.4061 -0.0381 0.0033 -0.0486 409 PHE A CZ 3204 N N . SER A 408 ? 0.2680 0.2707 0.5243 -0.0351 -0.0280 -0.0514 410 SER A N 3205 C CA . SER A 408 ? 0.2756 0.2660 0.5191 -0.0383 -0.0315 -0.0529 410 SER A CA 3206 C C . SER A 408 ? 0.2892 0.2827 0.5413 -0.0460 -0.0364 -0.0530 410 SER A C 3207 O O . SER A 408 ? 0.2823 0.2651 0.5262 -0.0509 -0.0381 -0.0541 410 SER A O 3208 C CB . SER A 408 ? 0.2861 0.2708 0.5170 -0.0336 -0.0355 -0.0544 410 SER A CB 3209 O OG . SER A 408 ? 0.3021 0.2934 0.5380 -0.0352 -0.0423 -0.0540 410 SER A OG 3210 N N . GLU A 409 ? 0.3060 0.3139 0.5757 -0.0473 -0.0394 -0.0517 411 GLU A N 3211 C CA . GLU A 409 ? 0.3147 0.3274 0.5947 -0.0552 -0.0456 -0.0515 411 GLU A CA 3212 C C . GLU A 409 ? 0.3264 0.3395 0.6129 -0.0624 -0.0400 -0.0511 411 GLU A C 3213 O O . GLU A 409 ? 0.3389 0.3537 0.6319 -0.0703 -0.0444 -0.0510 411 GLU A O 3214 C CB . GLU A 409 ? 0.3174 0.3470 0.6183 -0.0545 -0.0508 -0.0496 411 GLU A CB 3215 C CG . GLU A 409 ? 0.3923 0.4187 0.6850 -0.0533 -0.0614 -0.0492 411 GLU A CG 3216 C CD . GLU A 409 ? 0.5276 0.5675 0.8373 -0.0492 -0.0663 -0.0464 411 GLU A CD 3217 O OE1 . GLU A 409 ? 0.5660 0.6204 0.8992 -0.0480 -0.0626 -0.0454 411 GLU A OE1 3218 O OE2 . GLU A 409 ? 0.5956 0.6311 0.8949 -0.0472 -0.0739 -0.0452 411 GLU A OE2 3219 N N . TRP A 410 ? 0.3146 0.3255 0.5980 -0.0607 -0.0305 -0.0507 412 TRP A N 3220 C CA . TRP A 410 ? 0.3158 0.3268 0.6036 -0.0686 -0.0247 -0.0498 412 TRP A CA 3221 C C . TRP A 410 ? 0.3402 0.3307 0.6066 -0.0709 -0.0242 -0.0497 412 TRP A C 3222 O O . TRP A 410 ? 0.3640 0.3500 0.6281 -0.0772 -0.0187 -0.0481 412 TRP A O 3223 C CB . TRP A 410 ? 0.3086 0.3312 0.6076 -0.0669 -0.0142 -0.0492 412 TRP A CB 3224 C CG . TRP A 410 ? 0.2758 0.3192 0.6009 -0.0663 -0.0148 -0.0495 412 TRP A CG 3225 C CD1 . TRP A 410 ? 0.2653 0.3180 0.6005 -0.0580 -0.0173 -0.0500 412 TRP A CD1 3226 C CD2 . TRP A 410 ? 0.3133 0.3713 0.6602 -0.0744 -0.0132 -0.0491 412 TRP A CD2 3227 N NE1 . TRP A 410 ? 0.2678 0.3400 0.6308 -0.0594 -0.0181 -0.0499 412 TRP A NE1 3228 C CE2 . TRP A 410 ? 0.2809 0.3582 0.6527 -0.0693 -0.0152 -0.0495 412 TRP A CE2 3229 C CE3 . TRP A 410 ? 0.3119 0.3689 0.6608 -0.0857 -0.0105 -0.0480 412 TRP A CE3 3230 C CZ2 . TRP A 410 ? 0.2882 0.3853 0.6886 -0.0745 -0.0148 -0.0493 412 TRP A CZ2 3231 C CZ3 . TRP A 410 ? 0.3071 0.3849 0.6844 -0.0923 -0.0091 -0.0477 412 TRP A CZ3 3232 C CH2 . TRP A 410 ? 0.2567 0.3551 0.6603 -0.0862 -0.0114 -0.0485 412 TRP A CH2 3233 N N . GLY A 411 ? 0.3607 0.3378 0.6109 -0.0662 -0.0299 -0.0515 413 GLY A N 3234 C CA . GLY A 411 ? 0.3507 0.3066 0.5827 -0.0689 -0.0313 -0.0520 413 GLY A CA 3235 C C . GLY A 411 ? 0.3646 0.3084 0.5812 -0.0610 -0.0281 -0.0518 413 GLY A C 3236 O O . GLY A 411 ? 0.4038 0.3298 0.6062 -0.0602 -0.0303 -0.0527 413 GLY A O 3237 N N . ASN A 412 ? 0.3337 0.2869 0.5540 -0.0545 -0.0237 -0.0509 414 ASN A N 3238 C CA A ASN A 412 ? 0.3148 0.2572 0.5218 -0.0481 -0.0218 -0.0503 414 ASN A CA 3239 C CA B ASN A 412 ? 0.3167 0.2623 0.5259 -0.0476 -0.0211 -0.0502 414 ASN A CA 3240 C C . ASN A 412 ? 0.3129 0.2542 0.5147 -0.0394 -0.0251 -0.0529 414 ASN A C 3241 O O . ASN A 412 ? 0.2894 0.2408 0.4972 -0.0373 -0.0274 -0.0545 414 ASN A O 3242 C CB A ASN A 412 ? 0.2894 0.2372 0.4978 -0.0471 -0.0151 -0.0477 414 ASN A CB 3243 C CB B ASN A 412 ? 0.2819 0.2415 0.4999 -0.0451 -0.0155 -0.0490 414 ASN A CB 3244 C CG A ASN A 412 ? 0.2530 0.1943 0.4576 -0.0556 -0.0106 -0.0447 414 ASN A CG 3245 C CG B ASN A 412 ? 0.2649 0.2351 0.4958 -0.0524 -0.0102 -0.0479 414 ASN A CG 3246 O OD1 A ASN A 412 ? 0.1936 0.1468 0.4096 -0.0610 -0.0056 -0.0443 414 ASN A OD1 3247 O OD1 B ASN A 412 ? 0.2686 0.2342 0.4943 -0.0566 -0.0046 -0.0459 414 ASN A OD1 3248 N ND2 A ASN A 412 ? 0.1594 0.0817 0.3486 -0.0571 -0.0125 -0.0425 414 ASN A ND2 3249 N ND2 B ASN A 412 ? 0.1402 0.1248 0.3879 -0.0542 -0.0121 -0.0490 414 ASN A ND2 3250 N N . ASN A 413 ? 0.3181 0.2459 0.5081 -0.0348 -0.0258 -0.0532 415 ASN A N 3251 C CA . ASN A 413 ? 0.3256 0.2538 0.5117 -0.0261 -0.0272 -0.0559 415 ASN A CA 3252 C C . ASN A 413 ? 0.3149 0.2572 0.5074 -0.0214 -0.0244 -0.0544 415 ASN A C 3253 O O . ASN A 413 ? 0.3251 0.2696 0.5189 -0.0218 -0.0214 -0.0515 415 ASN A O 3254 C CB . ASN A 413 ? 0.3459 0.2589 0.5221 -0.0211 -0.0283 -0.0563 415 ASN A CB 3255 C CG . ASN A 413 ? 0.3758 0.2734 0.5443 -0.0227 -0.0317 -0.0597 415 ASN A CG 3256 O OD1 . ASN A 413 ? 0.3699 0.2680 0.5392 -0.0287 -0.0338 -0.0618 415 ASN A OD1 3257 N ND2 . ASN A 413 ? 0.3135 0.1960 0.4745 -0.0174 -0.0330 -0.0603 415 ASN A ND2 3258 N N . ALA A 414 ? 0.2943 0.2444 0.4887 -0.0178 -0.0255 -0.0564 416 ALA A N 3259 C CA . ALA A 414 ? 0.2658 0.2278 0.4659 -0.0144 -0.0237 -0.0550 416 ALA A CA 3260 C C . ALA A 414 ? 0.2612 0.2233 0.4564 -0.0088 -0.0242 -0.0573 416 ALA A C 3261 O O . ALA A 414 ? 0.2755 0.2324 0.4648 -0.0089 -0.0259 -0.0606 416 ALA A O 3262 C CB . ALA A 414 ? 0.2510 0.2238 0.4605 -0.0179 -0.0248 -0.0543 416 ALA A CB 3263 N N . PHE A 415 ? 0.2269 0.1947 0.4240 -0.0047 -0.0224 -0.0559 417 PHE A N 3264 C CA . PHE A 415 ? 0.2308 0.2012 0.4255 0.0002 -0.0216 -0.0579 417 PHE A CA 3265 C C . PHE A 415 ? 0.2310 0.2130 0.4307 0.0000 -0.0208 -0.0557 417 PHE A C 3266 O O . PHE A 415 ? 0.2373 0.2227 0.4414 -0.0007 -0.0202 -0.0530 417 PHE A O 3267 C CB . PHE A 415 ? 0.2335 0.1993 0.4276 0.0054 -0.0210 -0.0577 417 PHE A CB 3268 C CG . PHE A 415 ? 0.2418 0.1935 0.4305 0.0057 -0.0226 -0.0593 417 PHE A CG 3269 C CD1 . PHE A 415 ? 0.2328 0.1768 0.4197 0.0022 -0.0238 -0.0561 417 PHE A CD1 3270 C CD2 . PHE A 415 ? 0.2347 0.1790 0.4183 0.0088 -0.0225 -0.0641 417 PHE A CD2 3271 C CE1 . PHE A 415 ? 0.2468 0.1752 0.4274 0.0015 -0.0259 -0.0568 417 PHE A CE1 3272 C CE2 . PHE A 415 ? 0.2527 0.1811 0.4304 0.0087 -0.0246 -0.0657 417 PHE A CE2 3273 C CZ . PHE A 415 ? 0.2392 0.1593 0.4156 0.0050 -0.0267 -0.0616 417 PHE A CZ 3274 N N . PHE A 416 ? 0.2279 0.2146 0.4253 0.0000 -0.0206 -0.0568 418 PHE A N 3275 C CA . PHE A 416 ? 0.2110 0.2064 0.4121 -0.0011 -0.0206 -0.0539 418 PHE A CA 3276 C C . PHE A 416 ? 0.2218 0.2231 0.4212 0.0014 -0.0178 -0.0544 418 PHE A C 3277 O O . PHE A 416 ? 0.2398 0.2394 0.4332 0.0028 -0.0158 -0.0579 418 PHE A O 3278 C CB . PHE A 416 ? 0.2033 0.1995 0.4035 -0.0053 -0.0241 -0.0529 418 PHE A CB 3279 C CG . PHE A 416 ? 0.2178 0.2201 0.4232 -0.0064 -0.0254 -0.0492 418 PHE A CG 3280 C CD1 . PHE A 416 ? 0.1802 0.1864 0.3819 -0.0066 -0.0245 -0.0478 418 PHE A CD1 3281 C CD2 . PHE A 416 ? 0.1498 0.1534 0.3641 -0.0074 -0.0267 -0.0474 418 PHE A CD2 3282 C CE1 . PHE A 416 ? 0.2234 0.2327 0.4291 -0.0081 -0.0264 -0.0439 418 PHE A CE1 3283 C CE2 . PHE A 416 ? 0.1818 0.1888 0.4008 -0.0075 -0.0280 -0.0445 418 PHE A CE2 3284 C CZ . PHE A 416 ? 0.1701 0.1789 0.3845 -0.0080 -0.0285 -0.0425 418 PHE A CZ 3285 N N . TYR A 417 ? 0.2004 0.2083 0.4049 0.0017 -0.0170 -0.0516 419 TYR A N 3286 C CA . TYR A 417 ? 0.2247 0.2404 0.4299 0.0030 -0.0139 -0.0518 419 TYR A CA 3287 C C . TYR A 417 ? 0.2134 0.2342 0.4183 -0.0013 -0.0145 -0.0482 419 TYR A C 3288 O O . TYR A 417 ? 0.2022 0.2211 0.4095 -0.0034 -0.0175 -0.0454 419 TYR A O 3289 C CB . TYR A 417 ? 0.2181 0.2381 0.4309 0.0067 -0.0131 -0.0514 419 TYR A CB 3290 C CG . TYR A 417 ? 0.2028 0.2236 0.4196 0.0045 -0.0157 -0.0477 419 TYR A CG 3291 C CD1 . TYR A 417 ? 0.2090 0.2225 0.4252 0.0046 -0.0179 -0.0472 419 TYR A CD1 3292 C CD2 . TYR A 417 ? 0.2057 0.2331 0.4252 0.0016 -0.0157 -0.0450 419 TYR A CD2 3293 C CE1 . TYR A 417 ? 0.2421 0.2549 0.4595 0.0022 -0.0195 -0.0448 419 TYR A CE1 3294 C CE2 . TYR A 417 ? 0.2117 0.2376 0.4332 -0.0007 -0.0182 -0.0426 419 TYR A CE2 3295 C CZ . TYR A 417 ? 0.2666 0.2853 0.4866 -0.0002 -0.0198 -0.0429 419 TYR A CZ 3296 O OH . TYR A 417 ? 0.1953 0.2114 0.4151 -0.0027 -0.0214 -0.0415 419 TYR A OH 3297 N N . TYR A 418 ? 0.2186 0.2457 0.4209 -0.0023 -0.0112 -0.0483 420 TYR A N 3298 C CA . TYR A 418 ? 0.1974 0.2283 0.3986 -0.0071 -0.0118 -0.0441 420 TYR A CA 3299 C C . TYR A 418 ? 0.2171 0.2585 0.4249 -0.0069 -0.0077 -0.0437 420 TYR A C 3300 O O . TYR A 418 ? 0.2048 0.2525 0.4114 -0.0057 -0.0022 -0.0465 420 TYR A O 3301 C CB . TYR A 418 ? 0.2014 0.2298 0.3908 -0.0108 -0.0114 -0.0441 420 TYR A CB 3302 C CG . TYR A 418 ? 0.2104 0.2396 0.3952 -0.0167 -0.0131 -0.0388 420 TYR A CG 3303 C CD1 . TYR A 418 ? 0.1980 0.2226 0.3862 -0.0184 -0.0190 -0.0344 420 TYR A CD1 3304 C CD2 . TYR A 418 ? 0.2281 0.2619 0.4044 -0.0206 -0.0083 -0.0384 420 TYR A CD2 3305 C CE1 . TYR A 418 ? 0.2886 0.3110 0.4716 -0.0238 -0.0218 -0.0291 420 TYR A CE1 3306 C CE2 . TYR A 418 ? 0.2432 0.2757 0.4127 -0.0272 -0.0102 -0.0326 420 TYR A CE2 3307 C CZ . TYR A 418 ? 0.3310 0.3569 0.5039 -0.0287 -0.0178 -0.0276 420 TYR A CZ 3308 O OH . TYR A 418 ? 0.3123 0.3343 0.4784 -0.0351 -0.0209 -0.0213 420 TYR A OH 3309 N N . PHE A 419 ? 0.2042 0.2478 0.4192 -0.0081 -0.0102 -0.0406 421 PHE A N 3310 C CA . PHE A 419 ? 0.1993 0.2537 0.4230 -0.0084 -0.0080 -0.0398 421 PHE A CA 3311 C C . PHE A 419 ? 0.2213 0.2818 0.4429 -0.0150 -0.0057 -0.0363 421 PHE A C 3312 O O . PHE A 419 ? 0.2212 0.2756 0.4384 -0.0200 -0.0094 -0.0323 421 PHE A O 3313 C CB . PHE A 419 ? 0.1771 0.2293 0.4070 -0.0079 -0.0127 -0.0382 421 PHE A CB 3314 C CG . PHE A 419 ? 0.2007 0.2640 0.4410 -0.0086 -0.0127 -0.0370 421 PHE A CG 3315 C CD1 . PHE A 419 ? 0.2028 0.2725 0.4516 -0.0030 -0.0122 -0.0393 421 PHE A CD1 3316 C CD2 . PHE A 419 ? 0.1804 0.2468 0.4226 -0.0150 -0.0144 -0.0333 421 PHE A CD2 3317 C CE1 . PHE A 419 ? 0.2393 0.3210 0.5004 -0.0035 -0.0134 -0.0378 421 PHE A CE1 3318 C CE2 . PHE A 419 ? 0.1791 0.2567 0.4324 -0.0167 -0.0156 -0.0319 421 PHE A CE2 3319 C CZ . PHE A 419 ? 0.1736 0.2603 0.4373 -0.0109 -0.0152 -0.0341 421 PHE A CZ 3320 N N . GLU A 420 ? 0.2375 0.3094 0.4619 -0.0154 0.0007 -0.0378 422 GLU A N 3321 C CA . GLU A 420 ? 0.2684 0.3447 0.4876 -0.0231 0.0037 -0.0343 422 GLU A CA 3322 C C . GLU A 420 ? 0.2798 0.3726 0.5116 -0.0253 0.0085 -0.0336 422 GLU A C 3323 O O . GLU A 420 ? 0.3107 0.4115 0.5397 -0.0309 0.0146 -0.0323 422 GLU A O 3324 C CB . GLU A 420 ? 0.3066 0.3780 0.5104 -0.0248 0.0074 -0.0358 422 GLU A CB 3325 C CG . GLU A 420 ? 0.3563 0.4361 0.5604 -0.0211 0.0161 -0.0417 422 GLU A CG 3326 C CD . GLU A 420 ? 0.4262 0.4965 0.6127 -0.0212 0.0181 -0.0451 422 GLU A CD 3327 O OE1 . GLU A 420 ? 0.4022 0.4614 0.5755 -0.0258 0.0126 -0.0417 422 GLU A OE1 3328 O OE2 . GLU A 420 ? 0.4516 0.5258 0.6377 -0.0166 0.0250 -0.0516 422 GLU A OE2 3329 N N . HIS A 421 ? 0.2588 0.3571 0.5045 -0.0219 0.0051 -0.0340 423 HIS A N 3330 C CA . HIS A 421 ? 0.2441 0.3595 0.5049 -0.0245 0.0078 -0.0327 423 HIS A CA 3331 C C . HIS A 421 ? 0.2386 0.3525 0.5023 -0.0317 0.0014 -0.0274 423 HIS A C 3332 O O . HIS A 421 ? 0.2224 0.3267 0.4859 -0.0300 -0.0061 -0.0269 423 HIS A O 3333 C CB . HIS A 421 ? 0.2214 0.3464 0.4980 -0.0159 0.0076 -0.0365 423 HIS A CB 3334 C CG . HIS A 421 ? 0.2269 0.3714 0.5221 -0.0186 0.0089 -0.0348 423 HIS A CG 3335 N ND1 . HIS A 421 ? 0.2759 0.4374 0.5786 -0.0215 0.0186 -0.0358 423 HIS A ND1 3336 C CD2 . HIS A 421 ? 0.2220 0.3721 0.5296 -0.0204 0.0018 -0.0319 423 HIS A CD2 3337 C CE1 . HIS A 421 ? 0.2298 0.4081 0.5510 -0.0250 0.0174 -0.0333 423 HIS A CE1 3338 N NE2 . HIS A 421 ? 0.2239 0.3954 0.5484 -0.0242 0.0065 -0.0309 423 HIS A NE2 3339 N N . ARG A 422 ? 0.2523 0.3747 0.5178 -0.0405 0.0047 -0.0237 424 ARG A N 3340 C CA . ARG A 422 ? 0.2859 0.4074 0.5551 -0.0486 -0.0013 -0.0188 424 ARG A CA 3341 C C . ARG A 422 ? 0.2784 0.4170 0.5678 -0.0484 -0.0030 -0.0190 424 ARG A C 3342 O O . ARG A 422 ? 0.2803 0.4384 0.5829 -0.0487 0.0039 -0.0200 424 ARG A O 3343 C CB . ARG A 422 ? 0.2976 0.4195 0.5596 -0.0597 0.0021 -0.0137 424 ARG A CB 3344 C CG . ARG A 422 ? 0.3314 0.4491 0.5957 -0.0685 -0.0047 -0.0089 424 ARG A CG 3345 C CD . ARG A 422 ? 0.3382 0.4501 0.5914 -0.0795 -0.0029 -0.0031 424 ARG A CD 3346 N NE . ARG A 422 ? 0.3692 0.4846 0.6295 -0.0898 -0.0066 0.0014 424 ARG A NE 3347 C CZ . ARG A 422 ? 0.4527 0.5503 0.7053 -0.0953 -0.0148 0.0048 424 ARG A CZ 3348 N NH1 . ARG A 422 ? 0.3913 0.4662 0.6300 -0.0904 -0.0203 0.0042 424 ARG A NH1 3349 N NH2 . ARG A 422 ? 0.3911 0.4938 0.6509 -0.1060 -0.0175 0.0087 424 ARG A NH2 3350 N N . SER A 423 ? 0.2742 0.4059 0.5660 -0.0481 -0.0121 -0.0183 425 SER A N 3351 C CA . SER A 423 ? 0.2913 0.4374 0.6012 -0.0478 -0.0165 -0.0180 425 SER A CA 3352 C C . SER A 423 ? 0.2959 0.4597 0.6185 -0.0581 -0.0138 -0.0143 425 SER A C 3353 O O . SER A 423 ? 0.2920 0.4481 0.6051 -0.0679 -0.0140 -0.0104 425 SER A O 3354 C CB . SER A 423 ? 0.2915 0.4226 0.5951 -0.0481 -0.0272 -0.0175 425 SER A CB 3355 O OG . SER A 423 ? 0.3282 0.4718 0.6473 -0.0504 -0.0337 -0.0160 425 SER A OG 3356 N N . SER A 424 ? 0.3016 0.4890 0.6461 -0.0559 -0.0108 -0.0153 426 SER A N 3357 C CA . SER A 424 ? 0.3102 0.5185 0.6704 -0.0656 -0.0068 -0.0120 426 SER A CA 3358 C C . SER A 424 ? 0.3342 0.5374 0.6956 -0.0756 -0.0179 -0.0075 426 SER A C 3359 O O . SER A 424 ? 0.3248 0.5368 0.6918 -0.0874 -0.0166 -0.0035 426 SER A O 3360 C CB . SER A 424 ? 0.3130 0.5496 0.7012 -0.0593 -0.0020 -0.0148 426 SER A CB 3361 O OG . SER A 424 ? 0.2927 0.5315 0.6934 -0.0524 -0.0128 -0.0155 426 SER A OG 3362 N N . LYS A 425 ? 0.3467 0.5350 0.7016 -0.0715 -0.0286 -0.0085 427 LYS A N 3363 C CA . LYS A 425 ? 0.3818 0.5617 0.7341 -0.0809 -0.0395 -0.0053 427 LYS A CA 3364 C C . LYS A 425 ? 0.3865 0.5383 0.7137 -0.0865 -0.0420 -0.0042 427 LYS A C 3365 O O . LYS A 425 ? 0.4136 0.5546 0.7354 -0.0944 -0.0507 -0.0025 427 LYS A O 3366 C CB . LYS A 425 ? 0.3800 0.5582 0.7371 -0.0748 -0.0504 -0.0069 427 LYS A CB 3367 C CG . LYS A 425 ? 0.4488 0.6543 0.8337 -0.0688 -0.0506 -0.0073 427 LYS A CG 3368 C CD . LYS A 425 ? 0.5019 0.7031 0.8894 -0.0632 -0.0635 -0.0076 427 LYS A CD 3369 C CE . LYS A 425 ? 0.5212 0.7151 0.9043 -0.0746 -0.0767 -0.0044 427 LYS A CE 3370 N NZ . LYS A 425 ? 0.5228 0.7074 0.9011 -0.0701 -0.0895 -0.0046 427 LYS A NZ 3371 N N . LEU A 426 ? 0.3616 0.5013 0.6740 -0.0827 -0.0353 -0.0053 428 LEU A N 3372 C CA . LEU A 426 ? 0.3527 0.4655 0.6439 -0.0857 -0.0387 -0.0046 428 LEU A CA 3373 C C . LEU A 426 ? 0.3458 0.4517 0.6335 -0.0996 -0.0428 0.0001 428 LEU A C 3374 O O . LEU A 426 ? 0.3585 0.4758 0.6520 -0.1082 -0.0380 0.0043 428 LEU A O 3375 C CB . LEU A 426 ? 0.3560 0.4600 0.6349 -0.0799 -0.0316 -0.0056 428 LEU A CB 3376 C CG . LEU A 426 ? 0.3901 0.4677 0.6510 -0.0774 -0.0357 -0.0067 428 LEU A CG 3377 C CD1 . LEU A 426 ? 0.3749 0.4459 0.6331 -0.0676 -0.0380 -0.0115 428 LEU A CD1 3378 C CD2 . LEU A 426 ? 0.4490 0.5185 0.6990 -0.0771 -0.0310 -0.0049 428 LEU A CD2 3379 N N . PRO A 427 ? 0.3292 0.4162 0.6074 -0.1028 -0.0517 -0.0007 429 PRO A N 3380 C CA . PRO A 427 ? 0.3142 0.3927 0.5890 -0.1164 -0.0567 0.0033 429 PRO A CA 3381 C C . PRO A 427 ? 0.3122 0.3709 0.5713 -0.1193 -0.0542 0.0060 429 PRO A C 3382 O O . PRO A 427 ? 0.3083 0.3619 0.5648 -0.1310 -0.0557 0.0109 429 PRO A O 3383 C CB . PRO A 427 ? 0.3219 0.3842 0.5890 -0.1167 -0.0665 -0.0001 429 PRO A CB 3384 C CG . PRO A 427 ? 0.3158 0.3795 0.5823 -0.1042 -0.0663 -0.0050 429 PRO A CG 3385 C CD . PRO A 427 ? 0.3174 0.3904 0.5871 -0.0950 -0.0570 -0.0055 429 PRO A CD 3386 N N . TRP A 428 ? 0.2888 0.3366 0.5381 -0.1091 -0.0510 0.0034 430 TRP A N 3387 C CA . TRP A 428 ? 0.3014 0.3325 0.5376 -0.1106 -0.0493 0.0066 430 TRP A CA 3388 C C . TRP A 428 ? 0.2957 0.3412 0.5347 -0.1164 -0.0421 0.0119 430 TRP A C 3389 O O . TRP A 428 ? 0.2804 0.3490 0.5312 -0.1147 -0.0358 0.0110 430 TRP A O 3390 C CB . TRP A 428 ? 0.2809 0.2998 0.5088 -0.0982 -0.0482 0.0024 430 TRP A CB 3391 C CG . TRP A 428 ? 0.2517 0.2555 0.4749 -0.0925 -0.0534 -0.0033 430 TRP A CG 3392 C CD1 . TRP A 428 ? 0.2001 0.2103 0.4271 -0.0851 -0.0535 -0.0086 430 TRP A CD1 3393 C CD2 . TRP A 428 ? 0.2608 0.2401 0.4736 -0.0941 -0.0587 -0.0046 430 TRP A CD2 3394 N NE1 . TRP A 428 ? 0.2501 0.2419 0.4682 -0.0832 -0.0578 -0.0128 430 TRP A NE1 3395 C CE2 . TRP A 428 ? 0.2543 0.2269 0.4642 -0.0877 -0.0605 -0.0112 430 TRP A CE2 3396 C CE3 . TRP A 428 ? 0.2577 0.2183 0.4626 -0.1004 -0.0621 -0.0008 430 TRP A CE3 3397 C CZ2 . TRP A 428 ? 0.2166 0.1657 0.4162 -0.0867 -0.0640 -0.0153 430 TRP A CZ2 3398 C CZ3 . TRP A 428 ? 0.2629 0.1989 0.4589 -0.0985 -0.0668 -0.0048 430 TRP A CZ3 3399 C CH2 . TRP A 428 ? 0.2792 0.2106 0.4730 -0.0916 -0.0670 -0.0125 430 TRP A CH2 3400 N N . PRO A 429 ? 0.3084 0.3392 0.5358 -0.1235 -0.0428 0.0174 431 PRO A N 3401 C CA . PRO A 429 ? 0.3321 0.3748 0.5584 -0.1316 -0.0357 0.0233 431 PRO A CA 3402 C C . PRO A 429 ? 0.3452 0.3959 0.5679 -0.1227 -0.0281 0.0213 431 PRO A C 3403 O O . PRO A 429 ? 0.3557 0.3966 0.5737 -0.1112 -0.0302 0.0170 431 PRO A O 3404 C CB . PRO A 429 ? 0.3372 0.3554 0.5482 -0.1406 -0.0409 0.0301 431 PRO A CB 3405 C CG . PRO A 429 ? 0.3475 0.3420 0.5511 -0.1307 -0.0483 0.0260 431 PRO A CG 3406 C CD . PRO A 429 ? 0.3108 0.3129 0.5252 -0.1246 -0.0503 0.0186 431 PRO A CD 3407 N N . GLU A 430 ? 0.3589 0.4262 0.5829 -0.1284 -0.0193 0.0241 432 GLU A N 3408 C CA . GLU A 430 ? 0.3801 0.4554 0.5991 -0.1212 -0.0113 0.0215 432 GLU A CA 3409 C C . GLU A 430 ? 0.3630 0.4175 0.5640 -0.1160 -0.0148 0.0225 432 GLU A C 3410 O O . GLU A 430 ? 0.3339 0.3916 0.5330 -0.1064 -0.0117 0.0179 432 GLU A O 3411 C CB . GLU A 430 ? 0.3951 0.4877 0.6134 -0.1308 -0.0005 0.0250 432 GLU A CB 3412 C CG . GLU A 430 ? 0.5159 0.6383 0.7554 -0.1292 0.0083 0.0205 432 GLU A CG 3413 C CD . GLU A 430 ? 0.6838 0.8223 0.9235 -0.1423 0.0190 0.0250 432 GLU A CD 3414 O OE1 . GLU A 430 ? 0.7411 0.8754 0.9635 -0.1445 0.0258 0.0265 432 GLU A OE1 3415 O OE2 . GLU A 430 ? 0.7460 0.9001 1.0018 -0.1514 0.0202 0.0274 432 GLU A OE2 3416 N N . TRP A 431 ? 0.3739 0.4077 0.5620 -0.1229 -0.0214 0.0291 433 TRP A N 3417 C CA . TRP A 431 ? 0.3799 0.3950 0.5520 -0.1190 -0.0258 0.0315 433 TRP A CA 3418 C C . TRP A 431 ? 0.3675 0.3764 0.5451 -0.1046 -0.0303 0.0245 433 TRP A C 3419 O O . TRP A 431 ? 0.3788 0.3813 0.5489 -0.0983 -0.0317 0.0237 433 TRP A O 3420 C CB . TRP A 431 ? 0.3826 0.3751 0.5415 -0.1285 -0.0335 0.0403 433 TRP A CB 3421 C CG . TRP A 431 ? 0.3784 0.3529 0.5415 -0.1272 -0.0429 0.0400 433 TRP A CG 3422 C CD1 . TRP A 431 ? 0.3450 0.3153 0.5114 -0.1373 -0.0457 0.0430 433 TRP A CD1 3423 C CD2 . TRP A 431 ? 0.3197 0.2768 0.4834 -0.1158 -0.0505 0.0362 433 TRP A CD2 3424 N NE1 . TRP A 431 ? 0.3605 0.3106 0.5280 -0.1323 -0.0544 0.0404 433 TRP A NE1 3425 C CE2 . TRP A 431 ? 0.3035 0.2458 0.4697 -0.1191 -0.0569 0.0363 433 TRP A CE2 3426 C CE3 . TRP A 431 ? 0.3396 0.2926 0.5023 -0.1038 -0.0523 0.0326 433 TRP A CE3 3427 C CZ2 . TRP A 431 ? 0.3734 0.2974 0.5411 -0.1099 -0.0635 0.0321 433 TRP A CZ2 3428 C CZ3 . TRP A 431 ? 0.3075 0.2445 0.4743 -0.0947 -0.0591 0.0288 433 TRP A CZ3 3429 C CH2 . TRP A 431 ? 0.3680 0.2908 0.5370 -0.0973 -0.0639 0.0282 433 TRP A CH2 3430 N N . MET A 432 ? 0.3371 0.3482 0.5269 -0.1005 -0.0326 0.0197 434 MET A N 3431 C CA . MET A 432 ? 0.3167 0.3213 0.5104 -0.0884 -0.0360 0.0133 434 MET A CA 3432 C C . MET A 432 ? 0.2828 0.3031 0.4822 -0.0800 -0.0300 0.0076 434 MET A C 3433 O O . MET A 432 ? 0.2756 0.2910 0.4767 -0.0705 -0.0319 0.0029 434 MET A O 3434 C CB . MET A 432 ? 0.3118 0.3111 0.5130 -0.0877 -0.0405 0.0100 434 MET A CB 3435 C CG . MET A 432 ? 0.3638 0.3435 0.5582 -0.0955 -0.0472 0.0150 434 MET A CG 3436 S SD . MET A 432 ? 0.3564 0.3210 0.5530 -0.0957 -0.0537 0.0110 434 MET A SD 3437 C CE . MET A 432 ? 0.3339 0.2929 0.5327 -0.0812 -0.0538 0.0026 434 MET A CE 3438 N N . GLY A 433 ? 0.2539 0.2925 0.4568 -0.0834 -0.0224 0.0076 435 GLY A N 3439 C CA . GLY A 433 ? 0.2526 0.3039 0.4586 -0.0756 -0.0161 0.0022 435 GLY A CA 3440 C C . GLY A 433 ? 0.2646 0.3200 0.4817 -0.0660 -0.0174 -0.0042 435 GLY A C 3441 O O . GLY A 433 ? 0.2637 0.3233 0.4903 -0.0673 -0.0198 -0.0049 435 GLY A O 3442 N N . VAL A 434 ? 0.2467 0.3006 0.4615 -0.0572 -0.0162 -0.0086 436 VAL A N 3443 C CA . VAL A 434 ? 0.2325 0.2899 0.4558 -0.0485 -0.0167 -0.0142 436 VAL A CA 3444 C C . VAL A 434 ? 0.2414 0.2831 0.4622 -0.0450 -0.0232 -0.0153 436 VAL A C 3445 O O . VAL A 434 ? 0.2468 0.2802 0.4628 -0.0398 -0.0244 -0.0170 436 VAL A O 3446 C CB . VAL A 434 ? 0.2314 0.2933 0.4525 -0.0416 -0.0119 -0.0185 436 VAL A CB 3447 C CG1 . VAL A 434 ? 0.1885 0.2526 0.4175 -0.0334 -0.0127 -0.0235 436 VAL A CG1 3448 C CG2 . VAL A 434 ? 0.2009 0.2772 0.4223 -0.0450 -0.0036 -0.0186 436 VAL A CG2 3449 N N . MET A 435 ? 0.2233 0.2612 0.4473 -0.0482 -0.0271 -0.0145 437 MET A N 3450 C CA . MET A 435 ? 0.2262 0.2478 0.4460 -0.0469 -0.0321 -0.0151 437 MET A CA 3451 C C . MET A 435 ? 0.2251 0.2438 0.4463 -0.0390 -0.0321 -0.0203 437 MET A C 3452 O O . MET A 435 ? 0.2151 0.2429 0.4410 -0.0358 -0.0304 -0.0229 437 MET A O 3453 C CB . MET A 435 ? 0.2339 0.2507 0.4547 -0.0537 -0.0361 -0.0134 437 MET A CB 3454 C CG . MET A 435 ? 0.2305 0.2448 0.4480 -0.0632 -0.0372 -0.0074 437 MET A CG 3455 S SD . MET A 435 ? 0.3306 0.3410 0.5504 -0.0723 -0.0423 -0.0060 437 MET A SD 3456 C CE . MET A 435 ? 0.2497 0.2373 0.4627 -0.0675 -0.0474 -0.0107 437 MET A CE 3457 N N . HIS A 436 ? 0.2438 0.2490 0.4614 -0.0366 -0.0345 -0.0215 438 HIS A N 3458 C CA . HIS A 436 ? 0.2496 0.2491 0.4672 -0.0314 -0.0344 -0.0262 438 HIS A CA 3459 C C . HIS A 436 ? 0.2589 0.2600 0.4768 -0.0334 -0.0357 -0.0281 438 HIS A C 3460 O O . HIS A 436 ? 0.2652 0.2630 0.4819 -0.0392 -0.0388 -0.0264 438 HIS A O 3461 C CB . HIS A 436 ? 0.2531 0.2381 0.4685 -0.0303 -0.0366 -0.0269 438 HIS A CB 3462 C CG . HIS A 436 ? 0.2952 0.2741 0.5103 -0.0253 -0.0348 -0.0323 438 HIS A CG 3463 N ND1 . HIS A 436 ? 0.2376 0.2194 0.4556 -0.0199 -0.0320 -0.0345 438 HIS A ND1 3464 C CD2 . HIS A 436 ? 0.3420 0.3116 0.5532 -0.0258 -0.0350 -0.0360 438 HIS A CD2 3465 C CE1 . HIS A 436 ? 0.2700 0.2457 0.4868 -0.0173 -0.0297 -0.0391 438 HIS A CE1 3466 N NE2 . HIS A 436 ? 0.3356 0.3033 0.5473 -0.0206 -0.0312 -0.0404 438 HIS A NE2 3467 N N . GLY A 437 ? 0.2425 0.2477 0.4610 -0.0291 -0.0342 -0.0310 439 GLY A N 3468 C CA . GLY A 437 ? 0.2219 0.2276 0.4390 -0.0305 -0.0368 -0.0324 439 GLY A CA 3469 C C . GLY A 437 ? 0.2285 0.2487 0.4530 -0.0318 -0.0382 -0.0302 439 GLY A C 3470 O O . GLY A 437 ? 0.2250 0.2463 0.4492 -0.0323 -0.0416 -0.0308 439 GLY A O 3471 N N . TYR A 438 ? 0.2337 0.2653 0.4650 -0.0325 -0.0356 -0.0278 440 TYR A N 3472 C CA . TYR A 438 ? 0.2160 0.2637 0.4577 -0.0343 -0.0359 -0.0259 440 TYR A CA 3473 C C . TYR A 438 ? 0.2264 0.2840 0.4742 -0.0274 -0.0325 -0.0275 440 TYR A C 3474 O O . TYR A 438 ? 0.2323 0.3053 0.4910 -0.0274 -0.0305 -0.0266 440 TYR A O 3475 C CB . TYR A 438 ? 0.2232 0.2773 0.4685 -0.0417 -0.0346 -0.0221 440 TYR A CB 3476 C CG . TYR A 438 ? 0.2400 0.2844 0.4812 -0.0492 -0.0403 -0.0207 440 TYR A CG 3477 C CD1 . TYR A 438 ? 0.2353 0.2624 0.4664 -0.0510 -0.0415 -0.0207 440 TYR A CD1 3478 C CD2 . TYR A 438 ? 0.2586 0.3100 0.5063 -0.0536 -0.0453 -0.0198 440 TYR A CD2 3479 C CE1 . TYR A 438 ? 0.2060 0.2207 0.4318 -0.0572 -0.0467 -0.0207 440 TYR A CE1 3480 C CE2 . TYR A 438 ? 0.2376 0.2779 0.4795 -0.0609 -0.0512 -0.0193 440 TYR A CE2 3481 C CZ . TYR A 438 ? 0.2772 0.2985 0.5075 -0.0626 -0.0514 -0.0201 440 TYR A CZ 3482 O OH . TYR A 438 ? 0.2725 0.2812 0.4963 -0.0695 -0.0570 -0.0205 440 TYR A OH 3483 N N . GLU A 439 ? 0.2185 0.2676 0.4601 -0.0216 -0.0313 -0.0302 441 GLU A N 3484 C CA . GLU A 439 ? 0.2087 0.2628 0.4545 -0.0150 -0.0300 -0.0320 441 GLU A CA 3485 C C . GLU A 439 ? 0.2120 0.2620 0.4568 -0.0135 -0.0356 -0.0321 441 GLU A C 3486 O O . GLU A 439 ? 0.2157 0.2700 0.4658 -0.0084 -0.0368 -0.0325 441 GLU A O 3487 C CB . GLU A 439 ? 0.2134 0.2599 0.4525 -0.0107 -0.0263 -0.0344 441 GLU A CB 3488 C CG . GLU A 439 ? 0.1710 0.2042 0.4017 -0.0090 -0.0279 -0.0360 441 GLU A CG 3489 C CD . GLU A 439 ? 0.2507 0.2745 0.4753 -0.0132 -0.0290 -0.0358 441 GLU A CD 3490 O OE1 . GLU A 439 ? 0.2047 0.2298 0.4305 -0.0172 -0.0293 -0.0341 441 GLU A OE1 3491 O OE2 . GLU A 439 ? 0.2029 0.2171 0.4212 -0.0125 -0.0293 -0.0375 441 GLU A OE2 3492 N N . ILE A 440 ? 0.2032 0.2426 0.4395 -0.0177 -0.0390 -0.0319 442 ILE A N 3493 C CA . ILE A 440 ? 0.2118 0.2433 0.4415 -0.0176 -0.0440 -0.0320 442 ILE A CA 3494 C C . ILE A 440 ? 0.2204 0.2621 0.4594 -0.0170 -0.0502 -0.0297 442 ILE A C 3495 O O . ILE A 440 ? 0.2423 0.2810 0.4797 -0.0131 -0.0534 -0.0293 442 ILE A O 3496 C CB . ILE A 440 ? 0.2217 0.2401 0.4394 -0.0232 -0.0459 -0.0331 442 ILE A CB 3497 C CG1 . ILE A 440 ? 0.1962 0.2048 0.4072 -0.0217 -0.0399 -0.0358 442 ILE A CG1 3498 C CG2 . ILE A 440 ? 0.2270 0.2372 0.4351 -0.0244 -0.0516 -0.0330 442 ILE A CG2 3499 C CD1 . ILE A 440 ? 0.1720 0.1682 0.3739 -0.0261 -0.0403 -0.0378 442 ILE A CD1 3500 N N . GLU A 441 ? 0.2264 0.2796 0.4756 -0.0214 -0.0525 -0.0277 443 GLU A N 3501 C CA . GLU A 441 ? 0.2403 0.3069 0.5031 -0.0210 -0.0586 -0.0253 443 GLU A CA 3502 C C . GLU A 441 ? 0.2330 0.3106 0.5086 -0.0121 -0.0556 -0.0259 443 GLU A C 3503 O O . GLU A 441 ? 0.2524 0.3348 0.5360 -0.0083 -0.0618 -0.0244 443 GLU A O 3504 C CB . GLU A 441 ? 0.2424 0.3209 0.5153 -0.0284 -0.0603 -0.0231 443 GLU A CB 3505 C CG . GLU A 441 ? 0.2818 0.3706 0.5622 -0.0297 -0.0517 -0.0233 443 GLU A CG 3506 C CD . GLU A 441 ? 0.3329 0.4243 0.6147 -0.0399 -0.0532 -0.0209 443 GLU A CD 3507 O OE1 . GLU A 441 ? 0.3261 0.4017 0.5938 -0.0444 -0.0532 -0.0213 443 GLU A OE1 3508 O OE2 . GLU A 441 ? 0.3566 0.4660 0.6549 -0.0435 -0.0546 -0.0185 443 GLU A OE2 3509 N N . PHE A 442 ? 0.2268 0.3065 0.5032 -0.0087 -0.0469 -0.0283 444 PHE A N 3510 C CA . PHE A 442 ? 0.2121 0.2982 0.4973 0.0000 -0.0433 -0.0303 444 PHE A CA 3511 C C . PHE A 442 ? 0.2165 0.2879 0.4919 0.0051 -0.0465 -0.0309 444 PHE A C 3512 O O . PHE A 442 ? 0.1997 0.2741 0.4836 0.0115 -0.0502 -0.0305 444 PHE A O 3513 C CB . PHE A 442 ? 0.2085 0.2990 0.4938 0.0010 -0.0334 -0.0330 444 PHE A CB 3514 C CG . PHE A 442 ? 0.2043 0.3122 0.5020 -0.0032 -0.0297 -0.0320 444 PHE A CG 3515 C CD1 . PHE A 442 ? 0.1495 0.2565 0.4428 -0.0123 -0.0307 -0.0293 444 PHE A CD1 3516 C CD2 . PHE A 442 ? 0.1606 0.2862 0.4760 0.0017 -0.0258 -0.0335 444 PHE A CD2 3517 C CE1 . PHE A 442 ? 0.1518 0.2753 0.4570 -0.0179 -0.0277 -0.0275 444 PHE A CE1 3518 C CE2 . PHE A 442 ? 0.1880 0.3316 0.5162 -0.0032 -0.0219 -0.0323 444 PHE A CE2 3519 C CZ . PHE A 442 ? 0.1616 0.3042 0.4842 -0.0137 -0.0229 -0.0289 444 PHE A CZ 3520 N N . VAL A 443 ? 0.2095 0.2651 0.4681 0.0023 -0.0453 -0.0317 445 VAL A N 3521 C CA . VAL A 443 ? 0.2048 0.2453 0.4520 0.0051 -0.0479 -0.0317 445 VAL A CA 3522 C C . VAL A 443 ? 0.2227 0.2592 0.4681 0.0046 -0.0577 -0.0283 445 VAL A C 3523 O O . VAL A 443 ? 0.2299 0.2593 0.4730 0.0094 -0.0609 -0.0273 445 VAL A O 3524 C CB . VAL A 443 ? 0.2269 0.2536 0.4584 0.0010 -0.0440 -0.0332 445 VAL A CB 3525 C CG1 . VAL A 443 ? 0.1759 0.1879 0.3948 0.0014 -0.0465 -0.0326 445 VAL A CG1 3526 C CG2 . VAL A 443 ? 0.1935 0.2222 0.4263 0.0025 -0.0364 -0.0360 445 VAL A CG2 3527 N N . PHE A 444 ? 0.2159 0.2554 0.4610 -0.0015 -0.0632 -0.0262 446 PHE A N 3528 C CA . PHE A 444 ? 0.2159 0.2499 0.4559 -0.0034 -0.0739 -0.0226 446 PHE A CA 3529 C C . PHE A 444 ? 0.2306 0.2805 0.4911 0.0007 -0.0810 -0.0199 446 PHE A C 3530 O O . PHE A 444 ? 0.2414 0.2893 0.5014 0.0000 -0.0922 -0.0160 446 PHE A O 3531 C CB . PHE A 444 ? 0.2044 0.2301 0.4304 -0.0126 -0.0775 -0.0223 446 PHE A CB 3532 C CG . PHE A 444 ? 0.2198 0.2266 0.4237 -0.0156 -0.0732 -0.0245 446 PHE A CG 3533 C CD1 . PHE A 444 ? 0.1798 0.1837 0.3803 -0.0165 -0.0635 -0.0282 446 PHE A CD1 3534 C CD2 . PHE A 444 ? 0.1998 0.1924 0.3868 -0.0181 -0.0789 -0.0226 446 PHE A CD2 3535 C CE1 . PHE A 444 ? 0.2180 0.2070 0.4017 -0.0188 -0.0586 -0.0307 446 PHE A CE1 3536 C CE2 . PHE A 444 ? 0.2618 0.2386 0.4292 -0.0213 -0.0733 -0.0250 446 PHE A CE2 3537 C CZ . PHE A 444 ? 0.2203 0.1962 0.3875 -0.0213 -0.0625 -0.0295 446 PHE A CZ 3538 N N . GLY A 445 ? 0.2370 0.3033 0.5158 0.0051 -0.0746 -0.0219 447 GLY A N 3539 C CA . GLY A 445 ? 0.2331 0.3167 0.5353 0.0113 -0.0787 -0.0205 447 GLY A CA 3540 C C . GLY A 445 ? 0.2464 0.3460 0.5627 0.0057 -0.0854 -0.0176 447 GLY A C 3541 O O . GLY A 445 ? 0.2441 0.3562 0.5789 0.0097 -0.0934 -0.0149 447 GLY A O 3542 N N . LEU A 446 ? 0.2388 0.3385 0.5484 -0.0036 -0.0827 -0.0179 448 LEU A N 3543 C CA . LEU A 446 ? 0.2582 0.3725 0.5811 -0.0102 -0.0890 -0.0152 448 LEU A CA 3544 C C . LEU A 446 ? 0.2490 0.3900 0.6012 -0.0063 -0.0846 -0.0155 448 LEU A C 3545 O O . LEU A 446 ? 0.2539 0.4108 0.6248 -0.0079 -0.0928 -0.0125 448 LEU A O 3546 C CB . LEU A 446 ? 0.2517 0.3588 0.5612 -0.0217 -0.0885 -0.0153 448 LEU A CB 3547 C CG . LEU A 446 ? 0.2832 0.3658 0.5648 -0.0276 -0.0903 -0.0164 448 LEU A CG 3548 C CD1 . LEU A 446 ? 0.2463 0.3273 0.5236 -0.0389 -0.0960 -0.0153 448 LEU A CD1 3549 C CD2 . LEU A 446 ? 0.2523 0.3169 0.5162 -0.0245 -0.0956 -0.0160 448 LEU A CD2 3550 N N . PRO A 447 ? 0.2451 0.3915 0.6014 -0.0015 -0.0718 -0.0193 449 PRO A N 3551 C CA . PRO A 447 ? 0.2455 0.4188 0.6301 0.0019 -0.0665 -0.0201 449 PRO A CA 3552 C C . PRO A 447 ? 0.2437 0.4273 0.6489 0.0132 -0.0716 -0.0201 449 PRO A C 3553 O O . PRO A 447 ? 0.2310 0.4386 0.6629 0.0171 -0.0675 -0.0212 449 PRO A O 3554 C CB . PRO A 447 ? 0.2318 0.4053 0.6110 0.0035 -0.0516 -0.0246 449 PRO A CB 3555 C CG . PRO A 447 ? 0.2604 0.4103 0.6107 -0.0032 -0.0509 -0.0245 449 PRO A CG 3556 C CD . PRO A 447 ? 0.2208 0.3533 0.5585 -0.0019 -0.0617 -0.0226 449 PRO A CD 3557 N N . LEU A 448 ? 0.2623 0.4282 0.6560 0.0185 -0.0802 -0.0187 450 LEU A N 3558 C CA . LEU A 448 ? 0.2836 0.4571 0.6973 0.0296 -0.0877 -0.0175 450 LEU A CA 3559 C C . LEU A 448 ? 0.3159 0.5071 0.7506 0.0260 -0.1005 -0.0124 450 LEU A C 3560 O O . LEU A 448 ? 0.3354 0.5431 0.7975 0.0348 -0.1058 -0.0114 450 LEU A O 3561 C CB . LEU A 448 ? 0.2513 0.4000 0.6465 0.0356 -0.0940 -0.0165 450 LEU A CB 3562 C CG . LEU A 448 ? 0.2835 0.4142 0.6575 0.0375 -0.0823 -0.0213 450 LEU A CG 3563 C CD1 . LEU A 448 ? 0.1849 0.2893 0.5376 0.0405 -0.0887 -0.0195 450 LEU A CD1 3564 C CD2 . LEU A 448 ? 0.2636 0.4074 0.6535 0.0459 -0.0694 -0.0274 450 LEU A CD2 3565 N N . GLU A 449 ? 0.3504 0.5385 0.7739 0.0133 -0.1060 -0.0094 451 GLU A N 3566 C CA . GLU A 449 ? 0.3970 0.6015 0.8390 0.0077 -0.1188 -0.0046 451 GLU A CA 3567 C C . GLU A 449 ? 0.4114 0.6471 0.8833 0.0056 -0.1100 -0.0061 451 GLU A C 3568 O O . GLU A 449 ? 0.4089 0.6471 0.8741 -0.0048 -0.1026 -0.0069 451 GLU A O 3569 C CB . GLU A 449 ? 0.4102 0.5976 0.8269 -0.0057 -0.1281 -0.0015 451 GLU A CB 3570 C CG . GLU A 449 ? 0.4349 0.6369 0.8671 -0.0143 -0.1431 0.0036 451 GLU A CG 3571 C CD . GLU A 449 ? 0.4336 0.6349 0.8738 -0.0085 -0.1608 0.0086 451 GLU A CD 3572 O OE1 . GLU A 449 ? 0.3987 0.6240 0.8730 -0.0002 -0.1642 0.0100 451 GLU A OE1 3573 O OE2 . GLU A 449 ? 0.4600 0.6365 0.8720 -0.0122 -0.1710 0.0111 451 GLU A OE2 3574 N N . ARG A 450 ? 0.4477 0.7063 0.9523 0.0155 -0.1103 -0.0065 452 ARG A N 3575 C CA . ARG A 450 ? 0.4876 0.7798 1.0252 0.0140 -0.1017 -0.0079 452 ARG A CA 3576 C C . ARG A 450 ? 0.4953 0.8014 1.0411 -0.0017 -0.1090 -0.0033 452 ARG A C 3577 O O . ARG A 450 ? 0.4940 0.8181 1.0509 -0.0094 -0.0979 -0.0045 452 ARG A O 3578 C CB . ARG A 450 ? 0.4898 0.8046 1.0643 0.0286 -0.1031 -0.0091 452 ARG A CB 3579 C CG . ARG A 450 ? 0.5545 0.9027 1.1610 0.0306 -0.0867 -0.0137 452 ARG A CG 3580 C CD . ARG A 450 ? 0.6251 0.9970 1.2716 0.0471 -0.0866 -0.0162 452 ARG A CD 3581 N NE . ARG A 450 ? 0.6887 1.0872 1.3709 0.0457 -0.1010 -0.0107 452 ARG A NE 3582 C CZ . ARG A 450 ? 0.7357 1.1347 1.4346 0.0556 -0.1186 -0.0067 452 ARG A CZ 3583 N NH1 . ARG A 450 ? 0.7440 1.1168 1.4262 0.0676 -0.1239 -0.0074 452 ARG A NH1 3584 N NH2 . ARG A 450 ? 0.7397 1.1657 1.4729 0.0531 -0.1316 -0.0016 452 ARG A NH2 3585 N N . ARG A 451 ? 0.5069 0.8020 1.0433 -0.0078 -0.1272 0.0020 453 ARG A N 3586 C CA . ARG A 451 ? 0.5139 0.8176 1.0537 -0.0236 -0.1355 0.0060 453 ARG A CA 3587 C C . ARG A 451 ? 0.5163 0.8069 1.0312 -0.0368 -0.1256 0.0043 453 ARG A C 3588 O O . ARG A 451 ? 0.5172 0.8185 1.0394 -0.0502 -0.1288 0.0069 453 ARG A O 3589 C CB . ARG A 451 ? 0.5325 0.8251 1.0649 -0.0274 -0.1581 0.0116 453 ARG A CB 3590 C CG . ARG A 451 ? 0.5231 0.8410 1.0937 -0.0183 -0.1700 0.0151 453 ARG A CG 3591 C CD . ARG A 451 ? 0.5354 0.8352 1.0939 -0.0142 -0.1901 0.0199 453 ARG A CD 3592 N NE . ARG A 451 ? 0.5604 0.8876 1.1570 -0.0124 -0.2059 0.0251 453 ARG A NE 3593 C CZ . ARG A 451 ? 0.5599 0.9196 1.1896 -0.0197 -0.2051 0.0260 453 ARG A CZ 3594 N NH1 . ARG A 451 ? 0.5486 0.9146 1.1746 -0.0297 -0.1893 0.0225 453 ARG A NH1 3595 N NH2 . ARG A 451 ? 0.5427 0.9287 1.2093 -0.0177 -0.2204 0.0310 453 ARG A NH2 3596 N N . ASP A 452 ? 0.5051 0.7734 0.9929 -0.0329 -0.1141 0.0003 454 ASP A N 3597 C CA . ASP A 452 ? 0.5055 0.7551 0.9656 -0.0433 -0.1066 -0.0011 454 ASP A CA 3598 C C . ASP A 452 ? 0.4888 0.7514 0.9554 -0.0483 -0.0901 -0.0030 454 ASP A C 3599 O O . ASP A 452 ? 0.5123 0.7577 0.9559 -0.0565 -0.0854 -0.0034 454 ASP A O 3600 C CB . ASP A 452 ? 0.5051 0.7220 0.9308 -0.0383 -0.1049 -0.0038 454 ASP A CB 3601 C CG . ASP A 452 ? 0.5186 0.7104 0.9159 -0.0482 -0.1144 -0.0025 454 ASP A CG 3602 O OD1 . ASP A 452 ? 0.5621 0.7560 0.9629 -0.0550 -0.1284 0.0009 454 ASP A OD1 3603 O OD2 . ASP A 452 ? 0.5272 0.6966 0.8985 -0.0490 -0.1081 -0.0052 454 ASP A OD2 3604 N N . GLN A 453 ? 0.4682 0.7596 0.9646 -0.0436 -0.0814 -0.0041 455 GLN A N 3605 C CA A GLN A 453 ? 0.4432 0.7474 0.9443 -0.0499 -0.0657 -0.0053 455 GLN A CA 3606 C CA B GLN A 453 ? 0.4498 0.7547 0.9515 -0.0497 -0.0654 -0.0054 455 GLN A CA 3607 C C . GLN A 453 ? 0.4313 0.7171 0.9073 -0.0459 -0.0518 -0.0094 455 GLN A C 3608 O O . GLN A 453 ? 0.4442 0.7326 0.9145 -0.0539 -0.0412 -0.0092 455 GLN A O 3609 C CB A GLN A 453 ? 0.8997 1.2074 1.3996 -0.0674 -0.0679 -0.0012 455 GLN A CB 3610 C CB B GLN A 453 ? 0.4617 0.7703 0.9626 -0.0675 -0.0681 -0.0011 455 GLN A CB 3611 C CG A GLN A 453 ? 0.8581 1.2015 1.3951 -0.0734 -0.0684 0.0016 455 GLN A CG 3612 C CG B GLN A 453 ? 0.4948 0.8140 1.0118 -0.0758 -0.0846 0.0036 455 GLN A CG 3613 C CD A GLN A 453 ? 0.8484 1.2025 1.4056 -0.0711 -0.0860 0.0044 455 GLN A CD 3614 C CD B GLN A 453 ? 0.5178 0.8076 1.0046 -0.0866 -0.0956 0.0056 455 GLN A CD 3615 O OE1 A GLN A 453 ? 0.8825 1.2145 1.4218 -0.0670 -0.0986 0.0049 455 GLN A OE1 3616 O OE1 B GLN A 453 ? 0.5325 0.8062 1.0073 -0.0840 -0.1089 0.0060 455 GLN A OE1 3617 N NE2 A GLN A 453 ? 0.0905 0.5033 0.7071 -0.0688 -0.0711 0.0036 455 GLN A NE2 3618 N NE2 B GLN A 453 ? 0.5013 0.7821 0.9741 -0.0986 -0.0895 0.0066 455 GLN A NE2 3619 N N . TYR A 454 ? 0.3736 0.6402 0.8338 -0.0346 -0.0527 -0.0125 456 TYR A N 3620 C CA . TYR A 454 ? 0.3218 0.5787 0.7670 -0.0286 -0.0390 -0.0170 456 TYR A CA 3621 C C . TYR A 454 ? 0.3019 0.5842 0.7722 -0.0203 -0.0273 -0.0210 456 TYR A C 3622 O O . TYR A 454 ? 0.2805 0.5833 0.7788 -0.0149 -0.0316 -0.0207 456 TYR A O 3623 C CB . TYR A 454 ? 0.2969 0.5292 0.7222 -0.0191 -0.0431 -0.0194 456 TYR A CB 3624 C CG . TYR A 454 ? 0.2666 0.4725 0.6649 -0.0254 -0.0511 -0.0173 456 TYR A CG 3625 C CD1 . TYR A 454 ? 0.2737 0.4708 0.6686 -0.0265 -0.0652 -0.0147 456 TYR A CD1 3626 C CD2 . TYR A 454 ? 0.2254 0.4144 0.6011 -0.0299 -0.0446 -0.0183 456 TYR A CD2 3627 C CE1 . TYR A 454 ? 0.2813 0.4532 0.6499 -0.0320 -0.0709 -0.0140 456 TYR A CE1 3628 C CE2 . TYR A 454 ? 0.2888 0.4534 0.6411 -0.0343 -0.0509 -0.0174 456 TYR A CE2 3629 C CZ . TYR A 454 ? 0.2961 0.4523 0.6447 -0.0352 -0.0631 -0.0158 456 TYR A CZ 3630 O OH . TYR A 454 ? 0.3126 0.4448 0.6374 -0.0394 -0.0672 -0.0161 456 TYR A OH 3631 N N . THR A 455 ? 0.2819 0.5628 0.7425 -0.0191 -0.0127 -0.0248 457 THR A N 3632 C CA . THR A 455 ? 0.2523 0.5559 0.7340 -0.0113 0.0004 -0.0299 457 THR A CA 3633 C C . THR A 455 ? 0.2547 0.5516 0.7406 0.0051 -0.0021 -0.0345 457 THR A C 3634 O O . THR A 455 ? 0.2398 0.5135 0.7086 0.0090 -0.0118 -0.0336 457 THR A O 3635 C CB . THR A 455 ? 0.2499 0.5502 0.7146 -0.0149 0.0168 -0.0333 457 THR A CB 3636 O OG1 . THR A 455 ? 0.2276 0.4994 0.6633 -0.0102 0.0161 -0.0357 457 THR A OG1 3637 C CG2 . THR A 455 ? 0.2168 0.5202 0.6735 -0.0316 0.0199 -0.0281 457 THR A CG2 3638 N N . LYS A 456 ? 0.2450 0.5618 0.7538 0.0145 0.0073 -0.0397 458 LYS A N 3639 C CA . LYS A 456 ? 0.2593 0.5691 0.7728 0.0307 0.0067 -0.0450 458 LYS A CA 3640 C C . LYS A 456 ? 0.2458 0.5276 0.7265 0.0339 0.0128 -0.0494 458 LYS A C 3641 O O . LYS A 456 ? 0.2626 0.5238 0.7322 0.0423 0.0056 -0.0505 458 LYS A O 3642 C CB . LYS A 456 ? 0.2599 0.6012 0.8101 0.0399 0.0169 -0.0502 458 LYS A CB 3643 C CG . LYS A 456 ? 0.3269 0.6628 0.8864 0.0576 0.0169 -0.0563 458 LYS A CG 3644 C CD . LYS A 456 ? 0.4073 0.7481 0.9901 0.0658 -0.0005 -0.0519 458 LYS A CD 3645 C CE . LYS A 456 ? 0.4864 0.8026 1.0587 0.0804 -0.0051 -0.0556 458 LYS A CE 3646 N NZ . LYS A 456 ? 0.5093 0.8230 1.0979 0.0888 -0.0238 -0.0505 458 LYS A NZ 3647 N N . ALA A 457 ? 0.2330 0.5121 0.6962 0.0259 0.0246 -0.0511 459 ALA A N 3648 C CA . ALA A 457 ? 0.2248 0.4793 0.6588 0.0280 0.0289 -0.0549 459 ALA A CA 3649 C C . ALA A 457 ? 0.2298 0.4587 0.6422 0.0246 0.0155 -0.0499 459 ALA A C 3650 O O . ALA A 457 ? 0.2397 0.4484 0.6353 0.0300 0.0141 -0.0525 459 ALA A O 3651 C CB . ALA A 457 ? 0.2097 0.4656 0.6275 0.0190 0.0425 -0.0566 459 ALA A CB 3652 N N . GLU A 458 ? 0.2176 0.4480 0.6314 0.0157 0.0062 -0.0433 460 GLU A N 3653 C CA . GLU A 458 ? 0.2171 0.4243 0.6105 0.0118 -0.0051 -0.0393 460 GLU A CA 3654 C C . GLU A 458 ? 0.2179 0.4169 0.6163 0.0205 -0.0165 -0.0386 460 GLU A C 3655 O O . GLU A 458 ? 0.2108 0.3881 0.5906 0.0224 -0.0213 -0.0384 460 GLU A O 3656 C CB . GLU A 458 ? 0.2200 0.4313 0.6130 -0.0012 -0.0105 -0.0333 460 GLU A CB 3657 C CG . GLU A 458 ? 0.2356 0.4417 0.6113 -0.0110 -0.0019 -0.0326 460 GLU A CG 3658 C CD . GLU A 458 ? 0.2569 0.4660 0.6324 -0.0243 -0.0063 -0.0268 460 GLU A CD 3659 O OE1 . GLU A 458 ? 0.2590 0.4835 0.6537 -0.0269 -0.0119 -0.0243 460 GLU A OE1 3660 O OE2 . GLU A 458 ? 0.2878 0.4834 0.6441 -0.0322 -0.0047 -0.0247 460 GLU A OE2 3661 N N . GLU A 459 ? 0.2247 0.4419 0.6492 0.0257 -0.0209 -0.0378 461 GLU A N 3662 C CA . GLU A 459 ? 0.2393 0.4493 0.6695 0.0347 -0.0317 -0.0368 461 GLU A CA 3663 C C . GLU A 459 ? 0.2406 0.4338 0.6594 0.0452 -0.0270 -0.0421 461 GLU A C 3664 O O . GLU A 459 ? 0.2679 0.4401 0.6719 0.0480 -0.0349 -0.0406 461 GLU A O 3665 C CB . GLU A 459 ? 0.2224 0.4585 0.6870 0.0400 -0.0353 -0.0359 461 GLU A CB 3666 C CG . GLU A 459 ? 0.3119 0.5402 0.7841 0.0508 -0.0476 -0.0343 461 GLU A CG 3667 C CD . GLU A 459 ? 0.3760 0.6305 0.8866 0.0602 -0.0509 -0.0345 461 GLU A CD 3668 O OE1 . GLU A 459 ? 0.3763 0.6232 0.8936 0.0704 -0.0609 -0.0332 461 GLU A OE1 3669 O OE2 . GLU A 459 ? 0.4182 0.7003 0.9527 0.0575 -0.0437 -0.0356 461 GLU A OE2 3670 N N . ILE A 460 ? 0.2508 0.4524 0.6751 0.0500 -0.0137 -0.0484 462 ILE A N 3671 C CA . ILE A 460 ? 0.2639 0.4497 0.6770 0.0591 -0.0082 -0.0545 462 ILE A CA 3672 C C . ILE A 460 ? 0.2574 0.4181 0.6384 0.0530 -0.0077 -0.0543 462 ILE A C 3673 O O . ILE A 460 ? 0.2573 0.3985 0.6263 0.0582 -0.0113 -0.0557 462 ILE A O 3674 C CB . ILE A 460 ? 0.2906 0.4929 0.7168 0.0650 0.0076 -0.0625 462 ILE A CB 3675 C CG1 . ILE A 460 ? 0.3031 0.5316 0.7655 0.0735 0.0080 -0.0638 462 ILE A CG1 3676 C CG2 . ILE A 460 ? 0.3032 0.4880 0.7163 0.0736 0.0136 -0.0699 462 ILE A CG2 3677 C CD1 . ILE A 460 ? 0.3722 0.5929 0.8474 0.0869 -0.0028 -0.0637 462 ILE A CD1 3678 N N . LEU A 461 ? 0.2272 0.3886 0.5956 0.0418 -0.0038 -0.0523 463 LEU A N 3679 C CA . LEU A 461 ? 0.2226 0.3635 0.5651 0.0365 -0.0039 -0.0519 463 LEU A CA 3680 C C . LEU A 461 ? 0.2243 0.3494 0.5582 0.0355 -0.0161 -0.0473 463 LEU A C 3681 O O . LEU A 461 ? 0.2249 0.3312 0.5435 0.0375 -0.0178 -0.0484 463 LEU A O 3682 C CB . LEU A 461 ? 0.2220 0.3673 0.5557 0.0251 0.0006 -0.0495 463 LEU A CB 3683 C CG . LEU A 461 ? 0.2033 0.3284 0.5130 0.0196 -0.0013 -0.0482 463 LEU A CG 3684 C CD1 . LEU A 461 ? 0.2120 0.3233 0.5081 0.0246 0.0033 -0.0535 463 LEU A CD1 3685 C CD2 . LEU A 461 ? 0.1945 0.3233 0.4970 0.0087 0.0019 -0.0450 463 LEU A CD2 3686 N N . SER A 462 ? 0.2001 0.3329 0.5441 0.0324 -0.0243 -0.0424 464 SER A N 3687 C CA . SER A 462 ? 0.2080 0.3253 0.5406 0.0299 -0.0350 -0.0382 464 SER A CA 3688 C C . SER A 462 ? 0.2172 0.3227 0.5497 0.0392 -0.0407 -0.0387 464 SER A C 3689 O O . SER A 462 ? 0.2181 0.3040 0.5331 0.0383 -0.0445 -0.0376 464 SER A O 3690 C CB . SER A 462 ? 0.1977 0.3257 0.5404 0.0241 -0.0433 -0.0333 464 SER A CB 3691 O OG . SER A 462 ? 0.1784 0.2895 0.5061 0.0208 -0.0529 -0.0298 464 SER A OG 3692 N N . ARG A 463 ? 0.2162 0.3343 0.5694 0.0479 -0.0413 -0.0401 465 ARG A N 3693 C CA . ARG A 463 ? 0.2464 0.3532 0.6018 0.0575 -0.0474 -0.0402 465 ARG A CA 3694 C C . ARG A 463 ? 0.2571 0.3444 0.5943 0.0601 -0.0414 -0.0446 465 ARG A C 3695 O O . ARG A 463 ? 0.2767 0.3441 0.6011 0.0617 -0.0475 -0.0428 465 ARG A O 3696 C CB . ARG A 463 ? 0.2361 0.3620 0.6205 0.0680 -0.0467 -0.0425 465 ARG A CB 3697 C CG . ARG A 463 ? 0.2674 0.3804 0.6554 0.0793 -0.0533 -0.0428 465 ARG A CG 3698 C CD . ARG A 463 ? 0.3105 0.4161 0.6971 0.0777 -0.0693 -0.0349 465 ARG A CD 3699 N NE . ARG A 463 ? 0.3205 0.4046 0.7000 0.0850 -0.0781 -0.0328 465 ARG A NE 3700 C CZ . ARG A 463 ? 0.3487 0.4073 0.7013 0.0808 -0.0797 -0.0313 465 ARG A CZ 3701 N NH1 . ARG A 463 ? 0.1877 0.2397 0.5195 0.0705 -0.0725 -0.0325 465 ARG A NH1 3702 N NH2 . ARG A 463 ? 0.3876 0.4273 0.7351 0.0867 -0.0889 -0.0281 465 ARG A NH2 3703 N N . SER A 464 ? 0.2419 0.3344 0.5769 0.0594 -0.0298 -0.0500 466 SER A N 3704 C CA . SER A 464 ? 0.2662 0.3416 0.5853 0.0612 -0.0249 -0.0544 466 SER A CA 3705 C C . SER A 464 ? 0.2561 0.3144 0.5524 0.0522 -0.0279 -0.0512 466 SER A C 3706 O O . SER A 464 ? 0.2797 0.3195 0.5634 0.0532 -0.0304 -0.0514 466 SER A O 3707 C CB . SER A 464 ? 0.2621 0.3481 0.5840 0.0622 -0.0124 -0.0610 466 SER A CB 3708 O OG . SER A 464 ? 0.3203 0.3904 0.6238 0.0610 -0.0080 -0.0650 466 SER A OG 3709 N N . ILE A 465 ? 0.2522 0.3165 0.5445 0.0434 -0.0278 -0.0481 467 ILE A N 3710 C CA . ILE A 465 ? 0.2449 0.2956 0.5190 0.0356 -0.0297 -0.0457 467 ILE A CA 3711 C C . ILE A 465 ? 0.2500 0.2882 0.5182 0.0356 -0.0389 -0.0414 467 ILE A C 3712 O O . ILE A 465 ? 0.2503 0.2725 0.5041 0.0333 -0.0399 -0.0409 467 ILE A O 3713 C CB . ILE A 465 ? 0.2509 0.3109 0.5242 0.0272 -0.0281 -0.0435 467 ILE A CB 3714 C CG1 . ILE A 465 ? 0.2632 0.3306 0.5359 0.0253 -0.0192 -0.0468 467 ILE A CG1 3715 C CG2 . ILE A 465 ? 0.1946 0.2416 0.4531 0.0203 -0.0319 -0.0405 467 ILE A CG2 3716 C CD1 . ILE A 465 ? 0.1767 0.2540 0.4506 0.0171 -0.0178 -0.0439 467 ILE A CD1 3717 N N . VAL A 466 ? 0.2300 0.2760 0.5092 0.0373 -0.0458 -0.0380 468 VAL A N 3718 C CA . VAL A 466 ? 0.2291 0.2623 0.5010 0.0371 -0.0555 -0.0335 468 VAL A CA 3719 C C . VAL A 466 ? 0.2388 0.2559 0.5048 0.0432 -0.0570 -0.0343 468 VAL A C 3720 O O . VAL A 466 ? 0.2329 0.2326 0.4824 0.0395 -0.0601 -0.0317 468 VAL A O 3721 C CB . VAL A 466 ? 0.2222 0.2673 0.5090 0.0389 -0.0644 -0.0296 468 VAL A CB 3722 C CG1 . VAL A 466 ? 0.2253 0.2559 0.5050 0.0407 -0.0755 -0.0247 468 VAL A CG1 3723 C CG2 . VAL A 466 ? 0.1786 0.2327 0.4644 0.0298 -0.0650 -0.0278 468 VAL A CG2 3724 N N . LYS A 467 ? 0.2263 0.2483 0.5050 0.0520 -0.0539 -0.0381 469 LYS A N 3725 C CA . LYS A 467 ? 0.2363 0.2411 0.5093 0.0579 -0.0551 -0.0397 469 LYS A CA 3726 C C . LYS A 467 ? 0.2462 0.2372 0.5014 0.0526 -0.0489 -0.0424 469 LYS A C 3727 O O . LYS A 467 ? 0.2736 0.2456 0.5154 0.0509 -0.0523 -0.0404 469 LYS A O 3728 C CB . LYS A 467 ? 0.2323 0.2455 0.5236 0.0692 -0.0520 -0.0447 469 LYS A CB 3729 C CG . LYS A 467 ? 0.2347 0.2285 0.5199 0.0759 -0.0516 -0.0481 469 LYS A CG 3730 C CD . LYS A 467 ? 0.2639 0.2386 0.5412 0.0766 -0.0639 -0.0412 469 LYS A CD 3731 C CE . LYS A 467 ? 0.2864 0.2699 0.5842 0.0857 -0.0731 -0.0378 469 LYS A CE 3732 N NZ . LYS A 467 ? 0.2849 0.2485 0.5713 0.0847 -0.0861 -0.0299 469 LYS A NZ 3733 N N . ARG A 468 ? 0.2503 0.2502 0.5049 0.0493 -0.0403 -0.0466 470 ARG A N 3734 C CA . ARG A 468 ? 0.2538 0.2422 0.4934 0.0439 -0.0359 -0.0487 470 ARG A CA 3735 C C . ARG A 468 ? 0.2706 0.2494 0.4970 0.0356 -0.0392 -0.0440 470 ARG A C 3736 O O . ARG A 468 ? 0.2727 0.2367 0.4877 0.0326 -0.0393 -0.0438 470 ARG A O 3737 C CB . ARG A 468 ? 0.2378 0.2377 0.4783 0.0410 -0.0278 -0.0528 470 ARG A CB 3738 C CG . ARG A 468 ? 0.2541 0.2613 0.5030 0.0478 -0.0219 -0.0588 470 ARG A CG 3739 C CD . ARG A 468 ? 0.2458 0.2613 0.4907 0.0431 -0.0147 -0.0618 470 ARG A CD 3740 N NE . ARG A 468 ? 0.2203 0.2425 0.4698 0.0482 -0.0074 -0.0681 470 ARG A NE 3741 C CZ . ARG A 468 ? 0.2634 0.2746 0.5051 0.0513 -0.0041 -0.0741 470 ARG A CZ 3742 N NH1 . ARG A 468 ? 0.2199 0.2381 0.4651 0.0557 0.0036 -0.0803 470 ARG A NH1 3743 N NH2 . ARG A 468 ? 0.2688 0.2617 0.4988 0.0496 -0.0080 -0.0742 470 ARG A NH2 3744 N N . TRP A 469 ? 0.2620 0.2489 0.4895 0.0313 -0.0414 -0.0406 471 TRP A N 3745 C CA . TRP A 469 ? 0.2448 0.2233 0.4595 0.0237 -0.0430 -0.0373 471 TRP A CA 3746 C C . TRP A 469 ? 0.2629 0.2252 0.4682 0.0238 -0.0493 -0.0334 471 TRP A C 3747 O O . TRP A 469 ? 0.2712 0.2211 0.4633 0.0183 -0.0480 -0.0323 471 TRP A O 3748 C CB . TRP A 469 ? 0.2207 0.2095 0.4382 0.0198 -0.0448 -0.0352 471 TRP A CB 3749 C CG . TRP A 469 ? 0.2362 0.2320 0.4529 0.0146 -0.0387 -0.0373 471 TRP A CG 3750 C CD1 . TRP A 469 ? 0.2339 0.2270 0.4428 0.0082 -0.0382 -0.0363 471 TRP A CD1 3751 C CD2 . TRP A 469 ? 0.2152 0.2192 0.4375 0.0154 -0.0328 -0.0407 471 TRP A CD2 3752 N NE1 . TRP A 469 ? 0.2369 0.2365 0.4488 0.0061 -0.0332 -0.0385 471 TRP A NE1 3753 C CE2 . TRP A 469 ? 0.1827 0.1886 0.4017 0.0098 -0.0303 -0.0407 471 TRP A CE2 3754 C CE3 . TRP A 469 ? 0.2164 0.2257 0.4454 0.0203 -0.0295 -0.0439 471 TRP A CE3 3755 C CZ2 . TRP A 469 ? 0.1861 0.1987 0.4081 0.0088 -0.0260 -0.0424 471 TRP A CZ2 3756 C CZ3 . TRP A 469 ? 0.2025 0.2185 0.4325 0.0185 -0.0244 -0.0462 471 TRP A CZ3 3757 C CH2 . TRP A 469 ? 0.2205 0.2377 0.4467 0.0126 -0.0233 -0.0449 471 TRP A CH2 3758 N N . ALA A 470 ? 0.2581 0.2206 0.4707 0.0300 -0.0564 -0.0310 472 ALA A N 3759 C CA . ALA A 470 ? 0.2756 0.2217 0.4789 0.0304 -0.0644 -0.0260 472 ALA A CA 3760 C C . ALA A 470 ? 0.2772 0.2081 0.4748 0.0325 -0.0626 -0.0277 472 ALA A C 3761 O O . ALA A 470 ? 0.2956 0.2097 0.4779 0.0273 -0.0645 -0.0243 472 ALA A O 3762 C CB . ALA A 470 ? 0.2737 0.2250 0.4897 0.0377 -0.0738 -0.0229 472 ALA A CB 3763 N N . ASN A 471 ? 0.2617 0.1974 0.4700 0.0393 -0.0586 -0.0330 473 ASN A N 3764 C CA . ASN A 471 ? 0.2787 0.1987 0.4800 0.0400 -0.0564 -0.0356 473 ASN A CA 3765 C C . ASN A 471 ? 0.2876 0.2025 0.4762 0.0301 -0.0508 -0.0362 473 ASN A C 3766 O O . ASN A 471 ? 0.3087 0.2067 0.4859 0.0261 -0.0521 -0.0343 473 ASN A O 3767 C CB . ASN A 471 ? 0.2666 0.1916 0.4793 0.0485 -0.0522 -0.0425 473 ASN A CB 3768 C CG . ASN A 471 ? 0.2942 0.2162 0.5186 0.0598 -0.0583 -0.0422 473 ASN A CG 3769 O OD1 . ASN A 471 ? 0.3357 0.2487 0.5582 0.0611 -0.0675 -0.0359 473 ASN A OD1 3770 N ND2 . ASN A 471 ? 0.2712 0.2014 0.5080 0.0681 -0.0533 -0.0489 473 ASN A ND2 3771 N N . PHE A 472 ? 0.2606 0.1898 0.4518 0.0258 -0.0452 -0.0382 474 PHE A N 3772 C CA . PHE A 472 ? 0.2516 0.1780 0.4340 0.0171 -0.0405 -0.0384 474 PHE A CA 3773 C C . PHE A 472 ? 0.2694 0.1843 0.4391 0.0105 -0.0431 -0.0330 474 PHE A C 3774 O O . PHE A 472 ? 0.2822 0.1849 0.4428 0.0053 -0.0419 -0.0319 474 PHE A O 3775 C CB . PHE A 472 ? 0.2479 0.1903 0.4357 0.0141 -0.0352 -0.0406 474 PHE A CB 3776 C CG . PHE A 472 ? 0.2593 0.2000 0.4419 0.0067 -0.0307 -0.0413 474 PHE A CG 3777 C CD1 . PHE A 472 ? 0.2321 0.1687 0.4144 0.0054 -0.0286 -0.0443 474 PHE A CD1 3778 C CD2 . PHE A 472 ? 0.2168 0.1590 0.3950 0.0011 -0.0289 -0.0391 474 PHE A CD2 3779 C CE1 . PHE A 472 ? 0.2190 0.1563 0.3999 -0.0014 -0.0252 -0.0446 474 PHE A CE1 3780 C CE2 . PHE A 472 ? 0.2260 0.1686 0.4028 -0.0050 -0.0241 -0.0401 474 PHE A CE2 3781 C CZ . PHE A 472 ? 0.2506 0.1915 0.4300 -0.0062 -0.0226 -0.0425 474 PHE A CZ 3782 N N . ALA A 473 ? 0.2583 0.1759 0.4260 0.0102 -0.0470 -0.0293 475 ALA A N 3783 C CA . ALA A 473 ? 0.2542 0.1604 0.4064 0.0029 -0.0487 -0.0246 475 ALA A CA 3784 C C . ALA A 473 ? 0.2826 0.1688 0.4242 0.0024 -0.0541 -0.0203 475 ALA A C 3785 O O . ALA A 473 ? 0.2847 0.1590 0.4129 -0.0057 -0.0514 -0.0180 475 ALA A O 3786 C CB . ALA A 473 ? 0.2276 0.1387 0.3776 0.0022 -0.0532 -0.0218 475 ALA A CB 3787 N N . LYS A 474 ? 0.2963 0.1786 0.4444 0.0108 -0.0614 -0.0191 476 LYS A N 3788 C CA . LYS A 474 ? 0.3423 0.2031 0.4809 0.0115 -0.0681 -0.0145 476 LYS A CA 3789 C C . LYS A 474 ? 0.3553 0.2052 0.4913 0.0096 -0.0638 -0.0175 476 LYS A C 3790 O O . LYS A 474 ? 0.3824 0.2136 0.5043 0.0035 -0.0657 -0.0133 476 LYS A O 3791 C CB . LYS A 474 ? 0.3564 0.2164 0.5062 0.0228 -0.0775 -0.0131 476 LYS A CB 3792 C CG . LYS A 474 ? 0.3663 0.2367 0.5208 0.0249 -0.0844 -0.0094 476 LYS A CG 3793 C CD . LYS A 474 ? 0.4390 0.3102 0.6092 0.0371 -0.0936 -0.0083 476 LYS A CD 3794 C CE . LYS A 474 ? 0.5124 0.3961 0.6903 0.0388 -0.1021 -0.0042 476 LYS A CE 3795 N NZ . LYS A 474 ? 0.4949 0.3961 0.7001 0.0513 -0.1052 -0.0072 476 LYS A NZ 3796 N N . TYR A 475 ? 0.3367 0.1973 0.4849 0.0139 -0.0584 -0.0245 477 TYR A N 3797 C CA . TYR A 475 ? 0.3630 0.2116 0.5101 0.0146 -0.0569 -0.0281 477 TYR A CA 3798 C C . TYR A 475 ? 0.3538 0.2113 0.5032 0.0090 -0.0489 -0.0333 477 TYR A C 3799 O O . TYR A 475 ? 0.3648 0.2124 0.5121 0.0081 -0.0482 -0.0365 477 TYR A O 3800 C CB . TYR A 475 ? 0.3606 0.2082 0.5190 0.0269 -0.0600 -0.0324 477 TYR A CB 3801 C CG . TYR A 475 ? 0.3632 0.2050 0.5246 0.0345 -0.0691 -0.0275 477 TYR A CG 3802 C CD1 . TYR A 475 ? 0.3389 0.1966 0.5173 0.0448 -0.0704 -0.0300 477 TYR A CD1 3803 C CD2 . TYR A 475 ? 0.3711 0.1919 0.5191 0.0310 -0.0767 -0.0200 477 TYR A CD2 3804 C CE1 . TYR A 475 ? 0.3027 0.1574 0.4867 0.0516 -0.0800 -0.0250 477 TYR A CE1 3805 C CE2 . TYR A 475 ? 0.3944 0.2092 0.5453 0.0380 -0.0870 -0.0147 477 TYR A CE2 3806 C CZ . TYR A 475 ? 0.3592 0.1917 0.5291 0.0485 -0.0890 -0.0172 477 TYR A CZ 3807 O OH . TYR A 475 ? 0.3755 0.2034 0.5502 0.0552 -0.1004 -0.0113 477 TYR A OH 3808 N N . GLY A 476 ? 0.3388 0.2138 0.4923 0.0054 -0.0439 -0.0341 478 GLY A N 3809 C CA . GLY A 476 ? 0.3300 0.2160 0.4878 0.0008 -0.0374 -0.0382 478 GLY A CA 3810 C C . GLY A 476 ? 0.3264 0.2200 0.4928 0.0067 -0.0359 -0.0445 478 GLY A C 3811 O O . GLY A 476 ? 0.3430 0.2401 0.5105 0.0025 -0.0327 -0.0476 478 GLY A O 3812 N N . ASN A 477 ? 0.2980 0.1953 0.4708 0.0159 -0.0379 -0.0462 479 ASN A N 3813 C CA . ASN A 477 ? 0.3111 0.2136 0.4898 0.0217 -0.0353 -0.0527 479 ASN A CA 3814 C C . ASN A 477 ? 0.2892 0.2069 0.4788 0.0293 -0.0345 -0.0538 479 ASN A C 3815 O O . ASN A 477 ? 0.3339 0.2485 0.5281 0.0362 -0.0383 -0.0526 479 ASN A O 3816 C CB . ASN A 477 ? 0.3374 0.2211 0.5114 0.0257 -0.0379 -0.0556 479 ASN A CB 3817 C CG . ASN A 477 ? 0.3581 0.2413 0.5311 0.0270 -0.0343 -0.0633 479 ASN A CG 3818 O OD1 . ASN A 477 ? 0.3760 0.2742 0.5531 0.0273 -0.0300 -0.0664 479 ASN A OD1 3819 N ND2 . ASN A 477 ? 0.3995 0.2635 0.5651 0.0273 -0.0364 -0.0662 479 ASN A ND2 3820 N N . PRO A 478 ? 0.2646 0.1989 0.4593 0.0277 -0.0302 -0.0556 480 PRO A N 3821 C CA . PRO A 478 ? 0.2397 0.1898 0.4449 0.0322 -0.0297 -0.0547 480 PRO A CA 3822 C C . PRO A 478 ? 0.2599 0.2149 0.4725 0.0403 -0.0266 -0.0603 480 PRO A C 3823 O O . PRO A 478 ? 0.2341 0.2036 0.4517 0.0403 -0.0218 -0.0627 480 PRO A O 3824 C CB . PRO A 478 ? 0.1973 0.1600 0.4028 0.0259 -0.0261 -0.0542 480 PRO A CB 3825 C CG . PRO A 478 ? 0.2285 0.1857 0.4274 0.0222 -0.0236 -0.0577 480 PRO A CG 3826 C CD . PRO A 478 ? 0.2363 0.1759 0.4279 0.0210 -0.0265 -0.0573 480 PRO A CD 3827 N N . GLN A 479 ? 0.2851 0.2274 0.4977 0.0468 -0.0288 -0.0627 481 GLN A N 3828 C CA . GLN A 479 ? 0.3009 0.2471 0.5216 0.0561 -0.0248 -0.0692 481 GLN A CA 3829 C C . GLN A 479 ? 0.3075 0.2653 0.5445 0.0638 -0.0273 -0.0670 481 GLN A C 3830 O O . GLN A 479 ? 0.3157 0.2714 0.5542 0.0628 -0.0345 -0.0603 481 GLN A O 3831 C CB . GLN A 479 ? 0.2914 0.2168 0.5052 0.0604 -0.0258 -0.0739 481 GLN A CB 3832 C CG . GLN A 479 ? 0.3110 0.2230 0.5088 0.0515 -0.0252 -0.0755 481 GLN A CG 3833 C CD . GLN A 479 ? 0.3167 0.2404 0.5104 0.0459 -0.0192 -0.0791 481 GLN A CD 3834 O OE1 . GLN A 479 ? 0.3498 0.2861 0.5488 0.0500 -0.0135 -0.0833 481 GLN A OE1 3835 N NE2 . GLN A 479 ? 0.2343 0.1544 0.4192 0.0364 -0.0205 -0.0770 481 GLN A NE2 3836 N N . GLU A 480 ? 0.3070 0.2774 0.5559 0.0710 -0.0214 -0.0726 482 GLU A N 3837 C CA . GLU A 480 ? 0.3409 0.3234 0.6095 0.0801 -0.0235 -0.0719 482 GLU A CA 3838 C C . GLU A 480 ? 0.3675 0.3396 0.6389 0.0903 -0.0203 -0.0796 482 GLU A C 3839 O O . GLU A 480 ? 0.3832 0.3605 0.6535 0.0920 -0.0105 -0.0876 482 GLU A O 3840 C CB . GLU A 480 ? 0.3244 0.3333 0.6065 0.0788 -0.0179 -0.0721 482 GLU A CB 3841 C CG . GLU A 480 ? 0.3520 0.3768 0.6583 0.0875 -0.0211 -0.0705 482 GLU A CG 3842 C CD . GLU A 480 ? 0.4257 0.4463 0.7435 0.1006 -0.0186 -0.0772 482 GLU A CD 3843 O OE1 . GLU A 480 ? 0.4293 0.4426 0.7572 0.1091 -0.0271 -0.0748 482 GLU A OE1 3844 O OE2 . GLU A 480 ? 0.4966 0.5199 0.8124 0.1028 -0.0079 -0.0855 482 GLU A OE2 3845 N N . THR A 481 ? 0.3743 0.3280 0.6453 0.0960 -0.0283 -0.0776 483 THR A N 3846 C CA . THR A 481 ? 0.3919 0.3283 0.6606 0.1046 -0.0260 -0.0853 483 THR A CA 3847 C C . THR A 481 ? 0.4051 0.3508 0.6961 0.1196 -0.0227 -0.0913 483 THR A C 3848 O O . THR A 481 ? 0.3956 0.3286 0.6849 0.1272 -0.0183 -0.0998 483 THR A O 3849 C CB . THR A 481 ? 0.4071 0.3150 0.6634 0.1038 -0.0359 -0.0808 483 THR A CB 3850 O OG1 . THR A 481 ? 0.4069 0.3157 0.6749 0.1088 -0.0460 -0.0731 483 THR A OG1 3851 C CG2 . THR A 481 ? 0.3756 0.2739 0.6113 0.0893 -0.0379 -0.0757 483 THR A CG2 3852 N N . GLN A 482 ? 0.4113 0.3788 0.7238 0.1239 -0.0250 -0.0874 484 GLN A N 3853 C CA . GLN A 482 ? 0.4515 0.4276 0.7896 0.1393 -0.0244 -0.0918 484 GLN A CA 3854 C C . GLN A 482 ? 0.4532 0.4555 0.8074 0.1434 -0.0105 -0.1000 484 GLN A C 3855 O O . GLN A 482 ? 0.4496 0.4576 0.8226 0.1563 -0.0060 -0.1068 484 GLN A O 3856 C CB . GLN A 482 ? 0.4476 0.4312 0.8033 0.1431 -0.0375 -0.0821 484 GLN A CB 3857 C CG . GLN A 482 ? 0.4976 0.4562 0.8361 0.1381 -0.0512 -0.0729 484 GLN A CG 3858 C CD . GLN A 482 ? 0.5417 0.5068 0.8929 0.1395 -0.0650 -0.0626 484 GLN A CD 3859 O OE1 . GLN A 482 ? 0.5213 0.5080 0.8802 0.1335 -0.0662 -0.0581 484 GLN A OE1 3860 N NE2 . GLN A 482 ? 0.5880 0.5322 0.9397 0.1469 -0.0768 -0.0584 484 GLN A NE2 3861 N N . ASN A 483 ? 0.4709 0.4890 0.8179 0.1322 -0.0034 -0.0994 485 ASN A N 3862 C CA . ASN A 483 ? 0.5004 0.5459 0.8637 0.1344 0.0092 -0.1051 485 ASN A CA 3863 C C . ASN A 483 ? 0.5160 0.5607 0.8620 0.1296 0.0238 -0.1144 485 ASN A C 3864 O O . ASN A 483 ? 0.5258 0.5918 0.8750 0.1236 0.0332 -0.1154 485 ASN A O 3865 C CB . ASN A 483 ? 0.4808 0.5508 0.8566 0.1267 0.0057 -0.0965 485 ASN A CB 3866 C CG . ASN A 483 ? 0.5375 0.6161 0.9383 0.1345 -0.0062 -0.0901 485 ASN A CG 3867 O OD1 . ASN A 483 ? 0.4782 0.5446 0.8874 0.1459 -0.0121 -0.0914 485 ASN A OD1 3868 N ND2 . ASN A 483 ? 0.6897 0.7879 1.1013 0.1277 -0.0109 -0.0826 485 ASN A ND2 3869 N N . GLN A 484 ? 0.6591 0.6928 1.0306 0.2564 -0.0866 -0.1018 486 GLN A N 3870 C CA . GLN A 484 ? 0.6622 0.6936 1.0148 0.2482 -0.0558 -0.1079 486 GLN A CA 3871 C C . GLN A 484 ? 0.6231 0.6712 0.9621 0.2199 -0.0426 -0.1017 486 GLN A C 3872 O O . GLN A 484 ? 0.6268 0.6999 0.9782 0.2137 -0.0174 -0.1076 486 GLN A O 3873 C CB . GLN A 484 ? 0.6757 0.7391 1.0738 0.2673 -0.0331 -0.1226 486 GLN A CB 3874 C CG . GLN A 484 ? 0.7583 0.8297 1.2020 0.2990 -0.0495 -0.1300 486 GLN A CG 3875 C CD . GLN A 484 ? 0.8691 0.8810 1.2694 0.3154 -0.0649 -0.1303 486 GLN A CD 3876 O OE1 . GLN A 484 ? 0.9184 0.8895 1.2649 0.3071 -0.0542 -0.1301 486 GLN A OE1 3877 N NE2 . GLN A 484 ? 0.9065 0.9111 1.3301 0.3387 -0.0919 -0.1310 486 GLN A NE2 3878 N N . SER A 485 ? 0.5930 0.6253 0.9053 0.2032 -0.0585 -0.0898 487 SER A N 3879 C CA . SER A 485 ? 0.5443 0.5912 0.8459 0.1787 -0.0476 -0.0844 487 SER A CA 3880 C C . SER A 485 ? 0.5387 0.5547 0.7962 0.1667 -0.0351 -0.0840 487 SER A C 3881 O O . SER A 485 ? 0.5633 0.5393 0.7915 0.1728 -0.0408 -0.0846 487 SER A O 3882 C CB . SER A 485 ? 0.5252 0.5665 0.8152 0.1660 -0.0672 -0.0729 487 SER A CB 3883 O OG . SER A 485 ? 0.5704 0.6353 0.8989 0.1781 -0.0845 -0.0739 487 SER A OG 3884 N N . THR A 486 ? 0.4916 0.5245 0.7454 0.1493 -0.0203 -0.0831 488 THR A N 3885 C CA . THR A 486 ? 0.4710 0.4791 0.6872 0.1342 -0.0136 -0.0814 488 THR A CA 3886 C C . THR A 486 ? 0.4570 0.4357 0.6483 0.1246 -0.0297 -0.0716 488 THR A C 3887 O O . THR A 486 ? 0.4322 0.4186 0.6291 0.1187 -0.0400 -0.0637 488 THR A O 3888 C CB . THR A 486 ? 0.4463 0.4789 0.6662 0.1170 -0.0021 -0.0792 488 THR A CB 3889 O OG1 . THR A 486 ? 0.4745 0.5367 0.7203 0.1235 0.0153 -0.0866 488 THR A OG1 3890 C CG2 . THR A 486 ? 0.4461 0.4542 0.6319 0.1043 0.0024 -0.0790 488 THR A CG2 3891 N N . SER A 487 ? 0.4511 0.3934 0.6138 0.1230 -0.0309 -0.0727 489 SER A N 3892 C CA . SER A 487 ? 0.4667 0.3776 0.6051 0.1112 -0.0403 -0.0645 489 SER A CA 3893 C C . SER A 487 ? 0.4163 0.3382 0.5516 0.0899 -0.0348 -0.0594 489 SER A C 3894 O O . SER A 487 ? 0.4056 0.3406 0.5429 0.0843 -0.0256 -0.0641 489 SER A O 3895 C CB . SER A 487 ? 0.5071 0.3803 0.6223 0.1141 -0.0411 -0.0696 489 SER A CB 3896 O OG . SER A 487 ? 0.6144 0.4527 0.7118 0.1128 -0.0521 -0.0629 489 SER A OG 3897 N N . TRP A 488 ? 0.3777 0.2932 0.5069 0.0796 -0.0399 -0.0499 490 TRP A N 3898 C CA . TRP A 488 ? 0.3242 0.2506 0.4538 0.0614 -0.0339 -0.0453 490 TRP A CA 3899 C C . TRP A 488 ? 0.3242 0.2211 0.4396 0.0493 -0.0329 -0.0438 490 TRP A C 3900 O O . TRP A 488 ? 0.3253 0.1937 0.4263 0.0463 -0.0361 -0.0380 490 TRP A O 3901 C CB . TRP A 488 ? 0.3013 0.2327 0.4295 0.0576 -0.0381 -0.0370 490 TRP A CB 3902 C CG . TRP A 488 ? 0.3132 0.2615 0.4454 0.0423 -0.0308 -0.0335 490 TRP A CG 3903 C CD1 . TRP A 488 ? 0.2642 0.2169 0.4000 0.0303 -0.0228 -0.0353 490 TRP A CD1 3904 C CD2 . TRP A 488 ? 0.2799 0.2404 0.4125 0.0384 -0.0328 -0.0285 490 TRP A CD2 3905 N NE1 . TRP A 488 ? 0.2707 0.2380 0.4103 0.0207 -0.0183 -0.0316 490 TRP A NE1 3906 C CE2 . TRP A 488 ? 0.2500 0.2211 0.3855 0.0248 -0.0235 -0.0275 490 TRP A CE2 3907 C CE3 . TRP A 488 ? 0.2656 0.2259 0.3951 0.0456 -0.0439 -0.0252 490 TRP A CE3 3908 C CZ2 . TRP A 488 ? 0.2249 0.2041 0.3574 0.0182 -0.0226 -0.0234 490 TRP A CZ2 3909 C CZ3 . TRP A 488 ? 0.2702 0.2379 0.3955 0.0380 -0.0452 -0.0212 490 TRP A CZ3 3910 C CH2 . TRP A 488 ? 0.2992 0.2755 0.4246 0.0243 -0.0333 -0.0203 490 TRP A CH2 3911 N N . PRO A 489 ? 0.3206 0.2216 0.4397 0.0426 -0.0294 -0.0494 491 PRO A N 3912 C CA . PRO A 489 ? 0.3438 0.2218 0.4589 0.0304 -0.0312 -0.0497 491 PRO A CA 3913 C C . PRO A 489 ? 0.3381 0.2229 0.4634 0.0141 -0.0256 -0.0424 491 PRO A C 3914 O O . PRO A 489 ? 0.3158 0.2248 0.4482 0.0126 -0.0211 -0.0397 491 PRO A O 3915 C CB . PRO A 489 ? 0.3481 0.2312 0.4635 0.0310 -0.0328 -0.0589 491 PRO A CB 3916 C CG . PRO A 489 ? 0.3507 0.2672 0.4744 0.0336 -0.0263 -0.0589 491 PRO A CG 3917 C CD . PRO A 489 ? 0.3098 0.2384 0.4381 0.0434 -0.0242 -0.0546 491 PRO A CD 3918 N N . VAL A 490 ? 0.3543 0.2164 0.4804 0.0023 -0.0243 -0.0392 492 VAL A N 3919 C CA . VAL A 490 ? 0.3554 0.2245 0.4961 -0.0129 -0.0152 -0.0341 492 VAL A CA 3920 C C . VAL A 490 ? 0.3559 0.2498 0.5193 -0.0182 -0.0175 -0.0400 492 VAL A C 3921 O O . VAL A 490 ? 0.3601 0.2520 0.5240 -0.0147 -0.0275 -0.0479 492 VAL A O 3922 C CB . VAL A 490 ? 0.3928 0.2322 0.5332 -0.0258 -0.0091 -0.0292 492 VAL A CB 3923 C CG1 . VAL A 490 ? 0.4048 0.2083 0.5136 -0.0181 -0.0117 -0.0242 492 VAL A CG1 3924 C CG2 . VAL A 490 ? 0.4320 0.2655 0.5931 -0.0353 -0.0150 -0.0355 492 VAL A CG2 3925 N N . PHE A 491 ? 0.3418 0.2549 0.5184 -0.0248 -0.0091 -0.0364 493 PHE A N 3926 C CA . PHE A 491 ? 0.3517 0.2857 0.5511 -0.0300 -0.0117 -0.0408 493 PHE A CA 3927 C C . PHE A 491 ? 0.3905 0.3183 0.6181 -0.0431 -0.0111 -0.0422 493 PHE A C 3928 O O . PHE A 491 ? 0.4030 0.3258 0.6408 -0.0525 0.0028 -0.0367 493 PHE A O 3929 C CB . PHE A 491 ? 0.3039 0.2577 0.5064 -0.0311 -0.0023 -0.0366 493 PHE A CB 3930 C CG . PHE A 491 ? 0.2888 0.2621 0.5128 -0.0345 -0.0056 -0.0406 493 PHE A CG 3931 C CD1 . PHE A 491 ? 0.3504 0.3283 0.6060 -0.0443 -0.0020 -0.0415 493 PHE A CD1 3932 C CD2 . PHE A 491 ? 0.2801 0.2666 0.4940 -0.0279 -0.0109 -0.0429 493 PHE A CD2 3933 C CE1 . PHE A 491 ? 0.3045 0.2997 0.5820 -0.0451 -0.0074 -0.0454 493 PHE A CE1 3934 C CE2 . PHE A 491 ? 0.2816 0.2807 0.5095 -0.0301 -0.0149 -0.0456 493 PHE A CE2 3935 C CZ . PHE A 491 ? 0.2989 0.3021 0.5586 -0.0376 -0.0147 -0.0470 493 PHE A CZ 3936 N N . LYS A 492 ? 0.4173 0.3431 0.6568 -0.0442 -0.0261 -0.0499 494 LYS A N 3937 C CA . LYS A 492 ? 0.4677 0.3907 0.7418 -0.0570 -0.0299 -0.0528 494 LYS A CA 3938 C C . LYS A 492 ? 0.4663 0.4103 0.7665 -0.0578 -0.0409 -0.0584 494 LYS A C 3939 O O . LYS A 492 ? 0.4564 0.4061 0.7365 -0.0482 -0.0493 -0.0611 494 LYS A O 3940 C CB . LYS A 492 ? 0.5084 0.4036 0.7723 -0.0578 -0.0432 -0.0576 494 LYS A CB 3941 C CG . LYS A 492 ? 0.5914 0.4640 0.8513 -0.0654 -0.0313 -0.0516 494 LYS A CG 3942 C CD . LYS A 492 ? 0.7390 0.5780 0.9760 -0.0625 -0.0433 -0.0554 494 LYS A CD 3943 C CE . LYS A 492 ? 0.8336 0.6479 1.0754 -0.0758 -0.0311 -0.0487 494 LYS A CE 3944 N NZ . LYS A 492 ? 0.8718 0.6482 1.0746 -0.0685 -0.0339 -0.0468 494 LYS A NZ 3945 N N . SER A 493 ? 0.4858 0.4417 0.8315 -0.0690 -0.0389 -0.0596 495 SER A N 3946 C CA . SER A 493 ? 0.5141 0.4830 0.8915 -0.0700 -0.0581 -0.0672 495 SER A CA 3947 C C . SER A 493 ? 0.5341 0.4798 0.8900 -0.0661 -0.0843 -0.0749 495 SER A C 3948 O O . SER A 493 ? 0.5855 0.5081 0.9289 -0.0694 -0.0871 -0.0759 495 SER A O 3949 C CB . SER A 493 ? 0.5339 0.5155 0.9748 -0.0845 -0.0553 -0.0694 495 SER A CB 3950 O OG . SER A 493 ? 0.5702 0.5790 1.0439 -0.0844 -0.0437 -0.0683 495 SER A OG 3951 N N . THR A 494 ? 0.5075 0.4543 0.8571 -0.0595 -0.1041 -0.0805 496 THR A N 3952 C CA . THR A 494 ? 0.5421 0.4607 0.8609 -0.0545 -0.1296 -0.0885 496 THR A CA 3953 C C . THR A 494 ? 0.5113 0.4176 0.7712 -0.0416 -0.1217 -0.0866 496 THR A C 3954 O O . THR A 494 ? 0.5130 0.4212 0.7523 -0.0346 -0.1266 -0.0873 496 THR A O 3955 C CB . THR A 494 ? 0.5827 0.4779 0.9171 -0.0640 -0.1470 -0.0950 496 THR A CB 3956 O OG1 . THR A 494 ? 0.6591 0.5326 0.9610 -0.0624 -0.1357 -0.0926 496 THR A OG1 3957 C CG2 . THR A 494 ? 0.5848 0.5013 0.9903 -0.0798 -0.1446 -0.0948 496 THR A CG2 3958 N N . GLU A 495 ? 0.4827 0.3792 0.7189 -0.0384 -0.1073 -0.0834 497 GLU A N 3959 C CA . GLU A 495 ? 0.4703 0.3588 0.6590 -0.0255 -0.1003 -0.0833 497 GLU A CA 3960 C C . GLU A 495 ? 0.4126 0.3266 0.5975 -0.0212 -0.0820 -0.0763 497 GLU A C 3961 O O . GLU A 495 ? 0.4011 0.3141 0.5581 -0.0138 -0.0807 -0.0774 497 GLU A O 3962 C CB . GLU A 495 ? 0.5065 0.3731 0.6706 -0.0202 -0.0957 -0.0847 497 GLU A CB 3963 C CG . GLU A 495 ? 0.6274 0.4607 0.7804 -0.0221 -0.1162 -0.0934 497 GLU A CG 3964 C CD . GLU A 495 ? 0.8040 0.6125 0.9290 -0.0146 -0.1106 -0.0953 497 GLU A CD 3965 O OE1 . GLU A 495 ? 0.8684 0.6528 0.9519 -0.0032 -0.1142 -0.1021 497 GLU A OE1 3966 O OE2 . GLU A 495 ? 0.8755 0.6864 1.0176 -0.0193 -0.1009 -0.0896 497 GLU A OE2 3967 N N . GLN A 496 ? 0.3608 0.2942 0.5713 -0.0267 -0.0677 -0.0693 498 GLN A N 3968 C CA . GLN A 496 ? 0.3250 0.2801 0.5334 -0.0242 -0.0532 -0.0631 498 GLN A CA 3969 C C . GLN A 496 ? 0.3159 0.2702 0.4925 -0.0140 -0.0451 -0.0620 498 GLN A C 3970 O O . GLN A 496 ? 0.3019 0.2665 0.4665 -0.0105 -0.0414 -0.0614 498 GLN A O 3971 C CB . GLN A 496 ? 0.3343 0.3008 0.5539 -0.0259 -0.0605 -0.0645 498 GLN A CB 3972 C CG . GLN A 496 ? 0.3559 0.3317 0.6194 -0.0346 -0.0662 -0.0657 498 GLN A CG 3973 C CD . GLN A 496 ? 0.4242 0.4020 0.6969 -0.0331 -0.0841 -0.0704 498 GLN A CD 3974 O OE1 . GLN A 496 ? 0.5431 0.5126 0.8351 -0.0358 -0.1041 -0.0766 498 GLN A OE1 3975 N NE2 . GLN A 496 ? 0.3348 0.3203 0.5929 -0.0288 -0.0794 -0.0676 498 GLN A NE2 3976 N N . LYS A 497 ? 0.3247 0.2669 0.4904 -0.0093 -0.0419 -0.0621 499 LYS A N 3977 C CA . LYS A 497 ? 0.3134 0.2594 0.4592 0.0016 -0.0337 -0.0619 499 LYS A CA 3978 C C . LYS A 497 ? 0.2866 0.2541 0.4410 0.0014 -0.0232 -0.0546 499 LYS A C 3979 O O . LYS A 497 ? 0.2902 0.2585 0.4564 -0.0049 -0.0199 -0.0490 499 LYS A O 3980 C CB . LYS A 497 ? 0.3070 0.2324 0.4410 0.0089 -0.0352 -0.0647 499 LYS A CB 3981 C CG . LYS A 497 ? 0.3509 0.2509 0.4686 0.0105 -0.0465 -0.0733 499 LYS A CG 3982 C CD . LYS A 497 ? 0.3629 0.2370 0.4656 0.0187 -0.0485 -0.0771 499 LYS A CD 3983 C CE . LYS A 497 ? 0.3827 0.2227 0.4681 0.0169 -0.0641 -0.0862 499 LYS A CE 3984 N NZ . LYS A 497 ? 0.4497 0.2656 0.5191 0.0267 -0.0630 -0.0893 499 LYS A NZ 3985 N N . TYR A 498 ? 0.2597 0.2423 0.4072 0.0069 -0.0173 -0.0548 500 TYR A N 3986 C CA . TYR A 498 ? 0.2519 0.2520 0.4069 0.0073 -0.0111 -0.0489 500 TYR A CA 3987 C C . TYR A 498 ? 0.2581 0.2674 0.4109 0.0181 -0.0071 -0.0512 500 TYR A C 3988 O O . TYR A 498 ? 0.2719 0.2770 0.4158 0.0241 -0.0044 -0.0572 500 TYR A O 3989 C CB . TYR A 498 ? 0.2192 0.2345 0.3796 -0.0002 -0.0083 -0.0458 500 TYR A CB 3990 C CG . TYR A 498 ? 0.2609 0.2817 0.4122 0.0001 -0.0067 -0.0495 500 TYR A CG 3991 C CD1 . TYR A 498 ? 0.2415 0.2476 0.3828 -0.0018 -0.0134 -0.0538 500 TYR A CD1 3992 C CD2 . TYR A 498 ? 0.1670 0.2045 0.3185 0.0012 0.0006 -0.0484 500 TYR A CD2 3993 C CE1 . TYR A 498 ? 0.2511 0.2540 0.3748 -0.0019 -0.0119 -0.0559 500 TYR A CE1 3994 C CE2 . TYR A 498 ? 0.1725 0.2101 0.3115 -0.0003 0.0052 -0.0507 500 TYR A CE2 3995 C CZ . TYR A 498 ? 0.2445 0.2626 0.3658 -0.0016 -0.0004 -0.0540 500 TYR A CZ 3996 O OH . TYR A 498 ? 0.1924 0.2028 0.2921 -0.0032 0.0045 -0.0554 500 TYR A OH 3997 N N . LEU A 499 ? 0.2385 0.2599 0.3998 0.0205 -0.0067 -0.0468 501 LEU A N 3998 C CA . LEU A 499 ? 0.2413 0.2772 0.4120 0.0311 -0.0045 -0.0495 501 LEU A CA 3999 C C . LEU A 499 ? 0.2258 0.2882 0.4090 0.0259 0.0004 -0.0480 501 LEU A C 4000 O O . LEU A 499 ? 0.2249 0.2909 0.4083 0.0176 -0.0029 -0.0427 501 LEU A O 4001 C CB . LEU A 499 ? 0.2231 0.2504 0.3960 0.0385 -0.0129 -0.0461 501 LEU A CB 4002 C CG . LEU A 499 ? 0.2847 0.3280 0.4757 0.0522 -0.0153 -0.0492 501 LEU A CG 4003 C CD1 . LEU A 499 ? 0.2323 0.2710 0.4240 0.0639 -0.0091 -0.0573 501 LEU A CD1 4004 C CD2 . LEU A 499 ? 0.2464 0.2769 0.4355 0.0595 -0.0286 -0.0449 501 LEU A CD2 4005 N N . THR A 500 ? 0.2334 0.3115 0.4254 0.0298 0.0097 -0.0528 502 THR A N 4006 C CA . THR A 500 ? 0.2258 0.3287 0.4340 0.0239 0.0148 -0.0514 502 THR A CA 4007 C C . THR A 500 ? 0.2305 0.3533 0.4669 0.0312 0.0087 -0.0514 502 THR A C 4008 O O . THR A 500 ? 0.2434 0.3671 0.4908 0.0444 0.0081 -0.0557 502 THR A O 4009 C CB . THR A 500 ? 0.2456 0.3542 0.4494 0.0213 0.0307 -0.0558 502 THR A CB 4010 O OG1 . THR A 500 ? 0.2215 0.3351 0.4351 0.0334 0.0407 -0.0624 502 THR A OG1 4011 C CG2 . THR A 500 ? 0.2234 0.3055 0.3942 0.0155 0.0307 -0.0560 502 THR A CG2 4012 N N . LEU A 501 ? 0.1954 0.3319 0.4431 0.0235 0.0021 -0.0473 503 LEU A N 4013 C CA . LEU A 501 ? 0.1839 0.3378 0.4592 0.0294 -0.0100 -0.0473 503 LEU A CA 4014 C C . LEU A 501 ? 0.1985 0.3834 0.5040 0.0228 -0.0011 -0.0500 503 LEU A C 4015 O O . LEU A 501 ? 0.1710 0.3581 0.4696 0.0090 0.0017 -0.0470 503 LEU A O 4016 C CB . LEU A 501 ? 0.1873 0.3248 0.4455 0.0246 -0.0270 -0.0407 503 LEU A CB 4017 C CG . LEU A 501 ? 0.2055 0.3086 0.4320 0.0283 -0.0324 -0.0369 503 LEU A CG 4018 C CD1 . LEU A 501 ? 0.1093 0.1922 0.3125 0.0221 -0.0435 -0.0303 503 LEU A CD1 4019 C CD2 . LEU A 501 ? 0.2026 0.3022 0.4397 0.0447 -0.0395 -0.0399 503 LEU A CD2 4020 N N . ASN A 502 ? 0.2097 0.4182 0.5508 0.0326 0.0047 -0.0560 504 ASN A N 4021 C CA . ASN A 502 ? 0.2335 0.4734 0.6095 0.0256 0.0179 -0.0592 504 ASN A CA 4022 C C . ASN A 502 ? 0.2489 0.5175 0.6754 0.0393 0.0154 -0.0655 504 ASN A C 4023 O O . ASN A 502 ? 0.2530 0.5130 0.6812 0.0553 0.0040 -0.0674 504 ASN A O 4024 C CB . ASN A 502 ? 0.2206 0.4554 0.5779 0.0181 0.0446 -0.0611 504 ASN A CB 4025 C CG . ASN A 502 ? 0.3022 0.5253 0.6480 0.0315 0.0588 -0.0670 504 ASN A CG 4026 O OD1 . ASN A 502 ? 0.3324 0.5763 0.7121 0.0420 0.0699 -0.0737 504 ASN A OD1 4027 N ND2 . ASN A 502 ? 0.3175 0.5060 0.6161 0.0314 0.0591 -0.0657 504 ASN A ND2 4028 N N . THR A 503 ? 0.2615 0.5639 0.7314 0.0327 0.0265 -0.0689 505 THR A N 4029 C CA . THR A 503 ? 0.3012 0.6378 0.8314 0.0435 0.0204 -0.0749 505 THR A CA 4030 C C . THR A 503 ? 0.3599 0.7050 0.9058 0.0579 0.0461 -0.0831 505 THR A C 4031 O O . THR A 503 ? 0.3785 0.7436 0.9682 0.0756 0.0406 -0.0897 505 THR A O 4032 C CB . THR A 503 ? 0.2845 0.6530 0.8561 0.0267 0.0216 -0.0747 505 THR A CB 4033 O OG1 . THR A 503 ? 0.2852 0.6673 0.8900 0.0303 -0.0116 -0.0745 505 THR A OG1 4034 C CG2 . THR A 503 ? 0.2405 0.6412 0.8549 0.0232 0.0548 -0.0812 505 THR A CG2 4035 N N . GLU A 504 ? 0.3929 0.7184 0.8994 0.0522 0.0727 -0.0834 506 GLU A N 4036 C CA A GLU A 504 ? 0.4369 0.7655 0.9505 0.0636 0.1018 -0.0918 506 GLU A CA 4037 C CA B GLU A 504 ? 0.4317 0.7619 0.9483 0.0644 0.1009 -0.0921 506 GLU A CA 4038 C C . GLU A 504 ? 0.4630 0.7584 0.9407 0.0819 0.0953 -0.0944 506 GLU A C 4039 O O . GLU A 504 ? 0.4850 0.7905 0.9934 0.1018 0.0921 -0.1012 506 GLU A O 4040 C CB A GLU A 504 ? 0.4549 0.7705 0.9352 0.0485 0.1327 -0.0910 506 GLU A CB 4041 C CB B GLU A 504 ? 0.4449 0.7729 0.9449 0.0504 0.1363 -0.0931 506 GLU A CB 4042 C CG A GLU A 504 ? 0.4504 0.7658 0.9186 0.0255 0.1278 -0.0828 506 GLU A CG 4043 C CG B GLU A 504 ? 0.4326 0.8052 0.9949 0.0397 0.1549 -0.0959 506 GLU A CG 4044 C CD A GLU A 504 ? 0.4996 0.7816 0.9098 0.0142 0.1485 -0.0802 506 GLU A CD 4045 C CD B GLU A 504 ? 0.4136 0.8307 1.0553 0.0529 0.1411 -0.1020 506 GLU A CD 4046 O OE1 A GLU A 504 ? 0.5071 0.7508 0.8626 0.0180 0.1390 -0.0779 506 GLU A OE1 4047 O OE1 B GLU A 504 ? 0.4090 0.8503 1.0945 0.0660 0.1638 -0.1114 506 GLU A OE1 4048 O OE2 A GLU A 504 ? 0.5022 0.7950 0.9225 0.0014 0.1735 -0.0805 506 GLU A OE2 4049 O OE2 B GLU A 504 ? 0.3716 0.7972 1.0307 0.0512 0.1065 -0.0977 506 GLU A OE2 4050 N N . SER A 505 ? 0.4679 0.7234 0.8834 0.0753 0.0925 -0.0896 507 SER A N 4051 C CA . SER A 505 ? 0.5009 0.7212 0.8797 0.0892 0.0868 -0.0921 507 SER A CA 4052 C C . SER A 505 ? 0.4701 0.6566 0.7985 0.0780 0.0713 -0.0843 507 SER A C 4053 O O . SER A 505 ? 0.4673 0.6434 0.7684 0.0638 0.0795 -0.0811 507 SER A O 4054 C CB . SER A 505 ? 0.5533 0.7580 0.9116 0.0975 0.1155 -0.1009 507 SER A CB 4055 O OG . SER A 505 ? 0.6235 0.8078 0.9382 0.0819 0.1310 -0.0984 507 SER A OG 4056 N N . THR A 506 ? 0.4376 0.6093 0.7596 0.0848 0.0485 -0.0811 508 THR A N 4057 C CA . THR A 506 ? 0.4385 0.5770 0.7203 0.0791 0.0346 -0.0754 508 THR A CA 4058 C C . THR A 506 ? 0.4376 0.5444 0.6794 0.0795 0.0444 -0.0794 508 THR A C 4059 O O . THR A 506 ? 0.4537 0.5489 0.6907 0.0930 0.0522 -0.0868 508 THR A O 4060 C CB . THR A 506 ? 0.4518 0.5801 0.7400 0.0917 0.0155 -0.0742 508 THR A CB 4061 O OG1 . THR A 506 ? 0.5181 0.6717 0.8389 0.0912 0.0030 -0.0710 508 THR A OG1 4062 C CG2 . THR A 506 ? 0.4595 0.5554 0.7136 0.0858 0.0022 -0.0679 508 THR A CG2 4063 N N . ARG A 507 ? 0.3956 0.4861 0.6084 0.0654 0.0422 -0.0750 509 ARG A N 4064 C CA . ARG A 507 ? 0.3936 0.4519 0.5688 0.0650 0.0455 -0.0788 509 ARG A CA 4065 C C . ARG A 507 ? 0.3727 0.4089 0.5296 0.0573 0.0288 -0.0739 509 ARG A C 4066 O O . ARG A 507 ? 0.3526 0.3982 0.5180 0.0473 0.0205 -0.0667 509 ARG A O 4067 C CB . ARG A 507 ? 0.4065 0.4631 0.5634 0.0563 0.0603 -0.0800 509 ARG A CB 4068 C CG . ARG A 507 ? 0.4591 0.5262 0.6243 0.0649 0.0833 -0.0872 509 ARG A CG 4069 C CD . ARG A 507 ? 0.5832 0.6574 0.7404 0.0530 0.1001 -0.0855 509 ARG A CD 4070 N NE . ARG A 507 ? 0.7391 0.8271 0.9097 0.0589 0.1285 -0.0920 509 ARG A NE 4071 C CZ . ARG A 507 ? 0.7889 0.8683 0.9572 0.0745 0.1428 -0.1011 509 ARG A CZ 4072 N NH1 . ARG A 507 ? 0.7874 0.8408 0.9371 0.0867 0.1297 -0.1052 509 ARG A NH1 4073 N NH2 . ARG A 507 ? 0.8399 0.9362 1.0261 0.0776 0.1725 -0.1065 509 ARG A NH2 4074 N N . ILE A 508 ? 0.3697 0.3750 0.5024 0.0617 0.0243 -0.0784 510 ILE A N 4075 C CA A ILE A 508 ? 0.3475 0.3318 0.4659 0.0519 0.0104 -0.0752 510 ILE A CA 4076 C CA B ILE A 508 ? 0.3460 0.3303 0.4645 0.0520 0.0104 -0.0752 510 ILE A CA 4077 C C . ILE A 508 ? 0.3549 0.3274 0.4502 0.0437 0.0115 -0.0772 510 ILE A C 4078 O O . ILE A 508 ? 0.3736 0.3267 0.4425 0.0490 0.0179 -0.0842 510 ILE A O 4079 C CB A ILE A 508 ? 0.3681 0.3228 0.4747 0.0582 0.0011 -0.0788 510 ILE A CB 4080 C CB B ILE A 508 ? 0.3657 0.3201 0.4721 0.0583 0.0011 -0.0789 510 ILE A CB 4081 C CG1 A ILE A 508 ? 0.3449 0.3052 0.4691 0.0670 -0.0022 -0.0758 510 ILE A CG1 4082 C CG1 B ILE A 508 ? 0.3381 0.2971 0.4614 0.0681 -0.0018 -0.0765 510 ILE A CG1 4083 C CG2 A ILE A 508 ? 0.3579 0.2949 0.4584 0.0456 -0.0120 -0.0759 510 ILE A CG2 4084 C CG2 B ILE A 508 ? 0.3552 0.2924 0.4562 0.0458 -0.0120 -0.0758 510 ILE A CG2 4085 C CD1 A ILE A 508 ? 0.3152 0.2973 0.4586 0.0596 -0.0054 -0.0668 510 ILE A CD1 4086 C CD1 B ILE A 508 ? 0.3511 0.2787 0.4591 0.0795 -0.0064 -0.0824 510 ILE A CD1 4087 N N . MET A 509 ? 0.3301 0.3096 0.4315 0.0318 0.0045 -0.0715 511 MET A N 4088 C CA A MET A 509 ? 0.3374 0.3046 0.4195 0.0244 0.0005 -0.0723 511 MET A CA 4089 C CA B MET A 509 ? 0.3425 0.3074 0.4229 0.0250 0.0001 -0.0728 511 MET A CA 4090 C C . MET A 509 ? 0.3308 0.2868 0.4192 0.0166 -0.0164 -0.0707 511 MET A C 4091 O O . MET A 509 ? 0.3313 0.2910 0.4393 0.0148 -0.0207 -0.0678 511 MET A O 4092 C CB A MET A 509 ? 0.3265 0.3158 0.4156 0.0180 0.0093 -0.0674 511 MET A CB 4093 C CB B MET A 509 ? 0.3434 0.3265 0.4248 0.0196 0.0104 -0.0692 511 MET A CB 4094 C CG A MET A 509 ? 0.3130 0.3185 0.4055 0.0231 0.0277 -0.0690 511 MET A CG 4095 C CG B MET A 509 ? 0.3443 0.3382 0.4245 0.0263 0.0292 -0.0722 511 MET A CG 4096 S SD A MET A 509 ? 0.3899 0.3668 0.4431 0.0308 0.0409 -0.0777 511 MET A SD 4097 S SD B MET A 509 ? 0.3874 0.3996 0.4693 0.0172 0.0431 -0.0679 511 MET A SD 4098 C CE A MET A 509 ? 0.3780 0.3436 0.4025 0.0196 0.0457 -0.0745 511 MET A CE 4099 C CE B MET A 509 ? 0.3584 0.3317 0.3927 0.0121 0.0361 -0.0694 511 MET A CE 4100 N N . THR A 510 ? 0.3256 0.2670 0.3987 0.0119 -0.0258 -0.0726 512 THR A N 4101 C CA . THR A 510 ? 0.3166 0.2506 0.4040 0.0048 -0.0430 -0.0726 512 THR A CA 4102 C C . THR A 510 ? 0.2899 0.2303 0.3819 -0.0013 -0.0490 -0.0698 512 THR A C 4103 O O . THR A 510 ? 0.2935 0.2254 0.3590 -0.0002 -0.0465 -0.0701 512 THR A O 4104 C CB . THR A 510 ? 0.3592 0.2591 0.4267 0.0070 -0.0593 -0.0806 512 THR A CB 4105 O OG1 . THR A 510 ? 0.4045 0.2800 0.4286 0.0125 -0.0587 -0.0855 512 THR A OG1 4106 C CG2 . THR A 510 ? 0.3519 0.2433 0.4213 0.0121 -0.0558 -0.0830 512 THR A CG2 4107 N N . LYS A 511 ? 0.2553 0.2091 0.3803 -0.0076 -0.0544 -0.0668 513 LYS A N 4108 C CA . LYS A 511 ? 0.2702 0.2266 0.4053 -0.0116 -0.0644 -0.0661 513 LYS A CA 4109 C C . LYS A 511 ? 0.2787 0.2446 0.4010 -0.0117 -0.0542 -0.0617 513 LYS A C 4110 O O . LYS A 511 ? 0.3149 0.2643 0.4113 -0.0106 -0.0615 -0.0630 513 LYS A O 4111 C CB . LYS A 511 ? 0.3052 0.2332 0.4219 -0.0099 -0.0867 -0.0727 513 LYS A CB 4112 C CG . LYS A 511 ? 0.3637 0.2836 0.5041 -0.0128 -0.1017 -0.0778 513 LYS A CG 4113 C CD . LYS A 511 ? 0.4333 0.3188 0.5498 -0.0106 -0.1278 -0.0858 513 LYS A CD 4114 C CE . LYS A 511 ? 0.4825 0.3638 0.6297 -0.0158 -0.1412 -0.0905 513 LYS A CE 4115 N NZ . LYS A 511 ? 0.6003 0.4531 0.7426 -0.0163 -0.1750 -0.0989 513 LYS A NZ 4116 N N . LEU A 512 ? 0.2610 0.2482 0.3954 -0.0130 -0.0384 -0.0566 514 LEU A N 4117 C CA . LEU A 512 ? 0.2607 0.2596 0.3897 -0.0153 -0.0291 -0.0521 514 LEU A CA 4118 C C . LEU A 512 ? 0.2647 0.2587 0.3969 -0.0180 -0.0388 -0.0516 514 LEU A C 4119 O O . LEU A 512 ? 0.2483 0.2472 0.4077 -0.0192 -0.0456 -0.0524 514 LEU A O 4120 C CB . LEU A 512 ? 0.2186 0.2379 0.3669 -0.0174 -0.0182 -0.0473 514 LEU A CB 4121 C CG . LEU A 512 ? 0.2237 0.2547 0.3691 -0.0210 -0.0104 -0.0431 514 LEU A CG 4122 C CD1 . LEU A 512 ? 0.1936 0.2244 0.3198 -0.0200 -0.0035 -0.0438 514 LEU A CD1 4123 C CD2 . LEU A 512 ? 0.1939 0.2376 0.3521 -0.0221 -0.0039 -0.0392 514 LEU A CD2 4124 N N . ARG A 513 ? 0.2900 0.2727 0.3955 -0.0184 -0.0389 -0.0506 515 ARG A N 4125 C CA . ARG A 513 ? 0.3173 0.2922 0.4217 -0.0195 -0.0485 -0.0496 515 ARG A CA 4126 C C . ARG A 513 ? 0.3333 0.2973 0.4527 -0.0162 -0.0692 -0.0542 515 ARG A C 4127 O O . ARG A 513 ? 0.3387 0.3096 0.4828 -0.0158 -0.0751 -0.0541 515 ARG A O 4128 C CB . ARG A 513 ? 0.2887 0.2831 0.4148 -0.0229 -0.0392 -0.0454 515 ARG A CB 4129 C CG . ARG A 513 ? 0.3071 0.3118 0.4218 -0.0274 -0.0235 -0.0411 515 ARG A CG 4130 C CD . ARG A 513 ? 0.3662 0.3571 0.4517 -0.0315 -0.0211 -0.0384 515 ARG A CD 4131 N NE . ARG A 513 ? 0.3154 0.3216 0.4055 -0.0377 -0.0089 -0.0347 515 ARG A NE 4132 C CZ . ARG A 513 ? 0.4235 0.4448 0.5178 -0.0397 0.0019 -0.0341 515 ARG A CZ 4133 N NH1 . ARG A 513 ? 0.2808 0.3175 0.3848 -0.0456 0.0088 -0.0314 515 ARG A NH1 4134 N NH2 . ARG A 513 ? 0.4237 0.4432 0.5131 -0.0352 0.0044 -0.0372 515 ARG A NH2 4135 N N . ALA A 514 ? 0.3518 0.2986 0.4591 -0.0135 -0.0809 -0.0590 516 ALA A N 4136 C CA . ALA A 514 ? 0.3613 0.3021 0.4935 -0.0117 -0.1030 -0.0643 516 ALA A CA 4137 C C . ALA A 514 ? 0.3821 0.3116 0.5146 -0.0087 -0.1203 -0.0648 516 ALA A C 4138 O O . ALA A 514 ? 0.3418 0.2873 0.5196 -0.0080 -0.1282 -0.0668 516 ALA A O 4139 C CB . ALA A 514 ? 0.3956 0.3097 0.5028 -0.0092 -0.1176 -0.0702 516 ALA A CB 4140 N N . GLN A 515 ? 0.4155 0.3163 0.4979 -0.0067 -0.1246 -0.0632 517 GLN A N 4141 C CA . GLN A 515 ? 0.4605 0.3390 0.5318 -0.0021 -0.1465 -0.0638 517 GLN A CA 4142 C C . GLN A 515 ? 0.4164 0.3162 0.5160 -0.0025 -0.1371 -0.0600 517 GLN A C 4143 O O . GLN A 515 ? 0.4167 0.3191 0.5464 0.0026 -0.1534 -0.0627 517 GLN A O 4144 C CB . GLN A 515 ? 0.5267 0.3627 0.5277 -0.0013 -0.1488 -0.0614 517 GLN A CB 4145 C CG . GLN A 515 ? 0.6374 0.4292 0.5939 0.0031 -0.1723 -0.0666 517 GLN A CG 4146 C CD . GLN A 515 ? 0.7218 0.4656 0.6187 0.0062 -0.1861 -0.0639 517 GLN A CD 4147 O OE1 . GLN A 515 ? 0.7797 0.4835 0.6469 0.0121 -0.2167 -0.0680 517 GLN A OE1 4148 N NE2 . GLN A 515 ? 0.7119 0.4570 0.5906 0.0016 -0.1652 -0.0567 517 GLN A NE2 4149 N N . GLN A 516 ? 0.3778 0.2934 0.4706 -0.0080 -0.1112 -0.0546 518 GLN A N 4150 C CA . GLN A 516 ? 0.3521 0.2839 0.4654 -0.0090 -0.1010 -0.0514 518 GLN A CA 4151 C C . GLN A 516 ? 0.3190 0.2794 0.4894 -0.0073 -0.0984 -0.0544 518 GLN A C 4152 O O . GLN A 516 ? 0.3366 0.3003 0.5303 -0.0029 -0.1034 -0.0558 518 GLN A O 4153 C CB . GLN A 516 ? 0.3538 0.2950 0.4478 -0.0164 -0.0765 -0.0457 518 GLN A CB 4154 C CG . GLN A 516 ? 0.3845 0.2985 0.4256 -0.0200 -0.0735 -0.0423 518 GLN A CG 4155 C CD . GLN A 516 ? 0.4631 0.3730 0.4825 -0.0217 -0.0653 -0.0435 518 GLN A CD 4156 O OE1 . GLN A 516 ? 0.5442 0.4459 0.5338 -0.0269 -0.0508 -0.0404 518 GLN A OE1 4157 N NE2 . GLN A 516 ? 0.4165 0.3303 0.4516 -0.0174 -0.0739 -0.0484 518 GLN A NE2 4158 N N . CYS A 517 ? 0.2972 0.2756 0.4900 -0.0105 -0.0896 -0.0556 519 CYS A N 4159 C CA . CYS A 517 ? 0.2609 0.2644 0.5042 -0.0114 -0.0804 -0.0573 519 CYS A CA 4160 C C . CYS A 517 ? 0.2687 0.2748 0.5539 -0.0068 -0.1003 -0.0639 519 CYS A C 4161 O O . CYS A 517 ? 0.2822 0.3059 0.6113 -0.0052 -0.0938 -0.0660 519 CYS A O 4162 C CB . CYS A 517 ? 0.2206 0.2368 0.4679 -0.0171 -0.0637 -0.0553 519 CYS A CB 4163 S SG . CYS A 517 ? 0.3039 0.3236 0.5187 -0.0210 -0.0426 -0.0486 519 CYS A SG 4164 N N . ARG A 518 ? 0.2826 0.2692 0.5548 -0.0040 -0.1254 -0.0678 520 ARG A N 4165 C CA . ARG A 518 ? 0.2948 0.2819 0.6086 0.0015 -0.1513 -0.0747 520 ARG A CA 4166 C C . ARG A 518 ? 0.2969 0.2841 0.6252 0.0093 -0.1572 -0.0753 520 ARG A C 4167 O O . ARG A 518 ? 0.2796 0.2858 0.6658 0.0131 -0.1627 -0.0805 520 ARG A O 4168 C CB . ARG A 518 ? 0.3501 0.3060 0.6338 0.0047 -0.1825 -0.0787 520 ARG A CB 4169 C CG . ARG A 518 ? 0.4528 0.4079 0.7356 -0.0015 -0.1826 -0.0811 520 ARG A CG 4170 C CD . ARG A 518 ? 0.6002 0.5202 0.8556 0.0018 -0.2172 -0.0872 520 ARG A CD 4171 N NE . ARG A 518 ? 0.7043 0.6030 0.9045 -0.0012 -0.2074 -0.0857 520 ARG A NE 4172 C CZ . ARG A 518 ? 0.7555 0.6164 0.8861 0.0023 -0.2121 -0.0843 520 ARG A CZ 4173 N NH1 . ARG A 518 ? 0.7596 0.6056 0.8485 0.0004 -0.1988 -0.0839 520 ARG A NH1 4174 N NH2 . ARG A 518 ? 0.8140 0.6488 0.9153 0.0081 -0.2295 -0.0835 520 ARG A NH2 4175 N N . PHE A 519 ? 0.3106 0.2758 0.5871 0.0114 -0.1551 -0.0704 521 PHE A N 4176 C CA . PHE A 519 ? 0.3243 0.2828 0.6031 0.0188 -0.1590 -0.0700 521 PHE A CA 4177 C C . PHE A 519 ? 0.3005 0.2893 0.6228 0.0184 -0.1327 -0.0701 521 PHE A C 4178 O O . PHE A 519 ? 0.2940 0.2942 0.6629 0.0265 -0.1380 -0.0752 521 PHE A O 4179 C CB . PHE A 519 ? 0.3327 0.2571 0.5395 0.0176 -0.1579 -0.0633 521 PHE A CB 4180 C CG . PHE A 519 ? 0.3398 0.2560 0.5456 0.0237 -0.1574 -0.0621 521 PHE A CG 4181 C CD1 . PHE A 519 ? 0.2969 0.1930 0.5114 0.0360 -0.1867 -0.0662 521 PHE A CD1 4182 C CD2 . PHE A 519 ? 0.2939 0.2192 0.4901 0.0183 -0.1311 -0.0576 521 PHE A CD2 4183 C CE1 . PHE A 519 ? 0.3563 0.2427 0.5703 0.0430 -0.1861 -0.0656 521 PHE A CE1 4184 C CE2 . PHE A 519 ? 0.3263 0.2401 0.5193 0.0242 -0.1309 -0.0573 521 PHE A CE2 4185 C CZ . PHE A 519 ? 0.2987 0.1934 0.5018 0.0372 -0.1575 -0.0614 521 PHE A CZ 4186 N N . TRP A 520 ? 0.2948 0.2939 0.6002 0.0099 -0.1048 -0.0650 522 TRP A N 4187 C CA . TRP A 520 ? 0.2840 0.3003 0.6119 0.0094 -0.0795 -0.0645 522 TRP A CA 4188 C C . TRP A 520 ? 0.3084 0.3517 0.6985 0.0090 -0.0690 -0.0694 522 TRP A C 4189 O O . TRP A 520 ? 0.3052 0.3605 0.7313 0.0137 -0.0560 -0.0727 522 TRP A O 4190 C CB . TRP A 520 ? 0.2593 0.2746 0.5479 0.0002 -0.0579 -0.0578 522 TRP A CB 4191 C CG . TRP A 520 ? 0.2577 0.2510 0.4961 -0.0009 -0.0610 -0.0533 522 TRP A CG 4192 C CD1 . TRP A 520 ? 0.2761 0.2574 0.4723 -0.0070 -0.0628 -0.0489 522 TRP A CD1 4193 C CD2 . TRP A 520 ? 0.2543 0.2335 0.4807 0.0035 -0.0611 -0.0530 522 TRP A CD2 4194 N NE1 . TRP A 520 ? 0.2816 0.2432 0.4422 -0.0086 -0.0634 -0.0454 522 TRP A NE1 4195 C CE2 . TRP A 520 ? 0.3046 0.2627 0.4804 -0.0023 -0.0637 -0.0477 522 TRP A CE2 4196 C CE3 . TRP A 520 ? 0.2937 0.2745 0.5482 0.0122 -0.0586 -0.0574 522 TRP A CE3 4197 C CZ2 . TRP A 520 ? 0.2839 0.2202 0.4337 -0.0012 -0.0654 -0.0458 522 TRP A CZ2 4198 C CZ3 . TRP A 520 ? 0.2830 0.2406 0.5093 0.0156 -0.0616 -0.0561 522 TRP A CZ3 4199 C CH2 . TRP A 520 ? 0.3169 0.2516 0.4902 0.0081 -0.0657 -0.0500 522 TRP A CH2 4200 N N . THR A 521 ? 0.3375 0.3882 0.7396 0.0031 -0.0734 -0.0701 523 THR A N 4201 C CA . THR A 521 ? 0.3560 0.4299 0.8129 -0.0014 -0.0610 -0.0735 523 THR A CA 4202 C C . THR A 521 ? 0.3688 0.4564 0.8897 0.0045 -0.0799 -0.0819 523 THR A C 4203 O O . THR A 521 ? 0.3716 0.4816 0.9480 0.0035 -0.0624 -0.0855 523 THR A O 4204 C CB . THR A 521 ? 0.3547 0.4278 0.7954 -0.0114 -0.0556 -0.0703 523 THR A CB 4205 O OG1 . THR A 521 ? 0.3505 0.4140 0.7394 -0.0151 -0.0389 -0.0632 523 THR A OG1 4206 C CG2 . THR A 521 ? 0.3748 0.4669 0.8648 -0.0184 -0.0372 -0.0720 523 THR A CG2 4207 N N . SER A 522 ? 0.4021 0.4754 0.9175 0.0110 -0.1150 -0.0854 524 SER A N 4208 C CA . SER A 522 ? 0.4231 0.5113 1.0070 0.0162 -0.1379 -0.0944 524 SER A CA 4209 C C . SER A 522 ? 0.4485 0.5293 1.0431 0.0303 -0.1577 -0.0982 524 SER A C 4210 O O . SER A 522 ? 0.4808 0.5831 1.1470 0.0372 -0.1659 -0.1060 524 SER A O 4211 C CB . SER A 522 ? 0.4476 0.5243 1.0296 0.0126 -0.1697 -0.0978 524 SER A CB 4212 O OG . SER A 522 ? 0.4837 0.5537 1.0267 0.0012 -0.1542 -0.0925 524 SER A OG 4213 N N . PHE A 523 ? 0.4579 0.5074 0.9853 0.0351 -0.1673 -0.0933 525 PHE A N 4214 C CA . PHE A 523 ? 0.4629 0.4999 0.9962 0.0494 -0.1864 -0.0964 525 PHE A CA 4215 C C . PHE A 523 ? 0.4485 0.4898 0.9787 0.0540 -0.1578 -0.0944 525 PHE A C 4216 O O . PHE A 523 ? 0.4445 0.5004 1.0279 0.0650 -0.1573 -0.1007 525 PHE A O 4217 C CB . PHE A 523 ? 0.4966 0.4896 0.9628 0.0543 -0.2187 -0.0935 525 PHE A CB 4218 C CG . PHE A 523 ? 0.5677 0.5424 1.0315 0.0688 -0.2354 -0.0953 525 PHE A CG 4219 C CD1 . PHE A 523 ? 0.6227 0.6099 1.1552 0.0825 -0.2623 -0.1047 525 PHE A CD1 4220 C CD2 . PHE A 523 ? 0.5903 0.5403 0.9953 0.0692 -0.2223 -0.0885 525 PHE A CD2 4221 C CE1 . PHE A 523 ? 0.6469 0.6174 1.1822 0.0983 -0.2782 -0.1071 525 PHE A CE1 4222 C CE2 . PHE A 523 ? 0.6339 0.5636 1.0360 0.0832 -0.2372 -0.0902 525 PHE A CE2 4223 C CZ . PHE A 523 ? 0.6709 0.6099 1.1357 0.0986 -0.2646 -0.0993 525 PHE A CZ 4224 N N . PHE A 524 ? 0.4270 0.4546 0.8967 0.0463 -0.1352 -0.0863 526 PHE A N 4225 C CA . PHE A 524 ? 0.4046 0.4274 0.8618 0.0509 -0.1141 -0.0849 526 PHE A CA 4226 C C . PHE A 524 ? 0.3859 0.4376 0.9071 0.0557 -0.0882 -0.0911 526 PHE A C 4227 O O . PHE A 524 ? 0.3967 0.4423 0.9287 0.0675 -0.0859 -0.0947 526 PHE A O 4228 C CB . PHE A 524 ? 0.3810 0.3890 0.7725 0.0399 -0.0936 -0.0762 526 PHE A CB 4229 C CG . PHE A 524 ? 0.3897 0.3798 0.7526 0.0444 -0.0828 -0.0746 526 PHE A CG 4230 C CD1 . PHE A 524 ? 0.3626 0.3225 0.6959 0.0525 -0.1054 -0.0740 526 PHE A CD1 4231 C CD2 . PHE A 524 ? 0.3209 0.3187 0.6821 0.0405 -0.0516 -0.0738 526 PHE A CD2 4232 C CE1 . PHE A 524 ? 0.3527 0.2931 0.6598 0.0561 -0.0972 -0.0728 526 PHE A CE1 4233 C CE2 . PHE A 524 ? 0.3603 0.3373 0.6917 0.0443 -0.0439 -0.0731 526 PHE A CE2 4234 C CZ . PHE A 524 ? 0.3923 0.3415 0.6984 0.0519 -0.0668 -0.0727 526 PHE A CZ 4235 N N . PRO A 525 ? 0.3647 0.4442 0.9262 0.0469 -0.0670 -0.0925 527 PRO A N 4236 C CA . PRO A 525 ? 0.3614 0.4648 0.9804 0.0505 -0.0378 -0.0982 527 PRO A CA 4237 C C . PRO A 525 ? 0.3842 0.5028 1.0745 0.0664 -0.0543 -0.1084 527 PRO A C 4238 O O . PRO A 525 ? 0.3863 0.5192 1.1174 0.0730 -0.0284 -0.1139 527 PRO A O 4239 C CB . PRO A 525 ? 0.3383 0.4646 0.9898 0.0371 -0.0209 -0.0977 527 PRO A CB 4240 C CG . PRO A 525 ? 0.3550 0.4636 0.9412 0.0257 -0.0280 -0.0891 527 PRO A CG 4241 C CD . PRO A 525 ? 0.3606 0.4462 0.9103 0.0331 -0.0649 -0.0884 527 PRO A CD 4242 N N . LYS A 526 ? 0.3959 0.5095 1.1007 0.0732 -0.0965 -0.1116 528 LYS A N 4243 C CA . LYS A 526 ? 0.4163 0.5437 1.1920 0.0901 -0.1182 -0.1219 528 LYS A CA 4244 C C . LYS A 526 ? 0.4507 0.5520 1.1980 0.1067 -0.1258 -0.1228 528 LYS A C 4245 O O . LYS A 526 ? 0.4602 0.5754 1.2675 0.1226 -0.1260 -0.1317 528 LYS A O 4246 C CB . LYS A 526 ? 0.4231 0.5497 1.2231 0.0922 -0.1653 -0.1256 528 LYS A CB 4247 C CG . LYS A 526 ? 0.4209 0.5729 1.2602 0.0767 -0.1635 -0.1268 528 LYS A CG 4248 C CD . LYS A 526 ? 0.4384 0.5660 1.2468 0.0754 -0.2111 -0.1263 528 LYS A CD 4249 C CE . LYS A 526 ? 0.4051 0.5566 1.2738 0.0660 -0.2244 -0.1319 528 LYS A CE 4250 N NZ . LYS A 526 ? 0.4552 0.5968 1.2727 0.0487 -0.2110 -0.1247 528 LYS A NZ 4251 N N . VAL A 527 ? 0.4681 0.5307 1.1255 0.1028 -0.1321 -0.1139 529 VAL A N 4252 C CA . VAL A 527 ? 0.4947 0.5224 1.1098 0.1157 -0.1445 -0.1129 529 VAL A CA 4253 C C . VAL A 527 ? 0.5063 0.5407 1.1439 0.1252 -0.1121 -0.1178 529 VAL A C 4254 O O . VAL A 527 ? 0.4881 0.5461 1.1470 0.1171 -0.0736 -0.1187 529 VAL A O 4255 C CB . VAL A 527 ? 0.5086 0.4997 1.0267 0.1031 -0.1464 -0.1015 529 VAL A CB 4256 C CG1 . VAL A 527 ? 0.4949 0.4639 0.9627 0.1023 -0.1216 -0.0975 529 VAL A CG1 4257 C CG2 . VAL A 527 ? 0.5265 0.4850 1.0069 0.1067 -0.1891 -0.0989 529 VAL A CG2 4258 O OXT . VAL A 527 ? 0.5320 0.5454 1.1646 0.1413 -0.1221 -0.1214 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 ASP 1 3 3 ASP ASP A . n A 1 2 ILE 2 4 4 ILE ILE A . n A 1 3 ILE 3 5 5 ILE ILE A . n A 1 4 ILE 4 6 6 ILE ILE A . n A 1 5 ALA 5 7 7 ALA ALA A . n A 1 6 THR 6 8 8 THR THR A . n A 1 7 LYS 7 9 9 LYS LYS A . n A 1 8 ASN 8 10 10 ASN ASN A . n A 1 9 GLY 9 11 11 GLY GLY A . n A 1 10 LYS 10 12 12 LYS LYS A . n A 1 11 VAL 11 13 13 VAL VAL A . n A 1 12 ARG 12 14 14 ARG ARG A . n A 1 13 GLY 13 15 15 GLY GLY A . n A 1 14 MET 14 16 16 MET MET A . n A 1 15 GLN 15 17 17 GLN GLN A . n A 1 16 LEU 16 18 18 LEU LEU A . n A 1 17 THR 17 19 19 THR THR A . n A 1 18 VAL 18 20 20 VAL VAL A . n A 1 19 PHE 19 21 21 PHE PHE A . n A 1 20 GLY 20 22 22 GLY GLY A . n A 1 21 GLY 21 23 23 GLY GLY A . n A 1 22 THR 22 24 24 THR THR A . n A 1 23 VAL 23 25 25 VAL VAL A . n A 1 24 THR 24 26 26 THR THR A . n A 1 25 ALA 25 27 27 ALA ALA A . n A 1 26 PHE 26 28 28 PHE PHE A . n A 1 27 LEU 27 29 29 LEU LEU A . n A 1 28 GLY 28 30 30 GLY GLY A . n A 1 29 ILE 29 31 31 ILE ILE A . n A 1 30 PRO 30 32 32 PRO PRO A . n A 1 31 TYR 31 33 33 TYR TYR A . n A 1 32 ALA 32 34 34 ALA ALA A . n A 1 33 GLN 33 35 35 GLN GLN A . n A 1 34 PRO 34 36 36 PRO PRO A . n A 1 35 PRO 35 37 37 PRO PRO A . n A 1 36 LEU 36 38 38 LEU LEU A . n A 1 37 GLY 37 39 39 GLY GLY A . n A 1 38 ARG 38 40 40 ARG ARG A . n A 1 39 LEU 39 41 41 LEU LEU A . n A 1 40 ARG 40 42 42 ARG ARG A . n A 1 41 PHE 41 43 43 PHE PHE A . n A 1 42 LYS 42 44 44 LYS LYS A . n A 1 43 LYS 43 45 45 LYS LYS A . n A 1 44 PRO 44 46 46 PRO PRO A . n A 1 45 GLN 45 47 47 GLN GLN A . n A 1 46 SER 46 48 48 SER SER A . n A 1 47 LEU 47 49 49 LEU LEU A . n A 1 48 THR 48 50 50 THR THR A . n A 1 49 LYS 49 51 51 LYS LYS A . n A 1 50 TRP 50 52 52 TRP TRP A . n A 1 51 SER 51 53 53 SER SER A . n A 1 52 ASP 52 54 54 ASP ASP A . n A 1 53 ILE 53 55 55 ILE ILE A . n A 1 54 TRP 54 56 56 TRP TRP A . n A 1 55 ASN 55 57 57 ASN ASN A . n A 1 56 ALA 56 58 58 ALA ALA A . n A 1 57 THR 57 59 59 THR THR A . n A 1 58 LYS 58 60 60 LYS LYS A . n A 1 59 TYR 59 61 61 TYR TYR A . n A 1 60 ALA 60 62 62 ALA ALA A . n A 1 61 ASN 61 63 63 ASN ASN A . n A 1 62 SER 62 64 64 SER SER A . n A 1 63 CYS 63 65 65 CYS CYS A . n A 1 64 CYS 64 66 66 CYS CYS A . n A 1 65 GLN 65 67 67 GLN GLN A . n A 1 66 ASN 66 68 68 ASN ASN A . n A 1 67 ILE 67 69 69 ILE ILE A . n A 1 68 ASP 68 70 70 ASP ASP A . n A 1 69 GLN 69 71 71 GLN GLN A . n A 1 70 SER 70 72 72 SER SER A . n A 1 71 PHE 71 73 73 PHE PHE A . n A 1 72 PRO 72 74 74 PRO PRO A . n A 1 73 GLY 73 75 75 GLY GLY A . n A 1 74 PHE 74 76 76 PHE PHE A . n A 1 75 HIS 75 77 77 HIS HIS A . n A 1 76 GLY 76 78 78 GLY GLY A . n A 1 77 SER 77 79 79 SER SER A . n A 1 78 GLU 78 80 80 GLU GLU A . n A 1 79 MET 79 81 81 MET MET A . n A 1 80 TRP 80 82 82 TRP TRP A . n A 1 81 ASN 81 83 83 ASN ASN A . n A 1 82 PRO 82 84 84 PRO PRO A . n A 1 83 ASN 83 85 85 ASN ASN A . n A 1 84 THR 84 86 86 THR THR A . n A 1 85 ASP 85 87 87 ASP ASP A . n A 1 86 LEU 86 88 88 LEU LEU A . n A 1 87 SER 87 89 89 SER SER A . n A 1 88 GLU 88 90 90 GLU GLU A . n A 1 89 ASP 89 91 91 ASP ASP A . n A 1 90 CYS 90 92 92 CYS CYS A . n A 1 91 LEU 91 93 93 LEU LEU A . n A 1 92 TYR 92 94 94 TYR TYR A . n A 1 93 LEU 93 95 95 LEU LEU A . n A 1 94 ASN 94 96 96 ASN ASN A . n A 1 95 VAL 95 97 97 VAL VAL A . n A 1 96 TRP 96 98 98 TRP TRP A . n A 1 97 ILE 97 99 99 ILE ILE A . n A 1 98 PRO 98 100 100 PRO PRO A . n A 1 99 ALA 99 101 101 ALA ALA A . n A 1 100 PRO 100 102 102 PRO PRO A . n A 1 101 LYS 101 103 103 LYS LYS A . n A 1 102 PRO 102 104 104 PRO PRO A . n A 1 103 LYS 103 105 105 LYS LYS A . n A 1 104 ASN 104 106 106 ASN ASN A . n A 1 105 ALA 105 107 107 ALA ALA A . n A 1 106 THR 106 108 108 THR THR A . n A 1 107 VAL 107 109 109 VAL VAL A . n A 1 108 LEU 108 110 110 LEU LEU A . n A 1 109 ILE 109 111 111 ILE ILE A . n A 1 110 TRP 110 112 112 TRP TRP A . n A 1 111 ILE 111 113 113 ILE ILE A . n A 1 112 TYR 112 114 114 TYR TYR A . n A 1 113 GLY 113 115 115 GLY GLY A . n A 1 114 GLY 114 116 116 GLY GLY A . n A 1 115 GLY 115 117 117 GLY GLY A . n A 1 116 PHE 116 118 118 PHE PHE A . n A 1 117 GLN 117 119 119 GLN GLN A . n A 1 118 THR 118 120 120 THR THR A . n A 1 119 GLY 119 121 121 GLY GLY A . n A 1 120 THR 120 122 122 THR THR A . n A 1 121 SER 121 123 123 SER SER A . n A 1 122 SER 122 124 124 SER SER A . n A 1 123 LEU 123 125 125 LEU LEU A . n A 1 124 HIS 124 126 126 HIS HIS A . n A 1 125 VAL 125 127 127 VAL VAL A . n A 1 126 TYR 126 128 128 TYR TYR A . n A 1 127 ASP 127 129 129 ASP ASP A . n A 1 128 GLY 128 130 130 GLY GLY A . n A 1 129 LYS 129 131 131 LYS LYS A . n A 1 130 PHE 130 132 132 PHE PHE A . n A 1 131 LEU 131 133 133 LEU LEU A . n A 1 132 ALA 132 134 134 ALA ALA A . n A 1 133 ARG 133 135 135 ARG ARG A . n A 1 134 VAL 134 136 136 VAL VAL A . n A 1 135 GLU 135 137 137 GLU GLU A . n A 1 136 ARG 136 138 138 ARG ARG A . n A 1 137 VAL 137 139 139 VAL VAL A . n A 1 138 ILE 138 140 140 ILE ILE A . n A 1 139 VAL 139 141 141 VAL VAL A . n A 1 140 VAL 140 142 142 VAL VAL A . n A 1 141 SER 141 143 143 SER SER A . n A 1 142 MET 142 144 144 MET MET A . n A 1 143 ASN 143 145 145 ASN ASN A . n A 1 144 TYR 144 146 146 TYR TYR A . n A 1 145 ARG 145 147 147 ARG ARG A . n A 1 146 VAL 146 148 148 VAL VAL A . n A 1 147 GLY 147 149 149 GLY GLY A . n A 1 148 ALA 148 150 150 ALA ALA A . n A 1 149 LEU 149 151 151 LEU LEU A . n A 1 150 GLY 150 152 152 GLY GLY A . n A 1 151 PHE 151 153 153 PHE PHE A . n A 1 152 LEU 152 154 154 LEU LEU A . n A 1 153 ALA 153 155 155 ALA ALA A . n A 1 154 LEU 154 156 156 LEU LEU A . n A 1 155 PRO 155 157 157 PRO PRO A . n A 1 156 GLY 156 158 158 GLY GLY A . n A 1 157 ASN 157 159 159 ASN ASN A . n A 1 158 PRO 158 160 160 PRO PRO A . n A 1 159 GLU 159 161 161 GLU GLU A . n A 1 160 ALA 160 162 162 ALA ALA A . n A 1 161 PRO 161 163 163 PRO PRO A . n A 1 162 GLY 162 164 164 GLY GLY A . n A 1 163 ASN 163 165 165 ASN ASN A . n A 1 164 MET 164 166 166 MET MET A . n A 1 165 GLY 165 167 167 GLY GLY A . n A 1 166 LEU 166 168 168 LEU LEU A . n A 1 167 PHE 167 169 169 PHE PHE A . n A 1 168 ASP 168 170 170 ASP ASP A . n A 1 169 GLN 169 171 171 GLN GLN A . n A 1 170 GLN 170 172 172 GLN GLN A . n A 1 171 LEU 171 173 173 LEU LEU A . n A 1 172 ALA 172 174 174 ALA ALA A . n A 1 173 LEU 173 175 175 LEU LEU A . n A 1 174 GLN 174 176 176 GLN GLN A . n A 1 175 TRP 175 177 177 TRP TRP A . n A 1 176 VAL 176 178 178 VAL VAL A . n A 1 177 GLN 177 179 179 GLN GLN A . n A 1 178 LYS 178 180 180 LYS LYS A . n A 1 179 ASN 179 181 181 ASN ASN A . n A 1 180 ILE 180 182 182 ILE ILE A . n A 1 181 ALA 181 183 183 ALA ALA A . n A 1 182 ALA 182 184 184 ALA ALA A . n A 1 183 PHE 183 185 185 PHE PHE A . n A 1 184 GLY 184 186 186 GLY GLY A . n A 1 185 GLY 185 187 187 GLY GLY A . n A 1 186 ASN 186 188 188 ASN ASN A . n A 1 187 PRO 187 189 189 PRO PRO A . n A 1 188 LYS 188 190 190 LYS LYS A . n A 1 189 SER 189 191 191 SER SER A . n A 1 190 VAL 190 192 192 VAL VAL A . n A 1 191 THR 191 193 193 THR THR A . n A 1 192 LEU 192 194 194 LEU LEU A . n A 1 193 PHE 193 195 195 PHE PHE A . n A 1 194 GLY 194 196 196 GLY GLY A . n A 1 195 GLU 195 197 197 GLU GLU A . n A 1 196 SER 196 198 198 SER SER A . n A 1 197 ALA 197 199 199 ALA ALA A . n A 1 198 GLY 198 200 200 GLY GLY A . n A 1 199 ALA 199 201 201 ALA ALA A . n A 1 200 ALA 200 202 202 ALA ALA A . n A 1 201 SER 201 203 203 SER SER A . n A 1 202 VAL 202 204 204 VAL VAL A . n A 1 203 SER 203 205 205 SER SER A . n A 1 204 LEU 204 206 206 LEU LEU A . n A 1 205 HIS 205 207 207 HIS HIS A . n A 1 206 LEU 206 208 208 LEU LEU A . n A 1 207 LEU 207 209 209 LEU LEU A . n A 1 208 SER 208 210 210 SER SER A . n A 1 209 PRO 209 211 211 PRO PRO A . n A 1 210 GLY 210 212 212 GLY GLY A . n A 1 211 SER 211 213 213 SER SER A . n A 1 212 HIS 212 214 214 HIS HIS A . n A 1 213 SER 213 215 215 SER SER A . n A 1 214 LEU 214 216 216 LEU LEU A . n A 1 215 PHE 215 217 217 PHE PHE A . n A 1 216 THR 216 218 218 THR THR A . n A 1 217 ARG 217 219 219 ARG ARG A . n A 1 218 ALA 218 220 220 ALA ALA A . n A 1 219 ILE 219 221 221 ILE ILE A . n A 1 220 LEU 220 222 222 LEU LEU A . n A 1 221 GLN 221 223 223 GLN GLN A . n A 1 222 SER 222 224 224 SER SER A . n A 1 223 GLY 223 225 225 GLY GLY A . n A 1 224 SER 224 226 226 SER SER A . n A 1 225 PHE 225 227 227 PHE PHE A . n A 1 226 ASN 226 228 228 ASN ASN A . n A 1 227 ALA 227 229 229 ALA ALA A . n A 1 228 PRO 228 230 230 PRO PRO A . n A 1 229 TRP 229 231 231 TRP TRP A . n A 1 230 ALA 230 232 232 ALA ALA A . n A 1 231 VAL 231 233 233 VAL VAL A . n A 1 232 THR 232 234 234 THR THR A . n A 1 233 SER 233 235 235 SER SER A . n A 1 234 LEU 234 236 236 LEU LEU A . n A 1 235 TYR 235 237 237 TYR TYR A . n A 1 236 GLU 236 238 238 GLU GLU A . n A 1 237 ALA 237 239 239 ALA ALA A . n A 1 238 ARG 238 240 240 ARG ARG A . n A 1 239 ASN 239 241 241 ASN ASN A . n A 1 240 ARG 240 242 242 ARG ARG A . n A 1 241 THR 241 243 243 THR THR A . n A 1 242 LEU 242 244 244 LEU LEU A . n A 1 243 ASN 243 245 245 ASN ASN A . n A 1 244 LEU 244 246 246 LEU LEU A . n A 1 245 ALA 245 247 247 ALA ALA A . n A 1 246 LYS 246 248 248 LYS LYS A . n A 1 247 LEU 247 249 249 LEU LEU A . n A 1 248 THR 248 250 250 THR THR A . n A 1 249 GLY 249 251 251 GLY GLY A . n A 1 250 CYS 250 252 252 CYS CYS A . n A 1 251 SER 251 253 253 SER SER A . n A 1 252 ARG 252 254 254 ARG ARG A . n A 1 253 GLU 253 255 255 GLU GLU A . n A 1 254 ASN 254 256 256 ASN ASN A . n A 1 255 GLU 255 257 257 GLU GLU A . n A 1 256 THR 256 258 258 THR THR A . n A 1 257 GLU 257 259 259 GLU GLU A . n A 1 258 ILE 258 260 260 ILE ILE A . n A 1 259 ILE 259 261 261 ILE ILE A . n A 1 260 LYS 260 262 262 LYS LYS A . n A 1 261 CYS 261 263 263 CYS CYS A . n A 1 262 LEU 262 264 264 LEU LEU A . n A 1 263 ARG 263 265 265 ARG ARG A . n A 1 264 ASN 264 266 266 ASN ASN A . n A 1 265 LYS 265 267 267 LYS LYS A . n A 1 266 ASP 266 268 268 ASP ASP A . n A 1 267 PRO 267 269 269 PRO PRO A . n A 1 268 GLN 268 270 270 GLN GLN A . n A 1 269 GLU 269 271 271 GLU GLU A . n A 1 270 ILE 270 272 272 ILE ILE A . n A 1 271 LEU 271 273 273 LEU LEU A . n A 1 272 LEU 272 274 274 LEU LEU A . n A 1 273 ASN 273 275 275 ASN ASN A . n A 1 274 GLU 274 276 276 GLU GLU A . n A 1 275 ALA 275 277 277 ALA ALA A . n A 1 276 PHE 276 278 278 PHE PHE A . n A 1 277 VAL 277 279 279 VAL VAL A . n A 1 278 VAL 278 280 280 VAL VAL A . n A 1 279 PRO 279 281 281 PRO PRO A . n A 1 280 TYR 280 282 282 TYR TYR A . n A 1 281 GLY 281 283 283 GLY GLY A . n A 1 282 THR 282 284 284 THR THR A . n A 1 283 PRO 283 285 285 PRO PRO A . n A 1 284 LEU 284 286 286 LEU LEU A . n A 1 285 SER 285 287 287 SER SER A . n A 1 286 VAL 286 288 288 VAL VAL A . n A 1 287 ASN 287 289 289 ASN ASN A . n A 1 288 PHE 288 290 290 PHE PHE A . n A 1 289 GLY 289 291 291 GLY GLY A . n A 1 290 PRO 290 292 292 PRO PRO A . n A 1 291 THR 291 293 293 THR THR A . n A 1 292 VAL 292 294 294 VAL VAL A . n A 1 293 ASP 293 295 295 ASP ASP A . n A 1 294 GLY 294 296 296 GLY GLY A . n A 1 295 ASP 295 297 297 ASP ASP A . n A 1 296 PHE 296 298 298 PHE PHE A . n A 1 297 LEU 297 299 299 LEU LEU A . n A 1 298 THR 298 300 300 THR THR A . n A 1 299 ASP 299 301 301 ASP ASP A . n A 1 300 MET 300 302 302 MET MET A . n A 1 301 PRO 301 303 303 PRO PRO A . n A 1 302 ASP 302 304 304 ASP ASP A . n A 1 303 ILE 303 305 305 ILE ILE A . n A 1 304 LEU 304 306 306 LEU LEU A . n A 1 305 LEU 305 307 307 LEU LEU A . n A 1 306 GLU 306 308 308 GLU GLU A . n A 1 307 LEU 307 309 309 LEU LEU A . n A 1 308 GLY 308 310 310 GLY GLY A . n A 1 309 GLN 309 311 311 GLN GLN A . n A 1 310 PHE 310 312 312 PHE PHE A . n A 1 311 LYS 311 313 313 LYS LYS A . n A 1 312 LYS 312 314 314 LYS LYS A . n A 1 313 THR 313 315 315 THR THR A . n A 1 314 GLN 314 316 316 GLN GLN A . n A 1 315 ILE 315 317 317 ILE ILE A . n A 1 316 LEU 316 318 318 LEU LEU A . n A 1 317 VAL 317 319 319 VAL VAL A . n A 1 318 GLY 318 320 320 GLY GLY A . n A 1 319 VAL 319 321 321 VAL VAL A . n A 1 320 ASN 320 322 322 ASN ASN A . n A 1 321 LYS 321 323 323 LYS LYS A . n A 1 322 ASP 322 324 324 ASP ASP A . n A 1 323 GLU 323 325 325 GLU GLU A . n A 1 324 GLY 324 326 326 GLY GLY A . n A 1 325 THR 325 327 327 THR THR A . n A 1 326 ALA 326 328 328 ALA ALA A . n A 1 327 PHE 327 329 329 PHE PHE A . n A 1 328 LEU 328 330 330 LEU LEU A . n A 1 329 VAL 329 331 331 VAL VAL A . n A 1 330 TYR 330 332 332 TYR TYR A . n A 1 331 GLY 331 333 333 GLY GLY A . n A 1 332 ALA 332 334 334 ALA ALA A . n A 1 333 PRO 333 335 335 PRO PRO A . n A 1 334 GLY 334 336 336 GLY GLY A . n A 1 335 PHE 335 337 337 PHE PHE A . n A 1 336 SER 336 338 338 SER SER A . n A 1 337 LYS 337 339 339 LYS LYS A . n A 1 338 ASP 338 340 340 ASP ASP A . n A 1 339 ASN 339 341 341 ASN ASN A . n A 1 340 ASN 340 342 342 ASN ASN A . n A 1 341 SER 341 343 343 SER SER A . n A 1 342 ILE 342 344 344 ILE ILE A . n A 1 343 ILE 343 345 345 ILE ILE A . n A 1 344 THR 344 346 346 THR THR A . n A 1 345 ARG 345 347 347 ARG ARG A . n A 1 346 LYS 346 348 348 LYS LYS A . n A 1 347 GLU 347 349 349 GLU GLU A . n A 1 348 PHE 348 350 350 PHE PHE A . n A 1 349 GLN 349 351 351 GLN GLN A . n A 1 350 GLU 350 352 352 GLU GLU A . n A 1 351 GLY 351 353 353 GLY GLY A . n A 1 352 LEU 352 354 354 LEU LEU A . n A 1 353 LYS 353 355 355 LYS LYS A . n A 1 354 ILE 354 356 356 ILE ILE A . n A 1 355 PHE 355 357 357 PHE PHE A . n A 1 356 PHE 356 358 358 PHE PHE A . n A 1 357 PRO 357 359 359 PRO PRO A . n A 1 358 GLY 358 360 360 GLY GLY A . n A 1 359 VAL 359 361 361 VAL VAL A . n A 1 360 SER 360 362 362 SER SER A . n A 1 361 GLU 361 363 363 GLU GLU A . n A 1 362 PHE 362 364 364 PHE PHE A . n A 1 363 GLY 363 365 365 GLY GLY A . n A 1 364 LYS 364 366 366 LYS LYS A . n A 1 365 GLU 365 367 367 GLU GLU A . n A 1 366 SER 366 368 368 SER SER A . n A 1 367 ILE 367 369 369 ILE ILE A . n A 1 368 LEU 368 370 370 LEU LEU A . n A 1 369 PHE 369 371 371 PHE PHE A . n A 1 370 HIS 370 372 372 HIS HIS A . n A 1 371 TYR 371 373 373 TYR TYR A . n A 1 372 THR 372 374 374 THR THR A . n A 1 373 ASP 373 375 375 ASP ASP A . n A 1 374 TRP 374 376 376 TRP TRP A . n A 1 375 VAL 375 377 377 VAL VAL A . n A 1 376 ASP 376 378 378 ASP ASP A . n A 1 377 ASP 377 379 379 ASP ASP A . n A 1 378 GLN 378 380 380 GLN GLN A . n A 1 379 ARG 379 381 381 ARG ARG A . n A 1 380 PRO 380 382 382 PRO PRO A . n A 1 381 GLU 381 383 383 GLU GLU A . n A 1 382 ASN 382 384 384 ASN ASN A . n A 1 383 TYR 383 385 385 TYR TYR A . n A 1 384 ARG 384 386 386 ARG ARG A . n A 1 385 GLU 385 387 387 GLU GLU A . n A 1 386 ALA 386 388 388 ALA ALA A . n A 1 387 LEU 387 389 389 LEU LEU A . n A 1 388 GLY 388 390 390 GLY GLY A . n A 1 389 ASP 389 391 391 ASP ASP A . n A 1 390 VAL 390 392 392 VAL VAL A . n A 1 391 VAL 391 393 393 VAL VAL A . n A 1 392 GLY 392 394 394 GLY GLY A . n A 1 393 ASP 393 395 395 ASP ASP A . n A 1 394 TYR 394 396 396 TYR TYR A . n A 1 395 ASN 395 397 397 ASN ASN A . n A 1 396 PHE 396 398 398 PHE PHE A . n A 1 397 ILE 397 399 399 ILE ILE A . n A 1 398 CYS 398 400 400 CYS CYS A . n A 1 399 PRO 399 401 401 PRO PRO A . n A 1 400 ALA 400 402 402 ALA ALA A . n A 1 401 LEU 401 403 403 LEU LEU A . n A 1 402 GLU 402 404 404 GLU GLU A . n A 1 403 PHE 403 405 405 PHE PHE A . n A 1 404 THR 404 406 406 THR THR A . n A 1 405 LYS 405 407 407 LYS LYS A . n A 1 406 LYS 406 408 408 LYS LYS A . n A 1 407 PHE 407 409 409 PHE PHE A . n A 1 408 SER 408 410 410 SER SER A . n A 1 409 GLU 409 411 411 GLU GLU A . n A 1 410 TRP 410 412 412 TRP TRP A . n A 1 411 GLY 411 413 413 GLY GLY A . n A 1 412 ASN 412 414 414 ASN ASN A . n A 1 413 ASN 413 415 415 ASN ASN A . n A 1 414 ALA 414 416 416 ALA ALA A . n A 1 415 PHE 415 417 417 PHE PHE A . n A 1 416 PHE 416 418 418 PHE PHE A . n A 1 417 TYR 417 419 419 TYR TYR A . n A 1 418 TYR 418 420 420 TYR TYR A . n A 1 419 PHE 419 421 421 PHE PHE A . n A 1 420 GLU 420 422 422 GLU GLU A . n A 1 421 HIS 421 423 423 HIS HIS A . n A 1 422 ARG 422 424 424 ARG ARG A . n A 1 423 SER 423 425 425 SER SER A . n A 1 424 SER 424 426 426 SER SER A . n A 1 425 LYS 425 427 427 LYS LYS A . n A 1 426 LEU 426 428 428 LEU LEU A . n A 1 427 PRO 427 429 429 PRO PRO A . n A 1 428 TRP 428 430 430 TRP TRP A . n A 1 429 PRO 429 431 431 PRO PRO A . n A 1 430 GLU 430 432 432 GLU GLU A . n A 1 431 TRP 431 433 433 TRP TRP A . n A 1 432 MET 432 434 434 MET MET A . n A 1 433 GLY 433 435 435 GLY GLY A . n A 1 434 VAL 434 436 436 VAL VAL A . n A 1 435 MET 435 437 437 MET MET A . n A 1 436 HIS 436 438 438 HIS HIS A . n A 1 437 GLY 437 439 439 GLY GLY A . n A 1 438 TYR 438 440 440 TYR TYR A . n A 1 439 GLU 439 441 441 GLU GLU A . n A 1 440 ILE 440 442 442 ILE ILE A . n A 1 441 GLU 441 443 443 GLU GLU A . n A 1 442 PHE 442 444 444 PHE PHE A . n A 1 443 VAL 443 445 445 VAL VAL A . n A 1 444 PHE 444 446 446 PHE PHE A . n A 1 445 GLY 445 447 447 GLY GLY A . n A 1 446 LEU 446 448 448 LEU LEU A . n A 1 447 PRO 447 449 449 PRO PRO A . n A 1 448 LEU 448 450 450 LEU LEU A . n A 1 449 GLU 449 451 451 GLU GLU A . n A 1 450 ARG 450 452 452 ARG ARG A . n A 1 451 ARG 451 453 453 ARG ARG A . n A 1 452 ASP 452 454 454 ASP ASP A . n A 1 453 GLN 453 455 455 GLN GLN A . n A 1 454 TYR 454 456 456 TYR TYR A . n A 1 455 THR 455 457 457 THR THR A . n A 1 456 LYS 456 458 458 LYS LYS A . n A 1 457 ALA 457 459 459 ALA ALA A . n A 1 458 GLU 458 460 460 GLU GLU A . n A 1 459 GLU 459 461 461 GLU GLU A . n A 1 460 ILE 460 462 462 ILE ILE A . n A 1 461 LEU 461 463 463 LEU LEU A . n A 1 462 SER 462 464 464 SER SER A . n A 1 463 ARG 463 465 465 ARG ARG A . n A 1 464 SER 464 466 466 SER SER A . n A 1 465 ILE 465 467 467 ILE ILE A . n A 1 466 VAL 466 468 468 VAL VAL A . n A 1 467 LYS 467 469 469 LYS LYS A . n A 1 468 ARG 468 470 470 ARG ARG A . n A 1 469 TRP 469 471 471 TRP TRP A . n A 1 470 ALA 470 472 472 ALA ALA A . n A 1 471 ASN 471 473 473 ASN ASN A . n A 1 472 PHE 472 474 474 PHE PHE A . n A 1 473 ALA 473 475 475 ALA ALA A . n A 1 474 LYS 474 476 476 LYS LYS A . n A 1 475 TYR 475 477 477 TYR TYR A . n A 1 476 GLY 476 478 478 GLY GLY A . n A 1 477 ASN 477 479 479 ASN ASN A . n A 1 478 PRO 478 480 480 PRO PRO A . n A 1 479 GLN 479 481 481 GLN GLN A . n A 1 480 GLU 480 482 482 GLU GLU A . n A 1 481 THR 481 483 483 THR THR A . n A 1 482 GLN 482 484 484 GLN GLN A . n A 1 483 ASN 483 485 485 ASN ASN A . n A 1 484 GLN 484 486 486 GLN GLN A . n A 1 485 SER 485 487 487 SER SER A . n A 1 486 THR 486 488 488 THR THR A . n A 1 487 SER 487 489 489 SER SER A . n A 1 488 TRP 488 490 490 TRP TRP A . n A 1 489 PRO 489 491 491 PRO PRO A . n A 1 490 VAL 490 492 492 VAL VAL A . n A 1 491 PHE 491 493 493 PHE PHE A . n A 1 492 LYS 492 494 494 LYS LYS A . n A 1 493 SER 493 495 495 SER SER A . n A 1 494 THR 494 496 496 THR THR A . n A 1 495 GLU 495 497 497 GLU GLU A . n A 1 496 GLN 496 498 498 GLN GLN A . n A 1 497 LYS 497 499 499 LYS LYS A . n A 1 498 TYR 498 500 500 TYR TYR A . n A 1 499 LEU 499 501 501 LEU LEU A . n A 1 500 THR 500 502 502 THR THR A . n A 1 501 LEU 501 503 503 LEU LEU A . n A 1 502 ASN 502 504 504 ASN ASN A . n A 1 503 THR 503 505 505 THR THR A . n A 1 504 GLU 504 506 506 GLU GLU A . n A 1 505 SER 505 507 507 SER SER A . n A 1 506 THR 506 508 508 THR THR A . n A 1 507 ARG 507 509 509 ARG ARG A . n A 1 508 ILE 508 510 510 ILE ILE A . n A 1 509 MET 509 511 511 MET MET A . n A 1 510 THR 510 512 512 THR THR A . n A 1 511 LYS 511 513 513 LYS LYS A . n A 1 512 LEU 512 514 514 LEU LEU A . n A 1 513 ARG 513 515 515 ARG ARG A . n A 1 514 ALA 514 516 516 ALA ALA A . n A 1 515 GLN 515 517 517 GLN GLN A . n A 1 516 GLN 516 518 518 GLN GLN A . n A 1 517 CYS 517 519 519 CYS CYS A . n A 1 518 ARG 518 520 520 ARG ARG A . n A 1 519 PHE 519 521 521 PHE PHE A . n A 1 520 TRP 520 522 522 TRP TRP A . n A 1 521 THR 521 523 523 THR THR A . n A 1 522 SER 522 524 524 SER SER A . n A 1 523 PHE 523 525 525 PHE PHE A . n A 1 524 PHE 524 526 526 PHE PHE A . n A 1 525 PRO 525 527 527 PRO PRO A . n A 1 526 LYS 526 528 528 LYS LYS A . n A 1 527 VAL 527 529 529 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 UNX 1 1501 1501 UNX UNX A . C 2 UNX 1 1502 1502 UNX UNX A . D 2 UNX 1 1503 1503 UNX UNX A . E 2 UNX 1 1504 1504 UNX UNX A . F 2 UNX 1 1505 1505 UNX UNX A . G 2 UNX 1 1506 1506 UNX UNX A . H 2 UNX 1 1507 1507 UNX UNX A . I 2 UNX 1 1508 1508 UNX UNX A . J 2 UNX 1 1509 1509 UNX UNX A . K 2 UNX 1 1510 1510 UNX UNX A . L 2 UNX 1 1511 1511 UNX UNX A . M 2 UNX 1 1512 1512 UNX UNX A . N 2 UNX 1 1513 1513 UNX UNX A . O 2 UNX 1 1514 1514 UNX UNX A . P 2 UNX 1 1515 1515 UNX UNX A . Q 2 UNX 1 1516 1516 UNX UNX A . R 2 UNX 1 1517 1517 UNX UNX A . S 2 UNX 1 1518 1518 UNX UNX A . T 2 UNX 1 1519 1519 UNX UNX A . U 2 UNX 1 1520 1520 UNX UNX A . V 2 UNX 1 1521 1521 UNX UNX A . W 2 UNX 1 1522 1522 UNX UNX A . X 2 UNX 1 1523 1523 UNX UNX A . Y 3 VR 1 1530 1530 VR VR A . Z 4 GLY 1 1548 1548 GLY GLY A . AA 5 SO4 1 1549 1549 SO4 SO4 A . BA 5 SO4 1 1550 1550 SO4 SO4 A . CA 6 CA 1 1551 1551 CA CA A . DA 6 CA 1 1552 1552 CA CA A . EA 6 CA 1 1553 1553 CA CA A . FA 7 BR 1 1554 1554 BR BR A . GA 8 NA 1 1555 1555 NA NA A . HA 9 NAG 1 1556 1556 NAG NAG A . IA 9 NAG 2 1557 1557 NAG NAG A . JA 10 FUL 3 1558 1558 FUL FUL A . KA 9 NAG 1 1559 1559 NAG NAG A . LA 9 NAG 1 1560 1560 NAG NAG A . MA 9 NAG 1 1561 1561 NAG NAG A . NA 9 NAG 1 1562 1562 NAG NAG A . OA 9 NAG 1 1563 1563 NAG NAG A . PA 9 NAG 2 1564 1564 NAG NAG A . QA 10 FUL 3 1565 1565 FUL FUL A . RA 11 CL 1 1566 1566 CL CL A . SA 8 NA 1 1567 1567 NA NA A . TA 12 HOH 1 2001 2001 HOH HOH A . TA 12 HOH 2 2002 2002 HOH HOH A . TA 12 HOH 3 2003 2003 HOH HOH A . TA 12 HOH 4 2004 2004 HOH HOH A . TA 12 HOH 5 2005 2005 HOH HOH A . TA 12 HOH 6 2006 2006 HOH HOH A . TA 12 HOH 7 2007 2007 HOH HOH A . TA 12 HOH 8 2008 2008 HOH HOH A . TA 12 HOH 9 2009 2009 HOH HOH A . TA 12 HOH 10 2010 2010 HOH HOH A . TA 12 HOH 11 2011 2011 HOH HOH A . TA 12 HOH 12 2012 2012 HOH HOH A . TA 12 HOH 13 2013 2013 HOH HOH A . TA 12 HOH 14 2014 2014 HOH HOH A . TA 12 HOH 15 2015 2015 HOH HOH A . TA 12 HOH 16 2016 2016 HOH HOH A . TA 12 HOH 17 2017 2017 HOH HOH A . TA 12 HOH 18 2018 2018 HOH HOH A . TA 12 HOH 19 2019 2019 HOH HOH A . TA 12 HOH 20 2020 2020 HOH HOH A . TA 12 HOH 21 2021 2021 HOH HOH A . TA 12 HOH 22 2022 2022 HOH HOH A . TA 12 HOH 23 2023 2023 HOH HOH A . TA 12 HOH 24 2024 2024 HOH HOH A . TA 12 HOH 25 2025 2025 HOH HOH A . TA 12 HOH 26 2026 2026 HOH HOH A . TA 12 HOH 27 2027 2027 HOH HOH A . TA 12 HOH 28 2028 2028 HOH HOH A . TA 12 HOH 29 2029 2029 HOH HOH A . TA 12 HOH 30 2030 2030 HOH HOH A . TA 12 HOH 31 2031 2031 HOH HOH A . TA 12 HOH 32 2032 2032 HOH HOH A . TA 12 HOH 33 2033 2033 HOH HOH A . TA 12 HOH 34 2034 2034 HOH HOH A . TA 12 HOH 35 2035 2035 HOH HOH A . TA 12 HOH 36 2036 2036 HOH HOH A . TA 12 HOH 37 2037 2037 HOH HOH A . TA 12 HOH 38 2038 2038 HOH HOH A . TA 12 HOH 39 2039 2039 HOH HOH A . TA 12 HOH 40 2040 2040 HOH HOH A . TA 12 HOH 41 2041 2041 HOH HOH A . TA 12 HOH 42 2042 2042 HOH HOH A . TA 12 HOH 43 2043 2043 HOH HOH A . TA 12 HOH 44 2044 2044 HOH HOH A . TA 12 HOH 45 2045 2045 HOH HOH A . TA 12 HOH 46 2046 2046 HOH HOH A . TA 12 HOH 47 2047 2047 HOH HOH A . TA 12 HOH 48 2048 2048 HOH HOH A . TA 12 HOH 49 2049 2049 HOH HOH A . TA 12 HOH 50 2050 2050 HOH HOH A . TA 12 HOH 51 2051 2051 HOH HOH A . TA 12 HOH 52 2052 2052 HOH HOH A . TA 12 HOH 53 2053 2053 HOH HOH A . TA 12 HOH 54 2054 2054 HOH HOH A . TA 12 HOH 55 2055 2055 HOH HOH A . TA 12 HOH 56 2056 2056 HOH HOH A . TA 12 HOH 57 2057 2057 HOH HOH A . TA 12 HOH 58 2058 2058 HOH HOH A . TA 12 HOH 59 2059 2059 HOH HOH A . TA 12 HOH 60 2060 2060 HOH HOH A . TA 12 HOH 61 2061 2061 HOH HOH A . TA 12 HOH 62 2062 2062 HOH HOH A . TA 12 HOH 63 2063 2063 HOH HOH A . TA 12 HOH 64 2064 2064 HOH HOH A . TA 12 HOH 65 2065 2065 HOH HOH A . TA 12 HOH 66 2066 2066 HOH HOH A . TA 12 HOH 67 2067 2067 HOH HOH A . TA 12 HOH 68 2068 2068 HOH HOH A . TA 12 HOH 69 2069 2069 HOH HOH A . TA 12 HOH 70 2070 2070 HOH HOH A . TA 12 HOH 71 2071 2071 HOH HOH A . TA 12 HOH 72 2072 2072 HOH HOH A . TA 12 HOH 73 2073 2073 HOH HOH A . TA 12 HOH 74 2074 2074 HOH HOH A . TA 12 HOH 75 2075 2075 HOH HOH A . TA 12 HOH 76 2076 2076 HOH HOH A . TA 12 HOH 77 2077 2077 HOH HOH A . TA 12 HOH 78 2078 2078 HOH HOH A . TA 12 HOH 79 2079 2079 HOH HOH A . TA 12 HOH 80 2080 2080 HOH HOH A . TA 12 HOH 81 2081 2081 HOH HOH A . TA 12 HOH 82 2082 2082 HOH HOH A . TA 12 HOH 83 2083 2083 HOH HOH A . TA 12 HOH 84 2084 2084 HOH HOH A . TA 12 HOH 85 2085 2085 HOH HOH A . TA 12 HOH 86 2086 2086 HOH HOH A . TA 12 HOH 87 2087 2087 HOH HOH A . TA 12 HOH 88 2088 2088 HOH HOH A . TA 12 HOH 89 2089 2089 HOH HOH A . TA 12 HOH 90 2090 2090 HOH HOH A . TA 12 HOH 91 2091 2091 HOH HOH A . TA 12 HOH 92 2092 2092 HOH HOH A . TA 12 HOH 93 2093 2093 HOH HOH A . TA 12 HOH 94 2094 2094 HOH HOH A . TA 12 HOH 95 2095 2095 HOH HOH A . TA 12 HOH 96 2096 2096 HOH HOH A . TA 12 HOH 97 2097 2097 HOH HOH A . TA 12 HOH 98 2098 2098 HOH HOH A . TA 12 HOH 99 2099 2099 HOH HOH A . TA 12 HOH 100 2100 2100 HOH HOH A . TA 12 HOH 101 2101 2101 HOH HOH A . TA 12 HOH 102 2102 2102 HOH HOH A . TA 12 HOH 103 2103 2103 HOH HOH A . TA 12 HOH 104 2104 2104 HOH HOH A . TA 12 HOH 105 2105 2105 HOH HOH A . TA 12 HOH 106 2106 2106 HOH HOH A . TA 12 HOH 107 2107 2107 HOH HOH A . TA 12 HOH 108 2108 2108 HOH HOH A . TA 12 HOH 109 2109 2109 HOH HOH A . TA 12 HOH 110 2110 2110 HOH HOH A . TA 12 HOH 111 2111 2111 HOH HOH A . TA 12 HOH 112 2112 2112 HOH HOH A . TA 12 HOH 113 2113 2113 HOH HOH A . TA 12 HOH 114 2114 2114 HOH HOH A . TA 12 HOH 115 2115 2115 HOH HOH A . TA 12 HOH 116 2116 2116 HOH HOH A . TA 12 HOH 117 2117 2117 HOH HOH A . TA 12 HOH 118 2118 2118 HOH HOH A . TA 12 HOH 119 2119 2119 HOH HOH A . TA 12 HOH 120 2120 2120 HOH HOH A . TA 12 HOH 121 2121 2121 HOH HOH A . TA 12 HOH 122 2122 2122 HOH HOH A . TA 12 HOH 123 2123 2123 HOH HOH A . TA 12 HOH 124 2124 2124 HOH HOH A . TA 12 HOH 125 2125 2125 HOH HOH A . TA 12 HOH 126 2126 2126 HOH HOH A . TA 12 HOH 127 2127 2127 HOH HOH A . TA 12 HOH 128 2128 2128 HOH HOH A . TA 12 HOH 129 2129 2129 HOH HOH A . TA 12 HOH 130 2130 2130 HOH HOH A . TA 12 HOH 131 2131 2131 HOH HOH A . TA 12 HOH 132 2132 2132 HOH HOH A . TA 12 HOH 133 2133 2133 HOH HOH A . TA 12 HOH 134 2134 2134 HOH HOH A . TA 12 HOH 135 2135 2135 HOH HOH A . TA 12 HOH 136 2136 2136 HOH HOH A . TA 12 HOH 137 2137 2137 HOH HOH A . TA 12 HOH 138 2138 2138 HOH HOH A . TA 12 HOH 139 2139 2139 HOH HOH A . TA 12 HOH 140 2140 2140 HOH HOH A . TA 12 HOH 141 2141 2141 HOH HOH A . TA 12 HOH 142 2142 2142 HOH HOH A . TA 12 HOH 143 2143 2143 HOH HOH A . TA 12 HOH 144 2144 2144 HOH HOH A . TA 12 HOH 145 2145 2145 HOH HOH A . TA 12 HOH 146 2146 2146 HOH HOH A . TA 12 HOH 147 2147 2147 HOH HOH A . TA 12 HOH 148 2148 2148 HOH HOH A . TA 12 HOH 149 2149 2149 HOH HOH A . TA 12 HOH 150 2150 2150 HOH HOH A . TA 12 HOH 151 2151 2151 HOH HOH A . TA 12 HOH 152 2152 2152 HOH HOH A . TA 12 HOH 153 2153 2153 HOH HOH A . TA 12 HOH 154 2154 2154 HOH HOH A . TA 12 HOH 155 2155 2155 HOH HOH A . TA 12 HOH 156 2156 2156 HOH HOH A . TA 12 HOH 157 2157 2157 HOH HOH A . TA 12 HOH 158 2158 2158 HOH HOH A . TA 12 HOH 159 2159 2159 HOH HOH A . TA 12 HOH 160 2160 2160 HOH HOH A . TA 12 HOH 161 2161 2161 HOH HOH A . TA 12 HOH 162 2162 2162 HOH HOH A . TA 12 HOH 163 2163 2163 HOH HOH A . TA 12 HOH 164 2164 2164 HOH HOH A . TA 12 HOH 165 2165 2165 HOH HOH A . TA 12 HOH 166 2166 2166 HOH HOH A . TA 12 HOH 167 2167 2167 HOH HOH A . TA 12 HOH 168 2168 2168 HOH HOH A . TA 12 HOH 169 2169 2169 HOH HOH A . TA 12 HOH 170 2170 2170 HOH HOH A . TA 12 HOH 171 2171 2171 HOH HOH A . TA 12 HOH 172 2172 2172 HOH HOH A . TA 12 HOH 173 2173 2173 HOH HOH A . TA 12 HOH 174 2174 2174 HOH HOH A . TA 12 HOH 175 2175 2175 HOH HOH A . TA 12 HOH 176 2176 2176 HOH HOH A . TA 12 HOH 177 2177 2177 HOH HOH A . TA 12 HOH 178 2178 2178 HOH HOH A . TA 12 HOH 179 2179 2179 HOH HOH A . TA 12 HOH 180 2180 2180 HOH HOH A . TA 12 HOH 181 2181 2181 HOH HOH A . TA 12 HOH 182 2182 2182 HOH HOH A . TA 12 HOH 183 2183 2183 HOH HOH A . TA 12 HOH 184 2184 2184 HOH HOH A . TA 12 HOH 185 2185 2185 HOH HOH A . TA 12 HOH 186 2186 2186 HOH HOH A . TA 12 HOH 187 2187 2187 HOH HOH A . TA 12 HOH 188 2188 2188 HOH HOH A . TA 12 HOH 189 2189 2189 HOH HOH A . TA 12 HOH 190 2190 2190 HOH HOH A . TA 12 HOH 191 2191 2191 HOH HOH A . TA 12 HOH 192 2192 2192 HOH HOH A . TA 12 HOH 193 2193 2193 HOH HOH A . TA 12 HOH 194 2194 2194 HOH HOH A . TA 12 HOH 195 2195 2195 HOH HOH A . TA 12 HOH 196 2196 2196 HOH HOH A . TA 12 HOH 197 2197 2197 HOH HOH A . TA 12 HOH 198 2198 2198 HOH HOH A . TA 12 HOH 199 2199 2199 HOH HOH A . TA 12 HOH 200 2200 2200 HOH HOH A . TA 12 HOH 201 2201 2201 HOH HOH A . TA 12 HOH 202 2202 2202 HOH HOH A . TA 12 HOH 203 2203 2203 HOH HOH A . TA 12 HOH 204 2204 2204 HOH HOH A . TA 12 HOH 205 2205 2205 HOH HOH A . TA 12 HOH 206 2206 2206 HOH HOH A . TA 12 HOH 207 2207 2207 HOH HOH A . TA 12 HOH 208 2208 2208 HOH HOH A . TA 12 HOH 209 2209 2209 HOH HOH A . TA 12 HOH 210 2210 2210 HOH HOH A . TA 12 HOH 211 2211 2211 HOH HOH A . TA 12 HOH 212 2212 2212 HOH HOH A . TA 12 HOH 213 2213 2213 HOH HOH A . TA 12 HOH 214 2214 2214 HOH HOH A . TA 12 HOH 215 2215 2215 HOH HOH A . TA 12 HOH 216 2216 2216 HOH HOH A . TA 12 HOH 217 2217 2217 HOH HOH A . TA 12 HOH 218 2218 2218 HOH HOH A . TA 12 HOH 219 2219 2219 HOH HOH A . TA 12 HOH 220 2220 2220 HOH HOH A . TA 12 HOH 221 2221 2221 HOH HOH A . TA 12 HOH 222 2222 2222 HOH HOH A . TA 12 HOH 223 2223 2223 HOH HOH A . TA 12 HOH 224 2224 2224 HOH HOH A . TA 12 HOH 225 2225 2225 HOH HOH A . TA 12 HOH 226 2226 2226 HOH HOH A . TA 12 HOH 227 2227 2227 HOH HOH A . TA 12 HOH 228 2228 2228 HOH HOH A . TA 12 HOH 229 2229 2229 HOH HOH A . TA 12 HOH 230 2230 2230 HOH HOH A . TA 12 HOH 231 2231 2231 HOH HOH A . TA 12 HOH 232 2232 2232 HOH HOH A . TA 12 HOH 233 2233 2233 HOH HOH A . TA 12 HOH 234 2234 2234 HOH HOH A . TA 12 HOH 235 2235 2235 HOH HOH A . TA 12 HOH 236 2236 2236 HOH HOH A . TA 12 HOH 237 2237 2237 HOH HOH A . TA 12 HOH 238 2238 2238 HOH HOH A . TA 12 HOH 239 2239 2239 HOH HOH A . TA 12 HOH 240 2240 2240 HOH HOH A . TA 12 HOH 241 2241 2241 HOH HOH A . TA 12 HOH 242 2242 2242 HOH HOH A . TA 12 HOH 243 2243 2243 HOH HOH A . TA 12 HOH 244 2244 2244 HOH HOH A . TA 12 HOH 245 2245 2245 HOH HOH A . TA 12 HOH 246 2246 2246 HOH HOH A . TA 12 HOH 247 2247 2247 HOH HOH A . TA 12 HOH 248 2248 2248 HOH HOH A . TA 12 HOH 249 2249 2249 HOH HOH A . TA 12 HOH 250 2250 2250 HOH HOH A . TA 12 HOH 251 2251 2251 HOH HOH A . TA 12 HOH 252 2252 2252 HOH HOH A . TA 12 HOH 253 2253 2253 HOH HOH A . TA 12 HOH 254 2254 2254 HOH HOH A . TA 12 HOH 255 2255 2255 HOH HOH A . TA 12 HOH 256 2256 2256 HOH HOH A . TA 12 HOH 257 2257 2257 HOH HOH A . TA 12 HOH 258 2258 2258 HOH HOH A . TA 12 HOH 259 2259 2259 HOH HOH A . TA 12 HOH 260 2260 2260 HOH HOH A . TA 12 HOH 261 2261 2261 HOH HOH A . TA 12 HOH 262 2262 2262 HOH HOH A . TA 12 HOH 263 2263 2263 HOH HOH A . TA 12 HOH 264 2264 2264 HOH HOH A . TA 12 HOH 265 2265 2265 HOH HOH A . TA 12 HOH 266 2266 2266 HOH HOH A . TA 12 HOH 267 2267 2267 HOH HOH A . TA 12 HOH 268 2268 2268 HOH HOH A . TA 12 HOH 269 2269 2269 HOH HOH A . TA 12 HOH 270 2270 2270 HOH HOH A . TA 12 HOH 271 2271 2271 HOH HOH A . TA 12 HOH 272 2272 2272 HOH HOH A . TA 12 HOH 273 2273 2273 HOH HOH A . TA 12 HOH 274 2274 2274 HOH HOH A . TA 12 HOH 275 2275 2275 HOH HOH A . TA 12 HOH 276 2276 2276 HOH HOH A . TA 12 HOH 277 2277 2277 HOH HOH A . TA 12 HOH 278 2278 2278 HOH HOH A . TA 12 HOH 279 2279 2279 HOH HOH A . TA 12 HOH 280 2280 2280 HOH HOH A . TA 12 HOH 281 2281 2281 HOH HOH A . TA 12 HOH 282 2282 2282 HOH HOH A . TA 12 HOH 283 2283 2283 HOH HOH A . TA 12 HOH 284 2284 2284 HOH HOH A . TA 12 HOH 285 2285 2285 HOH HOH A . TA 12 HOH 286 2286 2286 HOH HOH A . TA 12 HOH 287 2287 2287 HOH HOH A . TA 12 HOH 288 2288 2288 HOH HOH A . TA 12 HOH 289 2289 2289 HOH HOH A . TA 12 HOH 290 2290 2290 HOH HOH A . TA 12 HOH 291 2291 2291 HOH HOH A . TA 12 HOH 292 2292 2292 HOH HOH A . TA 12 HOH 293 2293 2293 HOH HOH A . TA 12 HOH 294 2294 2294 HOH HOH A . TA 12 HOH 295 2295 2295 HOH HOH A . TA 12 HOH 296 2296 2296 HOH HOH A . TA 12 HOH 297 2297 2297 HOH HOH A . TA 12 HOH 298 2298 2298 HOH HOH A . TA 12 HOH 299 2299 2299 HOH HOH A . TA 12 HOH 300 2300 2300 HOH HOH A . TA 12 HOH 301 2301 2301 HOH HOH A . TA 12 HOH 302 2302 2302 HOH HOH A . TA 12 HOH 303 2303 2303 HOH HOH A . TA 12 HOH 304 2304 2304 HOH HOH A . TA 12 HOH 305 2305 2305 HOH HOH A . TA 12 HOH 306 2306 2306 HOH HOH A . TA 12 HOH 307 2307 2307 HOH HOH A . TA 12 HOH 308 2308 2308 HOH HOH A . TA 12 HOH 309 2309 2309 HOH HOH A . TA 12 HOH 310 2310 2310 HOH HOH A . TA 12 HOH 311 2311 2311 HOH HOH A . TA 12 HOH 312 2312 2312 HOH HOH A . TA 12 HOH 313 2313 2313 HOH HOH A . TA 12 HOH 314 2314 2314 HOH HOH A . TA 12 HOH 315 2315 2315 HOH HOH A . TA 12 HOH 316 2316 2316 HOH HOH A . TA 12 HOH 317 2317 2317 HOH HOH A . TA 12 HOH 318 2318 2318 HOH HOH A . TA 12 HOH 319 2319 2319 HOH HOH A . TA 12 HOH 320 2320 2320 HOH HOH A . TA 12 HOH 321 2321 2321 HOH HOH A . TA 12 HOH 322 2322 2322 HOH HOH A . TA 12 HOH 323 2323 2323 HOH HOH A . TA 12 HOH 324 2324 2324 HOH HOH A . TA 12 HOH 325 2325 2325 HOH HOH A . TA 12 HOH 326 2326 2326 HOH HOH A . TA 12 HOH 327 2327 2327 HOH HOH A . TA 12 HOH 328 2328 2328 HOH HOH A . TA 12 HOH 329 2329 2329 HOH HOH A . TA 12 HOH 330 2330 2330 HOH HOH A . TA 12 HOH 331 2331 2331 HOH HOH A . TA 12 HOH 332 2332 2332 HOH HOH A . TA 12 HOH 333 2333 2333 HOH HOH A . TA 12 HOH 334 2334 2334 HOH HOH A . TA 12 HOH 335 2335 2335 HOH HOH A . TA 12 HOH 336 2336 2336 HOH HOH A . TA 12 HOH 337 2337 2337 HOH HOH A . TA 12 HOH 338 2338 2338 HOH HOH A . TA 12 HOH 339 2339 2339 HOH HOH A . TA 12 HOH 340 2340 2340 HOH HOH A . TA 12 HOH 341 2341 2341 HOH HOH A . TA 12 HOH 342 2342 2342 HOH HOH A . TA 12 HOH 343 2343 2343 HOH HOH A . TA 12 HOH 344 2344 2344 HOH HOH A . TA 12 HOH 345 2345 2345 HOH HOH A . TA 12 HOH 346 2346 2346 HOH HOH A . TA 12 HOH 347 2347 2347 HOH HOH A . TA 12 HOH 348 2348 2348 HOH HOH A . TA 12 HOH 349 2349 2349 HOH HOH A . TA 12 HOH 350 2350 2350 HOH HOH A . TA 12 HOH 351 2351 2351 HOH HOH A . TA 12 HOH 352 2352 2352 HOH HOH A . TA 12 HOH 353 2353 2353 HOH HOH A . TA 12 HOH 354 2354 2354 HOH HOH A . TA 12 HOH 355 2355 2355 HOH HOH A . TA 12 HOH 356 2356 2356 HOH HOH A . TA 12 HOH 357 2357 2357 HOH HOH A . TA 12 HOH 358 2358 2358 HOH HOH A . TA 12 HOH 359 2359 2359 HOH HOH A . TA 12 HOH 360 2360 2360 HOH HOH A . TA 12 HOH 361 2361 2361 HOH HOH A . TA 12 HOH 362 2362 2362 HOH HOH A . TA 12 HOH 363 2363 2363 HOH HOH A . TA 12 HOH 364 2364 2364 HOH HOH A . TA 12 HOH 365 2365 2365 HOH HOH A . TA 12 HOH 366 2366 2366 HOH HOH A . TA 12 HOH 367 2367 2367 HOH HOH A . TA 12 HOH 368 2368 2368 HOH HOH A . TA 12 HOH 369 2369 2369 HOH HOH A . TA 12 HOH 370 2370 2370 HOH HOH A . TA 12 HOH 371 2371 2371 HOH HOH A . TA 12 HOH 372 2372 2372 HOH HOH A . TA 12 HOH 373 2373 2373 HOH HOH A . TA 12 HOH 374 2374 2374 HOH HOH A . TA 12 HOH 375 2375 2375 HOH HOH A . TA 12 HOH 376 2376 2376 HOH HOH A . TA 12 HOH 377 2377 2377 HOH HOH A . TA 12 HOH 378 2378 2378 HOH HOH A . TA 12 HOH 379 2379 2379 HOH HOH A . TA 12 HOH 380 2380 2380 HOH HOH A . TA 12 HOH 381 2381 2381 HOH HOH A . TA 12 HOH 382 2382 2382 HOH HOH A . TA 12 HOH 383 2383 2383 HOH HOH A . TA 12 HOH 384 2384 2384 HOH HOH A . TA 12 HOH 385 2385 2385 HOH HOH A . TA 12 HOH 386 2386 2386 HOH HOH A . TA 12 HOH 387 2387 2387 HOH HOH A . TA 12 HOH 388 2388 2388 HOH HOH A . TA 12 HOH 389 2389 2389 HOH HOH A . TA 12 HOH 390 2390 2390 HOH HOH A . TA 12 HOH 391 2391 2391 HOH HOH A . TA 12 HOH 392 2392 2392 HOH HOH A . TA 12 HOH 393 2393 2393 HOH HOH A . TA 12 HOH 394 2394 2394 HOH HOH A . TA 12 HOH 395 2395 2395 HOH HOH A . TA 12 HOH 396 2396 2396 HOH HOH A . TA 12 HOH 397 2397 2397 HOH HOH A . TA 12 HOH 398 2398 2398 HOH HOH A . TA 12 HOH 399 2399 2399 HOH HOH A . TA 12 HOH 400 2400 2400 HOH HOH A . TA 12 HOH 401 2401 2401 HOH HOH A . TA 12 HOH 402 2402 2402 HOH HOH A . TA 12 HOH 403 2403 2403 HOH HOH A . TA 12 HOH 404 2404 2404 HOH HOH A . TA 12 HOH 405 2405 2405 HOH HOH A . TA 12 HOH 406 2406 2406 HOH HOH A . TA 12 HOH 407 2407 2407 HOH HOH A . TA 12 HOH 408 2408 2408 HOH HOH A . TA 12 HOH 409 2409 2409 HOH HOH A . TA 12 HOH 410 2410 2410 HOH HOH A . TA 12 HOH 411 2411 2411 HOH HOH A . TA 12 HOH 412 2412 2412 HOH HOH A . TA 12 HOH 413 2413 2413 HOH HOH A . TA 12 HOH 414 2414 2414 HOH HOH A . TA 12 HOH 415 2415 2415 HOH HOH A . TA 12 HOH 416 2416 2416 HOH HOH A . TA 12 HOH 417 2417 2417 HOH HOH A . TA 12 HOH 418 2418 2418 HOH HOH A . TA 12 HOH 419 2419 2419 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 55 A ASN 57 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 104 A ASN 106 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 239 A ASN 241 ? ASN 'GLYCOSYLATION SITE' 4 A ASN 254 A ASN 256 ? ASN 'GLYCOSYLATION SITE' 5 A ASN 339 A ASN 341 ? ASN 'GLYCOSYLATION SITE' 6 A ASN 483 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 octameric _pdbx_struct_assembly.oligomeric_count 8 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1,2,3,4,5,6,7,8 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA,EA,FA,GA,HA,IA,JA,KA,LA,MA,NA,OA,PA,QA,RA,SA,TA # loop_ _pdbx_struct_assembly_prop.biol_id _pdbx_struct_assembly_prop.type _pdbx_struct_assembly_prop.value _pdbx_struct_assembly_prop.details 1 'ABSA (A^2)' 78560 ? 1 MORE -427.5 ? 1 'SSA (A^2)' 149640 ? # loop_ _pdbx_struct_oper_list.id _pdbx_struct_oper_list.type _pdbx_struct_oper_list.name _pdbx_struct_oper_list.symmetry_operation _pdbx_struct_oper_list.matrix[1][1] _pdbx_struct_oper_list.matrix[1][2] _pdbx_struct_oper_list.matrix[1][3] _pdbx_struct_oper_list.vector[1] _pdbx_struct_oper_list.matrix[2][1] _pdbx_struct_oper_list.matrix[2][2] _pdbx_struct_oper_list.matrix[2][3] _pdbx_struct_oper_list.vector[2] _pdbx_struct_oper_list.matrix[3][1] _pdbx_struct_oper_list.matrix[3][2] _pdbx_struct_oper_list.matrix[3][3] _pdbx_struct_oper_list.vector[3] 1 'identity operation' 1_555 x,y,z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 2 'crystal symmetry operation' 6_555 x,-y,-z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 3 'crystal symmetry operation' 2_555 -x,-y,z -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 4 'crystal symmetry operation' 5_555 -x,y,-z -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 5 'crystal symmetry operation' 3_555 -y,x,z 0.0000000000 -1.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 6 'crystal symmetry operation' 4_555 y,-x,z 0.0000000000 1.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 7 'crystal symmetry operation' 7_555 y,x,-z 0.0000000000 1.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 8 'crystal symmetry operation' 8_555 -y,-x,-z 0.0000000000 -1.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 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 NA _pdbx_struct_special_symmetry.auth_seq_id 1555 _pdbx_struct_special_symmetry.PDB_ins_code ? _pdbx_struct_special_symmetry.label_asym_id GA _pdbx_struct_special_symmetry.label_comp_id NA _pdbx_struct_special_symmetry.label_seq_id . # loop_ _pdbx_struct_conn_angle.id _pdbx_struct_conn_angle.ptnr1_label_atom_id _pdbx_struct_conn_angle.ptnr1_label_alt_id _pdbx_struct_conn_angle.ptnr1_label_asym_id _pdbx_struct_conn_angle.ptnr1_label_comp_id _pdbx_struct_conn_angle.ptnr1_label_seq_id _pdbx_struct_conn_angle.ptnr1_auth_atom_id _pdbx_struct_conn_angle.ptnr1_auth_asym_id _pdbx_struct_conn_angle.ptnr1_auth_comp_id _pdbx_struct_conn_angle.ptnr1_auth_seq_id _pdbx_struct_conn_angle.ptnr1_PDB_ins_code _pdbx_struct_conn_angle.ptnr1_symmetry _pdbx_struct_conn_angle.ptnr2_label_atom_id _pdbx_struct_conn_angle.ptnr2_label_alt_id _pdbx_struct_conn_angle.ptnr2_label_asym_id _pdbx_struct_conn_angle.ptnr2_label_comp_id _pdbx_struct_conn_angle.ptnr2_label_seq_id _pdbx_struct_conn_angle.ptnr2_auth_atom_id _pdbx_struct_conn_angle.ptnr2_auth_asym_id _pdbx_struct_conn_angle.ptnr2_auth_comp_id _pdbx_struct_conn_angle.ptnr2_auth_seq_id _pdbx_struct_conn_angle.ptnr2_PDB_ins_code _pdbx_struct_conn_angle.ptnr2_symmetry _pdbx_struct_conn_angle.ptnr3_label_atom_id _pdbx_struct_conn_angle.ptnr3_label_alt_id _pdbx_struct_conn_angle.ptnr3_label_asym_id _pdbx_struct_conn_angle.ptnr3_label_comp_id _pdbx_struct_conn_angle.ptnr3_label_seq_id _pdbx_struct_conn_angle.ptnr3_auth_atom_id _pdbx_struct_conn_angle.ptnr3_auth_asym_id _pdbx_struct_conn_angle.ptnr3_auth_comp_id _pdbx_struct_conn_angle.ptnr3_auth_seq_id _pdbx_struct_conn_angle.ptnr3_PDB_ins_code _pdbx_struct_conn_angle.ptnr3_symmetry _pdbx_struct_conn_angle.value _pdbx_struct_conn_angle.value_esd 1 O ? TA HOH . ? A HOH 2040 ? 1_555 CA ? CA CA . ? A CA 1551 ? 1_555 O ? TA HOH . ? A HOH 2179 ? 1_555 51.1 ? 2 O ? TA HOH . ? A HOH 2393 ? 7_555 CA ? EA CA . ? A CA 1553 ? 1_555 OH ? A TYR 418 ? A TYR 420 ? 1_555 73.8 ? # 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 2011-03-23 2 'Structure model' 1 1 2013-03-06 # _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' 'Data collection' 2 2 'Structure model' 'Version format compliance' # 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 -22.8790 -26.6810 -46.6410 0.3424 0.1814 0.2916 -0.0359 -0.1379 -0.0437 2.2656 2.2371 2.1828 -0.5723 -0.0972 -0.0434 -0.0120 0.5256 0.0879 -0.7579 -0.0290 0.1270 -0.1510 -0.1826 0.0411 'X-RAY DIFFRACTION' 2 ? refined -15.7770 -31.2650 -33.0530 0.0770 0.0426 0.2866 -0.0230 -0.0190 -0.0615 0.6671 1.1795 1.6219 0.2319 0.1273 0.1479 -0.0373 0.1235 -0.0813 -0.2502 0.0667 -0.0391 0.0173 0.0229 -0.0294 'X-RAY DIFFRACTION' 3 ? refined -7.1060 -38.8480 -28.2380 0.0817 0.0428 0.3556 0.0099 0.0025 -0.0824 1.3158 0.7034 1.5878 0.2875 0.0755 -0.0779 -0.0142 0.1235 -0.2787 -0.0818 0.0890 -0.2041 0.2901 0.1545 -0.0748 'X-RAY DIFFRACTION' 4 ? refined -15.1280 -47.2210 -3.6380 0.1852 0.0763 0.3274 -0.0436 -0.1219 0.0661 8.0806 1.7547 3.5042 0.3596 2.5191 -0.2220 0.2142 -0.6152 -0.5890 0.2799 0.1123 -0.0506 0.3573 -0.3485 -0.3265 'X-RAY DIFFRACTION' 5 ? refined -24.2160 -25.2890 -16.8780 0.0291 0.0719 0.2665 0.0030 -0.0206 -0.0409 1.0254 1.7873 1.3453 0.5092 0.2831 -0.0058 0.0077 -0.0984 0.0578 -0.0088 0.0112 0.1902 -0.0457 -0.2302 -0.0189 'X-RAY DIFFRACTION' 6 ? refined -14.8020 -24.5350 -6.3990 0.0595 0.0716 0.2151 -0.0137 -0.0207 -0.0502 0.9116 5.2397 2.3476 -0.1143 0.3527 0.4828 -0.0601 -0.0932 0.1994 0.3759 0.0558 -0.2856 -0.1512 -0.1316 0.0043 # 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 A 3 ? ? A 61 ? ? ? ? 'X-RAY DIFFRACTION' 2 2 A 62 ? ? A 254 ? ? ? ? 'X-RAY DIFFRACTION' 3 3 A 255 ? ? A 333 ? ? ? ? 'X-RAY DIFFRACTION' 4 4 A 334 ? ? A 392 ? ? ? ? 'X-RAY DIFFRACTION' 5 5 A 393 ? ? A 485 ? ? ? ? 'X-RAY DIFFRACTION' 6 6 A 486 ? ? A 529 ? ? ? ? # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal REFMAC refinement 5.5.0102 ? 1 XDS 'data reduction' . ? 2 XSCALE 'data scaling' . ? 3 MOLREP phasing . ? 4 # _pdbx_entry_details.entry_id 2XQG _pdbx_entry_details.compound_details ;ENGINEERED RESIDUE IN CHAIN A, ASN 45 TO GLN ENGINEERED RESIDUE IN CHAIN A, ASN 483 TO GLN ENGINEERED RESIDUE IN CHAIN A, ASN 509 TO GLN ENGINEERED RESIDUE IN CHAIN A, ASN 514 TO GLN ; _pdbx_entry_details.source_details ? _pdbx_entry_details.nonpolymer_details ? _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 OE2 A GLU 238 ? A UNK A UNX 1503 ? ? 1.61 2 1 UNK A UNX 1513 ? ? UNK A UNX 1514 ? ? 1.64 3 1 UNK A UNX 1520 ? ? UNK A UNX 1521 ? ? 1.87 4 1 N A THR 496 ? ? O A HOH 2379 ? ? 1.90 5 1 SG A CYS 66 ? ? O A HOH 2096 ? ? 1.92 6 1 UNK A UNX 1513 ? ? UNK A UNX 1515 ? ? 1.96 7 1 UNK A UNX 1516 ? ? UNK A UNX 1517 ? ? 1.96 8 1 O A HOH 2028 ? ? O A HOH 2096 ? ? 2.02 9 1 O A TRP 376 ? ? O A HOH 2289 ? ? 2.04 10 1 UNK A UNX 1517 ? ? UNK A UNX 1518 ? ? 2.05 11 1 UNK A UNX 1509 ? ? UNK A UNX 1510 ? ? 2.11 12 1 O A SER 495 ? ? O A HOH 2377 ? ? 2.13 13 1 OE1 A GLU 404 ? ? O A HOH 2313 ? ? 2.15 14 1 O A HOH 2080 ? ? O A HOH 2183 ? ? 2.16 15 1 O A HOH 2266 ? ? O A HOH 2331 ? ? 2.17 16 1 UNK A UNX 1508 ? ? UNK A UNX 1509 ? ? 2.19 # loop_ _pdbx_validate_rmsd_bond.id _pdbx_validate_rmsd_bond.PDB_model_num _pdbx_validate_rmsd_bond.auth_atom_id_1 _pdbx_validate_rmsd_bond.auth_asym_id_1 _pdbx_validate_rmsd_bond.auth_comp_id_1 _pdbx_validate_rmsd_bond.auth_seq_id_1 _pdbx_validate_rmsd_bond.PDB_ins_code_1 _pdbx_validate_rmsd_bond.label_alt_id_1 _pdbx_validate_rmsd_bond.auth_atom_id_2 _pdbx_validate_rmsd_bond.auth_asym_id_2 _pdbx_validate_rmsd_bond.auth_comp_id_2 _pdbx_validate_rmsd_bond.auth_seq_id_2 _pdbx_validate_rmsd_bond.PDB_ins_code_2 _pdbx_validate_rmsd_bond.label_alt_id_2 _pdbx_validate_rmsd_bond.bond_value _pdbx_validate_rmsd_bond.bond_target_value _pdbx_validate_rmsd_bond.bond_deviation _pdbx_validate_rmsd_bond.bond_standard_deviation _pdbx_validate_rmsd_bond.linker_flag 1 1 CE3 A TRP 231 ? ? CZ3 A TRP 231 ? ? 1.482 1.380 0.102 0.017 N 2 1 CD A GLN 455 ? A NE2 A GLN 455 ? A 2.223 1.324 0.899 0.025 N # loop_ _pdbx_validate_rmsd_angle.id _pdbx_validate_rmsd_angle.PDB_model_num _pdbx_validate_rmsd_angle.auth_atom_id_1 _pdbx_validate_rmsd_angle.auth_asym_id_1 _pdbx_validate_rmsd_angle.auth_comp_id_1 _pdbx_validate_rmsd_angle.auth_seq_id_1 _pdbx_validate_rmsd_angle.PDB_ins_code_1 _pdbx_validate_rmsd_angle.label_alt_id_1 _pdbx_validate_rmsd_angle.auth_atom_id_2 _pdbx_validate_rmsd_angle.auth_asym_id_2 _pdbx_validate_rmsd_angle.auth_comp_id_2 _pdbx_validate_rmsd_angle.auth_seq_id_2 _pdbx_validate_rmsd_angle.PDB_ins_code_2 _pdbx_validate_rmsd_angle.label_alt_id_2 _pdbx_validate_rmsd_angle.auth_atom_id_3 _pdbx_validate_rmsd_angle.auth_asym_id_3 _pdbx_validate_rmsd_angle.auth_comp_id_3 _pdbx_validate_rmsd_angle.auth_seq_id_3 _pdbx_validate_rmsd_angle.PDB_ins_code_3 _pdbx_validate_rmsd_angle.label_alt_id_3 _pdbx_validate_rmsd_angle.angle_value _pdbx_validate_rmsd_angle.angle_target_value _pdbx_validate_rmsd_angle.angle_deviation _pdbx_validate_rmsd_angle.angle_standard_deviation _pdbx_validate_rmsd_angle.linker_flag 1 1 NE A ARG 219 ? ? CZ A ARG 219 ? ? NH1 A ARG 219 ? ? 115.29 120.30 -5.01 0.50 N 2 1 CA A LEU 370 ? ? CB A LEU 370 ? ? CG A LEU 370 ? ? 132.31 115.30 17.01 2.30 N 3 1 NE A ARG 424 ? ? CZ A ARG 424 ? ? NH2 A ARG 424 ? ? 116.89 120.30 -3.41 0.50 N 4 1 OE1 A GLN 455 ? A CD A GLN 455 ? A NE2 A GLN 455 ? A 142.87 121.90 20.97 2.30 N 5 1 CG A GLN 455 ? A CD A GLN 455 ? A NE2 A GLN 455 ? A 91.11 116.70 -25.59 2.40 N # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 PHE A 43 ? ? 75.53 -2.03 2 1 LYS A 51 ? ? 105.10 139.90 3 1 ASP A 54 ? ? 117.11 171.01 4 1 ALA A 58 ? ? -101.53 63.42 5 1 GLN A 67 ? ? -170.48 149.75 6 1 CYS A 92 ? ? -141.08 11.55 7 1 LYS A 103 ? ? -30.66 119.28 8 1 ALA A 162 ? ? -162.10 69.65 9 1 ASN A 165 ? ? 58.44 16.52 10 1 SER A 198 ? ? 60.07 -123.70 11 1 ASP A 297 ? ? -135.44 -81.84 12 1 VAL A 377 ? ? 89.09 25.58 13 1 ASP A 378 ? ? -140.05 -41.77 14 1 ASP A 379 ? ? -35.73 146.37 15 1 GLN A 380 ? ? -106.26 76.98 16 1 PHE A 398 ? ? -126.06 -56.87 17 1 THR A 496 ? ? 92.23 -78.27 18 1 GLU A 506 ? ? -92.63 -64.45 # loop_ _pdbx_validate_peptide_omega.id _pdbx_validate_peptide_omega.PDB_model_num _pdbx_validate_peptide_omega.auth_comp_id_1 _pdbx_validate_peptide_omega.auth_asym_id_1 _pdbx_validate_peptide_omega.auth_seq_id_1 _pdbx_validate_peptide_omega.PDB_ins_code_1 _pdbx_validate_peptide_omega.label_alt_id_1 _pdbx_validate_peptide_omega.auth_comp_id_2 _pdbx_validate_peptide_omega.auth_asym_id_2 _pdbx_validate_peptide_omega.auth_seq_id_2 _pdbx_validate_peptide_omega.PDB_ins_code_2 _pdbx_validate_peptide_omega.label_alt_id_2 _pdbx_validate_peptide_omega.omega 1 1 VAL A 377 ? ? ASP A 378 ? ? -31.52 2 1 GLN A 380 ? ? ARG A 381 ? ? 56.53 # _pdbx_validate_planes.id 1 _pdbx_validate_planes.PDB_model_num 1 _pdbx_validate_planes.auth_comp_id GLN _pdbx_validate_planes.auth_asym_id A _pdbx_validate_planes.auth_seq_id 455 _pdbx_validate_planes.PDB_ins_code ? _pdbx_validate_planes.label_alt_id ? _pdbx_validate_planes.rmsd 0.079 _pdbx_validate_planes.type 'SIDE CHAIN' # _pdbx_validate_chiral.id 1 _pdbx_validate_chiral.PDB_model_num 1 _pdbx_validate_chiral.auth_atom_id C1 _pdbx_validate_chiral.label_alt_id ? _pdbx_validate_chiral.auth_asym_id A _pdbx_validate_chiral.auth_comp_id NAG _pdbx_validate_chiral.auth_seq_id 1563 _pdbx_validate_chiral.PDB_ins_code ? _pdbx_validate_chiral.details 'WRONG HAND' _pdbx_validate_chiral.omega . # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 'UNKNOWN ATOM OR ION' UNX 3 '2-METHYLPROPYL HYDROGEN (R)-METHYLPHOSPHONATE' VR 4 GLYCINE GLY 5 'SULFATE ION' SO4 6 'CALCIUM ION' CA 7 'BROMIDE ION' BR 8 'SODIUM ION' NA 9 N-ACETYL-D-GLUCOSAMINE NAG 10 BETA-L-FUCOSE FUL 11 'CHLORIDE ION' CL 12 water HOH #